data_7HYD
# 
_entry.id   7HYD 
# 
_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   7HYD         pdb_00007hyd 10.2210/pdb7hyd/pdb 
WWPDB D_1001408085 ?            ?                   
# 
_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                        7HYD 
_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 '2-[(3S)-1-(quinazolin-4-yl)piperidin-3-yl]acetamide' 270.330   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                            65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                  78.133    2   ?         ? ? ? 
5 water       nat water                                                 18.015    364 ?         ? ? ? 
# 
_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 '2-[(3S)-1-(quinazolin-4-yl)piperidin-3-yl]acetamide' A1BRX 
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 
A1BRX non-polymer         . '2-[(3S)-1-(quinazolin-4-yl)piperidin-3-yl]acetamide' ? 'C15 H18 N4 O'   270.330 
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        A1BRX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BRX 
_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 A1BRX 1   201 201 A1BRX 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 4 DMS   1   202 1   DMS   DMS C . 
H 5 HOH   1   301 642 HOH   HOH A . 
H 5 HOH   2   302 658 HOH   HOH A . 
H 5 HOH   3   303 99  HOH   HOH A . 
H 5 HOH   4   304 605 HOH   HOH A . 
H 5 HOH   5   305 611 HOH   HOH A . 
H 5 HOH   6   306 644 HOH   HOH A . 
H 5 HOH   7   307 67  HOH   HOH A . 
H 5 HOH   8   308 273 HOH   HOH A . 
H 5 HOH   9   309 155 HOH   HOH A . 
H 5 HOH   10  310 153 HOH   HOH A . 
H 5 HOH   11  311 231 HOH   HOH A . 
H 5 HOH   12  312 607 HOH   HOH A . 
H 5 HOH   13  313 115 HOH   HOH A . 
H 5 HOH   14  314 117 HOH   HOH A . 
H 5 HOH   15  315 223 HOH   HOH A . 
H 5 HOH   16  316 78  HOH   HOH A . 
H 5 HOH   17  317 19  HOH   HOH A . 
H 5 HOH   18  318 50  HOH   HOH A . 
H 5 HOH   19  319 54  HOH   HOH A . 
H 5 HOH   20  320 595 HOH   HOH A . 
H 5 HOH   21  321 124 HOH   HOH A . 
H 5 HOH   22  322 148 HOH   HOH A . 
H 5 HOH   23  323 596 HOH   HOH A . 
H 5 HOH   24  324 33  HOH   HOH A . 
H 5 HOH   25  325 176 HOH   HOH A . 
H 5 HOH   26  326 256 HOH   HOH A . 
H 5 HOH   27  327 102 HOH   HOH A . 
H 5 HOH   28  328 461 HOH   HOH A . 
H 5 HOH   29  329 237 HOH   HOH A . 
H 5 HOH   30  330 646 HOH   HOH A . 
H 5 HOH   31  331 47  HOH   HOH A . 
H 5 HOH   32  332 629 HOH   HOH A . 
H 5 HOH   33  333 208 HOH   HOH A . 
H 5 HOH   34  334 178 HOH   HOH A . 
H 5 HOH   35  335 209 HOH   HOH A . 
H 5 HOH   36  336 236 HOH   HOH A . 
H 5 HOH   37  337 614 HOH   HOH A . 
H 5 HOH   38  338 174 HOH   HOH A . 
H 5 HOH   39  339 70  HOH   HOH A . 
H 5 HOH   40  340 136 HOH   HOH A . 
H 5 HOH   41  341 77  HOH   HOH A . 
H 5 HOH   42  342 28  HOH   HOH A . 
H 5 HOH   43  343 608 HOH   HOH A . 
H 5 HOH   44  344 23  HOH   HOH A . 
H 5 HOH   45  345 44  HOH   HOH A . 
H 5 HOH   46  346 610 HOH   HOH A . 
H 5 HOH   47  347 122 HOH   HOH A . 
H 5 HOH   48  348 18  HOH   HOH A . 
H 5 HOH   49  349 8   HOH   HOH A . 
H 5 HOH   50  350 227 HOH   HOH A . 
H 5 HOH   51  351 141 HOH   HOH A . 
H 5 HOH   52  352 603 HOH   HOH A . 
H 5 HOH   53  353 217 HOH   HOH A . 
H 5 HOH   54  354 73  HOH   HOH A . 
H 5 HOH   55  355 129 HOH   HOH A . 
H 5 HOH   56  356 9   HOH   HOH A . 
H 5 HOH   57  357 280 HOH   HOH A . 
H 5 HOH   58  358 226 HOH   HOH A . 
H 5 HOH   59  359 647 HOH   HOH A . 
H 5 HOH   60  360 142 HOH   HOH A . 
H 5 HOH   61  361 609 HOH   HOH A . 
H 5 HOH   62  362 215 HOH   HOH A . 
H 5 HOH   63  363 625 HOH   HOH A . 
H 5 HOH   64  364 597 HOH   HOH A . 
H 5 HOH   65  365 41  HOH   HOH A . 
H 5 HOH   66  366 601 HOH   HOH A . 
H 5 HOH   67  367 228 HOH   HOH A . 
H 5 HOH   68  368 21  HOH   HOH A . 
H 5 HOH   69  369 51  HOH   HOH A . 
H 5 HOH   70  370 71  HOH   HOH A . 
H 5 HOH   71  371 82  HOH   HOH A . 
H 5 HOH   72  372 322 HOH   HOH A . 
H 5 HOH   73  373 166 HOH   HOH A . 
H 5 HOH   74  374 39  HOH   HOH A . 
H 5 HOH   75  375 80  HOH   HOH A . 
H 5 HOH   76  376 631 HOH   HOH A . 
H 5 HOH   77  377 4   HOH   HOH A . 
H 5 HOH   78  378 13  HOH   HOH A . 
H 5 HOH   79  379 79  HOH   HOH A . 
H 5 HOH   80  380 92  HOH   HOH A . 
H 5 HOH   81  381 617 HOH   HOH A . 
H 5 HOH   82  382 63  HOH   HOH A . 
H 5 HOH   83  383 43  HOH   HOH A . 
H 5 HOH   84  384 621 HOH   HOH A . 
H 5 HOH   85  385 16  HOH   HOH A . 
H 5 HOH   86  386 119 HOH   HOH A . 
H 5 HOH   87  387 76  HOH   HOH A . 
H 5 HOH   88  388 105 HOH   HOH A . 
H 5 HOH   89  389 11  HOH   HOH A . 
H 5 HOH   90  390 197 HOH   HOH A . 
H 5 HOH   91  391 205 HOH   HOH A . 
H 5 HOH   92  392 42  HOH   HOH A . 
H 5 HOH   93  393 306 HOH   HOH A . 
H 5 HOH   94  394 655 HOH   HOH A . 
H 5 HOH   95  395 641 HOH   HOH A . 
H 5 HOH   96  396 204 HOH   HOH A . 
H 5 HOH   97  397 34  HOH   HOH A . 
H 5 HOH   98  398 615 HOH   HOH A . 
H 5 HOH   99  399 623 HOH   HOH A . 
H 5 HOH   100 400 87  HOH   HOH A . 
H 5 HOH   101 401 60  HOH   HOH A . 
H 5 HOH   102 402 235 HOH   HOH A . 
H 5 HOH   103 403 149 HOH   HOH A . 
H 5 HOH   104 404 131 HOH   HOH A . 
H 5 HOH   105 405 133 HOH   HOH A . 
H 5 HOH   106 406 169 HOH   HOH A . 
H 5 HOH   107 407 259 HOH   HOH A . 
H 5 HOH   108 408 48  HOH   HOH A . 
H 5 HOH   109 409 38  HOH   HOH A . 
H 5 HOH   110 410 132 HOH   HOH A . 
H 5 HOH   111 411 592 HOH   HOH A . 
H 5 HOH   112 412 110 HOH   HOH A . 
H 5 HOH   113 413 200 HOH   HOH A . 
H 5 HOH   114 414 600 HOH   HOH A . 
H 5 HOH   115 415 198 HOH   HOH A . 
H 5 HOH   116 416 627 HOH   HOH A . 
H 5 HOH   117 417 649 HOH   HOH A . 
H 5 HOH   118 418 14  HOH   HOH A . 
H 5 HOH   119 419 139 HOH   HOH A . 
H 5 HOH   120 420 29  HOH   HOH A . 
H 5 HOH   121 421 164 HOH   HOH A . 
H 5 HOH   122 422 64  HOH   HOH A . 
H 5 HOH   123 423 307 HOH   HOH A . 
H 5 HOH   124 424 172 HOH   HOH A . 
H 5 HOH   125 425 287 HOH   HOH A . 
H 5 HOH   126 426 69  HOH   HOH A . 
H 5 HOH   127 427 574 HOH   HOH A . 
H 5 HOH   128 428 96  HOH   HOH A . 
H 5 HOH   129 429 12  HOH   HOH A . 
H 5 HOH   130 430 628 HOH   HOH A . 
H 5 HOH   131 431 497 HOH   HOH A . 
H 5 HOH   132 432 190 HOH   HOH A . 
H 5 HOH   133 433 186 HOH   HOH A . 
H 5 HOH   134 434 657 HOH   HOH A . 
H 5 HOH   135 435 214 HOH   HOH A . 
H 5 HOH   136 436 593 HOH   HOH A . 
H 5 HOH   137 437 471 HOH   HOH A . 
H 5 HOH   138 438 243 HOH   HOH A . 
H 5 HOH   139 439 594 HOH   HOH A . 
H 5 HOH   140 440 475 HOH   HOH A . 
H 5 HOH   141 441 74  HOH   HOH A . 
H 5 HOH   142 442 637 HOH   HOH A . 
H 5 HOH   143 443 276 HOH   HOH A . 
H 5 HOH   144 444 187 HOH   HOH A . 
H 5 HOH   145 445 123 HOH   HOH A . 
H 5 HOH   146 446 206 HOH   HOH A . 
H 5 HOH   147 447 212 HOH   HOH A . 
H 5 HOH   148 448 207 HOH   HOH A . 
H 5 HOH   149 449 165 HOH   HOH A . 
H 5 HOH   150 450 482 HOH   HOH A . 
H 5 HOH   151 451 290 HOH   HOH A . 
H 5 HOH   152 452 192 HOH   HOH A . 
H 5 HOH   153 453 500 HOH   HOH A . 
H 5 HOH   154 454 380 HOH   HOH A . 
H 5 HOH   155 455 496 HOH   HOH A . 
H 5 HOH   156 456 211 HOH   HOH A . 
H 5 HOH   157 457 146 HOH   HOH A . 
H 5 HOH   158 458 654 HOH   HOH A . 
H 5 HOH   159 459 650 HOH   HOH A . 
H 5 HOH   160 460 203 HOH   HOH A . 
H 5 HOH   161 461 531 HOH   HOH A . 
H 5 HOH   162 462 154 HOH   HOH A . 
H 5 HOH   163 463 486 HOH   HOH A . 
H 5 HOH   164 464 191 HOH   HOH A . 
H 5 HOH   165 465 126 HOH   HOH A . 
H 5 HOH   166 466 275 HOH   HOH A . 
H 5 HOH   167 467 620 HOH   HOH A . 
H 5 HOH   168 468 150 HOH   HOH A . 
H 5 HOH   169 469 229 HOH   HOH A . 
H 5 HOH   170 470 264 HOH   HOH A . 
H 5 HOH   171 471 239 HOH   HOH A . 
H 5 HOH   172 472 481 HOH   HOH A . 
H 5 HOH   173 473 175 HOH   HOH A . 
H 5 HOH   174 474 162 HOH   HOH A . 
H 5 HOH   175 475 466 HOH   HOH A . 
H 5 HOH   176 476 477 HOH   HOH A . 
H 5 HOH   177 477 476 HOH   HOH A . 
H 5 HOH   178 478 267 HOH   HOH A . 
H 5 HOH   179 479 479 HOH   HOH A . 
H 5 HOH   180 480 526 HOH   HOH A . 
H 5 HOH   181 481 577 HOH   HOH A . 
I 5 HOH   1   301 127 HOH   HOH C . 
I 5 HOH   2   302 616 HOH   HOH C . 
I 5 HOH   3   303 137 HOH   HOH C . 
I 5 HOH   4   304 112 HOH   HOH C . 
I 5 HOH   5   305 613 HOH   HOH C . 
I 5 HOH   6   306 484 HOH   HOH C . 
I 5 HOH   7   307 128 HOH   HOH C . 
I 5 HOH   8   308 5   HOH   HOH C . 
I 5 HOH   9   309 35  HOH   HOH C . 
I 5 HOH   10  310 81  HOH   HOH C . 
I 5 HOH   11  311 83  HOH   HOH C . 
I 5 HOH   12  312 233 HOH   HOH C . 
I 5 HOH   13  313 114 HOH   HOH C . 
I 5 HOH   14  314 138 HOH   HOH C . 
I 5 HOH   15  315 72  HOH   HOH C . 
I 5 HOH   16  316 622 HOH   HOH C . 
I 5 HOH   17  317 120 HOH   HOH C . 
I 5 HOH   18  318 52  HOH   HOH C . 
I 5 HOH   19  319 640 HOH   HOH C . 
I 5 HOH   20  320 100 HOH   HOH C . 
I 5 HOH   21  321 130 HOH   HOH C . 
I 5 HOH   22  322 55  HOH   HOH C . 
I 5 HOH   23  323 321 HOH   HOH C . 
I 5 HOH   24  324 88  HOH   HOH C . 
I 5 HOH   25  325 648 HOH   HOH C . 
I 5 HOH   26  326 103 HOH   HOH C . 
I 5 HOH   27  327 15  HOH   HOH C . 
I 5 HOH   28  328 161 HOH   HOH C . 
I 5 HOH   29  329 94  HOH   HOH C . 
I 5 HOH   30  330 118 HOH   HOH C . 
I 5 HOH   31  331 296 HOH   HOH C . 
I 5 HOH   32  332 58  HOH   HOH C . 
I 5 HOH   33  333 618 HOH   HOH C . 
I 5 HOH   34  334 24  HOH   HOH C . 
I 5 HOH   35  335 27  HOH   HOH C . 
I 5 HOH   36  336 598 HOH   HOH C . 
I 5 HOH   37  337 638 HOH   HOH C . 
I 5 HOH   38  338 156 HOH   HOH C . 
I 5 HOH   39  339 36  HOH   HOH C . 
I 5 HOH   40  340 160 HOH   HOH C . 
I 5 HOH   41  341 66  HOH   HOH C . 
I 5 HOH   42  342 651 HOH   HOH C . 
I 5 HOH   43  343 17  HOH   HOH C . 
I 5 HOH   44  344 2   HOH   HOH C . 
I 5 HOH   45  345 491 HOH   HOH C . 
I 5 HOH   46  346 645 HOH   HOH C . 
I 5 HOH   47  347 84  HOH   HOH C . 
I 5 HOH   48  348 26  HOH   HOH C . 
I 5 HOH   49  349 10  HOH   HOH C . 
I 5 HOH   50  350 143 HOH   HOH C . 
I 5 HOH   51  351 213 HOH   HOH C . 
I 5 HOH   52  352 49  HOH   HOH C . 
I 5 HOH   53  353 106 HOH   HOH C . 
I 5 HOH   54  354 630 HOH   HOH C . 
I 5 HOH   55  355 31  HOH   HOH C . 
I 5 HOH   56  356 469 HOH   HOH C . 
I 5 HOH   57  357 612 HOH   HOH C . 
I 5 HOH   58  358 90  HOH   HOH C . 
I 5 HOH   59  359 111 HOH   HOH C . 
I 5 HOH   60  360 32  HOH   HOH C . 
I 5 HOH   61  361 258 HOH   HOH C . 
I 5 HOH   62  362 171 HOH   HOH C . 
I 5 HOH   63  363 109 HOH   HOH C . 
I 5 HOH   64  364 653 HOH   HOH C . 
I 5 HOH   65  365 656 HOH   HOH C . 
I 5 HOH   66  366 599 HOH   HOH C . 
I 5 HOH   67  367 170 HOH   HOH C . 
I 5 HOH   68  368 498 HOH   HOH C . 
I 5 HOH   69  369 46  HOH   HOH C . 
I 5 HOH   70  370 606 HOH   HOH C . 
I 5 HOH   71  371 93  HOH   HOH C . 
I 5 HOH   72  372 59  HOH   HOH C . 
I 5 HOH   73  373 636 HOH   HOH C . 
I 5 HOH   74  374 85  HOH   HOH C . 
I 5 HOH   75  375 45  HOH   HOH C . 
I 5 HOH   76  376 157 HOH   HOH C . 
I 5 HOH   77  377 634 HOH   HOH C . 
I 5 HOH   78  378 40  HOH   HOH C . 
I 5 HOH   79  379 145 HOH   HOH C . 
I 5 HOH   80  380 147 HOH   HOH C . 
I 5 HOH   81  381 22  HOH   HOH C . 
I 5 HOH   82  382 65  HOH   HOH C . 
I 5 HOH   83  383 134 HOH   HOH C . 
I 5 HOH   84  384 75  HOH   HOH C . 
I 5 HOH   85  385 91  HOH   HOH C . 
I 5 HOH   86  386 37  HOH   HOH C . 
I 5 HOH   87  387 53  HOH   HOH C . 
I 5 HOH   88  388 240 HOH   HOH C . 
I 5 HOH   89  389 86  HOH   HOH C . 
I 5 HOH   90  390 20  HOH   HOH C . 
I 5 HOH   91  391 125 HOH   HOH C . 
I 5 HOH   92  392 633 HOH   HOH C . 
I 5 HOH   93  393 108 HOH   HOH C . 
I 5 HOH   94  394 121 HOH   HOH C . 
I 5 HOH   95  395 98  HOH   HOH C . 
I 5 HOH   96  396 116 HOH   HOH C . 
I 5 HOH   97  397 224 HOH   HOH C . 
I 5 HOH   98  398 97  HOH   HOH C . 
I 5 HOH   99  399 183 HOH   HOH C . 
I 5 HOH   100 400 107 HOH   HOH C . 
I 5 HOH   101 401 30  HOH   HOH C . 
I 5 HOH   102 402 179 HOH   HOH C . 
I 5 HOH   103 403 163 HOH   HOH C . 
I 5 HOH   104 404 254 HOH   HOH C . 
I 5 HOH   105 405 135 HOH   HOH C . 
I 5 HOH   106 406 68  HOH   HOH C . 
I 5 HOH   107 407 470 HOH   HOH C . 
I 5 HOH   108 408 57  HOH   HOH C . 
I 5 HOH   109 409 62  HOH   HOH C . 
I 5 HOH   110 410 101 HOH   HOH C . 
I 5 HOH   111 411 56  HOH   HOH C . 
I 5 HOH   112 412 3   HOH   HOH C . 
I 5 HOH   113 413 113 HOH   HOH C . 
I 5 HOH   114 414 6   HOH   HOH C . 
I 5 HOH   115 415 184 HOH   HOH C . 
I 5 HOH   116 416 624 HOH   HOH C . 
I 5 HOH   117 417 95  HOH   HOH C . 
I 5 HOH   118 418 619 HOH   HOH C . 
I 5 HOH   119 419 7   HOH   HOH C . 
I 5 HOH   120 420 140 HOH   HOH C . 
I 5 HOH   121 421 604 HOH   HOH C . 
I 5 HOH   122 422 152 HOH   HOH C . 
I 5 HOH   123 423 199 HOH   HOH C . 
I 5 HOH   124 424 602 HOH   HOH C . 
I 5 HOH   125 425 201 HOH   HOH C . 
I 5 HOH   126 426 507 HOH   HOH C . 
I 5 HOH   127 427 502 HOH   HOH C . 
I 5 HOH   128 428 329 HOH   HOH C . 
I 5 HOH   129 429 232 HOH   HOH C . 
I 5 HOH   130 430 252 HOH   HOH C . 
I 5 HOH   131 431 493 HOH   HOH C . 
I 5 HOH   132 432 195 HOH   HOH C . 
I 5 HOH   133 433 632 HOH   HOH C . 
I 5 HOH   134 434 257 HOH   HOH C . 
I 5 HOH   135 435 635 HOH   HOH C . 
I 5 HOH   136 436 643 HOH   HOH C . 
I 5 HOH   137 437 467 HOH   HOH C . 
I 5 HOH   138 438 639 HOH   HOH C . 
I 5 HOH   139 439 626 HOH   HOH C . 
I 5 HOH   140 440 194 HOH   HOH C . 
I 5 HOH   141 441 278 HOH   HOH C . 
I 5 HOH   142 442 159 HOH   HOH C . 
I 5 HOH   143 443 193 HOH   HOH C . 
I 5 HOH   144 444 460 HOH   HOH C . 
I 5 HOH   145 445 144 HOH   HOH C . 
I 5 HOH   146 446 660 HOH   HOH C . 
I 5 HOH   147 447 485 HOH   HOH C . 
I 5 HOH   148 448 464 HOH   HOH C . 
I 5 HOH   149 449 181 HOH   HOH C . 
I 5 HOH   150 450 255 HOH   HOH C . 
I 5 HOH   151 451 480 HOH   HOH C . 
I 5 HOH   152 452 185 HOH   HOH C . 
I 5 HOH   153 453 220 HOH   HOH C . 
I 5 HOH   154 454 472 HOH   HOH C . 
I 5 HOH   155 455 659 HOH   HOH C . 
I 5 HOH   156 456 248 HOH   HOH C . 
I 5 HOH   157 457 652 HOH   HOH C . 
I 5 HOH   158 458 104 HOH   HOH C . 
I 5 HOH   159 459 465 HOH   HOH C . 
I 5 HOH   160 460 462 HOH   HOH C . 
I 5 HOH   161 461 492 HOH   HOH C . 
I 5 HOH   162 462 180 HOH   HOH C . 
I 5 HOH   163 463 189 HOH   HOH C . 
I 5 HOH   164 464 251 HOH   HOH C . 
I 5 HOH   165 465 168 HOH   HOH C . 
I 5 HOH   166 466 499 HOH   HOH C . 
I 5 HOH   167 467 151 HOH   HOH C . 
I 5 HOH   168 468 478 HOH   HOH C . 
I 5 HOH   169 469 242 HOH   HOH C . 
I 5 HOH   170 470 474 HOH   HOH C . 
I 5 HOH   171 471 158 HOH   HOH C . 
I 5 HOH   172 472 281 HOH   HOH C . 
I 5 HOH   173 473 487 HOH   HOH C . 
I 5 HOH   174 474 501 HOH   HOH C . 
I 5 HOH   175 475 591 HOH   HOH C . 
I 5 HOH   176 476 483 HOH   HOH C . 
I 5 HOH   177 477 177 HOH   HOH C . 
I 5 HOH   178 478 513 HOH   HOH C . 
I 5 HOH   179 479 511 HOH   HOH C . 
I 5 HOH   180 480 504 HOH   HOH C . 
I 5 HOH   181 481 506 HOH   HOH C . 
I 5 HOH   182 482 580 HOH   HOH C . 
I 5 HOH   183 483 488 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           7HYD 
_cell.length_a           86.620 
_cell.length_b           57.020 
_cell.length_c           64.830 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.57 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HYD 
_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          7HYD 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.51 
_exptl_crystal.density_percent_sol   51.00 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-12-02 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92203 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HYD 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             43.17 
_reflns.d_resolution_high            1.44 
_reflns.number_obs                   56944 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.129 
_reflns.pdbx_netI_over_sigmaI        10.0 
_reflns.pdbx_redundancy              6.3 
_reflns.pdbx_Rrim_I_all              0.140 
_reflns.pdbx_Rpim_I_all              0.055 
_reflns.pdbx_CC_half                 0.994 
_reflns.pdbx_number_measured_all     357598 
_reflns.pdbx_chi_squared             0.95 
_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                  1.44 
_reflns_shell.d_res_low                   1.48 
_reflns_shell.number_measured_all         19567 
_reflns_shell.number_unique_obs           4185 
_reflns_shell.Rmerge_I_obs                1.254 
_reflns_shell.pdbx_chi_squared            0.95 
_reflns_shell.pdbx_redundancy             4.7 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.3 
_reflns_shell.pdbx_Rrim_I_all             1.420 
_reflns_shell.pdbx_Rpim_I_all             0.649 
_reflns_shell.pdbx_CC_half                0.355 
_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                                 7HYD 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     56943 
_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                             43.17 
_refine.ls_d_res_high                            1.440 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_R_factor_obs                          0.1890 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1879 
_refine.ls_R_factor_R_free                       0.2098 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.970 
_refine.ls_number_reflns_R_free                  2829 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.956 
_refine.B_iso_mean                               21.43 
_refine.aniso_B[1][1]                            -0.96310 
_refine.aniso_B[2][2]                            0.26950 
_refine.aniso_B[3][3]                            0.69360 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.34970 
_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             0.063 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.064 
_refine.pdbx_overall_SU_R_Blow_DPI               0.068 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.067 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HYD 
_refine_analyze.Luzzati_coordinate_error_obs    0.19 
_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         30 
_refine_hist.number_atoms_solvent             364 
_refine_hist.number_atoms_total               2560 
_refine_hist.d_res_high                       1.440 
_refine_hist.d_res_low                        43.17 
# 
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  2268 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.01  ? 2.00  3091 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  758  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  410  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2268 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.53  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.82 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  280  '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  2071 '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                       1.44 
_refine_ls_shell.d_res_low                        1.45 
_refine_ls_shell.number_reflns_R_work             1077 
_refine_ls_shell.R_factor_R_work                  0.2834 
_refine_ls_shell.percent_reflns_obs               99.82 
_refine_ls_shell.R_factor_R_free                  0.2593 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.44 
_refine_ls_shell.number_reflns_R_free             62 
_refine_ls_shell.number_reflns_all                1139 
_refine_ls_shell.R_factor_all                     0.2821 
# 
_struct.entry_id                  7HYD 
_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-0035291-001 (A71EV2A-x4351)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HYD 
_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 4 ? 
H N N 5 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HYD A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HYD C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,H 
2 1 B,F,G,I   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 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 ? ? ? ? ? ? ? 2.369 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.289 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.358 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.349 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.340 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.363 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.086 ? ? 
# 
_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_555 111.0 ? 
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_555 105.1 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 117.1 ? 
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_555 106.0 ? 
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_555 102.6 ? 
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_555 114.7 ? 
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_555 109.7 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.2 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 117.6 ? 
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_555 106.6 ? 
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_555 100.7 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.5 ? 
# 
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 VAL A 68  ? O VAL A 74  N GLY A 55  ? N GLY A 61  
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 ILE A 117 ? N ILE A 123 O ALA A 129 ? O ALA A 135 
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 LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7HYD 
_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_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A PHE 83  ? ? CA A PHE 83  ? ? C  A PHE 83  ? ? 78.66 110.40 -31.74 2.00 N 
2 1 N  A PRO 107 ? ? CA A PRO 107 ? ? CB A PRO 107 ? ? 95.75 103.30 -7.55  1.20 N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ARG 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     93 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -178.27 
_pdbx_validate_torsion.psi             -176.84 
# 
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 14.9845 8.1762   14.4463 -0.0258 -0.0216 0.0045 0.0111 0.0081 0.0045 1.2922 0.8873 0.6693 0.9321  
-0.4581 -0.3184 -0.0081 0.0415  0.1241 0.0416 0.0483 0.0293 -0.0220 -0.0728 -0.0402 
'X-RAY DIFFRACTION' 2 ? refined 25.8159 -20.1948 17.7574 -0.0268 -0.0207 0.0108 0.0107 0.0074 0.0164 0.6136 0.9295 0.2572 -0.2786 
-0.0676 -0.0999 -0.0059 -0.0019 0.1079 0.0298 0.0468 0.0034 0.0328  0.0033  -0.0409 
# 
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_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 480 ? 6.65  . 
2 1 O ? A HOH 481 ? 10.52 . 
3 1 O ? C HOH 478 ? 5.87  . 
4 1 O ? C HOH 479 ? 6.66  . 
5 1 O ? C HOH 480 ? 6.76  . 
6 1 O ? C HOH 481 ? 6.99  . 
7 1 O ? C HOH 482 ? 7.26  . 
8 1 O ? C HOH 483 ? 8.70  . 
# 
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 
A1BRX N1   N  N N 1   
A1BRX N3   N  Y N 2   
A1BRX C4   C  N N 3   
A1BRX C5   C  N N 4   
A1BRX C6   C  Y N 5   
A1BRX C7   C  Y N 6   
A1BRX C8   C  Y N 7   
A1BRX C10  C  Y N 8   
A1BRX C13  C  Y N 9   
A1BRX O    O  N N 10  
A1BRX C    C  N N 11  
A1BRX N    N  N N 12  
A1BRX C1   C  N N 13  
A1BRX C2   C  N S 14  
A1BRX C14  C  N N 15  
A1BRX C3   C  N N 16  
A1BRX N2   N  Y N 17  
A1BRX C12  C  Y N 18  
A1BRX C11  C  Y N 19  
A1BRX C9   C  Y N 20  
A1BRX H7   H  N N 21  
A1BRX H8   H  N N 22  
A1BRX H10  H  N N 23  
A1BRX H9   H  N N 24  
A1BRX H11  H  N N 25  
A1BRX H13  H  N N 26  
A1BRX H1   H  N N 27  
A1BRX H2   H  N N 28  
A1BRX H4   H  N N 29  
A1BRX H3   H  N N 30  
A1BRX H    H  N N 31  
A1BRX H16  H  N N 32  
A1BRX H17  H  N N 33  
A1BRX H6   H  N N 34  
A1BRX H5   H  N N 35  
A1BRX H15  H  N N 36  
A1BRX H14  H  N N 37  
A1BRX H12  H  N N 38  
ALA   N    N  N N 39  
ALA   CA   C  N S 40  
ALA   C    C  N N 41  
ALA   O    O  N N 42  
ALA   CB   C  N N 43  
ALA   OXT  O  N N 44  
ALA   H    H  N N 45  
ALA   H2   H  N N 46  
ALA   HA   H  N N 47  
ALA   HB1  H  N N 48  
ALA   HB2  H  N N 49  
ALA   HB3  H  N N 50  
ALA   HXT  H  N N 51  
ARG   N    N  N N 52  
ARG   CA   C  N S 53  
ARG   C    C  N N 54  
ARG   O    O  N N 55  
ARG   CB   C  N N 56  
ARG   CG   C  N N 57  
ARG   CD   C  N N 58  
ARG   NE   N  N N 59  
ARG   CZ   C  N N 60  
ARG   NH1  N  N N 61  
ARG   NH2  N  N N 62  
ARG   OXT  O  N N 63  
ARG   H    H  N N 64  
ARG   H2   H  N N 65  
ARG   HA   H  N N 66  
ARG   HB2  H  N N 67  
ARG   HB3  H  N N 68  
ARG   HG2  H  N N 69  
ARG   HG3  H  N N 70  
ARG   HD2  H  N N 71  
ARG   HD3  H  N N 72  
ARG   HE   H  N N 73  
ARG   HH11 H  N N 74  
ARG   HH12 H  N N 75  
ARG   HH21 H  N N 76  
ARG   HH22 H  N N 77  
ARG   HXT  H  N N 78  
ASN   N    N  N N 79  
ASN   CA   C  N S 80  
ASN   C    C  N N 81  
ASN   O    O  N N 82  
ASN   CB   C  N N 83  
ASN   CG   C  N N 84  
ASN   OD1  O  N N 85  
ASN   ND2  N  N N 86  
ASN   OXT  O  N N 87  
ASN   H    H  N N 88  
ASN   H2   H  N N 89  
ASN   HA   H  N N 90  
ASN   HB2  H  N N 91  
ASN   HB3  H  N N 92  
ASN   HD21 H  N N 93  
ASN   HD22 H  N N 94  
ASN   HXT  H  N N 95  
ASP   N    N  N N 96  
ASP   CA   C  N S 97  
ASP   C    C  N N 98  
ASP   O    O  N N 99  
ASP   CB   C  N N 100 
ASP   CG   C  N N 101 
ASP   OD1  O  N N 102 
ASP   OD2  O  N N 103 
ASP   OXT  O  N N 104 
ASP   H    H  N N 105 
ASP   H2   H  N N 106 
ASP   HA   H  N N 107 
ASP   HB2  H  N N 108 
ASP   HB3  H  N N 109 
ASP   HD2  H  N N 110 
ASP   HXT  H  N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
DMS   S    S  N N 126 
DMS   O    O  N N 127 
DMS   C1   C  N N 128 
DMS   C2   C  N N 129 
DMS   H11  H  N N 130 
DMS   H12  H  N N 131 
DMS   H13  H  N N 132 
DMS   H21  H  N N 133 
DMS   H22  H  N N 134 
DMS   H23  H  N N 135 
GLN   N    N  N N 136 
GLN   CA   C  N S 137 
GLN   C    C  N N 138 
GLN   O    O  N N 139 
GLN   CB   C  N N 140 
GLN   CG   C  N N 141 
GLN   CD   C  N N 142 
GLN   OE1  O  N N 143 
GLN   NE2  N  N N 144 
GLN   OXT  O  N N 145 
GLN   H    H  N N 146 
GLN   H2   H  N N 147 
GLN   HA   H  N N 148 
GLN   HB2  H  N N 149 
GLN   HB3  H  N N 150 
GLN   HG2  H  N N 151 
GLN   HG3  H  N N 152 
GLN   HE21 H  N N 153 
GLN   HE22 H  N N 154 
GLN   HXT  H  N N 155 
GLU   N    N  N N 156 
GLU   CA   C  N S 157 
GLU   C    C  N N 158 
GLU   O    O  N N 159 
GLU   CB   C  N N 160 
GLU   CG   C  N N 161 
GLU   CD   C  N N 162 
GLU   OE1  O  N N 163 
GLU   OE2  O  N N 164 
GLU   OXT  O  N N 165 
GLU   H    H  N N 166 
GLU   H2   H  N N 167 
GLU   HA   H  N N 168 
GLU   HB2  H  N N 169 
GLU   HB3  H  N N 170 
GLU   HG2  H  N N 171 
GLU   HG3  H  N N 172 
GLU   HE2  H  N N 173 
GLU   HXT  H  N N 174 
GLY   N    N  N N 175 
GLY   CA   C  N N 176 
GLY   C    C  N N 177 
GLY   O    O  N N 178 
GLY   OXT  O  N N 179 
GLY   H    H  N N 180 
GLY   H2   H  N N 181 
GLY   HA2  H  N N 182 
GLY   HA3  H  N N 183 
GLY   HXT  H  N N 184 
HIS   N    N  N N 185 
HIS   CA   C  N S 186 
HIS   C    C  N N 187 
HIS   O    O  N N 188 
HIS   CB   C  N N 189 
HIS   CG   C  Y N 190 
HIS   ND1  N  Y N 191 
HIS   CD2  C  Y N 192 
HIS   CE1  C  Y N 193 
HIS   NE2  N  Y N 194 
HIS   OXT  O  N N 195 
HIS   H    H  N N 196 
HIS   H2   H  N N 197 
HIS   HA   H  N N 198 
HIS   HB2  H  N N 199 
HIS   HB3  H  N N 200 
HIS   HD1  H  N N 201 
HIS   HD2  H  N N 202 
HIS   HE1  H  N N 203 
HIS   HE2  H  N N 204 
HIS   HXT  H  N N 205 
HOH   O    O  N N 206 
HOH   H1   H  N N 207 
HOH   H2   H  N N 208 
ILE   N    N  N N 209 
ILE   CA   C  N S 210 
ILE   C    C  N N 211 
ILE   O    O  N N 212 
ILE   CB   C  N S 213 
ILE   CG1  C  N N 214 
ILE   CG2  C  N N 215 
ILE   CD1  C  N N 216 
ILE   OXT  O  N N 217 
ILE   H    H  N N 218 
ILE   H2   H  N N 219 
ILE   HA   H  N N 220 
ILE   HB   H  N N 221 
ILE   HG12 H  N N 222 
ILE   HG13 H  N N 223 
ILE   HG21 H  N N 224 
ILE   HG22 H  N N 225 
ILE   HG23 H  N N 226 
ILE   HD11 H  N N 227 
ILE   HD12 H  N N 228 
ILE   HD13 H  N N 229 
ILE   HXT  H  N N 230 
LEU   N    N  N N 231 
LEU   CA   C  N S 232 
LEU   C    C  N N 233 
LEU   O    O  N N 234 
LEU   CB   C  N N 235 
LEU   CG   C  N N 236 
LEU   CD1  C  N N 237 
LEU   CD2  C  N N 238 
LEU   OXT  O  N N 239 
LEU   H    H  N N 240 
LEU   H2   H  N N 241 
LEU   HA   H  N N 242 
LEU   HB2  H  N N 243 
LEU   HB3  H  N N 244 
LEU   HG   H  N N 245 
LEU   HD11 H  N N 246 
LEU   HD12 H  N N 247 
LEU   HD13 H  N N 248 
LEU   HD21 H  N N 249 
LEU   HD22 H  N N 250 
LEU   HD23 H  N N 251 
LEU   HXT  H  N N 252 
LYS   N    N  N N 253 
LYS   CA   C  N S 254 
LYS   C    C  N N 255 
LYS   O    O  N N 256 
LYS   CB   C  N N 257 
LYS   CG   C  N N 258 
LYS   CD   C  N N 259 
LYS   CE   C  N N 260 
LYS   NZ   N  N N 261 
LYS   OXT  O  N N 262 
LYS   H    H  N N 263 
LYS   H2   H  N N 264 
LYS   HA   H  N N 265 
LYS   HB2  H  N N 266 
LYS   HB3  H  N N 267 
LYS   HG2  H  N N 268 
LYS   HG3  H  N N 269 
LYS   HD2  H  N N 270 
LYS   HD3  H  N N 271 
LYS   HE2  H  N N 272 
LYS   HE3  H  N N 273 
LYS   HZ1  H  N N 274 
LYS   HZ2  H  N N 275 
LYS   HZ3  H  N N 276 
LYS   HXT  H  N N 277 
MET   N    N  N N 278 
MET   CA   C  N S 279 
MET   C    C  N N 280 
MET   O    O  N N 281 
MET   CB   C  N N 282 
MET   CG   C  N N 283 
MET   SD   S  N N 284 
MET   CE   C  N N 285 
MET   OXT  O  N N 286 
MET   H    H  N N 287 
MET   H2   H  N N 288 
MET   HA   H  N N 289 
MET   HB2  H  N N 290 
MET   HB3  H  N N 291 
MET   HG2  H  N N 292 
MET   HG3  H  N N 293 
MET   HE1  H  N N 294 
MET   HE2  H  N N 295 
MET   HE3  H  N N 296 
MET   HXT  H  N N 297 
PHE   N    N  N N 298 
PHE   CA   C  N S 299 
PHE   C    C  N N 300 
PHE   O    O  N N 301 
PHE   CB   C  N N 302 
PHE   CG   C  Y N 303 
PHE   CD1  C  Y N 304 
PHE   CD2  C  Y N 305 
PHE   CE1  C  Y N 306 
PHE   CE2  C  Y N 307 
PHE   CZ   C  Y N 308 
PHE   OXT  O  N N 309 
PHE   H    H  N N 310 
PHE   H2   H  N N 311 
PHE   HA   H  N N 312 
PHE   HB2  H  N N 313 
PHE   HB3  H  N N 314 
PHE   HD1  H  N N 315 
PHE   HD2  H  N N 316 
PHE   HE1  H  N N 317 
PHE   HE2  H  N N 318 
PHE   HZ   H  N N 319 
PHE   HXT  H  N N 320 
PRO   N    N  N N 321 
PRO   CA   C  N S 322 
PRO   C    C  N N 323 
PRO   O    O  N N 324 
PRO   CB   C  N N 325 
PRO   CG   C  N N 326 
PRO   CD   C  N N 327 
PRO   OXT  O  N N 328 
PRO   H    H  N N 329 
PRO   HA   H  N N 330 
PRO   HB2  H  N N 331 
PRO   HB3  H  N N 332 
PRO   HG2  H  N N 333 
PRO   HG3  H  N N 334 
PRO   HD2  H  N N 335 
PRO   HD3  H  N N 336 
PRO   HXT  H  N N 337 
SER   N    N  N N 338 
SER   CA   C  N S 339 
SER   C    C  N N 340 
SER   O    O  N N 341 
SER   CB   C  N N 342 
SER   OG   O  N N 343 
SER   OXT  O  N N 344 
SER   H    H  N N 345 
SER   H2   H  N N 346 
SER   HA   H  N N 347 
SER   HB2  H  N N 348 
SER   HB3  H  N N 349 
SER   HG   H  N N 350 
SER   HXT  H  N N 351 
THR   N    N  N N 352 
THR   CA   C  N S 353 
THR   C    C  N N 354 
THR   O    O  N N 355 
THR   CB   C  N R 356 
THR   OG1  O  N N 357 
THR   CG2  C  N N 358 
THR   OXT  O  N N 359 
THR   H    H  N N 360 
THR   H2   H  N N 361 
THR   HA   H  N N 362 
THR   HB   H  N N 363 
THR   HG1  H  N N 364 
THR   HG21 H  N N 365 
THR   HG22 H  N N 366 
THR   HG23 H  N N 367 
THR   HXT  H  N N 368 
TRP   N    N  N N 369 
TRP   CA   C  N S 370 
TRP   C    C  N N 371 
TRP   O    O  N N 372 
TRP   CB   C  N N 373 
TRP   CG   C  Y N 374 
TRP   CD1  C  Y N 375 
TRP   CD2  C  Y N 376 
TRP   NE1  N  Y N 377 
TRP   CE2  C  Y N 378 
TRP   CE3  C  Y N 379 
TRP   CZ2  C  Y N 380 
TRP   CZ3  C  Y N 381 
TRP   CH2  C  Y N 382 
TRP   OXT  O  N N 383 
TRP   H    H  N N 384 
TRP   H2   H  N N 385 
TRP   HA   H  N N 386 
TRP   HB2  H  N N 387 
TRP   HB3  H  N N 388 
TRP   HD1  H  N N 389 
TRP   HE1  H  N N 390 
TRP   HE3  H  N N 391 
TRP   HZ2  H  N N 392 
TRP   HZ3  H  N N 393 
TRP   HH2  H  N N 394 
TRP   HXT  H  N N 395 
TYR   N    N  N N 396 
TYR   CA   C  N S 397 
TYR   C    C  N N 398 
TYR   O    O  N N 399 
TYR   CB   C  N N 400 
TYR   CG   C  Y N 401 
TYR   CD1  C  Y N 402 
TYR   CD2  C  Y N 403 
TYR   CE1  C  Y N 404 
TYR   CE2  C  Y N 405 
TYR   CZ   C  Y N 406 
TYR   OH   O  N N 407 
TYR   OXT  O  N N 408 
TYR   H    H  N N 409 
TYR   H2   H  N N 410 
TYR   HA   H  N N 411 
TYR   HB2  H  N N 412 
TYR   HB3  H  N N 413 
TYR   HD1  H  N N 414 
TYR   HD2  H  N N 415 
TYR   HE1  H  N N 416 
TYR   HE2  H  N N 417 
TYR   HH   H  N N 418 
TYR   HXT  H  N N 419 
VAL   N    N  N N 420 
VAL   CA   C  N S 421 
VAL   C    C  N N 422 
VAL   O    O  N N 423 
VAL   CB   C  N N 424 
VAL   CG1  C  N N 425 
VAL   CG2  C  N N 426 
VAL   OXT  O  N N 427 
VAL   H    H  N N 428 
VAL   H2   H  N N 429 
VAL   HA   H  N N 430 
VAL   HB   H  N N 431 
VAL   HG11 H  N N 432 
VAL   HG12 H  N N 433 
VAL   HG13 H  N N 434 
VAL   HG21 H  N N 435 
VAL   HG22 H  N N 436 
VAL   HG23 H  N N 437 
VAL   HXT  H  N N 438 
ZN    ZN   ZN N N 439 
# 
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 
A1BRX N   C    sing N N 1   
A1BRX C   O    doub N N 2   
A1BRX C1  C    sing N N 3   
A1BRX C2  C1   sing N N 4   
A1BRX C2  C3   sing N N 5   
A1BRX C3  C4   sing N N 6   
A1BRX C4  C5   sing N N 7   
A1BRX C5  N1   sing N N 8   
A1BRX C6  N1   sing N N 9   
A1BRX C6  N2   doub Y N 10  
A1BRX N2  C7   sing Y N 11  
A1BRX C7  N3   doub Y N 12  
A1BRX N3  C8   sing Y N 13  
A1BRX C8  C9   doub Y N 14  
A1BRX C9  C10  sing Y N 15  
A1BRX C10 C11  doub Y N 16  
A1BRX C11 C12  sing Y N 17  
A1BRX C12 C13  doub Y N 18  
A1BRX C13 C6   sing Y N 19  
A1BRX C8  C13  sing Y N 20  
A1BRX N1  C14  sing N N 21  
A1BRX C14 C2   sing N N 22  
A1BRX C4  H7   sing N N 23  
A1BRX C4  H8   sing N N 24  
A1BRX C5  H10  sing N N 25  
A1BRX C5  H9   sing N N 26  
A1BRX C7  H11  sing N N 27  
A1BRX C10 H13  sing N N 28  
A1BRX N   H1   sing N N 29  
A1BRX N   H2   sing N N 30  
A1BRX C1  H4   sing N N 31  
A1BRX C1  H3   sing N N 32  
A1BRX C2  H    sing N N 33  
A1BRX C14 H16  sing N N 34  
A1BRX C14 H17  sing N N 35  
A1BRX C3  H6   sing N N 36  
A1BRX C3  H5   sing N N 37  
A1BRX C12 H15  sing N N 38  
A1BRX C11 H14  sing N N 39  
A1BRX C9  H12  sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
DMS   S   O    doub N N 123 
DMS   S   C1   sing N N 124 
DMS   S   C2   sing N N 125 
DMS   C1  H11  sing N N 126 
DMS   C1  H12  sing N N 127 
DMS   C1  H13  sing N N 128 
DMS   C2  H21  sing N N 129 
DMS   C2  H22  sing N N 130 
DMS   C2  H23  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_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                    7HYD 
_atom_sites.fract_transf_matrix[1][1]   0.011545 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000923 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017538 
_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]   0.015474 
_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   ? 17.797 7.997   24.810 1.00 16.43  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.019 8.135   23.993 1.00 16.50  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.140 6.910   23.071 1.00 15.85  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.440 5.904   23.266 1.00 17.29  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.240 8.190   24.914 1.00 19.28  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.310 6.958   25.618 1.00 22.39  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.067 6.984   22.112 1.00 14.17  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.291 5.875   21.193 1.00 13.68  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.715 6.361   19.820 1.00 13.37  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.391 7.477   19.419 1.00 15.08  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.404 5.494   19.095 1.00 12.27  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.877 5.862   17.770 1.00 13.15  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.827 4.641   16.860 1.00 12.16  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.724 3.499   17.323 1.00 12.88  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.317 6.373   17.894 1.00 14.29  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.926 4.873   15.546 1.00 12.10  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.107 3.816   14.546 1.00 11.57  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.584 3.909   14.148 1.00 12.29  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.089 5.024   13.862 1.00 12.75  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.230 4.039   13.281 1.00 11.94  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.746 4.195   13.616 1.00 13.56  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.429 2.881   12.279 1.00 12.97  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.958 4.796   12.414 1.00 15.34  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.286 2.752   14.107 1.00 12.91  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.682 2.763   13.697 1.00 13.93  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.785 1.932   12.419 1.00 14.69  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.747 0.693   12.488 1.00 14.75  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.573 2.165   14.812 1.00 14.70  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.616 3.053   16.032 1.00 14.69  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.486 4.131   16.103 1.00 15.29  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.789 2.814   17.121 1.00 15.95  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.491 4.987   17.200 1.00 16.22  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.809 3.645   18.240 1.00 17.00  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.654 4.741   18.266 1.00 17.70  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.660 5.610   19.353 1.00 19.74  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.856 2.612   11.260 1.00 14.36  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.917 1.966   9.960  1.00 14.81  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.149 2.449   9.231  1.00 15.94  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.378 3.667   9.159  1.00 15.33  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.613 2.221   9.139  1.00 16.22  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.285 3.711   9.021  1.00 17.26  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.730 1.587   7.758  1.00 17.97  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.010 1.524   8.763  1.00 16.77  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.268 1.946   8.132  1.00 16.93  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.091 2.837   9.050  1.00 17.19  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.209 2.551   10.249 1.00 17.08  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.543 3.982   8.526  1.00 15.47  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.246 4.968   9.355  1.00 14.87  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.352 6.154   9.690  1.00 14.84  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.822 7.301   9.813  1.00 15.99  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.576 5.414   8.761  1.00 16.82  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.652 4.360   8.892  1.00 21.52  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.392 4.295   9.887  1.00 24.02  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.730 3.496   7.912  1.00 20.81  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.053 5.859   9.915  1.00 13.72  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.094 6.902   10.296 1.00 13.48  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.434 6.596   11.634 1.00 13.15  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.164 5.407   11.942 1.00 13.61  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.962 7.003   9.241  1.00 14.29  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.454 7.413   7.865  1.00 15.65  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.098 8.632   7.663  1.00 16.32  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.296 6.572   6.774  1.00 16.74  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.605 8.983   6.412  1.00 17.02  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.746 6.940   5.512  1.00 17.48  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.361 8.161   5.326  1.00 18.65  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.847 8.513   4.077  1.00 22.26  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.120 7.656   12.381 1.00 12.16  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.331 7.568   13.617 1.00 12.36  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.098 8.438   13.379 1.00 12.45  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.257 9.636   13.103 1.00 13.37  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.139 8.113   14.828 1.00 12.99  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.327 8.428   16.096 1.00 13.78  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.269 8.796   17.252 1.00 14.82  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.741 9.866   18.106 1.00 16.47  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.069 9.659   19.238 1.00 18.38  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.828 8.420   19.660 1.00 18.25  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.641 10.688  19.957 1.00 18.67  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.890 7.839   13.415 1.00 11.68  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.621 8.569   13.194 1.00 11.75  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.953 8.764   14.530 1.00 12.22  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.655 7.777   15.215 1.00 12.59  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.672 7.792   12.266 1.00 12.91  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.457 8.660   11.883 1.00 14.25  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.401 7.271   11.022 1.00 12.93  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.729 10.039  14.909 1.00 11.96  ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.103 10.354  16.197 0.50 12.19  ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.170 10.400  16.216 0.50 14.20  ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.992 11.369  16.018 1.00 13.26  ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.863 12.017  14.943 1.00 13.96  ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.139 10.920  17.218 0.50 10.99  ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.271 11.128  17.085 0.50 17.12  ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 23.092 9.862   17.695 0.50 11.55  ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.903 11.202  18.550 0.50 17.47  ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.854 12.180  16.673 0.50 8.26   ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.654 10.532  16.932 0.50 18.82  ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.158 11.558  17.090 1.00 12.30  ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.145 12.614  17.028 1.00 12.13  ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.944 13.944  17.036 1.00 12.73  ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.883 14.111  17.846 1.00 12.81  ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.310 12.593  18.315 1.00 11.16  ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.445 11.363  18.402 1.00 12.38  ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.851 10.340  19.001 1.00 13.14  ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.250 11.417  17.792 1.00 12.47  ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.583 14.885  16.160 1.00 12.23  ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.359 16.161  16.117 1.00 12.30  ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.330 16.853  17.486 1.00 14.17  ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.349 17.392  17.948 1.00 15.95  ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.765 17.070  15.066 1.00 13.66  ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.557 18.385  14.833 1.00 15.05  ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.788 19.256  13.839 1.00 16.31  ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.526 20.443  13.376 1.00 17.22  ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.503 21.616  14.005 1.00 19.88  ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.913 21.730  15.194 1.00 18.78  ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 20.108 22.684  13.467 1.00 19.83  ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.177 16.739  18.185 1.00 12.79  ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 18.040 17.431  19.473 1.00 15.40  ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.896 16.821  20.602 1.00 16.13  ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 19.052 17.465  21.661 1.00 17.66  ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.560 17.602  19.903 1.00 16.27  ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.889 16.363  20.394 1.00 16.05  ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.258 15.485  19.520 1.00 16.65  ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.726 15.915  21.662 1.00 17.51  ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.739 14.521  20.289 1.00 16.84  ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 14.999 14.740  21.580 1.00 17.94  ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.429 15.603  20.394 1.00 16.33  ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.293 14.916  21.362 1.00 15.54  ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.768 14.858  20.900 1.00 16.60  ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.597 14.246  21.577 1.00 17.37  ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.762 13.520  21.676 1.00 15.33  ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.358 13.511  22.291 1.00 16.13  ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.936 12.070  22.538 1.00 16.80  ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.340 14.286  23.631 1.00 17.80  ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 22.109 15.489  19.740 1.00 15.55  ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.475 15.464  19.258 1.00 15.97  ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.454 16.091  20.250 1.00 16.64  ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 24.131 17.102  20.907 1.00 17.22  ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.564 16.184  17.910 1.00 15.19  ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.642 15.488  20.364 1.00 16.49  ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.693 15.982  21.272 1.00 16.22  ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.592 16.991  20.560 1.00 17.13  ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.528 17.131  19.328 1.00 15.85  ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.562 14.791  21.750 1.00 18.55  ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.276 14.267  20.620 1.00 18.91  ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.753 13.682  22.425 1.00 18.74  ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.522 17.664  21.309 1.00 16.73  ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.489 18.549  20.678 1.00 17.61  ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.347 17.731  19.685 1.00 17.07  ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.651 18.214  18.591 1.00 17.16  ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.423 19.220  21.724 1.00 20.78  ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.640 19.873  21.101 1.00 28.63  ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.555 21.106  20.461 1.00 32.82  ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.907 19.397  20.956 1.00 32.41  ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.775 21.384  20.030 1.00 33.51  ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.626 20.374  20.272 1.00 34.64  ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.715 16.469  20.058 1.00 15.41  ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.549 15.677  19.150 1.00 16.39  ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.779 15.383  17.857 1.00 16.31  ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.362 15.431  16.782 1.00 16.88  ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 32.005 14.358  19.790 1.00 18.73  ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.974 13.621  18.890 1.00 27.26  ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.135 14.045  18.710 1.00 29.83  ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.506 12.537  18.245 1.00 28.70  ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.437 15.169  17.952 1.00 14.70  ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.654 14.962  16.732 1.00 14.02  ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.727 16.226  15.835 1.00 13.89  ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.942 16.102  14.631 1.00 14.70  ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.182 14.686  17.052 1.00 15.06  ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.948 13.325  17.652 1.00 17.05  ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.582 12.357  17.180 1.00 16.28  ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 26.097 13.221  18.591 1.00 16.94  ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.504 17.427  16.410 1.00 13.80  ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.543 18.653  15.604 1.00 13.85  ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.949 18.914  15.046 1.00 14.56  ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.069 19.478  13.945 1.00 15.27  ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 28.070 19.847  16.469 1.00 14.25  ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.571 19.917  16.598 1.00 13.95  ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.813 19.586  17.685 1.00 15.87  ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.650 20.380  15.593 1.00 15.54  ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.472 19.845  17.431 1.00 15.74  ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.351 20.327  16.144 1.00 15.87  ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.808 20.837  14.278 1.00 16.97  ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.214 20.702  15.398 1.00 16.65  ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.699 21.193  13.554 1.00 17.15  ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.435 21.185  14.117 1.00 17.39  ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 31.012 18.504  15.780 1.00 14.25  ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.393 18.709  15.323 1.00 15.50  ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.829 17.713  14.249 1.00 16.88  ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.854 17.913  13.614 1.00 17.59  ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.339 18.662  16.521 1.00 15.62  ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 32.025 16.640  14.027 1.00 15.39  ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.294 15.601  13.019 1.00 14.70  ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 31.018 15.409  12.172 1.00 14.33  ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.651 14.285  11.806 1.00 14.50  ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.680 14.282  13.731 1.00 15.92  ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 34.021 14.441  14.399 1.00 18.16  ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.044 14.382  13.736 1.00 20.76  ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 34.039 14.752  15.701 1.00 18.05  ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.354 16.507  11.841 1.00 13.52  ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.064 16.497  11.161 1.00 13.53  ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.151 16.054  9.711  1.00 15.29  ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 30.013 16.530  8.954  1.00 16.40  ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.492 17.935  11.198 1.00 14.12  ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.105 18.082  10.623 1.00 14.89  ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.096 17.325  11.456 1.00 14.52  ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.671 19.552  10.572 1.00 17.05  ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.201 15.188  9.302  1.00 14.89  ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.058 14.773  7.913  1.00 14.71  ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.812 15.477  7.317  1.00 14.39  ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.874 16.038  6.220  1.00 15.92  ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.930 13.231  7.810  1.00 14.91  ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.566 12.804  6.378  1.00 16.19  ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.237 12.558  8.271  1.00 15.32  ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.673 15.437  8.050  1.00 14.22  ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.404 15.984  7.565  1.00 13.84  ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.445 16.197  8.721  1.00 14.01  ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.479 15.424  9.698  1.00 13.19  ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.782 14.984  6.546  1.00 14.98  ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.372 15.254  6.093  1.00 16.48  ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.973 16.127  5.121  1.00 18.60  ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.170 14.636  6.596  1.00 16.14  ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.596 16.076  4.974  1.00 18.79  ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.085 15.150  5.854  1.00 17.49  ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.911 13.685  7.584  1.00 16.45  ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.754 14.734  6.075  1.00 18.00  ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.605 13.262  7.779  1.00 17.29  ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.542 13.795  7.046  1.00 18.21  ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.604 17.244  8.637  1.00 14.74  ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.601 17.432  9.668  1.00 14.70  ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.368 18.070  9.043  1.00 16.30  ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.476 18.873  8.102  1.00 17.05  ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.122 18.283  10.833 1.00 15.88  ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.729 19.639  10.459 1.00 17.76  ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.771 20.811  10.281 1.00 20.84  ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.113 21.778  9.549  1.00 20.97  ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.666 20.775  10.868 1.00 18.95  ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.196 17.774  9.598  1.00 15.65  ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.952 18.342  9.088  1.00 15.11  ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.980 18.515  10.262 1.00 15.51  ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.495 17.526  10.821 1.00 15.58  ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.362 17.398  8.022  1.00 17.26  ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.120 17.938  7.370  1.00 21.80  ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.305 18.553  8.076  1.00 25.16  ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.950 17.722  6.163  1.00 24.80  ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.783 19.768  10.694 1.00 15.95  ? 36  SER   A N   1 
ATOM   245  C  CA  . SER   A 1 30  ? 15.917 20.096  11.819 1.00 16.72  ? 36  SER   A CA  1 
ATOM   246  C  C   . SER   A 1 30  ? 14.473 19.658  11.554 1.00 17.49  ? 36  SER   A C   1 
ATOM   247  O  O   . SER   A 1 30  ? 13.819 19.165  12.483 1.00 18.21  ? 36  SER   A O   1 
ATOM   248  C  CB  . SER   A 1 30  ? 15.994 21.595  12.108 1.00 19.35  ? 36  SER   A CB  1 
ATOM   249  O  OG  . SER   A 1 30  ? 15.043 21.951  13.095 1.00 23.98  ? 36  SER   A OG  1 
ATOM   250  N  N   . SER   A 1 31  ? 13.978 19.818  10.312 1.00 17.58  ? 37  SER   A N   1 
ATOM   251  C  CA  . SER   A 1 31  ? 12.589 19.405  10.017 1.00 17.94  ? 37  SER   A CA  1 
ATOM   252  C  C   . SER   A 1 31  ? 12.351 17.908  10.223 1.00 17.55  ? 37  SER   A C   1 
ATOM   253  O  O   . SER   A 1 31  ? 11.204 17.524  10.450 1.00 18.89  ? 37  SER   A O   1 
ATOM   254  C  CB  . SER   A 1 31  ? 12.158 19.797  8.605  1.00 20.79  ? 37  SER   A CB  1 
ATOM   255  O  OG  . SER   A 1 31  ? 12.758 18.984  7.612  1.00 25.54  ? 37  SER   A OG  1 
ATOM   256  N  N   . ARG   A 1 32  ? 13.407 17.086  10.161 1.00 15.37  ? 38  ARG   A N   1 
ATOM   257  C  CA  . ARG   A 1 32  ? 13.315 15.625  10.358 1.00 15.02  ? 38  ARG   A CA  1 
ATOM   258  C  C   . ARG   A 1 32  ? 13.798 15.161  11.751 1.00 15.26  ? 38  ARG   A C   1 
ATOM   259  O  O   . ARG   A 1 32  ? 13.697 13.956  12.067 1.00 15.00  ? 38  ARG   A O   1 
ATOM   260  C  CB  . ARG   A 1 32  ? 14.187 14.908  9.304  1.00 15.44  ? 38  ARG   A CB  1 
ATOM   261  C  CG  . ARG   A 1 32  ? 13.674 15.105  7.877  1.00 17.88  ? 38  ARG   A CG  1 
ATOM   262  C  CD  . ARG   A 1 32  ? 14.552 14.407  6.863  1.00 16.87  ? 38  ARG   A CD  1 
ATOM   263  N  NE  . ARG   A 1 32  ? 14.410 12.960  6.989  1.00 14.73  ? 38  ARG   A NE  1 
ATOM   264  C  CZ  . ARG   A 1 32  ? 14.557 12.104  5.987  1.00 16.06  ? 38  ARG   A CZ  1 
ATOM   265  N  NH1 . ARG   A 1 32  ? 14.809 12.550  4.749  1.00 17.89  ? 38  ARG   A NH1 1 
ATOM   266  N  NH2 . ARG   A 1 32  ? 14.400 10.790  6.196  1.00 14.89  ? 38  ARG   A NH2 1 
ATOM   267  N  N   . ASP   A 1 33  ? 14.380 16.083  12.561 1.00 14.34  ? 39  ASP   A N   1 
ATOM   268  C  CA  . ASP   A 1 33  ? 14.997 15.739  13.835 1.00 13.52  ? 39  ASP   A CA  1 
ATOM   269  C  C   . ASP   A 1 33  ? 16.119 14.720  13.669 1.00 12.54  ? 39  ASP   A C   1 
ATOM   270  O  O   . ASP   A 1 33  ? 16.339 13.863  14.539 1.00 13.17  ? 39  ASP   A O   1 
ATOM   271  C  CB  . ASP   A 1 33  ? 13.973 15.263  14.895 1.00 13.64  ? 39  ASP   A CB  1 
ATOM   272  C  CG  . ASP   A 1 33  ? 14.602 15.031  16.269 1.00 15.17  ? 39  ASP   A CG  1 
ATOM   273  O  OD1 . ASP   A 1 33  ? 15.443 15.853  16.692 1.00 15.17  ? 39  ASP   A OD1 1 
ATOM   274  O  OD2 . ASP   A 1 33  ? 14.239 14.038  16.942 1.00 15.33  ? 39  ASP   A OD2 1 
ATOM   275  N  N   . LEU   A 1 34  ? 16.901 14.857  12.576 1.00 12.05  ? 40  LEU   A N   1 
ATOM   276  C  CA  . LEU   A 1 34  ? 17.998 13.916  12.341 1.00 11.74  ? 40  LEU   A CA  1 
ATOM   277  C  C   . LEU   A 1 34  ? 19.363 14.607  12.216 1.00 12.00  ? 40  LEU   A C   1 
ATOM   278  O  O   . LEU   A 1 34  ? 19.453 15.707  11.660 1.00 12.86  ? 40  LEU   A O   1 
ATOM   279  C  CB  . LEU   A 1 34  ? 17.775 13.101  11.085 1.00 13.08  ? 40  LEU   A CB  1 
ATOM   280  C  CG  . LEU   A 1 34  ? 16.688 11.998  11.144 1.00 14.37  ? 40  LEU   A CG  1 
ATOM   281  C  CD1 . LEU   A 1 34  ? 16.600 11.264  9.807  1.00 14.45  ? 40  LEU   A CD1 1 
ATOM   282  C  CD2 . LEU   A 1 34  ? 16.966 10.983  12.278 1.00 14.21  ? 40  LEU   A CD2 1 
ATOM   283  N  N   . LEU   A 1 35  ? 20.410 13.933  12.690 1.00 11.75  ? 41  LEU   A N   1 
ATOM   284  C  CA  . LEU   A 1 35  ? 21.797 14.395  12.526 1.00 11.98  ? 41  LEU   A CA  1 
ATOM   285  C  C   . LEU   A 1 35  ? 22.637 13.159  12.371 1.00 12.86  ? 41  LEU   A C   1 
ATOM   286  O  O   . LEU   A 1 35  ? 22.417 12.131  13.037 1.00 12.39  ? 41  LEU   A O   1 
ATOM   287  C  CB  . LEU   A 1 35  ? 22.273 15.231  13.750 1.00 12.31  ? 41  LEU   A CB  1 
ATOM   288  C  CG  . LEU   A 1 35  ? 23.701 15.799  13.641 1.00 13.24  ? 41  LEU   A CG  1 
ATOM   289  C  CD1 . LEU   A 1 35  ? 23.802 17.168  14.327 1.00 14.35  ? 41  LEU   A CD1 1 
ATOM   290  C  CD2 . LEU   A 1 35  ? 24.729 14.851  14.306 1.00 13.90  ? 41  LEU   A CD2 1 
ATOM   291  N  N   . VAL   A 1 36  ? 23.601 13.242  11.431 1.00 12.28  ? 42  VAL   A N   1 
ATOM   292  C  CA  . VAL   A 1 36  ? 24.526 12.154  11.138 1.00 11.76  ? 42  VAL   A CA  1 
ATOM   293  C  C   . VAL   A 1 36  ? 25.939 12.655  11.306 1.00 11.82  ? 42  VAL   A C   1 
ATOM   294  O  O   . VAL   A 1 36  ? 26.261 13.722  10.760 1.00 12.62  ? 42  VAL   A O   1 
ATOM   295  C  CB  . VAL   A 1 36  ? 24.317 11.571  9.724  1.00 12.42  ? 42  VAL   A CB  1 
ATOM   296  C  CG1 . VAL   A 1 36  ? 25.333 10.457  9.463  1.00 13.80  ? 42  VAL   A CG1 1 
ATOM   297  C  CG2 . VAL   A 1 36  ? 22.876 11.034  9.585  1.00 13.49  ? 42  VAL   A CG2 1 
ATOM   298  N  N   . SER   A 1 37  ? 26.768 11.957  12.112 1.00 11.80  ? 43  SER   A N   1 
ATOM   299  C  CA  . SER   A 1 37  ? 28.180 12.318  12.295 1.00 12.42  ? 43  SER   A CA  1 
ATOM   300  C  C   . SER   A 1 37  ? 29.049 11.145  11.834 1.00 13.75  ? 43  SER   A C   1 
ATOM   301  O  O   . SER   A 1 37  ? 28.566 10.020  11.614 1.00 13.65  ? 43  SER   A O   1 
ATOM   302  C  CB  . SER   A 1 37  ? 28.454 12.670  13.751 1.00 13.59  ? 43  SER   A CB  1 
ATOM   303  O  OG  . SER   A 1 37  ? 28.133 11.586  14.603 1.00 14.25  ? 43  SER   A OG  1 
ATOM   304  N  N   . SER   A 1 38  ? 30.348 11.405  11.648 1.00 15.22  ? 44  SER   A N   1 
ATOM   305  C  CA  . SER   A 1 38  ? 31.267 10.352  11.191 1.00 15.86  ? 44  SER   A CA  1 
ATOM   306  C  C   . SER   A 1 38  ? 31.892 9.620   12.383 1.00 17.50  ? 44  SER   A C   1 
ATOM   307  O  O   . SER   A 1 38  ? 32.072 10.225  13.460 1.00 18.67  ? 44  SER   A O   1 
ATOM   308  C  CB  . SER   A 1 38  ? 32.354 10.967  10.315 1.00 17.45  ? 44  SER   A CB  1 
ATOM   309  O  OG  . SER   A 1 38  ? 33.065 11.927  11.088 1.00 19.76  ? 44  SER   A OG  1 
ATOM   310  N  N   . THR   A 1 39  ? 32.207 8.308   12.197 1.00 17.33  ? 45  THR   A N   1 
ATOM   311  C  CA  . THR   A 1 39  ? 32.792 7.500   13.261 1.00 18.98  ? 45  THR   A CA  1 
ATOM   312  C  C   . THR   A 1 39  ? 34.137 6.919   12.823 1.00 21.47  ? 45  THR   A C   1 
ATOM   313  O  O   . THR   A 1 39  ? 34.364 6.705   11.626 1.00 21.30  ? 45  THR   A O   1 
ATOM   314  C  CB  . THR   A 1 39  ? 31.868 6.324   13.631 1.00 19.89  ? 45  THR   A CB  1 
ATOM   315  O  OG1 . THR   A 1 39  ? 31.733 5.432   12.520 1.00 21.09  ? 45  THR   A OG1 1 
ATOM   316  C  CG2 . THR   A 1 39  ? 30.492 6.784   14.090 1.00 19.69  ? 45  THR   A CG2 1 
ATOM   317  N  N   . THR   A 1 40  ? 35.005 6.631   13.802 1.00 22.13  ? 46  THR   A N   1 
ATOM   318  C  CA  . THR   A 1 40  ? 36.286 6.006   13.500 1.00 24.39  ? 46  THR   A CA  1 
ATOM   319  C  C   . THR   A 1 40  ? 36.073 4.499   13.265 1.00 24.61  ? 46  THR   A C   1 
ATOM   320  O  O   . THR   A 1 40  ? 36.634 3.942   12.317 1.00 25.46  ? 46  THR   A O   1 
ATOM   321  C  CB  . THR   A 1 40  ? 37.287 6.293   14.639 1.00 28.40  ? 46  THR   A CB  1 
ATOM   322  O  OG1 . THR   A 1 40  ? 36.778 5.752   15.854 1.00 32.10  ? 46  THR   A OG1 1 
ATOM   323  C  CG2 . THR   A 1 40  ? 37.518 7.779   14.827 1.00 28.88  ? 46  THR   A CG2 1 
ATOM   324  N  N   . ALA   A 1 41  ? 35.243 3.854   14.102 1.00 24.77  ? 47  ALA   A N   1 
ATOM   325  C  CA  . ALA   A 1 41  ? 34.977 2.419   13.935 1.00 25.36  ? 47  ALA   A CA  1 
ATOM   326  C  C   . ALA   A 1 41  ? 33.738 2.151   13.065 1.00 24.57  ? 47  ALA   A C   1 
ATOM   327  O  O   . ALA   A 1 41  ? 32.793 2.944   13.085 1.00 23.97  ? 47  ALA   A O   1 
ATOM   328  C  CB  . ALA   A 1 41  ? 34.753 1.765   15.292 1.00 26.77  ? 47  ALA   A CB  1 
ATOM   329  N  N   . GLN   A 1 42  ? 33.723 1.007   12.356 1.00 23.28  ? 48  GLN   A N   1 
ATOM   330  C  CA  . GLN   A 1 42  ? 32.576 0.618   11.535 1.00 23.35  ? 48  GLN   A CA  1 
ATOM   331  C  C   . GLN   A 1 42  ? 31.486 0.014   12.392 1.00 22.25  ? 48  GLN   A C   1 
ATOM   332  O  O   . GLN   A 1 42  ? 31.762 -0.777  13.306 1.00 23.11  ? 48  GLN   A O   1 
ATOM   333  C  CB  . GLN   A 1 42  ? 32.972 -0.371  10.441 1.00 25.84  ? 48  GLN   A CB  1 
ATOM   334  C  CG  . GLN   A 1 42  ? 33.778 0.268   9.316  1.00 31.07  ? 48  GLN   A CG  1 
ATOM   335  C  CD  . GLN   A 1 42  ? 34.151 -0.757  8.287  1.00 38.57  ? 48  GLN   A CD  1 
ATOM   336  O  OE1 . GLN   A 1 42  ? 35.055 -1.593  8.502  1.00 39.98  ? 48  GLN   A OE1 1 
ATOM   337  N  NE2 . GLN   A 1 42  ? 33.425 -0.749  7.174  1.00 39.79  ? 48  GLN   A NE2 1 
ATOM   338  N  N   . GLY   A 1 43  ? 30.248 0.370   12.065 1.00 19.11  ? 49  GLY   A N   1 
ATOM   339  C  CA  . GLY   A 1 43  ? 29.068 -0.097  12.782 1.00 19.03  ? 49  GLY   A CA  1 
ATOM   340  C  C   . GLY   A 1 43  ? 28.476 -1.344  12.183 1.00 18.61  ? 49  GLY   A C   1 
ATOM   341  O  O   . GLY   A 1 43  ? 28.802 -1.720  11.054 1.00 18.73  ? 49  GLY   A O   1 
ATOM   342  N  N   . CYS   A 1 44  ? 27.567 -1.977  12.958 1.00 17.61  ? 50  CYS   A N   1 
ATOM   343  C  CA  . CYS   A 1 44  ? 26.947 -3.262  12.617 1.00 17.34  ? 50  CYS   A CA  1 
ATOM   344  C  C   . CYS   A 1 44  ? 25.486 -3.210  12.156 1.00 16.68  ? 50  CYS   A C   1 
ATOM   345  O  O   . CYS   A 1 44  ? 24.939 -4.258  11.771 1.00 17.33  ? 50  CYS   A O   1 
ATOM   346  C  CB  . CYS   A 1 44  ? 27.088 -4.225  13.792 1.00 18.58  ? 50  CYS   A CB  1 
ATOM   347  S  SG  . CYS   A 1 44  ? 28.798 -4.674  14.141 1.00 22.70  ? 50  CYS   A SG  1 
ATOM   348  N  N   . ASP   A 1 45  ? 24.835 -2.051  12.280 1.00 14.74  ? 51  ASP   A N   1 
ATOM   349  C  CA  . ASP   A 1 45  ? 23.441 -1.959  11.866 1.00 14.55  ? 51  ASP   A CA  1 
ATOM   350  C  C   . ASP   A 1 45  ? 23.342 -1.895  10.338 1.00 16.76  ? 51  ASP   A C   1 
ATOM   351  O  O   . ASP   A 1 45  ? 24.226 -1.336  9.677  1.00 18.18  ? 51  ASP   A O   1 
ATOM   352  C  CB  . ASP   A 1 45  ? 22.832 -0.701  12.492 1.00 13.66  ? 51  ASP   A CB  1 
ATOM   353  C  CG  . ASP   A 1 45  ? 22.722 -0.763  14.015 1.00 15.54  ? 51  ASP   A CG  1 
ATOM   354  O  OD1 . ASP   A 1 45  ? 22.380 -1.862  14.543 1.00 15.96  ? 51  ASP   A OD1 1 
ATOM   355  O  OD2 . ASP   A 1 45  ? 22.918 0.295   14.686 1.00 15.81  ? 51  ASP   A OD2 1 
ATOM   356  N  N   . THR   A 1 46  ? 22.283 -2.468  9.786  1.00 17.59  ? 52  THR   A N   1 
ATOM   357  C  CA  . THR   A 1 46  ? 21.984 -2.389  8.347  1.00 19.16  ? 52  THR   A CA  1 
ATOM   358  C  C   . THR   A 1 46  ? 20.655 -1.639  8.197  1.00 17.50  ? 52  THR   A C   1 
ATOM   359  O  O   . THR   A 1 46  ? 19.759 -1.810  9.026  1.00 18.05  ? 52  THR   A O   1 
ATOM   360  C  CB  . THR   A 1 46  ? 21.888 -3.751  7.714  1.00 23.67  ? 52  THR   A CB  1 
ATOM   361  O  OG1 . THR   A 1 46  ? 20.880 -4.462  8.392  1.00 27.70  ? 52  THR   A OG1 1 
ATOM   362  C  CG2 . THR   A 1 46  ? 23.223 -4.494  7.824  1.00 25.22  ? 52  THR   A CG2 1 
ATOM   363  N  N   . ILE   A 1 47  ? 20.558 -0.777  7.186  1.00 16.11  ? 53  ILE   A N   1 
ATOM   364  C  CA  . ILE   A 1 47  ? 19.338 -0.022  6.977  1.00 15.28  ? 53  ILE   A CA  1 
ATOM   365  C  C   . ILE   A 1 47  ? 18.366 -0.789  6.082  1.00 16.08  ? 53  ILE   A C   1 
ATOM   366  O  O   . ILE   A 1 47  ? 18.753 -1.325  5.024  1.00 16.62  ? 53  ILE   A O   1 
ATOM   367  C  CB  . ILE   A 1 47  ? 19.654 1.360   6.351  1.00 15.49  ? 53  ILE   A CB  1 
ATOM   368  C  CG1 . ILE   A 1 47  ? 20.778 2.102   7.126  1.00 16.48  ? 53  ILE   A CG1 1 
ATOM   369  C  CG2 . ILE   A 1 47  ? 18.382 2.221   6.237  1.00 14.95  ? 53  ILE   A CG2 1 
ATOM   370  C  CD1 . ILE   A 1 47  ? 20.371 2.452   8.586  1.00 18.02  ? 53  ILE   A CD1 1 
ATOM   371  N  N   . ALA   A 1 48  ? 17.087 -0.786  6.468  1.00 14.24  ? 54  ALA   A N   1 
ATOM   372  C  CA  . ALA   A 1 48  ? 16.017 -1.387  5.667  1.00 14.16  ? 54  ALA   A CA  1 
ATOM   373  C  C   . ALA   A 1 48  ? 15.781 -0.537  4.420  1.00 16.18  ? 54  ALA   A C   1 
ATOM   374  O  O   . ALA   A 1 48  ? 15.777 0.702   4.482  1.00 15.95  ? 54  ALA   A O   1 
ATOM   375  C  CB  . ALA   A 1 48  ? 14.723 -1.413  6.472  1.00 15.09  ? 54  ALA   A CB  1 
ATOM   376  N  N   . ARG   A 1 49  ? 15.543 -1.216  3.264  1.00 17.81  ? 55  ARG   A N   1 
ATOM   377  C  CA  . ARG   A 1 49  ? 15.202 -0.517  2.033  1.00 18.71  ? 55  ARG   A CA  1 
ATOM   378  C  C   . ARG   A 1 49  ? 13.906 -1.193  1.571  1.00 21.09  ? 55  ARG   A C   1 
ATOM   379  O  O   . ARG   A 1 49  ? 13.952 -2.224  0.887  1.00 22.17  ? 55  ARG   A O   1 
ATOM   380  C  CB  . ARG   A 1 49  ? 16.352 -0.644  1.004  1.00 19.38  ? 55  ARG   A CB  1 
ATOM   381  C  CG  . ARG   A 1 49  ? 17.705 -0.090  1.496  1.00 20.14  ? 55  ARG   A CG  1 
ATOM   382  C  CD  . ARG   A 1 49  ? 17.728 1.429   1.798  1.00 18.73  ? 55  ARG   A CD  1 
ATOM   383  N  NE  . ARG   A 1 49  ? 19.051 1.868   2.281  1.00 16.97  ? 55  ARG   A NE  1 
ATOM   384  C  CZ  . ARG   A 1 49  ? 19.266 3.020   2.922  1.00 18.63  ? 55  ARG   A CZ  1 
ATOM   385  N  NH1 . ARG   A 1 49  ? 18.268 3.881   3.114  1.00 18.32  ? 55  ARG   A NH1 1 
ATOM   386  N  NH2 . ARG   A 1 49  ? 20.489 3.328   3.363  1.00 19.35  ? 55  ARG   A NH2 1 
ATOM   387  N  N   . CYS   A 1 50  ? 12.756 -0.632  2.004  1.00 21.00  ? 56  CYS   A N   1 
ATOM   388  C  CA  . CYS   A 1 50  ? 11.429 -1.275  1.874  1.00 21.84  ? 56  CYS   A CA  1 
ATOM   389  C  C   . CYS   A 1 50  ? 10.281 -0.298  2.181  1.00 22.63  ? 56  CYS   A C   1 
ATOM   390  O  O   . CYS   A 1 50  ? 10.511 0.838   2.589  1.00 23.99  ? 56  CYS   A O   1 
ATOM   391  C  CB  . CYS   A 1 50  ? 11.401 -2.423  2.872  1.00 21.51  ? 56  CYS   A CB  1 
ATOM   392  S  SG  . CYS   A 1 50  ? 11.338 -1.831  4.592  1.00 20.88  ? 56  CYS   A SG  1 
ATOM   393  N  N   . ASP   A 1 51  ? 8.988  -0.798  2.096  1.00 24.40  ? 57  ASP   A N   1 
ATOM   394  C  CA  . ASP   A 1 51  ? 7.845  0.018   2.488  1.00 26.10  ? 57  ASP   A CA  1 
ATOM   395  C  C   . ASP   A 1 51  ? 7.055  -0.712  3.593  1.00 24.92  ? 57  ASP   A C   1 
ATOM   396  O  O   . ASP   A 1 51  ? 5.838  -0.530  3.716  1.00 26.04  ? 57  ASP   A O   1 
ATOM   397  C  CB  . ASP   A 1 51  ? 6.918  0.363   1.305  1.00 32.06  ? 57  ASP   A CB  1 
ATOM   398  C  CG  . ASP   A 1 51  ? 6.283  -0.845  0.648  1.00 41.31  ? 57  ASP   A CG  1 
ATOM   399  O  OD1 . ASP   A 1 51  ? 6.670  -1.998  1.003  1.00 42.52  ? 57  ASP   A OD1 1 
ATOM   400  O  OD2 . ASP   A 1 51  ? 5.409  -0.649  -0.233 1.00 45.43  ? 57  ASP   A OD2 1 
ATOM   401  N  N   . CYS   A 1 52  ? 7.747  -1.477  4.461  1.00 21.52  ? 58  CYS   A N   1 
ATOM   402  C  CA  . CYS   A 1 52  ? 7.088  -2.131  5.613  1.00 19.11  ? 58  CYS   A CA  1 
ATOM   403  C  C   . CYS   A 1 52  ? 6.331  -1.099  6.451  1.00 19.92  ? 58  CYS   A C   1 
ATOM   404  O  O   . CYS   A 1 52  ? 6.779  0.038   6.624  1.00 20.08  ? 58  CYS   A O   1 
ATOM   405  C  CB  . CYS   A 1 52  ? 8.106  -2.876  6.487  1.00 18.84  ? 58  CYS   A CB  1 
ATOM   406  S  SG  . CYS   A 1 52  ? 8.784  -4.429  5.804  1.00 20.53  ? 58  CYS   A SG  1 
ATOM   407  N  N   . GLN   A 1 53  ? 5.199  -1.526  6.987  1.00 18.17  ? 59  GLN   A N   1 
ATOM   408  C  CA  . GLN   A 1 53  ? 4.422  -0.755  7.943  1.00 17.60  ? 59  GLN   A CA  1 
ATOM   409  C  C   . GLN   A 1 53  ? 4.216  -1.548  9.239  1.00 15.98  ? 59  GLN   A C   1 
ATOM   410  O  O   . GLN   A 1 53  ? 3.363  -1.186  10.042 1.00 16.91  ? 59  GLN   A O   1 
ATOM   411  C  CB  . GLN   A 1 53  ? 3.060  -0.294  7.403  1.00 21.02  ? 59  GLN   A CB  1 
ATOM   412  C  CG  . GLN   A 1 53  ? 3.150  0.832   6.405  1.00 24.92  ? 59  GLN   A CG  1 
ATOM   413  C  CD  . GLN   A 1 53  ? 1.762  1.368   6.067  1.00 30.06  ? 59  GLN   A CD  1 
ATOM   414  O  OE1 . GLN   A 1 53  ? 1.261  1.181   4.966  1.00 32.72  ? 59  GLN   A OE1 1 
ATOM   415  N  NE2 . GLN   A 1 53  ? 1.083  2.029   7.016  1.00 26.17  ? 59  GLN   A NE2 1 
ATOM   416  N  N   . THR   A 1 54  ? 4.981  -2.651  9.454  1.00 14.79  ? 60  THR   A N   1 
ATOM   417  C  CA  . THR   A 1 54  ? 4.994  -3.375  10.720 1.00 15.13  ? 60  THR   A CA  1 
ATOM   418  C  C   . THR   A 1 54  ? 6.449  -3.639  11.103 1.00 14.37  ? 60  THR   A C   1 
ATOM   419  O  O   . THR   A 1 54  ? 7.308  -3.841  10.230 1.00 15.10  ? 60  THR   A O   1 
ATOM   420  C  CB  . THR   A 1 54  ? 4.225  -4.669  10.704 1.00 18.57  ? 60  THR   A CB  1 
ATOM   421  O  OG1 . THR   A 1 54  ? 4.828  -5.592  9.828  1.00 23.81  ? 60  THR   A OG1 1 
ATOM   422  C  CG2 . THR   A 1 54  ? 2.785  -4.491  10.325 1.00 17.45  ? 60  THR   A CG2 1 
ATOM   423  N  N   . GLY   A 1 55  ? 6.718  -3.555  12.383 1.00 13.02  ? 61  GLY   A N   1 
ATOM   424  C  CA  . GLY   A 1 55  ? 8.084  -3.748  12.863 1.00 12.74  ? 61  GLY   A CA  1 
ATOM   425  C  C   . GLY   A 1 55  ? 8.092  -3.818  14.383 1.00 11.86  ? 61  GLY   A C   1 
ATOM   426  O  O   . GLY   A 1 55  ? 7.056  -4.031  15.009 1.00 12.91  ? 61  GLY   A O   1 
ATOM   427  N  N   . VAL   A 1 56  ? 9.272  -3.612  14.994 1.00 11.09  ? 62  VAL   A N   1 
ATOM   428  C  CA  . VAL   A 1 56  ? 9.441  -3.691  16.438 1.00 10.76  ? 62  VAL   A CA  1 
ATOM   429  C  C   . VAL   A 1 56  ? 10.309 -2.520  16.882 1.00 10.86  ? 62  VAL   A C   1 
ATOM   430  O  O   . VAL   A 1 56  ? 11.293 -2.230  16.194 1.00 11.99  ? 62  VAL   A O   1 
ATOM   431  C  CB  . VAL   A 1 56  ? 10.148 -5.030  16.762 1.00 12.67  ? 62  VAL   A CB  1 
ATOM   432  C  CG1 . VAL   A 1 56  ? 10.522 -5.118  18.235 1.00 14.61  ? 62  VAL   A CG1 1 
ATOM   433  C  CG2 . VAL   A 1 56  ? 9.246  -6.219  16.368 1.00 13.35  ? 62  VAL   A CG2 1 
ATOM   434  N  N   . TYR   A 1 57  ? 9.940  -1.812  17.961 1.00 10.28  ? 63  TYR   A N   1 
ATOM   435  C  CA  . TYR   A 1 57  ? 10.804 -0.721  18.418 1.00 10.62  ? 63  TYR   A CA  1 
ATOM   436  C  C   . TYR   A 1 57  ? 11.241 -0.933  19.871 1.00 11.23  ? 63  TYR   A C   1 
ATOM   437  O  O   . TYR   A 1 57  ? 10.538 -1.586  20.651 1.00 11.91  ? 63  TYR   A O   1 
ATOM   438  C  CB  . TYR   A 1 57  ? 10.123 0.685   18.284 1.00 10.87  ? 63  TYR   A CB  1 
ATOM   439  C  CG  . TYR   A 1 57  ? 9.161  1.052   19.401 1.00 10.70  ? 63  TYR   A CG  1 
ATOM   440  C  CD1 . TYR   A 1 57  ? 7.867  0.546   19.422 1.00 11.48  ? 63  TYR   A CD1 1 
ATOM   441  C  CD2 . TYR   A 1 57  ? 9.512  1.982   20.376 1.00 11.38  ? 63  TYR   A CD2 1 
ATOM   442  C  CE1 . TYR   A 1 57  ? 6.969  0.902   20.426 1.00 12.49  ? 63  TYR   A CE1 1 
ATOM   443  C  CE2 . TYR   A 1 57  ? 8.610  2.369   21.373 1.00 11.80  ? 63  TYR   A CE2 1 
ATOM   444  C  CZ  . TYR   A 1 57  ? 7.341  1.832   21.385 1.00 12.93  ? 63  TYR   A CZ  1 
ATOM   445  O  OH  . TYR   A 1 57  ? 6.455  2.187   22.385 1.00 15.19  ? 63  TYR   A OH  1 
ATOM   446  N  N   . TYR   A 1 58  ? 12.388 -0.336  20.250 1.00 11.05  ? 64  TYR   A N   1 
ATOM   447  C  CA  . TYR   A 1 58  ? 12.862 -0.412  21.615 1.00 11.29  ? 64  TYR   A CA  1 
ATOM   448  C  C   . TYR   A 1 58  ? 12.386 0.786   22.422 1.00 11.19  ? 64  TYR   A C   1 
ATOM   449  O  O   . TYR   A 1 58  ? 12.637 1.941   22.010 1.00 12.15  ? 64  TYR   A O   1 
ATOM   450  C  CB  . TYR   A 1 58  ? 14.398 -0.486  21.673 1.00 11.69  ? 64  TYR   A CB  1 
ATOM   451  C  CG  . TYR   A 1 58  ? 14.879 -0.648  23.095 1.00 12.23  ? 64  TYR   A CG  1 
ATOM   452  C  CD1 . TYR   A 1 58  ? 14.535 -1.764  23.839 1.00 12.64  ? 64  TYR   A CD1 1 
ATOM   453  C  CD2 . TYR   A 1 58  ? 15.637 0.345   23.713 1.00 13.59  ? 64  TYR   A CD2 1 
ATOM   454  C  CE1 . TYR   A 1 58  ? 14.904 -1.879  25.174 1.00 14.70  ? 64  TYR   A CE1 1 
ATOM   455  C  CE2 . TYR   A 1 58  ? 16.036 0.226   25.037 1.00 13.79  ? 64  TYR   A CE2 1 
ATOM   456  C  CZ  . TYR   A 1 58  ? 15.683 -0.893  25.757 1.00 15.71  ? 64  TYR   A CZ  1 
ATOM   457  O  OH  . TYR   A 1 58  ? 16.089 -1.020  27.079 1.00 17.95  ? 64  TYR   A OH  1 
ATOM   458  N  N   . CYS   A 1 59  ? 11.787 0.493   23.592 1.00 11.00  ? 65  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 59  ? 11.280 1.510   24.522 1.00 11.80  ? 65  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 59  ? 12.113 1.466   25.817 1.00 13.22  ? 65  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 59  ? 11.894 0.556   26.652 1.00 13.66  ? 65  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 59  ? 9.817  1.225   24.816 1.00 12.96  ? 65  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 59  ? 9.079  2.356   26.027 1.00 13.91  ? 65  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 60  ? 13.057 2.422   25.994 1.00 12.18  ? 66  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 60  ? 13.933 2.380   27.175 1.00 13.57  ? 66  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 60  ? 13.198 2.555   28.497 1.00 14.12  ? 66  SER   A C   1 
ATOM   467  O  O   . SER   A 1 60  ? 13.584 1.955   29.499 1.00 15.77  ? 66  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 60  ? 15.071 3.399   27.065 1.00 15.21  ? 66  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 60  ? 14.631 4.741   27.202 1.00 17.91  ? 66  SER   A OG  1 
ATOM   470  N  N   . SER   A 1 61  ? 12.067 3.324   28.488 1.00 13.04  ? 67  SER   A N   1 
ATOM   471  C  CA  . SER   A 1 61  ? 11.257 3.546   29.685 1.00 13.50  ? 67  SER   A CA  1 
ATOM   472  C  C   . SER   A 1 61  ? 10.459 2.337   30.132 1.00 13.93  ? 67  SER   A C   1 
ATOM   473  O  O   . SER   A 1 61  ? 9.811  2.393   31.169 1.00 15.26  ? 67  SER   A O   1 
ATOM   474  C  CB  . SER   A 1 61  ? 10.349 4.761   29.533 1.00 14.79  ? 67  SER   A CB  1 
ATOM   475  O  OG  . SER   A 1 61  ? 9.366  4.617   28.536 1.00 16.46  ? 67  SER   A OG  1 
ATOM   476  N  N   . ARG   A 1 62  ? 10.534 1.221   29.364 1.00 13.53  ? 68  ARG   A N   1 
ATOM   477  C  CA  . ARG   A 1 62  ? 9.930  -0.050  29.752 1.00 14.15  ? 68  ARG   A CA  1 
ATOM   478  C  C   . ARG   A 1 62  ? 10.947 -1.206  29.659 1.00 15.63  ? 68  ARG   A C   1 
ATOM   479  O  O   . ARG   A 1 62  ? 10.566 -2.353  29.925 1.00 15.56  ? 68  ARG   A O   1 
ATOM   480  C  CB  . ARG   A 1 62  ? 8.726  -0.363  28.829 1.00 15.08  ? 68  ARG   A CB  1 
ATOM   481  C  CG  . ARG   A 1 62  ? 7.559  0.628   28.957 1.00 16.42  ? 68  ARG   A CG  1 
ATOM   482  C  CD  . ARG   A 1 62  ? 6.778  0.348   30.219 1.00 15.75  ? 68  ARG   A CD  1 
ATOM   483  N  NE  . ARG   A 1 62  ? 5.654  1.272   30.386 1.00 17.98  ? 68  ARG   A NE  1 
ATOM   484  C  CZ  . ARG   A 1 62  ? 5.720  2.436   31.026 1.00 18.51  ? 68  ARG   A CZ  1 
ATOM   485  N  NH1 . ARG   A 1 62  ? 6.876  2.853   31.552 1.00 18.43  ? 68  ARG   A NH1 1 
ATOM   486  N  NH2 . ARG   A 1 62  ? 4.623  3.191   31.166 1.00 19.11  ? 68  ARG   A NH2 1 
ATOM   487  N  N   . ARG   A 1 63  ? 12.198 -0.953  29.191 1.00 15.66  ? 69  ARG   A N   1 
ATOM   488  C  CA  . ARG   A 1 63  ? 13.183 -2.026  28.904 1.00 16.49  ? 69  ARG   A CA  1 
ATOM   489  C  C   . ARG   A 1 63  ? 12.538 -3.143  28.037 1.00 17.30  ? 69  ARG   A C   1 
ATOM   490  O  O   . ARG   A 1 63  ? 12.667 -4.348  28.324 1.00 19.37  ? 69  ARG   A O   1 
ATOM   491  C  CB  . ARG   A 1 63  ? 13.736 -2.646  30.189 1.00 18.88  ? 69  ARG   A CB  1 
ATOM   492  C  CG  . ARG   A 1 63  ? 14.651 -1.704  30.907 1.00 20.02  ? 69  ARG   A CG  1 
ATOM   493  C  CD  . ARG   A 1 63  ? 15.565 -2.521  31.798 1.00 21.17  ? 69  ARG   A CD  1 
ATOM   494  N  NE  . ARG   A 1 63  ? 16.362 -1.582  32.575 1.00 22.87  ? 69  ARG   A NE  1 
ATOM   495  C  CZ  . ARG   A 1 63  ? 16.063 -1.188  33.814 1.00 21.74  ? 69  ARG   A CZ  1 
ATOM   496  N  NH1 . ARG   A 1 63  ? 14.972 -1.651  34.424 1.00 20.36  ? 69  ARG   A NH1 1 
ATOM   497  N  NH2 . ARG   A 1 63  ? 16.831 -0.305  34.436 1.00 22.38  ? 69  ARG   A NH2 1 
ATOM   498  N  N   . LYS   A 1 64  ? 11.759 -2.727  27.051 1.00 15.27  ? 70  LYS   A N   1 
ATOM   499  C  CA  . LYS   A 1 64  ? 11.037 -3.691  26.232 1.00 15.46  ? 70  LYS   A CA  1 
ATOM   500  C  C   . LYS   A 1 64  ? 11.036 -3.316  24.788 1.00 14.49  ? 70  LYS   A C   1 
ATOM   501  O  O   . LYS   A 1 64  ? 10.957 -2.132  24.442 1.00 14.84  ? 70  LYS   A O   1 
ATOM   502  C  CB  . LYS   A 1 64  ? 9.577  -3.772  26.710 1.00 18.86  ? 70  LYS   A CB  1 
ATOM   503  C  CG  . LYS   A 1 64  ? 8.880  -5.104  26.389 1.00 28.82  ? 70  LYS   A CG  1 
ATOM   504  C  CD  . LYS   A 1 64  ? 8.210  -5.668  27.630 1.00 36.84  ? 70  LYS   A CD  1 
ATOM   505  C  CE  . LYS   A 1 64  ? 7.372  -6.892  27.291 1.00 41.59  ? 70  LYS   A CE  1 
ATOM   506  N  NZ  . LYS   A 1 64  ? 8.010  -7.765  26.263 1.00 42.34  ? 70  LYS   A NZ  1 
ATOM   507  N  N   . HIS   A 1 65  ? 11.004 -4.340  23.928 1.00 13.31  ? 71  HIS   A N   1 
ATOM   508  C  CA  . HIS   A 1 65  ? 10.810 -4.177  22.482 1.00 12.38  ? 71  HIS   A CA  1 
ATOM   509  C  C   . HIS   A 1 65  ? 9.344  -4.504  22.178 1.00 13.85  ? 71  HIS   A C   1 
ATOM   510  O  O   . HIS   A 1 65  ? 8.850  -5.568  22.581 1.00 16.85  ? 71  HIS   A O   1 
ATOM   511  C  CB  . HIS   A 1 65  ? 11.729 -5.138  21.690 1.00 11.99  ? 71  HIS   A CB  1 
ATOM   512  C  CG  . HIS   A 1 65  ? 13.187 -4.821  21.845 1.00 13.45  ? 71  HIS   A CG  1 
ATOM   513  N  ND1 . HIS   A 1 65  ? 13.899 -4.160  20.867 1.00 16.66  ? 71  HIS   A ND1 1 
ATOM   514  C  CD2 . HIS   A 1 65  ? 14.033 -5.159  22.853 1.00 13.69  ? 71  HIS   A CD2 1 
ATOM   515  C  CE1 . HIS   A 1 65  ? 15.161 -4.116  21.299 1.00 14.82  ? 71  HIS   A CE1 1 
ATOM   516  N  NE2 . HIS   A 1 65  ? 15.279 -4.687  22.483 1.00 15.96  ? 71  HIS   A NE2 1 
ATOM   517  N  N   . TYR   A 1 66  ? 8.653  -3.602  21.467 1.00 12.53  ? 72  TYR   A N   1 
ATOM   518  C  CA  . TYR   A 1 66  ? 7.232  -3.816  21.187 1.00 12.57  ? 72  TYR   A CA  1 
ATOM   519  C  C   . TYR   A 1 66  ? 6.976  -3.927  19.704 1.00 12.50  ? 72  TYR   A C   1 
ATOM   520  O  O   . TYR   A 1 66  ? 7.447  -3.079  18.944 1.00 11.41  ? 72  TYR   A O   1 
ATOM   521  C  CB  . TYR   A 1 66  ? 6.419  -2.568  21.665 1.00 12.81  ? 72  TYR   A CB  1 
ATOM   522  C  CG  . TYR   A 1 66  ? 6.343  -2.388  23.174 1.00 13.27  ? 72  TYR   A CG  1 
ATOM   523  C  CD1 . TYR   A 1 66  ? 5.507  -3.179  23.945 1.00 14.60  ? 72  TYR   A CD1 1 
ATOM   524  C  CD2 . TYR   A 1 66  ? 7.098  -1.421  23.817 1.00 13.62  ? 72  TYR   A CD2 1 
ATOM   525  C  CE1 . TYR   A 1 66  ? 5.367  -2.968  25.306 1.00 15.75  ? 72  TYR   A CE1 1 
ATOM   526  C  CE2 . TYR   A 1 66  ? 6.984  -1.209  25.181 1.00 14.95  ? 72  TYR   A CE2 1 
ATOM   527  C  CZ  . TYR   A 1 66  ? 6.116  -1.988  25.928 1.00 16.18  ? 72  TYR   A CZ  1 
ATOM   528  O  OH  . TYR   A 1 66  ? 6.011  -1.812  27.299 1.00 19.04  ? 72  TYR   A OH  1 
ATOM   529  N  N   . PRO   A 1 67  ? 6.153  -4.919  19.299 1.00 12.59  ? 73  PRO   A N   1 
ATOM   530  C  CA  . PRO   A 1 67  ? 5.747  -4.977  17.884 1.00 12.80  ? 73  PRO   A CA  1 
ATOM   531  C  C   . PRO   A 1 67  ? 4.678  -3.902  17.621 1.00 13.40  ? 73  PRO   A C   1 
ATOM   532  O  O   . PRO   A 1 67  ? 3.741  -3.722  18.440 1.00 14.87  ? 73  PRO   A O   1 
ATOM   533  C  CB  . PRO   A 1 67  ? 5.115  -6.374  17.727 1.00 13.84  ? 73  PRO   A CB  1 
ATOM   534  C  CG  . PRO   A 1 67  ? 4.723  -6.789  19.113 1.00 14.69  ? 73  PRO   A CG  1 
ATOM   535  C  CD  . PRO   A 1 67  ? 5.590  -6.020  20.122 1.00 12.17  ? 73  PRO   A CD  1 
ATOM   536  N  N   . VAL   A 1 68  ? 4.828  -3.205  16.512 1.00 12.36  ? 74  VAL   A N   1 
ATOM   537  C  CA  . VAL   A 1 68  ? 3.880  -2.136  16.176 1.00 13.88  ? 74  VAL   A CA  1 
ATOM   538  C  C   . VAL   A 1 68  ? 3.548  -2.106  14.708 1.00 13.03  ? 74  VAL   A C   1 
ATOM   539  O  O   . VAL   A 1 68  ? 4.381  -2.454  13.869 1.00 12.99  ? 74  VAL   A O   1 
ATOM   540  C  CB  . VAL   A 1 68  ? 4.447  -0.739  16.584 1.00 15.89  ? 74  VAL   A CB  1 
ATOM   541  C  CG1 . VAL   A 1 68  ? 4.410  -0.536  18.091 1.00 16.67  ? 74  VAL   A CG1 1 
ATOM   542  C  CG2 . VAL   A 1 68  ? 5.852  -0.505  16.028 1.00 16.51  ? 74  VAL   A CG2 1 
ATOM   543  N  N   . SER   A 1 69  ? 2.350  -1.550  14.377 1.00 13.21  ? 75  SER   A N   1 
ATOM   544  C  CA  . SER   A 1 69  ? 1.999  -1.131  13.024 1.00 14.15  ? 75  SER   A CA  1 
ATOM   545  C  C   . SER   A 1 69  ? 2.228  0.392   12.994 1.00 13.63  ? 75  SER   A C   1 
ATOM   546  O  O   . SER   A 1 69  ? 1.876  1.085   13.958 1.00 14.11  ? 75  SER   A O   1 
ATOM   547  C  CB  . SER   A 1 69  ? 0.518  -1.372  12.750 1.00 17.76  ? 75  SER   A CB  1 
ATOM   548  O  OG  . SER   A 1 69  ? 0.275  -2.767  12.808 1.00 24.35  ? 75  SER   A OG  1 
ATOM   549  N  N   . PHE   A 1 70  ? 2.828  0.908   11.929 1.00 13.79  ? 76  PHE   A N   1 
ATOM   550  C  CA  . PHE   A 1 70  ? 3.144  2.327   11.848 1.00 14.24  ? 76  PHE   A CA  1 
ATOM   551  C  C   . PHE   A 1 70  ? 2.757  2.920   10.515 1.00 15.28  ? 76  PHE   A C   1 
ATOM   552  O  O   . PHE   A 1 70  ? 2.682  2.221   9.502  1.00 16.48  ? 76  PHE   A O   1 
ATOM   553  C  CB  . PHE   A 1 70  ? 4.637  2.602   12.191 1.00 13.99  ? 76  PHE   A CB  1 
ATOM   554  C  CG  . PHE   A 1 70  ? 5.642  1.786   11.395 1.00 14.42  ? 76  PHE   A CG  1 
ATOM   555  C  CD1 . PHE   A 1 70  ? 6.061  0.533   11.837 1.00 14.20  ? 76  PHE   A CD1 1 
ATOM   556  C  CD2 . PHE   A 1 70  ? 6.207  2.289   10.241 1.00 14.22  ? 76  PHE   A CD2 1 
ATOM   557  C  CE1 . PHE   A 1 70  ? 6.973  -0.215  11.103 1.00 14.81  ? 76  PHE   A CE1 1 
ATOM   558  C  CE2 . PHE   A 1 70  ? 7.153  1.541   9.524  1.00 15.23  ? 76  PHE   A CE2 1 
ATOM   559  C  CZ  . PHE   A 1 70  ? 7.525  0.297   9.969  1.00 14.38  ? 76  PHE   A CZ  1 
ATOM   560  N  N   . SER   A 1 71  ? 2.463  4.224   10.524 1.00 15.15  ? 77  SER   A N   1 
ATOM   561  C  CA  . SER   A 1 71  ? 2.047  4.903   9.304  1.00 15.63  ? 77  SER   A CA  1 
ATOM   562  C  C   . SER   A 1 71  ? 3.226  5.151   8.328  1.00 15.50  ? 77  SER   A C   1 
ATOM   563  O  O   . SER   A 1 71  ? 4.400  5.015   8.696  1.00 15.14  ? 77  SER   A O   1 
ATOM   564  C  CB  . SER   A 1 71  ? 1.317  6.207   9.656  1.00 17.21  ? 77  SER   A CB  1 
ATOM   565  O  OG  . SER   A 1 71  ? 2.206  7.108   10.306 1.00 18.53  ? 77  SER   A OG  1 
ATOM   566  N  N   . LYS   A 1 72  ? 2.921  5.515   7.086  1.00 15.77  ? 78  LYS   A N   1 
ATOM   567  C  CA  . LYS   A 1 72  ? 3.957  5.832   6.109  1.00 16.40  ? 78  LYS   A CA  1 
ATOM   568  C  C   . LYS   A 1 72  ? 4.588  7.170   6.466  1.00 17.29  ? 78  LYS   A C   1 
ATOM   569  O  O   . LYS   A 1 72  ? 3.903  8.049   7.021  1.00 17.88  ? 78  LYS   A O   1 
ATOM   570  C  CB  . LYS   A 1 72  ? 3.344  5.857   4.702  1.00 19.39  ? 78  LYS   A CB  1 
ATOM   571  C  CG  . LYS   A 1 72  ? 2.942  4.450   4.267  1.00 22.74  ? 78  LYS   A CG  1 
ATOM   572  C  CD  . LYS   A 1 72  ? 2.657  4.368   2.768  1.00 30.33  ? 78  LYS   A CD  1 
ATOM   573  C  CE  . LYS   A 1 72  ? 2.318  2.950   2.350  1.00 36.55  ? 78  LYS   A CE  1 
ATOM   574  N  NZ  . LYS   A 1 72  ? 2.387  2.780   0.871  1.00 40.45  ? 78  LYS   A NZ  1 
ATOM   575  N  N   . PRO   A 1 73  ? 5.873  7.380   6.147  1.00 16.98  ? 79  PRO   A N   1 
ATOM   576  C  CA  . PRO   A 1 73  ? 6.518  8.664   6.475  1.00 17.27  ? 79  PRO   A CA  1 
ATOM   577  C  C   . PRO   A 1 73  ? 5.737  9.850   5.899  1.00 18.81  ? 79  PRO   A C   1 
ATOM   578  O  O   . PRO   A 1 73  ? 5.370  9.837   4.729  1.00 20.94  ? 79  PRO   A O   1 
ATOM   579  C  CB  . PRO   A 1 73  ? 7.902  8.574   5.807  1.00 18.89  ? 79  PRO   A CB  1 
ATOM   580  C  CG  . PRO   A 1 73  ? 8.077  7.183   5.372  1.00 20.34  ? 79  PRO   A CG  1 
ATOM   581  C  CD  . PRO   A 1 73  ? 6.782  6.447   5.436  1.00 17.76  ? 79  PRO   A CD  1 
ATOM   582  N  N   . SER   A 1 74  ? 5.423  10.823  6.749  1.00 19.09  ? 80  SER   A N   1 
ATOM   583  C  CA  . SER   A 1 74  ? 4.564  11.939  6.336  1.00 20.99  ? 80  SER   A CA  1 
ATOM   584  C  C   . SER   A 1 74  ? 4.947  13.216  7.096  1.00 20.22  ? 80  SER   A C   1 
ATOM   585  O  O   . SER   A 1 74  ? 5.773  13.197  8.005  1.00 18.56  ? 80  SER   A O   1 
ATOM   586  C  CB  . SER   A 1 74  ? 3.087  11.624  6.636  1.00 26.40  ? 80  SER   A CB  1 
ATOM   587  O  OG  . SER   A 1 74  ? 2.722  10.282  6.366  1.00 34.84  ? 80  SER   A OG  1 
ATOM   588  N  N   . LEU   A 1 75  ? 4.263  14.324  6.750  1.00 20.72  ? 81  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 75  ? 4.441  15.616  7.387  1.00 22.31  ? 81  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 75  ? 3.342  15.682  8.461  1.00 23.89  ? 81  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 75  ? 2.137  15.720  8.138  1.00 25.78  ? 81  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 75  ? 4.255  16.733  6.318  1.00 23.42  ? 81  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 75  ? 4.542  18.131  6.765  1.00 26.42  ? 81  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 75  ? 6.008  18.322  7.058  1.00 27.00  ? 81  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 75  ? 4.122  19.144  5.677  1.00 27.63  ? 81  LEU   A CD2 1 
ATOM   596  N  N   . ILE   A 1 76  ? 3.763  15.569  9.756  1.00 22.86  ? 82  ILE   A N   1 
ATOM   597  C  CA  . ILE   A 1 76  ? 2.804  15.554  10.895 1.00 24.42  ? 82  ILE   A CA  1 
ATOM   598  C  C   . ILE   A 1 76  ? 3.038  16.742  11.838 1.00 24.87  ? 82  ILE   A C   1 
ATOM   599  O  O   . ILE   A 1 76  ? 4.197  17.126  12.072 1.00 23.30  ? 82  ILE   A O   1 
ATOM   600  C  CB  . ILE   A 1 76  ? 2.978  14.273  11.721 1.00 25.99  ? 82  ILE   A CB  1 
ATOM   601  C  CG1 . ILE   A 1 76  ? 2.942  12.998  10.874 1.00 28.35  ? 82  ILE   A CG1 1 
ATOM   602  C  CG2 . ILE   A 1 76  ? 1.996  14.218  12.867 1.00 27.11  ? 82  ILE   A CG2 1 
ATOM   603  C  CD1 . ILE   A 1 76  ? 1.575  12.386  10.741 1.00 31.13  ? 82  ILE   A CD1 1 
ATOM   604  N  N   . PHE   A 1 77  ? 1.959  17.173  12.485 1.00 25.89  ? 83  PHE   A N   1 
ATOM   605  C  CA  . PHE   A 1 77  ? 2.163  18.205  13.562 1.00 26.63  ? 83  PHE   A CA  1 
ATOM   606  C  C   . PHE   A 1 77  ? 2.696  17.618  14.848 1.00 26.34  ? 83  PHE   A C   1 
ATOM   607  O  O   . PHE   A 1 77  ? 2.163  16.588  15.299 1.00 27.96  ? 83  PHE   A O   1 
ATOM   608  C  CB  . PHE   A 1 77  ? 0.959  18.333  14.469 1.00 28.55  ? 83  PHE   A CB  1 
ATOM   609  C  CG  . PHE   A 1 77  ? 0.831  19.701  15.088 1.00 31.14  ? 83  PHE   A CG  1 
ATOM   610  C  CD1 . PHE   A 1 77  ? 0.908  20.836  14.310 1.00 33.37  ? 83  PHE   A CD1 1 
ATOM   611  C  CD2 . PHE   A 1 77  ? 0.654  19.863  16.446 1.00 33.24  ? 83  PHE   A CD2 1 
ATOM   612  C  CE1 . PHE   A 1 77  ? 0.787  22.092  14.868 1.00 35.22  ? 83  PHE   A CE1 1 
ATOM   613  C  CE2 . PHE   A 1 77  ? 0.569  21.131  17.003 1.00 34.12  ? 83  PHE   A CE2 1 
ATOM   614  C  CZ  . PHE   A 1 77  ? 0.625  22.244  16.211 1.00 35.03  ? 83  PHE   A CZ  1 
ATOM   615  N  N   . VAL   A 1 78  ? 3.759  18.270  15.363 1.00 24.28  ? 84  VAL   A N   1 
ATOM   616  C  CA  . VAL   A 1 78  ? 4.308  17.878  16.712 1.00 23.57  ? 84  VAL   A CA  1 
ATOM   617  C  C   . VAL   A 1 78  ? 4.094  19.019  17.738 1.00 23.33  ? 84  VAL   A C   1 
ATOM   618  O  O   . VAL   A 1 78  ? 4.367  20.083  17.353 1.00 23.40  ? 84  VAL   A O   1 
ATOM   619  C  CB  . VAL   A 1 78  ? 5.834  17.573  16.673 1.00 23.27  ? 84  VAL   A CB  1 
ATOM   620  C  CG1 . VAL   A 1 78  ? 6.301  17.219  18.069 1.00 23.35  ? 84  VAL   A CG1 1 
ATOM   621  C  CG2 . VAL   A 1 78  ? 6.132  16.405  15.754 1.00 23.08  ? 84  VAL   A CG2 1 
ATOM   622  N  N   . GLU   A 1 79  ? 3.603  18.690  18.965 1.00 24.06  ? 85  GLU   A N   1 
ATOM   623  C  CA  . GLU   A 1 79  ? 3.433  19.695  20.127 1.00 25.44  ? 85  GLU   A CA  1 
ATOM   624  C  C   . GLU   A 1 79  ? 4.754  20.410  20.502 1.00 26.24  ? 85  GLU   A C   1 
ATOM   625  O  O   . GLU   A 1 79  ? 5.805  19.843  20.394 1.00 25.60  ? 85  GLU   A O   1 
ATOM   626  C  CB  . GLU   A 1 79  ? 2.753  19.060  21.351 1.00 28.61  ? 85  GLU   A CB  1 
ATOM   627  C  CG  . GLU   A 1 79  ? 1.245  18.930  21.178 1.00 37.34  ? 85  GLU   A CG  1 
ATOM   628  C  CD  . GLU   A 1 79  ? 0.687  20.077  20.358 1.00 49.50  ? 85  GLU   A CD  1 
ATOM   629  O  OE1 . GLU   A 1 79  ? 0.727  21.217  20.807 1.00 51.37  ? 85  GLU   A OE1 1 
ATOM   630  O  OE2 . GLU   A 1 79  ? 0.219  19.817  19.267 1.00 54.50  ? 85  GLU   A OE2 1 
ATOM   631  N  N   . ALA   A 1 80  ? 4.572  21.624  21.016 1.00 27.44  ? 86  ALA   A N   1 
ATOM   632  C  CA  . ALA   A 1 80  ? 5.728  22.439  21.430 1.00 28.95  ? 86  ALA   A CA  1 
ATOM   633  C  C   . ALA   A 1 80  ? 6.417  21.695  22.460 1.00 30.92  ? 86  ALA   A C   1 
ATOM   634  O  O   . ALA   A 1 80  ? 5.725  21.014  23.218 1.00 32.07  ? 86  ALA   A O   1 
ATOM   635  C  CB  . ALA   A 1 80  ? 5.349  23.785  21.919 1.00 29.48  ? 86  ALA   A CB  1 
ATOM   636  N  N   . SER   A 1 81  ? 7.732  21.771  22.370 1.00 30.43  ? 87  SER   A N   1 
ATOM   637  C  CA  A SER   A 1 81  ? 8.627  21.053  23.304 0.50 30.44  ? 87  SER   A CA  1 
ATOM   638  C  CA  B SER   A 1 81  ? 8.627  21.053  23.304 0.50 30.44  ? 87  SER   A CA  1 
ATOM   639  C  C   . SER   A 1 81  ? 9.695  22.135  23.613 1.00 30.63  ? 87  SER   A C   1 
ATOM   640  O  O   . SER   A 1 81  ? 9.861  23.239  22.987 1.00 30.73  ? 87  SER   A O   1 
ATOM   641  C  CB  A SER   A 1 81  ? 9.259  19.930  22.576 0.50 31.46  ? 87  SER   A CB  1 
ATOM   642  C  CB  B SER   A 1 81  ? 9.259  19.931  22.576 0.50 31.46  ? 87  SER   A CB  1 
ATOM   643  O  OG  A SER   A 1 81  ? 10.292 20.359  21.716 0.50 32.43  ? 87  SER   A OG  1 
ATOM   644  O  OG  B SER   A 1 81  ? 10.292 20.360  21.715 0.50 32.43  ? 87  SER   A OG  1 
ATOM   645  N  N   . GLU   A 1 82  ? 10.593 21.736  24.487 1.00 30.92  ? 88  GLU   A N   1 
ATOM   646  C  CA  . GLU   A 1 82  ? 11.711 22.656  24.797 1.00 31.59  ? 88  GLU   A CA  1 
ATOM   647  C  C   . GLU   A 1 82  ? 12.770 22.396  23.756 1.00 28.38  ? 88  GLU   A C   1 
ATOM   648  O  O   . GLU   A 1 82  ? 13.740 23.037  23.770 1.00 28.25  ? 88  GLU   A O   1 
ATOM   649  C  CB  . GLU   A 1 82  ? 12.110 22.244  26.182 1.00 36.87  ? 88  GLU   A CB  1 
ATOM   650  C  CG  . GLU   A 1 82  ? 12.704 20.859  26.381 1.00 43.92  ? 88  GLU   A CG  1 
ATOM   651  C  CD  . GLU   A 1 82  ? 12.014 20.188  27.549 1.00 54.30  ? 88  GLU   A CD  1 
ATOM   652  O  OE1 . GLU   A 1 82  ? 12.589 19.258  28.154 1.00 57.09  ? 88  GLU   A OE1 1 
ATOM   653  O  OE2 . GLU   A 1 82  ? 10.878 20.609  27.850 1.00 56.22  ? 88  GLU   A OE2 1 
ATOM   654  N  N   . TYR   A 1 83  ? 12.516 21.462  22.874 1.00 25.64  ? 89  TYR   A N   1 
ATOM   655  C  CA  . TYR   A 1 83  ? 13.447 21.157  21.733 1.00 23.90  ? 89  TYR   A CA  1 
ATOM   656  C  C   . TYR   A 1 83  ? 12.976 21.725  20.433 1.00 22.17  ? 89  TYR   A C   1 
ATOM   657  O  O   . TYR   A 1 83  ? 13.810 22.153  19.670 1.00 21.35  ? 89  TYR   A O   1 
ATOM   658  C  CB  . TYR   A 1 83  ? 13.652 19.635  21.616 1.00 23.77  ? 89  TYR   A CB  1 
ATOM   659  C  CG  . TYR   A 1 83  ? 14.378 19.069  22.821 1.00 25.05  ? 89  TYR   A CG  1 
ATOM   660  C  CD1 . TYR   A 1 83  ? 15.729 19.291  23.014 1.00 26.93  ? 89  TYR   A CD1 1 
ATOM   661  C  CD2 . TYR   A 1 83  ? 13.689 18.419  23.828 1.00 27.37  ? 89  TYR   A CD2 1 
ATOM   662  C  CE1 . TYR   A 1 83  ? 16.401 18.780  24.110 1.00 29.11  ? 89  TYR   A CE1 1 
ATOM   663  C  CE2 . TYR   A 1 83  ? 14.349 17.903  24.934 1.00 29.22  ? 89  TYR   A CE2 1 
ATOM   664  C  CZ  . TYR   A 1 83  ? 15.711 18.090  25.088 1.00 31.02  ? 89  TYR   A CZ  1 
ATOM   665  O  OH  . TYR   A 1 83  ? 16.370 17.597  26.190 1.00 33.12  ? 89  TYR   A OH  1 
ATOM   666  N  N   . TYR   A 1 84  ? 11.638 21.700  20.188 1.00 22.78  ? 90  TYR   A N   1 
ATOM   667  C  CA  . TYR   A 1 84  ? 11.083 22.284  18.938 1.00 22.41  ? 90  TYR   A CA  1 
ATOM   668  C  C   . TYR   A 1 84  ? 9.831  23.185  19.156 1.00 24.26  ? 90  TYR   A C   1 
ATOM   669  O  O   . TYR   A 1 84  ? 9.003  22.770  19.869 1.00 24.49  ? 90  TYR   A O   1 
ATOM   670  C  CB  . TYR   A 1 84  ? 10.801 21.060  18.062 1.00 21.19  ? 90  TYR   A CB  1 
ATOM   671  C  CG  . TYR   A 1 84  ? 12.060 20.404  17.553 1.00 18.43  ? 90  TYR   A CG  1 
ATOM   672  C  CD1 . TYR   A 1 84  ? 12.872 21.011  16.611 1.00 18.16  ? 90  TYR   A CD1 1 
ATOM   673  C  CD2 . TYR   A 1 84  ? 12.419 19.155  18.006 1.00 17.98  ? 90  TYR   A CD2 1 
ATOM   674  C  CE1 . TYR   A 1 84  ? 14.002 20.371  16.116 1.00 17.56  ? 90  TYR   A CE1 1 
ATOM   675  C  CE2 . TYR   A 1 84  ? 13.556 18.511  17.543 1.00 17.94  ? 90  TYR   A CE2 1 
ATOM   676  C  CZ  . TYR   A 1 84  ? 14.343 19.117  16.586 1.00 16.97  ? 90  TYR   A CZ  1 
ATOM   677  O  OH  . TYR   A 1 84  ? 15.437 18.462  16.102 1.00 16.52  ? 90  TYR   A OH  1 
ATOM   678  N  N   . PRO   A 1 85  ? 9.624  24.248  18.344 1.00 25.19  ? 91  PRO   A N   1 
ATOM   679  C  CA  . PRO   A 1 85  ? 8.414  25.041  18.458 1.00 26.45  ? 91  PRO   A CA  1 
ATOM   680  C  C   . PRO   A 1 85  ? 7.291  24.097  17.991 1.00 26.80  ? 91  PRO   A C   1 
ATOM   681  O  O   . PRO   A 1 85  ? 7.634  22.986  17.533 1.00 25.64  ? 91  PRO   A O   1 
ATOM   682  C  CB  . PRO   A 1 85  ? 8.666  26.244  17.522 1.00 27.85  ? 91  PRO   A CB  1 
ATOM   683  C  CG  . PRO   A 1 85  ? 9.705  25.757  16.553 1.00 28.28  ? 91  PRO   A CG  1 
ATOM   684  C  CD  . PRO   A 1 85  ? 10.519 24.738  17.324 1.00 25.03  ? 91  PRO   A CD  1 
ATOM   685  N  N   . ALA   A 1 86  ? 5.996  24.444  18.249 1.00 27.75  ? 92  ALA   A N   1 
ATOM   686  C  CA  . ALA   A 1 86  ? 5.042  23.411  17.759 1.00 28.17  ? 92  ALA   A CA  1 
ATOM   687  C  C   . ALA   A 1 86  ? 5.246  23.600  16.264 1.00 28.47  ? 92  ALA   A C   1 
ATOM   688  O  O   . ALA   A 1 86  ? 5.491  24.695  15.919 1.00 29.77  ? 92  ALA   A O   1 
ATOM   689  C  CB  . ALA   A 1 86  ? 3.606  23.475  18.243 1.00 28.07  ? 92  ALA   A CB  1 
ATOM   690  N  N   . ARG   A 1 87  ? 5.104  22.540  15.467 1.00 27.83  ? 93  ARG   A N   1 
ATOM   691  C  CA  . ARG   A 1 87  ? 5.590  22.662  14.100 1.00 26.83  ? 93  ARG   A CA  1 
ATOM   692  C  C   . ARG   A 1 87  ? 5.320  21.394  13.309 1.00 26.99  ? 93  ARG   A C   1 
ATOM   693  O  O   . ARG   A 1 87  ? 4.665  20.454  13.872 1.00 26.47  ? 93  ARG   A O   1 
ATOM   694  C  CB  . ARG   A 1 87  ? 7.090  22.795  14.225 1.00 27.29  ? 93  ARG   A CB  1 
ATOM   695  C  CG  . ARG   A 1 87  ? 7.808  21.442  14.283 1.00 28.19  ? 93  ARG   A CG  1 
ATOM   696  C  CD  . ARG   A 1 87  ? 9.317  21.589  14.426 1.00 28.87  ? 93  ARG   A CD  1 
ATOM   697  N  NE  . ARG   A 1 87  ? 10.285 20.532  14.102 1.00 28.75  ? 93  ARG   A NE  1 
ATOM   698  C  CZ  . ARG   A 1 87  ? 10.418 19.384  14.720 1.00 31.66  ? 93  ARG   A CZ  1 
ATOM   699  N  NH1 . ARG   A 1 87  ? 9.588  19.059  15.696 1.00 30.70  ? 93  ARG   A NH1 1 
ATOM   700  N  NH2 . ARG   A 1 87  ? 11.354 18.532  14.331 1.00 25.17  ? 93  ARG   A NH2 1 
ATOM   701  N  N   . TYR   A 1 88  ? 5.797  21.402  12.060 1.00 27.41  ? 94  TYR   A N   1 
ATOM   702  C  CA  . TYR   A 1 88  ? 5.554  20.278  11.099 1.00 27.52  ? 94  TYR   A CA  1 
ATOM   703  C  C   . TYR   A 1 88  ? 6.843  19.476  10.930 1.00 24.86  ? 94  TYR   A C   1 
ATOM   704  O  O   . TYR   A 1 88  ? 7.848  19.935  10.368 1.00 26.10  ? 94  TYR   A O   1 
ATOM   705  C  CB  . TYR   A 1 88  ? 4.997  20.791  9.751  1.00 28.53  ? 94  TYR   A CB  1 
ATOM   706  C  CG  . TYR   A 1 88  ? 3.504  20.948  9.849  1.00 29.86  ? 94  TYR   A CG  1 
ATOM   707  C  CD1 . TYR   A 1 88  ? 2.648  19.861  9.835  1.00 30.50  ? 94  TYR   A CD1 1 
ATOM   708  C  CD2 . TYR   A 1 88  ? 2.949  22.184  10.096 1.00 31.47  ? 94  TYR   A CD2 1 
ATOM   709  C  CE1 . TYR   A 1 88  ? 1.278  19.998  9.954  1.00 32.44  ? 94  TYR   A CE1 1 
ATOM   710  C  CE2 . TYR   A 1 88  ? 1.583  22.340  10.237 1.00 32.98  ? 94  TYR   A CE2 1 
ATOM   711  C  CZ  . TYR   A 1 88  ? 0.742  21.250  10.162 1.00 34.27  ? 94  TYR   A CZ  1 
ATOM   712  O  OH  . TYR   A 1 88  ? -0.601 21.440  10.281 1.00 37.53  ? 94  TYR   A OH  1 
ATOM   713  N  N   . GLN   A 1 89  ? 6.820  18.262  11.493 1.00 21.47  ? 95  GLN   A N   1 
ATOM   714  C  CA  . GLN   A 1 89  ? 8.035  17.424  11.323 1.00 19.29  ? 95  GLN   A CA  1 
ATOM   715  C  C   . GLN   A 1 89  ? 7.802  16.525  10.119 1.00 18.16  ? 95  GLN   A C   1 
ATOM   716  O  O   . GLN   A 1 89  ? 6.748  15.933  10.000 1.00 18.27  ? 95  GLN   A O   1 
ATOM   717  C  CB  . GLN   A 1 89  ? 8.247  16.587  12.592 1.00 18.87  ? 95  GLN   A CB  1 
ATOM   718  C  CG  . GLN   A 1 89  ? 9.546  15.793  12.511 1.00 17.95  ? 95  GLN   A CG  1 
ATOM   719  C  CD  . GLN   A 1 89  ? 10.047 15.177  13.796 1.00 16.55  ? 95  GLN   A CD  1 
ATOM   720  O  OE1 . GLN   A 1 89  ? 10.221 15.854  14.795 1.00 19.71  ? 95  GLN   A OE1 1 
ATOM   721  N  NE2 . GLN   A 1 89  ? 10.377 13.892  13.748 1.00 16.44  ? 95  GLN   A NE2 1 
ATOM   722  N  N   . SER   A 1 90  ? 8.794  16.488  9.236  1.00 16.93  ? 96  SER   A N   1 
ATOM   723  C  CA  . SER   A 1 90  ? 8.685  15.687  8.035  1.00 16.51  ? 96  SER   A CA  1 
ATOM   724  C  C   . SER   A 1 90  ? 9.283  14.284  8.195  1.00 16.72  ? 96  SER   A C   1 
ATOM   725  O  O   . SER   A 1 90  ? 10.060 14.032  9.141  1.00 16.84  ? 96  SER   A O   1 
ATOM   726  C  CB  . SER   A 1 90  ? 9.371  16.414  6.880  1.00 19.67  ? 96  SER   A CB  1 
ATOM   727  O  OG  . SER   A 1 90  ? 10.765 16.492  7.150  1.00 21.96  ? 96  SER   A OG  1 
ATOM   728  N  N   . HIS   A 1 91  ? 8.883  13.366  7.265  1.00 16.49  ? 97  HIS   A N   1 
ATOM   729  C  CA  . HIS   A 1 91  ? 9.388  12.000  7.223  1.00 15.88  ? 97  HIS   A CA  1 
ATOM   730  C  C   . HIS   A 1 91  ? 9.149  11.284  8.577  1.00 15.67  ? 97  HIS   A C   1 
ATOM   731  O  O   . HIS   A 1 91  ? 9.980  10.466  8.994  1.00 15.97  ? 97  HIS   A O   1 
ATOM   732  C  CB  . HIS   A 1 91  ? 10.908 11.991  6.848  1.00 16.61  ? 97  HIS   A CB  1 
ATOM   733  C  CG  . HIS   A 1 91  ? 11.200 12.575  5.485  1.00 18.26  ? 97  HIS   A CG  1 
ATOM   734  N  ND1 . HIS   A 1 91  ? 11.330 11.766  4.364  1.00 20.12  ? 97  HIS   A ND1 1 
ATOM   735  C  CD2 . HIS   A 1 91  ? 11.348 13.868  5.105  1.00 20.19  ? 97  HIS   A CD2 1 
ATOM   736  C  CE1 . HIS   A 1 91  ? 11.584 12.588  3.349  1.00 20.55  ? 97  HIS   A CE1 1 
ATOM   737  N  NE2 . HIS   A 1 91  ? 11.595 13.859  3.742  1.00 21.14  ? 97  HIS   A NE2 1 
ATOM   738  N  N   . LEU   A 1 92  ? 8.022  11.574  9.214  1.00 14.35  ? 98  LEU   A N   1 
ATOM   739  C  CA  . LEU   A 1 92  ? 7.691  11.015  10.532 1.00 14.71  ? 98  LEU   A CA  1 
ATOM   740  C  C   . LEU   A 1 92  ? 6.610  9.931   10.376 1.00 14.32  ? 98  LEU   A C   1 
ATOM   741  O  O   . LEU   A 1 92  ? 5.684  10.078  9.576  1.00 14.60  ? 98  LEU   A O   1 
ATOM   742  C  CB  . LEU   A 1 92  ? 7.149  12.146  11.432 1.00 15.50  ? 98  LEU   A CB  1 
ATOM   743  C  CG  . LEU   A 1 92  ? 6.880  11.743  12.898 1.00 17.58  ? 98  LEU   A CG  1 
ATOM   744  C  CD1 . LEU   A 1 92  ? 8.162  11.457  13.610 1.00 16.88  ? 98  LEU   A CD1 1 
ATOM   745  C  CD2 . LEU   A 1 92  ? 6.131  12.867  13.660 1.00 19.48  ? 98  LEU   A CD2 1 
ATOM   746  N  N   . MET   A 1 93  ? 6.749  8.820   11.134 1.00 14.89  ? 99  MET   A N   1 
ATOM   747  C  CA  . MET   A 1 93  ? 5.767  7.718   11.100 1.00 14.67  ? 99  MET   A CA  1 
ATOM   748  C  C   . MET   A 1 93  ? 5.195  7.555   12.502 1.00 14.55  ? 99  MET   A C   1 
ATOM   749  O  O   . MET   A 1 93  ? 5.955  7.647   13.463 1.00 15.31  ? 99  MET   A O   1 
ATOM   750  C  CB  . MET   A 1 93  ? 6.502  6.437   10.730 1.00 15.05  ? 99  MET   A CB  1 
ATOM   751  C  CG  . MET   A 1 93  ? 7.186  6.550   9.369  1.00 16.60  ? 99  MET   A CG  1 
ATOM   752  S  SD  . MET   A 1 93  ? 8.271  5.157   8.923  1.00 19.14  ? 99  MET   A SD  1 
ATOM   753  C  CE  . MET   A 1 93  ? 9.532  5.345   10.151 1.00 20.94  ? 99  MET   A CE  1 
ATOM   754  N  N   . LEU   A 1 94  ? 3.883  7.336   12.636 1.00 13.16  ? 100 LEU   A N   1 
ATOM   755  C  CA  . LEU   A 1 94  ? 3.279  7.225   13.967 1.00 14.54  ? 100 LEU   A CA  1 
ATOM   756  C  C   . LEU   A 1 94  ? 2.806  5.813   14.230 1.00 14.56  ? 100 LEU   A C   1 
ATOM   757  O  O   . LEU   A 1 94  ? 2.369  5.102   13.318 1.00 15.74  ? 100 LEU   A O   1 
ATOM   758  C  CB  . LEU   A 1 94  ? 2.038  8.160   14.116 1.00 16.82  ? 100 LEU   A CB  1 
ATOM   759  C  CG  . LEU   A 1 94  ? 2.303  9.643   14.058 1.00 20.90  ? 100 LEU   A CG  1 
ATOM   760  C  CD1 . LEU   A 1 94  ? 1.041  10.437  14.381 1.00 23.06  ? 100 LEU   A CD1 1 
ATOM   761  C  CD2 . LEU   A 1 94  ? 3.386  10.092  15.073 1.00 21.75  ? 100 LEU   A CD2 1 
ATOM   762  N  N   . ALA   A 1 95  ? 2.844  5.425   15.510 1.00 13.91  ? 101 ALA   A N   1 
ATOM   763  C  CA  . ALA   A 1 95  ? 2.300  4.138   15.960 1.00 13.31  ? 101 ALA   A CA  1 
ATOM   764  C  C   . ALA   A 1 95  ? 1.700  4.348   17.362 1.00 13.50  ? 101 ALA   A C   1 
ATOM   765  O  O   . ALA   A 1 95  ? 1.980  5.357   18.040 1.00 14.39  ? 101 ALA   A O   1 
ATOM   766  C  CB  . ALA   A 1 95  ? 3.398  3.059   16.041 1.00 13.67  ? 101 ALA   A CB  1 
ATOM   767  N  N   . VAL   A 1 96  ? 0.871  3.394   17.791 1.00 13.35  ? 102 VAL   A N   1 
ATOM   768  C  CA  . VAL   A 1 96  ? 0.338  3.412   19.130 1.00 13.33  ? 102 VAL   A CA  1 
ATOM   769  C  C   . VAL   A 1 96  ? 1.367  2.710   20.009 1.00 15.01  ? 102 VAL   A C   1 
ATOM   770  O  O   . VAL   A 1 96  ? 1.696  1.547   19.787 1.00 15.09  ? 102 VAL   A O   1 
ATOM   771  C  CB  . VAL   A 1 96  ? -1.012 2.670   19.168 1.00 13.96  ? 102 VAL   A CB  1 
ATOM   772  C  CG1 . VAL   A 1 96  ? -1.523 2.525   20.609 1.00 14.62  ? 102 VAL   A CG1 1 
ATOM   773  C  CG2 . VAL   A 1 96  ? -2.003 3.411   18.261 1.00 13.91  ? 102 VAL   A CG2 1 
ATOM   774  N  N   . GLY   A 1 97  ? 1.877  3.431   20.991 1.00 15.57  ? 103 GLY   A N   1 
ATOM   775  C  CA  . GLY   A 1 97  ? 2.876  2.876   21.893 1.00 16.75  ? 103 GLY   A CA  1 
ATOM   776  C  C   . GLY   A 1 97  ? 3.350  3.878   22.915 1.00 17.55  ? 103 GLY   A C   1 
ATOM   777  O  O   . GLY   A 1 97  ? 3.100  5.076   22.798 1.00 18.46  ? 103 GLY   A O   1 
ATOM   778  N  N   . HIS   A 1 98  ? 3.677  3.256   24.031 1.00 17.80  ? 104 HIS   A N   1 
ATOM   779  C  CA  . HIS   A 1 98  ? 4.247  4.113   25.064 1.00 18.25  ? 104 HIS   A CA  1 
ATOM   780  C  C   . HIS   A 1 98  ? 5.551  4.791   24.628 1.00 18.86  ? 104 HIS   A C   1 
ATOM   781  O  O   . HIS   A 1 98  ? 6.350  4.087   23.951 1.00 19.24  ? 104 HIS   A O   1 
ATOM   782  C  CB  . HIS   A 1 98  ? 4.407  3.263   26.368 1.00 19.14  ? 104 HIS   A CB  1 
ATOM   783  C  CG  . HIS   A 1 98  ? 4.890  4.102   27.495 1.00 20.12  ? 104 HIS   A CG  1 
ATOM   784  N  ND1 . HIS   A 1 98  ? 4.078  5.046   28.055 1.00 21.34  ? 104 HIS   A ND1 1 
ATOM   785  C  CD2 . HIS   A 1 98  ? 6.088  4.226   28.116 1.00 20.06  ? 104 HIS   A CD2 1 
ATOM   786  C  CE1 . HIS   A 1 98  ? 4.726  5.711   28.979 1.00 20.72  ? 104 HIS   A CE1 1 
ATOM   787  N  NE2 . HIS   A 1 98  ? 5.964  5.220   29.052 1.00 20.15  ? 104 HIS   A NE2 1 
ATOM   788  N  N   . SER   A 1 99  ? 5.839  6.051   25.037 1.00 18.75  ? 105 SER   A N   1 
ATOM   789  C  CA  . SER   A 1 99  ? 7.040  6.854   24.823 1.00 20.93  ? 105 SER   A CA  1 
ATOM   790  C  C   . SER   A 1 99  ? 7.178  7.861   25.972 1.00 22.94  ? 105 SER   A C   1 
ATOM   791  O  O   . SER   A 1 99  ? 6.106  8.307   26.440 1.00 27.25  ? 105 SER   A O   1 
ATOM   792  C  CB  . SER   A 1 99  ? 7.012  7.700   23.448 1.00 24.16  ? 105 SER   A CB  1 
ATOM   793  O  OG  . SER   A 1 99  ? 8.263  8.292   23.242 1.00 31.27  ? 105 SER   A OG  1 
ATOM   794  N  N   . GLU   A 1 100 ? 8.425  8.167   26.435 1.00 18.84  ? 106 GLU   A N   1 
ATOM   795  C  CA  . GLU   A 1 100 ? 8.750  9.334   27.252 1.00 18.00  ? 106 GLU   A CA  1 
ATOM   796  C  C   . GLU   A 1 100 ? 9.872  10.034  26.446 1.00 17.35  ? 106 GLU   A C   1 
ATOM   797  O  O   . GLU   A 1 100 ? 10.453 9.395   25.604 1.00 16.40  ? 106 GLU   A O   1 
ATOM   798  C  CB  . GLU   A 1 100 ? 9.197  8.802   28.616 1.00 18.95  ? 106 GLU   A CB  1 
ATOM   799  C  CG  . GLU   A 1 100 ? 8.034  8.138   29.316 1.00 19.31  ? 106 GLU   A CG  1 
ATOM   800  C  CD  . GLU   A 1 100 ? 8.201  7.581   30.718 1.00 24.43  ? 106 GLU   A CD  1 
ATOM   801  O  OE1 . GLU   A 1 100 ? 9.027  8.095   31.457 1.00 26.82  ? 106 GLU   A OE1 1 
ATOM   802  O  OE2 . GLU   A 1 100 ? 7.482  6.647   31.021 1.00 23.79  ? 106 GLU   A OE2 1 
ATOM   803  N  N   . PRO   A 1 101 ? 10.220 11.290  26.777 1.00 17.53  ? 107 PRO   A N   1 
ATOM   804  C  CA  . PRO   A 1 101 ? 11.193 12.075  25.986 1.00 17.77  ? 107 PRO   A CA  1 
ATOM   805  C  C   . PRO   A 1 101 ? 12.528 11.315  25.862 1.00 17.59  ? 107 PRO   A C   1 
ATOM   806  O  O   . PRO   A 1 101 ? 13.099 11.307  24.812 1.00 17.85  ? 107 PRO   A O   1 
ATOM   807  C  CB  . PRO   A 1 101 ? 11.157 13.336  26.901 1.00 19.49  ? 107 PRO   A CB  1 
ATOM   808  C  CG  . PRO   A 1 101 ? 9.772  13.449  27.395 1.00 19.91  ? 107 PRO   A CG  1 
ATOM   809  C  CD  . PRO   A 1 101 ? 9.585  12.037  27.867 1.00 18.23  ? 107 PRO   A CD  1 
ATOM   810  N  N   . GLY   A 1 102 ? 12.894 10.658  26.935 1.00 16.05  ? 108 GLY   A N   1 
ATOM   811  C  CA  . GLY   A 1 102 ? 14.202 9.899   26.998 1.00 15.47  ? 108 GLY   A CA  1 
ATOM   812  C  C   . GLY   A 1 102 ? 14.268 8.710   26.118 1.00 13.99  ? 108 GLY   A C   1 
ATOM   813  O  O   . GLY   A 1 102 ? 15.353 8.130   25.954 1.00 15.29  ? 108 GLY   A O   1 
ATOM   814  N  N   . ASP   A 1 103 ? 13.104 8.349   25.611 1.00 12.49  ? 109 ASP   A N   1 
ATOM   815  C  CA  . ASP   A 1 103 ? 13.037 7.137   24.780 1.00 12.86  ? 109 ASP   A CA  1 
ATOM   816  C  C   . ASP   A 1 103 ? 13.544 7.507   23.374 1.00 13.31  ? 109 ASP   A C   1 
ATOM   817  O  O   . ASP   A 1 103 ? 13.746 6.636   22.551 1.00 13.19  ? 109 ASP   A O   1 
ATOM   818  C  CB  . ASP   A 1 103 ? 11.592 6.633   24.761 1.00 13.08  ? 109 ASP   A CB  1 
ATOM   819  C  CG  . ASP   A 1 103 ? 11.281 5.883   26.040 1.00 14.36  ? 109 ASP   A CG  1 
ATOM   820  O  OD1 . ASP   A 1 103 ? 12.172 5.200   26.513 1.00 14.60  ? 109 ASP   A OD1 1 
ATOM   821  O  OD2 . ASP   A 1 103 ? 10.127 5.958   26.497 1.00 14.92  ? 109 ASP   A OD2 1 
ATOM   822  N  N   . CYS   A 1 104 ? 13.606 8.781   23.052 1.00 13.27  ? 110 CYS   A N   1 
ATOM   823  C  CA  . CYS   A 1 104 ? 14.118 9.033   21.654 1.00 13.87  ? 110 CYS   A CA  1 
ATOM   824  C  C   . CYS   A 1 104 ? 15.538 8.438   21.427 1.00 13.84  ? 110 CYS   A C   1 
ATOM   825  O  O   . CYS   A 1 104 ? 16.370 8.499   22.279 1.00 13.82  ? 110 CYS   A O   1 
ATOM   826  C  CB  . CYS   A 1 104 ? 14.270 10.444  21.167 1.00 14.54  ? 110 CYS   A CB  1 
ATOM   827  S  SG  . CYS   A 1 104 ? 12.712 11.365  21.194 1.00 16.22  ? 110 CYS   A SG  1 
ATOM   828  N  N   . GLY   A 1 105 ? 15.707 7.907   20.218 1.00 12.70  ? 111 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 105 ? 16.917 7.192   19.857 1.00 12.65  ? 111 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 105 ? 16.734 5.683   19.786 1.00 12.54  ? 111 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 105 ? 17.580 4.977   19.217 1.00 13.00  ? 111 GLY   A O   1 
ATOM   832  N  N   . GLY   A 1 106 ? 15.648 5.175   20.379 1.00 12.02  ? 112 GLY   A N   1 
ATOM   833  C  CA  . GLY   A 1 106 ? 15.366 3.749   20.296 1.00 11.66  ? 112 GLY   A CA  1 
ATOM   834  C  C   . GLY   A 1 106 ? 15.126 3.352   18.840 1.00 11.20  ? 112 GLY   A C   1 
ATOM   835  O  O   . GLY   A 1 106 ? 14.448 4.091   18.122 1.00 11.91  ? 112 GLY   A O   1 
ATOM   836  N  N   . ILE   A 1 107 ? 15.633 2.173   18.411 1.00 11.16  ? 113 ILE   A N   1 
ATOM   837  C  CA  . ILE   A 1 107 ? 15.480 1.762   17.028 1.00 11.29  ? 113 ILE   A CA  1 
ATOM   838  C  C   . ILE   A 1 107 ? 14.138 1.112   16.752 1.00 11.06  ? 113 ILE   A C   1 
ATOM   839  O  O   . ILE   A 1 107 ? 13.674 0.291   17.559 1.00 10.81  ? 113 ILE   A O   1 
ATOM   840  C  CB  . ILE   A 1 107 ? 16.643 0.796   16.653 1.00 11.56  ? 113 ILE   A CB  1 
ATOM   841  C  CG1 . ILE   A 1 107 ? 17.938 1.630   16.421 1.00 12.39  ? 113 ILE   A CG1 1 
ATOM   842  C  CG2 . ILE   A 1 107 ? 16.331 -0.110  15.436 1.00 12.48  ? 113 ILE   A CG2 1 
ATOM   843  C  CD1 . ILE   A 1 107 ? 19.176 0.814   16.246 1.00 14.69  ? 113 ILE   A CD1 1 
ATOM   844  N  N   . LEU   A 1 108 ? 13.553 1.424   15.581 1.00 10.50  ? 114 LEU   A N   1 
ATOM   845  C  CA  . LEU   A 1 108 ? 12.418 0.718   15.011 1.00 10.54  ? 114 LEU   A CA  1 
ATOM   846  C  C   . LEU   A 1 108 ? 13.022 -0.115  13.862 1.00 10.74  ? 114 LEU   A C   1 
ATOM   847  O  O   . LEU   A 1 108 ? 13.799 0.431   13.033 1.00 11.40  ? 114 LEU   A O   1 
ATOM   848  C  CB  . LEU   A 1 108 ? 11.417 1.735   14.390 1.00 10.86  ? 114 LEU   A CB  1 
ATOM   849  C  CG  . LEU   A 1 108 ? 10.296 1.121   13.517 1.00 12.04  ? 114 LEU   A CG  1 
ATOM   850  C  CD1 . LEU   A 1 108 ? 9.311  0.315   14.375 1.00 11.82  ? 114 LEU   A CD1 1 
ATOM   851  C  CD2 . LEU   A 1 108 ? 9.519  2.244   12.771 1.00 13.71  ? 114 LEU   A CD2 1 
ATOM   852  N  N   . ARG   A 1 109 ? 12.738 -1.430  13.838 1.00 10.73  ? 115 ARG   A N   1 
ATOM   853  C  CA  . ARG   A 1 109 ? 13.311 -2.320  12.807 1.00 11.49  ? 115 ARG   A CA  1 
ATOM   854  C  C   . ARG   A 1 109 ? 12.224 -3.213  12.223 1.00 13.11  ? 115 ARG   A C   1 
ATOM   855  O  O   . ARG   A 1 109 ? 11.217 -3.514  12.882 1.00 12.52  ? 115 ARG   A O   1 
ATOM   856  C  CB  . ARG   A 1 109 ? 14.448 -3.162  13.404 1.00 12.45  ? 115 ARG   A CB  1 
ATOM   857  C  CG  . ARG   A 1 109 ? 13.957 -4.102  14.518 1.00 12.91  ? 115 ARG   A CG  1 
ATOM   858  C  CD  . ARG   A 1 109 ? 15.207 -4.830  15.020 1.00 14.38  ? 115 ARG   A CD  1 
ATOM   859  N  NE  . ARG   A 1 109 ? 16.004 -3.978  15.886 1.00 16.10  ? 115 ARG   A NE  1 
ATOM   860  C  CZ  . ARG   A 1 109 ? 17.305 -3.755  15.757 1.00 15.15  ? 115 ARG   A CZ  1 
ATOM   861  N  NH1 . ARG   A 1 109 ? 17.963 -4.201  14.686 1.00 15.21  ? 115 ARG   A NH1 1 
ATOM   862  N  NH2 . ARG   A 1 109 ? 17.952 -3.021  16.660 1.00 16.43  ? 115 ARG   A NH2 1 
ATOM   863  N  N   . CYS   A 1 110 ? 12.439 -3.658  11.002 1.00 15.04  ? 116 CYS   A N   1 
ATOM   864  C  CA  . CYS   A 1 110 ? 11.540 -4.622  10.342 1.00 17.05  ? 116 CYS   A CA  1 
ATOM   865  C  C   . CYS   A 1 110 ? 12.390 -5.837  9.905  1.00 19.01  ? 116 CYS   A C   1 
ATOM   866  O  O   . CYS   A 1 110 ? 13.590 -5.914  10.236 1.00 18.70  ? 116 CYS   A O   1 
ATOM   867  C  CB  . CYS   A 1 110 ? 10.871 -3.951  9.160  1.00 17.78  ? 116 CYS   A CB  1 
ATOM   868  S  SG  . CYS   A 1 110 ? 12.060 -3.542  7.852  1.00 17.51  ? 116 CYS   A SG  1 
ATOM   869  N  N   . GLN   A 1 111 ? 11.785 -6.767  9.109  1.00 21.28  ? 117 GLN   A N   1 
ATOM   870  C  CA  . GLN   A 1 111 ? 12.538 -7.901  8.626  1.00 22.98  ? 117 GLN   A CA  1 
ATOM   871  C  C   . GLN   A 1 111 ? 13.751 -7.525  7.766  1.00 24.21  ? 117 GLN   A C   1 
ATOM   872  O  O   . GLN   A 1 111 ? 14.692 -8.313  7.674  1.00 26.86  ? 117 GLN   A O   1 
ATOM   873  C  CB  . GLN   A 1 111 ? 11.619 -8.877  7.840  1.00 27.45  ? 117 GLN   A CB  1 
ATOM   874  C  CG  . GLN   A 1 111 ? 11.108 -8.281  6.540  1.00 32.31  ? 117 GLN   A CG  1 
ATOM   875  C  CD  . GLN   A 1 111 ? 10.158 -9.192  5.788  1.00 38.35  ? 117 GLN   A CD  1 
ATOM   876  O  OE1 . GLN   A 1 111 ? 8.928  -9.038  5.849  1.00 40.01  ? 117 GLN   A OE1 1 
ATOM   877  N  NE2 . GLN   A 1 111 ? 10.709 -10.135 5.039  1.00 37.18  ? 117 GLN   A NE2 1 
ATOM   878  N  N   . HIS   A 1 112 ? 13.763 -6.316  7.191  1.00 21.39  ? 118 HIS   A N   1 
ATOM   879  C  CA  . HIS   A 1 112 ? 14.865 -5.897  6.286  1.00 20.75  ? 118 HIS   A CA  1 
ATOM   880  C  C   . HIS   A 1 112 ? 16.004 -5.143  6.988  1.00 20.57  ? 118 HIS   A C   1 
ATOM   881  O  O   . HIS   A 1 112 ? 17.044 -4.876  6.363  1.00 22.69  ? 118 HIS   A O   1 
ATOM   882  C  CB  . HIS   A 1 112 ? 14.275 -5.028  5.154  1.00 22.36  ? 118 HIS   A CB  1 
ATOM   883  C  CG  . HIS   A 1 112 ? 13.145 -5.703  4.417  1.00 25.70  ? 118 HIS   A CG  1 
ATOM   884  N  ND1 . HIS   A 1 112 ? 11.821 -5.328  4.607  1.00 27.84  ? 118 HIS   A ND1 1 
ATOM   885  C  CD2 . HIS   A 1 112 ? 13.186 -6.699  3.491  1.00 28.28  ? 118 HIS   A CD2 1 
ATOM   886  C  CE1 . HIS   A 1 112 ? 11.100 -6.105  3.809  1.00 30.03  ? 118 HIS   A CE1 1 
ATOM   887  N  NE2 . HIS   A 1 112 ? 11.875 -6.967  3.136  1.00 29.95  ? 118 HIS   A NE2 1 
ATOM   888  N  N   . GLY   A 1 113 ? 15.789 -4.720  8.249  1.00 18.20  ? 119 GLY   A N   1 
ATOM   889  C  CA  . GLY   A 1 113 ? 16.806 -3.934  8.940  1.00 16.78  ? 119 GLY   A CA  1 
ATOM   890  C  C   . GLY   A 1 113 ? 16.224 -2.749  9.704  1.00 14.78  ? 119 GLY   A C   1 
ATOM   891  O  O   . GLY   A 1 113 ? 15.040 -2.748  10.067 1.00 14.77  ? 119 GLY   A O   1 
ATOM   892  N  N   . VAL   A 1 114 ? 17.070 -1.725  9.972  1.00 13.42  ? 120 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 114 ? 16.637 -0.544  10.729 1.00 13.47  ? 120 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 114 ? 15.789 0.357   9.855  1.00 12.74  ? 120 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 114 ? 16.212 0.724   8.748  1.00 12.84  ? 120 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 114 ? 17.864 0.220   11.283 1.00 13.09  ? 120 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 114 ? 17.469 1.525   11.972 1.00 13.90  ? 120 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 114 ? 18.657 -0.677  12.230 1.00 14.02  ? 120 VAL   A CG2 1 
ATOM   899  N  N   . VAL   A 1 115 ? 14.649 0.775   10.387 1.00 11.87  ? 121 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 115 ? 13.706 1.627   9.671  1.00 12.51  ? 121 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 115 ? 13.850 3.078   10.122 1.00 12.27  ? 121 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 115 ? 13.718 4.001   9.324  1.00 13.09  ? 121 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 115 ? 12.255 1.147   9.985  1.00 14.05  ? 121 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 115 ? 11.184 2.121   9.463  1.00 15.33  ? 121 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 115 ? 12.019 -0.255  9.460  1.00 13.92  ? 121 VAL   A CG2 1 
ATOM   906  N  N   . GLY   A 1 116 ? 14.068 3.298   11.428 1.00 11.76  ? 122 GLY   A N   1 
ATOM   907  C  CA  . GLY   A 1 116 ? 14.187 4.668   11.948 1.00 12.16  ? 122 GLY   A CA  1 
ATOM   908  C  C   . GLY   A 1 116 ? 14.404 4.694   13.444 1.00 12.41  ? 122 GLY   A C   1 
ATOM   909  O  O   . GLY   A 1 116 ? 14.734 3.648   14.025 1.00 11.85  ? 122 GLY   A O   1 
ATOM   910  N  N   . ILE   A 1 117 ? 14.310 5.884   14.062 1.00 11.89  ? 123 ILE   A N   1 
ATOM   911  C  CA  . ILE   A 1 117 ? 14.520 5.998   15.515 1.00 11.40  ? 123 ILE   A CA  1 
ATOM   912  C  C   . ILE   A 1 117 ? 13.396 6.778   16.148 1.00 11.72  ? 123 ILE   A C   1 
ATOM   913  O  O   . ILE   A 1 117 ? 12.779 7.656   15.512 1.00 12.52  ? 123 ILE   A O   1 
ATOM   914  C  CB  . ILE   A 1 117 ? 15.874 6.675   15.882 1.00 11.36  ? 123 ILE   A CB  1 
ATOM   915  C  CG1 . ILE   A 1 117 ? 16.024 7.994   15.139 1.00 12.53  ? 123 ILE   A CG1 1 
ATOM   916  C  CG2 . ILE   A 1 117 ? 17.031 5.724   15.609 1.00 12.66  ? 123 ILE   A CG2 1 
ATOM   917  C  CD1 . ILE   A 1 117 ? 17.313 8.743   15.628 1.00 13.45  ? 123 ILE   A CD1 1 
ATOM   918  N  N   . VAL   A 1 118 ? 13.086 6.464   17.413 1.00 11.58  ? 124 VAL   A N   1 
ATOM   919  C  CA  . VAL   A 1 118 ? 12.053 7.213   18.149 1.00 10.90  ? 124 VAL   A CA  1 
ATOM   920  C  C   . VAL   A 1 118 ? 12.425 8.723   18.134 1.00 11.42  ? 124 VAL   A C   1 
ATOM   921  O  O   . VAL   A 1 118 ? 13.604 9.054   18.399 1.00 11.51  ? 124 VAL   A O   1 
ATOM   922  C  CB  . VAL   A 1 118 ? 11.919 6.717   19.600 1.00 11.71  ? 124 VAL   A CB  1 
ATOM   923  C  CG1 . VAL   A 1 118 ? 10.961 7.596   20.403 1.00 12.06  ? 124 VAL   A CG1 1 
ATOM   924  C  CG2 . VAL   A 1 118 ? 11.480 5.241   19.646 1.00 12.47  ? 124 VAL   A CG2 1 
ATOM   925  N  N   . SER   A 1 119 ? 11.476 9.550   17.730 1.00 12.05  ? 125 SER   A N   1 
ATOM   926  C  CA  . SER   A 1 119 ? 11.689 11.008  17.552 1.00 13.69  ? 125 SER   A CA  1 
ATOM   927  C  C   . SER   A 1 119 ? 10.607 11.862  18.281 1.00 15.55  ? 125 SER   A C   1 
ATOM   928  O  O   . SER   A 1 119 ? 10.931 12.916  18.488 1.00 17.84  ? 125 SER   A O   1 
ATOM   929  C  CB  . SER   A 1 119 ? 11.875 11.443  16.035 1.00 15.74  ? 125 SER   A CB  1 
ATOM   930  O  OG  . SER   A 1 119 ? 11.999 12.834  15.923 1.00 16.01  ? 125 SER   A OG  1 
ATOM   931  N  N   . THR   A 1 120 ? 9.338  11.371  18.322 1.00 14.25  ? 126 THR   A N   1 
ATOM   932  C  CA  . THR   A 1 120 ? 8.166  12.069  18.979 1.00 15.26  ? 126 THR   A CA  1 
ATOM   933  C  C   . THR   A 1 120 ? 7.343  11.032  19.790 1.00 16.92  ? 126 THR   A C   1 
ATOM   934  O  O   . THR   A 1 120 ? 7.571  9.882   19.630 1.00 16.17  ? 126 THR   A O   1 
ATOM   935  C  CB  . THR   A 1 120 ? 7.225  12.836  18.023 1.00 16.32  ? 126 THR   A CB  1 
ATOM   936  O  OG1 . THR   A 1 120 ? 6.454  11.917  17.245 1.00 18.26  ? 126 THR   A OG1 1 
ATOM   937  C  CG2 . THR   A 1 120 ? 7.922  13.771  17.062 1.00 16.66  ? 126 THR   A CG2 1 
ATOM   938  N  N   . GLY   A 1 121 ? 6.295  11.518  20.478 1.00 18.95  ? 127 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 121 ? 5.420  10.584  21.238 1.00 21.91  ? 127 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 121 ? 4.462  11.336  22.183 1.00 25.08  ? 127 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 121 ? 4.492  12.559  22.223 1.00 26.31  ? 127 GLY   A O   1 
ATOM   942  N  N   . GLY   A 1 122 ? 3.649  10.589  22.910 1.00 26.50  ? 128 GLY   A N   1 
ATOM   943  C  CA  . GLY   A 1 122 ? 2.851  11.294  23.916 1.00 27.69  ? 128 GLY   A CA  1 
ATOM   944  C  C   . GLY   A 1 122 ? 1.484  10.695  23.806 1.00 30.00  ? 128 GLY   A C   1 
ATOM   945  O  O   . GLY   A 1 122 ? 1.080  10.313  22.716 1.00 30.01  ? 128 GLY   A O   1 
ATOM   946  N  N   . ASN   A 1 123 ? 0.833  10.578  24.923 1.00 29.87  ? 129 ASN   A N   1 
ATOM   947  C  CA  . ASN   A 1 123 ? -0.552 10.032  24.939 1.00 30.63  ? 129 ASN   A CA  1 
ATOM   948  C  C   . ASN   A 1 123 ? -0.767 8.710   24.200 1.00 27.81  ? 129 ASN   A C   1 
ATOM   949  O  O   . ASN   A 1 123 ? -1.926 8.558   23.730 1.00 27.89  ? 129 ASN   A O   1 
ATOM   950  C  CB  . ASN   A 1 123 ? -1.579 11.082  24.506 1.00 33.82  ? 129 ASN   A CB  1 
ATOM   951  C  CG  . ASN   A 1 123 ? -1.548 12.301  25.394 1.00 39.16  ? 129 ASN   A CG  1 
ATOM   952  O  OD1 . ASN   A 1 123 ? -1.653 12.195  26.615 1.00 42.27  ? 129 ASN   A OD1 1 
ATOM   953  N  ND2 . ASN   A 1 123 ? -1.423 13.463  24.776 1.00 38.55  ? 129 ASN   A ND2 1 
ATOM   954  N  N   . GLY   A 1 124 ? 0.203  7.818   24.213 1.00 24.13  ? 130 GLY   A N   1 
ATOM   955  C  CA  . GLY   A 1 124 ? 0.000  6.478   23.611 1.00 22.72  ? 130 GLY   A CA  1 
ATOM   956  C  C   . GLY   A 1 124 ? 0.282  6.581   22.149 1.00 19.14  ? 130 GLY   A C   1 
ATOM   957  O  O   . GLY   A 1 124 ? 0.039  5.659   21.484 1.00 19.18  ? 130 GLY   A O   1 
ATOM   958  N  N   . LEU   A 1 125 ? 0.977  7.666   21.825 1.00 17.76  ? 131 LEU   A N   1 
ATOM   959  C  CA  . LEU   A 1 125 ? 1.526  7.702   20.429 1.00 17.90  ? 131 LEU   A CA  1 
ATOM   960  C  C   . LEU   A 1 125 ? 3.030  7.757   20.465 1.00 18.04  ? 131 LEU   A C   1 
ATOM   961  O  O   . LEU   A 1 125 ? 3.576  8.483   21.281 1.00 20.39  ? 131 LEU   A O   1 
ATOM   962  C  CB  . LEU   A 1 125 ? 1.178  8.948   19.655 1.00 18.72  ? 131 LEU   A CB  1 
ATOM   963  C  CG  . LEU   A 1 125 ? -0.330 9.072   19.454 1.00 20.38  ? 131 LEU   A CG  1 
ATOM   964  C  CD1 . LEU   A 1 125 ? -0.661 10.495  19.090 1.00 22.46  ? 131 LEU   A CD1 1 
ATOM   965  C  CD2 . LEU   A 1 125 ? -0.873 8.088   18.429 1.00 20.79  ? 131 LEU   A CD2 1 
ATOM   966  N  N   . VAL   A 1 126 ? 3.600  7.082   19.463 1.00 14.94  ? 132 VAL   A N   1 
ATOM   967  C  CA  . VAL   A 1 126 ? 5.072  7.240   19.353 1.00 13.78  ? 132 VAL   A CA  1 
ATOM   968  C  C   . VAL   A 1 126 ? 5.347  7.531   17.886 1.00 13.75  ? 132 VAL   A C   1 
ATOM   969  O  O   . VAL   A 1 126 ? 4.725  6.917   17.050 1.00 14.66  ? 132 VAL   A O   1 
ATOM   970  C  CB  . VAL   A 1 126 ? 5.829  5.972   19.836 1.00 14.13  ? 132 VAL   A CB  1 
ATOM   971  C  CG1 . VAL   A 1 126 ? 5.327  4.704   19.176 1.00 14.54  ? 132 VAL   A CG1 1 
ATOM   972  C  CG2 . VAL   A 1 126 ? 7.338  6.147   19.741 1.00 14.09  ? 132 VAL   A CG2 1 
ATOM   973  N  N   . GLY   A 1 127 ? 6.274  8.465   17.673 1.00 12.95  ? 133 GLY   A N   1 
ATOM   974  C  CA  . GLY   A 1 127 ? 6.622  8.801   16.270 1.00 12.74  ? 133 GLY   A CA  1 
ATOM   975  C  C   . GLY   A 1 127 ? 8.066  8.405   16.022 1.00 13.26  ? 133 GLY   A C   1 
ATOM   976  O  O   . GLY   A 1 127 ? 8.913  8.526   16.869 1.00 13.98  ? 133 GLY   A O   1 
ATOM   977  N  N   . PHE   A 1 128 ? 8.298  7.981   14.793 1.00 12.30  ? 134 PHE   A N   1 
ATOM   978  C  CA  . PHE   A 1 128 ? 9.646  7.537   14.382 1.00 12.14  ? 134 PHE   A CA  1 
ATOM   979  C  C   . PHE   A 1 128 ? 10.174 8.370   13.180 1.00 13.31  ? 134 PHE   A C   1 
ATOM   980  O  O   . PHE   A 1 128 ? 9.456  8.590   12.306 1.00 14.22  ? 134 PHE   A O   1 
ATOM   981  C  CB  . PHE   A 1 128 ? 9.486  6.083   13.930 1.00 12.47  ? 134 PHE   A CB  1 
ATOM   982  C  CG  . PHE   A 1 128 ? 8.894  5.175   14.986 1.00 12.07  ? 134 PHE   A CG  1 
ATOM   983  C  CD1 . PHE   A 1 128 ? 9.627  4.707   16.069 1.00 12.38  ? 134 PHE   A CD1 1 
ATOM   984  C  CD2 . PHE   A 1 128 ? 7.601  4.722   14.835 1.00 12.31  ? 134 PHE   A CD2 1 
ATOM   985  C  CE1 . PHE   A 1 128 ? 9.060  3.846   16.992 1.00 12.39  ? 134 PHE   A CE1 1 
ATOM   986  C  CE2 . PHE   A 1 128 ? 7.024  3.878   15.762 1.00 12.88  ? 134 PHE   A CE2 1 
ATOM   987  C  CZ  . PHE   A 1 128 ? 7.755  3.442   16.844 1.00 11.68  ? 134 PHE   A CZ  1 
ATOM   988  N  N   . ALA   A 1 129 ? 11.444 8.756   13.298 1.00 12.18  ? 135 ALA   A N   1 
ATOM   989  C  CA  . ALA   A 1 129 ? 12.064 9.503   12.146 1.00 12.19  ? 135 ALA   A CA  1 
ATOM   990  C  C   . ALA   A 1 129 ? 12.537 8.418   11.178 1.00 12.44  ? 135 ALA   A C   1 
ATOM   991  O  O   . ALA   A 1 129 ? 13.342 7.590   11.614 1.00 12.23  ? 135 ALA   A O   1 
ATOM   992  C  CB  . ALA   A 1 129 ? 13.197 10.418  12.620 1.00 12.36  ? 135 ALA   A CB  1 
ATOM   993  N  N   . ASP   A 1 130 ? 11.981 8.424   9.977  1.00 12.55  ? 136 ASP   A N   1 
ATOM   994  C  CA  . ASP   A 1 130 ? 12.368 7.409   8.989  1.00 13.11  ? 136 ASP   A CA  1 
ATOM   995  C  C   . ASP   A 1 130 ? 13.771 7.689   8.490  1.00 13.70  ? 136 ASP   A C   1 
ATOM   996  O  O   . ASP   A 1 130 ? 14.173 8.866   8.343  1.00 13.90  ? 136 ASP   A O   1 
ATOM   997  C  CB  . ASP   A 1 130 ? 11.407 7.517   7.774  1.00 14.78  ? 136 ASP   A CB  1 
ATOM   998  C  CG  . ASP   A 1 130 ? 11.675 6.490   6.702  1.00 20.49  ? 136 ASP   A CG  1 
ATOM   999  O  OD1 . ASP   A 1 130 ? 11.761 5.294   7.035  1.00 19.69  ? 136 ASP   A OD1 1 
ATOM   1000 O  OD2 . ASP   A 1 130 ? 11.860 6.896   5.524  1.00 25.77  ? 136 ASP   A OD2 1 
ATOM   1001 N  N   . VAL   A 1 131 ? 14.519 6.617   8.196  1.00 12.44  ? 137 VAL   A N   1 
ATOM   1002 C  CA  . VAL   A 1 131 ? 15.844 6.778   7.548  1.00 11.83  ? 137 VAL   A CA  1 
ATOM   1003 C  C   . VAL   A 1 131 ? 15.961 5.942   6.247  1.00 12.51  ? 137 VAL   A C   1 
ATOM   1004 O  O   . VAL   A 1 131 ? 17.025 5.940   5.629  1.00 12.68  ? 137 VAL   A O   1 
ATOM   1005 C  CB  . VAL   A 1 131 ? 17.027 6.411   8.478  1.00 12.08  ? 137 VAL   A CB  1 
ATOM   1006 C  CG1 . VAL   A 1 131 ? 17.078 7.322   9.715  1.00 13.21  ? 137 VAL   A CG1 1 
ATOM   1007 C  CG2 . VAL   A 1 131 ? 17.008 4.938   8.876  1.00 13.27  ? 137 VAL   A CG2 1 
ATOM   1008 N  N   . ARG   A 1 132 ? 14.885 5.244   5.829  1.00 13.55  ? 138 ARG   A N   1 
ATOM   1009 C  CA  . ARG   A 1 132 ? 14.963 4.342   4.687  1.00 13.19  ? 138 ARG   A CA  1 
ATOM   1010 C  C   . ARG   A 1 132 ? 15.218 5.046   3.363  1.00 14.99  ? 138 ARG   A C   1 
ATOM   1011 O  O   . ARG   A 1 132 ? 15.637 4.385   2.383  1.00 16.08  ? 138 ARG   A O   1 
ATOM   1012 C  CB  . ARG   A 1 132 ? 13.691 3.491   4.604  1.00 14.12  ? 138 ARG   A CB  1 
ATOM   1013 C  CG  . ARG   A 1 132 ? 13.545 2.530   5.801  1.00 14.26  ? 138 ARG   A CG  1 
ATOM   1014 C  CD  . ARG   A 1 132 ? 12.232 1.784   5.668  1.00 15.07  ? 138 ARG   A CD  1 
ATOM   1015 N  NE  . ARG   A 1 132 ? 11.102 2.689   5.937  1.00 16.61  ? 138 ARG   A NE  1 
ATOM   1016 C  CZ  . ARG   A 1 132 ? 9.825  2.296   6.002  1.00 19.06  ? 138 ARG   A CZ  1 
ATOM   1017 N  NH1 . ARG   A 1 132 ? 9.494  1.037   5.718  1.00 18.60  ? 138 ARG   A NH1 1 
ATOM   1018 N  NH2 . ARG   A 1 132 ? 8.872  3.172   6.304  1.00 19.58  ? 138 ARG   A NH2 1 
ATOM   1019 N  N   . ASP   A 1 133 ? 14.912 6.358   3.282  1.00 14.34  ? 139 ASP   A N   1 
ATOM   1020 C  CA  . ASP   A 1 133 ? 15.163 7.076   2.033  1.00 15.34  ? 139 ASP   A CA  1 
ATOM   1021 C  C   . ASP   A 1 133 ? 16.600 7.600   1.921  1.00 15.84  ? 139 ASP   A C   1 
ATOM   1022 O  O   . ASP   A 1 133 ? 16.969 8.118   0.855  1.00 17.14  ? 139 ASP   A O   1 
ATOM   1023 C  CB  . ASP   A 1 133 ? 14.173 8.259   1.896  1.00 17.13  ? 139 ASP   A CB  1 
ATOM   1024 C  CG  . ASP   A 1 133 ? 14.395 9.317   2.971  1.00 20.81  ? 139 ASP   A CG  1 
ATOM   1025 O  OD1 . ASP   A 1 133 ? 14.551 8.942   4.158  1.00 18.40  ? 139 ASP   A OD1 1 
ATOM   1026 O  OD2 . ASP   A 1 133 ? 14.392 10.514  2.639  1.00 22.60  ? 139 ASP   A OD2 1 
ATOM   1027 N  N   . LEU   A 1 134 ? 17.416 7.499   3.003  1.00 15.29  ? 140 LEU   A N   1 
ATOM   1028 C  CA  . LEU   A 1 134 ? 18.782 8.055   3.029  1.00 14.92  ? 140 LEU   A CA  1 
ATOM   1029 C  C   . LEU   A 1 134 ? 19.730 7.001   2.461  1.00 15.64  ? 140 LEU   A C   1 
ATOM   1030 O  O   . LEU   A 1 134 ? 20.419 6.286   3.213  1.00 15.43  ? 140 LEU   A O   1 
ATOM   1031 C  CB  . LEU   A 1 134 ? 19.149 8.429   4.479  1.00 14.34  ? 140 LEU   A CB  1 
ATOM   1032 C  CG  . LEU   A 1 134 ? 18.184 9.458   5.111  1.00 14.93  ? 140 LEU   A CG  1 
ATOM   1033 C  CD1 . LEU   A 1 134 ? 18.565 9.717   6.548  1.00 15.25  ? 140 LEU   A CD1 1 
ATOM   1034 C  CD2 . LEU   A 1 134 ? 18.205 10.799  4.356  1.00 15.65  ? 140 LEU   A CD2 1 
ATOM   1035 N  N   . LEU   A 1 135 ? 19.697 6.849   1.129  1.00 15.26  ? 141 LEU   A N   1 
ATOM   1036 C  CA  . LEU   A 1 135 ? 20.453 5.764   0.495  1.00 15.94  ? 141 LEU   A CA  1 
ATOM   1037 C  C   . LEU   A 1 135 ? 21.953 5.884   0.697  1.00 16.41  ? 141 LEU   A C   1 
ATOM   1038 O  O   . LEU   A 1 135 ? 22.667 4.868   0.705  1.00 17.51  ? 141 LEU   A O   1 
ATOM   1039 C  CB  . LEU   A 1 135 ? 20.098 5.653   -1.018 1.00 17.36  ? 141 LEU   A CB  1 
ATOM   1040 C  CG  . LEU   A 1 135 ? 18.585 5.652   -1.328 1.00 19.68  ? 141 LEU   A CG  1 
ATOM   1041 C  CD1 . LEU   A 1 135 ? 18.365 5.388   -2.807 1.00 21.63  ? 141 LEU   A CD1 1 
ATOM   1042 C  CD2 . LEU   A 1 135 ? 17.807 4.605   -0.479 1.00 20.43  ? 141 LEU   A CD2 1 
ATOM   1043 N  N   . TRP   A 1 136 ? 22.436 7.126   0.845  1.00 15.69  ? 142 TRP   A N   1 
ATOM   1044 C  CA  . TRP   A 1 136 ? 23.860 7.371   1.022  1.00 15.49  ? 142 TRP   A CA  1 
ATOM   1045 C  C   . TRP   A 1 136 ? 24.423 6.777   2.310  1.00 16.33  ? 142 TRP   A C   1 
ATOM   1046 O  O   . TRP   A 1 136 ? 25.643 6.641   2.420  1.00 16.91  ? 142 TRP   A O   1 
ATOM   1047 C  CB  . TRP   A 1 136 ? 24.161 8.879   0.904  1.00 15.64  ? 142 TRP   A CB  1 
ATOM   1048 C  CG  . TRP   A 1 136 ? 23.357 9.726   1.836  1.00 15.10  ? 142 TRP   A CG  1 
ATOM   1049 C  CD1 . TRP   A 1 136 ? 22.189 10.374  1.561  1.00 16.06  ? 142 TRP   A CD1 1 
ATOM   1050 C  CD2 . TRP   A 1 136 ? 23.685 10.040  3.205  1.00 15.37  ? 142 TRP   A CD2 1 
ATOM   1051 N  NE1 . TRP   A 1 136 ? 21.750 11.057  2.686  1.00 16.92  ? 142 TRP   A NE1 1 
ATOM   1052 C  CE2 . TRP   A 1 136 ? 22.673 10.890  3.693  1.00 16.03  ? 142 TRP   A CE2 1 
ATOM   1053 C  CE3 . TRP   A 1 136 ? 24.773 9.733   4.040  1.00 16.62  ? 142 TRP   A CE3 1 
ATOM   1054 C  CZ2 . TRP   A 1 136 ? 22.700 11.397  5.006  1.00 16.71  ? 142 TRP   A CZ2 1 
ATOM   1055 C  CZ3 . TRP   A 1 136 ? 24.809 10.254  5.320  1.00 17.41  ? 142 TRP   A CZ3 1 
ATOM   1056 C  CH2 . TRP   A 1 136 ? 23.789 11.082  5.786  1.00 17.00  ? 142 TRP   A CH2 1 
ATOM   1057 N  N   . LEU   A 1 137 ? 23.555 6.403   3.296  1.00 15.82  ? 143 LEU   A N   1 
ATOM   1058 C  CA  . LEU   A 1 137 ? 24.080 5.762   4.508  1.00 17.54  ? 143 LEU   A CA  1 
ATOM   1059 C  C   . LEU   A 1 137 ? 24.785 4.444   4.193  1.00 20.19  ? 143 LEU   A C   1 
ATOM   1060 O  O   . LEU   A 1 137 ? 25.642 4.024   4.979  1.00 20.45  ? 143 LEU   A O   1 
ATOM   1061 C  CB  . LEU   A 1 137 ? 22.947 5.496   5.505  1.00 16.27  ? 143 LEU   A CB  1 
ATOM   1062 C  CG  . LEU   A 1 137 ? 22.396 6.741   6.197  1.00 15.90  ? 143 LEU   A CG  1 
ATOM   1063 C  CD1 . LEU   A 1 137 ? 21.124 6.390   6.974  1.00 16.13  ? 143 LEU   A CD1 1 
ATOM   1064 C  CD2 . LEU   A 1 137 ? 23.467 7.378   7.155  1.00 16.90  ? 143 LEU   A CD2 1 
ATOM   1065 N  N   . ASP   A 1 138 ? 24.421 3.784   3.050  1.00 22.96  ? 144 ASP   A N   1 
ATOM   1066 C  CA  . ASP   A 1 138 ? 24.984 2.485   2.651  1.00 26.00  ? 144 ASP   A CA  1 
ATOM   1067 C  C   . ASP   A 1 138 ? 26.314 2.564   1.915  1.00 30.22  ? 144 ASP   A C   1 
ATOM   1068 O  O   . ASP   A 1 138 ? 26.825 1.515   1.511  1.00 30.68  ? 144 ASP   A O   1 
ATOM   1069 C  CB  . ASP   A 1 138 ? 24.010 1.731   1.701  1.00 27.42  ? 144 ASP   A CB  1 
ATOM   1070 C  CG  . ASP   A 1 138 ? 22.655 1.389   2.270  1.00 32.35  ? 144 ASP   A CG  1 
ATOM   1071 O  OD1 . ASP   A 1 138 ? 22.498 1.452   3.494  1.00 32.22  ? 144 ASP   A OD1 1 
ATOM   1072 O  OD2 . ASP   A 1 138 ? 21.733 1.072   1.479  1.00 38.36  ? 144 ASP   A OD2 1 
ATOM   1073 N  N   . GLU   A 1 139 ? 26.865 3.765   1.692  1.00 32.55  ? 145 GLU   A N   1 
ATOM   1074 C  CA  . GLU   A 1 139 ? 28.103 3.889   0.904  1.00 35.93  ? 145 GLU   A CA  1 
ATOM   1075 C  C   . GLU   A 1 139 ? 29.073 4.947   1.468  1.00 38.53  ? 145 GLU   A C   1 
ATOM   1076 O  O   . GLU   A 1 139 ? 28.733 5.646   2.425  1.00 38.33  ? 145 GLU   A O   1 
ATOM   1077 C  CB  . GLU   A 1 139 ? 27.710 4.239   -0.544 1.00 39.17  ? 145 GLU   A CB  1 
ATOM   1078 C  CG  . GLU   A 1 139 ? 26.994 5.576   -0.619 1.00 45.97  ? 145 GLU   A CG  1 
ATOM   1079 C  CD  . GLU   A 1 139 ? 26.177 5.840   -1.870 1.00 54.55  ? 145 GLU   A CD  1 
ATOM   1080 O  OE1 . GLU   A 1 139 ? 26.002 7.032   -2.218 1.00 55.12  ? 145 GLU   A OE1 1 
ATOM   1081 O  OE2 . GLU   A 1 139 ? 25.699 4.862   -2.494 1.00 58.02  ? 145 GLU   A OE2 1 
ATOM   1082 N  N   . GLU   A 1 140 ? 30.269 5.063   0.847  1.00 41.13  ? 146 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 140 ? 31.355 6.011   1.148  1.00 44.19  ? 146 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 140 ? 32.107 5.649   2.423  1.00 45.78  ? 146 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 140 ? 33.321 5.440   2.356  1.00 46.71  ? 146 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 140 ? 30.874 7.474   1.150  1.00 47.83  ? 146 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 140 ? 31.859 8.494   1.711  1.00 55.48  ? 146 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 140 ? 32.789 9.137   0.696  1.00 64.59  ? 146 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 140 ? 32.698 10.372  0.507  1.00 66.35  ? 146 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 140 ? 33.608 8.409   0.087  1.00 67.69  ? 146 GLU   A OE2 1 
ATOM   1091 N  N   . SER   B 1 1   ? 21.896 -21.277 7.627  1.00 18.74  ? 7   SER   C N   1 
ATOM   1092 C  CA  . SER   B 1 1   ? 20.779 -21.073 8.569  1.00 18.36  ? 7   SER   C CA  1 
ATOM   1093 C  C   . SER   B 1 1   ? 20.751 -22.189 9.646  1.00 18.89  ? 7   SER   C C   1 
ATOM   1094 O  O   . SER   B 1 1   ? 21.405 -23.226 9.474  1.00 20.29  ? 7   SER   C O   1 
ATOM   1095 C  CB  . SER   B 1 1   ? 19.461 -21.116 7.805  1.00 21.70  ? 7   SER   C CB  1 
ATOM   1096 O  OG  . SER   B 1 1   ? 19.288 -22.409 7.253  1.00 25.55  ? 7   SER   C OG  1 
ATOM   1097 N  N   . GLY   B 1 2   ? 19.966 -21.974 10.715 1.00 18.38  ? 8   GLY   C N   1 
ATOM   1098 C  CA  . GLY   B 1 2   ? 19.829 -22.955 11.783 1.00 17.46  ? 8   GLY   C CA  1 
ATOM   1099 C  C   . GLY   B 1 2   ? 19.524 -22.330 13.123 1.00 16.51  ? 8   GLY   C C   1 
ATOM   1100 O  O   . GLY   B 1 2   ? 19.925 -21.197 13.391 1.00 16.64  ? 8   GLY   C O   1 
ATOM   1101 N  N   . ALA   B 1 3   ? 18.865 -23.100 14.001 1.00 15.08  ? 9   ALA   C N   1 
ATOM   1102 C  CA  . ALA   B 1 3   ? 18.531 -22.603 15.337 1.00 14.55  ? 9   ALA   C CA  1 
ATOM   1103 C  C   . ALA   B 1 3   ? 18.657 -23.731 16.364 1.00 13.62  ? 9   ALA   C C   1 
ATOM   1104 O  O   . ALA   B 1 3   ? 18.713 -24.916 15.978 1.00 14.48  ? 9   ALA   C O   1 
ATOM   1105 C  CB  . ALA   B 1 3   ? 17.089 -22.069 15.341 1.00 16.11  ? 9   ALA   C CB  1 
ATOM   1106 N  N   . ILE   B 1 4   ? 18.692 -23.370 17.655 1.00 13.40  ? 10  ILE   C N   1 
ATOM   1107 C  CA  . ILE   B 1 4   ? 18.622 -24.305 18.782 1.00 13.03  ? 10  ILE   C CA  1 
ATOM   1108 C  C   . ILE   B 1 4   ? 17.208 -24.115 19.375 1.00 14.43  ? 10  ILE   C C   1 
ATOM   1109 O  O   . ILE   B 1 4   ? 16.772 -22.971 19.579 1.00 15.30  ? 10  ILE   C O   1 
ATOM   1110 C  CB  . ILE   B 1 4   ? 19.664 -23.980 19.868 1.00 13.53  ? 10  ILE   C CB  1 
ATOM   1111 C  CG1 . ILE   B 1 4   ? 21.104 -23.864 19.297 1.00 15.05  ? 10  ILE   C CG1 1 
ATOM   1112 C  CG2 . ILE   B 1 4   ? 19.604 -25.051 20.981 1.00 14.91  ? 10  ILE   C CG2 1 
ATOM   1113 C  CD1 . ILE   B 1 4   ? 22.061 -23.207 20.285 1.00 15.69  ? 10  ILE   C CD1 1 
ATOM   1114 N  N   . TYR   B 1 5   ? 16.512 -25.221 19.684 1.00 14.01  ? 11  TYR   C N   1 
ATOM   1115 C  CA  . TYR   B 1 5   ? 15.164 -25.150 20.249 1.00 14.61  ? 11  TYR   C CA  1 
ATOM   1116 C  C   . TYR   B 1 5   ? 15.224 -25.827 21.626 1.00 16.24  ? 11  TYR   C C   1 
ATOM   1117 O  O   . TYR   B 1 5   ? 15.275 -27.053 21.694 1.00 17.52  ? 11  TYR   C O   1 
ATOM   1118 C  CB  . TYR   B 1 5   ? 14.132 -25.863 19.336 1.00 15.18  ? 11  TYR   C CB  1 
ATOM   1119 C  CG  . TYR   B 1 5   ? 13.936 -25.109 18.034 1.00 15.91  ? 11  TYR   C CG  1 
ATOM   1120 C  CD1 . TYR   B 1 5   ? 13.110 -23.983 17.972 1.00 16.23  ? 11  TYR   C CD1 1 
ATOM   1121 C  CD2 . TYR   B 1 5   ? 14.626 -25.473 16.884 1.00 16.91  ? 11  TYR   C CD2 1 
ATOM   1122 C  CE1 . TYR   B 1 5   ? 12.994 -23.245 16.801 1.00 17.31  ? 11  TYR   C CE1 1 
ATOM   1123 C  CE2 . TYR   B 1 5   ? 14.511 -24.743 15.704 1.00 17.96  ? 11  TYR   C CE2 1 
ATOM   1124 C  CZ  . TYR   B 1 5   ? 13.676 -23.645 15.661 1.00 18.61  ? 11  TYR   C CZ  1 
ATOM   1125 O  OH  . TYR   B 1 5   ? 13.580 -22.909 14.494 1.00 20.09  ? 11  TYR   C OH  1 
ATOM   1126 N  N   . VAL   B 1 6   ? 15.278 -25.046 22.712 1.00 16.60  ? 12  VAL   C N   1 
ATOM   1127 C  CA  . VAL   B 1 6   ? 15.369 -25.587 24.078 1.00 17.04  ? 12  VAL   C CA  1 
ATOM   1128 C  C   . VAL   B 1 6   ? 14.247 -24.992 24.928 1.00 17.57  ? 12  VAL   C C   1 
ATOM   1129 O  O   . VAL   B 1 6   ? 14.061 -23.773 24.912 1.00 16.89  ? 12  VAL   C O   1 
ATOM   1130 C  CB  . VAL   B 1 6   ? 16.773 -25.334 24.675 1.00 18.43  ? 12  VAL   C CB  1 
ATOM   1131 C  CG1 . VAL   B 1 6   ? 17.148 -23.842 24.599 1.00 18.17  ? 12  VAL   C CG1 1 
ATOM   1132 C  CG2 . VAL   B 1 6   ? 16.832 -25.849 26.108 1.00 19.85  ? 12  VAL   C CG2 1 
ATOM   1133 N  N   . GLY   B 1 7   ? 13.418 -25.830 25.587 1.00 18.52  ? 13  GLY   C N   1 
ATOM   1134 C  CA  . GLY   B 1 7   ? 12.283 -25.311 26.352 1.00 18.36  ? 13  GLY   C CA  1 
ATOM   1135 C  C   . GLY   B 1 7   ? 11.357 -24.464 25.479 1.00 18.90  ? 13  GLY   C C   1 
ATOM   1136 O  O   . GLY   B 1 7   ? 11.084 -24.831 24.332 1.00 19.75  ? 13  GLY   C O   1 
ATOM   1137 N  N   . ASN   B 1 8   ? 11.019 -23.269 25.934 1.00 18.24  ? 14  ASN   C N   1 
ATOM   1138 C  CA  . ASN   B 1 8   ? 10.227 -22.351 25.113 1.00 18.52  ? 14  ASN   C CA  1 
ATOM   1139 C  C   . ASN   B 1 8   ? 11.113 -21.252 24.537 1.00 17.53  ? 14  ASN   C C   1 
ATOM   1140 O  O   . ASN   B 1 8   ? 10.655 -20.119 24.384 1.00 17.13  ? 14  ASN   C O   1 
ATOM   1141 C  CB  . ASN   B 1 8   ? 9.019  -21.785 25.855 1.00 20.47  ? 14  ASN   C CB  1 
ATOM   1142 C  CG  . ASN   B 1 8   ? 7.911  -22.822 25.984 1.00 27.27  ? 14  ASN   C CG  1 
ATOM   1143 O  OD1 . ASN   B 1 8   ? 7.047  -22.948 25.109 1.00 30.03  ? 14  ASN   C OD1 1 
ATOM   1144 N  ND2 . ASN   B 1 8   ? 7.967  -23.609 27.043 1.00 29.33  ? 14  ASN   C ND2 1 
ATOM   1145 N  N   . TYR   B 1 9   ? 12.349 -21.619 24.154 1.00 15.74  ? 15  TYR   C N   1 
ATOM   1146 C  CA  . TYR   B 1 9   ? 13.286 -20.659 23.550 1.00 15.80  ? 15  TYR   C CA  1 
ATOM   1147 C  C   . TYR   B 1 9   ? 13.755 -21.121 22.176 1.00 15.35  ? 15  TYR   C C   1 
ATOM   1148 O  O   . TYR   B 1 9   ? 13.961 -22.329 21.958 1.00 16.27  ? 15  TYR   C O   1 
ATOM   1149 C  CB  . TYR   B 1 9   ? 14.550 -20.487 24.437 1.00 16.04  ? 15  TYR   C CB  1 
ATOM   1150 C  CG  . TYR   B 1 9   ? 14.231 -19.966 25.831 1.00 18.30  ? 15  TYR   C CG  1 
ATOM   1151 C  CD1 . TYR   B 1 9   ? 13.695 -18.698 26.015 1.00 19.76  ? 15  TYR   C CD1 1 
ATOM   1152 C  CD2 . TYR   B 1 9   ? 14.514 -20.724 26.964 1.00 20.79  ? 15  TYR   C CD2 1 
ATOM   1153 C  CE1 . TYR   B 1 9   ? 13.370 -18.231 27.287 1.00 22.47  ? 15  TYR   C CE1 1 
ATOM   1154 C  CE2 . TYR   B 1 9   ? 14.228 -20.249 28.244 1.00 22.71  ? 15  TYR   C CE2 1 
ATOM   1155 C  CZ  . TYR   B 1 9   ? 13.689 -18.988 28.399 1.00 24.87  ? 15  TYR   C CZ  1 
ATOM   1156 O  OH  . TYR   B 1 9   ? 13.408 -18.506 29.664 1.00 29.77  ? 15  TYR   C OH  1 
ATOM   1157 N  N   . ARG   B 1 10  ? 13.994 -20.158 21.280 1.00 13.96  ? 16  ARG   C N   1 
ATOM   1158 C  CA  . ARG   B 1 10  ? 14.607 -20.392 19.961 1.00 13.86  ? 16  ARG   C CA  1 
ATOM   1159 C  C   . ARG   B 1 10  ? 15.875 -19.531 19.946 1.00 13.94  ? 16  ARG   C C   1 
ATOM   1160 O  O   . ARG   B 1 10  ? 15.782 -18.314 20.132 1.00 13.86  ? 16  ARG   C O   1 
ATOM   1161 C  CB  . ARG   B 1 10  ? 13.658 -19.950 18.810 1.00 15.61  ? 16  ARG   C CB  1 
ATOM   1162 C  CG  . ARG   B 1 10  ? 14.310 -19.779 17.418 1.00 14.70  ? 16  ARG   C CG  1 
ATOM   1163 C  CD  . ARG   B 1 10  ? 13.226 -19.490 16.370 1.00 14.46  ? 16  ARG   C CD  1 
ATOM   1164 N  NE  . ARG   B 1 10  ? 13.664 -18.532 15.351 1.00 16.60  ? 16  ARG   C NE  1 
ATOM   1165 C  CZ  . ARG   B 1 10  ? 14.167 -18.857 14.158 1.00 19.00  ? 16  ARG   C CZ  1 
ATOM   1166 N  NH1 . ARG   B 1 10  ? 14.359 -20.133 13.832 1.00 20.33  ? 16  ARG   C NH1 1 
ATOM   1167 N  NH2 . ARG   B 1 10  ? 14.500 -17.906 13.287 1.00 18.73  ? 16  ARG   C NH2 1 
ATOM   1168 N  N   . VAL   B 1 11  ? 17.048 -20.143 19.746 1.00 12.49  ? 17  VAL   C N   1 
ATOM   1169 C  CA  . VAL   B 1 11  ? 18.334 -19.427 19.707 1.00 12.61  ? 17  VAL   C CA  1 
ATOM   1170 C  C   . VAL   B 1 11  ? 18.816 -19.373 18.284 1.00 13.05  ? 17  VAL   C C   1 
ATOM   1171 O  O   . VAL   B 1 11  ? 18.999 -20.426 17.642 1.00 13.55  ? 17  VAL   C O   1 
ATOM   1172 C  CB  . VAL   B 1 11  ? 19.409 -20.128 20.576 1.00 13.86  ? 17  VAL   C CB  1 
ATOM   1173 C  CG1 . VAL   B 1 11  ? 20.662 -19.252 20.690 1.00 15.40  ? 17  VAL   C CG1 1 
ATOM   1174 C  CG2 . VAL   B 1 11  ? 18.850 -20.527 21.958 1.00 15.32  ? 17  VAL   C CG2 1 
ATOM   1175 N  N   . VAL   B 1 12  ? 19.035 -18.152 17.757 1.00 12.96  ? 18  VAL   C N   1 
ATOM   1176 C  CA  A VAL   B 1 12  ? 19.497 -17.981 16.372 0.50 12.38  ? 18  VAL   C CA  1 
ATOM   1177 C  CA  B VAL   B 1 12  ? 19.430 -17.937 16.358 0.50 14.39  ? 18  VAL   C CA  1 
ATOM   1178 C  C   . VAL   B 1 12  ? 20.632 -16.970 16.288 1.00 13.55  ? 18  VAL   C C   1 
ATOM   1179 O  O   . VAL   B 1 12  ? 20.869 -16.200 17.240 1.00 13.92  ? 18  VAL   C O   1 
ATOM   1180 C  CB  A VAL   B 1 12  ? 18.339 -17.502 15.448 0.50 11.84  ? 18  VAL   C CB  1 
ATOM   1181 C  CB  B VAL   B 1 12  ? 18.228 -17.275 15.581 0.50 17.72  ? 18  VAL   C CB  1 
ATOM   1182 C  CG1 A VAL   B 1 12  ? 17.336 -18.605 15.204 0.50 12.19  ? 18  VAL   C CG1 1 
ATOM   1183 C  CG1 B VAL   B 1 12  ? 18.405 -17.365 14.078 0.50 18.29  ? 18  VAL   C CG1 1 
ATOM   1184 C  CG2 A VAL   B 1 12  ? 17.712 -16.183 15.956 0.50 9.91   ? 18  VAL   C CG2 1 
ATOM   1185 C  CG2 B VAL   B 1 12  ? 16.866 -17.829 15.987 0.50 20.26  ? 18  VAL   C CG2 1 
ATOM   1186 N  N   . ASN   B 1 13  ? 21.331 -16.923 15.119 1.00 12.67  ? 19  ASN   C N   1 
ATOM   1187 C  CA  . ASN   B 1 13  ? 22.338 -15.881 14.917 1.00 12.21  ? 19  ASN   C CA  1 
ATOM   1188 C  C   . ASN   B 1 13  ? 21.532 -14.526 14.864 1.00 12.25  ? 19  ASN   C C   1 
ATOM   1189 O  O   . ASN   B 1 13  ? 20.512 -14.436 14.182 1.00 13.11  ? 19  ASN   C O   1 
ATOM   1190 C  CB  . ASN   B 1 13  ? 23.005 -16.043 13.551 1.00 13.44  ? 19  ASN   C CB  1 
ATOM   1191 C  CG  . ASN   B 1 13  ? 23.862 -17.302 13.488 1.00 12.85  ? 19  ASN   C CG  1 
ATOM   1192 O  OD1 . ASN   B 1 13  ? 23.400 -18.381 13.058 1.00 13.97  ? 19  ASN   C OD1 1 
ATOM   1193 N  ND2 . ASN   B 1 13  ? 25.127 -17.183 13.920 1.00 13.07  ? 19  ASN   C ND2 1 
ATOM   1194 N  N   . ARG   B 1 14  ? 22.029 -13.494 15.565 1.00 12.44  ? 20  ARG   C N   1 
ATOM   1195 C  CA  . ARG   B 1 14  ? 21.283 -12.205 15.589 1.00 12.70  ? 20  ARG   C CA  1 
ATOM   1196 C  C   . ARG   B 1 14  ? 21.116 -11.655 14.164 1.00 13.69  ? 20  ARG   C C   1 
ATOM   1197 O  O   . ARG   B 1 14  ? 20.038 -11.132 13.812 1.00 14.42  ? 20  ARG   C O   1 
ATOM   1198 C  CB  . ARG   B 1 14  ? 22.013 -11.185 16.440 1.00 13.04  ? 20  ARG   C CB  1 
ATOM   1199 C  CG  . ARG   B 1 14  ? 21.212 -9.854  16.654 1.00 13.50  ? 20  ARG   C CG  1 
ATOM   1200 C  CD  . ARG   B 1 14  ? 22.094 -8.904  17.444 1.00 14.53  ? 20  ARG   C CD  1 
ATOM   1201 N  NE  . ARG   B 1 14  ? 21.422 -7.669  17.898 1.00 15.34  ? 20  ARG   C NE  1 
ATOM   1202 C  CZ  . ARG   B 1 14  ? 21.312 -6.569  17.156 1.00 15.82  ? 20  ARG   C CZ  1 
ATOM   1203 N  NH1 . ARG   B 1 14  ? 21.699 -6.576  15.881 1.00 16.55  ? 20  ARG   C NH1 1 
ATOM   1204 N  NH2 . ARG   B 1 14  ? 20.799 -5.454  17.677 1.00 15.28  ? 20  ARG   C NH2 1 
ATOM   1205 N  N   . HIS   B 1 15  ? 22.136 -11.880 13.312 1.00 13.06  ? 21  HIS   C N   1 
ATOM   1206 C  CA  . HIS   B 1 15  ? 22.085 -11.340 11.940 1.00 13.74  ? 21  HIS   C CA  1 
ATOM   1207 C  C   . HIS   B 1 15  ? 21.073 -12.064 11.033 1.00 14.96  ? 21  HIS   C C   1 
ATOM   1208 O  O   . HIS   B 1 15  ? 20.749 -11.532 9.962  1.00 16.54  ? 21  HIS   C O   1 
ATOM   1209 C  CB  . HIS   B 1 15  ? 23.481 -11.248 11.273 1.00 14.17  ? 21  HIS   C CB  1 
ATOM   1210 C  CG  . HIS   B 1 15  ? 24.060 -12.563 10.834 1.00 14.42  ? 21  HIS   C CG  1 
ATOM   1211 N  ND1 . HIS   B 1 15  ? 24.804 -13.362 11.701 1.00 15.61  ? 21  HIS   C ND1 1 
ATOM   1212 C  CD2 . HIS   B 1 15  ? 24.039 -13.142 9.607  1.00 15.77  ? 21  HIS   C CD2 1 
ATOM   1213 C  CE1 . HIS   B 1 15  ? 25.181 -14.413 10.974 1.00 16.45  ? 21  HIS   C CE1 1 
ATOM   1214 N  NE2 . HIS   B 1 15  ? 24.740 -14.322 9.713  1.00 15.98  ? 21  HIS   C NE2 1 
ATOM   1215 N  N   . LEU   B 1 16  ? 20.559 -13.236 11.476 1.00 13.74  ? 22  LEU   C N   1 
ATOM   1216 C  CA  . LEU   B 1 16  ? 19.537 -13.981 10.717 1.00 14.80  ? 22  LEU   C CA  1 
ATOM   1217 C  C   . LEU   B 1 16  ? 18.155 -13.926 11.402 1.00 15.62  ? 22  LEU   C C   1 
ATOM   1218 O  O   . LEU   B 1 16  ? 17.230 -14.622 10.952 1.00 16.33  ? 22  LEU   C O   1 
ATOM   1219 C  CB  . LEU   B 1 16  ? 19.989 -15.426 10.522 1.00 15.10  ? 22  LEU   C CB  1 
ATOM   1220 C  CG  . LEU   B 1 16  ? 21.295 -15.582 9.714  1.00 15.60  ? 22  LEU   C CG  1 
ATOM   1221 C  CD1 . LEU   B 1 16  ? 21.682 -17.047 9.625  1.00 15.75  ? 22  LEU   C CD1 1 
ATOM   1222 C  CD2 . LEU   B 1 16  ? 21.145 -15.004 8.302  1.00 15.14  ? 22  LEU   C CD2 1 
ATOM   1223 N  N   . ALA   B 1 17  ? 17.998 -13.152 12.523 1.00 15.61  ? 23  ALA   C N   1 
ATOM   1224 C  CA  . ALA   B 1 17  ? 16.721 -13.100 13.223 1.00 15.80  ? 23  ALA   C CA  1 
ATOM   1225 C  C   . ALA   B 1 17  ? 15.612 -12.547 12.320 1.00 16.36  ? 23  ALA   C C   1 
ATOM   1226 O  O   . ALA   B 1 17  ? 15.868 -11.618 11.520 1.00 17.48  ? 23  ALA   C O   1 
ATOM   1227 C  CB  . ALA   B 1 17  ? 16.840 -12.251 14.484 1.00 16.20  ? 23  ALA   C CB  1 
ATOM   1228 N  N   . THR   B 1 18  ? 14.397 -13.109 12.477 1.00 16.76  ? 24  THR   C N   1 
ATOM   1229 C  CA  . THR   B 1 18  ? 13.249 -12.705 11.668 1.00 16.72  ? 24  THR   C CA  1 
ATOM   1230 C  C   . THR   B 1 18  ? 12.436 -11.630 12.425 1.00 17.18  ? 24  THR   C C   1 
ATOM   1231 O  O   . THR   B 1 18  ? 12.672 -11.357 13.609 1.00 17.72  ? 24  THR   C O   1 
ATOM   1232 C  CB  . THR   B 1 18  ? 12.319 -13.948 11.450 1.00 17.79  ? 24  THR   C CB  1 
ATOM   1233 O  OG1 . THR   B 1 18  ? 11.801 -14.378 12.699 1.00 18.33  ? 24  THR   C OG1 1 
ATOM   1234 C  CG2 . THR   B 1 18  ? 13.022 -15.112 10.750 1.00 18.62  ? 24  THR   C CG2 1 
ATOM   1235 N  N   . HIS   B 1 19  ? 11.403 -11.039 11.744 1.00 17.36  ? 25  HIS   C N   1 
ATOM   1236 C  CA  . HIS   B 1 19  ? 10.496 -10.111 12.429 1.00 18.41  ? 25  HIS   C CA  1 
ATOM   1237 C  C   . HIS   B 1 19  ? 9.805  -10.858 13.595 1.00 17.96  ? 25  HIS   C C   1 
ATOM   1238 O  O   . HIS   B 1 19  ? 9.672  -10.272 14.664 1.00 19.50  ? 25  HIS   C O   1 
ATOM   1239 C  CB  . HIS   B 1 19  ? 9.392  -9.597  11.465 1.00 19.87  ? 25  HIS   C CB  1 
ATOM   1240 C  CG  . HIS   B 1 19  ? 8.258  -8.893  12.178 1.00 22.67  ? 25  HIS   C CG  1 
ATOM   1241 N  ND1 . HIS   B 1 19  ? 8.402  -7.614  12.690 1.00 25.67  ? 25  HIS   C ND1 1 
ATOM   1242 C  CD2 . HIS   B 1 19  ? 7.031  -9.361  12.518 1.00 24.90  ? 25  HIS   C CD2 1 
ATOM   1243 C  CE1 . HIS   B 1 19  ? 7.238  -7.313  13.248 1.00 26.10  ? 25  HIS   C CE1 1 
ATOM   1244 N  NE2 . HIS   B 1 19  ? 6.390  -8.347  13.207 1.00 25.71  ? 25  HIS   C NE2 1 
ATOM   1245 N  N   . ASN   B 1 20  ? 9.403  -12.127 13.405 1.00 17.69  ? 26  ASN   C N   1 
ATOM   1246 C  CA  . ASN   B 1 20  ? 8.741  -12.858 14.490 1.00 18.47  ? 26  ASN   C CA  1 
ATOM   1247 C  C   . ASN   B 1 20  ? 9.672  -13.019 15.675 1.00 17.67  ? 26  ASN   C C   1 
ATOM   1248 O  O   . ASN   B 1 20  ? 9.244  -12.902 16.820 1.00 17.18  ? 26  ASN   C O   1 
ATOM   1249 C  CB  . ASN   B 1 20  ? 8.207  -14.231 14.034 1.00 19.77  ? 26  ASN   C CB  1 
ATOM   1250 C  CG  . ASN   B 1 20  ? 7.410  -14.921 15.141 1.00 26.90  ? 26  ASN   C CG  1 
ATOM   1251 O  OD1 . ASN   B 1 20  ? 6.284  -14.516 15.466 1.00 30.45  ? 26  ASN   C OD1 1 
ATOM   1252 N  ND2 . ASN   B 1 20  ? 7.988  -15.940 15.786 1.00 28.09  ? 26  ASN   C ND2 1 
ATOM   1253 N  N   . ASP   B 1 21  ? 10.992 -13.232 15.410 1.00 16.38  ? 27  ASP   C N   1 
ATOM   1254 C  CA  . ASP   B 1 21  ? 11.936 -13.325 16.518 1.00 16.16  ? 27  ASP   C CA  1 
ATOM   1255 C  C   . ASP   B 1 21  ? 11.970 -11.999 17.308 1.00 16.48  ? 27  ASP   C C   1 
ATOM   1256 O  O   . ASP   B 1 21  ? 11.921 -12.020 18.534 1.00 17.21  ? 27  ASP   C O   1 
ATOM   1257 C  CB  . ASP   B 1 21  ? 13.359 -13.630 16.015 1.00 15.96  ? 27  ASP   C CB  1 
ATOM   1258 C  CG  . ASP   B 1 21  ? 13.548 -15.038 15.529 1.00 16.18  ? 27  ASP   C CG  1 
ATOM   1259 O  OD1 . ASP   B 1 21  ? 12.979 -15.963 16.159 1.00 16.93  ? 27  ASP   C OD1 1 
ATOM   1260 O  OD2 . ASP   B 1 21  ? 14.259 -15.223 14.496 1.00 16.78  ? 27  ASP   C OD2 1 
ATOM   1261 N  N   . TRP   B 1 22  ? 12.082 -10.844 16.604 1.00 16.26  ? 28  TRP   C N   1 
ATOM   1262 C  CA  . TRP   B 1 22  ? 12.126 -9.559  17.299 1.00 16.35  ? 28  TRP   C CA  1 
ATOM   1263 C  C   . TRP   B 1 22  ? 10.796 -9.256  18.021 1.00 15.68  ? 28  TRP   C C   1 
ATOM   1264 O  O   . TRP   B 1 22  ? 10.792 -8.619  19.091 1.00 16.03  ? 28  TRP   C O   1 
ATOM   1265 C  CB  . TRP   B 1 22  ? 12.495 -8.451  16.320 1.00 15.89  ? 28  TRP   C CB  1 
ATOM   1266 C  CG  . TRP   B 1 22  ? 13.974 -8.405  16.033 1.00 15.53  ? 28  TRP   C CG  1 
ATOM   1267 C  CD1 . TRP   B 1 22  ? 14.623 -8.903  14.933 1.00 15.88  ? 28  TRP   C CD1 1 
ATOM   1268 C  CD2 . TRP   B 1 22  ? 14.990 -7.829  16.869 1.00 15.06  ? 28  TRP   C CD2 1 
ATOM   1269 N  NE1 . TRP   B 1 22  ? 15.984 -8.639  15.022 1.00 16.72  ? 28  TRP   C NE1 1 
ATOM   1270 C  CE2 . TRP   B 1 22  ? 16.231 -7.995  16.205 1.00 16.28  ? 28  TRP   C CE2 1 
ATOM   1271 C  CE3 . TRP   B 1 22  ? 14.970 -7.145  18.092 1.00 17.36  ? 28  TRP   C CE3 1 
ATOM   1272 C  CZ2 . TRP   B 1 22  ? 17.423 -7.491  16.709 1.00 16.60  ? 28  TRP   C CZ2 1 
ATOM   1273 C  CZ3 . TRP   B 1 22  ? 16.170 -6.650  18.596 1.00 17.93  ? 28  TRP   C CZ3 1 
ATOM   1274 C  CH2 . TRP   B 1 22  ? 17.375 -6.827  17.899 1.00 17.08  ? 28  TRP   C CH2 1 
ATOM   1275 N  N   . ALA   B 1 23  ? 9.670  -9.699  17.439 1.00 15.63  ? 29  ALA   C N   1 
ATOM   1276 C  CA  . ALA   B 1 23  ? 8.346  -9.475  18.047 1.00 16.72  ? 29  ALA   C CA  1 
ATOM   1277 C  C   . ALA   B 1 23  ? 8.079  -10.349 19.287 1.00 18.70  ? 29  ALA   C C   1 
ATOM   1278 O  O   . ALA   B 1 23  ? 7.103  -10.109 20.018 1.00 19.73  ? 29  ALA   C O   1 
ATOM   1279 C  CB  . ALA   B 1 23  ? 7.248  -9.724  17.021 1.00 17.09  ? 29  ALA   C CB  1 
ATOM   1280 N  N   . ASN   B 1 24  ? 8.931  -11.382 19.507 1.00 17.91  ? 30  ASN   C N   1 
ATOM   1281 C  CA  . ASN   B 1 24  ? 8.832  -12.294 20.649 1.00 17.23  ? 30  ASN   C CA  1 
ATOM   1282 C  C   . ASN   B 1 24  ? 10.225 -12.365 21.331 1.00 17.54  ? 30  ASN   C C   1 
ATOM   1283 O  O   . ASN   B 1 24  ? 10.654 -13.431 21.773 1.00 17.17  ? 30  ASN   C O   1 
ATOM   1284 C  CB  . ASN   B 1 24  ? 8.374  -13.679 20.130 1.00 19.33  ? 30  ASN   C CB  1 
ATOM   1285 C  CG  . ASN   B 1 24  ? 6.966  -13.627 19.646 1.00 20.02  ? 30  ASN   C CG  1 
ATOM   1286 O  OD1 . ASN   B 1 24  ? 6.029  -13.649 20.465 1.00 22.29  ? 30  ASN   C OD1 1 
ATOM   1287 N  ND2 . ASN   B 1 24  ? 6.789  -13.506 18.350 1.00 20.14  ? 30  ASN   C ND2 1 
ATOM   1288 N  N   . LEU   B 1 25  ? 10.931 -11.232 21.414 1.00 17.33  ? 31  LEU   C N   1 
ATOM   1289 C  CA  . LEU   B 1 25  ? 12.296 -11.201 21.923 1.00 16.65  ? 31  LEU   C CA  1 
ATOM   1290 C  C   . LEU   B 1 25  ? 12.427 -11.516 23.407 1.00 17.92  ? 31  LEU   C C   1 
ATOM   1291 O  O   . LEU   B 1 25  ? 11.644 -11.011 24.226 1.00 18.74  ? 31  LEU   C O   1 
ATOM   1292 C  CB  . LEU   B 1 25  ? 12.880 -9.803  21.654 1.00 17.22  ? 31  LEU   C CB  1 
ATOM   1293 C  CG  . LEU   B 1 25  ? 14.328 -9.630  22.023 1.00 17.92  ? 31  LEU   C CG  1 
ATOM   1294 C  CD1 . LEU   B 1 25  ? 15.209 -10.495 21.125 1.00 17.58  ? 31  LEU   C CD1 1 
ATOM   1295 C  CD2 . LEU   B 1 25  ? 14.750 -8.163  21.923 1.00 19.60  ? 31  LEU   C CD2 1 
ATOM   1296 N  N   . VAL   B 1 26  ? 13.432 -12.340 23.746 1.00 16.97  ? 32  VAL   C N   1 
ATOM   1297 C  CA  . VAL   B 1 26  ? 13.783 -12.631 25.138 1.00 17.08  ? 32  VAL   C CA  1 
ATOM   1298 C  C   . VAL   B 1 26  ? 15.105 -11.920 25.478 1.00 18.26  ? 32  VAL   C C   1 
ATOM   1299 O  O   . VAL   B 1 26  ? 15.209 -11.242 26.505 1.00 19.67  ? 32  VAL   C O   1 
ATOM   1300 C  CB  . VAL   B 1 26  ? 13.910 -14.150 25.368 1.00 17.65  ? 32  VAL   C CB  1 
ATOM   1301 C  CG1 . VAL   B 1 26  ? 14.459 -14.447 26.765 1.00 19.44  ? 32  VAL   C CG1 1 
ATOM   1302 C  CG2 . VAL   B 1 26  ? 12.562 -14.840 25.182 1.00 18.36  ? 32  VAL   C CG2 1 
ATOM   1303 N  N   . TRP   B 1 27  ? 16.114 -12.042 24.592 1.00 17.11  ? 33  TRP   C N   1 
ATOM   1304 C  CA  . TRP   B 1 27  ? 17.432 -11.471 24.850 1.00 16.69  ? 33  TRP   C CA  1 
ATOM   1305 C  C   . TRP   B 1 27  ? 18.230 -11.420 23.533 1.00 17.24  ? 33  TRP   C C   1 
ATOM   1306 O  O   . TRP   B 1 27  ? 18.039 -12.287 22.670 1.00 16.66  ? 33  TRP   C O   1 
ATOM   1307 C  CB  . TRP   B 1 27  ? 18.176 -12.366 25.871 1.00 18.06  ? 33  TRP   C CB  1 
ATOM   1308 C  CG  . TRP   B 1 27  ? 19.647 -12.092 26.069 1.00 18.97  ? 33  TRP   C CG  1 
ATOM   1309 C  CD1 . TRP   B 1 27  ? 20.206 -11.138 26.873 1.00 20.82  ? 33  TRP   C CD1 1 
ATOM   1310 C  CD2 . TRP   B 1 27  ? 20.744 -12.801 25.466 1.00 18.47  ? 33  TRP   C CD2 1 
ATOM   1311 N  NE1 . TRP   B 1 27  ? 21.586 -11.220 26.825 1.00 21.51  ? 33  TRP   C NE1 1 
ATOM   1312 C  CE2 . TRP   B 1 27  ? 21.939 -12.233 25.965 1.00 19.68  ? 33  TRP   C CE2 1 
ATOM   1313 C  CE3 . TRP   B 1 27  ? 20.832 -13.842 24.526 1.00 18.10  ? 33  TRP   C CE3 1 
ATOM   1314 C  CZ2 . TRP   B 1 27  ? 23.199 -12.686 25.576 1.00 19.50  ? 33  TRP   C CZ2 1 
ATOM   1315 C  CZ3 . TRP   B 1 27  ? 22.083 -14.297 24.162 1.00 19.13  ? 33  TRP   C CZ3 1 
ATOM   1316 C  CH2 . TRP   B 1 27  ? 23.242 -13.711 24.672 1.00 19.36  ? 33  TRP   C CH2 1 
ATOM   1317 N  N   . GLU   B 1 28  ? 19.072 -10.394 23.374 1.00 16.10  ? 34  GLU   C N   1 
ATOM   1318 C  CA  . GLU   B 1 28  ? 19.926 -10.316 22.197 1.00 16.37  ? 34  GLU   C CA  1 
ATOM   1319 C  C   . GLU   B 1 28  ? 21.221 -9.639  22.565 1.00 16.33  ? 34  GLU   C C   1 
ATOM   1320 O  O   . GLU   B 1 28  ? 21.248 -8.746  23.449 1.00 16.27  ? 34  GLU   C O   1 
ATOM   1321 C  CB  . GLU   B 1 28  ? 19.241 -9.599  21.026 1.00 16.65  ? 34  GLU   C CB  1 
ATOM   1322 C  CG  . GLU   B 1 28  ? 18.685 -8.218  21.325 1.00 17.63  ? 34  GLU   C CG  1 
ATOM   1323 C  CD  . GLU   B 1 28  ? 19.665 -7.064  21.258 1.00 21.21  ? 34  GLU   C CD  1 
ATOM   1324 O  OE1 . GLU   B 1 28  ? 19.435 -6.029  21.925 1.00 22.53  ? 34  GLU   C OE1 1 
ATOM   1325 O  OE2 . GLU   B 1 28  ? 20.651 -7.173  20.497 1.00 18.54  ? 34  GLU   C OE2 1 
ATOM   1326 N  N   . ASP   B 1 29  ? 22.299 -10.000 21.869 1.00 14.92  ? 35  ASP   C N   1 
ATOM   1327 C  CA  . ASP   B 1 29  ? 23.592 -9.379  22.121 1.00 15.49  ? 35  ASP   C CA  1 
ATOM   1328 C  C   . ASP   B 1 29  ? 24.373 -9.341  20.794 1.00 15.38  ? 35  ASP   C C   1 
ATOM   1329 O  O   . ASP   B 1 29  ? 24.772 -10.393 20.294 1.00 15.76  ? 35  ASP   C O   1 
ATOM   1330 C  CB  . ASP   B 1 29  ? 24.320 -10.185 23.191 1.00 17.15  ? 35  ASP   C CB  1 
ATOM   1331 C  CG  . ASP   B 1 29  ? 25.646 -9.600  23.589 1.00 21.79  ? 35  ASP   C CG  1 
ATOM   1332 O  OD1 . ASP   B 1 29  ? 26.359 -9.098  22.703 1.00 22.91  ? 35  ASP   C OD1 1 
ATOM   1333 O  OD2 . ASP   B 1 29  ? 26.003 -9.706  24.778 1.00 24.07  ? 35  ASP   C OD2 1 
ATOM   1334 N  N   . SER   B 1 30  ? 24.524 -8.139  20.198 1.00 15.42  ? 36  SER   C N   1 
ATOM   1335 C  CA  A SER   B 1 30  ? 25.231 -7.973  18.923 0.50 15.40  ? 36  SER   C CA  1 
ATOM   1336 C  CA  B SER   B 1 30  ? 25.198 -8.032  18.921 0.50 15.85  ? 36  SER   C CA  1 
ATOM   1337 C  C   . SER   B 1 30  ? 26.681 -8.422  19.013 1.00 15.77  ? 36  SER   C C   1 
ATOM   1338 O  O   . SER   B 1 30  ? 27.201 -9.024  18.055 1.00 15.44  ? 36  SER   C O   1 
ATOM   1339 C  CB  A SER   B 1 30  ? 25.192 -6.516  18.453 0.50 16.02  ? 36  SER   C CB  1 
ATOM   1340 C  CB  B SER   B 1 30  ? 25.014 -6.632  18.345 0.50 17.91  ? 36  SER   C CB  1 
ATOM   1341 O  OG  A SER   B 1 30  ? 26.128 -6.273  17.404 0.50 15.26  ? 36  SER   C OG  1 
ATOM   1342 O  OG  B SER   B 1 30  ? 25.548 -5.666  19.229 0.50 20.15  ? 36  SER   C OG  1 
ATOM   1343 N  N   . SER   B 1 31  ? 27.347 -8.132  20.154 1.00 16.35  ? 37  SER   C N   1 
ATOM   1344 C  CA  . SER   B 1 31  ? 28.755 -8.521  20.277 1.00 16.91  ? 37  SER   C CA  1 
ATOM   1345 C  C   . SER   B 1 31  ? 28.943 -10.034 20.222 1.00 15.94  ? 37  SER   C C   1 
ATOM   1346 O  O   . SER   B 1 31  ? 30.051 -10.477 19.891 1.00 17.30  ? 37  SER   C O   1 
ATOM   1347 C  CB  . SER   B 1 31  ? 29.381 -7.974  21.556 1.00 21.20  ? 37  SER   C CB  1 
ATOM   1348 O  OG  . SER   B 1 31  ? 28.936 -8.673  22.703 1.00 26.09  ? 37  SER   C OG  1 
ATOM   1349 N  N   . ARG   B 1 32  ? 27.884 -10.825 20.540 1.00 14.58  ? 38  ARG   C N   1 
ATOM   1350 C  CA  . ARG   B 1 32  ? 27.971 -12.292 20.498 1.00 14.15  ? 38  ARG   C CA  1 
ATOM   1351 C  C   . ARG   B 1 32  ? 27.319 -12.889 19.220 1.00 14.05  ? 38  ARG   C C   1 
ATOM   1352 O  O   . ARG   B 1 32  ? 27.374 -14.111 19.021 1.00 13.75  ? 38  ARG   C O   1 
ATOM   1353 C  CB  . ARG   B 1 32  ? 27.222 -12.893 21.717 1.00 15.60  ? 38  ARG   C CB  1 
ATOM   1354 C  CG  . ARG   B 1 32  ? 27.885 -12.547 23.037 1.00 17.36  ? 38  ARG   C CG  1 
ATOM   1355 C  CD  . ARG   B 1 32  ? 27.129 -13.127 24.230 1.00 15.38  ? 38  ARG   C CD  1 
ATOM   1356 N  NE  . ARG   B 1 32  ? 27.220 -14.600 24.257 1.00 14.66  ? 38  ARG   C NE  1 
ATOM   1357 C  CZ  . ARG   B 1 32  ? 27.190 -15.337 25.367 1.00 17.41  ? 38  ARG   C CZ  1 
ATOM   1358 N  NH1 . ARG   B 1 32  ? 27.088 -14.757 26.557 1.00 17.74  ? 38  ARG   C NH1 1 
ATOM   1359 N  NH2 . ARG   B 1 32  ? 27.341 -16.661 25.299 1.00 15.43  ? 38  ARG   C NH2 1 
ATOM   1360 N  N   . ASP   B 1 33  ? 26.652 -12.048 18.403 1.00 13.25  ? 39  ASP   C N   1 
ATOM   1361 C  CA  . ASP   B 1 33  ? 25.877 -12.500 17.257 1.00 12.98  ? 39  ASP   C CA  1 
ATOM   1362 C  C   . ASP   B 1 33  ? 24.784 -13.472 17.694 1.00 13.23  ? 39  ASP   C C   1 
ATOM   1363 O  O   . ASP   B 1 33  ? 24.489 -14.416 16.954 1.00 13.21  ? 39  ASP   C O   1 
ATOM   1364 C  CB  . ASP   B 1 33  ? 26.742 -13.109 16.154 1.00 12.57  ? 39  ASP   C CB  1 
ATOM   1365 C  CG  . ASP   B 1 33  ? 25.946 -13.445 14.887 1.00 14.95  ? 39  ASP   C CG  1 
ATOM   1366 O  OD1 . ASP   B 1 33  ? 25.049 -12.658 14.516 1.00 15.61  ? 39  ASP   C OD1 1 
ATOM   1367 O  OD2 . ASP   B 1 33  ? 26.244 -14.462 14.247 1.00 13.05  ? 39  ASP   C OD2 1 
ATOM   1368 N  N   . LEU   B 1 34  ? 24.136 -13.221 18.864 1.00 12.78  ? 40  LEU   C N   1 
ATOM   1369 C  CA  . LEU   B 1 34  ? 23.069 -14.114 19.347 1.00 13.05  ? 40  LEU   C CA  1 
ATOM   1370 C  C   . LEU   B 1 34  ? 21.755 -13.378 19.589 1.00 13.41  ? 40  LEU   C C   1 
ATOM   1371 O  O   . LEU   B 1 34  ? 21.766 -12.224 20.049 1.00 13.52  ? 40  LEU   C O   1 
ATOM   1372 C  CB  . LEU   B 1 34  ? 23.455 -14.819 20.644 1.00 13.51  ? 40  LEU   C CB  1 
ATOM   1373 C  CG  . LEU   B 1 34  ? 24.515 -15.927 20.536 1.00 14.80  ? 40  LEU   C CG  1 
ATOM   1374 C  CD1 . LEU   B 1 34  ? 24.760 -16.560 21.928 1.00 14.88  ? 40  LEU   C CD1 1 
ATOM   1375 C  CD2 . LEU   B 1 34  ? 24.088 -17.032 19.566 1.00 14.66  ? 40  LEU   C CD2 1 
ATOM   1376 N  N   . LEU   B 1 35  ? 20.641 -14.084 19.351 1.00 12.88  ? 41  LEU   C N   1 
ATOM   1377 C  CA  . LEU   B 1 35  ? 19.309 -13.576 19.671 1.00 13.20  ? 41  LEU   C CA  1 
ATOM   1378 C  C   . LEU   B 1 35  ? 18.473 -14.787 20.096 1.00 13.94  ? 41  LEU   C C   1 
ATOM   1379 O  O   . LEU   B 1 35  ? 18.598 -15.867 19.499 1.00 14.97  ? 41  LEU   C O   1 
ATOM   1380 C  CB  . LEU   B 1 35  ? 18.665 -12.844 18.454 1.00 12.86  ? 41  LEU   C CB  1 
ATOM   1381 C  CG  . LEU   B 1 35  ? 17.274 -12.253 18.737 1.00 13.54  ? 41  LEU   C CG  1 
ATOM   1382 C  CD1 . LEU   B 1 35  ? 17.074 -10.942 17.980 1.00 15.17  ? 41  LEU   C CD1 1 
ATOM   1383 C  CD2 . LEU   B 1 35  ? 16.165 -13.272 18.357 1.00 14.10  ? 41  LEU   C CD2 1 
ATOM   1384 N  N   . VAL   B 1 36  ? 17.691 -14.611 21.156 1.00 13.57  ? 42  VAL   C N   1 
ATOM   1385 C  CA  . VAL   B 1 36  ? 16.789 -15.627 21.698 1.00 13.42  ? 42  VAL   C CA  1 
ATOM   1386 C  C   . VAL   B 1 36  ? 15.383 -15.095 21.681 1.00 14.19  ? 42  VAL   C C   1 
ATOM   1387 O  O   . VAL   B 1 36  ? 15.152 -13.981 22.168 1.00 15.87  ? 42  VAL   C O   1 
ATOM   1388 C  CB  . VAL   B 1 36  ? 17.194 -16.078 23.119 1.00 14.72  ? 42  VAL   C CB  1 
ATOM   1389 C  CG1 . VAL   B 1 36  ? 16.228 -17.153 23.626 1.00 15.73  ? 42  VAL   C CG1 1 
ATOM   1390 C  CG2 . VAL   B 1 36  ? 18.640 -16.615 23.101 1.00 15.39  ? 42  VAL   C CG2 1 
ATOM   1391 N  N   . SER   B 1 37  ? 14.448 -15.865 21.108 1.00 13.53  ? 43  SER   C N   1 
ATOM   1392 C  CA  . SER   B 1 37  ? 13.032 -15.487 21.074 1.00 14.50  ? 43  SER   C CA  1 
ATOM   1393 C  C   . SER   B 1 37  ? 12.226 -16.579 21.761 1.00 16.09  ? 43  SER   C C   1 
ATOM   1394 O  O   . SER   B 1 37  ? 12.721 -17.686 21.990 1.00 15.95  ? 43  SER   C O   1 
ATOM   1395 C  CB  . SER   B 1 37  ? 12.540 -15.290 19.645 1.00 15.29  ? 43  SER   C CB  1 
ATOM   1396 O  OG  . SER   B 1 37  ? 12.705 -16.456 18.851 1.00 16.64  ? 43  SER   C OG  1 
ATOM   1397 N  N   . SER   B 1 38  ? 10.976 -16.266 22.146 1.00 16.10  ? 44  SER   C N   1 
ATOM   1398 C  CA  . SER   B 1 38  ? 10.115 -17.251 22.814 1.00 17.61  ? 44  SER   C CA  1 
ATOM   1399 C  C   . SER   B 1 38  ? 9.299  -18.049 21.780 1.00 19.96  ? 44  SER   C C   1 
ATOM   1400 O  O   . SER   B 1 38  ? 9.004  -17.549 20.701 1.00 20.69  ? 44  SER   C O   1 
ATOM   1401 C  CB  . SER   B 1 38  ? 9.193  -16.540 23.805 1.00 19.64  ? 44  SER   C CB  1 
ATOM   1402 O  OG  . SER   B 1 38  ? 8.369  -15.630 23.096 1.00 23.36  ? 44  SER   C OG  1 
ATOM   1403 N  N   . THR   B 1 39  ? 8.964  -19.302 22.097 1.00 19.96  ? 45  THR   C N   1 
ATOM   1404 C  CA  . THR   B 1 39  ? 8.213  -20.185 21.212 1.00 20.64  ? 45  THR   C CA  1 
ATOM   1405 C  C   . THR   B 1 39  ? 6.916  -20.646 21.912 1.00 23.20  ? 45  THR   C C   1 
ATOM   1406 O  O   . THR   B 1 39  ? 6.854  -20.712 23.140 1.00 22.82  ? 45  THR   C O   1 
ATOM   1407 C  CB  . THR   B 1 39  ? 9.054  -21.440 20.848 1.00 21.01  ? 45  THR   C CB  1 
ATOM   1408 O  OG1 . THR   B 1 39  ? 9.319  -22.185 22.024 1.00 22.04  ? 45  THR   C OG1 1 
ATOM   1409 C  CG2 . THR   B 1 39  ? 10.396 -21.099 20.171 1.00 20.60  ? 45  THR   C CG2 1 
ATOM   1410 N  N   . THR   B 1 40  ? 5.914  -20.999 21.119 1.00 25.07  ? 46  THR   C N   1 
ATOM   1411 C  CA  . THR   B 1 40  ? 4.666  -21.542 21.664 1.00 27.15  ? 46  THR   C CA  1 
ATOM   1412 C  C   . THR   B 1 40  ? 4.877  -23.025 22.009 1.00 27.31  ? 46  THR   C C   1 
ATOM   1413 O  O   . THR   B 1 40  ? 4.455  -23.482 23.073 1.00 28.55  ? 46  THR   C O   1 
ATOM   1414 C  CB  . THR   B 1 40  ? 3.513  -21.320 20.677 1.00 31.36  ? 46  THR   C CB  1 
ATOM   1415 O  OG1 . THR   B 1 40  ? 3.851  -21.966 19.447 1.00 35.39  ? 46  THR   C OG1 1 
ATOM   1416 C  CG2 . THR   B 1 40  ? 3.289  -19.850 20.390 1.00 31.28  ? 46  THR   C CG2 1 
ATOM   1417 N  N   . ALA   B 1 41  ? 5.563  -23.774 21.122 1.00 26.04  ? 47  ALA   C N   1 
ATOM   1418 C  CA  . ALA   B 1 41  ? 5.821  -25.189 21.368 1.00 26.05  ? 47  ALA   C CA  1 
ATOM   1419 C  C   . ALA   B 1 41  ? 7.150  -25.426 22.096 1.00 24.82  ? 47  ALA   C C   1 
ATOM   1420 O  O   . ALA   B 1 41  ? 8.081  -24.659 21.908 1.00 24.41  ? 47  ALA   C O   1 
ATOM   1421 C  CB  . ALA   B 1 41  ? 5.837  -25.946 20.050 1.00 27.14  ? 47  ALA   C CB  1 
ATOM   1422 N  N   . GLN   B 1 42  ? 7.253  -26.496 22.889 1.00 24.55  ? 48  GLN   C N   1 
ATOM   1423 C  CA  . GLN   B 1 42  ? 8.500  -26.822 23.577 1.00 24.68  ? 48  GLN   C CA  1 
ATOM   1424 C  C   . GLN   B 1 42  ? 9.465  -27.500 22.620 1.00 23.63  ? 48  GLN   C C   1 
ATOM   1425 O  O   . GLN   B 1 42  ? 9.058  -28.347 21.824 1.00 24.85  ? 48  GLN   C O   1 
ATOM   1426 C  CB  . GLN   B 1 42  ? 8.245  -27.724 24.795 1.00 28.73  ? 48  GLN   C CB  1 
ATOM   1427 C  CG  . GLN   B 1 42  ? 7.648  -26.960 25.972 1.00 37.96  ? 48  GLN   C CG  1 
ATOM   1428 C  CD  . GLN   B 1 42  ? 7.483  -27.896 27.135 1.00 48.89  ? 48  GLN   C CD  1 
ATOM   1429 O  OE1 . GLN   B 1 42  ? 6.537  -28.697 27.192 1.00 51.90  ? 48  GLN   C OE1 1 
ATOM   1430 N  NE2 . GLN   B 1 42  ? 8.411  -27.833 28.082 1.00 51.59  ? 48  GLN   C NE2 1 
ATOM   1431 N  N   . GLY   B 1 43  ? 10.741 -27.135 22.732 1.00 21.58  ? 49  GLY   C N   1 
ATOM   1432 C  CA  . GLY   B 1 43  ? 11.820 -27.704 21.934 1.00 20.82  ? 49  GLY   C CA  1 
ATOM   1433 C  C   . GLY   B 1 43  ? 12.486 -28.854 22.662 1.00 20.70  ? 49  GLY   C C   1 
ATOM   1434 O  O   . GLY   B 1 43  ? 12.262 -29.045 23.864 1.00 21.90  ? 49  GLY   C O   1 
ATOM   1435 N  N   . CYS   B 1 44  ? 13.279 -29.624 21.946 1.00 19.33  ? 50  CYS   C N   1 
ATOM   1436 C  CA  . CYS   B 1 44  ? 13.871 -30.836 22.523 1.00 20.03  ? 50  CYS   C CA  1 
ATOM   1437 C  C   . CYS   B 1 44  ? 15.378 -30.862 22.581 1.00 20.15  ? 50  CYS   C C   1 
ATOM   1438 O  O   . CYS   B 1 44  ? 15.943 -31.911 22.939 1.00 21.91  ? 50  CYS   C O   1 
ATOM   1439 C  CB  . CYS   B 1 44  ? 13.340 -32.034 21.756 1.00 20.87  ? 50  CYS   C CB  1 
ATOM   1440 S  SG  . CYS   B 1 44  ? 11.534 -32.182 21.879 1.00 28.81  ? 50  CYS   C SG  1 
ATOM   1441 N  N   . ASP   B 1 45  ? 16.051 -29.778 22.186 1.00 17.04  ? 51  ASP   C N   1 
ATOM   1442 C  CA  . ASP   B 1 45  ? 17.508 -29.760 22.230 1.00 16.89  ? 51  ASP   C CA  1 
ATOM   1443 C  C   . ASP   B 1 45  ? 17.929 -29.556 23.704 1.00 17.75  ? 51  ASP   C C   1 
ATOM   1444 O  O   . ASP   B 1 45  ? 17.213 -28.905 24.498 1.00 19.17  ? 51  ASP   C O   1 
ATOM   1445 C  CB  . ASP   B 1 45  ? 18.074 -28.599 21.381 1.00 17.42  ? 51  ASP   C CB  1 
ATOM   1446 C  CG  . ASP   B 1 45  ? 17.891 -28.790 19.890 1.00 21.82  ? 51  ASP   C CG  1 
ATOM   1447 O  OD1 . ASP   B 1 45  ? 17.894 -29.950 19.435 1.00 21.16  ? 51  ASP   C OD1 1 
ATOM   1448 O  OD2 . ASP   B 1 45  ? 17.739 -27.763 19.166 1.00 18.50  ? 51  ASP   C OD2 1 
ATOM   1449 N  N   . THR   B 1 46  ? 19.064 -30.154 24.073 1.00 16.36  ? 52  THR   C N   1 
ATOM   1450 C  CA  . THR   B 1 46  ? 19.657 -29.989 25.396 1.00 16.16  ? 52  THR   C CA  1 
ATOM   1451 C  C   . THR   B 1 46  ? 20.919 -29.149 25.217 1.00 16.05  ? 52  THR   C C   1 
ATOM   1452 O  O   . THR   B 1 46  ? 21.737 -29.464 24.335 1.00 16.51  ? 52  THR   C O   1 
ATOM   1453 C  CB  . THR   B 1 46  ? 20.091 -31.370 25.926 1.00 18.37  ? 52  THR   C CB  1 
ATOM   1454 O  OG1 . THR   B 1 46  ? 18.913 -32.172 26.123 1.00 20.81  ? 52  THR   C OG1 1 
ATOM   1455 C  CG2 . THR   B 1 46  ? 20.923 -31.277 27.207 1.00 19.78  ? 52  THR   C CG2 1 
ATOM   1456 N  N   . ILE   B 1 47  ? 21.104 -28.124 26.060 1.00 15.33  ? 53  ILE   C N   1 
ATOM   1457 C  CA  . ILE   B 1 47  ? 22.319 -27.338 26.011 1.00 14.33  ? 53  ILE   C CA  1 
ATOM   1458 C  C   . ILE   B 1 47  ? 23.405 -28.021 26.856 1.00 13.75  ? 53  ILE   C C   1 
ATOM   1459 O  O   . ILE   B 1 47  ? 23.148 -28.468 27.986 1.00 15.04  ? 53  ILE   C O   1 
ATOM   1460 C  CB  . ILE   B 1 47  ? 22.062 -25.948 26.605 1.00 15.43  ? 53  ILE   C CB  1 
ATOM   1461 C  CG1 . ILE   B 1 47  ? 20.844 -25.269 25.954 1.00 16.10  ? 53  ILE   C CG1 1 
ATOM   1462 C  CG2 . ILE   B 1 47  ? 23.328 -25.088 26.494 1.00 16.18  ? 53  ILE   C CG2 1 
ATOM   1463 C  CD1 . ILE   B 1 47  ? 21.079 -25.090 24.397 1.00 17.44  ? 53  ILE   C CD1 1 
ATOM   1464 N  N   . ALA   B 1 48  ? 24.627 -28.076 26.305 1.00 13.01  ? 54  ALA   C N   1 
ATOM   1465 C  CA  . ALA   B 1 48  ? 25.753 -28.637 27.060 1.00 12.49  ? 54  ALA   C CA  1 
ATOM   1466 C  C   . ALA   B 1 48  ? 26.102 -27.717 28.229 1.00 13.17  ? 54  ALA   C C   1 
ATOM   1467 O  O   . ALA   B 1 48  ? 26.089 -26.488 28.057 1.00 13.94  ? 54  ALA   C O   1 
ATOM   1468 C  CB  . ALA   B 1 48  ? 26.977 -28.750 26.162 1.00 12.96  ? 54  ALA   C CB  1 
ATOM   1469 N  N   . ARG   B 1 49  ? 26.438 -28.317 29.396 1.00 13.54  ? 55  ARG   C N   1 
ATOM   1470 C  CA  . ARG   B 1 49  ? 26.898 -27.552 30.548 1.00 13.55  ? 55  ARG   C CA  1 
ATOM   1471 C  C   . ARG   B 1 49  ? 28.228 -28.212 30.923 1.00 14.17  ? 55  ARG   C C   1 
ATOM   1472 O  O   . ARG   B 1 49  ? 28.268 -29.244 31.612 1.00 16.08  ? 55  ARG   C O   1 
ATOM   1473 C  CB  . ARG   B 1 49  ? 25.882 -27.604 31.689 1.00 13.88  ? 55  ARG   C CB  1 
ATOM   1474 C  CG  . ARG   B 1 49  ? 24.535 -27.024 31.279 1.00 13.21  ? 55  ARG   C CG  1 
ATOM   1475 C  CD  . ARG   B 1 49  ? 24.543 -25.532 30.899 1.00 15.52  ? 55  ARG   C CD  1 
ATOM   1476 N  NE  . ARG   B 1 49  ? 23.190 -25.097 30.532 1.00 16.40  ? 55  ARG   C NE  1 
ATOM   1477 C  CZ  . ARG   B 1 49  ? 22.926 -23.995 29.825 1.00 17.10  ? 55  ARG   C CZ  1 
ATOM   1478 N  NH1 . ARG   B 1 49  ? 23.905 -23.181 29.455 1.00 15.77  ? 55  ARG   C NH1 1 
ATOM   1479 N  NH2 . ARG   B 1 49  ? 21.670 -23.694 29.489 1.00 17.15  ? 55  ARG   C NH2 1 
ATOM   1480 N  N   . CYS   B 1 50  ? 29.323 -27.645 30.388 1.00 14.27  ? 56  CYS   C N   1 
ATOM   1481 C  CA  . CYS   B 1 50  ? 30.649 -28.281 30.438 1.00 14.47  ? 56  CYS   C CA  1 
ATOM   1482 C  C   . CYS   B 1 50  ? 31.735 -27.327 29.929 1.00 15.36  ? 56  CYS   C C   1 
ATOM   1483 O  O   . CYS   B 1 50  ? 31.435 -26.214 29.469 1.00 15.42  ? 56  CYS   C O   1 
ATOM   1484 C  CB  . CYS   B 1 50  ? 30.593 -29.502 29.516 1.00 14.94  ? 56  CYS   C CB  1 
ATOM   1485 S  SG  . CYS   B 1 50  ? 30.463 -29.048 27.753 1.00 15.07  ? 56  CYS   C SG  1 
ATOM   1486 N  N   . ASP   B 1 51  ? 33.030 -27.805 29.969 1.00 15.32  ? 57  ASP   C N   1 
ATOM   1487 C  CA  . ASP   B 1 51  ? 34.132 -27.059 29.377 1.00 16.58  ? 57  ASP   C CA  1 
ATOM   1488 C  C   . ASP   B 1 51  ? 34.806 -27.907 28.275 1.00 16.76  ? 57  ASP   C C   1 
ATOM   1489 O  O   . ASP   B 1 51  ? 35.996 -27.772 28.016 1.00 17.93  ? 57  ASP   C O   1 
ATOM   1490 C  CB  . ASP   B 1 51  ? 35.150 -26.616 30.426 1.00 18.92  ? 57  ASP   C CB  1 
ATOM   1491 C  CG  . ASP   B 1 51  ? 35.843 -27.750 31.136 1.00 24.81  ? 57  ASP   C CG  1 
ATOM   1492 O  OD1 . ASP   B 1 51  ? 35.470 -28.924 30.897 1.00 24.34  ? 57  ASP   C OD1 1 
ATOM   1493 O  OD2 . ASP   B 1 51  ? 36.794 -27.464 31.924 1.00 29.82  ? 57  ASP   C OD2 1 
ATOM   1494 N  N   . CYS   B 1 52  ? 34.033 -28.752 27.567 1.00 15.42  ? 58  CYS   C N   1 
ATOM   1495 C  CA  . CYS   B 1 52  ? 34.588 -29.543 26.434 1.00 13.36  ? 58  CYS   C CA  1 
ATOM   1496 C  C   . CYS   B 1 52  ? 35.250 -28.626 25.423 1.00 13.86  ? 58  CYS   C C   1 
ATOM   1497 O  O   . CYS   B 1 52  ? 34.781 -27.494 25.186 1.00 15.18  ? 58  CYS   C O   1 
ATOM   1498 C  CB  . CYS   B 1 52  ? 33.496 -30.357 25.731 1.00 13.80  ? 58  CYS   C CB  1 
ATOM   1499 S  SG  . CYS   B 1 52  ? 32.902 -31.794 26.649 1.00 15.51  ? 58  CYS   C SG  1 
ATOM   1500 N  N   . GLN   B 1 53  ? 36.308 -29.135 24.813 1.00 13.69  ? 59  GLN   C N   1 
ATOM   1501 C  CA  . GLN   B 1 53  ? 36.974 -28.475 23.692 1.00 14.02  ? 59  GLN   C CA  1 
ATOM   1502 C  C   . GLN   B 1 53  ? 37.032 -29.410 22.480 1.00 13.24  ? 59  GLN   C C   1 
ATOM   1503 O  O   . GLN   B 1 53  ? 37.814 -29.166 21.548 1.00 13.80  ? 59  GLN   C O   1 
ATOM   1504 C  CB  . GLN   B 1 53  ? 38.393 -27.989 24.042 1.00 15.49  ? 59  GLN   C CB  1 
ATOM   1505 C  CG  . GLN   B 1 53  ? 38.384 -26.738 24.937 1.00 19.72  ? 59  GLN   C CG  1 
ATOM   1506 C  CD  . GLN   B 1 53  ? 39.766 -26.180 25.112 1.00 23.69  ? 59  GLN   C CD  1 
ATOM   1507 O  OE1 . GLN   B 1 53  ? 40.322 -26.257 26.215 1.00 26.45  ? 59  GLN   C OE1 1 
ATOM   1508 N  NE2 . GLN   B 1 53  ? 40.360 -25.650 24.027 1.00 20.48  ? 59  GLN   C NE2 1 
ATOM   1509 N  N   . THR   B 1 54  ? 36.248 -30.517 22.459 1.00 12.93  ? 60  THR   C N   1 
ATOM   1510 C  CA  . THR   B 1 54  ? 36.149 -31.361 21.274 1.00 13.83  ? 60  THR   C CA  1 
ATOM   1511 C  C   . THR   B 1 54  ? 34.664 -31.656 21.053 1.00 13.56  ? 60  THR   C C   1 
ATOM   1512 O  O   . THR   B 1 54  ? 33.884 -31.741 22.003 1.00 14.04  ? 60  THR   C O   1 
ATOM   1513 C  CB  . THR   B 1 54  ? 36.912 -32.661 21.340 1.00 17.02  ? 60  THR   C CB  1 
ATOM   1514 O  OG1 . THR   B 1 54  ? 36.363 -33.456 22.361 1.00 20.03  ? 60  THR   C OG1 1 
ATOM   1515 C  CG2 . THR   B 1 54  ? 38.394 -32.442 21.581 1.00 17.42  ? 60  THR   C CG2 1 
ATOM   1516 N  N   . GLY   B 1 55  ? 34.273 -31.703 19.785 1.00 12.66  ? 61  GLY   C N   1 
ATOM   1517 C  CA  . GLY   B 1 55  ? 32.876 -31.957 19.450 1.00 12.33  ? 61  GLY   C CA  1 
ATOM   1518 C  C   . GLY   B 1 55  ? 32.741 -32.169 17.954 1.00 12.13  ? 61  GLY   C C   1 
ATOM   1519 O  O   . GLY   B 1 55  ? 33.729 -32.462 17.269 1.00 12.92  ? 61  GLY   C O   1 
ATOM   1520 N  N   . VAL   B 1 56  ? 31.508 -32.072 17.451 1.00 11.32  ? 62  VAL   C N   1 
ATOM   1521 C  CA  . VAL   B 1 56  ? 31.216 -32.265 16.027 1.00 11.03  ? 62  VAL   C CA  1 
ATOM   1522 C  C   . VAL   B 1 56  ? 30.309 -31.128 15.575 1.00 10.97  ? 62  VAL   C C   1 
ATOM   1523 O  O   . VAL   B 1 56  ? 29.355 -30.818 16.284 1.00 11.84  ? 62  VAL   C O   1 
ATOM   1524 C  CB  . VAL   B 1 56  ? 30.479 -33.614 15.867 1.00 11.99  ? 62  VAL   C CB  1 
ATOM   1525 C  CG1 . VAL   B 1 56  ? 29.997 -33.809 14.415 1.00 13.96  ? 62  VAL   C CG1 1 
ATOM   1526 C  CG2 . VAL   B 1 56  ? 31.417 -34.772 16.277 1.00 12.33  ? 62  VAL   C CG2 1 
ATOM   1527 N  N   . TYR   B 1 57  ? 30.573 -30.519 14.394 1.00 10.82  ? 63  TYR   C N   1 
ATOM   1528 C  CA  . TYR   B 1 57  ? 29.676 -29.442 13.930 1.00 10.45  ? 63  TYR   C CA  1 
ATOM   1529 C  C   . TYR   B 1 57  ? 29.122 -29.792 12.552 1.00 11.33  ? 63  TYR   C C   1 
ATOM   1530 O  O   . TYR   B 1 57  ? 29.769 -30.512 11.782 1.00 12.26  ? 63  TYR   C O   1 
ATOM   1531 C  CB  . TYR   B 1 57  ? 30.362 -28.055 13.897 1.00 10.94  ? 63  TYR   C CB  1 
ATOM   1532 C  CG  . TYR   B 1 57  ? 31.221 -27.765 12.673 1.00 10.93  ? 63  TYR   C CG  1 
ATOM   1533 C  CD1 . TYR   B 1 57  ? 32.517 -28.245 12.581 1.00 12.66  ? 63  TYR   C CD1 1 
ATOM   1534 C  CD2 . TYR   B 1 57  ? 30.766 -26.914 11.663 1.00 11.36  ? 63  TYR   C CD2 1 
ATOM   1535 C  CE1 . TYR   B 1 57  ? 33.325 -27.946 11.481 1.00 13.38  ? 63  TYR   C CE1 1 
ATOM   1536 C  CE2 . TYR   B 1 57  ? 31.578 -26.581 10.575 1.00 11.95  ? 63  TYR   C CE2 1 
ATOM   1537 C  CZ  . TYR   B 1 57  ? 32.860 -27.089 10.496 1.00 12.96  ? 63  TYR   C CZ  1 
ATOM   1538 O  OH  . TYR   B 1 57  ? 33.696 -26.776 9.425  1.00 14.57  ? 63  TYR   C OH  1 
ATOM   1539 N  N   . TYR   B 1 58  ? 27.947 -29.218 12.236 1.00 11.39  ? 64  TYR   C N   1 
ATOM   1540 C  CA  . TYR   B 1 58  ? 27.350 -29.421 10.923 1.00 11.71  ? 64  TYR   C CA  1 
ATOM   1541 C  C   . TYR   B 1 58  ? 27.741 -28.280 9.998  1.00 11.50  ? 64  TYR   C C   1 
ATOM   1542 O  O   . TYR   B 1 58  ? 27.522 -27.090 10.339 1.00 11.60  ? 64  TYR   C O   1 
ATOM   1543 C  CB  . TYR   B 1 58  ? 25.820 -29.507 10.999 1.00 12.41  ? 64  TYR   C CB  1 
ATOM   1544 C  CG  . TYR   B 1 58  ? 25.222 -29.789 9.629  1.00 13.20  ? 64  TYR   C CG  1 
ATOM   1545 C  CD1 . TYR   B 1 58  ? 25.567 -30.931 8.923  1.00 14.40  ? 64  TYR   C CD1 1 
ATOM   1546 C  CD2 . TYR   B 1 58  ? 24.378 -28.879 9.022  1.00 13.51  ? 64  TYR   C CD2 1 
ATOM   1547 C  CE1 . TYR   B 1 58  ? 25.067 -31.178 7.639  1.00 14.66  ? 64  TYR   C CE1 1 
ATOM   1548 C  CE2 . TYR   B 1 58  ? 23.854 -29.118 7.749  1.00 14.12  ? 64  TYR   C CE2 1 
ATOM   1549 C  CZ  . TYR   B 1 58  ? 24.207 -30.271 7.057  1.00 15.69  ? 64  TYR   C CZ  1 
ATOM   1550 O  OH  . TYR   B 1 58  ? 23.717 -30.512 5.766  1.00 18.49  ? 64  TYR   C OH  1 
ATOM   1551 N  N   . CYS   B 1 59  ? 28.243 -28.647 8.807  1.00 11.64  ? 65  CYS   C N   1 
ATOM   1552 C  CA  . CYS   B 1 59  ? 28.667 -27.686 7.772  1.00 12.24  ? 65  CYS   C CA  1 
ATOM   1553 C  C   . CYS   B 1 59  ? 27.727 -27.858 6.552  1.00 13.15  ? 65  CYS   C C   1 
ATOM   1554 O  O   . CYS   B 1 59  ? 27.906 -28.814 5.773  1.00 13.84  ? 65  CYS   C O   1 
ATOM   1555 C  CB  . CYS   B 1 59  ? 30.102 -27.961 7.380  1.00 13.08  ? 65  CYS   C CB  1 
ATOM   1556 S  SG  . CYS   B 1 59  ? 30.701 -26.889 6.046  1.00 15.34  ? 65  CYS   C SG  1 
ATOM   1557 N  N   . SER   B 1 60  ? 26.726 -26.953 6.404  1.00 13.21  ? 66  SER   C N   1 
ATOM   1558 C  CA  A SER   B 1 60  ? 25.745 -27.138 5.341  0.50 14.49  ? 66  SER   C CA  1 
ATOM   1559 C  CA  B SER   B 1 60  ? 25.740 -27.096 5.347  0.50 13.95  ? 66  SER   C CA  1 
ATOM   1560 C  C   . SER   B 1 60  ? 26.356 -27.023 3.954  1.00 14.42  ? 66  SER   C C   1 
ATOM   1561 O  O   . SER   B 1 60  ? 25.907 -27.736 3.057  1.00 16.31  ? 66  SER   C O   1 
ATOM   1562 C  CB  A SER   B 1 60  ? 24.566 -26.189 5.499  0.50 17.47  ? 66  SER   C CB  1 
ATOM   1563 C  CB  B SER   B 1 60  ? 24.665 -26.031 5.483  0.50 15.31  ? 66  SER   C CB  1 
ATOM   1564 O  OG  A SER   B 1 60  ? 24.988 -24.839 5.446  0.50 20.21  ? 66  SER   C OG  1 
ATOM   1565 O  OG  B SER   B 1 60  ? 23.678 -26.263 4.496  0.50 15.41  ? 66  SER   C OG  1 
ATOM   1566 N  N   . SER   B 1 61  ? 27.387 -26.195 3.788  1.00 14.61  ? 67  SER   C N   1 
ATOM   1567 C  CA  . SER   B 1 61  ? 28.015 -26.062 2.465  1.00 15.15  ? 67  SER   C CA  1 
ATOM   1568 C  C   . SER   B 1 61  ? 28.841 -27.273 2.039  1.00 16.18  ? 67  SER   C C   1 
ATOM   1569 O  O   . SER   B 1 61  ? 29.307 -27.319 0.888  1.00 17.48  ? 67  SER   C O   1 
ATOM   1570 C  CB  . SER   B 1 61  ? 28.857 -24.808 2.402  1.00 15.82  ? 67  SER   C CB  1 
ATOM   1571 O  OG  . SER   B 1 61  ? 29.958 -24.899 3.279  1.00 17.58  ? 67  SER   C OG  1 
ATOM   1572 N  N   . ARG   B 1 62  ? 28.993 -28.266 2.918  1.00 14.62  ? 68  ARG   C N   1 
ATOM   1573 C  CA  . ARG   B 1 62  ? 29.618 -29.527 2.547  1.00 14.28  ? 68  ARG   C CA  1 
ATOM   1574 C  C   . ARG   B 1 62  ? 28.672 -30.720 2.781  1.00 15.74  ? 68  ARG   C C   1 
ATOM   1575 O  O   . ARG   B 1 62  ? 29.084 -31.870 2.572  1.00 17.30  ? 68  ARG   C O   1 
ATOM   1576 C  CB  . ARG   B 1 62  ? 30.910 -29.744 3.343  1.00 14.33  ? 68  ARG   C CB  1 
ATOM   1577 C  CG  . ARG   B 1 62  ? 31.977 -28.657 3.129  1.00 19.41  ? 68  ARG   C CG  1 
ATOM   1578 C  CD  . ARG   B 1 62  ? 32.652 -28.902 1.810  1.00 19.39  ? 68  ARG   C CD  1 
ATOM   1579 N  NE  . ARG   B 1 62  ? 33.695 -27.907 1.531  1.00 20.36  ? 68  ARG   C NE  1 
ATOM   1580 C  CZ  . ARG   B 1 62  ? 33.499 -26.758 0.899  1.00 24.15  ? 68  ARG   C CZ  1 
ATOM   1581 N  NH1 . ARG   B 1 62  ? 32.289 -26.433 0.453  1.00 25.27  ? 68  ARG   C NH1 1 
ATOM   1582 N  NH2 . ARG   B 1 62  ? 34.528 -25.951 0.634  1.00 24.66  ? 68  ARG   C NH2 1 
ATOM   1583 N  N   . ARG   B 1 63  ? 27.451 -30.472 3.325  1.00 16.45  ? 69  ARG   C N   1 
ATOM   1584 C  CA  . ARG   B 1 63  ? 26.499 -31.524 3.746  1.00 17.91  ? 69  ARG   C CA  1 
ATOM   1585 C  C   . ARG   B 1 63  ? 27.216 -32.575 4.619  1.00 18.47  ? 69  ARG   C C   1 
ATOM   1586 O  O   . ARG   B 1 63  ? 27.077 -33.786 4.409  1.00 20.24  ? 69  ARG   C O   1 
ATOM   1587 C  CB  . ARG   B 1 63  ? 25.861 -32.209 2.521  1.00 19.44  ? 69  ARG   C CB  1 
ATOM   1588 C  CG  . ARG   B 1 63  ? 25.021 -31.301 1.654  1.00 23.69  ? 69  ARG   C CG  1 
ATOM   1589 C  CD  . ARG   B 1 63  ? 23.739 -30.965 2.324  1.00 29.73  ? 69  ARG   C CD  1 
ATOM   1590 N  NE  . ARG   B 1 63  ? 22.744 -30.493 1.369  1.00 33.76  ? 69  ARG   C NE  1 
ATOM   1591 C  CZ  . ARG   B 1 63  ? 22.556 -29.219 1.054  1.00 35.64  ? 69  ARG   C CZ  1 
ATOM   1592 N  NH1 . ARG   B 1 63  ? 23.323 -28.271 1.589  1.00 34.24  ? 69  ARG   C NH1 1 
ATOM   1593 N  NH2 . ARG   B 1 63  ? 21.597 -28.879 0.207  1.00 35.20  ? 69  ARG   C NH2 1 
ATOM   1594 N  N   . LYS   B 1 64  ? 28.072 -32.081 5.535  1.00 16.37  ? 70  LYS   C N   1 
ATOM   1595 C  CA  . LYS   B 1 64  ? 28.865 -32.990 6.346  1.00 16.00  ? 70  LYS   C CA  1 
ATOM   1596 C  C   . LYS   B 1 64  ? 28.966 -32.522 7.777  1.00 15.48  ? 70  LYS   C C   1 
ATOM   1597 O  O   . LYS   B 1 64  ? 29.019 -31.308 8.034  1.00 15.20  ? 70  LYS   C O   1 
ATOM   1598 C  CB  . LYS   B 1 64  ? 30.289 -33.040 5.790  1.00 20.17  ? 70  LYS   C CB  1 
ATOM   1599 C  CG  . LYS   B 1 64  ? 30.442 -34.041 4.657  1.00 30.92  ? 70  LYS   C CG  1 
ATOM   1600 C  CD  . LYS   B 1 64  ? 31.674 -34.911 4.830  1.00 39.12  ? 70  LYS   C CD  1 
ATOM   1601 C  CE  . LYS   B 1 64  ? 31.886 -35.727 3.572  1.00 45.76  ? 70  LYS   C CE  1 
ATOM   1602 N  NZ  . LYS   B 1 64  ? 31.688 -34.911 2.340  1.00 49.05  ? 70  LYS   C NZ  1 
ATOM   1603 N  N   . HIS   B 1 65  ? 29.098 -33.492 8.702  1.00 14.57  ? 71  HIS   C N   1 
ATOM   1604 C  CA  . HIS   B 1 65  ? 29.387 -33.211 10.109 1.00 13.91  ? 71  HIS   C CA  1 
ATOM   1605 C  C   . HIS   B 1 65  ? 30.875 -33.479 10.313 1.00 15.33  ? 71  HIS   C C   1 
ATOM   1606 O  O   . HIS   B 1 65  ? 31.369 -34.564 9.925  1.00 17.90  ? 71  HIS   C O   1 
ATOM   1607 C  CB  . HIS   B 1 65  ? 28.572 -34.112 11.044 1.00 13.56  ? 71  HIS   C CB  1 
ATOM   1608 C  CG  . HIS   B 1 65  ? 27.097 -33.833 10.980 1.00 12.89  ? 71  HIS   C CG  1 
ATOM   1609 N  ND1 . HIS   B 1 65  ? 26.441 -33.070 11.951 1.00 15.54  ? 71  HIS   C ND1 1 
ATOM   1610 C  CD2 . HIS   B 1 65  ? 26.184 -34.265 10.083 1.00 13.89  ? 71  HIS   C CD2 1 
ATOM   1611 C  CE1 . HIS   B 1 65  ? 25.154 -33.085 11.623 1.00 15.26  ? 71  HIS   C CE1 1 
ATOM   1612 N  NE2 . HIS   B 1 65  ? 24.946 -33.794 10.522 1.00 16.62  ? 71  HIS   C NE2 1 
ATOM   1613 N  N   . TYR   B 1 66  ? 31.610 -32.514 10.894 1.00 13.02  ? 72  TYR   C N   1 
ATOM   1614 C  CA  . TYR   B 1 66  ? 33.046 -32.705 11.069 1.00 12.73  ? 72  TYR   C CA  1 
ATOM   1615 C  C   . TYR   B 1 66  ? 33.410 -32.743 12.545 1.00 12.15  ? 72  TYR   C C   1 
ATOM   1616 O  O   . TYR   B 1 66  ? 32.993 -31.859 13.289 1.00 11.83  ? 72  TYR   C O   1 
ATOM   1617 C  CB  . TYR   B 1 66  ? 33.800 -31.501 10.481 1.00 13.56  ? 72  TYR   C CB  1 
ATOM   1618 C  CG  . TYR   B 1 66  ? 33.759 -31.407 8.965  1.00 15.31  ? 72  TYR   C CG  1 
ATOM   1619 C  CD1 . TYR   B 1 66  ? 34.590 -32.185 8.180  1.00 16.72  ? 72  TYR   C CD1 1 
ATOM   1620 C  CD2 . TYR   B 1 66  ? 32.926 -30.500 8.326  1.00 16.33  ? 72  TYR   C CD2 1 
ATOM   1621 C  CE1 . TYR   B 1 66  ? 34.620 -32.042 6.795  1.00 17.26  ? 72  TYR   C CE1 1 
ATOM   1622 C  CE2 . TYR   B 1 66  ? 32.941 -30.349 6.940  1.00 16.53  ? 72  TYR   C CE2 1 
ATOM   1623 C  CZ  . TYR   B 1 66  ? 33.775 -31.139 6.173  1.00 17.63  ? 72  TYR   C CZ  1 
ATOM   1624 O  OH  . TYR   B 1 66  ? 33.766 -30.969 4.792  1.00 19.87  ? 72  TYR   C OH  1 
ATOM   1625 N  N   . PRO   B 1 67  ? 34.239 -33.723 12.956 1.00 12.70  ? 73  PRO   C N   1 
ATOM   1626 C  CA  . PRO   B 1 67  ? 34.764 -33.684 14.335 1.00 12.53  ? 73  PRO   C CA  1 
ATOM   1627 C  C   . PRO   B 1 67  ? 35.856 -32.615 14.435 1.00 12.92  ? 73  PRO   C C   1 
ATOM   1628 O  O   . PRO   B 1 67  ? 36.709 -32.514 13.527 1.00 14.86  ? 73  PRO   C O   1 
ATOM   1629 C  CB  . PRO   B 1 67  ? 35.370 -35.081 14.535 1.00 14.97  ? 73  PRO   C CB  1 
ATOM   1630 C  CG  . PRO   B 1 67  ? 35.611 -35.618 13.187 1.00 16.89  ? 73  PRO   C CG  1 
ATOM   1631 C  CD  . PRO   B 1 67  ? 34.757 -34.873 12.167 1.00 13.70  ? 73  PRO   C CD  1 
ATOM   1632 N  N   . VAL   B 1 68  ? 35.811 -31.812 15.480 1.00 11.92  ? 74  VAL   C N   1 
ATOM   1633 C  CA  . VAL   B 1 68  ? 36.783 -30.717 15.621 1.00 13.13  ? 74  VAL   C CA  1 
ATOM   1634 C  C   . VAL   B 1 68  ? 37.206 -30.524 17.046 1.00 12.22  ? 74  VAL   C C   1 
ATOM   1635 O  O   . VAL   B 1 68  ? 36.451 -30.799 17.985 1.00 12.70  ? 74  VAL   C O   1 
ATOM   1636 C  CB  . VAL   B 1 68  ? 36.178 -29.350 15.119 1.00 15.05  ? 74  VAL   C CB  1 
ATOM   1637 C  CG1 . VAL   B 1 68  ? 36.147 -29.263 13.586 1.00 17.14  ? 74  VAL   C CG1 1 
ATOM   1638 C  CG2 . VAL   B 1 68  ? 34.823 -29.049 15.765 1.00 15.28  ? 74  VAL   C CG2 1 
ATOM   1639 N  N   . SER   B 1 69  ? 38.414 -29.949 17.218 1.00 12.31  ? 75  SER   C N   1 
ATOM   1640 C  CA  . SER   B 1 69  ? 38.872 -29.362 18.476 1.00 12.68  ? 75  SER   C CA  1 
ATOM   1641 C  C   . SER   B 1 69  ? 38.601 -27.850 18.376 1.00 12.35  ? 75  SER   C C   1 
ATOM   1642 O  O   . SER   B 1 69  ? 38.762 -27.246 17.303 1.00 13.11  ? 75  SER   C O   1 
ATOM   1643 C  CB  . SER   B 1 69  ? 40.381 -29.550 18.628 1.00 15.51  ? 75  SER   C CB  1 
ATOM   1644 O  OG  . SER   B 1 69  ? 40.650 -30.936 18.766 1.00 21.67  ? 75  SER   C OG  1 
ATOM   1645 N  N   . PHE   B 1 70  ? 38.100 -27.247 19.444 1.00 11.29  ? 76  PHE   C N   1 
ATOM   1646 C  CA  . PHE   B 1 70  ? 37.754 -25.819 19.414 1.00 12.16  ? 76  PHE   C CA  1 
ATOM   1647 C  C   . PHE   B 1 70  ? 38.254 -25.081 20.652 1.00 13.08  ? 76  PHE   C C   1 
ATOM   1648 O  O   . PHE   B 1 70  ? 38.419 -25.687 21.720 1.00 13.14  ? 76  PHE   C O   1 
ATOM   1649 C  CB  . PHE   B 1 70  ? 36.255 -25.568 19.182 1.00 12.41  ? 76  PHE   C CB  1 
ATOM   1650 C  CG  . PHE   B 1 70  ? 35.351 -26.296 20.159 1.00 11.86  ? 76  PHE   C CG  1 
ATOM   1651 C  CD1 . PHE   B 1 70  ? 34.909 -27.588 19.893 1.00 11.73  ? 76  PHE   C CD1 1 
ATOM   1652 C  CD2 . PHE   B 1 70  ? 34.908 -25.673 21.312 1.00 13.39  ? 76  PHE   C CD2 1 
ATOM   1653 C  CE1 . PHE   B 1 70  ? 34.104 -28.263 20.805 1.00 11.77  ? 76  PHE   C CE1 1 
ATOM   1654 C  CE2 . PHE   B 1 70  ? 34.065 -26.340 22.202 1.00 13.41  ? 76  PHE   C CE2 1 
ATOM   1655 C  CZ  . PHE   B 1 70  ? 33.665 -27.624 21.944 1.00 12.33  ? 76  PHE   C CZ  1 
ATOM   1656 N  N   . SER   B 1 71  ? 38.533 -23.793 20.500 1.00 12.67  ? 77  SER   C N   1 
ATOM   1657 C  CA  . SER   B 1 71  ? 39.127 -23.012 21.582 1.00 14.05  ? 77  SER   C CA  1 
ATOM   1658 C  C   . SER   B 1 71  ? 38.115 -22.635 22.661 1.00 15.71  ? 77  SER   C C   1 
ATOM   1659 O  O   . SER   B 1 71  ? 36.896 -22.841 22.495 1.00 15.59  ? 77  SER   C O   1 
ATOM   1660 C  CB  . SER   B 1 71  ? 39.847 -21.794 21.006 1.00 14.59  ? 77  SER   C CB  1 
ATOM   1661 O  OG  . SER   B 1 71  ? 38.902 -20.926 20.389 1.00 16.63  ? 77  SER   C OG  1 
ATOM   1662 N  N   . LYS   B 1 72  ? 38.580 -22.068 23.776 1.00 17.15  ? 78  LYS   C N   1 
ATOM   1663 C  CA  . LYS   B 1 72  ? 37.670 -21.657 24.846 1.00 17.59  ? 78  LYS   C CA  1 
ATOM   1664 C  C   . LYS   B 1 72  ? 36.988 -20.337 24.436 1.00 17.11  ? 78  LYS   C C   1 
ATOM   1665 O  O   . LYS   B 1 72  ? 37.581 -19.535 23.717 1.00 17.25  ? 78  LYS   C O   1 
ATOM   1666 C  CB  . LYS   B 1 72  ? 38.478 -21.460 26.145 1.00 22.84  ? 78  LYS   C CB  1 
ATOM   1667 C  CG  . LYS   B 1 72  ? 39.088 -22.765 26.636 1.00 30.27  ? 78  LYS   C CG  1 
ATOM   1668 C  CD  . LYS   B 1 72  ? 39.335 -22.769 28.146 1.00 40.37  ? 78  LYS   C CD  1 
ATOM   1669 C  CE  . LYS   B 1 72  ? 39.572 -24.172 28.676 1.00 46.47  ? 78  LYS   C CE  1 
ATOM   1670 N  NZ  . LYS   B 1 72  ? 39.640 -24.191 30.165 1.00 50.29  ? 78  LYS   C NZ  1 
ATOM   1671 N  N   . PRO   B 1 73  ? 35.752 -20.099 24.885 1.00 16.45  ? 79  PRO   C N   1 
ATOM   1672 C  CA  . PRO   B 1 73  ? 35.030 -18.857 24.464 1.00 16.78  ? 79  PRO   C CA  1 
ATOM   1673 C  C   . PRO   B 1 73  ? 35.816 -17.612 24.848 1.00 17.88  ? 79  PRO   C C   1 
ATOM   1674 O  O   . PRO   B 1 73  ? 36.245 -17.479 26.004 1.00 19.82  ? 79  PRO   C O   1 
ATOM   1675 C  CB  . PRO   B 1 73  ? 33.731 -18.878 25.265 1.00 18.26  ? 79  PRO   C CB  1 
ATOM   1676 C  CG  . PRO   B 1 73  ? 33.630 -20.241 25.862 1.00 19.80  ? 79  PRO   C CG  1 
ATOM   1677 C  CD  . PRO   B 1 73  ? 34.945 -20.966 25.772 1.00 17.30  ? 79  PRO   C CD  1 
ATOM   1678 N  N   . SER   B 1 74  ? 36.075 -16.725 23.880 1.00 16.30  ? 80  SER   C N   1 
ATOM   1679 C  CA  . SER   B 1 74  ? 36.933 -15.561 24.112 1.00 16.86  ? 80  SER   C CA  1 
ATOM   1680 C  C   . SER   B 1 74  ? 36.523 -14.383 23.229 1.00 16.80  ? 80  SER   C C   1 
ATOM   1681 O  O   . SER   B 1 74  ? 35.629 -14.514 22.381 1.00 16.17  ? 80  SER   C O   1 
ATOM   1682 C  CB  . SER   B 1 74  ? 38.381 -15.908 23.753 1.00 20.25  ? 80  SER   C CB  1 
ATOM   1683 O  OG  . SER   B 1 74  ? 38.779 -17.169 24.263 1.00 27.36  ? 80  SER   C OG  1 
ATOM   1684 N  N   . LEU   B 1 75  ? 37.187 -13.224 23.423 1.00 17.17  ? 81  LEU   C N   1 
ATOM   1685 C  CA  . LEU   B 1 75  ? 36.989 -12.012 22.618 1.00 18.35  ? 81  LEU   C CA  1 
ATOM   1686 C  C   . LEU   B 1 75  ? 38.003 -12.085 21.469 1.00 19.49  ? 81  LEU   C C   1 
ATOM   1687 O  O   . LEU   B 1 75  ? 39.228 -12.022 21.714 1.00 20.67  ? 81  LEU   C O   1 
ATOM   1688 C  CB  . LEU   B 1 75  ? 37.227 -10.755 23.503 1.00 20.06  ? 81  LEU   C CB  1 
ATOM   1689 C  CG  . LEU   B 1 75  ? 36.946 -9.417  22.849 1.00 23.60  ? 81  LEU   C CG  1 
ATOM   1690 C  CD1 . LEU   B 1 75  ? 35.474 -9.231  22.615 1.00 23.20  ? 81  LEU   C CD1 1 
ATOM   1691 C  CD2 . LEU   B 1 75  ? 37.436 -8.274  23.751 1.00 25.65  ? 81  LEU   C CD2 1 
ATOM   1692 N  N   . ILE   B 1 76  ? 37.519 -12.324 20.237 1.00 19.68  ? 82  ILE   C N   1 
ATOM   1693 C  CA  . ILE   B 1 76  ? 38.367 -12.574 19.056 1.00 20.47  ? 82  ILE   C CA  1 
ATOM   1694 C  C   . ILE   B 1 76  ? 38.108 -11.488 18.008 1.00 20.46  ? 82  ILE   C C   1 
ATOM   1695 O  O   . ILE   B 1 76  ? 36.943 -11.159 17.752 1.00 19.10  ? 82  ILE   C O   1 
ATOM   1696 C  CB  . ILE   B 1 76  ? 37.943 -13.967 18.461 1.00 22.57  ? 82  ILE   C CB  1 
ATOM   1697 C  CG1 . ILE   B 1 76  ? 38.199 -15.161 19.431 1.00 24.77  ? 82  ILE   C CG1 1 
ATOM   1698 C  CG2 . ILE   B 1 76  ? 38.575 -14.236 17.079 1.00 24.72  ? 82  ILE   C CG2 1 
ATOM   1699 C  CD1 . ILE   B 1 76  ? 39.634 -15.562 19.602 1.00 26.11  ? 82  ILE   C CD1 1 
ATOM   1700 N  N   . PHE   B 1 77  ? 39.173 -11.018 17.332 1.00 20.64  ? 83  PHE   C N   1 
ATOM   1701 C  CA  . PHE   B 1 77  ? 38.997 -10.084 16.218 1.00 21.23  ? 83  PHE   C CA  1 
ATOM   1702 C  C   . PHE   B 1 77  ? 38.625 -10.932 14.982 1.00 21.06  ? 83  PHE   C C   1 
ATOM   1703 O  O   . PHE   B 1 77  ? 39.297 -11.933 14.648 1.00 22.76  ? 83  PHE   C O   1 
ATOM   1704 C  CB  . PHE   B 1 77  ? 40.283 -9.288  15.931 1.00 21.75  ? 83  PHE   C CB  1 
ATOM   1705 C  CG  . PHE   B 1 77  ? 40.027 -8.139  14.973 1.00 22.46  ? 83  PHE   C CG  1 
ATOM   1706 C  CD1 . PHE   B 1 77  ? 39.323 -7.020  15.383 1.00 23.60  ? 83  PHE   C CD1 1 
ATOM   1707 C  CD2 . PHE   B 1 77  ? 40.399 -8.230  13.638 1.00 23.79  ? 83  PHE   C CD2 1 
ATOM   1708 C  CE1 . PHE   B 1 77  ? 39.016 -5.996  14.481 1.00 24.86  ? 83  PHE   C CE1 1 
ATOM   1709 C  CE2 . PHE   B 1 77  ? 40.119 -7.200  12.749 1.00 24.62  ? 83  PHE   C CE2 1 
ATOM   1710 C  CZ  . PHE   B 1 77  ? 39.430 -6.090  13.169 1.00 24.54  ? 83  PHE   C CZ  1 
ATOM   1711 N  N   . VAL   B 1 78  ? 37.500 -10.559 14.346 1.00 18.35  ? 84  VAL   C N   1 
ATOM   1712 C  CA  . VAL   B 1 78  ? 36.980 -11.275 13.192 1.00 18.03  ? 84  VAL   C CA  1 
ATOM   1713 C  C   . VAL   B 1 78  ? 37.059 -10.348 11.971 1.00 18.20  ? 84  VAL   C C   1 
ATOM   1714 O  O   . VAL   B 1 78  ? 36.610 -9.196  12.057 1.00 18.45  ? 84  VAL   C O   1 
ATOM   1715 C  CB  . VAL   B 1 78  ? 35.516 -11.703 13.467 1.00 18.82  ? 84  VAL   C CB  1 
ATOM   1716 C  CG1 . VAL   B 1 78  ? 34.969 -12.494 12.280 1.00 19.24  ? 84  VAL   C CG1 1 
ATOM   1717 C  CG2 . VAL   B 1 78  ? 35.405 -12.518 14.771 1.00 19.31  ? 84  VAL   C CG2 1 
ATOM   1718 N  N   . GLU   B 1 79  ? 37.591 -10.851 10.835 1.00 17.63  ? 85  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 79  ? 37.620 -10.062 9.607  1.00 17.62  ? 85  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 79  ? 36.202 -9.801  9.080  1.00 17.77  ? 85  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 79  ? 35.242 -10.482 9.461  1.00 16.91  ? 85  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 79  ? 38.458 -10.743 8.503  1.00 20.65  ? 85  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 79  ? 39.945 -10.752 8.825  1.00 25.58  ? 85  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 79  ? 40.546 -9.379  9.079  1.00 35.72  ? 85  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 79  ? 40.290 -8.448  8.281  1.00 38.45  ? 85  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 79  ? 41.250 -9.222  10.102 1.00 39.89  ? 85  GLU   C OE2 1 
ATOM   1727 N  N   . ALA   B 1 80  ? 36.063 -8.792  8.209  1.00 18.02  ? 86  ALA   C N   1 
ATOM   1728 C  CA  . ALA   B 1 80  ? 34.778 -8.440  7.619  1.00 18.35  ? 86  ALA   C CA  1 
ATOM   1729 C  C   . ALA   B 1 80  ? 34.161 -9.644  6.888  1.00 18.31  ? 86  ALA   C C   1 
ATOM   1730 O  O   . ALA   B 1 80  ? 34.881 -10.443 6.271  1.00 20.29  ? 86  ALA   C O   1 
ATOM   1731 C  CB  . ALA   B 1 80  ? 34.992 -7.305  6.612  1.00 19.22  ? 86  ALA   C CB  1 
ATOM   1732 N  N   . SER   B 1 81  ? 32.857 -9.807  7.048  1.00 17.66  ? 87  SER   C N   1 
ATOM   1733 C  CA  . SER   B 1 81  ? 32.125 -10.830 6.361  1.00 18.94  ? 87  SER   C CA  1 
ATOM   1734 C  C   . SER   B 1 81  ? 31.000 -10.147 5.553  1.00 20.28  ? 87  SER   C C   1 
ATOM   1735 O  O   . SER   B 1 81  ? 30.853 -8.908  5.596  1.00 20.87  ? 87  SER   C O   1 
ATOM   1736 C  CB  . SER   B 1 81  ? 31.537 -11.813 7.371  1.00 18.06  ? 87  SER   C CB  1 
ATOM   1737 O  OG  . SER   B 1 81  ? 30.517 -11.158 8.115  1.00 17.85  ? 87  SER   C OG  1 
ATOM   1738 N  N   . GLU   B 1 82  ? 30.177 -10.948 4.873  1.00 21.02  ? 88  GLU   C N   1 
ATOM   1739 C  CA  . GLU   B 1 82  ? 29.073 -10.331 4.125  1.00 22.23  ? 88  GLU   C CA  1 
ATOM   1740 C  C   . GLU   B 1 82  ? 27.988 -9.725  5.055  1.00 21.99  ? 88  GLU   C C   1 
ATOM   1741 O  O   . GLU   B 1 82  ? 27.221 -8.876  4.609  1.00 23.21  ? 88  GLU   C O   1 
ATOM   1742 C  CB  . GLU   B 1 82  ? 28.495 -11.308 3.104  1.00 26.70  ? 88  GLU   C CB  1 
ATOM   1743 C  CG  . GLU   B 1 82  ? 27.624 -12.387 3.684  1.00 33.87  ? 88  GLU   C CG  1 
ATOM   1744 C  CD  . GLU   B 1 82  ? 26.910 -13.197 2.618  1.00 40.16  ? 88  GLU   C CD  1 
ATOM   1745 O  OE1 . GLU   B 1 82  ? 27.495 -13.374 1.521  1.00 40.54  ? 88  GLU   C OE1 1 
ATOM   1746 O  OE2 . GLU   B 1 82  ? 25.773 -13.660 2.885  1.00 41.08  ? 88  GLU   C OE2 1 
ATOM   1747 N  N   . TYR   B 1 83  ? 27.999 -10.059 6.350  1.00 19.48  ? 89  TYR   C N   1 
ATOM   1748 C  CA  . TYR   B 1 83  ? 26.975 -9.595  7.292  1.00 18.37  ? 89  TYR   C CA  1 
ATOM   1749 C  C   . TYR   B 1 83  ? 27.495 -8.732  8.495  1.00 18.90  ? 89  TYR   C C   1 
ATOM   1750 O  O   . TYR   B 1 83  ? 26.664 -8.177  9.215  1.00 20.23  ? 89  TYR   C O   1 
ATOM   1751 C  CB  . TYR   B 1 83  ? 26.145 -10.811 7.793  1.00 17.80  ? 89  TYR   C CB  1 
ATOM   1752 C  CG  . TYR   B 1 83  ? 26.987 -11.992 8.254  1.00 17.60  ? 89  TYR   C CG  1 
ATOM   1753 C  CD1 . TYR   B 1 83  ? 27.410 -12.975 7.356  1.00 17.14  ? 89  TYR   C CD1 1 
ATOM   1754 C  CD2 . TYR   B 1 83  ? 27.377 -12.115 9.577  1.00 17.30  ? 89  TYR   C CD2 1 
ATOM   1755 C  CE1 . TYR   B 1 83  ? 28.190 -14.052 7.779  1.00 16.52  ? 89  TYR   C CE1 1 
ATOM   1756 C  CE2 . TYR   B 1 83  ? 28.119 -13.207 10.016 1.00 17.61  ? 89  TYR   C CE2 1 
ATOM   1757 C  CZ  . TYR   B 1 83  ? 28.540 -14.159 9.110  1.00 16.68  ? 89  TYR   C CZ  1 
ATOM   1758 O  OH  . TYR   B 1 83  ? 29.335 -15.213 9.514  1.00 17.35  ? 89  TYR   C OH  1 
ATOM   1759 N  N   . TYR   B 1 84  ? 28.831 -8.591  8.722  1.00 17.34  ? 90  TYR   C N   1 
ATOM   1760 C  CA  . TYR   B 1 84  ? 29.380 -7.689  9.758  1.00 16.67  ? 90  TYR   C CA  1 
ATOM   1761 C  C   . TYR   B 1 84  ? 30.698 -7.100  9.251  1.00 16.98  ? 90  TYR   C C   1 
ATOM   1762 O  O   . TYR   B 1 84  ? 31.421 -7.753  8.506  1.00 17.55  ? 90  TYR   C O   1 
ATOM   1763 C  CB  . TYR   B 1 84  ? 29.714 -8.431  11.089 1.00 15.80  ? 90  TYR   C CB  1 
ATOM   1764 C  CG  . TYR   B 1 84  ? 28.536 -8.850  11.945 1.00 14.76  ? 90  TYR   C CG  1 
ATOM   1765 C  CD1 . TYR   B 1 84  ? 27.637 -7.912  12.459 1.00 15.10  ? 90  TYR   C CD1 1 
ATOM   1766 C  CD2 . TYR   B 1 84  ? 28.348 -10.163 12.286 1.00 14.99  ? 90  TYR   C CD2 1 
ATOM   1767 C  CE1 . TYR   B 1 84  ? 26.567 -8.299  13.281 1.00 15.42  ? 90  TYR   C CE1 1 
ATOM   1768 C  CE2 . TYR   B 1 84  ? 27.264 -10.569 13.072 1.00 14.92  ? 90  TYR   C CE2 1 
ATOM   1769 C  CZ  . TYR   B 1 84  ? 26.396 -9.635  13.610 1.00 16.13  ? 90  TYR   C CZ  1 
ATOM   1770 O  OH  . TYR   B 1 84  ? 25.331 -10.028 14.422 1.00 15.82  ? 90  TYR   C OH  1 
ATOM   1771 N  N   . PRO   B 1 85  ? 31.055 -5.896  9.704  1.00 17.68  ? 91  PRO   C N   1 
ATOM   1772 C  CA  . PRO   B 1 85  ? 32.397 -5.383  9.403  1.00 18.31  ? 91  PRO   C CA  1 
ATOM   1773 C  C   . PRO   B 1 85  ? 33.433 -6.134  10.258 1.00 18.42  ? 91  PRO   C C   1 
ATOM   1774 O  O   . PRO   B 1 85  ? 33.098 -6.971  11.127 1.00 18.17  ? 91  PRO   C O   1 
ATOM   1775 C  CB  . PRO   B 1 85  ? 32.279 -3.914  9.840  1.00 19.09  ? 91  PRO   C CB  1 
ATOM   1776 C  CG  . PRO   B 1 85  ? 31.358 -3.945  10.985 1.00 19.38  ? 91  PRO   C CG  1 
ATOM   1777 C  CD  . PRO   B 1 85  ? 30.323 -5.018  10.649 1.00 18.09  ? 91  PRO   C CD  1 
ATOM   1778 N  N   . ALA   B 1 86  ? 34.731 -5.832  10.039 1.00 18.00  ? 92  ALA   C N   1 
ATOM   1779 C  CA  . ALA   B 1 86  ? 35.788 -6.385  10.889 1.00 19.37  ? 92  ALA   C CA  1 
ATOM   1780 C  C   . ALA   B 1 86  ? 35.592 -5.816  12.304 1.00 20.37  ? 92  ALA   C C   1 
ATOM   1781 O  O   . ALA   B 1 86  ? 35.330 -4.604  12.434 1.00 22.41  ? 92  ALA   C O   1 
ATOM   1782 C  CB  . ALA   B 1 86  ? 37.162 -5.970  10.352 1.00 19.88  ? 92  ALA   C CB  1 
ATOM   1783 N  N   . ARG   B 1 87  ? 35.602 -6.681  13.329 1.00 19.54  ? 93  ARG   C N   1 
ATOM   1784 C  CA  . ARG   B 1 87  ? 35.318 -6.206  14.689 1.00 19.36  ? 93  ARG   C CA  1 
ATOM   1785 C  C   . ARG   B 1 87  ? 35.688 -7.297  15.712 1.00 19.63  ? 93  ARG   C C   1 
ATOM   1786 O  O   . ARG   B 1 87  ? 35.915 -8.447  15.335 1.00 19.41  ? 93  ARG   C O   1 
ATOM   1787 C  CB  . ARG   B 1 87  ? 33.799 -5.911  14.821 1.00 19.80  ? 93  ARG   C CB  1 
ATOM   1788 C  CG  . ARG   B 1 87  ? 32.950 -7.203  14.680 1.00 19.13  ? 93  ARG   C CG  1 
ATOM   1789 C  CD  . ARG   B 1 87  ? 31.448 -6.989  14.846 1.00 18.78  ? 93  ARG   C CD  1 
ATOM   1790 N  NE  . ARG   B 1 87  ? 30.754 -8.261  15.059 1.00 18.62  ? 93  ARG   C NE  1 
ATOM   1791 C  CZ  . ARG   B 1 87  ? 29.660 -8.437  15.793 1.00 20.42  ? 93  ARG   C CZ  1 
ATOM   1792 N  NH1 . ARG   B 1 87  ? 29.043 -7.399  16.342 1.00 19.80  ? 93  ARG   C NH1 1 
ATOM   1793 N  NH2 . ARG   B 1 87  ? 29.182 -9.650  15.989 1.00 19.00  ? 93  ARG   C NH2 1 
ATOM   1794 N  N   . TYR   B 1 88  ? 35.620 -6.964  17.015 1.00 20.10  ? 94  TYR   C N   1 
ATOM   1795 C  CA  . TYR   B 1 88  ? 35.783 -7.973  18.058 1.00 21.36  ? 94  TYR   C CA  1 
ATOM   1796 C  C   . TYR   B 1 88  ? 34.425 -8.611  18.338 1.00 19.91  ? 94  TYR   C C   1 
ATOM   1797 O  O   . TYR   B 1 88  ? 33.416 -7.909  18.497 1.00 21.12  ? 94  TYR   C O   1 
ATOM   1798 C  CB  . TYR   B 1 88  ? 36.262 -7.313  19.363 1.00 23.83  ? 94  TYR   C CB  1 
ATOM   1799 C  CG  . TYR   B 1 88  ? 37.723 -6.974  19.281 1.00 26.67  ? 94  TYR   C CG  1 
ATOM   1800 C  CD1 . TYR   B 1 88  ? 38.688 -7.947  19.460 1.00 27.99  ? 94  TYR   C CD1 1 
ATOM   1801 C  CD2 . TYR   B 1 88  ? 38.137 -5.691  18.940 1.00 28.86  ? 94  TYR   C CD2 1 
ATOM   1802 C  CE1 . TYR   B 1 88  ? 40.041 -7.642  19.356 1.00 30.19  ? 94  TYR   C CE1 1 
ATOM   1803 C  CE2 . TYR   B 1 88  ? 39.475 -5.375  18.828 1.00 30.10  ? 94  TYR   C CE2 1 
ATOM   1804 C  CZ  . TYR   B 1 88  ? 40.425 -6.346  19.050 1.00 31.81  ? 94  TYR   C CZ  1 
ATOM   1805 O  OH  . TYR   B 1 88  ? 41.746 -5.989  18.918 1.00 35.40  ? 94  TYR   C OH  1 
ATOM   1806 N  N   . GLN   B 1 89  ? 34.396 -9.940  18.361 1.00 17.99  ? 95  GLN   C N   1 
ATOM   1807 C  CA  . GLN   B 1 89  ? 33.184 -10.669 18.716 1.00 16.73  ? 95  GLN   C CA  1 
ATOM   1808 C  C   . GLN   B 1 89  ? 33.485 -11.421 20.012 1.00 15.77  ? 95  GLN   C C   1 
ATOM   1809 O  O   . GLN   B 1 89  ? 34.590 -11.996 20.168 1.00 16.52  ? 95  GLN   C O   1 
ATOM   1810 C  CB  . GLN   B 1 89  ? 32.777 -11.616 17.569 1.00 16.96  ? 95  GLN   C CB  1 
ATOM   1811 C  CG  . GLN   B 1 89  ? 31.503 -12.393 17.886 1.00 17.91  ? 95  GLN   C CG  1 
ATOM   1812 C  CD  . GLN   B 1 89  ? 30.830 -13.008 16.675 1.00 16.28  ? 95  GLN   C CD  1 
ATOM   1813 O  OE1 . GLN   B 1 89  ? 30.794 -12.420 15.576 1.00 17.21  ? 95  GLN   C OE1 1 
ATOM   1814 N  NE2 . GLN   B 1 89  ? 30.278 -14.184 16.873 1.00 15.38  ? 95  GLN   C NE2 1 
ATOM   1815 N  N   . SER   B 1 90  ? 32.572 -11.366 20.967 1.00 15.46  ? 96  SER   C N   1 
ATOM   1816 C  CA  . SER   B 1 90  ? 32.768 -12.017 22.257 1.00 14.93  ? 96  SER   C CA  1 
ATOM   1817 C  C   . SER   B 1 90  ? 32.170 -13.428 22.333 1.00 14.37  ? 96  SER   C C   1 
ATOM   1818 O  O   . SER   B 1 90  ? 31.306 -13.771 21.526 1.00 13.90  ? 96  SER   C O   1 
ATOM   1819 C  CB  . SER   B 1 90  ? 32.215 -11.135 23.384 1.00 16.32  ? 96  SER   C CB  1 
ATOM   1820 O  OG  . SER   B 1 90  ? 30.811 -11.090 23.268 1.00 17.58  ? 96  SER   C OG  1 
ATOM   1821 N  N   . HIS   B 1 91  ? 32.626 -14.211 23.329 1.00 14.17  ? 97  HIS   C N   1 
ATOM   1822 C  CA  . HIS   B 1 91  ? 32.129 -15.575 23.594 1.00 13.20  ? 97  HIS   C CA  1 
ATOM   1823 C  C   . HIS   B 1 91  ? 32.215 -16.445 22.323 1.00 13.88  ? 97  HIS   C C   1 
ATOM   1824 O  O   . HIS   B 1 91  ? 31.325 -17.266 22.072 1.00 14.95  ? 97  HIS   C O   1 
ATOM   1825 C  CB  . HIS   B 1 91  ? 30.676 -15.514 24.140 1.00 14.84  ? 97  HIS   C CB  1 
ATOM   1826 C  CG  . HIS   B 1 91  ? 30.560 -14.764 25.449 1.00 17.41  ? 97  HIS   C CG  1 
ATOM   1827 N  ND1 . HIS   B 1 91  ? 30.539 -15.431 26.665 1.00 19.21  ? 97  HIS   C ND1 1 
ATOM   1828 C  CD2 . HIS   B 1 91  ? 30.454 -13.424 25.681 1.00 18.41  ? 97  HIS   C CD2 1 
ATOM   1829 C  CE1 . HIS   B 1 91  ? 30.401 -14.490 27.598 1.00 19.25  ? 97  HIS   C CE1 1 
ATOM   1830 N  NE2 . HIS   B 1 91  ? 30.330 -13.263 27.057 1.00 19.51  ? 97  HIS   C NE2 1 
ATOM   1831 N  N   . LEU   B 1 92  ? 33.292 -16.272 21.558 1.00 13.14  ? 98  LEU   C N   1 
ATOM   1832 C  CA  . LEU   B 1 92  ? 33.475 -16.974 20.300 1.00 13.23  ? 98  LEU   C CA  1 
ATOM   1833 C  C   . LEU   B 1 92  ? 34.573 -18.036 20.473 1.00 13.23  ? 98  LEU   C C   1 
ATOM   1834 O  O   . LEU   B 1 92  ? 35.569 -17.811 21.171 1.00 13.68  ? 98  LEU   C O   1 
ATOM   1835 C  CB  . LEU   B 1 92  ? 33.950 -15.958 19.218 1.00 14.70  ? 98  LEU   C CB  1 
ATOM   1836 C  CG  . LEU   B 1 92  ? 34.060 -16.531 17.800 1.00 16.42  ? 98  LEU   C CG  1 
ATOM   1837 C  CD1 . LEU   B 1 92  ? 32.690 -16.883 17.249 1.00 16.90  ? 98  LEU   C CD1 1 
ATOM   1838 C  CD2 . LEU   B 1 92  ? 34.773 -15.528 16.840 1.00 17.38  ? 98  LEU   C CD2 1 
ATOM   1839 N  N   . MET   B 1 93  ? 34.358 -19.209 19.860 1.00 12.81  ? 99  MET   C N   1 
ATOM   1840 C  CA  . MET   B 1 93  ? 35.318 -20.321 19.907 1.00 12.27  ? 99  MET   C CA  1 
ATOM   1841 C  C   . MET   B 1 93  ? 35.736 -20.637 18.471 1.00 13.33  ? 99  MET   C C   1 
ATOM   1842 O  O   . MET   B 1 93  ? 34.871 -20.669 17.615 1.00 13.93  ? 99  MET   C O   1 
ATOM   1843 C  CB  . MET   B 1 93  ? 34.602 -21.554 20.491 1.00 13.98  ? 99  MET   C CB  1 
ATOM   1844 C  CG  . MET   B 1 93  ? 34.109 -21.286 21.891 1.00 16.65  ? 99  MET   C CG  1 
ATOM   1845 S  SD  . MET   B 1 93  ? 33.085 -22.603 22.545 1.00 17.08  ? 99  MET   C SD  1 
ATOM   1846 C  CE  . MET   B 1 93  ? 31.692 -22.547 21.435 1.00 17.95  ? 99  MET   C CE  1 
ATOM   1847 N  N   . LEU   B 1 94  ? 37.009 -20.911 18.213 1.00 12.63  ? 100 LEU   C N   1 
ATOM   1848 C  CA  . LEU   B 1 94  ? 37.460 -21.168 16.844 1.00 13.68  ? 100 LEU   C CA  1 
ATOM   1849 C  C   . LEU   B 1 94  ? 37.926 -22.596 16.692 1.00 13.85  ? 100 LEU   C C   1 
ATOM   1850 O  O   . LEU   B 1 94  ? 38.463 -23.198 17.637 1.00 14.31  ? 100 LEU   C O   1 
ATOM   1851 C  CB  . LEU   B 1 94  ? 38.711 -20.307 16.476 1.00 14.60  ? 100 LEU   C CB  1 
ATOM   1852 C  CG  . LEU   B 1 94  ? 38.520 -18.803 16.430 1.00 16.37  ? 100 LEU   C CG  1 
ATOM   1853 C  CD1 . LEU   B 1 94  ? 39.829 -18.110 16.012 1.00 19.46  ? 100 LEU   C CD1 1 
ATOM   1854 C  CD2 . LEU   B 1 94  ? 37.345 -18.404 15.500 1.00 17.34  ? 100 LEU   C CD2 1 
ATOM   1855 N  N   . ALA   B 1 95  ? 37.771 -23.114 15.471 1.00 13.39  ? 101 ALA   C N   1 
ATOM   1856 C  CA  . ALA   B 1 95  ? 38.310 -24.417 15.108 1.00 13.23  ? 101 ALA   C CA  1 
ATOM   1857 C  C   . ALA   B 1 95  ? 38.868 -24.303 13.674 1.00 12.60  ? 101 ALA   C C   1 
ATOM   1858 O  O   . ALA   B 1 95  ? 38.493 -23.386 12.925 1.00 13.05  ? 101 ALA   C O   1 
ATOM   1859 C  CB  . ALA   B 1 95  ? 37.213 -25.501 15.161 1.00 13.73  ? 101 ALA   C CB  1 
ATOM   1860 N  N   . VAL   B 1 96  ? 39.739 -25.249 13.289 1.00 12.93  ? 102 VAL   C N   1 
ATOM   1861 C  CA  . VAL   B 1 96  ? 40.213 -25.328 11.920 1.00 14.35  ? 102 VAL   C CA  1 
ATOM   1862 C  C   . VAL   B 1 96  ? 39.141 -26.091 11.126 1.00 14.70  ? 102 VAL   C C   1 
ATOM   1863 O  O   . VAL   B 1 96  ? 38.833 -27.260 11.417 1.00 15.53  ? 102 VAL   C O   1 
ATOM   1864 C  CB  . VAL   B 1 96  ? 41.569 -26.049 11.890 1.00 15.88  ? 102 VAL   C CB  1 
ATOM   1865 C  CG1 . VAL   B 1 96  ? 42.044 -26.231 10.445 1.00 16.90  ? 102 VAL   C CG1 1 
ATOM   1866 C  CG2 . VAL   B 1 96  ? 42.574 -25.248 12.698 1.00 16.21  ? 102 VAL   C CG2 1 
ATOM   1867 N  N   . GLY   B 1 97  ? 38.560 -25.431 10.151 1.00 15.50  ? 103 GLY   C N   1 
ATOM   1868 C  CA  . GLY   B 1 97  ? 37.470 -26.037 9.380  1.00 17.05  ? 103 GLY   C CA  1 
ATOM   1869 C  C   . GLY   B 1 97  ? 36.812 -25.075 8.438  1.00 17.20  ? 103 GLY   C C   1 
ATOM   1870 O  O   . GLY   B 1 97  ? 37.126 -23.870 8.430  1.00 18.46  ? 103 GLY   C O   1 
ATOM   1871 N  N   . HIS   B 1 98  ? 35.924 -25.611 7.610  1.00 15.57  ? 104 HIS   C N   1 
ATOM   1872 C  CA  . HIS   B 1 98  ? 35.259 -24.796 6.608  1.00 16.02  ? 104 HIS   C CA  1 
ATOM   1873 C  C   . HIS   B 1 98  ? 33.983 -24.103 7.132  1.00 16.12  ? 104 HIS   C C   1 
ATOM   1874 O  O   . HIS   B 1 98  ? 33.166 -24.720 7.825  1.00 15.56  ? 104 HIS   C O   1 
ATOM   1875 C  CB  . HIS   B 1 98  ? 34.892 -25.672 5.420  1.00 18.26  ? 104 HIS   C CB  1 
ATOM   1876 C  CG  . HIS   B 1 98  ? 34.384 -24.877 4.276  1.00 21.76  ? 104 HIS   C CG  1 
ATOM   1877 N  ND1 . HIS   B 1 98  ? 35.200 -23.974 3.608  1.00 24.52  ? 104 HIS   C ND1 1 
ATOM   1878 C  CD2 . HIS   B 1 98  ? 33.128 -24.788 3.784  1.00 23.88  ? 104 HIS   C CD2 1 
ATOM   1879 C  CE1 . HIS   B 1 98  ? 34.424 -23.388 2.712  1.00 26.88  ? 104 HIS   C CE1 1 
ATOM   1880 N  NE2 . HIS   B 1 98  ? 33.173 -23.867 2.761  1.00 26.51  ? 104 HIS   C NE2 1 
ATOM   1881 N  N   . SER   B 1 99  ? 33.787 -22.827 6.741  1.00 16.12  ? 105 SER   C N   1 
ATOM   1882 C  CA  . SER   B 1 99  ? 32.562 -22.097 7.116  1.00 16.77  ? 105 SER   C CA  1 
ATOM   1883 C  C   . SER   B 1 99  ? 32.327 -20.950 6.112  1.00 18.20  ? 105 SER   C C   1 
ATOM   1884 O  O   . SER   B 1 99  ? 33.197 -20.090 5.981  1.00 20.99  ? 105 SER   C O   1 
ATOM   1885 C  CB  . SER   B 1 99  ? 32.735 -21.480 8.497  1.00 17.53  ? 105 SER   C CB  1 
ATOM   1886 O  OG  . SER   B 1 99  ? 31.606 -20.704 8.878  1.00 17.81  ? 105 SER   C OG  1 
ATOM   1887 N  N   . GLU   B 1 100 ? 31.177 -20.956 5.432  1.00 17.71  ? 106 GLU   C N   1 
ATOM   1888 C  CA  . GLU   B 1 100 ? 30.728 -19.889 4.495  1.00 17.39  ? 106 GLU   C CA  1 
ATOM   1889 C  C   . GLU   B 1 100 ? 29.574 -19.178 5.217  1.00 16.04  ? 106 GLU   C C   1 
ATOM   1890 O  O   . GLU   B 1 100 ? 29.002 -19.711 6.182  1.00 15.80  ? 106 GLU   C O   1 
ATOM   1891 C  CB  . GLU   B 1 100 ? 30.106 -20.510 3.189  1.00 20.94  ? 106 GLU   C CB  1 
ATOM   1892 C  CG  . GLU   B 1 100 ? 30.823 -21.666 2.579  1.00 30.40  ? 106 GLU   C CG  1 
ATOM   1893 C  CD  . GLU   B 1 100 ? 31.393 -21.510 1.196  1.00 36.68  ? 106 GLU   C CD  1 
ATOM   1894 O  OE1 . GLU   B 1 100 ? 31.387 -20.390 0.631  1.00 41.11  ? 106 GLU   C OE1 1 
ATOM   1895 O  OE2 . GLU   B 1 100 ? 31.942 -22.522 0.722  1.00 36.89  ? 106 GLU   C OE2 1 
ATOM   1896 N  N   . PRO   B 1 101 ? 29.154 -17.981 4.749  1.00 16.27  ? 107 PRO   C N   1 
ATOM   1897 C  CA  . PRO   B 1 101 ? 28.031 -17.307 5.420  1.00 15.99  ? 107 PRO   C CA  1 
ATOM   1898 C  C   . PRO   B 1 101 ? 26.792 -18.182 5.587  1.00 15.83  ? 107 PRO   C C   1 
ATOM   1899 O  O   . PRO   B 1 101 ? 26.162 -18.123 6.648  1.00 16.96  ? 107 PRO   C O   1 
ATOM   1900 C  CB  . PRO   B 1 101 ? 27.719 -16.122 4.470  1.00 17.76  ? 107 PRO   C CB  1 
ATOM   1901 C  CG  . PRO   B 1 101 ? 29.007 -15.854 3.789  1.00 20.13  ? 107 PRO   C CG  1 
ATOM   1902 C  CD  . PRO   B 1 101 ? 29.730 -17.164 3.648  1.00 17.89  ? 107 PRO   C CD  1 
ATOM   1903 N  N   . GLY   B 1 102 ? 26.481 -19.027 4.578  1.00 14.97  ? 108 GLY   C N   1 
ATOM   1904 C  CA  . GLY   B 1 102 ? 25.263 -19.853 4.667  1.00 15.73  ? 108 GLY   C CA  1 
ATOM   1905 C  C   . GLY   B 1 102 ? 25.335 -20.950 5.719  1.00 14.81  ? 108 GLY   C C   1 
ATOM   1906 O  O   . GLY   B 1 102 ? 24.338 -21.607 6.039  1.00 15.94  ? 108 GLY   C O   1 
ATOM   1907 N  N   . ASP   B 1 103 ? 26.550 -21.213 6.233  1.00 13.12  ? 109 ASP   C N   1 
ATOM   1908 C  CA  . ASP   B 1 103 ? 26.735 -22.223 7.277  1.00 13.07  ? 109 ASP   C CA  1 
ATOM   1909 C  C   . ASP   B 1 103 ? 26.326 -21.752 8.660  1.00 13.50  ? 109 ASP   C C   1 
ATOM   1910 O  O   . ASP   B 1 103 ? 26.220 -22.558 9.597  1.00 13.35  ? 109 ASP   C O   1 
ATOM   1911 C  CB  . ASP   B 1 103 ? 28.211 -22.686 7.324  1.00 13.07  ? 109 ASP   C CB  1 
ATOM   1912 C  CG  . ASP   B 1 103 ? 28.541 -23.487 6.088  1.00 15.02  ? 109 ASP   C CG  1 
ATOM   1913 O  OD1 . ASP   B 1 103 ? 27.685 -24.244 5.635  1.00 15.58  ? 109 ASP   C OD1 1 
ATOM   1914 O  OD2 . ASP   B 1 103 ? 29.671 -23.337 5.554  1.00 17.44  ? 109 ASP   C OD2 1 
ATOM   1915 N  N   . CYS   B 1 104 ? 26.136 -20.418 8.852  1.00 12.42  ? 110 CYS   C N   1 
ATOM   1916 C  CA  . CYS   B 1 104 ? 25.727 -19.869 10.157 1.00 13.06  ? 110 CYS   C CA  1 
ATOM   1917 C  C   . CYS   B 1 104 ? 24.490 -20.565 10.663 1.00 13.44  ? 110 CYS   C C   1 
ATOM   1918 O  O   . CYS   B 1 104 ? 23.558 -20.775 9.891  1.00 14.32  ? 110 CYS   C O   1 
ATOM   1919 C  CB  . CYS   B 1 104 ? 25.498 -18.364 10.050 1.00 13.39  ? 110 CYS   C CB  1 
ATOM   1920 S  SG  . CYS   B 1 104 ? 27.034 -17.400 9.957  1.00 15.49  ? 110 CYS   C SG  1 
ATOM   1921 N  N   . GLY   B 1 105 ? 24.502 -20.926 11.931 1.00 11.24  ? 111 GLY   C N   1 
ATOM   1922 C  CA  . GLY   B 1 105 ? 23.351 -21.604 12.532 1.00 11.93  ? 111 GLY   C CA  1 
ATOM   1923 C  C   . GLY   B 1 105 ? 23.546 -23.112 12.688 1.00 12.02  ? 111 GLY   C C   1 
ATOM   1924 O  O   . GLY   B 1 105 ? 22.775 -23.778 13.397 1.00 13.30  ? 111 GLY   C O   1 
ATOM   1925 N  N   . GLY   B 1 106 ? 24.582 -23.667 12.029 1.00 11.99  ? 112 GLY   C N   1 
ATOM   1926 C  CA  . GLY   B 1 106 ? 24.901 -25.101 12.166 1.00 12.98  ? 112 GLY   C CA  1 
ATOM   1927 C  C   . GLY   B 1 106 ? 25.284 -25.395 13.608 1.00 12.30  ? 112 GLY   C C   1 
ATOM   1928 O  O   . GLY   B 1 106 ? 25.995 -24.588 14.224 1.00 12.23  ? 112 GLY   C O   1 
ATOM   1929 N  N   . ILE   B 1 107 ? 24.823 -26.542 14.153 1.00 11.70  ? 113 ILE   C N   1 
ATOM   1930 C  CA  . ILE   B 1 107 ? 25.101 -26.846 15.544 1.00 12.33  ? 113 ILE   C CA  1 
ATOM   1931 C  C   . ILE   B 1 107 ? 26.477 -27.481 15.738 1.00 11.58  ? 113 ILE   C C   1 
ATOM   1932 O  O   . ILE   B 1 107 ? 26.887 -28.356 14.972 1.00 11.68  ? 113 ILE   C O   1 
ATOM   1933 C  CB  . ILE   B 1 107 ? 23.970 -27.759 16.119 1.00 15.57  ? 113 ILE   C CB  1 
ATOM   1934 C  CG1 . ILE   B 1 107 ? 22.714 -26.843 16.478 1.00 18.00  ? 113 ILE   C CG1 1 
ATOM   1935 C  CG2 . ILE   B 1 107 ? 24.426 -28.603 17.339 1.00 15.48  ? 113 ILE   C CG2 1 
ATOM   1936 C  CD1 . ILE   B 1 107 ? 21.416 -27.592 16.898 1.00 21.82  ? 113 ILE   C CD1 1 
ATOM   1937 N  N   . LEU   B 1 108 ? 27.159 -27.055 16.845 1.00 11.25  ? 114 LEU   C N   1 
ATOM   1938 C  CA  . LEU   B 1 108 ? 28.345 -27.725 17.360 1.00 10.33  ? 114 LEU   C CA  1 
ATOM   1939 C  C   . LEU   B 1 108 ? 27.839 -28.473 18.626 1.00 10.90  ? 114 LEU   C C   1 
ATOM   1940 O  O   . LEU   B 1 108 ? 27.188 -27.873 19.482 1.00 11.07  ? 114 LEU   C O   1 
ATOM   1941 C  CB  . LEU   B 1 108 ? 29.393 -26.664 17.768 1.00 10.31  ? 114 LEU   C CB  1 
ATOM   1942 C  CG  . LEU   B 1 108 ? 30.609 -27.177 18.570 1.00 12.02  ? 114 LEU   C CG  1 
ATOM   1943 C  CD1 . LEU   B 1 108 ? 31.480 -28.084 17.722 1.00 12.34  ? 114 LEU   C CD1 1 
ATOM   1944 C  CD2 . LEU   B 1 108 ? 31.425 -25.995 19.099 1.00 12.94  ? 114 LEU   C CD2 1 
ATOM   1945 N  N   . ARG   B 1 109 ? 28.124 -29.780 18.707 1.00 10.99  ? 115 ARG   C N   1 
ATOM   1946 C  CA  . ARG   B 1 109 ? 27.661 -30.569 19.857 1.00 11.23  ? 115 ARG   C CA  1 
ATOM   1947 C  C   . ARG   B 1 109 ? 28.796 -31.411 20.431 1.00 12.55  ? 115 ARG   C C   1 
ATOM   1948 O  O   . ARG   B 1 109 ? 29.726 -31.822 19.716 1.00 13.13  ? 115 ARG   C O   1 
ATOM   1949 C  CB  . ARG   B 1 109 ? 26.512 -31.482 19.451 1.00 14.77  ? 115 ARG   C CB  1 
ATOM   1950 C  CG  . ARG   B 1 109 ? 26.909 -32.486 18.384 1.00 20.78  ? 115 ARG   C CG  1 
ATOM   1951 C  CD  . ARG   B 1 109 ? 25.672 -33.311 17.971 1.00 28.67  ? 115 ARG   C CD  1 
ATOM   1952 N  NE  . ARG   B 1 109 ? 24.750 -32.568 17.094 1.00 36.07  ? 115 ARG   C NE  1 
ATOM   1953 C  CZ  . ARG   B 1 109 ? 23.489 -32.252 17.410 1.00 44.10  ? 115 ARG   C CZ  1 
ATOM   1954 N  NH1 . ARG   B 1 109 ? 22.994 -32.566 18.605 1.00 44.88  ? 115 ARG   C NH1 1 
ATOM   1955 N  NH2 . ARG   B 1 109 ? 22.729 -31.583 16.548 1.00 46.00  ? 115 ARG   C NH2 1 
ATOM   1956 N  N   . CYS   B 1 110 ? 28.705 -31.648 21.727 1.00 12.57  ? 116 CYS   C N   1 
ATOM   1957 C  CA  . CYS   B 1 110 ? 29.669 -32.549 22.408 1.00 13.33  ? 116 CYS   C CA  1 
ATOM   1958 C  C   . CYS   B 1 110 ? 28.831 -33.668 23.094 1.00 14.59  ? 116 CYS   C C   1 
ATOM   1959 O  O   . CYS   B 1 110 ? 27.592 -33.756 22.882 1.00 14.32  ? 116 CYS   C O   1 
ATOM   1960 C  CB  . CYS   B 1 110 ? 30.471 -31.758 23.426 1.00 13.51  ? 116 CYS   C CB  1 
ATOM   1961 S  SG  . CYS   B 1 110 ? 29.424 -31.112 24.745 1.00 13.37  ? 116 CYS   C SG  1 
ATOM   1962 N  N   . GLN   B 1 111 ? 29.482 -34.517 23.948 1.00 15.05  ? 117 GLN   C N   1 
ATOM   1963 C  CA  . GLN   B 1 111 ? 28.706 -35.561 24.632 1.00 17.19  ? 117 GLN   C CA  1 
ATOM   1964 C  C   . GLN   B 1 111 ? 27.617 -35.007 25.541 1.00 17.35  ? 117 GLN   C C   1 
ATOM   1965 O  O   . GLN   B 1 111 ? 26.653 -35.724 25.860 1.00 19.80  ? 117 GLN   C O   1 
ATOM   1966 C  CB  . GLN   B 1 111 ? 29.632 -36.484 25.465 1.00 19.79  ? 117 GLN   C CB  1 
ATOM   1967 C  CG  . GLN   B 1 111 ? 30.324 -35.749 26.602 1.00 22.96  ? 117 GLN   C CG  1 
ATOM   1968 C  CD  . GLN   B 1 111 ? 31.306 -36.606 27.376 1.00 32.63  ? 117 GLN   C CD  1 
ATOM   1969 O  OE1 . GLN   B 1 111 ? 32.524 -36.526 27.167 1.00 35.03  ? 117 GLN   C OE1 1 
ATOM   1970 N  NE2 . GLN   B 1 111 ? 30.786 -37.400 28.308 1.00 32.96  ? 117 GLN   C NE2 1 
ATOM   1971 N  N   . HIS   B 1 112 ? 27.716 -33.712 25.949 1.00 15.27  ? 118 HIS   C N   1 
ATOM   1972 C  CA  . HIS   B 1 112 ? 26.730 -33.164 26.890 1.00 15.24  ? 118 HIS   C CA  1 
ATOM   1973 C  C   . HIS   B 1 112 ? 25.557 -32.460 26.211 1.00 16.03  ? 118 HIS   C C   1 
ATOM   1974 O  O   . HIS   B 1 112 ? 24.596 -32.084 26.887 1.00 17.26  ? 118 HIS   C O   1 
ATOM   1975 C  CB  . HIS   B 1 112 ? 27.441 -32.203 27.851 1.00 16.28  ? 118 HIS   C CB  1 
ATOM   1976 C  CG  . HIS   B 1 112 ? 28.626 -32.820 28.552 1.00 16.03  ? 118 HIS   C CG  1 
ATOM   1977 N  ND1 . HIS   B 1 112 ? 29.939 -32.544 28.166 1.00 16.70  ? 118 HIS   C ND1 1 
ATOM   1978 C  CD2 . HIS   B 1 112 ? 28.656 -33.654 29.621 1.00 17.73  ? 118 HIS   C CD2 1 
ATOM   1979 C  CE1 . HIS   B 1 112 ? 30.717 -33.228 28.980 1.00 17.71  ? 118 HIS   C CE1 1 
ATOM   1980 N  NE2 . HIS   B 1 112 ? 29.990 -33.941 29.857 1.00 18.18  ? 118 HIS   C NE2 1 
ATOM   1981 N  N   . GLY   B 1 113 ? 25.652 -32.217 24.899 1.00 14.73  ? 119 GLY   C N   1 
ATOM   1982 C  CA  . GLY   B 1 113 ? 24.588 -31.504 24.206 1.00 14.27  ? 119 GLY   C CA  1 
ATOM   1983 C  C   . GLY   B 1 113 ? 25.090 -30.432 23.250 1.00 12.85  ? 119 GLY   C C   1 
ATOM   1984 O  O   . GLY   B 1 113 ? 26.208 -30.520 22.739 1.00 12.86  ? 119 GLY   C O   1 
ATOM   1985 N  N   . VAL   B 1 114 ? 24.235 -29.439 22.971 1.00 12.42  ? 120 VAL   C N   1 
ATOM   1986 C  CA  . VAL   B 1 114 ? 24.588 -28.366 22.070 1.00 12.37  ? 120 VAL   C CA  1 
ATOM   1987 C  C   . VAL   B 1 114 ? 25.520 -27.370 22.754 1.00 12.40  ? 120 VAL   C C   1 
ATOM   1988 O  O   . VAL   B 1 114 ? 25.202 -26.818 23.833 1.00 13.88  ? 120 VAL   C O   1 
ATOM   1989 C  CB  . VAL   B 1 114 ? 23.290 -27.662 21.602 1.00 13.34  ? 120 VAL   C CB  1 
ATOM   1990 C  CG1 . VAL   B 1 114 ? 23.620 -26.428 20.735 1.00 14.06  ? 120 VAL   C CG1 1 
ATOM   1991 C  CG2 . VAL   B 1 114 ? 22.381 -28.665 20.853 1.00 14.92  ? 120 VAL   C CG2 1 
ATOM   1992 N  N   . VAL   B 1 115 ? 26.660 -27.132 22.129 1.00 11.19  ? 121 VAL   C N   1 
ATOM   1993 C  CA  . VAL   B 1 115 ? 27.669 -26.190 22.662 1.00 11.98  ? 121 VAL   C CA  1 
ATOM   1994 C  C   . VAL   B 1 115 ? 27.479 -24.775 22.121 1.00 13.20  ? 121 VAL   C C   1 
ATOM   1995 O  O   . VAL   B 1 115 ? 27.699 -23.777 22.837 1.00 13.02  ? 121 VAL   C O   1 
ATOM   1996 C  CB  . VAL   B 1 115 ? 29.057 -26.705 22.243 1.00 13.49  ? 121 VAL   C CB  1 
ATOM   1997 C  CG1 . VAL   B 1 115 ? 30.157 -25.691 22.588 1.00 13.78  ? 121 VAL   C CG1 1 
ATOM   1998 C  CG2 . VAL   B 1 115 ? 29.340 -28.081 22.843 1.00 13.93  ? 121 VAL   C CG2 1 
ATOM   1999 N  N   . GLY   B 1 116 ? 27.111 -24.686 20.834 1.00 11.89  ? 122 GLY   C N   1 
ATOM   2000 C  CA  . GLY   B 1 116 ? 26.916 -23.384 20.211 1.00 13.36  ? 122 GLY   C CA  1 
ATOM   2001 C  C   . GLY   B 1 116 ? 26.535 -23.539 18.747 1.00 11.35  ? 122 GLY   C C   1 
ATOM   2002 O  O   . GLY   B 1 116 ? 26.207 -24.645 18.293 1.00 12.22  ? 122 GLY   C O   1 
ATOM   2003 N  N   . ILE   B 1 117 ? 26.523 -22.384 18.018 1.00 11.14  ? 123 ILE   C N   1 
ATOM   2004 C  CA  . ILE   B 1 117 ? 26.178 -22.422 16.606 1.00 11.57  ? 123 ILE   C CA  1 
ATOM   2005 C  C   . ILE   B 1 117 ? 27.213 -21.678 15.790 1.00 11.64  ? 123 ILE   C C   1 
ATOM   2006 O  O   . ILE   B 1 117 ? 27.853 -20.724 16.260 1.00 12.03  ? 123 ILE   C O   1 
ATOM   2007 C  CB  . ILE   B 1 117 ? 24.787 -21.781 16.335 1.00 12.87  ? 123 ILE   C CB  1 
ATOM   2008 C  CG1 . ILE   B 1 117 ? 24.687 -20.395 16.985 1.00 13.53  ? 123 ILE   C CG1 1 
ATOM   2009 C  CG2 . ILE   B 1 117 ? 23.652 -22.717 16.810 1.00 14.09  ? 123 ILE   C CG2 1 
ATOM   2010 C  CD1 . ILE   B 1 117 ? 23.313 -19.664 16.562 1.00 13.21  ? 123 ILE   C CD1 1 
ATOM   2011 N  N   . VAL   B 1 118 ? 27.397 -22.123 14.544 1.00 10.94  ? 124 VAL   C N   1 
ATOM   2012 C  CA  . VAL   B 1 118 ? 28.331 -21.432 13.636 1.00 11.08  ? 124 VAL   C CA  1 
ATOM   2013 C  C   . VAL   B 1 118 ? 27.964 -19.938 13.512 1.00 11.45  ? 124 VAL   C C   1 
ATOM   2014 O  O   . VAL   B 1 118 ? 26.772 -19.596 13.357 1.00 12.16  ? 124 VAL   C O   1 
ATOM   2015 C  CB  . VAL   B 1 118 ? 28.345 -22.107 12.239 1.00 11.02  ? 124 VAL   C CB  1 
ATOM   2016 C  CG1 . VAL   B 1 118 ? 29.181 -21.316 11.246 1.00 12.16  ? 124 VAL   C CG1 1 
ATOM   2017 C  CG2 . VAL   B 1 118 ? 28.814 -23.567 12.313 1.00 12.12  ? 124 VAL   C CG2 1 
ATOM   2018 N  N   . SER   B 1 119 ? 28.999 -19.055 13.603 1.00 10.85  ? 125 SER   C N   1 
ATOM   2019 C  CA  . SER   B 1 119 ? 28.768 -17.610 13.475 1.00 11.90  ? 125 SER   C CA  1 
ATOM   2020 C  C   . SER   B 1 119 ? 29.784 -16.915 12.598 1.00 12.65  ? 125 SER   C C   1 
ATOM   2021 O  O   . SER   B 1 119 ? 29.474 -15.848 12.057 1.00 13.39  ? 125 SER   C O   1 
ATOM   2022 C  CB  . SER   B 1 119 ? 28.774 -16.989 14.866 1.00 13.96  ? 125 SER   C CB  1 
ATOM   2023 O  OG  . SER   B 1 119 ? 28.698 -15.566 14.807 1.00 15.44  ? 125 SER   C OG  1 
ATOM   2024 N  N   . THR   B 1 120 ? 31.031 -17.459 12.479 1.00 11.88  ? 126 THR   C N   1 
ATOM   2025 C  CA  . THR   B 1 120 ? 32.069 -16.792 11.677 1.00 11.80  ? 126 THR   C CA  1 
ATOM   2026 C  C   . THR   B 1 120 ? 32.746 -17.801 10.746 1.00 12.14  ? 126 THR   C C   1 
ATOM   2027 O  O   . THR   B 1 120 ? 32.665 -19.025 10.958 1.00 12.66  ? 126 THR   C O   1 
ATOM   2028 C  CB  . THR   B 1 120 ? 33.141 -16.090 12.582 1.00 12.22  ? 126 THR   C CB  1 
ATOM   2029 O  OG1 . THR   B 1 120 ? 34.017 -17.055 13.185 1.00 14.06  ? 126 THR   C OG1 1 
ATOM   2030 C  CG2 . THR   B 1 120 ? 32.525 -15.164 13.615 1.00 13.70  ? 126 THR   C CG2 1 
ATOM   2031 N  N   . GLY   B 1 121 ? 33.453 -17.301 9.755  1.00 13.96  ? 127 GLY   C N   1 
ATOM   2032 C  CA  . GLY   B 1 121 ? 34.229 -18.153 8.849  1.00 16.60  ? 127 GLY   C CA  1 
ATOM   2033 C  C   . GLY   B 1 121 ? 35.248 -17.345 8.073  1.00 19.90  ? 127 GLY   C C   1 
ATOM   2034 O  O   . GLY   B 1 121 ? 35.112 -16.144 7.937  1.00 21.58  ? 127 GLY   C O   1 
ATOM   2035 N  N   . GLY   B 1 122 ? 36.211 -18.014 7.489  1.00 22.52  ? 128 GLY   C N   1 
ATOM   2036 C  CA  . GLY   B 1 122 ? 37.268 -17.349 6.727  1.00 24.54  ? 128 GLY   C CA  1 
ATOM   2037 C  C   . GLY   B 1 122 ? 38.647 -17.751 7.200  1.00 24.58  ? 128 GLY   C C   1 
ATOM   2038 O  O   . GLY   B 1 122 ? 38.812 -18.183 8.335  1.00 23.92  ? 128 GLY   C O   1 
ATOM   2039 N  N   . ASN   B 1 123 ? 39.654 -17.601 6.341  1.00 23.96  ? 129 ASN   C N   1 
ATOM   2040 C  CA  . ASN   B 1 123 ? 41.034 -17.981 6.656  1.00 24.81  ? 129 ASN   C CA  1 
ATOM   2041 C  C   . ASN   B 1 123 ? 41.189 -19.454 7.087  1.00 22.94  ? 129 ASN   C C   1 
ATOM   2042 O  O   . ASN   B 1 123 ? 42.132 -19.785 7.793  1.00 25.33  ? 129 ASN   C O   1 
ATOM   2043 C  CB  . ASN   B 1 123 ? 41.658 -17.031 7.693  1.00 29.19  ? 129 ASN   C CB  1 
ATOM   2044 C  CG  . ASN   B 1 123 ? 42.495 -15.922 7.089  1.00 37.15  ? 129 ASN   C CG  1 
ATOM   2045 O  OD1 . ASN   B 1 123 ? 42.838 -15.928 5.897  1.00 39.03  ? 129 ASN   C OD1 1 
ATOM   2046 N  ND2 . ASN   B 1 123 ? 42.863 -14.936 7.897  1.00 39.75  ? 129 ASN   C ND2 1 
ATOM   2047 N  N   . GLY   B 1 124 ? 40.276 -20.316 6.644  1.00 20.44  ? 130 GLY   C N   1 
ATOM   2048 C  CA  . GLY   B 1 124 ? 40.327 -21.732 7.018  1.00 18.80  ? 130 GLY   C CA  1 
ATOM   2049 C  C   . GLY   B 1 124 ? 39.931 -22.009 8.459  1.00 17.73  ? 130 GLY   C C   1 
ATOM   2050 O  O   . GLY   B 1 124 ? 40.216 -23.096 8.978  1.00 17.66  ? 130 GLY   C O   1 
ATOM   2051 N  N   . LEU   B 1 125 ? 39.256 -21.051 9.106  1.00 16.65  ? 131 LEU   C N   1 
ATOM   2052 C  CA  . LEU   B 1 125 ? 38.774 -21.198 10.481 1.00 16.34  ? 131 LEU   C CA  1 
ATOM   2053 C  C   . LEU   B 1 125 ? 37.259 -21.081 10.527 1.00 16.00  ? 131 LEU   C C   1 
ATOM   2054 O  O   . LEU   B 1 125 ? 36.663 -20.332 9.744  1.00 18.30  ? 131 LEU   C O   1 
ATOM   2055 C  CB  . LEU   B 1 125 ? 39.376 -20.139 11.407 1.00 17.61  ? 131 LEU   C CB  1 
ATOM   2056 C  CG  . LEU   B 1 125 ? 40.911 -20.145 11.457 1.00 19.67  ? 131 LEU   C CG  1 
ATOM   2057 C  CD1 . LEU   B 1 125 ? 41.471 -18.780 11.866 1.00 23.43  ? 131 LEU   C CD1 1 
ATOM   2058 C  CD2 . LEU   B 1 125 ? 41.436 -21.322 12.268 1.00 20.12  ? 131 LEU   C CD2 1 
ATOM   2059 N  N   . VAL   B 1 126 ? 36.645 -21.795 11.455 1.00 13.04  ? 132 VAL   C N   1 
ATOM   2060 C  CA  . VAL   B 1 126 ? 35.211 -21.682 11.677 1.00 12.13  ? 132 VAL   C CA  1 
ATOM   2061 C  C   . VAL   B 1 126 ? 35.039 -21.201 13.141 1.00 12.49  ? 132 VAL   C C   1 
ATOM   2062 O  O   . VAL   B 1 126 ? 35.710 -21.712 14.051 1.00 12.43  ? 132 VAL   C O   1 
ATOM   2063 C  CB  . VAL   B 1 126 ? 34.467 -23.021 11.413 1.00 13.09  ? 132 VAL   C CB  1 
ATOM   2064 C  CG1 . VAL   B 1 126 ? 35.121 -24.179 12.135 1.00 14.53  ? 132 VAL   C CG1 1 
ATOM   2065 C  CG2 . VAL   B 1 126 ? 32.980 -22.935 11.810 1.00 12.85  ? 132 VAL   C CG2 1 
ATOM   2066 N  N   . GLY   B 1 127 ? 34.166 -20.218 13.331 1.00 11.98  ? 133 GLY   C N   1 
ATOM   2067 C  CA  . GLY   B 1 127 ? 33.922 -19.704 14.676 1.00 11.84  ? 133 GLY   C CA  1 
ATOM   2068 C  C   . GLY   B 1 127 ? 32.503 -20.011 15.141 1.00 12.33  ? 133 GLY   C C   1 
ATOM   2069 O  O   . GLY   B 1 127 ? 31.542 -19.874 14.370 1.00 12.21  ? 133 GLY   C O   1 
ATOM   2070 N  N   . PHE   B 1 128 ? 32.373 -20.421 16.406 1.00 10.77  ? 134 PHE   C N   1 
ATOM   2071 C  CA  . PHE   B 1 128 ? 31.072 -20.780 16.989 1.00 10.59  ? 134 PHE   C CA  1 
ATOM   2072 C  C   . PHE   B 1 128 ? 30.723 -19.845 18.136 1.00 12.11  ? 134 PHE   C C   1 
ATOM   2073 O  O   . PHE   B 1 128 ? 31.564 -19.606 18.999 1.00 12.42  ? 134 PHE   C O   1 
ATOM   2074 C  CB  . PHE   B 1 128 ? 31.120 -22.228 17.572 1.00 10.99  ? 134 PHE   C CB  1 
ATOM   2075 C  CG  . PHE   B 1 128 ? 31.667 -23.243 16.583 1.00 10.66  ? 134 PHE   C CG  1 
ATOM   2076 C  CD1 . PHE   B 1 128 ? 30.824 -23.877 15.678 1.00 10.84  ? 134 PHE   C CD1 1 
ATOM   2077 C  CD2 . PHE   B 1 128 ? 33.002 -23.605 16.605 1.00 12.08  ? 134 PHE   C CD2 1 
ATOM   2078 C  CE1 . PHE   B 1 128 ? 31.319 -24.825 14.803 1.00 11.21  ? 134 PHE   C CE1 1 
ATOM   2079 C  CE2 . PHE   B 1 128 ? 33.513 -24.548 15.715 1.00 12.77  ? 134 PHE   C CE2 1 
ATOM   2080 C  CZ  . PHE   B 1 128 ? 32.678 -25.150 14.820 1.00 11.41  ? 134 PHE   C CZ  1 
ATOM   2081 N  N   . ALA   B 1 129 ? 29.475 -19.375 18.168 1.00 12.18  ? 135 ALA   C N   1 
ATOM   2082 C  CA  . ALA   B 1 129 ? 28.977 -18.556 19.281 1.00 12.17  ? 135 ALA   C CA  1 
ATOM   2083 C  C   . ALA   B 1 129 ? 28.595 -19.545 20.406 1.00 12.58  ? 135 ALA   C C   1 
ATOM   2084 O  O   . ALA   B 1 129 ? 27.692 -20.386 20.234 1.00 12.95  ? 135 ALA   C O   1 
ATOM   2085 C  CB  . ALA   B 1 129 ? 27.737 -17.768 18.844 1.00 12.80  ? 135 ALA   C CB  1 
ATOM   2086 N  N   . ASP   B 1 130 ? 29.266 -19.433 21.555 1.00 12.66  ? 136 ASP   C N   1 
ATOM   2087 C  CA  . ASP   B 1 130 ? 29.002 -20.338 22.671 1.00 12.95  ? 136 ASP   C CA  1 
ATOM   2088 C  C   . ASP   B 1 130 ? 27.661 -20.013 23.281 1.00 13.99  ? 136 ASP   C C   1 
ATOM   2089 O  O   . ASP   B 1 130 ? 27.287 -18.828 23.378 1.00 13.67  ? 136 ASP   C O   1 
ATOM   2090 C  CB  . ASP   B 1 130 ? 30.068 -20.094 23.755 1.00 14.19  ? 136 ASP   C CB  1 
ATOM   2091 C  CG  . ASP   B 1 130 ? 29.954 -21.021 24.948 1.00 18.50  ? 136 ASP   C CG  1 
ATOM   2092 O  OD1 . ASP   B 1 130 ? 29.845 -22.242 24.749 1.00 18.09  ? 136 ASP   C OD1 1 
ATOM   2093 O  OD2 . ASP   B 1 130 ? 29.919 -20.507 26.081 1.00 20.98  ? 136 ASP   C OD2 1 
ATOM   2094 N  N   . VAL   B 1 131 ? 26.960 -21.036 23.770 1.00 12.16  ? 137 VAL   C N   1 
ATOM   2095 C  CA  . VAL   B 1 131 ? 25.718 -20.815 24.549 1.00 11.96  ? 137 VAL   C CA  1 
ATOM   2096 C  C   . VAL   B 1 131 ? 25.769 -21.503 25.927 1.00 13.15  ? 137 VAL   C C   1 
ATOM   2097 O  O   . VAL   B 1 131 ? 24.800 -21.429 26.671 1.00 13.83  ? 137 VAL   C O   1 
ATOM   2098 C  CB  . VAL   B 1 131 ? 24.435 -21.276 23.793 1.00 12.96  ? 137 VAL   C CB  1 
ATOM   2099 C  CG1 . VAL   B 1 131 ? 24.259 -20.482 22.479 1.00 13.66  ? 137 VAL   C CG1 1 
ATOM   2100 C  CG2 . VAL   B 1 131 ? 24.467 -22.769 23.514 1.00 12.85  ? 137 VAL   C CG2 1 
ATOM   2101 N  N   . ARG   B 1 132 ? 26.892 -22.148 26.273 1.00 12.93  ? 138 ARG   C N   1 
ATOM   2102 C  CA  . ARG   B 1 132 ? 26.963 -22.931 27.516 1.00 12.36  ? 138 ARG   C CA  1 
ATOM   2103 C  C   . ARG   B 1 132 ? 26.913 -22.097 28.787 1.00 13.78  ? 138 ARG   C C   1 
ATOM   2104 O  O   . ARG   B 1 132 ? 26.626 -22.657 29.856 1.00 14.84  ? 138 ARG   C O   1 
ATOM   2105 C  CB  . ARG   B 1 132 ? 28.213 -23.790 27.508 1.00 11.70  ? 138 ARG   C CB  1 
ATOM   2106 C  CG  . ARG   B 1 132 ? 28.210 -24.843 26.394 1.00 13.10  ? 138 ARG   C CG  1 
ATOM   2107 C  CD  . ARG   B 1 132 ? 29.523 -25.612 26.432 1.00 14.08  ? 138 ARG   C CD  1 
ATOM   2108 N  NE  . ARG   B 1 132 ? 30.614 -24.736 25.996 1.00 14.20  ? 138 ARG   C NE  1 
ATOM   2109 C  CZ  . ARG   B 1 132 ? 31.872 -25.122 25.868 1.00 15.76  ? 138 ARG   C CZ  1 
ATOM   2110 N  NH1 . ARG   B 1 132 ? 32.242 -26.353 26.235 1.00 15.27  ? 138 ARG   C NH1 1 
ATOM   2111 N  NH2 . ARG   B 1 132 ? 32.783 -24.279 25.397 1.00 15.72  ? 138 ARG   C NH2 1 
ATOM   2112 N  N   . ASP   B 1 133 ? 27.204 -20.792 28.694 1.00 13.73  ? 139 ASP   C N   1 
ATOM   2113 C  CA  . ASP   B 1 133 ? 27.144 -19.924 29.863 1.00 14.98  ? 139 ASP   C CA  1 
ATOM   2114 C  C   . ASP   B 1 133 ? 25.741 -19.381 30.110 1.00 16.36  ? 139 ASP   C C   1 
ATOM   2115 O  O   . ASP   B 1 133 ? 25.531 -18.751 31.168 1.00 16.95  ? 139 ASP   C O   1 
ATOM   2116 C  CB  . ASP   B 1 133 ? 28.131 -18.739 29.744 1.00 16.49  ? 139 ASP   C CB  1 
ATOM   2117 C  CG  . ASP   B 1 133 ? 27.775 -17.810 28.602 1.00 19.49  ? 139 ASP   C CG  1 
ATOM   2118 O  OD1 . ASP   B 1 133 ? 27.435 -18.312 27.522 1.00 17.48  ? 139 ASP   C OD1 1 
ATOM   2119 O  OD2 . ASP   B 1 133 ? 27.802 -16.561 28.806 1.00 21.32  ? 139 ASP   C OD2 1 
ATOM   2120 N  N   . LEU   B 1 134 ? 24.779 -19.588 29.157 1.00 16.00  ? 140 LEU   C N   1 
ATOM   2121 C  CA  . LEU   B 1 134 ? 23.425 -19.016 29.276 1.00 15.29  ? 140 LEU   C CA  1 
ATOM   2122 C  C   . LEU   B 1 134 ? 22.578 -20.006 30.059 1.00 15.06  ? 140 LEU   C C   1 
ATOM   2123 O  O   . LEU   B 1 134 ? 21.764 -20.756 29.489 1.00 14.83  ? 140 LEU   C O   1 
ATOM   2124 C  CB  . LEU   B 1 134 ? 22.874 -18.774 27.862 1.00 14.58  ? 140 LEU   C CB  1 
ATOM   2125 C  CG  . LEU   B 1 134 ? 23.723 -17.827 27.000 1.00 15.97  ? 140 LEU   C CG  1 
ATOM   2126 C  CD1 . LEU   B 1 134 ? 23.158 -17.741 25.576 1.00 16.15  ? 140 LEU   C CD1 1 
ATOM   2127 C  CD2 . LEU   B 1 134 ? 23.805 -16.403 27.642 1.00 16.86  ? 140 LEU   C CD2 1 
ATOM   2128 N  N   . LEU   B 1 135 ? 22.794 -20.030 31.399 1.00 16.11  ? 141 LEU   C N   1 
ATOM   2129 C  CA  . LEU   B 1 135 ? 22.141 -21.060 32.215 1.00 16.54  ? 141 LEU   C CA  1 
ATOM   2130 C  C   . LEU   B 1 135 ? 20.636 -20.955 32.242 1.00 16.65  ? 141 LEU   C C   1 
ATOM   2131 O  O   . LEU   B 1 135 ? 19.948 -21.967 32.428 1.00 17.71  ? 141 LEU   C O   1 
ATOM   2132 C  CB  . LEU   B 1 135 ? 22.726 -21.091 33.659 1.00 16.87  ? 141 LEU   C CB  1 
ATOM   2133 C  CG  . LEU   B 1 135 ? 24.275 -21.096 33.738 1.00 18.90  ? 141 LEU   C CG  1 
ATOM   2134 C  CD1 . LEU   B 1 135 ? 24.752 -21.178 35.189 1.00 19.87  ? 141 LEU   C CD1 1 
ATOM   2135 C  CD2 . LEU   B 1 135 ? 24.902 -22.236 32.884 1.00 20.12  ? 141 LEU   C CD2 1 
ATOM   2136 N  N   . TRP   B 1 136 ? 20.131 -19.732 32.058 1.00 15.83  ? 142 TRP   C N   1 
ATOM   2137 C  CA  . TRP   B 1 136 ? 18.694 -19.471 32.076 1.00 17.09  ? 142 TRP   C CA  1 
ATOM   2138 C  C   . TRP   B 1 136 ? 17.958 -20.177 30.930 1.00 17.68  ? 142 TRP   C C   1 
ATOM   2139 O  O   . TRP   B 1 136 ? 16.733 -20.308 31.002 1.00 19.48  ? 142 TRP   C O   1 
ATOM   2140 C  CB  . TRP   B 1 136 ? 18.417 -17.954 32.082 1.00 17.66  ? 142 TRP   C CB  1 
ATOM   2141 C  CG  . TRP   B 1 136 ? 19.104 -17.209 30.977 1.00 17.93  ? 142 TRP   C CG  1 
ATOM   2142 C  CD1 . TRP   B 1 136 ? 20.292 -16.550 31.042 1.00 18.24  ? 142 TRP   C CD1 1 
ATOM   2143 C  CD2 . TRP   B 1 136 ? 18.602 -17.000 29.636 1.00 17.73  ? 142 TRP   C CD2 1 
ATOM   2144 N  NE1 . TRP   B 1 136 ? 20.576 -15.956 29.820 1.00 18.71  ? 142 TRP   C NE1 1 
ATOM   2145 C  CE2 . TRP   B 1 136 ? 19.549 -16.216 28.945 1.00 18.66  ? 142 TRP   C CE2 1 
ATOM   2146 C  CE3 . TRP   B 1 136 ? 17.441 -17.381 28.976 1.00 18.25  ? 142 TRP   C CE3 1 
ATOM   2147 C  CZ2 . TRP   B 1 136 ? 19.364 -15.808 27.620 1.00 18.65  ? 142 TRP   C CZ2 1 
ATOM   2148 C  CZ3 . TRP   B 1 136 ? 17.245 -16.958 27.678 1.00 19.37  ? 142 TRP   C CZ3 1 
ATOM   2149 C  CH2 . TRP   B 1 136 ? 18.207 -16.200 27.007 1.00 19.09  ? 142 TRP   C CH2 1 
ATOM   2150 N  N   . LEU   B 1 137 ? 18.672 -20.653 29.875 1.00 17.06  ? 143 LEU   C N   1 
ATOM   2151 C  CA  . LEU   B 1 137 ? 17.977 -21.396 28.815 1.00 17.03  ? 143 LEU   C CA  1 
ATOM   2152 C  C   . LEU   B 1 137 ? 17.332 -22.688 29.361 1.00 20.70  ? 143 LEU   C C   1 
ATOM   2153 O  O   . LEU   B 1 137 ? 16.377 -23.188 28.760 1.00 22.28  ? 143 LEU   C O   1 
ATOM   2154 C  CB  . LEU   B 1 137 ? 18.926 -21.759 27.670 1.00 16.58  ? 143 LEU   C CB  1 
ATOM   2155 C  CG  . LEU   B 1 137 ? 19.388 -20.586 26.803 1.00 16.59  ? 143 LEU   C CG  1 
ATOM   2156 C  CD1 . LEU   B 1 137 ? 20.561 -21.001 25.883 1.00 16.71  ? 143 LEU   C CD1 1 
ATOM   2157 C  CD2 . LEU   B 1 137 ? 18.226 -20.041 25.951 1.00 17.42  ? 143 LEU   C CD2 1 
ATOM   2158 N  N   . ASP   B 1 138 ? 17.869 -23.240 30.483 1.00 20.42  ? 144 ASP   C N   1 
ATOM   2159 C  CA  . ASP   B 1 138 ? 17.391 -24.489 31.085 1.00 21.81  ? 144 ASP   C CA  1 
ATOM   2160 C  C   . ASP   B 1 138 ? 16.182 -24.316 32.007 1.00 24.64  ? 144 ASP   C C   1 
ATOM   2161 O  O   . ASP   B 1 138 ? 15.757 -25.315 32.589 1.00 25.29  ? 144 ASP   C O   1 
ATOM   2162 C  CB  . ASP   B 1 138 ? 18.497 -25.140 31.945 1.00 21.22  ? 144 ASP   C CB  1 
ATOM   2163 C  CG  . ASP   B 1 138 ? 19.744 -25.573 31.192 1.00 23.18  ? 144 ASP   C CG  1 
ATOM   2164 O  OD1 . ASP   B 1 138 ? 19.710 -25.615 29.946 1.00 23.23  ? 144 ASP   C OD1 1 
ATOM   2165 O  OD2 . ASP   B 1 138 ? 20.774 -25.846 31.860 1.00 24.54  ? 144 ASP   C OD2 1 
ATOM   2166 N  N   . GLU   B 1 139 ? 15.644 -23.101 32.167 1.00 26.30  ? 145 GLU   C N   1 
ATOM   2167 C  CA  . GLU   B 1 139 ? 14.533 -22.886 33.109 1.00 30.96  ? 145 GLU   C CA  1 
ATOM   2168 C  C   . GLU   B 1 139 ? 13.498 -21.854 32.595 1.00 35.17  ? 145 GLU   C C   1 
ATOM   2169 O  O   . GLU   B 1 139 ? 13.697 -21.259 31.538 1.00 35.29  ? 145 GLU   C O   1 
ATOM   2170 C  CB  . GLU   B 1 139 ? 15.137 -22.414 34.448 1.00 35.40  ? 145 GLU   C CB  1 
ATOM   2171 C  CG  . GLU   B 1 139 ? 15.851 -21.082 34.301 1.00 43.72  ? 145 GLU   C CG  1 
ATOM   2172 C  CD  . GLU   B 1 139 ? 16.823 -20.686 35.395 1.00 53.69  ? 145 GLU   C CD  1 
ATOM   2173 O  OE1 . GLU   B 1 139 ? 17.039 -19.465 35.583 1.00 55.02  ? 145 GLU   C OE1 1 
ATOM   2174 O  OE2 . GLU   B 1 139 ? 17.371 -21.595 36.059 1.00 57.00  ? 145 GLU   C OE2 1 
ATOM   2175 N  N   . GLU   B 1 140 ? 12.415 -21.623 33.382 1.00 38.13  ? 146 GLU   C N   1 
ATOM   2176 C  CA  . GLU   B 1 140 ? 11.333 -20.642 33.165 1.00 41.06  ? 146 GLU   C CA  1 
ATOM   2177 C  C   . GLU   B 1 140 ? 10.380 -21.064 32.063 1.00 43.79  ? 146 GLU   C C   1 
ATOM   2178 O  O   . GLU   B 1 140 ? 9.175  -21.165 32.322 1.00 45.28  ? 146 GLU   C O   1 
ATOM   2179 C  CB  . GLU   B 1 140 ? 11.865 -19.213 32.957 1.00 43.32  ? 146 GLU   C CB  1 
ATOM   2180 C  CG  . GLU   B 1 140 ? 10.858 -18.187 32.460 1.00 49.74  ? 146 GLU   C CG  1 
ATOM   2181 C  CD  . GLU   B 1 140 ? 10.142 -17.401 33.543 1.00 56.80  ? 146 GLU   C CD  1 
ATOM   2182 O  OE1 . GLU   B 1 140 ? 10.313 -16.161 33.582 1.00 58.97  ? 146 GLU   C OE1 1 
ATOM   2183 O  OE2 . GLU   B 1 140 ? 9.407  -18.021 34.345 1.00 58.96  ? 146 GLU   C OE2 1 
HETATM 2184 N  N1  . A1BRX C 2 .   ? 9.418  14.441  22.364 1.00 45.50  ? 201 A1BRX A N1  1 
HETATM 2185 N  N3  . A1BRX C 2 .   ? 8.314  10.504  23.255 1.00 46.78  ? 201 A1BRX A N3  1 
HETATM 2186 C  C4  . A1BRX C 2 .   ? 10.501 16.451  23.298 1.00 45.13  ? 201 A1BRX A C4  1 
HETATM 2187 C  C5  . A1BRX C 2 .   ? 10.137 15.000  23.509 1.00 45.43  ? 201 A1BRX A C5  1 
HETATM 2188 C  C6  . A1BRX C 2 .   ? 8.892  13.154  22.614 1.00 45.95  ? 201 A1BRX A C6  1 
HETATM 2189 C  C7  . A1BRX C 2 .   ? 9.193  10.898  22.351 1.00 46.09  ? 201 A1BRX A C7  1 
HETATM 2190 C  C8  . A1BRX C 2 .   ? 7.670  11.508  23.920 1.00 46.73  ? 201 A1BRX A C8  1 
HETATM 2191 C  C10 . A1BRX C 2 .   ? 6.104  12.119  25.649 1.00 47.10  ? 201 A1BRX A C10 1 
HETATM 2192 C  C13 . A1BRX C 2 .   ? 7.892  12.872  23.639 1.00 46.57  ? 201 A1BRX A C13 1 
HETATM 2193 O  O   . A1BRX C 2 .   ? 9.768  16.997  18.114 1.00 40.83  ? 201 A1BRX A O   1 
HETATM 2194 C  C   . A1BRX C 2 .   ? 10.680 16.189  18.253 1.00 40.48  ? 201 A1BRX A C   1 
HETATM 2195 N  N   . A1BRX C 2 .   ? 11.191 15.481  17.235 1.00 37.71  ? 201 A1BRX A N   1 
HETATM 2196 C  C1  . A1BRX C 2 .   ? 11.449 16.087  19.556 1.00 42.36  ? 201 A1BRX A C1  1 
HETATM 2197 C  C2  . A1BRX C 2 .   ? 10.587 16.014  20.825 1.00 44.10  ? 201 A1BRX A C2  1 
HETATM 2198 C  C14 . A1BRX C 2 .   ? 10.273 14.566  21.182 1.00 44.63  ? 201 A1BRX A C14 1 
HETATM 2199 C  C3  . A1BRX C 2 .   ? 11.282 16.667  22.004 1.00 44.98  ? 201 A1BRX A C3  1 
HETATM 2200 N  N2  . A1BRX C 2 .   ? 9.511  12.137  21.960 1.00 46.22  ? 201 A1BRX A N2  1 
HETATM 2201 C  C12 . A1BRX C 2 .   ? 7.171  13.838  24.392 1.00 46.97  ? 201 A1BRX A C12 1 
HETATM 2202 C  C11 . A1BRX C 2 .   ? 6.301  13.453  25.371 1.00 47.24  ? 201 A1BRX A C11 1 
HETATM 2203 C  C9  . A1BRX C 2 .   ? 6.766  11.156  24.946 1.00 46.88  ? 201 A1BRX A C9  1 
HETATM 2204 ZN ZN  . ZN    D 3 .   ? 11.001 -3.859  5.769  1.00 20.70  2 202 ZN    A ZN  1 
HETATM 2205 S  S   . DMS   E 4 .   ? 19.129 -2.340  24.423 1.00 79.08  ? 203 DMS   A S   1 
HETATM 2206 O  O   . DMS   E 4 .   ? 18.784 -3.779  24.710 1.00 78.92  ? 203 DMS   A O   1 
HETATM 2207 C  C1  . DMS   E 4 .   ? 20.872 -2.257  23.922 1.00 79.06  ? 203 DMS   A C1  1 
HETATM 2208 C  C2  . DMS   E 4 .   ? 18.437 -1.904  22.809 1.00 79.00  ? 203 DMS   A C2  1 
HETATM 2209 ZN ZN  . ZN    F 3 .   ? 30.649 -31.171 26.765 1.00 14.73  2 201 ZN    C ZN  1 
HETATM 2210 S  S   . DMS   G 4 .   ? 20.580 -31.786 9.103  1.00 100.36 ? 202 DMS   C S   1 
HETATM 2211 O  O   . DMS   G 4 .   ? 21.399 -32.057 7.880  1.00 100.41 ? 202 DMS   C O   1 
HETATM 2212 C  C1  . DMS   G 4 .   ? 21.634 -31.988 10.553 1.00 100.27 ? 202 DMS   C C1  1 
HETATM 2213 C  C2  . DMS   G 4 .   ? 20.376 -29.996 9.262  1.00 100.33 ? 202 DMS   C C2  1 
HETATM 2214 O  O   . HOH   H 5 .   ? 8.400  24.717  23.829 1.00 32.45  ? 301 HOH   A O   1 
HETATM 2215 O  O   . HOH   H 5 .   ? 2.087  22.802  21.729 1.00 32.53  ? 302 HOH   A O   1 
HETATM 2216 O  O   . HOH   H 5 .   ? 35.363 -3.885  7.839  1.00 25.79  ? 303 HOH   A O   1 
HETATM 2217 O  O   . HOH   H 5 .   ? 11.251 8.996   4.396  1.00 22.83  ? 304 HOH   A O   1 
HETATM 2218 O  O   . HOH   H 5 .   ? 17.905 -5.985  24.026 1.00 27.20  ? 305 HOH   A O   1 
HETATM 2219 O  O   . HOH   H 5 .   ? 12.339 21.696  13.165 1.00 46.67  ? 306 HOH   A O   1 
HETATM 2220 O  O   . HOH   H 5 .   ? 17.435 0.873   28.198 1.00 27.43  ? 307 HOH   A O   1 
HETATM 2221 O  O   . HOH   H 5 .   ? 12.324 -5.953  30.314 1.00 43.96  ? 308 HOH   A O   1 
HETATM 2222 O  O   . HOH   H 5 .   ? 37.570 14.741  14.154 1.00 42.58  ? 309 HOH   A O   1 
HETATM 2223 O  O   . HOH   H 5 .   ? 28.117 3.281   4.862  1.00 34.24  ? 310 HOH   A O   1 
HETATM 2224 O  O   . HOH   H 5 .   ? 4.546  9.648   28.022 1.00 37.56  ? 311 HOH   A O   1 
HETATM 2225 O  O   . HOH   H 5 .   ? 13.882 2.887   1.188  1.00 24.33  ? 312 HOH   A O   1 
HETATM 2226 O  O   . HOH   H 5 .   ? 38.334 4.714   10.491 1.00 47.98  ? 313 HOH   A O   1 
HETATM 2227 O  O   . HOH   H 5 .   ? 23.401 21.728  7.252  1.00 25.28  ? 314 HOH   A O   1 
HETATM 2228 O  O   . HOH   H 5 .   ? 31.366 -2.482  15.284 1.00 49.02  ? 315 HOH   A O   1 
HETATM 2229 O  O   . HOH   H 5 .   ? 10.724 10.129  31.405 1.00 22.05  ? 316 HOH   A O   1 
HETATM 2230 O  O   . HOH   H 5 .   ? 1.734  5.793   27.070 1.00 37.86  ? 317 HOH   A O   1 
HETATM 2231 O  O   . HOH   H 5 .   ? 33.787 14.072  9.709  1.00 32.74  ? 318 HOH   A O   1 
HETATM 2232 O  O   . HOH   H 5 .   ? 4.591  -3.506  28.768 1.00 30.02  ? 319 HOH   A O   1 
HETATM 2233 O  O   . HOH   H 5 .   ? 12.376 16.612  28.080 1.00 42.51  ? 320 HOH   A O   1 
HETATM 2234 O  O   . HOH   H 5 .   ? 2.976  9.431   9.117  1.00 32.23  ? 321 HOH   A O   1 
HETATM 2235 O  O   . HOH   H 5 .   ? 2.722  -2.954  20.795 1.00 25.14  ? 322 HOH   A O   1 
HETATM 2236 O  O   . HOH   H 5 .   ? 8.680  18.850  19.717 1.00 25.87  ? 323 HOH   A O   1 
HETATM 2237 O  O   . HOH   H 5 .   ? 19.461 9.985   19.650 1.00 14.36  ? 324 HOH   A O   1 
HETATM 2238 O  O   . HOH   H 5 .   ? 30.440 10.447  15.587 1.00 31.81  ? 325 HOH   A O   1 
HETATM 2239 O  O   . HOH   H 5 .   ? 3.437  20.893  24.632 1.00 45.09  ? 326 HOH   A O   1 
HETATM 2240 O  O   . HOH   H 5 .   ? 25.110 4.918   21.452 1.00 37.59  ? 327 HOH   A O   1 
HETATM 2241 O  O   . HOH   H 5 .   ? 20.166 -4.464  10.996 1.00 36.49  ? 328 HOH   A O   1 
HETATM 2242 O  O   . HOH   H 5 .   ? 19.657 20.034  22.246 1.00 44.97  ? 329 HOH   A O   1 
HETATM 2243 O  O   . HOH   H 5 .   ? 27.786 8.118   1.620  1.00 34.65  ? 330 HOH   A O   1 
HETATM 2244 O  O   . HOH   H 5 .   ? -0.008 1.298   15.889 1.00 13.11  ? 331 HOH   A O   1 
HETATM 2245 O  O   . HOH   H 5 .   ? 21.880 2.399   -0.883 1.00 36.82  ? 332 HOH   A O   1 
HETATM 2246 O  O   . HOH   H 5 .   ? 23.421 11.705  22.057 1.00 38.14  ? 333 HOH   A O   1 
HETATM 2247 O  O   . HOH   H 5 .   ? 15.000 11.320  0.116  1.00 38.61  ? 334 HOH   A O   1 
HETATM 2248 O  O   . HOH   H 5 .   ? 3.743  -8.084  9.875  1.00 47.74  ? 335 HOH   A O   1 
HETATM 2249 O  O   . HOH   H 5 .   ? 33.987 -2.332  13.495 1.00 33.41  ? 336 HOH   A O   1 
HETATM 2250 O  O   . HOH   H 5 .   ? 30.017 11.438  18.349 1.00 30.00  ? 337 HOH   A O   1 
HETATM 2251 O  O   . HOH   H 5 .   ? -2.064 -3.656  11.733 1.00 55.54  ? 338 HOH   A O   1 
HETATM 2252 O  O   . HOH   H 5 .   ? 29.900 -1.568  8.563  1.00 35.02  ? 339 HOH   A O   1 
HETATM 2253 O  O   . HOH   H 5 .   ? 5.682  5.501   32.735 1.00 25.01  ? 340 HOH   A O   1 
HETATM 2254 O  O   . HOH   H 5 .   ? 16.708 3.816   23.664 1.00 18.04  ? 341 HOH   A O   1 
HETATM 2255 O  O   . HOH   H 5 .   ? 14.056 13.746  23.999 1.00 22.17  ? 342 HOH   A O   1 
HETATM 2256 O  O   . HOH   H 5 .   ? 26.840 -1.287  8.844  1.00 25.24  ? 343 HOH   A O   1 
HETATM 2257 O  O   . HOH   H 5 .   ? 6.097  2.578   5.840  1.00 28.71  ? 344 HOH   A O   1 
HETATM 2258 O  O   . HOH   H 5 .   ? 22.699 0.824   17.373 1.00 17.02  ? 345 HOH   A O   1 
HETATM 2259 O  O   . HOH   H 5 .   ? 0.521  -0.912  19.417 1.00 21.25  ? 346 HOH   A O   1 
HETATM 2260 O  O   . HOH   H 5 .   ? 21.836 4.815   24.815 1.00 46.15  ? 347 HOH   A O   1 
HETATM 2261 O  O   . HOH   H 5 .   ? 10.738 5.586   3.379  1.00 25.47  ? 348 HOH   A O   1 
HETATM 2262 O  O   . HOH   H 5 .   ? 13.841 3.945   23.485 1.00 13.50  ? 349 HOH   A O   1 
HETATM 2263 O  O   . HOH   H 5 .   ? 16.989 -3.526  27.828 1.00 35.97  ? 350 HOH   A O   1 
HETATM 2264 O  O   . HOH   H 5 .   ? 31.659 19.903  11.721 1.00 22.14  ? 351 HOH   A O   1 
HETATM 2265 O  O   . HOH   H 5 .   ? 11.338 12.707  11.213 1.00 16.56  ? 352 HOH   A O   1 
HETATM 2266 O  O   . HOH   H 5 .   ? 36.538 17.787  14.299 1.00 35.80  ? 353 HOH   A O   1 
HETATM 2267 O  O   . HOH   H 5 .   ? 20.909 -4.165  14.066 1.00 18.64  ? 354 HOH   A O   1 
HETATM 2268 O  O   . HOH   H 5 .   ? 11.656 17.812  4.875  1.00 35.42  ? 355 HOH   A O   1 
HETATM 2269 O  O   . HOH   H 5 .   ? 28.938 3.314   12.609 1.00 15.71  ? 356 HOH   A O   1 
HETATM 2270 O  O   . HOH   H 5 .   ? 4.745  -5.470  14.369 1.00 45.19  ? 357 HOH   A O   1 
HETATM 2271 O  O   . HOH   H 5 .   ? 5.197  26.426  20.053 1.00 34.51  ? 358 HOH   A O   1 
HETATM 2272 O  O   . HOH   H 5 .   ? 2.092  14.305  16.918 1.00 33.83  ? 359 HOH   A O   1 
HETATM 2273 O  O   . HOH   H 5 .   ? 28.864 15.862  4.257  1.00 38.40  ? 360 HOH   A O   1 
HETATM 2274 O  O   . HOH   H 5 .   ? 20.617 -1.124  2.927  1.00 32.12  ? 361 HOH   A O   1 
HETATM 2275 O  O   . HOH   H 5 .   ? 32.314 1.967   6.015  1.00 38.88  ? 362 HOH   A O   1 
HETATM 2276 O  O   . HOH   H 5 .   ? 6.675  -6.946  23.749 1.00 27.46  ? 363 HOH   A O   1 
HETATM 2277 O  O   . HOH   H 5 .   ? 13.257 11.395  9.223  1.00 14.07  ? 364 HOH   A O   1 
HETATM 2278 O  O   . HOH   H 5 .   ? 12.362 11.139  29.674 1.00 19.17  ? 365 HOH   A O   1 
HETATM 2279 O  O   . HOH   H 5 .   ? 18.407 21.905  9.588  1.00 20.53  ? 366 HOH   A O   1 
HETATM 2280 O  O   . HOH   H 5 .   ? 7.131  26.462  14.429 1.00 40.92  ? 367 HOH   A O   1 
HETATM 2281 O  O   . HOH   H 5 .   ? 17.657 19.965  17.034 1.00 16.92  ? 368 HOH   A O   1 
HETATM 2282 O  O   . HOH   H 5 .   ? 9.738  3.953   33.540 1.00 15.57  ? 369 HOH   A O   1 
HETATM 2283 O  O   . HOH   H 5 .   ? 30.503 2.789   14.765 1.00 24.31  ? 370 HOH   A O   1 
HETATM 2284 O  O   . HOH   H 5 .   ? 20.799 -2.593  16.797 1.00 15.65  ? 371 HOH   A O   1 
HETATM 2285 O  O   . HOH   H 5 .   ? 24.105 -3.478  16.137 1.00 36.25  ? 372 HOH   A O   1 
HETATM 2286 O  O   . HOH   H 5 .   ? 19.158 16.989  26.370 1.00 40.50  ? 373 HOH   A O   1 
HETATM 2287 O  O   . HOH   H 5 .   ? 8.470  6.507   33.771 1.00 23.03  ? 374 HOH   A O   1 
HETATM 2288 O  O   . HOH   H 5 .   ? 19.455 2.818   19.317 1.00 19.13  ? 375 HOH   A O   1 
HETATM 2289 O  O   . HOH   H 5 .   ? 18.152 17.917  4.346  1.00 35.91  ? 376 HOH   A O   1 
HETATM 2290 O  O   . HOH   H 5 .   ? 7.415  20.136  17.719 1.00 24.53  ? 377 HOH   A O   1 
HETATM 2291 O  O   . HOH   H 5 .   ? 4.213  0.442   23.969 1.00 18.85  ? 378 HOH   A O   1 
HETATM 2292 O  O   . HOH   H 5 .   ? 22.851 -0.729  5.319  1.00 24.15  ? 379 HOH   A O   1 
HETATM 2293 O  O   . HOH   H 5 .   ? 1.620  11.633  27.477 1.00 49.70  ? 380 HOH   A O   1 
HETATM 2294 O  O   . HOH   H 5 .   ? 17.230 5.911   26.796 1.00 28.76  ? 381 HOH   A O   1 
HETATM 2295 O  O   . HOH   H 5 .   ? 17.959 10.537  26.159 1.00 24.23  ? 382 HOH   A O   1 
HETATM 2296 O  O   . HOH   H 5 .   ? 34.100 18.557  10.810 1.00 25.89  ? 383 HOH   A O   1 
HETATM 2297 O  O   . HOH   H 5 .   ? 11.665 -7.025  24.763 1.00 29.82  ? 384 HOH   A O   1 
HETATM 2298 O  O   . HOH   H 5 .   ? 3.900  -3.940  6.049  1.00 29.39  ? 385 HOH   A O   1 
HETATM 2299 O  O   . HOH   H 5 .   ? 15.278 15.118  3.491  1.00 31.63  ? 386 HOH   A O   1 
HETATM 2300 O  O   . HOH   H 5 .   ? 14.472 -2.478  17.913 1.00 18.23  ? 387 HOH   A O   1 
HETATM 2301 O  O   . HOH   H 5 .   ? 32.012 8.707   7.560  1.00 23.32  ? 388 HOH   A O   1 
HETATM 2302 O  O   . HOH   H 5 .   ? 30.385 4.569   5.676  1.00 25.23  ? 389 HOH   A O   1 
HETATM 2303 O  O   . HOH   H 5 .   ? 25.443 19.589  21.696 1.00 33.05  ? 390 HOH   A O   1 
HETATM 2304 O  O   . HOH   H 5 .   ? 25.235 17.711  4.472  1.00 40.97  ? 391 HOH   A O   1 
HETATM 2305 O  O   . HOH   H 5 .   ? 36.294 -0.385  12.348 1.00 37.02  ? 392 HOH   A O   1 
HETATM 2306 O  O   . HOH   H 5 .   ? 5.074  8.206   2.319  1.00 33.14  ? 393 HOH   A O   1 
HETATM 2307 O  O   . HOH   H 5 .   ? 8.486  -6.441  9.570  1.00 33.45  ? 394 HOH   A O   1 
HETATM 2308 O  O   . HOH   H 5 .   ? 2.431  16.057  19.501 1.00 41.73  ? 395 HOH   A O   1 
HETATM 2309 O  O   . HOH   H 5 .   ? 17.181 -5.452  12.150 1.00 41.46  ? 396 HOH   A O   1 
HETATM 2310 O  O   . HOH   H 5 .   ? 27.166 -1.362  15.802 1.00 25.82  ? 397 HOH   A O   1 
HETATM 2311 O  O   . HOH   H 5 .   ? 7.382  13.872  4.785  1.00 23.85  ? 398 HOH   A O   1 
HETATM 2312 O  O   . HOH   H 5 .   ? 28.054 17.533  24.214 1.00 24.48  ? 399 HOH   A O   1 
HETATM 2313 O  O   . HOH   H 5 .   ? 19.557 -0.608  33.354 1.00 39.79  ? 400 HOH   A O   1 
HETATM 2314 O  O   . HOH   H 5 .   ? 19.843 13.269  2.253  1.00 35.36  ? 401 HOH   A O   1 
HETATM 2315 O  O   . HOH   H 5 .   ? 6.300  24.019  10.786 1.00 45.26  ? 402 HOH   A O   1 
HETATM 2316 O  O   . HOH   H 5 .   ? 33.966 4.941   16.541 1.00 32.98  ? 403 HOH   A O   1 
HETATM 2317 O  O   . HOH   H 5 .   ? 30.931 15.570  22.870 1.00 30.12  ? 404 HOH   A O   1 
HETATM 2318 O  O   . HOH   H 5 .   ? 0.162  5.757   6.023  1.00 28.67  ? 405 HOH   A O   1 
HETATM 2319 O  O   . HOH   H 5 .   ? 35.845 15.124  10.971 1.00 39.90  ? 406 HOH   A O   1 
HETATM 2320 O  O   . HOH   H 5 .   ? 23.331 14.499  24.447 1.00 52.82  ? 407 HOH   A O   1 
HETATM 2321 O  O   . HOH   H 5 .   ? 3.428  7.664   24.337 1.00 32.65  ? 408 HOH   A O   1 
HETATM 2322 O  O   . HOH   H 5 .   ? 0.516  -1.257  16.721 1.00 18.29  ? 409 HOH   A O   1 
HETATM 2323 O  O   . HOH   H 5 .   ? 22.423 19.430  19.581 1.00 34.51  ? 410 HOH   A O   1 
HETATM 2324 O  O   . HOH   H 5 .   ? 6.036  14.627  20.687 1.00 56.36  ? 411 HOH   A O   1 
HETATM 2325 O  O   . HOH   H 5 .   ? 3.451  -0.274  21.428 1.00 21.29  ? 412 HOH   A O   1 
HETATM 2326 O  O   . HOH   H 5 .   ? 34.123 7.562   16.549 1.00 32.17  ? 413 HOH   A O   1 
HETATM 2327 O  O   . HOH   H 5 .   ? 17.583 0.661   20.174 1.00 19.90  ? 414 HOH   A O   1 
HETATM 2328 O  O   . HOH   H 5 .   ? 3.074  0.725   28.888 1.00 48.45  ? 415 HOH   A O   1 
HETATM 2329 O  O   . HOH   H 5 .   ? 9.178  3.536   2.998  1.00 30.24  ? 416 HOH   A O   1 
HETATM 2330 O  O   . HOH   H 5 .   ? 8.585  19.107  26.540 1.00 122.57 ? 417 HOH   A O   1 
HETATM 2331 O  O   . HOH   H 5 .   ? 15.222 21.753  8.323  1.00 33.61  ? 418 HOH   A O   1 
HETATM 2332 O  O   . HOH   H 5 .   ? 16.682 -4.005  2.781  1.00 29.31  ? 419 HOH   A O   1 
HETATM 2333 O  O   . HOH   H 5 .   ? 23.340 19.121  6.342  1.00 20.17  ? 420 HOH   A O   1 
HETATM 2334 O  O   . HOH   H 5 .   ? 16.651 21.096  19.256 1.00 28.22  ? 421 HOH   A O   1 
HETATM 2335 O  O   . HOH   H 5 .   ? 17.192 -2.358  19.566 1.00 20.10  ? 422 HOH   A O   1 
HETATM 2336 O  O   . HOH   H 5 .   ? 23.302 16.859  23.877 1.00 47.62  ? 423 HOH   A O   1 
HETATM 2337 O  O   . HOH   H 5 .   ? -2.693 23.366  9.063  1.00 55.02  ? 424 HOH   A O   1 
HETATM 2338 O  O   . HOH   H 5 .   ? 16.682 -9.317  5.513  1.00 54.61  ? 425 HOH   A O   1 
HETATM 2339 O  O   . HOH   H 5 .   ? 23.522 8.222   21.755 1.00 26.21  ? 426 HOH   A O   1 
HETATM 2340 O  O   . HOH   H 5 .   ? 1.109  -5.126  17.504 1.00 33.95  ? 427 HOH   A O   1 
HETATM 2341 O  O   . HOH   H 5 .   ? 22.825 3.264   20.790 1.00 24.35  ? 428 HOH   A O   1 
HETATM 2342 O  O   . HOH   H 5 .   ? 21.148 9.929   21.885 1.00 18.32  ? 429 HOH   A O   1 
HETATM 2343 O  O   . HOH   H 5 .   ? 19.527 9.369   -0.793 1.00 31.33  ? 430 HOH   A O   1 
HETATM 2344 O  O   . HOH   H 5 .   ? 13.896 -10.751 4.843  1.00 65.88  ? 431 HOH   A O   1 
HETATM 2345 O  O   . HOH   H 5 .   ? 8.579  -8.871  2.572  1.00 61.98  ? 432 HOH   A O   1 
HETATM 2346 O  O   . HOH   H 5 .   ? 34.049 11.787  -2.177 1.00 76.83  ? 433 HOH   A O   1 
HETATM 2347 O  O   . HOH   H 5 .   ? 1.111  3.583   26.123 1.00 35.62  ? 434 HOH   A O   1 
HETATM 2348 O  O   . HOH   H 5 .   ? 30.151 12.190  -0.671 1.00 78.40  ? 435 HOH   A O   1 
HETATM 2349 O  O   . HOH   H 5 .   ? 5.801  16.723  21.640 1.00 34.05  ? 436 HOH   A O   1 
HETATM 2350 O  O   . HOH   H 5 .   ? 8.490  11.443  31.572 1.00 38.43  ? 437 HOH   A O   1 
HETATM 2351 O  O   . HOH   H 5 .   ? 35.547 4.013   18.530 1.00 48.65  ? 438 HOH   A O   1 
HETATM 2352 O  O   . HOH   H 5 .   ? 5.594  17.705  24.143 1.00 48.60  ? 439 HOH   A O   1 
HETATM 2353 O  O   . HOH   H 5 .   ? 7.510  -4.799  2.835  1.00 38.87  ? 440 HOH   A O   1 
HETATM 2354 O  O   . HOH   H 5 .   ? 15.265 14.278  26.292 1.00 34.38  ? 441 HOH   A O   1 
HETATM 2355 O  O   . HOH   H 5 .   ? 31.857 7.151   5.388  1.00 36.65  ? 442 HOH   A O   1 
HETATM 2356 O  O   . HOH   H 5 .   ? 28.110 0.589   4.701  1.00 59.86  ? 443 HOH   A O   1 
HETATM 2357 O  O   . HOH   H 5 .   ? 19.267 -3.369  33.841 1.00 40.50  ? 444 HOH   A O   1 
HETATM 2358 O  O   . HOH   H 5 .   ? 38.702 1.133   13.438 1.00 58.29  ? 445 HOH   A O   1 
HETATM 2359 O  O   . HOH   H 5 .   ? 18.808 3.392   25.914 1.00 48.08  ? 446 HOH   A O   1 
HETATM 2360 O  O   . HOH   H 5 .   ? 6.617  -11.083 3.798  1.00 68.05  ? 447 HOH   A O   1 
HETATM 2361 O  O   . HOH   H 5 .   ? 14.896 13.182  28.781 1.00 44.53  ? 448 HOH   A O   1 
HETATM 2362 O  O   . HOH   H 5 .   ? 18.705 2.238   22.722 1.00 36.97  ? 449 HOH   A O   1 
HETATM 2363 O  O   . HOH   H 5 .   ? 2.099  -5.491  14.603 1.00 44.22  ? 450 HOH   A O   1 
HETATM 2364 O  O   . HOH   H 5 .   ? 2.763  -0.127  26.322 1.00 34.77  ? 451 HOH   A O   1 
HETATM 2365 O  O   . HOH   H 5 .   ? 16.788 -5.073  34.328 1.00 32.42  ? 452 HOH   A O   1 
HETATM 2366 O  O   . HOH   H 5 .   ? 13.600 24.559  10.615 1.00 52.60  ? 453 HOH   A O   1 
HETATM 2367 O  O   . HOH   H 5 .   ? 19.508 0.945   26.665 1.00 57.77  ? 454 HOH   A O   1 
HETATM 2368 O  O   . HOH   H 5 .   ? 2.263  11.995  2.794  1.00 52.81  ? 455 HOH   A O   1 
HETATM 2369 O  O   . HOH   H 5 .   ? 29.723 0.582   16.530 1.00 35.75  ? 456 HOH   A O   1 
HETATM 2370 O  O   . HOH   H 5 .   ? 23.804 1.004   19.751 1.00 32.94  ? 457 HOH   A O   1 
HETATM 2371 O  O   . HOH   H 5 .   ? 0.113  0.210   23.302 1.00 33.83  ? 458 HOH   A O   1 
HETATM 2372 O  O   . HOH   H 5 .   ? 17.773 24.326  10.503 1.00 37.49  ? 459 HOH   A O   1 
HETATM 2373 O  O   . HOH   H 5 .   ? 27.287 3.634   22.990 1.00 67.61  ? 460 HOH   A O   1 
HETATM 2374 O  O   . HOH   H 5 .   ? 11.933 24.322  14.783 1.00 40.06  ? 461 HOH   A O   1 
HETATM 2375 O  O   . HOH   H 5 .   ? 30.410 6.961   17.847 1.00 36.95  ? 462 HOH   A O   1 
HETATM 2376 O  O   . HOH   H 5 .   ? -2.191 20.285  23.811 1.00 55.11  ? 463 HOH   A O   1 
HETATM 2377 O  O   . HOH   H 5 .   ? 37.758 -4.488  6.809  1.00 32.60  ? 464 HOH   A O   1 
HETATM 2378 O  O   . HOH   H 5 .   ? 31.263 4.412   16.931 1.00 26.54  ? 465 HOH   A O   1 
HETATM 2379 O  O   . HOH   H 5 .   ? 17.984 -4.828  29.930 1.00 60.98  ? 466 HOH   A O   1 
HETATM 2380 O  O   . HOH   H 5 .   ? 21.438 -1.110  18.874 1.00 31.79  ? 467 HOH   A O   1 
HETATM 2381 O  O   . HOH   H 5 .   ? 12.450 -5.119  32.990 1.00 30.45  ? 468 HOH   A O   1 
HETATM 2382 O  O   . HOH   H 5 .   ? 2.426  -5.076  22.559 1.00 33.34  ? 469 HOH   A O   1 
HETATM 2383 O  O   . HOH   H 5 .   ? 23.361 -3.058  3.617  1.00 46.69  ? 470 HOH   A O   1 
HETATM 2384 O  O   . HOH   H 5 .   ? 29.730 13.580  3.407  1.00 55.01  ? 471 HOH   A O   1 
HETATM 2385 O  O   . HOH   H 5 .   ? 34.708 9.195   7.627  1.00 45.17  ? 472 HOH   A O   1 
HETATM 2386 O  O   . HOH   H 5 .   ? 1.291  -4.098  6.335  1.00 43.81  ? 473 HOH   A O   1 
HETATM 2387 O  O   . HOH   H 5 .   ? 8.101  16.885  26.214 1.00 45.55  ? 474 HOH   A O   1 
HETATM 2388 O  O   . HOH   H 5 .   ? 29.063 1.414   19.058 1.00 45.25  ? 475 HOH   A O   1 
HETATM 2389 O  O   . HOH   H 5 .   ? 4.148  -6.948  23.444 1.00 45.50  ? 476 HOH   A O   1 
HETATM 2390 O  O   . HOH   H 5 .   ? 5.954  -12.881 5.868  1.00 65.40  ? 477 HOH   A O   1 
HETATM 2391 O  O   . HOH   H 5 .   ? 0.946  -7.761  11.866 1.00 47.48  ? 478 HOH   A O   1 
HETATM 2392 O  O   . HOH   H 5 .   ? 1.559  19.242  25.618 1.00 67.78  ? 479 HOH   A O   1 
HETATM 2393 O  O   . HOH   H 5 .   ? 41.047 16.968  12.530 1.00 73.02  ? 480 HOH   A O   1 
HETATM 2394 O  O   . HOH   H 5 .   ? 36.406 5.817   26.370 1.00 60.96  ? 481 HOH   A O   1 
HETATM 2395 O  O   . HOH   I 5 .   ? 17.641 -33.306 24.092 1.00 41.84  ? 301 HOH   C O   1 
HETATM 2396 O  O   . HOH   I 5 .   ? 38.364 -7.376  7.128  1.00 23.20  ? 302 HOH   C O   1 
HETATM 2397 O  O   . HOH   I 5 .   ? 31.104 -23.826 -1.242 1.00 23.87  ? 303 HOH   C O   1 
HETATM 2398 O  O   . HOH   I 5 .   ? 19.785 -4.171  20.203 1.00 23.94  ? 304 HOH   C O   1 
HETATM 2399 O  O   . HOH   I 5 .   ? 38.973 -18.632 21.581 1.00 25.80  ? 305 HOH   C O   1 
HETATM 2400 O  O   . HOH   I 5 .   ? 7.763  -21.544 34.513 1.00 56.77  ? 306 HOH   C O   1 
HETATM 2401 O  O   . HOH   I 5 .   ? 26.829 -7.857  2.204  1.00 51.64  ? 307 HOH   C O   1 
HETATM 2402 O  O   . HOH   I 5 .   ? 20.765 -18.747 12.849 1.00 14.84  ? 308 HOH   C O   1 
HETATM 2403 O  O   . HOH   I 5 .   ? 37.355 -31.956 11.021 1.00 25.91  ? 309 HOH   C O   1 
HETATM 2404 O  O   . HOH   I 5 .   ? 30.795 -18.132 26.903 1.00 19.86  ? 310 HOH   C O   1 
HETATM 2405 O  O   . HOH   I 5 .   ? 17.918 -27.583 16.514 1.00 17.72  ? 311 HOH   C O   1 
HETATM 2406 O  O   . HOH   I 5 .   ? 18.778 -32.432 19.836 1.00 41.78  ? 312 HOH   C O   1 
HETATM 2407 O  O   . HOH   I 5 .   ? 9.974  -8.939  23.955 1.00 27.98  ? 313 HOH   C O   1 
HETATM 2408 O  O   . HOH   I 5 .   ? 14.744 -23.940 12.315 1.00 32.76  ? 314 HOH   C O   1 
HETATM 2409 O  O   . HOH   I 5 .   ? 13.344 -11.120 28.430 1.00 35.98  ? 315 HOH   C O   1 
HETATM 2410 O  O   . HOH   I 5 .   ? 18.589 -8.873  13.706 1.00 28.78  ? 316 HOH   C O   1 
HETATM 2411 O  O   . HOH   I 5 .   ? 10.287 -17.577 18.334 1.00 27.72  ? 317 HOH   C O   1 
HETATM 2412 O  O   . HOH   I 5 .   ? 22.948 -5.903  21.103 1.00 20.50  ? 318 HOH   C O   1 
HETATM 2413 O  O   . HOH   I 5 .   ? 24.643 -5.946  15.173 1.00 28.28  ? 319 HOH   C O   1 
HETATM 2414 O  O   . HOH   I 5 .   ? 40.135 -29.570 11.931 1.00 23.93  ? 320 HOH   C O   1 
HETATM 2415 O  O   . HOH   I 5 .   ? 36.329 -26.131 34.231 1.00 36.81  ? 321 HOH   C O   1 
HETATM 2416 O  O   . HOH   I 5 .   ? 22.027 -28.574 4.917  1.00 26.30  ? 322 HOH   C O   1 
HETATM 2417 O  O   . HOH   I 5 .   ? 36.430 -2.550  11.054 1.00 33.80  ? 323 HOH   C O   1 
HETATM 2418 O  O   . HOH   I 5 .   ? 13.918 -24.161 29.357 1.00 33.92  ? 324 HOH   C O   1 
HETATM 2419 O  O   . HOH   I 5 .   ? 14.983 -18.586 32.168 1.00 43.34  ? 325 HOH   C O   1 
HETATM 2420 O  O   . HOH   I 5 .   ? 37.153 -18.705 28.277 1.00 27.83  ? 326 HOH   C O   1 
HETATM 2421 O  O   . HOH   I 5 .   ? 40.603 -27.223 15.273 1.00 13.61  ? 327 HOH   C O   1 
HETATM 2422 O  O   . HOH   I 5 .   ? 26.581 -5.523  9.911  1.00 22.77  ? 328 HOH   C O   1 
HETATM 2423 O  O   . HOH   I 5 .   ? 6.803  -9.231  22.617 1.00 35.57  ? 329 HOH   C O   1 
HETATM 2424 O  O   . HOH   I 5 .   ? 9.210  -8.012  21.270 1.00 24.09  ? 330 HOH   C O   1 
HETATM 2425 O  O   . HOH   I 5 .   ? 16.879 -9.405  27.727 1.00 41.04  ? 331 HOH   C O   1 
HETATM 2426 O  O   . HOH   I 5 .   ? 23.904 -8.204  9.433  1.00 22.37  ? 332 HOH   C O   1 
HETATM 2427 O  O   . HOH   I 5 .   ? 10.478 -16.863 14.994 1.00 29.09  ? 333 HOH   C O   1 
HETATM 2428 O  O   . HOH   I 5 .   ? 30.981 -21.500 28.441 1.00 17.85  ? 334 HOH   C O   1 
HETATM 2429 O  O   . HOH   I 5 .   ? 32.495 -23.665 29.206 1.00 19.31  ? 335 HOH   C O   1 
HETATM 2430 O  O   . HOH   I 5 .   ? 29.947 -15.237 19.602 1.00 15.94  ? 336 HOH   C O   1 
HETATM 2431 O  O   . HOH   I 5 .   ? 21.812 -26.225 34.406 1.00 29.17  ? 337 HOH   C O   1 
HETATM 2432 O  O   . HOH   I 5 .   ? 16.806 -15.386 8.316  1.00 53.78  ? 338 HOH   C O   1 
HETATM 2433 O  O   . HOH   I 5 .   ? 11.959 -24.245 21.725 1.00 18.05  ? 339 HOH   C O   1 
HETATM 2434 O  O   . HOH   I 5 .   ? 20.802 -25.704 13.804 1.00 22.13  ? 340 HOH   C O   1 
HETATM 2435 O  O   . HOH   I 5 .   ? 24.759 -15.788 7.333  1.00 18.26  ? 341 HOH   C O   1 
HETATM 2436 O  O   . HOH   I 5 .   ? 36.053 -28.659 2.832  1.00 41.59  ? 342 HOH   C O   1 
HETATM 2437 O  O   . HOH   I 5 .   ? 26.053 -25.248 8.824  1.00 15.77  ? 343 HOH   C O   1 
HETATM 2438 O  O   . HOH   I 5 .   ? 35.195 -13.199 8.779  1.00 18.92  ? 344 HOH   C O   1 
HETATM 2439 O  O   . HOH   I 5 .   ? 23.619 -33.661 28.988 1.00 30.75  ? 345 HOH   C O   1 
HETATM 2440 O  O   . HOH   I 5 .   ? 31.115 -32.597 0.782  1.00 34.30  ? 346 HOH   C O   1 
HETATM 2441 O  O   . HOH   I 5 .   ? 29.808 -13.116 13.041 1.00 15.86  ? 347 HOH   C O   1 
HETATM 2442 O  O   . HOH   I 5 .   ? 19.226 -27.752 28.188 1.00 19.59  ? 348 HOH   C O   1 
HETATM 2443 O  O   . HOH   I 5 .   ? 10.625 -16.941 12.463 1.00 34.71  ? 349 HOH   C O   1 
HETATM 2444 O  O   . HOH   I 5 .   ? 29.716 -31.372 32.794 1.00 29.67  ? 350 HOH   C O   1 
HETATM 2445 O  O   . HOH   I 5 .   ? 19.093 -11.450 7.663  1.00 50.10  ? 351 HOH   C O   1 
HETATM 2446 O  O   . HOH   I 5 .   ? 22.965 -8.513  14.037 1.00 17.59  ? 352 HOH   C O   1 
HETATM 2447 O  O   . HOH   I 5 .   ? 4.314  -10.430 19.581 1.00 30.16  ? 353 HOH   C O   1 
HETATM 2448 O  O   . HOH   I 5 .   ? 25.842 -37.894 24.214 1.00 34.94  ? 354 HOH   C O   1 
HETATM 2449 O  O   . HOH   I 5 .   ? 30.824 -6.086  5.947  1.00 45.51  ? 355 HOH   C O   1 
HETATM 2450 O  O   . HOH   I 5 .   ? 4.646  -16.195 17.091 1.00 52.74  ? 356 HOH   C O   1 
HETATM 2451 O  O   . HOH   I 5 .   ? 11.442 -22.455 28.638 1.00 28.74  ? 357 HOH   C O   1 
HETATM 2452 O  O   . HOH   I 5 .   ? 32.097 -10.447 13.797 1.00 19.93  ? 358 HOH   C O   1 
HETATM 2453 O  O   . HOH   I 5 .   ? 23.211 -25.380 8.945  1.00 19.11  ? 359 HOH   C O   1 
HETATM 2454 O  O   . HOH   I 5 .   ? 32.976 -9.831  11.126 1.00 15.05  ? 360 HOH   C O   1 
HETATM 2455 O  O   . HOH   I 5 .   ? 37.910 -23.562 4.449  1.00 43.64  ? 361 HOH   C O   1 
HETATM 2456 O  O   . HOH   I 5 .   ? 30.058 -15.961 30.471 1.00 33.18  ? 362 HOH   C O   1 
HETATM 2457 O  O   . HOH   I 5 .   ? 23.924 -3.320  18.942 1.00 35.97  ? 363 HOH   C O   1 
HETATM 2458 O  O   . HOH   I 5 .   ? 22.289 -23.761 6.248  1.00 34.80  ? 364 HOH   C O   1 
HETATM 2459 O  O   . HOH   I 5 .   ? 37.690 -31.448 25.797 1.00 29.55  ? 365 HOH   C O   1 
HETATM 2460 O  O   . HOH   I 5 .   ? 28.123 -16.372 22.154 1.00 16.20  ? 366 HOH   C O   1 
HETATM 2461 O  O   . HOH   I 5 .   ? 27.077 -35.633 20.765 1.00 28.50  ? 367 HOH   C O   1 
HETATM 2462 O  O   . HOH   I 5 .   ? 20.165 -31.929 15.291 1.00 44.51  ? 368 HOH   C O   1 
HETATM 2463 O  O   . HOH   I 5 .   ? 31.270 -12.198 10.694 1.00 15.69  ? 369 HOH   C O   1 
HETATM 2464 O  O   . HOH   I 5 .   ? 33.097 -30.332 31.729 1.00 21.85  ? 370 HOH   C O   1 
HETATM 2465 O  O   . HOH   I 5 .   ? 14.843 -18.393 10.465 1.00 36.42  ? 371 HOH   C O   1 
HETATM 2466 O  O   . HOH   I 5 .   ? 10.093 -24.863 19.850 1.00 21.34  ? 372 HOH   C O   1 
HETATM 2467 O  O   . HOH   I 5 .   ? 13.181 -29.489 19.059 1.00 31.56  ? 373 HOH   C O   1 
HETATM 2468 O  O   . HOH   I 5 .   ? 32.272 -34.507 24.717 1.00 33.14  ? 374 HOH   C O   1 
HETATM 2469 O  O   . HOH   I 5 .   ? 22.973 -28.179 12.643 1.00 22.19  ? 375 HOH   C O   1 
HETATM 2470 O  O   . HOH   I 5 .   ? 22.413 -13.721 29.648 1.00 37.44  ? 376 HOH   C O   1 
HETATM 2471 O  O   . HOH   I 5 .   ? 43.231 -25.219 23.780 1.00 28.88  ? 377 HOH   C O   1 
HETATM 2472 O  O   . HOH   I 5 .   ? 35.616 -24.648 24.823 1.00 22.06  ? 378 HOH   C O   1 
HETATM 2473 O  O   . HOH   I 5 .   ? 4.801  -28.033 23.232 1.00 33.29  ? 379 HOH   C O   1 
HETATM 2474 O  O   . HOH   I 5 .   ? 26.463 -31.240 14.891 1.00 20.69  ? 380 HOH   C O   1 
HETATM 2475 O  O   . HOH   I 5 .   ? 34.357 -13.478 25.561 1.00 21.50  ? 381 HOH   C O   1 
HETATM 2476 O  O   . HOH   I 5 .   ? 27.102 -19.083 1.722  1.00 24.87  ? 382 HOH   C O   1 
HETATM 2477 O  O   . HOH   I 5 .   ? 3.870  -8.314  14.699 1.00 26.07  ? 383 HOH   C O   1 
HETATM 2478 O  O   . HOH   I 5 .   ? 8.840  -13.289 10.776 1.00 24.92  ? 384 HOH   C O   1 
HETATM 2479 O  O   . HOH   I 5 .   ? 37.484 -29.992 33.238 1.00 62.16  ? 385 HOH   C O   1 
HETATM 2480 O  O   . HOH   I 5 .   ? 21.764 -18.870 5.953  1.00 28.41  ? 386 HOH   C O   1 
HETATM 2481 O  O   . HOH   I 5 .   ? 26.054 -31.035 30.902 1.00 17.23  ? 387 HOH   C O   1 
HETATM 2482 O  O   . HOH   I 5 .   ? 11.020 -6.442  13.320 1.00 23.63  ? 388 HOH   C O   1 
HETATM 2483 O  O   . HOH   I 5 .   ? 36.300 -21.318 6.921  1.00 25.88  ? 389 HOH   C O   1 
HETATM 2484 O  O   . HOH   I 5 .   ? 30.343 -18.098 8.387  1.00 25.48  ? 390 HOH   C O   1 
HETATM 2485 O  O   . HOH   I 5 .   ? 10.833 -11.986 9.020  1.00 34.34  ? 391 HOH   C O   1 
HETATM 2486 O  O   . HOH   I 5 .   ? 35.015 -34.942 18.198 1.00 35.21  ? 392 HOH   C O   1 
HETATM 2487 O  O   . HOH   I 5 .   ? 35.757 -28.544 7.897  1.00 20.25  ? 393 HOH   C O   1 
HETATM 2488 O  O   . HOH   I 5 .   ? 37.081 -29.265 10.134 1.00 22.33  ? 394 HOH   C O   1 
HETATM 2489 O  O   . HOH   I 5 .   ? 30.105 -10.403 27.785 1.00 47.91  ? 395 HOH   C O   1 
HETATM 2490 O  O   . HOH   I 5 .   ? 34.546 -23.338 -0.766 1.00 37.12  ? 396 HOH   C O   1 
HETATM 2491 O  O   . HOH   I 5 .   ? 42.352 -16.958 3.153  1.00 52.32  ? 397 HOH   C O   1 
HETATM 2492 O  O   . HOH   I 5 .   ? 4.072  -12.737 17.415 1.00 45.17  ? 398 HOH   C O   1 
HETATM 2493 O  O   . HOH   I 5 .   ? 38.993 -12.957 25.773 1.00 29.82  ? 399 HOH   C O   1 
HETATM 2494 O  O   . HOH   I 5 .   ? 31.533 -13.535 4.299  1.00 33.05  ? 400 HOH   C O   1 
HETATM 2495 O  O   . HOH   I 5 .   ? 26.627 -12.003 27.609 1.00 27.58  ? 401 HOH   C O   1 
HETATM 2496 O  O   . HOH   I 5 .   ? 35.024 -4.113  17.685 1.00 29.52  ? 402 HOH   C O   1 
HETATM 2497 O  O   . HOH   I 5 .   ? 24.353 -13.837 5.510  1.00 38.82  ? 403 HOH   C O   1 
HETATM 2498 O  O   . HOH   I 5 .   ? 9.742  -18.457 26.707 1.00 33.21  ? 404 HOH   C O   1 
HETATM 2499 O  O   . HOH   I 5 .   ? 5.769  -16.889 22.273 1.00 50.84  ? 405 HOH   C O   1 
HETATM 2500 O  O   . HOH   I 5 .   ? 32.800 -14.385 9.438  1.00 16.16  ? 406 HOH   C O   1 
HETATM 2501 O  O   . HOH   I 5 .   ? 23.065 -33.437 5.427  1.00 34.14  ? 407 HOH   C O   1 
HETATM 2502 O  O   . HOH   I 5 .   ? 38.760 -16.097 3.876  1.00 46.92  ? 408 HOH   C O   1 
HETATM 2503 O  O   . HOH   I 5 .   ? 17.231 -25.381 12.828 1.00 27.44  ? 409 HOH   C O   1 
HETATM 2504 O  O   . HOH   I 5 .   ? 41.756 -12.473 18.014 1.00 27.57  ? 410 HOH   C O   1 
HETATM 2505 O  O   . HOH   I 5 .   ? 18.662 -8.264  25.531 1.00 21.76  ? 411 HOH   C O   1 
HETATM 2506 O  O   . HOH   I 5 .   ? 40.061 -29.875 14.640 1.00 17.77  ? 412 HOH   C O   1 
HETATM 2507 O  O   . HOH   I 5 .   ? 33.862 -36.027 8.913  1.00 36.82  ? 413 HOH   C O   1 
HETATM 2508 O  O   . HOH   I 5 .   ? 26.475 -6.068  22.266 1.00 33.28  ? 414 HOH   C O   1 
HETATM 2509 O  O   . HOH   I 5 .   ? 9.762  -24.781 29.232 1.00 45.73  ? 415 HOH   C O   1 
HETATM 2510 O  O   . HOH   I 5 .   ? 16.395 -20.552 11.581 1.00 26.62  ? 416 HOH   C O   1 
HETATM 2511 O  O   . HOH   I 5 .   ? 20.435 -32.219 22.237 1.00 34.14  ? 417 HOH   C O   1 
HETATM 2512 O  O   . HOH   I 5 .   ? 6.574  -22.895 18.329 1.00 33.70  ? 418 HOH   C O   1 
HETATM 2513 O  O   . HOH   I 5 .   ? 6.535  -20.093 18.229 1.00 33.23  ? 419 HOH   C O   1 
HETATM 2514 O  O   . HOH   I 5 .   ? 37.863 -20.548 4.722  1.00 36.19  ? 420 HOH   C O   1 
HETATM 2515 O  O   . HOH   I 5 .   ? 18.815 -19.084 10.908 1.00 19.87  ? 421 HOH   C O   1 
HETATM 2516 O  O   . HOH   I 5 .   ? 34.064 -15.602 27.269 1.00 37.60  ? 422 HOH   C O   1 
HETATM 2517 O  O   . HOH   I 5 .   ? 5.942  -12.369 23.346 1.00 47.30  ? 423 HOH   C O   1 
HETATM 2518 O  O   . HOH   I 5 .   ? 23.346 -17.592 33.348 1.00 20.24  ? 424 HOH   C O   1 
HETATM 2519 O  O   . HOH   I 5 .   ? 20.199 -19.675 36.083 1.00 34.64  ? 425 HOH   C O   1 
HETATM 2520 O  O   . HOH   I 5 .   ? 11.701 -21.643 36.593 1.00 64.27  ? 426 HOH   C O   1 
HETATM 2521 O  O   . HOH   I 5 .   ? 39.093 -21.329 31.801 1.00 51.88  ? 427 HOH   C O   1 
HETATM 2522 O  O   . HOH   I 5 .   ? 24.065 -35.082 20.526 1.00 70.22  ? 428 HOH   C O   1 
HETATM 2523 O  O   . HOH   I 5 .   ? 17.002 -31.555 28.797 1.00 52.73  ? 429 HOH   C O   1 
HETATM 2524 O  O   . HOH   I 5 .   ? 15.236 -18.137 38.141 1.00 43.37  ? 430 HOH   C O   1 
HETATM 2525 O  O   . HOH   I 5 .   ? 30.564 -4.424  17.008 1.00 46.19  ? 431 HOH   C O   1 
HETATM 2526 O  O   . HOH   I 5 .   ? 40.668 -11.128 24.697 1.00 62.06  ? 432 HOH   C O   1 
HETATM 2527 O  O   . HOH   I 5 .   ? 23.447 -31.060 13.233 1.00 33.21  ? 433 HOH   C O   1 
HETATM 2528 O  O   . HOH   I 5 .   ? 19.883 -29.128 3.238  1.00 64.66  ? 434 HOH   C O   1 
HETATM 2529 O  O   . HOH   I 5 .   ? 34.076 -31.890 29.608 1.00 30.57  ? 435 HOH   C O   1 
HETATM 2530 O  O   . HOH   I 5 .   ? 31.753 -15.724 6.890  1.00 34.78  ? 436 HOH   C O   1 
HETATM 2531 O  O   . HOH   I 5 .   ? 23.764 -15.665 31.511 1.00 31.99  ? 437 HOH   C O   1 
HETATM 2532 O  O   . HOH   I 5 .   ? 10.230 -19.951 28.900 1.00 39.73  ? 438 HOH   C O   1 
HETATM 2533 O  O   . HOH   I 5 .   ? 8.847  -19.268 16.938 1.00 33.19  ? 439 HOH   C O   1 
HETATM 2534 O  O   . HOH   I 5 .   ? 12.091 -18.944 10.779 1.00 56.82  ? 440 HOH   C O   1 
HETATM 2535 O  O   . HOH   I 5 .   ? 9.046  -12.776 26.070 1.00 59.86  ? 441 HOH   C O   1 
HETATM 2536 O  O   . HOH   I 5 .   ? 18.502 -30.318 -1.069 1.00 56.28  ? 442 HOH   C O   1 
HETATM 2537 O  O   . HOH   I 5 .   ? 21.502 -26.792 10.225 1.00 34.07  ? 443 HOH   C O   1 
HETATM 2538 O  O   . HOH   I 5 .   ? 21.090 -17.450 34.737 1.00 27.89  ? 444 HOH   C O   1 
HETATM 2539 O  O   . HOH   I 5 .   ? 33.757 -20.433 -2.273 1.00 38.99  ? 445 HOH   C O   1 
HETATM 2540 O  O   . HOH   I 5 .   ? 22.886 -16.692 5.386  1.00 38.71  ? 446 HOH   C O   1 
HETATM 2541 O  O   . HOH   I 5 .   ? 6.807  -18.700 26.447 1.00 51.39  ? 447 HOH   C O   1 
HETATM 2542 O  O   . HOH   I 5 .   ? 37.147 -29.166 5.687  1.00 43.32  ? 448 HOH   C O   1 
HETATM 2543 O  O   . HOH   I 5 .   ? 16.408 -27.536 14.129 1.00 35.34  ? 449 HOH   C O   1 
HETATM 2544 O  O   . HOH   I 5 .   ? 12.825 -25.869 11.859 1.00 57.32  ? 450 HOH   C O   1 
HETATM 2545 O  O   . HOH   I 5 .   ? 30.371 -13.088 31.146 1.00 49.67  ? 451 HOH   C O   1 
HETATM 2546 O  O   . HOH   I 5 .   ? 36.626 -14.334 28.650 1.00 55.80  ? 452 HOH   C O   1 
HETATM 2547 O  O   . HOH   I 5 .   ? 22.229 -3.030  20.727 1.00 52.32  ? 453 HOH   C O   1 
HETATM 2548 O  O   . HOH   I 5 .   ? 15.258 -16.346 33.449 1.00 53.65  ? 454 HOH   C O   1 
HETATM 2549 O  O   . HOH   I 5 .   ? 6.253  -12.678 10.606 1.00 44.52  ? 455 HOH   C O   1 
HETATM 2550 O  O   . HOH   I 5 .   ? 22.970 -8.650  7.165  1.00 47.78  ? 456 HOH   C O   1 
HETATM 2551 O  O   . HOH   I 5 .   ? 32.093 -32.115 33.099 1.00 34.27  ? 457 HOH   C O   1 
HETATM 2552 O  O   . HOH   I 5 .   ? 32.549 -19.384 29.260 1.00 32.88  ? 458 HOH   C O   1 
HETATM 2553 O  O   . HOH   I 5 .   ? 10.084 -21.334 16.411 1.00 34.92  ? 459 HOH   C O   1 
HETATM 2554 O  O   . HOH   I 5 .   ? 22.698 -11.841 6.104  1.00 37.85  ? 460 HOH   C O   1 
HETATM 2555 O  O   . HOH   I 5 .   ? 5.441  -10.372 9.491  1.00 59.56  ? 461 HOH   C O   1 
HETATM 2556 O  O   . HOH   I 5 .   ? 17.062 -28.917 28.873 1.00 41.36  ? 462 HOH   C O   1 
HETATM 2557 O  O   . HOH   I 5 .   ? 9.041  -23.548 17.711 1.00 30.22  ? 463 HOH   C O   1 
HETATM 2558 O  O   . HOH   I 5 .   ? 37.839 -11.170 27.340 1.00 63.50  ? 464 HOH   C O   1 
HETATM 2559 O  O   . HOH   I 5 .   ? 18.010 -16.588 38.901 1.00 54.76  ? 465 HOH   C O   1 
HETATM 2560 O  O   . HOH   I 5 .   ? 37.131 -22.943 -1.562 1.00 36.22  ? 466 HOH   C O   1 
HETATM 2561 O  O   . HOH   I 5 .   ? 35.194 -23.055 29.141 1.00 33.99  ? 467 HOH   C O   1 
HETATM 2562 O  O   . HOH   I 5 .   ? 39.260 -2.602  10.739 1.00 37.49  ? 468 HOH   C O   1 
HETATM 2563 O  O   . HOH   I 5 .   ? 19.372 -17.661 5.860  1.00 41.56  ? 469 HOH   C O   1 
HETATM 2564 O  O   . HOH   I 5 .   ? 21.356 -14.637 4.340  1.00 50.47  ? 470 HOH   C O   1 
HETATM 2565 O  O   . HOH   I 5 .   ? 34.353 -10.722 26.464 1.00 46.48  ? 471 HOH   C O   1 
HETATM 2566 O  O   . HOH   I 5 .   ? 3.268  -9.447  17.094 1.00 40.32  ? 472 HOH   C O   1 
HETATM 2567 O  O   . HOH   I 5 .   ? 12.804 -28.964 33.939 1.00 61.53  ? 473 HOH   C O   1 
HETATM 2568 O  O   . HOH   I 5 .   ? 19.409 -15.015 34.654 1.00 40.56  ? 474 HOH   C O   1 
HETATM 2569 O  O   . HOH   I 5 .   ? 41.459 -34.446 23.352 1.00 57.10  ? 475 HOH   C O   1 
HETATM 2570 O  O   . HOH   I 5 .   ? 10.378 -16.135 7.853  1.00 60.05  ? 476 HOH   C O   1 
HETATM 2571 O  O   . HOH   I 5 .   ? 1.977  -10.285 10.795 1.00 63.64  ? 477 HOH   C O   1 
HETATM 2572 O  O   . HOH   I 5 .   ? 36.764 -4.705  22.307 1.00 45.34  ? 478 HOH   C O   1 
HETATM 2573 O  O   . HOH   I 5 .   ? 30.685 -1.537  20.184 1.00 48.77  ? 479 HOH   C O   1 
HETATM 2574 O  O   . HOH   I 5 .   ? 39.234 -7.431  26.679 1.00 64.56  ? 480 HOH   C O   1 
HETATM 2575 O  O   . HOH   I 5 .   ? 5.453  -14.716 8.256  1.00 57.76  ? 481 HOH   C O   1 
HETATM 2576 O  O   . HOH   I 5 .   ? 2.074  -12.286 8.898  1.00 67.68  ? 482 HOH   C O   1 
HETATM 2577 O  O   . HOH   I 5 .   ? 40.818 -8.392  29.681 1.00 55.01  ? 483 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   ? 0.2161 0.2066 0.2017 -0.0130 0.0029  -0.0126 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2144 0.2061 0.2066 -0.0106 -0.0005 -0.0097 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2031 0.1972 0.2021 -0.0056 -0.0033 -0.0046 7   SER   A C   
4    O O   . SER   A 1   ? 0.2215 0.2165 0.2190 -0.0051 -0.0036 -0.0028 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2499 0.2449 0.2376 -0.0171 -0.0052 -0.0080 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2888 0.2881 0.2737 -0.0195 -0.0099 -0.0029 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1791 0.1739 0.1855 -0.0028 -0.0047 -0.0028 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1701 0.1663 0.1834 0.0010  -0.0058 0.0007  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1642 0.1598 0.1840 0.0042  -0.0040 -0.0001 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1867 0.1804 0.2060 0.0046  -0.0015 -0.0028 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1477 0.1445 0.1740 0.0060  -0.0046 0.0024  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1571 0.1538 0.1888 0.0077  -0.0026 0.0013  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1431 0.1396 0.1792 0.0092  -0.0004 0.0021  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1519 0.1481 0.1893 0.0094  -0.0009 0.0041  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1694 0.1680 0.2057 0.0067  -0.0048 0.0023  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1416 0.1381 0.1800 0.0094  0.0024  0.0005  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1338 0.1297 0.1762 0.0092  0.0059  -0.0003 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1397 0.1366 0.1905 0.0096  0.0064  -0.0002 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1452 0.1434 0.1960 0.0090  0.0055  -0.0008 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1396 0.1362 0.1777 0.0072  0.0089  -0.0022 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1622 0.1595 0.1938 0.0070  0.0080  -0.0015 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1522 0.1476 0.1927 0.0051  0.0136  -0.0043 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1845 0.1849 0.2134 0.0046  0.0093  -0.0013 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1450 0.1412 0.2043 0.0106  0.0085  0.0007  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1539 0.1517 0.2236 0.0112  0.0099  0.0010  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1631 0.1584 0.2368 0.0099  0.0172  -0.0028 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1630 0.1552 0.2423 0.0108  0.0206  -0.0026 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1597 0.1596 0.2393 0.0134  0.0065  0.0063  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1603 0.1635 0.2345 0.0124  -0.0003 0.0093  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1663 0.1730 0.2417 0.0112  -0.0027 0.0094  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1788 0.1815 0.2459 0.0117  -0.0037 0.0114  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1795 0.1885 0.2482 0.0088  -0.0079 0.0109  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1934 0.1988 0.2539 0.0092  -0.0087 0.0129  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2011 0.2094 0.2622 0.0075  -0.0106 0.0123  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2289 0.2390 0.2821 0.0036  -0.0146 0.0126  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1599 0.1559 0.2299 0.0070  0.0200  -0.0063 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1659 0.1600 0.2368 0.0036  0.0275  -0.0110 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1772 0.1734 0.2549 0.0024  0.0303  -0.0128 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1697 0.1689 0.2439 0.0019  0.0266  -0.0118 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1881 0.1826 0.2457 -0.0012 0.0283  -0.0132 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2022 0.2004 0.2531 -0.0019 0.0234  -0.0110 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2110 0.2042 0.2674 -0.0071 0.0363  -0.0185 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1847 0.1789 0.2737 0.0024  0.0373  -0.0155 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1830 0.1798 0.2804 0.0015  0.0406  -0.0173 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1828 0.1843 0.2860 0.0052  0.0334  -0.0121 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1792 0.1818 0.2880 0.0093  0.0284  -0.0070 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1611 0.1658 0.2608 0.0028  0.0321  -0.0131 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1512 0.1600 0.2538 0.0048  0.0254  -0.0089 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1556 0.1639 0.2442 0.0036  0.0194  -0.0077 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1700 0.1804 0.2570 0.0026  0.0162  -0.0067 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1715 0.1842 0.2832 0.0035  0.0281  -0.0101 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2241 0.2388 0.3548 0.0065  0.0325  -0.0091 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2505 0.2698 0.3922 0.0098  0.0278  -0.0035 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.2145 0.2260 0.3500 0.0049  0.0418  -0.0142 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1454 0.1507 0.2251 0.0038  0.0184  -0.0076 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1462 0.1507 0.2152 0.0034  0.0138  -0.0062 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1433 0.1466 0.2099 0.0061  0.0097  -0.0037 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1485 0.1507 0.2178 0.0075  0.0110  -0.0032 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1598 0.1633 0.2199 0.0002  0.0162  -0.0078 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1767 0.1819 0.2360 -0.0043 0.0198  -0.0099 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1845 0.1912 0.2442 -0.0053 0.0180  -0.0089 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1911 0.1964 0.2486 -0.0085 0.0256  -0.0133 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1930 0.2017 0.2519 -0.0101 0.0213  -0.0106 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2004 0.2078 0.2559 -0.0141 0.0293  -0.0155 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2144 0.2238 0.2703 -0.0148 0.0267  -0.0137 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2602 0.2720 0.3136 -0.0211 0.0303  -0.0157 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1325 0.1356 0.1937 0.0061  0.0056  -0.0025 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1371 0.1389 0.1934 0.0072  0.0025  -0.0011 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1417 0.1412 0.1901 0.0067  0.0029  -0.0020 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1540 0.1527 0.2013 0.0057  0.0028  -0.0024 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1441 0.1478 0.2016 0.0064  -0.0018 0.0006  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1572 0.1594 0.2069 0.0054  -0.0044 0.0008  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1692 0.1745 0.2192 0.0025  -0.0086 0.0026  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1941 0.1966 0.2350 -0.0006 -0.0090 0.0001  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2207 0.2226 0.2548 -0.0026 -0.0103 0.0000  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2180 0.2222 0.2533 -0.0016 -0.0122 0.0032  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2283 0.2268 0.2545 -0.0061 -0.0091 -0.0036 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1337 0.1321 0.1780 0.0074  0.0038  -0.0019 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1365 0.1341 0.1760 0.0073  0.0043  -0.0016 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1441 0.1399 0.1802 0.0083  0.0029  -0.0017 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1493 0.1452 0.1838 0.0087  0.0022  -0.0015 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1512 0.1505 0.1887 0.0063  0.0063  -0.0012 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1685 0.1691 0.2039 0.0062  0.0063  0.0010  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1503 0.1512 0.1900 0.0038  0.0089  -0.0024 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1419 0.1355 0.1770 0.0083  0.0031  -0.0024 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1469 0.1381 0.1781 0.0081  0.0033  -0.0039 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1724 0.1635 0.2037 0.0080  0.0033  -0.0039 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1608 0.1498 0.1931 0.0093  0.0062  -0.0039 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1681 0.1577 0.2047 0.0102  0.0071  -0.0017 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1328 0.1226 0.1622 0.0054  0.0018  -0.0057 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.2103 0.1999 0.2403 0.0053  0.0019  -0.0058 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1384 0.1318 0.1685 0.0042  -0.0017 -0.0041 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.2174 0.2052 0.2413 0.0028  0.0020  -0.0080 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.0979 0.0857 0.1301 0.0046  0.0027  -0.0065 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2296 0.2226 0.2628 0.0044  -0.0010 -0.0043 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1504 0.1372 0.1800 0.0092  0.0081  -0.0059 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1477 0.1319 0.1814 0.0109  0.0120  -0.0059 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1561 0.1356 0.1921 0.0098  0.0136  -0.0077 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1594 0.1367 0.1907 0.0064  0.0129  -0.0111 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1374 0.1193 0.1675 0.0100  0.0150  -0.0093 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1522 0.1383 0.1799 0.0107  0.0138  -0.0078 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1634 0.1508 0.1850 0.0087  0.0110  -0.0084 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1506 0.1393 0.1838 0.0134  0.0156  -0.0049 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1477 0.1260 0.1912 0.0120  0.0156  -0.0048 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1495 0.1223 0.1956 0.0107  0.0175  -0.0063 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.1766 0.1425 0.2194 0.0082  0.0221  -0.0126 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.2016 0.1640 0.2405 0.0043  0.0223  -0.0162 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1636 0.1360 0.2195 0.0136  0.0193  -0.0010 20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1820 0.1484 0.2416 0.0124  0.0213  -0.0015 20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.1940 0.1604 0.2653 0.0156  0.0230  0.0055  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.2058 0.1670 0.2815 0.0145  0.0243  0.0067  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.2410 0.1926 0.3217 0.0146  0.0303  0.0035  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2290 0.1753 0.3093 0.0148  0.0357  -0.0024 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2403 0.1871 0.3259 0.0136  0.0315  0.0056  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.1593 0.1240 0.2027 0.0092  0.0259  -0.0144 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.1959 0.1535 0.2357 0.0057  0.0319  -0.0214 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.2091 0.1679 0.2359 -0.0008 0.0290  -0.0260 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.2322 0.1854 0.2534 -0.0063 0.0335  -0.0324 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.2057 0.1614 0.2512 0.0083  0.0382  -0.0226 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.2030 0.1643 0.2427 0.0081  0.0360  -0.0224 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.2068 0.1754 0.2504 0.0122  0.0320  -0.0161 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.2250 0.1854 0.2550 0.0035  0.0378  -0.0279 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.2106 0.1820 0.2474 0.0106  0.0315  -0.0180 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.2287 0.1956 0.2574 0.0054  0.0347  -0.0246 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.2107 0.1766 0.2333 -0.0008 0.0219  -0.0224 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.2028 0.1719 0.2157 -0.0065 0.0177  -0.0240 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.2150 0.1874 0.2284 -0.0080 0.0124  -0.0215 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.2250 0.2018 0.2331 -0.0123 0.0079  -0.0208 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.1995 0.1739 0.2090 -0.0056 0.0144  -0.0214 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.2109 0.1830 0.2189 -0.0053 0.0196  -0.0242 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.2188 0.1964 0.2232 -0.0048 0.0157  -0.0211 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.2363 0.2034 0.2365 -0.0123 0.0246  -0.0313 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.1997 0.1707 0.2203 -0.0048 0.0129  -0.0195 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.2034 0.1778 0.2255 -0.0062 0.0088  -0.0176 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.2143 0.1876 0.2303 -0.0134 0.0083  -0.0212 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.2251 0.1917 0.2375 -0.0170 0.0133  -0.0264 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.1916 0.1642 0.2212 -0.0028 0.0102  -0.0154 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.2102 0.1904 0.2259 -0.0159 0.0026  -0.0185 24  THR   A N   
139  C CA  . THR   A 18  ? 0.2081 0.1900 0.2182 -0.0238 0.0006  -0.0205 24  THR   A CA  
140  C C   . THR   A 18  ? 0.2190 0.1989 0.2331 -0.0248 0.0015  -0.0212 24  THR   A C   
141  O O   . THR   A 18  ? 0.2008 0.1794 0.2222 -0.0193 0.0026  -0.0192 24  THR   A O   
142  C CB  . THR   A 18  ? 0.2340 0.2262 0.2445 -0.0259 -0.0067 -0.0152 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.2337 0.2303 0.2545 -0.0207 -0.0092 -0.0107 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2368 0.2313 0.2438 -0.0251 -0.0083 -0.0132 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.2154 0.1962 0.2241 -0.0330 0.0005  -0.0238 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.2256 0.2054 0.2379 -0.0347 0.0009  -0.0243 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.2128 0.2011 0.2345 -0.0300 -0.0041 -0.0181 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.2127 0.1990 0.2402 -0.0271 -0.0025 -0.0175 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.2680 0.2494 0.2722 -0.0456 -0.0003 -0.0275 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.3653 0.3488 0.3739 -0.0478 -0.0017 -0.0266 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.4210 0.3948 0.4312 -0.0474 0.0041  -0.0303 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.4078 0.4023 0.4213 -0.0496 -0.0080 -0.0217 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.4269 0.4057 0.4406 -0.0501 0.0011  -0.0284 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.4360 0.4278 0.4525 -0.0513 -0.0061 -0.0233 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.1879 0.1855 0.2120 -0.0295 -0.0095 -0.0134 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.1944 0.1992 0.2291 -0.0252 -0.0126 -0.0083 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.1931 0.1937 0.2328 -0.0176 -0.0090 -0.0081 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.1976 0.1998 0.2439 -0.0155 -0.0083 -0.0070 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.2194 0.2339 0.2583 -0.0253 -0.0182 -0.0027 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.3207 0.3421 0.3730 -0.0212 -0.0198 0.0019  26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.3497 0.3763 0.4073 -0.0241 -0.0214 0.0032  26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.3369 0.3581 0.3955 -0.0148 -0.0183 0.0039  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.1758 0.1713 0.2115 -0.0146 -0.0064 -0.0095 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1668 0.1595 0.2063 -0.0089 -0.0035 -0.0087 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1664 0.1541 0.2072 -0.0091 -0.0004 -0.0100 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1745 0.1639 0.2200 -0.0071 0.0002  -0.0081 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1827 0.1715 0.2181 -0.0063 -0.0014 -0.0096 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.2068 0.1999 0.2413 -0.0053 -0.0040 -0.0075 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1933 0.1915 0.2338 -0.0036 -0.0061 -0.0045 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.2080 0.1990 0.2367 -0.0064 -0.0034 -0.0090 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1687 0.1500 0.2055 -0.0121 0.0022  -0.0133 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1704 0.1460 0.2097 -0.0122 0.0054  -0.0137 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1771 0.1568 0.2194 -0.0151 0.0034  -0.0128 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.1854 0.1634 0.2313 -0.0142 0.0049  -0.0112 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.1798 0.1464 0.2152 -0.0153 0.0099  -0.0181 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.1775 0.1389 0.2137 -0.0113 0.0138  -0.0184 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.2039 0.1637 0.2354 -0.0121 0.0154  -0.0214 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.1964 0.1545 0.2397 -0.0064 0.0166  -0.0148 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.2023 0.1576 0.2383 -0.0075 0.0197  -0.0206 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.2014 0.1561 0.2453 -0.0039 0.0201  -0.0158 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.2122 0.1708 0.2616 -0.0046 0.0162  -0.0101 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.2093 0.1620 0.2615 0.0011  0.0228  -0.0115 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.2129 0.1697 0.2690 -0.0005 0.0183  -0.0055 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.2162 0.1701 0.2746 0.0025  0.0215  -0.0059 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1714 0.1572 0.2128 -0.0189 -0.0001 -0.0132 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.1841 0.1752 0.2298 -0.0217 -0.0020 -0.0122 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.1966 0.1945 0.2501 -0.0180 -0.0030 -0.0089 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.2027 0.2045 0.2610 -0.0196 -0.0032 -0.0082 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.1845 0.1812 0.2277 -0.0278 -0.0058 -0.0127 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1771 0.1760 0.2316 -0.0134 -0.0028 -0.0074 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1645 0.1684 0.2257 -0.0105 -0.0022 -0.0055 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1620 0.1619 0.2204 -0.0074 0.0006  -0.0052 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1628 0.1650 0.2230 -0.0050 0.0013  -0.0045 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.1762 0.1865 0.2424 -0.0090 -0.0048 -0.0034 30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.2008 0.2176 0.2718 -0.0125 -0.0082 -0.0019 30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2293 0.2510 0.3084 -0.0130 -0.0075 -0.0011 30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.2008 0.2184 0.2665 -0.0161 -0.0117 -0.0016 30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1549 0.1491 0.2097 -0.0079 0.0022  -0.0053 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1565 0.1481 0.2095 -0.0056 0.0039  -0.0036 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1769 0.1724 0.2316 -0.0064 0.0052  -0.0019 31  LEU   A C   
201  O O   . LEU   A 25  ? 0.1899 0.1868 0.2463 -0.0092 0.0059  -0.0018 31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1667 0.1515 0.2185 -0.0061 0.0054  -0.0029 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1768 0.1598 0.2292 -0.0036 0.0067  0.0005  31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1728 0.1556 0.2231 -0.0007 0.0066  -0.0004 31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.2055 0.1817 0.2606 -0.0036 0.0089  0.0023  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1719 0.1689 0.2250 -0.0049 0.0058  -0.0008 32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1687 0.1694 0.2210 -0.0074 0.0075  0.0005  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1657 0.1655 0.2156 -0.0078 0.0070  0.0050  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1847 0.1864 0.2340 -0.0114 0.0073  0.0080  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1702 0.1738 0.2226 -0.0068 0.0090  -0.0015 32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1864 0.1933 0.2355 -0.0111 0.0116  -0.0010 32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1728 0.1782 0.2312 -0.0062 0.0098  -0.0043 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1644 0.1620 0.2138 -0.0044 0.0062  0.0062  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1592 0.1573 0.2092 -0.0041 0.0057  0.0116  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1622 0.1563 0.2139 0.0003  0.0059  0.0114  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1528 0.1459 0.2023 0.0021  0.0060  0.0074  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1727 0.1773 0.2191 -0.0071 0.0056  0.0135  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1902 0.1982 0.2376 -0.0072 0.0042  0.0201  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.2152 0.2266 0.2648 -0.0100 0.0027  0.0273  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1855 0.1950 0.2327 -0.0047 0.0039  0.0209  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2154 0.2312 0.2674 -0.0093 0.0011  0.0333  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.1999 0.2146 0.2501 -0.0061 0.0020  0.0290  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1907 0.1983 0.2360 -0.0018 0.0047  0.0164  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.2046 0.2231 0.2563 -0.0045 0.0013  0.0321  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.2003 0.2108 0.2457 -0.0005 0.0042  0.0189  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.2090 0.2250 0.2579 -0.0017 0.0026  0.0264  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1706 0.1624 0.2271 0.0019  0.0064  0.0160  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1704 0.1586 0.2296 0.0059  0.0080  0.0155  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1874 0.1779 0.2541 0.0074  0.0081  0.0232  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.1950 0.1867 0.2659 0.0057  0.0072  0.0290  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.1878 0.1677 0.2479 0.0068  0.0106  0.0106  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.2119 0.1868 0.2763 0.0055  0.0119  0.0121  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.2490 0.2196 0.3231 0.0081  0.0147  0.0174  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2497 0.2184 0.3286 0.0069  0.0149  0.0217  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.2241 0.1935 0.3023 0.0114  0.0171  0.0177  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1780 0.1692 0.2473 0.0104  0.0091  0.0241  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1667 0.1615 0.2457 0.0124  0.0092  0.0325  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1714 0.1620 0.2560 0.0170  0.0132  0.0301  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1731 0.1662 0.2528 0.0174  0.0130  0.0268  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1914 0.1973 0.2671 0.0091  0.0053  0.0379  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2431 0.2556 0.3294 0.0100  0.0039  0.0486  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2834 0.2926 0.3801 0.0151  0.0069  0.0503  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2787 0.3004 0.3633 0.0051  0.0000  0.0555  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1761 0.1593 0.2706 0.0199  0.0175  0.0309  36  SER   A N   
245  C CA  . SER   A 30  ? 0.1855 0.1633 0.2863 0.0237  0.0232  0.0276  36  SER   A CA  
246  C C   . SER   A 30  ? 0.1900 0.1761 0.2986 0.0263  0.0225  0.0342  36  SER   A C   
247  O O   . SER   A 30  ? 0.1997 0.1851 0.3070 0.0279  0.0254  0.0296  36  SER   A O   
248  C CB  . SER   A 30  ? 0.2186 0.1863 0.3305 0.0257  0.0292  0.0276  36  SER   A CB  
249  O OG  . SER   A 30  ? 0.2761 0.2387 0.3962 0.0291  0.0362  0.0245  36  SER   A OG  
250  N N   . SER   A 31  ? 0.1856 0.1806 0.3018 0.0260  0.0185  0.0453  37  SER   A N   
251  C CA  . SER   A 31  ? 0.1840 0.1891 0.3084 0.0277  0.0170  0.0528  37  SER   A CA  
252  C C   . SER   A 31  ? 0.1815 0.1926 0.2929 0.0251  0.0143  0.0484  37  SER   A C   
253  O O   . SER   A 31  ? 0.1947 0.2115 0.3115 0.0269  0.0149  0.0511  37  SER   A O   
254  C CB  . SER   A 31  ? 0.2136 0.2291 0.3471 0.0260  0.0119  0.0667  37  SER   A CB  
255  O OG  . SER   A 31  ? 0.2759 0.2988 0.3959 0.0194  0.0058  0.0678  37  SER   A OG  
256  N N   . ARG   A 32  ? 0.1594 0.1691 0.2556 0.0211  0.0118  0.0418  38  ARG   A N   
257  C CA  . ARG   A 32  ? 0.1575 0.1713 0.2418 0.0185  0.0098  0.0373  38  ARG   A CA  
258  C C   . ARG   A 32  ? 0.1660 0.1714 0.2424 0.0197  0.0129  0.0268  38  ARG   A C   
259  O O   . ARG   A 32  ? 0.1648 0.1725 0.2327 0.0181  0.0117  0.0233  38  ARG   A O   
260  C CB  . ARG   A 32  ? 0.1649 0.1829 0.2390 0.0129  0.0057  0.0374  38  ARG   A CB  
261  C CG  . ARG   A 32  ? 0.1910 0.2195 0.2689 0.0090  0.0019  0.0476  38  ARG   A CG  
262  C CD  . ARG   A 32  ? 0.1808 0.2126 0.2474 0.0022  -0.0006 0.0460  38  ARG   A CD  
263  N NE  . ARG   A 32  ? 0.1563 0.1904 0.2131 -0.0006 -0.0005 0.0407  38  ARG   A NE  
264  C CZ  . ARG   A 32  ? 0.1740 0.2140 0.2221 -0.0078 -0.0018 0.0407  38  ARG   A CZ  
265  N NH1 . ARG   A 32  ? 0.1956 0.2414 0.2427 -0.0137 -0.0041 0.0462  38  ARG   A NH1 
266  N NH2 . ARG   A 32  ? 0.1617 0.2020 0.2021 -0.0100 -0.0006 0.0353  38  ARG   A NH2 
267  N N   . ASP   A 33  ? 0.1567 0.1528 0.2352 0.0214  0.0166  0.0221  39  ASP   A N   
268  C CA  . ASP   A 33  ? 0.1515 0.1410 0.2213 0.0206  0.0186  0.0131  39  ASP   A CA  
269  C C   . ASP   A 33  ? 0.1423 0.1332 0.2010 0.0173  0.0146  0.0100  39  ASP   A C   
270  O O   . ASP   A 33  ? 0.1530 0.1429 0.2043 0.0162  0.0142  0.0053  39  ASP   A O   
271  C CB  . ASP   A 33  ? 0.1533 0.1426 0.2225 0.0219  0.0217  0.0100  39  ASP   A CB  
272  C CG  . ASP   A 33  ? 0.1780 0.1609 0.2377 0.0196  0.0237  0.0014  39  ASP   A CG  
273  O OD1 . ASP   A 33  ? 0.1805 0.1568 0.2391 0.0182  0.0257  -0.0025 39  ASP   A OD1 
274  O OD2 . ASP   A 33  ? 0.1815 0.1664 0.2346 0.0185  0.0230  -0.0011 39  ASP   A OD2 
275  N N   . LEU   A 34  ? 0.1353 0.1285 0.1939 0.0155  0.0119  0.0129  40  LEU   A N   
276  C CA  . LEU   A 34  ? 0.1336 0.1281 0.1844 0.0127  0.0092  0.0100  40  LEU   A CA  
277  C C   . LEU   A 34  ? 0.1382 0.1290 0.1888 0.0112  0.0090  0.0080  40  LEU   A C   
278  O O   . LEU   A 34  ? 0.1479 0.1371 0.2036 0.0113  0.0097  0.0111  40  LEU   A O   
279  C CB  . LEU   A 34  ? 0.1487 0.1504 0.1977 0.0102  0.0070  0.0137  40  LEU   A CB  
280  C CG  . LEU   A 34  ? 0.1643 0.1707 0.2108 0.0099  0.0066  0.0145  40  LEU   A CG  
281  C CD1 . LEU   A 34  ? 0.1642 0.1774 0.2074 0.0054  0.0051  0.0174  40  LEU   A CD1 
282  C CD2 . LEU   A 34  ? 0.1653 0.1684 0.2061 0.0105  0.0071  0.0090  40  LEU   A CD2 
283  N N   . LEU   A 35  ? 0.1369 0.1270 0.1825 0.0097  0.0078  0.0039  41  LEU   A N   
284  C CA  . LEU   A 35  ? 0.1404 0.1288 0.1859 0.0077  0.0071  0.0022  41  LEU   A CA  
285  C C   . LEU   A 35  ? 0.1512 0.1431 0.1942 0.0064  0.0054  0.0007  41  LEU   A C   
286  O O   . LEU   A 35  ? 0.1457 0.1386 0.1864 0.0071  0.0047  -0.0006 41  LEU   A O   
287  C CB  . LEU   A 35  ? 0.1468 0.1294 0.1913 0.0071  0.0083  -0.0017 41  LEU   A CB  
288  C CG  . LEU   A 35  ? 0.1589 0.1404 0.2036 0.0044  0.0074  -0.0032 41  LEU   A CG  
289  C CD1 . LEU   A 35  ? 0.1751 0.1497 0.2202 0.0031  0.0102  -0.0057 41  LEU   A CD1 
290  C CD2 . LEU   A 35  ? 0.1672 0.1521 0.2090 0.0027  0.0047  -0.0053 41  LEU   A CD2 
291  N N   . VAL   A 36  ? 0.1427 0.1366 0.1873 0.0044  0.0051  0.0011  42  VAL   A N   
292  C CA  . VAL   A 36  ? 0.1349 0.1318 0.1802 0.0033  0.0050  -0.0004 42  VAL   A CA  
293  C C   . VAL   A 36  ? 0.1348 0.1315 0.1829 0.0020  0.0044  -0.0018 42  VAL   A C   
294  O O   . VAL   A 36  ? 0.1449 0.1406 0.1938 0.0004  0.0048  -0.0011 42  VAL   A O   
295  C CB  . VAL   A 36  ? 0.1423 0.1428 0.1869 0.0009  0.0067  0.0006  42  VAL   A CB  
296  C CG1 . VAL   A 36  ? 0.1583 0.1606 0.2055 -0.0002 0.0084  -0.0021 42  VAL   A CG1 
297  C CG2 . VAL   A 36  ? 0.1563 0.1583 0.1978 0.0012  0.0068  0.0024  42  VAL   A CG2 
298  N N   . SER   A 37  ? 0.1333 0.1315 0.1837 0.0023  0.0030  -0.0030 43  SER   A N   
299  C CA  . SER   A 37  ? 0.1391 0.1392 0.1936 0.0007  0.0019  -0.0035 43  SER   A CA  
300  C C   . SER   A 37  ? 0.1522 0.1566 0.2136 0.0011  0.0031  -0.0034 43  SER   A C   
301  O O   . SER   A 37  ? 0.1505 0.1552 0.2128 0.0025  0.0048  -0.0035 43  SER   A O   
302  C CB  . SER   A 37  ? 0.1548 0.1542 0.2074 -0.0002 -0.0010 -0.0038 43  SER   A CB  
303  O OG  . SER   A 37  ? 0.1628 0.1639 0.2150 0.0011  -0.0026 -0.0028 43  SER   A OG  
304  N N   . SER   A 38  ? 0.1678 0.1753 0.2353 -0.0004 0.0030  -0.0035 44  SER   A N   
305  C CA  . SER   A 38  ? 0.1714 0.1829 0.2485 0.0003  0.0053  -0.0035 44  SER   A CA  
306  C C   . SER   A 38  ? 0.1883 0.2037 0.2728 0.0020  0.0021  -0.0005 44  SER   A C   
307  O O   . SER   A 38  ? 0.2037 0.2202 0.2853 0.0006  -0.0025 0.0012  44  SER   A O   
308  C CB  . SER   A 38  ? 0.1891 0.2032 0.2707 -0.0023 0.0074  -0.0047 44  SER   A CB  
309  O OG  . SER   A 38  ? 0.2176 0.2334 0.2996 -0.0038 0.0036  -0.0035 44  SER   A OG  
310  N N   . THR   A 39  ? 0.1823 0.1996 0.2764 0.0043  0.0047  0.0004  45  THR   A N   
311  C CA  . THR   A 39  ? 0.1986 0.2202 0.3022 0.0062  0.0013  0.0052  45  THR   A CA  
312  C C   . THR   A 39  ? 0.2228 0.2497 0.3435 0.0074  0.0042  0.0068  45  THR   A C   
313  O O   . THR   A 39  ? 0.2198 0.2452 0.3444 0.0073  0.0108  0.0029  45  THR   A O   
314  C CB  . THR   A 39  ? 0.2116 0.2300 0.3143 0.0087  0.0020  0.0063  45  THR   A CB  
315  O OG1 . THR   A 39  ? 0.2260 0.2415 0.3336 0.0100  0.0091  0.0032  45  THR   A OG1 
316  C CG2 . THR   A 39  ? 0.2156 0.2295 0.3032 0.0078  -0.0002 0.0049  45  THR   A CG2 
317  N N   . THR   A 40  ? 0.2252 0.2591 0.3566 0.0081  -0.0005 0.0130  46  THR   A N   
318  C CA  . THR   A 40  ? 0.2450 0.2852 0.3964 0.0100  0.0021  0.0160  46  THR   A CA  
319  C C   . THR   A 40  ? 0.2450 0.2822 0.4080 0.0144  0.0075  0.0170  46  THR   A C   
320  O O   . THR   A 40  ? 0.2518 0.2883 0.4272 0.0159  0.0153  0.0142  46  THR   A O   
321  C CB  . THR   A 40  ? 0.2897 0.3401 0.4492 0.0085  -0.0058 0.0237  46  THR   A CB  
322  O OG1 . THR   A 40  ? 0.3369 0.3886 0.4939 0.0087  -0.0117 0.0295  46  THR   A OG1 
323  C CG2 . THR   A 40  ? 0.2992 0.3513 0.4469 0.0033  -0.0098 0.0216  46  THR   A CG2 
324  N N   . ALA   A 41  ? 0.2493 0.2840 0.4079 0.0158  0.0042  0.0203  47  ALA   A N   
325  C CA  . ALA   A 41  ? 0.2546 0.2852 0.4238 0.0196  0.0095  0.0213  47  ALA   A CA  
326  C C   . ALA   A 41  ? 0.2523 0.2732 0.4080 0.0187  0.0158  0.0134  47  ALA   A C   
327  O O   . ALA   A 41  ? 0.2517 0.2698 0.3891 0.0161  0.0129  0.0102  47  ALA   A O   
328  C CB  . ALA   A 41  ? 0.2704 0.3039 0.4428 0.0210  0.0026  0.0300  47  ALA   A CB  
329  N N   . GLN   A 42  ? 0.2343 0.2503 0.3999 0.0206  0.0244  0.0107  48  GLN   A N   
330  C CA  . GLN   A 42  ? 0.2422 0.2499 0.3953 0.0184  0.0306  0.0035  48  GLN   A CA  
331  C C   . GLN   A 42  ? 0.2318 0.2360 0.3775 0.0195  0.0268  0.0065  48  GLN   A C   
332  O O   . GLN   A 42  ? 0.2385 0.2441 0.3957 0.0228  0.0241  0.0134  48  GLN   A O   
333  C CB  . GLN   A 42  ? 0.2712 0.2742 0.4362 0.0184  0.0425  -0.0019 48  GLN   A CB  
334  C CG  . GLN   A 42  ? 0.3360 0.3412 0.5032 0.0153  0.0481  -0.0075 48  GLN   A CG  
335  C CD  . GLN   A 42  ? 0.4289 0.4289 0.6076 0.0142  0.0613  -0.0139 48  GLN   A CD  
336  O OE1 . GLN   A 42  ? 0.4392 0.4396 0.6404 0.0185  0.0661  -0.0110 48  GLN   A OE1 
337  N NE2 . GLN   A 42  ? 0.4511 0.4459 0.6150 0.0080  0.0677  -0.0224 48  GLN   A NE2 
338  N N   . GLY   A 43  ? 0.1994 0.1997 0.3268 0.0166  0.0266  0.0020  49  GLY   A N   
339  C CA  . GLY   A 43  ? 0.2025 0.1997 0.3208 0.0168  0.0235  0.0038  49  GLY   A CA  
340  C C   . GLY   A 43  ? 0.1990 0.1893 0.3187 0.0163  0.0313  0.0001  49  GLY   A C   
341  O O   . GLY   A 43  ? 0.2000 0.1873 0.3241 0.0143  0.0399  -0.0056 49  GLY   A O   
342  N N   . CYS   A 44  ? 0.1889 0.1766 0.3037 0.0170  0.0286  0.0028  50  CYS   A N   
343  C CA  . CYS   A 44  ? 0.1873 0.1680 0.3036 0.0163  0.0354  0.0002  50  CYS   A CA  
344  C C   . CYS   A 44  ? 0.1859 0.1637 0.2841 0.0119  0.0365  -0.0047 50  CYS   A C   
345  O O   . CYS   A 44  ? 0.1962 0.1681 0.2940 0.0100  0.0427  -0.0079 50  CYS   A O   
346  C CB  . CYS   A 44  ? 0.1997 0.1794 0.3268 0.0201  0.0325  0.0080  50  CYS   A CB  
347  S SG  . CYS   A 44  ? 0.2418 0.2250 0.3956 0.0252  0.0332  0.0151  50  CYS   A SG  
348  N N   . ASP   A 45  ? 0.1644 0.1465 0.2491 0.0103  0.0305  -0.0047 51  ASP   A N   
349  C CA  . ASP   A 45  ? 0.1672 0.1485 0.2372 0.0065  0.0309  -0.0079 51  ASP   A CA  
350  C C   . ASP   A 45  ? 0.1970 0.1777 0.2622 0.0009  0.0376  -0.0143 51  ASP   A C   
351  O O   . ASP   A 45  ? 0.2130 0.1956 0.2822 0.0002  0.0395  -0.0162 51  ASP   A O   
352  C CB  . ASP   A 45  ? 0.1576 0.1437 0.2179 0.0070  0.0232  -0.0053 51  ASP   A CB  
353  C CG  . ASP   A 45  ? 0.1808 0.1678 0.2419 0.0102  0.0171  0.0000  51  ASP   A CG  
354  O OD1 . ASP   A 45  ? 0.1864 0.1703 0.2496 0.0108  0.0179  0.0018  51  ASP   A OD1 
355  O OD2 . ASP   A 45  ? 0.1840 0.1745 0.2425 0.0111  0.0117  0.0021  51  ASP   A OD2 
356  N N   . THR   A 46  ? 0.2111 0.1898 0.2674 -0.0038 0.0411  -0.0176 52  THR   A N   
357  C CA  . THR   A 46  ? 0.2334 0.2130 0.2817 -0.0114 0.0465  -0.0232 52  THR   A CA  
358  C C   . THR   A 46  ? 0.2150 0.2004 0.2497 -0.0146 0.0411  -0.0212 52  THR   A C   
359  O O   . THR   A 46  ? 0.2228 0.2085 0.2543 -0.0125 0.0371  -0.0182 52  THR   A O   
360  C CB  . THR   A 46  ? 0.2923 0.2654 0.3417 -0.0161 0.0561  -0.0289 52  THR   A CB  
361  O OG1 . THR   A 46  ? 0.3455 0.3162 0.3908 -0.0156 0.0545  -0.0271 52  THR   A OG1 
362  C CG2 . THR   A 46  ? 0.3083 0.2755 0.3746 -0.0123 0.0627  -0.0304 52  THR   A CG2 
363  N N   . ILE   A 47  ? 0.1977 0.1883 0.2261 -0.0196 0.0407  -0.0220 53  ILE   A N   
364  C CA  . ILE   A 47  ? 0.1882 0.1854 0.2069 -0.0223 0.0355  -0.0185 53  ILE   A CA  
365  C C   . ILE   A 47  ? 0.2009 0.1998 0.2101 -0.0313 0.0394  -0.0213 53  ILE   A C   
366  O O   . ILE   A 47  ? 0.2092 0.2066 0.2155 -0.0387 0.0463  -0.0268 53  ILE   A O   
367  C CB  . ILE   A 47  ? 0.1894 0.1923 0.2069 -0.0235 0.0322  -0.0160 53  ILE   A CB  
368  C CG1 . ILE   A 47  ? 0.1997 0.2005 0.2260 -0.0162 0.0294  -0.0144 53  ILE   A CG1 
369  C CG2 . ILE   A 47  ? 0.1822 0.1923 0.1934 -0.0250 0.0264  -0.0105 53  ILE   A CG2 
370  C CD1 . ILE   A 47  ? 0.2186 0.2186 0.2473 -0.0091 0.0236  -0.0103 53  ILE   A CD1 
371  N N   . ALA   A 48  ? 0.1781 0.1809 0.1821 -0.0316 0.0353  -0.0178 54  ALA   A N   
372  C CA  . ALA   A 48  ? 0.1791 0.1858 0.1732 -0.0408 0.0375  -0.0191 54  ALA   A CA  
373  C C   . ALA   A 48  ? 0.2038 0.2197 0.1913 -0.0487 0.0357  -0.0170 54  ALA   A C   
374  O O   . ALA   A 48  ? 0.1982 0.2193 0.1884 -0.0452 0.0299  -0.0112 54  ALA   A O   
375  C CB  . ALA   A 48  ? 0.1904 0.2006 0.1824 -0.0383 0.0326  -0.0146 54  ALA   A CB  
376  N N   . ARG   A 49  ? 0.2269 0.2447 0.2051 -0.0606 0.0410  -0.0213 55  ARG   A N   
377  C CA  . ARG   A 49  ? 0.2375 0.2658 0.2075 -0.0705 0.0388  -0.0182 55  ARG   A CA  
378  C C   . ARG   A 49  ? 0.2689 0.3037 0.2287 -0.0804 0.0388  -0.0176 55  ARG   A C   
379  O O   . ARG   A 49  ? 0.2864 0.3179 0.2381 -0.0906 0.0464  -0.0250 55  ARG   A O   
380  C CB  . ARG   A 49  ? 0.2479 0.2731 0.2152 -0.0775 0.0459  -0.0249 55  ARG   A CB  
381  C CG  . ARG   A 49  ? 0.2559 0.2748 0.2345 -0.0678 0.0465  -0.0259 55  ARG   A CG  
382  C CD  . ARG   A 49  ? 0.2345 0.2594 0.2178 -0.0612 0.0376  -0.0174 55  ARG   A CD  
383  N NE  . ARG   A 49  ? 0.2110 0.2298 0.2041 -0.0532 0.0386  -0.0191 55  ARG   A NE  
384  C CZ  . ARG   A 49  ? 0.2294 0.2495 0.2289 -0.0452 0.0322  -0.0134 55  ARG   A CZ  
385  N NH1 . ARG   A 49  ? 0.2237 0.2502 0.2221 -0.0436 0.0253  -0.0059 55  ARG   A NH1 
386  N NH2 . ARG   A 49  ? 0.2374 0.2526 0.2452 -0.0391 0.0333  -0.0153 55  ARG   A NH2 
387  N N   . CYS   A 50  ? 0.2644 0.3079 0.2255 -0.0775 0.0309  -0.0090 56  CYS   A N   
388  C CA  . CYS   A 50  ? 0.2752 0.3254 0.2293 -0.0846 0.0298  -0.0072 56  CYS   A CA  
389  C C   . CYS   A 50  ? 0.2794 0.3420 0.2384 -0.0809 0.0206  0.0042  56  CYS   A C   
390  O O   . CYS   A 50  ? 0.2932 0.3572 0.2613 -0.0721 0.0159  0.0099  56  CYS   A O   
391  C CB  . CYS   A 50  ? 0.2740 0.3131 0.2303 -0.0793 0.0344  -0.0131 56  CYS   A CB  
392  S SG  . CYS   A 50  ? 0.2631 0.2980 0.2324 -0.0622 0.0288  -0.0082 56  CYS   A SG  
393  N N   . ASP   A 51  ? 0.3007 0.3717 0.2548 -0.0871 0.0186  0.0074  57  ASP   A N   
394  C CA  . ASP   A 51  ? 0.3158 0.3985 0.2775 -0.0827 0.0108  0.0182  57  ASP   A CA  
395  C C   . ASP   A 51  ? 0.3012 0.3804 0.2651 -0.0775 0.0116  0.0165  57  ASP   A C   
396  O O   . ASP   A 51  ? 0.3107 0.4011 0.2775 -0.0786 0.0072  0.0237  57  ASP   A O   
397  C CB  . ASP   A 51  ? 0.3870 0.4876 0.3436 -0.0953 0.0058  0.0269  57  ASP   A CB  
398  C CG  . ASP   A 51  ? 0.5073 0.6123 0.4501 -0.1098 0.0090  0.0227  57  ASP   A CG  
399  O OD1 . ASP   A 51  ? 0.5289 0.6209 0.4659 -0.1104 0.0164  0.0118  57  ASP   A OD1 
400  O OD2 . ASP   A 51  ? 0.5555 0.6769 0.4937 -0.1211 0.0041  0.0306  57  ASP   A OD2 
401  N N   . CYS   A 52  ? 0.2630 0.3274 0.2274 -0.0713 0.0169  0.0082  58  CYS   A N   
402  C CA  . CYS   A 52  ? 0.2331 0.2934 0.1997 -0.0659 0.0175  0.0070  58  CYS   A CA  
403  C C   . CYS   A 52  ? 0.2376 0.3046 0.2147 -0.0569 0.0117  0.0150  58  CYS   A C   
404  O O   . CYS   A 52  ? 0.2369 0.3042 0.2220 -0.0499 0.0090  0.0186  58  CYS   A O   
405  C CB  . CYS   A 52  ? 0.2346 0.2786 0.2028 -0.0593 0.0227  -0.0007 58  CYS   A CB  
406  S SG  . CYS   A 52  ? 0.2625 0.2957 0.2217 -0.0686 0.0321  -0.0112 58  CYS   A SG  
407  N N   . GLN   A 53  ? 0.2138 0.2855 0.1912 -0.0572 0.0107  0.0170  59  GLN   A N   
408  C CA  . GLN   A 53  ? 0.2015 0.2779 0.1893 -0.0486 0.0073  0.0227  59  GLN   A CA  
409  C C   . GLN   A 53  ? 0.1841 0.2518 0.1711 -0.0438 0.0100  0.0180  59  GLN   A C   
410  O O   . GLN   A 53  ? 0.1924 0.2644 0.1858 -0.0391 0.0086  0.0214  59  GLN   A O   
411  C CB  . GLN   A 53  ? 0.2375 0.3313 0.2298 -0.0532 0.0028  0.0321  59  GLN   A CB  
412  C CG  . GLN   A 53  ? 0.2817 0.3856 0.2795 -0.0552 -0.0014 0.0401  59  GLN   A CG  
413  C CD  . GLN   A 53  ? 0.3378 0.4599 0.3445 -0.0578 -0.0064 0.0516  59  GLN   A CD  
414  O OE1 . GLN   A 53  ? 0.3688 0.5037 0.3706 -0.0689 -0.0096 0.0569  59  GLN   A OE1 
415  N NE2 . GLN   A 53  ? 0.2831 0.4074 0.3037 -0.0482 -0.0071 0.0558  59  GLN   A NE2 
416  N N   . THR   A 54  ? 0.1755 0.2310 0.1554 -0.0453 0.0144  0.0104  60  THR   A N   
417  C CA  . THR   A 54  ? 0.1830 0.2292 0.1625 -0.0405 0.0165  0.0068  60  THR   A CA  
418  C C   . THR   A 54  ? 0.1777 0.2105 0.1578 -0.0360 0.0191  0.0019  60  THR   A C   
419  O O   . THR   A 54  ? 0.1889 0.2180 0.1667 -0.0395 0.0216  -0.0011 60  THR   A O   
420  C CB  . THR   A 54  ? 0.2293 0.2751 0.2013 -0.0476 0.0192  0.0044  60  THR   A CB  
421  O OG1 . THR   A 54  ? 0.3001 0.3399 0.2648 -0.0551 0.0236  -0.0010 60  THR   A OG1 
422  C CG2 . THR   A 54  ? 0.2102 0.2707 0.1821 -0.0529 0.0164  0.0097  60  THR   A CG2 
423  N N   . GLY   A 55  ? 0.1615 0.1881 0.1451 -0.0287 0.0185  0.0017  61  GLY   A N   
424  C CA  . GLY   A 55  ? 0.1607 0.1766 0.1467 -0.0242 0.0199  -0.0012 61  GLY   A CA  
425  C C   . GLY   A 55  ? 0.1504 0.1619 0.1382 -0.0186 0.0185  -0.0005 61  GLY   A C   
426  O O   . GLY   A 55  ? 0.1633 0.1780 0.1490 -0.0193 0.0179  0.0007  61  GLY   A O   
427  N N   . VAL   A 56  ? 0.1417 0.1466 0.1332 -0.0138 0.0178  -0.0010 62  VAL   A N   
428  C CA  . VAL   A 56  ? 0.1385 0.1397 0.1306 -0.0101 0.0160  0.0001  62  VAL   A CA  
429  C C   . VAL   A 56  ? 0.1385 0.1395 0.1347 -0.0055 0.0135  0.0009  62  VAL   A C   
430  O O   . VAL   A 56  ? 0.1522 0.1515 0.1518 -0.0045 0.0138  0.0002  62  VAL   A O   
431  C CB  . VAL   A 56  ? 0.1654 0.1580 0.1579 -0.0108 0.0179  -0.0004 62  VAL   A CB  
432  C CG1 . VAL   A 56  ? 0.1907 0.1803 0.1839 -0.0079 0.0150  0.0022  62  VAL   A CG1 
433  C CG2 . VAL   A 56  ? 0.1760 0.1675 0.1639 -0.0161 0.0212  -0.0018 62  VAL   A CG2 
434  N N   . TYR   A 57  ? 0.1307 0.1335 0.1262 -0.0034 0.0118  0.0017  63  TYR   A N   
435  C CA  . TYR   A 57  ? 0.1345 0.1363 0.1329 -0.0002 0.0100  0.0016  63  TYR   A CA  
436  C C   . TYR   A 57  ? 0.1441 0.1426 0.1398 -0.0002 0.0082  0.0022  63  TYR   A C   
437  O O   . TYR   A 57  ? 0.1542 0.1527 0.1455 -0.0022 0.0084  0.0027  63  TYR   A O   
438  C CB  . TYR   A 57  ? 0.1350 0.1418 0.1361 0.0014  0.0105  0.0015  63  TYR   A CB  
439  C CG  . TYR   A 57  ? 0.1329 0.1415 0.1322 0.0014  0.0117  0.0008  63  TYR   A CG  
440  C CD1 . TYR   A 57  ? 0.1419 0.1546 0.1397 -0.0004 0.0132  0.0014  63  TYR   A CD1 
441  C CD2 . TYR   A 57  ? 0.1423 0.1487 0.1413 0.0025  0.0120  -0.0010 63  TYR   A CD2 
442  C CE1 . TYR   A 57  ? 0.1543 0.1689 0.1514 -0.0005 0.0152  0.0003  63  TYR   A CE1 
443  C CE2 . TYR   A 57  ? 0.1478 0.1554 0.1452 0.0017  0.0146  -0.0028 63  TYR   A CE2 
444  C CZ  . TYR   A 57  ? 0.1609 0.1727 0.1579 0.0005  0.0164  -0.0021 63  TYR   A CZ  
445  O OH  . TYR   A 57  ? 0.1894 0.2025 0.1853 -0.0005 0.0198  -0.0044 63  TYR   A OH  
446  N N   . TYR   A 58  ? 0.1418 0.1385 0.1396 0.0013  0.0062  0.0025  64  TYR   A N   
447  C CA  . TYR   A 58  ? 0.1464 0.1417 0.1409 -0.0002 0.0036  0.0038  64  TYR   A CA  
448  C C   . TYR   A 58  ? 0.1458 0.1429 0.1364 -0.0012 0.0045  0.0012  64  TYR   A C   
449  O O   . TYR   A 58  ? 0.1568 0.1543 0.1507 0.0006  0.0056  -0.0008 64  TYR   A O   
450  C CB  . TYR   A 58  ? 0.1505 0.1441 0.1496 0.0007  0.0007  0.0062  64  TYR   A CB  
451  C CG  . TYR   A 58  ? 0.1585 0.1526 0.1538 -0.0023 -0.0030 0.0092  64  TYR   A CG  
452  C CD1 . TYR   A 58  ? 0.1648 0.1583 0.1572 -0.0047 -0.0044 0.0126  64  TYR   A CD1 
453  C CD2 . TYR   A 58  ? 0.1756 0.1713 0.1695 -0.0038 -0.0052 0.0088  64  TYR   A CD2 
454  C CE1 . TYR   A 58  ? 0.1919 0.1872 0.1795 -0.0088 -0.0084 0.0162  64  TYR   A CE1 
455  C CE2 . TYR   A 58  ? 0.1793 0.1768 0.1679 -0.0085 -0.0090 0.0118  64  TYR   A CE2 
456  C CZ  . TYR   A 58  ? 0.2045 0.2023 0.1901 -0.0111 -0.0109 0.0159  64  TYR   A CZ  
457  O OH  . TYR   A 58  ? 0.2338 0.2348 0.2135 -0.0170 -0.0154 0.0200  64  TYR   A OH  
458  N N   . CYS   A 59  ? 0.1455 0.1431 0.1295 -0.0046 0.0046  0.0010  65  CYS   A N   
459  C CA  . CYS   A 59  ? 0.1568 0.1552 0.1363 -0.0069 0.0070  -0.0027 65  CYS   A CA  
460  C C   . CYS   A 59  ? 0.1773 0.1752 0.1499 -0.0120 0.0038  -0.0017 65  CYS   A C   
461  O O   . CYS   A 59  ? 0.1847 0.1832 0.1513 -0.0159 0.0019  0.0009  65  CYS   A O   
462  C CB  . CYS   A 59  ? 0.1717 0.1722 0.1484 -0.0082 0.0105  -0.0043 65  CYS   A CB  
463  S SG  . CYS   A 59  ? 0.1852 0.1860 0.1572 -0.0117 0.0158  -0.0100 65  CYS   A SG  
464  N N   . SER   A 60  ? 0.1643 0.1615 0.1372 -0.0128 0.0028  -0.0031 66  SER   A N   
465  C CA  . SER   A 60  ? 0.1837 0.1821 0.1498 -0.0190 -0.0011 -0.0011 66  SER   A CA  
466  C C   . SER   A 60  ? 0.1941 0.1933 0.1490 -0.0262 0.0012  -0.0044 66  SER   A C   
467  O O   . SER   A 60  ? 0.2166 0.2183 0.1643 -0.0325 -0.0030 -0.0006 66  SER   A O   
468  C CB  . SER   A 60  ? 0.2039 0.2019 0.1721 -0.0194 -0.0024 -0.0023 66  SER   A CB  
469  O OG  . SER   A 60  ? 0.2395 0.2352 0.2056 -0.0205 0.0032  -0.0092 66  SER   A OG  
470  N N   . SER   A 61  ? 0.1812 0.1789 0.1356 -0.0255 0.0083  -0.0109 67  SER   A N   
471  C CA  . SER   A 61  ? 0.1901 0.1881 0.1347 -0.0324 0.0126  -0.0155 67  SER   A CA  
472  C C   . SER   A 61  ? 0.1965 0.1967 0.1362 -0.0347 0.0115  -0.0125 67  SER   A C   
473  O O   . SER   A 61  ? 0.2160 0.2171 0.1466 -0.0414 0.0148  -0.0160 67  SER   A O   
474  C CB  . SER   A 61  ? 0.2059 0.2014 0.1545 -0.0305 0.0216  -0.0232 67  SER   A CB  
475  O OG  . SER   A 61  ? 0.2234 0.2198 0.1821 -0.0232 0.0243  -0.0224 67  SER   A OG  
476  N N   . ARG   A 62  ? 0.1892 0.1900 0.1347 -0.0299 0.0073  -0.0064 68  ARG   A N   
477  C CA  . ARG   A 62  ? 0.1981 0.2002 0.1394 -0.0323 0.0055  -0.0025 68  ARG   A CA  
478  C C   . ARG   A 62  ? 0.2160 0.2180 0.1597 -0.0319 -0.0018 0.0060  68  ARG   A C   
479  O O   . ARG   A 62  ? 0.2159 0.2180 0.1575 -0.0335 -0.0035 0.0103  68  ARG   A O   
480  C CB  . ARG   A 62  ? 0.2077 0.2100 0.1551 -0.0270 0.0096  -0.0040 68  ARG   A CB  
481  C CG  . ARG   A 62  ? 0.2240 0.2276 0.1723 -0.0269 0.0172  -0.0109 68  ARG   A CG  
482  C CD  . ARG   A 62  ? 0.2184 0.2235 0.1564 -0.0341 0.0200  -0.0132 68  ARG   A CD  
483  N NE  . ARG   A 62  ? 0.2453 0.2515 0.1862 -0.0339 0.0285  -0.0201 68  ARG   A NE  
484  C CZ  . ARG   A 62  ? 0.2534 0.2578 0.1922 -0.0370 0.0340  -0.0265 68  ARG   A CZ  
485  N NH1 . ARG   A 62  ? 0.2554 0.2574 0.1875 -0.0415 0.0311  -0.0271 68  ARG   A NH1 
486  N NH2 . ARG   A 62  ? 0.2590 0.2640 0.2030 -0.0363 0.0430  -0.0325 68  ARG   A NH2 
487  N N   . ARG   A 63  ? 0.2145 0.2161 0.1646 -0.0291 -0.0054 0.0088  69  ARG   A N   
488  C CA  . ARG   A 63  ? 0.2226 0.2239 0.1798 -0.0269 -0.0110 0.0170  69  ARG   A CA  
489  C C   . ARG   A 63  ? 0.2321 0.2303 0.1951 -0.0224 -0.0090 0.0185  69  ARG   A C   
490  O O   . ARG   A 63  ? 0.2582 0.2552 0.2226 -0.0235 -0.0117 0.0247  69  ARG   A O   
491  C CB  . ARG   A 63  ? 0.2538 0.2584 0.2051 -0.0341 -0.0171 0.0242  69  ARG   A CB  
492  C CG  . ARG   A 63  ? 0.2685 0.2770 0.2152 -0.0395 -0.0202 0.0242  69  ARG   A CG  
493  C CD  . ARG   A 63  ? 0.2816 0.2949 0.2280 -0.0449 -0.0283 0.0351  69  ARG   A CD  
494  N NE  . ARG   A 63  ? 0.3036 0.3220 0.2432 -0.0523 -0.0315 0.0348  69  ARG   A NE  
495  C CZ  . ARG   A 63  ? 0.2932 0.3153 0.2175 -0.0633 -0.0320 0.0329  69  ARG   A CZ  
496  N NH1 . ARG   A 63  ? 0.2790 0.3005 0.1939 -0.0677 -0.0294 0.0313  69  ARG   A NH1 
497  N NH2 . ARG   A 63  ? 0.3021 0.3286 0.2197 -0.0709 -0.0343 0.0319  69  ARG   A NH2 
498  N N   . LYS   A 64  ? 0.2058 0.2028 0.1714 -0.0183 -0.0041 0.0129  70  LYS   A N   
499  C CA  . LYS   A 64  ? 0.2079 0.2028 0.1768 -0.0158 -0.0017 0.0133  70  LYS   A CA  
500  C C   . LYS   A 64  ? 0.1935 0.1877 0.1696 -0.0109 0.0011  0.0102  70  LYS   A C   
501  O O   . LYS   A 64  ? 0.1968 0.1929 0.1740 -0.0092 0.0028  0.0065  70  LYS   A O   
502  C CB  . LYS   A 64  ? 0.2527 0.2496 0.2143 -0.0190 0.0015  0.0103  70  LYS   A CB  
503  C CG  . LYS   A 64  ? 0.3796 0.3745 0.3411 -0.0196 0.0025  0.0125  70  LYS   A CG  
504  C CD  . LYS   A 64  ? 0.4837 0.4796 0.4364 -0.0255 0.0016  0.0146  70  LYS   A CD  
505  C CE  . LYS   A 64  ? 0.5448 0.5384 0.4970 -0.0265 0.0032  0.0164  70  LYS   A CE  
506  N NZ  . LYS   A 64  ? 0.5532 0.5416 0.5140 -0.0229 0.0034  0.0186  70  LYS   A NZ  
507  N N   . HIS   A 65  ? 0.1780 0.1693 0.1585 -0.0094 0.0023  0.0116  71  HIS   A N   
508  C CA  . HIS   A 65  ? 0.1647 0.1560 0.1498 -0.0068 0.0055  0.0086  71  HIS   A CA  
509  C C   . HIS   A 65  ? 0.1838 0.1776 0.1649 -0.0089 0.0085  0.0066  71  HIS   A C   
510  O O   . HIS   A 65  ? 0.2236 0.2154 0.2014 -0.0116 0.0089  0.0081  71  HIS   A O   
511  C CB  . HIS   A 65  ? 0.1590 0.1454 0.1512 -0.0054 0.0062  0.0104  71  HIS   A CB  
512  C CG  . HIS   A 65  ? 0.1757 0.1610 0.1744 -0.0031 0.0035  0.0130  71  HIS   A CG  
513  N ND1 . HIS   A 65  ? 0.2144 0.2000 0.2185 -0.0006 0.0046  0.0108  71  HIS   A ND1 
514  C CD2 . HIS   A 65  ? 0.1781 0.1628 0.1792 -0.0035 -0.0005 0.0183  71  HIS   A CD2 
515  C CE1 . HIS   A 65  ? 0.1894 0.1744 0.1994 0.0009  0.0016  0.0143  71  HIS   A CE1 
516  N NE2 . HIS   A 65  ? 0.2042 0.1892 0.2130 -0.0008 -0.0018 0.0192  71  HIS   A NE2 
517  N N   . TYR   A 66  ? 0.1650 0.1636 0.1473 -0.0079 0.0103  0.0040  72  TYR   A N   
518  C CA  . TYR   A 66  ? 0.1648 0.1680 0.1447 -0.0101 0.0127  0.0030  72  TYR   A CA  
519  C C   . TYR   A 66  ? 0.1621 0.1680 0.1449 -0.0107 0.0141  0.0025  72  TYR   A C   
520  O O   . TYR   A 66  ? 0.1463 0.1539 0.1333 -0.0086 0.0138  0.0022  72  TYR   A O   
521  C CB  . TYR   A 66  ? 0.1656 0.1746 0.1464 -0.0089 0.0138  0.0016  72  TYR   A CB  
522  C CG  . TYR   A 66  ? 0.1736 0.1813 0.1494 -0.0105 0.0138  0.0007  72  TYR   A CG  
523  C CD1 . TYR   A 66  ? 0.1921 0.2005 0.1621 -0.0141 0.0147  0.0009  72  TYR   A CD1 
524  C CD2 . TYR   A 66  ? 0.1786 0.1847 0.1543 -0.0095 0.0132  -0.0007 72  TYR   A CD2 
525  C CE1 . TYR   A 66  ? 0.2088 0.2169 0.1728 -0.0170 0.0152  -0.0002 72  TYR   A CE1 
526  C CE2 . TYR   A 66  ? 0.1977 0.2032 0.1670 -0.0128 0.0137  -0.0022 72  TYR   A CE2 
527  C CZ  . TYR   A 66  ? 0.2149 0.2216 0.1781 -0.0168 0.0148  -0.0020 72  TYR   A CZ  
528  O OH  . TYR   A 66  ? 0.2538 0.2604 0.2092 -0.0216 0.0155  -0.0036 72  TYR   A OH  
529  N N   . PRO   A 67  ? 0.1640 0.1708 0.1436 -0.0146 0.0159  0.0024  73  PRO   A N   
530  C CA  . PRO   A 67  ? 0.1649 0.1762 0.1453 -0.0174 0.0173  0.0019  73  PRO   A CA  
531  C C   . PRO   A 67  ? 0.1678 0.1898 0.1515 -0.0169 0.0167  0.0035  73  PRO   A C   
532  O O   . PRO   A 67  ? 0.1851 0.2110 0.1688 -0.0166 0.0170  0.0042  73  PRO   A O   
533  C CB  . PRO   A 67  ? 0.1804 0.1897 0.1556 -0.0229 0.0196  0.0011  73  PRO   A CB  
534  C CG  . PRO   A 67  ? 0.1930 0.1999 0.1652 -0.0225 0.0190  0.0021  73  PRO   A CG  
535  C CD  . PRO   A 67  ? 0.1612 0.1654 0.1357 -0.0177 0.0166  0.0030  73  PRO   A CD  
536  N N   . VAL   A 68  ? 0.1519 0.1785 0.1393 -0.0169 0.0160  0.0046  74  VAL   A N   
537  C CA  . VAL   A 68  ? 0.1655 0.2028 0.1591 -0.0159 0.0151  0.0080  74  VAL   A CA  
538  C C   . VAL   A 68  ? 0.1519 0.1972 0.1461 -0.0207 0.0141  0.0106  74  VAL   A C   
539  O O   . VAL   A 68  ? 0.1538 0.1952 0.1445 -0.0235 0.0144  0.0089  74  VAL   A O   
540  C CB  . VAL   A 68  ? 0.1891 0.2251 0.1896 -0.0097 0.0145  0.0085  74  VAL   A CB  
541  C CG1 . VAL   A 68  ? 0.2007 0.2323 0.2005 -0.0067 0.0158  0.0062  74  VAL   A CG1 
542  C CG2 . VAL   A 68  ? 0.1990 0.2291 0.1993 -0.0085 0.0135  0.0072  74  VAL   A CG2 
543  N N   . SER   A 69  ? 0.1481 0.2055 0.1481 -0.0217 0.0130  0.0155  75  SER   A N   
544  C CA  . SER   A 69  ? 0.1556 0.2236 0.1584 -0.0260 0.0107  0.0204  75  SER   A CA  
545  C C   . SER   A 69  ? 0.1443 0.2152 0.1584 -0.0196 0.0093  0.0245  75  SER   A C   
546  O O   . SER   A 69  ? 0.1480 0.2183 0.1697 -0.0135 0.0106  0.0248  75  SER   A O   
547  C CB  . SER   A 69  ? 0.1962 0.2775 0.2013 -0.0308 0.0097  0.0252  75  SER   A CB  
548  O OG  . SER   A 69  ? 0.2842 0.3623 0.2786 -0.0372 0.0115  0.0211  75  SER   A OG  
549  N N   . PHE   A 70  ? 0.1453 0.2184 0.1604 -0.0213 0.0073  0.0270  76  PHE   A N   
550  C CA  . PHE   A 70  ? 0.1470 0.2214 0.1727 -0.0155 0.0061  0.0309  76  PHE   A CA  
551  C C   . PHE   A 70  ? 0.1543 0.2412 0.1852 -0.0198 0.0025  0.0392  76  PHE   A C   
552  O O   . PHE   A 70  ? 0.1704 0.2627 0.1930 -0.0285 0.0009  0.0400  76  PHE   A O   
553  C CB  . PHE   A 70  ? 0.1492 0.2107 0.1718 -0.0115 0.0073  0.0254  76  PHE   A CB  
554  C CG  . PHE   A 70  ? 0.1595 0.2160 0.1723 -0.0168 0.0075  0.0215  76  PHE   A CG  
555  C CD1 . PHE   A 70  ? 0.1623 0.2105 0.1666 -0.0187 0.0098  0.0154  76  PHE   A CD1 
556  C CD2 . PHE   A 70  ? 0.1559 0.2155 0.1689 -0.0198 0.0059  0.0239  76  PHE   A CD2 
557  C CE1 . PHE   A 70  ? 0.1740 0.2169 0.1716 -0.0232 0.0115  0.0114  76  PHE   A CE1 
558  C CE2 . PHE   A 70  ? 0.1733 0.2278 0.1778 -0.0250 0.0075  0.0192  76  PHE   A CE2 
559  C CZ  . PHE   A 70  ? 0.1677 0.2135 0.1653 -0.0263 0.0107  0.0128  76  PHE   A CZ  
560  N N   . SER   A 71  ? 0.1463 0.2382 0.1912 -0.0144 0.0014  0.0456  77  SER   A N   
561  C CA  . SER   A 71  ? 0.1455 0.2506 0.1977 -0.0181 -0.0028 0.0558  77  SER   A CA  
562  C C   . SER   A 71  ? 0.1473 0.2489 0.1930 -0.0217 -0.0046 0.0553  77  SER   A C   
563  O O   . SER   A 71  ? 0.1492 0.2378 0.1882 -0.0192 -0.0021 0.0474  77  SER   A O   
564  C CB  . SER   A 71  ? 0.1569 0.2678 0.2290 -0.0106 -0.0026 0.0638  77  SER   A CB  
565  O OG  . SER   A 71  ? 0.1763 0.2749 0.2530 -0.0029 0.0004  0.0597  77  SER   A OG  
566  N N   . LYS   A 72  ? 0.1457 0.2599 0.1937 -0.0282 -0.0090 0.0643  78  LYS   A N   
567  C CA  . LYS   A 72  ? 0.1562 0.2686 0.1983 -0.0325 -0.0106 0.0645  78  LYS   A CA  
568  C C   . LYS   A 72  ? 0.1657 0.2716 0.2195 -0.0235 -0.0101 0.0666  78  LYS   A C   
569  O O   . LYS   A 72  ? 0.1671 0.2758 0.2365 -0.0162 -0.0099 0.0723  78  LYS   A O   
570  C CB  . LYS   A 72  ? 0.1889 0.3183 0.2294 -0.0436 -0.0159 0.0746  78  LYS   A CB  
571  C CG  . LYS   A 72  ? 0.2350 0.3686 0.2602 -0.0548 -0.0153 0.0702  78  LYS   A CG  
572  C CD  . LYS   A 72  ? 0.3284 0.4773 0.3466 -0.0690 -0.0199 0.0777  78  LYS   A CD  
573  C CE  . LYS   A 72  ? 0.4119 0.5633 0.4135 -0.0813 -0.0180 0.0716  78  LYS   A CE  
574  N NZ  . LYS   A 72  ? 0.4616 0.6241 0.4513 -0.0973 -0.0208 0.0752  78  LYS   A NZ  
575  N N   . PRO   A 73  ? 0.1668 0.2640 0.2142 -0.0239 -0.0092 0.0619  79  PRO   A N   
576  C CA  . PRO   A 73  ? 0.1693 0.2598 0.2270 -0.0161 -0.0085 0.0634  79  PRO   A CA  
577  C C   . PRO   A 73  ? 0.1796 0.2816 0.2533 -0.0149 -0.0122 0.0771  79  PRO   A C   
578  O O   . PRO   A 73  ? 0.2029 0.3176 0.2753 -0.0231 -0.0169 0.0857  79  PRO   A O   
579  C CB  . PRO   A 73  ? 0.1954 0.2795 0.2427 -0.0203 -0.0082 0.0584  79  PRO   A CB  
580  C CG  . PRO   A 73  ? 0.2187 0.3030 0.2509 -0.0287 -0.0070 0.0521  79  PRO   A CG  
581  C CD  . PRO   A 73  ? 0.1834 0.2767 0.2148 -0.0322 -0.0081 0.0549  79  PRO   A CD  
582  N N   . SER   A 74  ? 0.1794 0.2773 0.2685 -0.0054 -0.0097 0.0792  80  SER   A N   
583  C CA  . SER   A 74  ? 0.1936 0.3018 0.3022 -0.0028 -0.0121 0.0929  80  SER   A CA  
584  C C   . SER   A 74  ? 0.1829 0.2799 0.3055 0.0071  -0.0076 0.0920  80  SER   A C   
585  O O   . SER   A 74  ? 0.1689 0.2514 0.2849 0.0110  -0.0030 0.0806  80  SER   A O   
586  C CB  . SER   A 74  ? 0.2549 0.3745 0.3736 -0.0019 -0.0125 0.0987  80  SER   A CB  
587  O OG  . SER   A 74  ? 0.3643 0.4911 0.4683 -0.0105 -0.0149 0.0962  80  SER   A OG  
588  N N   . LEU   A 75  ? 0.1799 0.2842 0.3231 0.0106  -0.0087 0.1046  81  LEU   A N   
589  C CA  . LEU   A 75  ? 0.1979 0.2922 0.3576 0.0196  -0.0034 0.1050  81  LEU   A CA  
590  C C   . LEU   A 75  ? 0.2134 0.3075 0.3870 0.0263  0.0024  0.1037  81  LEU   A C   
591  O O   . LEU   A 75  ? 0.2277 0.3359 0.4161 0.0266  0.0003  0.1147  81  LEU   A O   
592  C CB  . LEU   A 75  ? 0.2035 0.3065 0.3799 0.0193  -0.0077 0.1210  81  LEU   A CB  
593  C CG  . LEU   A 75  ? 0.2393 0.3312 0.4332 0.0275  -0.0022 0.1225  81  LEU   A CG  
594  C CD1 . LEU   A 75  ? 0.2569 0.3328 0.4361 0.0272  0.0005  0.1106  81  LEU   A CD1 
595  C CD2 . LEU   A 75  ? 0.2444 0.3475 0.4579 0.0271  -0.0071 0.1412  81  LEU   A CD2 
596  N N   . ILE   A 76  ? 0.2069 0.2865 0.3750 0.0307  0.0095  0.0902  82  ILE   A N   
597  C CA  . ILE   A 76  ? 0.2244 0.3019 0.4014 0.0357  0.0163  0.0858  82  ILE   A CA  
598  C C   . ILE   A 76  ? 0.2304 0.2942 0.4204 0.0429  0.0254  0.0807  82  ILE   A C   
599  O O   . ILE   A 76  ? 0.2180 0.2689 0.3986 0.0428  0.0274  0.0730  82  ILE   A O   
600  C CB  . ILE   A 76  ? 0.2534 0.3256 0.4084 0.0322  0.0171  0.0727  82  ILE   A CB  
601  C CG1 . ILE   A 76  ? 0.2844 0.3680 0.4250 0.0243  0.0097  0.0755  82  ILE   A CG1 
602  C CG2 . ILE   A 76  ? 0.2674 0.3353 0.4275 0.0363  0.0248  0.0657  82  ILE   A CG2 
603  C CD1 . ILE   A 76  ? 0.3111 0.4102 0.4613 0.0229  0.0078  0.0839  82  ILE   A CD1 
604  N N   . PHE   A 77  ? 0.2359 0.3014 0.4465 0.0486  0.0321  0.0837  83  PHE   A N   
605  C CA  . PHE   A 77  ? 0.2459 0.2972 0.4685 0.0546  0.0429  0.0769  83  PHE   A CA  
606  C C   . PHE   A 77  ? 0.2522 0.2920 0.4567 0.0528  0.0489  0.0601  83  PHE   A C   
607  O O   . PHE   A 77  ? 0.2732 0.3186 0.4706 0.0508  0.0485  0.0570  83  PHE   A O   
608  C CB  . PHE   A 77  ? 0.2579 0.3153 0.5115 0.0613  0.0492  0.0861  83  PHE   A CB  
609  C CG  . PHE   A 77  ? 0.2909 0.3328 0.5595 0.0670  0.0611  0.0806  83  PHE   A CG  
610  C CD1 . PHE   A 77  ? 0.3184 0.3538 0.5958 0.0689  0.0610  0.0858  83  PHE   A CD1 
611  C CD2 . PHE   A 77  ? 0.3191 0.3520 0.5917 0.0694  0.0729  0.0692  83  PHE   A CD2 
612  C CE1 . PHE   A 77  ? 0.3426 0.3623 0.6333 0.0734  0.0728  0.0797  83  PHE   A CE1 
613  C CE2 . PHE   A 77  ? 0.3311 0.3487 0.6167 0.0733  0.0852  0.0627  83  PHE   A CE2 
614  C CZ  . PHE   A 77  ? 0.3416 0.3524 0.6368 0.0755  0.0852  0.0682  83  PHE   A CZ  
615  N N   . VAL   A 78  ? 0.2344 0.2589 0.4294 0.0522  0.0533  0.0498  84  VAL   A N   
616  C CA  . VAL   A 78  ? 0.2349 0.2489 0.4119 0.0491  0.0582  0.0348  84  VAL   A CA  
617  C C   . VAL   A 78  ? 0.2323 0.2334 0.4207 0.0521  0.0707  0.0273  84  VAL   A C   
618  O O   . VAL   A 78  ? 0.2320 0.2262 0.4308 0.0545  0.0736  0.0295  84  VAL   A O   
619  C CB  . VAL   A 78  ? 0.2406 0.2487 0.3948 0.0441  0.0520  0.0290  84  VAL   A CB  
620  C CG1 . VAL   A 78  ? 0.2506 0.2496 0.3870 0.0402  0.0559  0.0154  84  VAL   A CG1 
621  C CG2 . VAL   A 78  ? 0.2378 0.2574 0.3818 0.0407  0.0411  0.0357  84  VAL   A CG2 
622  N N   . GLU   A 79  ? 0.2440 0.2411 0.4290 0.0509  0.0787  0.0177  85  GLU   A N   
623  C CA  . GLU   A 79  ? 0.2627 0.2468 0.4571 0.0522  0.0925  0.0086  85  GLU   A CA  
624  C C   . GLU   A 79  ? 0.2827 0.2528 0.4615 0.0475  0.0944  -0.0014 85  GLU   A C   
625  O O   . GLU   A 79  ? 0.2814 0.2519 0.4392 0.0428  0.0856  -0.0035 85  GLU   A O   
626  C CB  . GLU   A 79  ? 0.3042 0.2882 0.4947 0.0499  0.1001  -0.0002 85  GLU   A CB  
627  C CG  . GLU   A 79  ? 0.4034 0.4000 0.6152 0.0551  0.1020  0.0086  85  GLU   A CG  
628  C CD  . GLU   A 79  ? 0.5464 0.5435 0.7908 0.0630  0.1086  0.0178  85  GLU   A CD  
629  O OE1 . GLU   A 79  ? 0.5711 0.5548 0.8258 0.0645  0.1209  0.0107  85  GLU   A OE1 
630  O OE2 . GLU   A 79  ? 0.5999 0.6110 0.8599 0.0671  0.1014  0.0327  85  GLU   A OE2 
631  N N   . ALA   A 80  ? 0.2986 0.2559 0.4881 0.0484  0.1067  -0.0080 86  ALA   A N   
632  C CA  . ALA   A 80  ? 0.3270 0.2707 0.5025 0.0429  0.1100  -0.0183 86  ALA   A CA  
633  C C   . ALA   A 80  ? 0.3617 0.3036 0.5095 0.0342  0.1079  -0.0294 86  ALA   A C   
634  O O   . ALA   A 80  ? 0.3768 0.3222 0.5195 0.0320  0.1109  -0.0340 86  ALA   A O   
635  C CB  . ALA   A 80  ? 0.3328 0.2628 0.5246 0.0442  0.1262  -0.0253 86  ALA   A CB  
636  N N   . SER   A 81  ? 0.3627 0.3004 0.4931 0.0290  0.1020  -0.0329 87  SER   A N   
637  C CA  A SER   A 81  ? 0.3717 0.3080 0.4768 0.0201  0.0992  -0.0421 87  SER   A CA  
638  C CA  B SER   A 81  ? 0.3717 0.3080 0.4768 0.0201  0.0992  -0.0421 87  SER   A CA  
639  C C   . SER   A 81  ? 0.3810 0.3052 0.4777 0.0140  0.1038  -0.0506 87  SER   A C   
640  O O   . SER   A 81  ? 0.3800 0.2964 0.4914 0.0173  0.1101  -0.0498 87  SER   A O   
641  C CB  A SER   A 81  ? 0.3855 0.3324 0.4774 0.0196  0.0848  -0.0355 87  SER   A CB  
642  C CB  B SER   A 81  ? 0.3855 0.3324 0.4774 0.0196  0.0848  -0.0355 87  SER   A CB  
643  O OG  A SER   A 81  ? 0.3982 0.3445 0.4896 0.0206  0.0780  -0.0306 87  SER   A OG  
644  O OG  B SER   A 81  ? 0.3982 0.3445 0.4896 0.0206  0.0780  -0.0306 87  SER   A OG  
645  N N   . GLU   A 82  ? 0.3926 0.3156 0.4665 0.0046  0.1003  -0.0579 88  GLU   A N   
646  C CA  . GLU   A 82  ? 0.4071 0.3199 0.4734 -0.0020 0.1041  -0.0652 88  GLU   A CA  
647  C C   . GLU   A 82  ? 0.3651 0.2798 0.4335 0.0013  0.0947  -0.0574 88  GLU   A C   
648  O O   . GLU   A 82  ? 0.3665 0.2727 0.4339 -0.0022 0.0981  -0.0614 88  GLU   A O   
649  C CB  . GLU   A 82  ? 0.4824 0.3933 0.5254 -0.0144 0.1046  -0.0753 88  GLU   A CB  
650  C CG  . GLU   A 82  ? 0.5736 0.4949 0.6002 -0.0176 0.0905  -0.0706 88  GLU   A CG  
651  C CD  . GLU   A 82  ? 0.7126 0.6331 0.7175 -0.0307 0.0900  -0.0786 88  GLU   A CD  
652  O OE1 . GLU   A 82  ? 0.7512 0.6696 0.7484 -0.0362 0.0867  -0.0800 88  GLU   A OE1 
653  O OE2 . GLU   A 82  ? 0.7392 0.6619 0.7349 -0.0362 0.0927  -0.0829 88  GLU   A OE2 
654  N N   . TYR   A 83  ? 0.3256 0.2508 0.3980 0.0076  0.0841  -0.0465 89  TYR   A N   
655  C CA  . TYR   A 83  ? 0.3024 0.2301 0.3755 0.0097  0.0755  -0.0397 89  TYR   A CA  
656  C C   . TYR   A 83  ? 0.2734 0.2021 0.3666 0.0179  0.0758  -0.0301 89  TYR   A C   
657  O O   . TYR   A 83  ? 0.2628 0.1901 0.3583 0.0186  0.0721  -0.0261 89  TYR   A O   
658  C CB  . TYR   A 83  ? 0.3011 0.2397 0.3623 0.0088  0.0635  -0.0351 89  TYR   A CB  
659  C CG  . TYR   A 83  ? 0.3233 0.2625 0.3658 0.0006  0.0614  -0.0420 89  TYR   A CG  
660  C CD1 . TYR   A 83  ? 0.3516 0.2884 0.3833 -0.0059 0.0584  -0.0454 89  TYR   A CD1 
661  C CD2 . TYR   A 83  ? 0.3538 0.2964 0.3898 -0.0015 0.0624  -0.0445 89  TYR   A CD2 
662  C CE1 . TYR   A 83  ? 0.3837 0.3232 0.3992 -0.0139 0.0549  -0.0495 89  TYR   A CE1 
663  C CE2 . TYR   A 83  ? 0.3822 0.3267 0.4012 -0.0096 0.0592  -0.0490 89  TYR   A CE2 
664  C CZ  . TYR   A 83  ? 0.4088 0.3519 0.4179 -0.0161 0.0556  -0.0512 89  TYR   A CZ  
665  O OH  . TYR   A 83  ? 0.4395 0.3861 0.4329 -0.0247 0.0516  -0.0539 89  TYR   A OH  
666  N N   . TYR   A 84  ? 0.2751 0.2072 0.3832 0.0238  0.0796  -0.0255 90  TYR   A N   
667  C CA  . TYR   A 84  ? 0.2626 0.1977 0.3913 0.0312  0.0790  -0.0143 90  TYR   A CA  
668  C C   . TYR   A 84  ? 0.2805 0.2121 0.4291 0.0359  0.0901  -0.0141 90  TYR   A C   
669  O O   . TYR   A 84  ? 0.2837 0.2170 0.4297 0.0350  0.0943  -0.0192 90  TYR   A O   
670  C CB  . TYR   A 84  ? 0.2422 0.1920 0.3709 0.0342  0.0678  -0.0034 90  TYR   A CB  
671  C CG  . TYR   A 84  ? 0.2111 0.1654 0.3238 0.0305  0.0573  -0.0021 90  TYR   A CG  
672  C CD1 . TYR   A 84  ? 0.2078 0.1599 0.3223 0.0302  0.0541  0.0017  90  TYR   A CD1 
673  C CD2 . TYR   A 84  ? 0.2083 0.1691 0.3058 0.0275  0.0511  -0.0042 90  TYR   A CD2 
674  C CE1 . TYR   A 84  ? 0.2030 0.1596 0.3045 0.0269  0.0456  0.0025  90  TYR   A CE1 
675  C CE2 . TYR   A 84  ? 0.2106 0.1750 0.2961 0.0245  0.0430  -0.0033 90  TYR   A CE2 
676  C CZ  . TYR   A 84  ? 0.1983 0.1605 0.2858 0.0242  0.0406  -0.0005 90  TYR   A CZ  
677  O OH  . TYR   A 84  ? 0.1949 0.1609 0.2721 0.0214  0.0336  0.0000  90  TYR   A OH  
678  N N   . PRO   A 85  ? 0.2862 0.2146 0.4563 0.0415  0.0942  -0.0067 91  PRO   A N   
679  C CA  . PRO   A 85  ? 0.2945 0.2220 0.4885 0.0475  0.1041  -0.0037 91  PRO   A CA  
680  C C   . PRO   A 85  ? 0.2910 0.2353 0.4921 0.0518  0.0962  0.0076  91  PRO   A C   
681  O O   . PRO   A 85  ? 0.2771 0.2320 0.4651 0.0499  0.0838  0.0130  91  PRO   A O   
682  C CB  . PRO   A 85  ? 0.3075 0.2279 0.5228 0.0522  0.1084  0.0035  91  PRO   A CB  
683  C CG  . PRO   A 85  ? 0.3146 0.2406 0.5195 0.0504  0.0956  0.0109  91  PRO   A CG  
684  C CD  . PRO   A 85  ? 0.2828 0.2098 0.4583 0.0428  0.0892  0.0010  91  PRO   A CD  
685  N N   . ALA   A 86  ? 0.2946 0.2419 0.5179 0.0574  0.1036  0.0119  92  ALA   A N   
686  C CA  . ALA   A 86  ? 0.2914 0.2557 0.5233 0.0610  0.0962  0.0238  92  ALA   A CA  
687  C C   . ALA   A 86  ? 0.2891 0.2619 0.5307 0.0636  0.0862  0.0394  92  ALA   A C   
688  O O   . ALA   A 86  ? 0.3028 0.2685 0.5597 0.0666  0.0901  0.0439  92  ALA   A O   
689  C CB  . ALA   A 86  ? 0.2811 0.2470 0.5383 0.0667  0.1069  0.0258  92  ALA   A CB  
690  N N   . ARG   A 87  ? 0.2806 0.2669 0.5097 0.0608  0.0735  0.0461  93  ARG   A N   
691  C CA  . ARG   A 87  ? 0.2643 0.2586 0.4966 0.0606  0.0636  0.0591  93  ARG   A CA  
692  C C   . ARG   A 87  ? 0.2641 0.2752 0.4863 0.0573  0.0523  0.0662  93  ARG   A C   
693  O O   . ARG   A 87  ? 0.2599 0.2747 0.4711 0.0553  0.0520  0.0602  93  ARG   A O   
694  C CB  . ARG   A 87  ? 0.2795 0.2633 0.4943 0.0563  0.0612  0.0523  93  ARG   A CB  
695  C CG  . ARG   A 87  ? 0.2992 0.2864 0.4854 0.0498  0.0531  0.0450  93  ARG   A CG  
696  C CD  . ARG   A 87  ? 0.3176 0.2924 0.4868 0.0458  0.0548  0.0333  93  ARG   A CD  
697  N NE  . ARG   A 87  ? 0.3215 0.3010 0.4697 0.0406  0.0456  0.0312  93  ARG   A NE  
698  C CZ  . ARG   A 87  ? 0.3623 0.3457 0.4948 0.0376  0.0424  0.0257  93  ARG   A CZ  
699  N NH1 . ARG   A 87  ? 0.3493 0.3340 0.4830 0.0386  0.0465  0.0221  93  ARG   A NH1 
700  N NH2 . ARG   A 87  ? 0.2845 0.2705 0.4013 0.0334  0.0354  0.0242  93  ARG   A NH2 
701  N N   . TYR   A 88  ? 0.2657 0.2861 0.4896 0.0555  0.0432  0.0782  94  TYR   A N   
702  C CA  . TYR   A 88  ? 0.2666 0.3015 0.4778 0.0503  0.0328  0.0837  94  TYR   A CA  
703  C C   . TYR   A 88  ? 0.2433 0.2727 0.4285 0.0443  0.0283  0.0746  94  TYR   A C   
704  O O   . TYR   A 88  ? 0.2625 0.2846 0.4448 0.0434  0.0278  0.0738  94  TYR   A O   
705  C CB  . TYR   A 88  ? 0.2698 0.3183 0.4957 0.0497  0.0256  0.1017  94  TYR   A CB  
706  C CG  . TYR   A 88  ? 0.2746 0.3340 0.5261 0.0546  0.0277  0.1131  94  TYR   A CG  
707  C CD1 . TYR   A 88  ? 0.2789 0.3521 0.5280 0.0523  0.0240  0.1160  94  TYR   A CD1 
708  C CD2 . TYR   A 88  ? 0.2870 0.3422 0.5664 0.0618  0.0344  0.1204  94  TYR   A CD2 
709  C CE1 . TYR   A 88  ? 0.2914 0.3759 0.5654 0.0568  0.0259  0.1269  94  TYR   A CE1 
710  C CE2 . TYR   A 88  ? 0.2938 0.3595 0.5997 0.0669  0.0369  0.1315  94  TYR   A CE2 
711  C CZ  . TYR   A 88  ? 0.3059 0.3869 0.6092 0.0644  0.0324  0.1349  94  TYR   A CZ  
712  O OH  . TYR   A 88  ? 0.3342 0.4269 0.6649 0.0694  0.0348  0.1463  94  TYR   A OH  
713  N N   . GLN   A 89  ? 0.2052 0.2381 0.3725 0.0404  0.0253  0.0679  95  GLN   A N   
714  C CA  . GLN   A 89  ? 0.1863 0.2155 0.3311 0.0350  0.0210  0.0602  95  GLN   A CA  
715  C C   . GLN   A 89  ? 0.1699 0.2129 0.3073 0.0292  0.0127  0.0676  95  GLN   A C   
716  O O   . GLN   A 89  ? 0.1664 0.2203 0.3077 0.0284  0.0108  0.0729  95  GLN   A O   
717  C CB  . GLN   A 89  ? 0.1883 0.2099 0.3189 0.0343  0.0246  0.0469  95  GLN   A CB  
718  C CG  . GLN   A 89  ? 0.1843 0.2026 0.2953 0.0295  0.0205  0.0403  95  GLN   A CG  
719  C CD  . GLN   A 89  ? 0.1735 0.1827 0.2725 0.0289  0.0240  0.0284  95  GLN   A CD  
720  O OE1 . GLN   A 89  ? 0.2152 0.2158 0.3178 0.0310  0.0303  0.0227  95  GLN   A OE1 
721  N NE2 . GLN   A 89  ? 0.1765 0.1874 0.2609 0.0252  0.0200  0.0247  95  GLN   A NE2 
722  N N   . SER   A 90  ? 0.1575 0.2007 0.2851 0.0246  0.0082  0.0685  96  SER   A N   
723  C CA  . SER   A 90  ? 0.1508 0.2062 0.2703 0.0175  0.0014  0.0744  96  SER   A CA  
724  C C   . SER   A 90  ? 0.1608 0.2142 0.2604 0.0127  0.0005  0.0644  96  SER   A C   
725  O O   . SER   A 90  ? 0.1685 0.2109 0.2604 0.0149  0.0039  0.0539  96  SER   A O   
726  C CB  . SER   A 90  ? 0.1896 0.2473 0.3104 0.0140  -0.0023 0.0817  96  SER   A CB  
727  O OG  . SER   A 90  ? 0.2260 0.2722 0.3362 0.0136  -0.0004 0.0721  96  SER   A OG  
728  N N   . HIS   A 91  ? 0.1567 0.2212 0.2487 0.0057  -0.0039 0.0684  97  HIS   A N   
729  C CA  . HIS   A 91  ? 0.1552 0.2181 0.2301 0.0004  -0.0041 0.0599  97  HIS   A CA  
730  C C   . HIS   A 91  ? 0.1560 0.2120 0.2275 0.0046  -0.0003 0.0512  97  HIS   A C   
731  O O   . HIS   A 91  ? 0.1659 0.2147 0.2262 0.0035  0.0011  0.0424  97  HIS   A O   
732  C CB  . HIS   A 91  ? 0.1702 0.2257 0.2354 -0.0022 -0.0038 0.0540  97  HIS   A CB  
733  C CG  . HIS   A 91  ? 0.1885 0.2509 0.2544 -0.0079 -0.0074 0.0618  97  HIS   A CG  
734  N ND1 . HIS   A 91  ? 0.2133 0.2832 0.2678 -0.0176 -0.0096 0.0624  97  HIS   A ND1 
735  C CD2 . HIS   A 91  ? 0.2093 0.2722 0.2855 -0.0060 -0.0086 0.0693  97  HIS   A CD2 
736  C CE1 . HIS   A 91  ? 0.2160 0.2913 0.2733 -0.0217 -0.0126 0.0702  97  HIS   A CE1 
737  N NE2 . HIS   A 91  ? 0.2203 0.2917 0.2910 -0.0146 -0.0125 0.0751  97  HIS   A NE2 
738  N N   . LEU   A 92  ? 0.1348 0.1938 0.2168 0.0089  0.0014  0.0544  98  LEU   A N   
739  C CA  . LEU   A 92  ? 0.1422 0.1953 0.2215 0.0123  0.0052  0.0468  98  LEU   A CA  
740  C C   . LEU   A 92  ? 0.1352 0.1978 0.2111 0.0085  0.0037  0.0489  98  LEU   A C   
741  O O   . LEU   A 92  ? 0.1322 0.2070 0.2154 0.0060  0.0007  0.0582  98  LEU   A O   
742  C CB  . LEU   A 92  ? 0.1486 0.1978 0.2426 0.0193  0.0099  0.0477  98  LEU   A CB  
743  C CG  . LEU   A 92  ? 0.1783 0.2206 0.2690 0.0220  0.0148  0.0391  98  LEU   A CG  
744  C CD1 . LEU   A 92  ? 0.1775 0.2085 0.2555 0.0212  0.0158  0.0296  98  LEU   A CD1 
745  C CD2 . LEU   A 92  ? 0.1979 0.2375 0.3047 0.0278  0.0209  0.0401  98  LEU   A CD2 
746  N N   . MET   A 93  ? 0.1478 0.2052 0.2126 0.0074  0.0053  0.0408  99  MET   A N   
747  C CA  . MET   A 93  ? 0.1442 0.2089 0.2045 0.0035  0.0045  0.0415  99  MET   A CA  
748  C C   . MET   A 93  ? 0.1434 0.2037 0.2057 0.0078  0.0085  0.0368  99  MET   A C   
749  O O   . MET   A 93  ? 0.1581 0.2076 0.2163 0.0107  0.0111  0.0298  99  MET   A O   
750  C CB  . MET   A 93  ? 0.1553 0.2165 0.2002 -0.0024 0.0037  0.0357  99  MET   A CB  
751  C CG  . MET   A 93  ? 0.1751 0.2396 0.2162 -0.0079 0.0010  0.0385  99  MET   A CG  
752  S SD  . MET   A 93  ? 0.2147 0.2725 0.2401 -0.0144 0.0024  0.0302  99  MET   A SD  
753  C CE  . MET   A 93  ? 0.2422 0.2858 0.2678 -0.0070 0.0050  0.0228  99  MET   A CE  
754  N N   . LEU   A 94  ? 0.1209 0.1899 0.1892 0.0075  0.0089  0.0407  100 LEU   A N   
755  C CA  . LEU   A 94  ? 0.1389 0.2043 0.2093 0.0109  0.0134  0.0361  100 LEU   A CA  
756  C C   . LEU   A 94  ? 0.1422 0.2096 0.2016 0.0063  0.0129  0.0330  100 LEU   A C   
757  O O   . LEU   A 94  ? 0.1554 0.2313 0.2111 0.0008  0.0096  0.0369  100 LEU   A O   
758  C CB  . LEU   A 94  ? 0.1588 0.2323 0.2480 0.0152  0.0161  0.0427  100 LEU   A CB  
759  C CG  . LEU   A 94  ? 0.2067 0.2770 0.3103 0.0208  0.0185  0.0458  100 LEU   A CG  
760  C CD1 . LEU   A 94  ? 0.2249 0.3019 0.3492 0.0256  0.0229  0.0514  100 LEU   A CD1 
761  C CD2 . LEU   A 94  ? 0.2246 0.2795 0.3222 0.0235  0.0229  0.0361  100 LEU   A CD2 
762  N N   . ALA   A 95  ? 0.1383 0.1980 0.1923 0.0078  0.0164  0.0261  101 ALA   A N   
763  C CA  . ALA   A 95  ? 0.1333 0.1941 0.1782 0.0039  0.0165  0.0233  101 ALA   A CA  
764  C C   . ALA   A 95  ? 0.1358 0.1937 0.1834 0.0067  0.0215  0.0194  101 ALA   A C   
765  O O   . ALA   A 95  ? 0.1470 0.1994 0.2003 0.0108  0.0251  0.0168  101 ALA   A O   
766  C CB  . ALA   A 95  ? 0.1458 0.1976 0.1760 0.0007  0.0150  0.0180  101 ALA   A CB  
767  N N   . VAL   A 96  ? 0.1344 0.1957 0.1772 0.0036  0.0222  0.0184  102 VAL   A N   
768  C CA  . VAL   A 96  ? 0.1352 0.1937 0.1778 0.0046  0.0270  0.0139  102 VAL   A CA  
769  C C   . VAL   A 96  ? 0.1651 0.2123 0.1929 0.0025  0.0265  0.0076  102 VAL   A C   
770  O O   . VAL   A 96  ? 0.1701 0.2153 0.1879 -0.0012 0.0234  0.0073  102 VAL   A O   
771  C CB  . VAL   A 96  ? 0.1393 0.2075 0.1835 0.0015  0.0277  0.0163  102 VAL   A CB  
772  C CG1 . VAL   A 96  ? 0.1497 0.2145 0.1911 0.0012  0.0331  0.0108  102 VAL   A CG1 
773  C CG2 . VAL   A 96  ? 0.1287 0.2101 0.1899 0.0035  0.0274  0.0245  102 VAL   A CG2 
774  N N   . GLY   A 97  ? 0.1748 0.2148 0.2020 0.0043  0.0297  0.0030  103 GLY   A N   
775  C CA  . GLY   A 97  ? 0.1971 0.2281 0.2114 0.0017  0.0286  -0.0016 103 GLY   A CA  
776  C C   . GLY   A 97  ? 0.2093 0.2341 0.2234 0.0025  0.0325  -0.0065 103 GLY   A C   
777  O O   . GLY   A 97  ? 0.2171 0.2425 0.2417 0.0058  0.0365  -0.0069 103 GLY   A O   
778  N N   . HIS   A 98  ? 0.2185 0.2374 0.2205 -0.0013 0.0314  -0.0099 104 HIS   A N   
779  C CA  . HIS   A 98  ? 0.2272 0.2404 0.2257 -0.0031 0.0347  -0.0150 104 HIS   A CA  
780  C C   . HIS   A 98  ? 0.2362 0.2448 0.2355 -0.0014 0.0321  -0.0150 104 HIS   A C   
781  O O   . HIS   A 98  ? 0.2425 0.2500 0.2385 -0.0011 0.0263  -0.0119 104 HIS   A O   
782  C CB  . HIS   A 98  ? 0.2440 0.2547 0.2284 -0.0096 0.0337  -0.0175 104 HIS   A CB  
783  C CG  . HIS   A 98  ? 0.2599 0.2661 0.2387 -0.0137 0.0379  -0.0234 104 HIS   A CG  
784  N ND1 . HIS   A 98  ? 0.2739 0.2801 0.2570 -0.0144 0.0466  -0.0288 104 HIS   A ND1 
785  C CD2 . HIS   A 98  ? 0.2634 0.2653 0.2335 -0.0177 0.0349  -0.0247 104 HIS   A CD2 
786  C CE1 . HIS   A 98  ? 0.2704 0.2714 0.2456 -0.0196 0.0491  -0.0342 104 HIS   A CE1 
787  N NE2 . HIS   A 98  ? 0.2666 0.2657 0.2333 -0.0221 0.0417  -0.0315 104 HIS   A NE2 
788  N N   . SER   A 99  ? 0.2342 0.2395 0.2387 -0.0002 0.0370  -0.0186 105 SER   A N   
789  C CA  . SER   A 99  ? 0.2634 0.2640 0.2679 0.0004  0.0353  -0.0195 105 SER   A CA  
790  C C   . SER   A 99  ? 0.2910 0.2862 0.2945 -0.0024 0.0424  -0.0264 105 SER   A C   
791  O O   . SER   A 99  ? 0.3434 0.3391 0.3528 -0.0020 0.0498  -0.0296 105 SER   A O   
792  C CB  . SER   A 99  ? 0.2998 0.3024 0.3158 0.0061  0.0336  -0.0149 105 SER   A CB  
793  O OG  . SER   A 99  ? 0.3843 0.3909 0.4131 0.0098  0.0384  -0.0132 105 SER   A OG  
794  N N   . GLU   A 100 ? 0.2435 0.2343 0.2379 -0.0068 0.0403  -0.0291 106 GLU   A N   
795  C CA  . GLU   A 100 ? 0.2360 0.2209 0.2272 -0.0112 0.0466  -0.0362 106 GLU   A CA  
796  C C   . GLU   A 100 ? 0.2276 0.2093 0.2225 -0.0089 0.0436  -0.0348 106 GLU   A C   
797  O O   . GLU   A 100 ? 0.2139 0.1984 0.2107 -0.0055 0.0363  -0.0289 106 GLU   A O   
798  C CB  . GLU   A 100 ? 0.2537 0.2379 0.2283 -0.0207 0.0452  -0.0397 106 GLU   A CB  
799  C CG  . GLU   A 100 ? 0.2584 0.2459 0.2292 -0.0232 0.0482  -0.0408 106 GLU   A CG  
800  C CD  . GLU   A 100 ? 0.3288 0.3167 0.2828 -0.0336 0.0474  -0.0436 106 GLU   A CD  
801  O OE1 . GLU   A 100 ? 0.3631 0.3482 0.3077 -0.0408 0.0472  -0.0471 106 GLU   A OE1 
802  O OE2 . GLU   A 100 ? 0.3210 0.3125 0.2706 -0.0356 0.0469  -0.0422 106 GLU   A OE2 
803  N N   . PRO   A 101 ? 0.2313 0.2067 0.2280 -0.0109 0.0498  -0.0405 107 PRO   A N   
804  C CA  . PRO   A 101 ? 0.2340 0.2064 0.2349 -0.0086 0.0471  -0.0389 107 PRO   A CA  
805  C C   . PRO   A 101 ? 0.2335 0.2088 0.2262 -0.0108 0.0373  -0.0347 107 PRO   A C   
806  O O   . PRO   A 101 ? 0.2340 0.2109 0.2333 -0.0059 0.0327  -0.0298 107 PRO   A O   
807  C CB  . PRO   A 101 ? 0.2590 0.2234 0.2579 -0.0138 0.0559  -0.0475 107 PRO   A CB  
808  C CG  . PRO   A 101 ? 0.2631 0.2262 0.2672 -0.0134 0.0654  -0.0519 107 PRO   A CG  
809  C CD  . PRO   A 101 ? 0.2421 0.2122 0.2385 -0.0150 0.0607  -0.0490 107 PRO   A CD  
810  N N   . GLY   A 102 ? 0.2178 0.1945 0.1973 -0.0183 0.0342  -0.0361 108 GLY   A N   
811  C CA  . GLY   A 102 ? 0.2112 0.1917 0.1851 -0.0207 0.0251  -0.0312 108 GLY   A CA  
812  C C   . GLY   A 102 ? 0.1894 0.1746 0.1675 -0.0153 0.0188  -0.0239 108 GLY   A C   
813  O O   . GLY   A 102 ? 0.2053 0.1932 0.1824 -0.0158 0.0121  -0.0193 108 GLY   A O   
814  N N   . ASP   A 103 ? 0.1682 0.1548 0.1515 -0.0107 0.0213  -0.0228 109 ASP   A N   
815  C CA  . ASP   A 103 ? 0.1704 0.1607 0.1577 -0.0064 0.0166  -0.0169 109 ASP   A CA  
816  C C   . ASP   A 103 ? 0.1729 0.1633 0.1694 -0.0010 0.0150  -0.0141 109 ASP   A C   
817  O O   . ASP   A 103 ? 0.1698 0.1626 0.1687 0.0014  0.0113  -0.0100 109 ASP   A O   
818  C CB  . ASP   A 103 ? 0.1717 0.1644 0.1608 -0.0045 0.0195  -0.0165 109 ASP   A CB  
819  C CG  . ASP   A 103 ? 0.1911 0.1846 0.1700 -0.0103 0.0195  -0.0178 109 ASP   A CG  
820  O OD1 . ASP   A 103 ? 0.1961 0.1902 0.1684 -0.0141 0.0143  -0.0153 109 ASP   A OD1 
821  O OD2 . ASP   A 103 ? 0.1980 0.1922 0.1765 -0.0111 0.0247  -0.0208 109 ASP   A OD2 
822  N N   . CYS   A 104 ? 0.1717 0.1592 0.1732 0.0004  0.0183  -0.0165 110 CYS   A N   
823  C CA  . CYS   A 104 ? 0.1766 0.1645 0.1859 0.0046  0.0165  -0.0134 110 CYS   A CA  
824  C C   . CYS   A 104 ? 0.1765 0.1657 0.1836 0.0036  0.0108  -0.0109 110 CYS   A C   
825  O O   . CYS   A 104 ? 0.1784 0.1670 0.1798 -0.0004 0.0085  -0.0118 110 CYS   A O   
826  C CB  . CYS   A 104 ? 0.1847 0.1684 0.1992 0.0054  0.0206  -0.0160 110 CYS   A CB  
827  S SG  . CYS   A 104 ? 0.2029 0.1860 0.2275 0.0092  0.0278  -0.0164 110 CYS   A SG  
828  N N   . GLY   A 105 ? 0.1597 0.1512 0.1716 0.0065  0.0088  -0.0074 111 GLY   A N   
829  C CA  . GLY   A 105 ? 0.1585 0.1510 0.1709 0.0062  0.0049  -0.0052 111 GLY   A CA  
830  C C   . GLY   A 105 ? 0.1570 0.1512 0.1683 0.0062  0.0031  -0.0028 111 GLY   A C   
831  O O   . GLY   A 105 ? 0.1615 0.1563 0.1762 0.0069  0.0014  -0.0008 111 GLY   A O   
832  N N   . GLY   A 106 ? 0.1516 0.1464 0.1589 0.0054  0.0043  -0.0031 112 GLY   A N   
833  C CA  . GLY   A 106 ? 0.1471 0.1426 0.1533 0.0051  0.0033  -0.0009 112 GLY   A CA  
834  C C   . GLY   A 106 ? 0.1394 0.1362 0.1498 0.0068  0.0046  -0.0001 112 GLY   A C   
835  O O   . GLY   A 106 ? 0.1471 0.1459 0.1594 0.0077  0.0064  -0.0005 112 GLY   A O   
836  N N   . ILE   A 107 ? 0.1387 0.1344 0.1508 0.0065  0.0042  0.0012  113 ILE   A N   
837  C CA  . ILE   A 107 ? 0.1394 0.1359 0.1538 0.0062  0.0064  0.0008  113 ILE   A CA  
838  C C   . ILE   A 107 ? 0.1370 0.1354 0.1478 0.0044  0.0082  0.0008  113 ILE   A C   
839  O O   . ILE   A 107 ? 0.1354 0.1324 0.1430 0.0036  0.0080  0.0013  113 ILE   A O   
840  C CB  . ILE   A 107 ? 0.1422 0.1357 0.1612 0.0063  0.0070  0.0012  113 ILE   A CB  
841  C CG1 . ILE   A 107 ? 0.1510 0.1446 0.1750 0.0076  0.0059  0.0012  113 ILE   A CG1 
842  C CG2 . ILE   A 107 ? 0.1541 0.1468 0.1733 0.0040  0.0109  -0.0004 113 ILE   A CG2 
843  C CD1 . ILE   A 107 ? 0.1784 0.1700 0.2099 0.0084  0.0066  0.0022  113 ILE   A CD1 
844  N N   . LEU   A 108 ? 0.1286 0.1307 0.1396 0.0030  0.0096  0.0008  114 LEU   A N   
845  C CA  . LEU   A 108 ? 0.1291 0.1344 0.1369 -0.0001 0.0112  0.0011  114 LEU   A CA  
846  C C   . LEU   A 108 ? 0.1324 0.1358 0.1399 -0.0035 0.0136  -0.0007 114 LEU   A C   
847  O O   . LEU   A 108 ? 0.1398 0.1437 0.1497 -0.0038 0.0140  -0.0012 114 LEU   A O   
848  C CB  . LEU   A 108 ? 0.1302 0.1428 0.1396 -0.0006 0.0106  0.0034  114 LEU   A CB  
849  C CG  . LEU   A 108 ? 0.1441 0.1627 0.1506 -0.0053 0.0115  0.0048  114 LEU   A CG  
850  C CD1 . LEU   A 108 ? 0.1423 0.1612 0.1456 -0.0060 0.0121  0.0045  114 LEU   A CD1 
851  C CD2 . LEU   A 108 ? 0.1609 0.1883 0.1718 -0.0057 0.0100  0.0093  114 LEU   A CD2 
852  N N   . ARG   A 109 ? 0.1341 0.1346 0.1388 -0.0063 0.0161  -0.0021 115 ARG   A N   
853  C CA  . ARG   A 109 ? 0.1450 0.1421 0.1497 -0.0103 0.0204  -0.0051 115 ARG   A CA  
854  C C   . ARG   A 109 ? 0.1669 0.1659 0.1653 -0.0165 0.0231  -0.0065 115 ARG   A C   
855  O O   . ARG   A 109 ? 0.1599 0.1606 0.1553 -0.0167 0.0219  -0.0051 115 ARG   A O   
856  C CB  . ARG   A 109 ? 0.1578 0.1470 0.1683 -0.0074 0.0221  -0.0059 115 ARG   A CB  
857  C CG  . ARG   A 109 ? 0.1651 0.1508 0.1746 -0.0065 0.0216  -0.0043 115 ARG   A CG  
858  C CD  . ARG   A 109 ? 0.1831 0.1621 0.2012 -0.0035 0.0227  -0.0031 115 ARG   A CD  
859  N NE  . ARG   A 109 ? 0.2029 0.1838 0.2250 0.0009  0.0177  0.0001  115 ARG   A NE  
860  C CZ  . ARG   A 109 ? 0.1885 0.1683 0.2188 0.0034  0.0177  0.0008  115 ARG   A CZ  
861  N NH1 . ARG   A 109 ? 0.1885 0.1653 0.2243 0.0023  0.0230  -0.0022 115 ARG   A NH1 
862  N NH2 . ARG   A 109 ? 0.2030 0.1854 0.2358 0.0061  0.0127  0.0041  115 ARG   A NH2 
863  N N   . CYS   A 110 ? 0.1924 0.1909 0.1883 -0.0224 0.0274  -0.0098 116 CYS   A N   
864  C CA  . CYS   A 110 ? 0.2199 0.2194 0.2086 -0.0304 0.0310  -0.0122 116 CYS   A CA  
865  C C   . CYS   A 110 ? 0.2476 0.2371 0.2378 -0.0335 0.0385  -0.0179 116 CYS   A C   
866  O O   . CYS   A 110 ? 0.2430 0.2261 0.2415 -0.0283 0.0401  -0.0187 116 CYS   A O   
867  C CB  . CYS   A 110 ? 0.2275 0.2374 0.2107 -0.0371 0.0296  -0.0109 116 CYS   A CB  
868  S SG  . CYS   A 110 ? 0.2242 0.2335 0.2075 -0.0412 0.0328  -0.0141 116 CYS   A SG  
869  N N   . GLN   A 111 ? 0.2789 0.2676 0.2619 -0.0426 0.0439  -0.0220 117 GLN   A N   
870  C CA  . GLN   A 111 ? 0.3033 0.2815 0.2883 -0.0462 0.0528  -0.0285 117 GLN   A CA  
871  C C   . GLN   A 111 ? 0.3181 0.2944 0.3072 -0.0471 0.0568  -0.0320 117 GLN   A C   
872  O O   . GLN   A 111 ? 0.3525 0.3189 0.3490 -0.0462 0.0642  -0.0364 117 GLN   A O   
873  C CB  . GLN   A 111 ? 0.3635 0.3413 0.3382 -0.0578 0.0586  -0.0333 117 GLN   A CB  
874  C CG  . GLN   A 111 ? 0.4250 0.4135 0.3893 -0.0680 0.0579  -0.0343 117 GLN   A CG  
875  C CD  . GLN   A 111 ? 0.5049 0.4948 0.4574 -0.0811 0.0628  -0.0386 117 GLN   A CD  
876  O OE1 . GLN   A 111 ? 0.5248 0.5245 0.4707 -0.0849 0.0576  -0.0345 117 GLN   A OE1 
877  N NE2 . GLN   A 111 ? 0.4941 0.4746 0.4440 -0.0888 0.0734  -0.0473 117 GLN   A NE2 
878  N N   . HIS   A 112 ? 0.2803 0.2659 0.2664 -0.0481 0.0522  -0.0296 118 HIS   A N   
879  C CA  . HIS   A 112 ? 0.2716 0.2565 0.2602 -0.0502 0.0559  -0.0330 118 HIS   A CA  
880  C C   . HIS   A 112 ? 0.2662 0.2492 0.2662 -0.0398 0.0524  -0.0298 118 HIS   A C   
881  O O   . HIS   A 112 ? 0.2921 0.2737 0.2962 -0.0405 0.0560  -0.0327 118 HIS   A O   
882  C CB  . HIS   A 112 ? 0.2917 0.2880 0.2700 -0.0588 0.0529  -0.0315 118 HIS   A CB  
883  C CG  . HIS   A 112 ? 0.3366 0.3372 0.3027 -0.0707 0.0555  -0.0338 118 HIS   A CG  
884  N ND1 . HIS   A 112 ? 0.3620 0.3729 0.3229 -0.0723 0.0484  -0.0275 118 HIS   A ND1 
885  C CD2 . HIS   A 112 ? 0.3732 0.3694 0.3319 -0.0821 0.0647  -0.0417 118 HIS   A CD2 
886  C CE1 . HIS   A 112 ? 0.3925 0.4059 0.3426 -0.0847 0.0525  -0.0312 118 HIS   A CE1 
887  N NE2 . HIS   A 112 ? 0.3954 0.3996 0.3430 -0.0914 0.0626  -0.0402 118 HIS   A NE2 
888  N N   . GLY   A 113 ? 0.2344 0.2185 0.2387 -0.0312 0.0454  -0.0240 119 GLY   A N   
889  C CA  . GLY   A 113 ? 0.2135 0.1971 0.2269 -0.0229 0.0414  -0.0209 119 GLY   A CA  
890  C C   . GLY   A 113 ? 0.1865 0.1768 0.1982 -0.0182 0.0329  -0.0151 119 GLY   A C   
891  O O   . GLY   A 113 ? 0.1870 0.1809 0.1933 -0.0191 0.0300  -0.0128 119 GLY   A O   
892  N N   . VAL   A 114 ? 0.1671 0.1587 0.1840 -0.0135 0.0295  -0.0130 120 VAL   A N   
893  C CA  . VAL   A 114 ? 0.1664 0.1627 0.1828 -0.0092 0.0230  -0.0085 120 VAL   A CA  
894  C C   . VAL   A 114 ? 0.1564 0.1602 0.1675 -0.0131 0.0211  -0.0067 120 VAL   A C   
895  O O   . VAL   A 114 ? 0.1573 0.1634 0.1673 -0.0171 0.0227  -0.0077 120 VAL   A O   
896  C CB  . VAL   A 114 ? 0.1597 0.1545 0.1831 -0.0041 0.0206  -0.0074 120 VAL   A CB  
897  C CG1 . VAL   A 114 ? 0.1692 0.1675 0.1916 -0.0008 0.0154  -0.0041 120 VAL   A CG1 
898  C CG2 . VAL   A 114 ? 0.1711 0.1605 0.2012 -0.0005 0.0212  -0.0070 120 VAL   A CG2 
899  N N   . VAL   A 115 ? 0.1446 0.1526 0.1536 -0.0117 0.0177  -0.0033 121 VAL   A N   
900  C CA  . VAL   A 115 ? 0.1507 0.1671 0.1576 -0.0146 0.0153  0.0005  121 VAL   A CA  
901  C C   . VAL   A 115 ? 0.1453 0.1633 0.1577 -0.0093 0.0118  0.0040  121 VAL   A C   
902  O O   . VAL   A 115 ? 0.1534 0.1766 0.1672 -0.0109 0.0103  0.0074  121 VAL   A O   
903  C CB  . VAL   A 115 ? 0.1699 0.1906 0.1735 -0.0163 0.0145  0.0024  121 VAL   A CB  
904  C CG1 . VAL   A 115 ? 0.1821 0.2131 0.1873 -0.0179 0.0112  0.0085  121 VAL   A CG1 
905  C CG2 . VAL   A 115 ? 0.1708 0.1899 0.1682 -0.0229 0.0184  -0.0012 121 VAL   A CG2 
906  N N   . GLY   A 116 ? 0.1394 0.1528 0.1546 -0.0036 0.0108  0.0034  122 GLY   A N   
907  C CA  . GLY   A 116 ? 0.1430 0.1564 0.1628 0.0007  0.0088  0.0054  122 GLY   A CA  
908  C C   . GLY   A 116 ? 0.1476 0.1561 0.1679 0.0046  0.0084  0.0036  122 GLY   A C   
909  O O   . GLY   A 116 ? 0.1424 0.1475 0.1603 0.0044  0.0088  0.0016  122 GLY   A O   
910  N N   . ILE   A 117 ? 0.1402 0.1480 0.1637 0.0075  0.0078  0.0043  123 ILE   A N   
911  C CA  . ILE   A 117 ? 0.1358 0.1393 0.1579 0.0094  0.0078  0.0020  123 ILE   A CA  
912  C C   . ILE   A 117 ? 0.1389 0.1435 0.1629 0.0109  0.0094  0.0024  123 ILE   A C   
913  O O   . ILE   A 117 ? 0.1461 0.1537 0.1758 0.0121  0.0103  0.0051  123 ILE   A O   
914  C CB  . ILE   A 117 ? 0.1362 0.1359 0.1595 0.0101  0.0068  0.0004  123 ILE   A CB  
915  C CG1 . ILE   A 117 ? 0.1494 0.1496 0.1773 0.0110  0.0074  0.0017  123 ILE   A CG1 
916  C CG2 . ILE   A 117 ? 0.1531 0.1516 0.1762 0.0091  0.0057  -0.0001 123 ILE   A CG2 
917  C CD1 . ILE   A 117 ? 0.1620 0.1583 0.1906 0.0110  0.0067  -0.0004 123 ILE   A CD1 
918  N N   . VAL   A 118 ? 0.1392 0.1416 0.1594 0.0106  0.0102  0.0001  124 VAL   A N   
919  C CA  . VAL   A 118 ? 0.1297 0.1323 0.1522 0.0117  0.0133  -0.0009 124 VAL   A CA  
920  C C   . VAL   A 118 ? 0.1354 0.1349 0.1635 0.0134  0.0154  -0.0018 124 VAL   A C   
921  O O   . VAL   A 118 ? 0.1387 0.1343 0.1643 0.0125  0.0143  -0.0038 124 VAL   A O   
922  C CB  . VAL   A 118 ? 0.1431 0.1431 0.1586 0.0096  0.0141  -0.0042 124 VAL   A CB  
923  C CG1 . VAL   A 118 ? 0.1470 0.1462 0.1650 0.0100  0.0190  -0.0068 124 VAL   A CG1 
924  C CG2 . VAL   A 118 ? 0.1536 0.1558 0.1643 0.0079  0.0124  -0.0029 124 VAL   A CG2 
925  N N   . SER   A 119 ? 0.1398 0.1414 0.1765 0.0158  0.0185  0.0003  125 SER   A N   
926  C CA  . SER   A 119 ? 0.1594 0.1573 0.2037 0.0178  0.0213  0.0002  125 SER   A CA  
927  C C   . SER   A 119 ? 0.1811 0.1773 0.2326 0.0197  0.0276  -0.0015 125 SER   A C   
928  O O   . SER   A 119 ? 0.2109 0.2009 0.2660 0.0201  0.0319  -0.0047 125 SER   A O   
929  C CB  . SER   A 119 ? 0.1815 0.1836 0.2330 0.0192  0.0189  0.0064  125 SER   A CB  
930  O OG  . SER   A 119 ? 0.1830 0.1816 0.2435 0.0214  0.0217  0.0076  125 SER   A OG  
931  N N   . THR   A 120 ? 0.1616 0.1634 0.2163 0.0205  0.0289  0.0006  126 THR   A N   
932  C CA  . THR   A 120 ? 0.1716 0.1723 0.2358 0.0227  0.0360  -0.0010 126 THR   A CA  
933  C C   . THR   A 120 ? 0.1939 0.1971 0.2520 0.0205  0.0377  -0.0041 126 THR   A C   
934  O O   . THR   A 120 ? 0.1862 0.1931 0.2351 0.0182  0.0327  -0.0030 126 THR   A O   
935  C CB  . THR   A 120 ? 0.1771 0.1842 0.2590 0.0271  0.0371  0.0072  126 THR   A CB  
936  O OG1 . THR   A 120 ? 0.1980 0.2155 0.2802 0.0266  0.0329  0.0130  126 THR   A OG1 
937  C CG2 . THR   A 120 ? 0.1798 0.1857 0.2677 0.0287  0.0348  0.0117  126 THR   A CG2 
938  N N   . GLY   A 121 ? 0.2185 0.2194 0.2822 0.0211  0.0453  -0.0080 127 GLY   A N   
939  C CA  . GLY   A 121 ? 0.2569 0.2604 0.3152 0.0187  0.0475  -0.0109 127 GLY   A CA  
940  C C   . GLY   A 121 ? 0.2936 0.2960 0.3633 0.0203  0.0573  -0.0142 127 GLY   A C   
941  O O   . GLY   A 121 ? 0.3067 0.3046 0.3886 0.0233  0.0632  -0.0149 127 GLY   A O   
942  N N   . GLY   A 122 ? 0.3123 0.3175 0.3770 0.0176  0.0597  -0.0170 128 GLY   A N   
943  C CA  . GLY   A 122 ? 0.3247 0.3291 0.3984 0.0180  0.0700  -0.0215 128 GLY   A CA  
944  C C   . GLY   A 122 ? 0.3476 0.3627 0.4296 0.0200  0.0698  -0.0163 128 GLY   A C   
945  O O   . GLY   A 122 ? 0.3426 0.3663 0.4313 0.0230  0.0633  -0.0073 128 GLY   A O   
946  N N   . ASN   A 123 ? 0.3464 0.3614 0.4271 0.0172  0.0771  -0.0221 129 ASN   A N   
947  C CA  . ASN   A 123 ? 0.3493 0.3743 0.4401 0.0188  0.0794  -0.0184 129 ASN   A CA  
948  C C   . ASN   A 123 ? 0.3132 0.3474 0.3962 0.0173  0.0697  -0.0119 129 ASN   A C   
949  O O   . ASN   A 123 ? 0.3065 0.3515 0.4019 0.0197  0.0691  -0.0053 129 ASN   A O   
950  C CB  . ASN   A 123 ? 0.3791 0.4090 0.4968 0.0262  0.0844  -0.0122 129 ASN   A CB  
951  C CG  . ASN   A 123 ? 0.4458 0.4672 0.5747 0.0275  0.0979  -0.0199 129 ASN   A CG  
952  O OD1 . ASN   A 123 ? 0.4890 0.5065 0.6108 0.0228  0.1059  -0.0292 129 ASN   A OD1 
953  N ND2 . ASN   A 123 ? 0.4333 0.4514 0.5800 0.0332  0.1011  -0.0163 129 ASN   A ND2 
954  N N   . GLY   A 124 ? 0.2746 0.3047 0.3374 0.0123  0.0633  -0.0143 130 GLY   A N   
955  C CA  . GLY   A 124 ? 0.2574 0.2939 0.3119 0.0101  0.0554  -0.0095 130 GLY   A CA  
956  C C   . GLY   A 124 ? 0.2092 0.2500 0.2680 0.0128  0.0479  -0.0018 130 GLY   A C   
957  O O   . GLY   A 124 ? 0.2096 0.2560 0.2631 0.0106  0.0425  0.0022  130 GLY   A O   
958  N N   . LEU   A 125 ? 0.1902 0.2277 0.2571 0.0166  0.0480  -0.0001 131 LEU   A N   
959  C CA  . LEU   A 125 ? 0.1902 0.2310 0.2588 0.0178  0.0408  0.0066  131 LEU   A CA  
960  C C   . LEU   A 125 ? 0.1990 0.2301 0.2565 0.0167  0.0378  0.0028  131 LEU   A C   
961  O O   . LEU   A 125 ? 0.2325 0.2551 0.2872 0.0165  0.0420  -0.0033 131 LEU   A O   
962  C CB  . LEU   A 125 ? 0.1922 0.2387 0.2805 0.0228  0.0424  0.0135  131 LEU   A CB  
963  C CG  . LEU   A 125 ? 0.2044 0.2629 0.3071 0.0242  0.0445  0.0194  131 LEU   A CG  
964  C CD1 . LEU   A 125 ? 0.2217 0.2838 0.3479 0.0301  0.0488  0.0254  131 LEU   A CD1 
965  C CD2 . LEU   A 125 ? 0.2075 0.2771 0.3053 0.0204  0.0368  0.0261  131 LEU   A CD2 
966  N N   . VAL   A 126 ? 0.1611 0.1939 0.2128 0.0153  0.0312  0.0064  132 VAL   A N   
967  C CA  . VAL   A 126 ? 0.1514 0.1765 0.1956 0.0148  0.0283  0.0040  132 VAL   A CA  
968  C C   . VAL   A 126 ? 0.1473 0.1771 0.1980 0.0161  0.0244  0.0103  132 VAL   A C   
969  O O   . VAL   A 126 ? 0.1557 0.1937 0.2076 0.0144  0.0215  0.0153  132 VAL   A O   
970  C CB  . VAL   A 126 ? 0.1621 0.1835 0.1913 0.0107  0.0247  0.0010  132 VAL   A CB  
971  C CG1 . VAL   A 126 ? 0.1662 0.1939 0.1922 0.0083  0.0216  0.0045  132 VAL   A CG1 
972  C CG2 . VAL   A 126 ? 0.1654 0.1805 0.1893 0.0104  0.0216  -0.0004 132 VAL   A CG2 
973  N N   . GLY   A 127 ? 0.1376 0.1626 0.1917 0.0181  0.0244  0.0101  133 GLY   A N   
974  C CA  . GLY   A 127 ? 0.1319 0.1612 0.1909 0.0184  0.0207  0.0162  133 GLY   A CA  
975  C C   . GLY   A 127 ? 0.1437 0.1673 0.1929 0.0163  0.0174  0.0133  133 GLY   A C   
976  O O   . GLY   A 127 ? 0.1572 0.1728 0.2011 0.0165  0.0186  0.0079  133 GLY   A O   
977  N N   . PHE   A 128 ? 0.1306 0.1590 0.1777 0.0137  0.0136  0.0171  134 PHE   A N   
978  C CA  . PHE   A 128 ? 0.1327 0.1565 0.1722 0.0117  0.0113  0.0145  134 PHE   A CA  
979  C C   . PHE   A 128 ? 0.1450 0.1712 0.1893 0.0113  0.0096  0.0188  134 PHE   A C   
980  O O   . PHE   A 128 ? 0.1522 0.1869 0.2013 0.0096  0.0080  0.0251  134 PHE   A O   
981  C CB  . PHE   A 128 ? 0.1390 0.1649 0.1699 0.0074  0.0097  0.0136  134 PHE   A CB  
982  C CG  . PHE   A 128 ? 0.1359 0.1606 0.1621 0.0069  0.0110  0.0109  134 PHE   A CG  
983  C CD1 . PHE   A 128 ? 0.1442 0.1616 0.1645 0.0073  0.0113  0.0063  134 PHE   A CD1 
984  C CD2 . PHE   A 128 ? 0.1361 0.1679 0.1639 0.0055  0.0114  0.0136  134 PHE   A CD2 
985  C CE1 . PHE   A 128 ? 0.1462 0.1628 0.1618 0.0062  0.0122  0.0046  134 PHE   A CE1 
986  C CE2 . PHE   A 128 ? 0.1452 0.1759 0.1683 0.0046  0.0127  0.0111  134 PHE   A CE2 
987  C CZ  . PHE   A 128 ? 0.1348 0.1576 0.1515 0.0050  0.0131  0.0066  134 PHE   A CZ  
988  N N   . ALA   A 129 ? 0.1334 0.1533 0.1761 0.0120  0.0095  0.0159  135 ALA   A N   
989  C CA  . ALA   A 129 ? 0.1319 0.1536 0.1777 0.0108  0.0078  0.0195  135 ALA   A CA  
990  C C   . ALA   A 129 ? 0.1367 0.1613 0.1746 0.0057  0.0060  0.0188  135 ALA   A C   
991  O O   . ALA   A 129 ? 0.1378 0.1573 0.1697 0.0050  0.0066  0.0136  135 ALA   A O   
992  C CB  . ALA   A 129 ? 0.1364 0.1502 0.1829 0.0130  0.0088  0.0159  135 ALA   A CB  
993  N N   . ASP   A 130 ? 0.1351 0.1680 0.1736 0.0015  0.0042  0.0242  136 ASP   A N   
994  C CA  . ASP   A 130 ? 0.1442 0.1796 0.1744 -0.0051 0.0040  0.0226  136 ASP   A CA  
995  C C   . ASP   A 130 ? 0.1536 0.1847 0.1821 -0.0063 0.0045  0.0199  136 ASP   A C   
996  O O   . ASP   A 130 ? 0.1547 0.1850 0.1885 -0.0041 0.0035  0.0227  136 ASP   A O   
997  C CB  . ASP   A 130 ? 0.1613 0.2083 0.1920 -0.0110 0.0015  0.0300  136 ASP   A CB  
998  C CG  . ASP   A 130 ? 0.2360 0.2860 0.2565 -0.0199 0.0022  0.0276  136 ASP   A CG  
999  O OD1 . ASP   A 130 ? 0.2294 0.2752 0.2436 -0.0214 0.0049  0.0215  136 ASP   A OD1 
1000 O OD2 . ASP   A 130 ? 0.3014 0.3575 0.3203 -0.0259 0.0006  0.0315  136 ASP   A OD2 
1001 N N   . VAL   A 131 ? 0.1409 0.1689 0.1629 -0.0098 0.0066  0.0145  137 VAL   A N   
1002 C CA  . VAL   A 131 ? 0.1344 0.1597 0.1555 -0.0119 0.0079  0.0119  137 VAL   A CA  
1003 C C   . VAL   A 131 ? 0.1442 0.1731 0.1582 -0.0207 0.0102  0.0100  137 VAL   A C   
1004 O O   . VAL   A 131 ? 0.1473 0.1742 0.1603 -0.0234 0.0124  0.0070  137 VAL   A O   
1005 C CB  . VAL   A 131 ? 0.1397 0.1566 0.1625 -0.0075 0.0096  0.0063  137 VAL   A CB  
1006 C CG1 . VAL   A 131 ? 0.1537 0.1670 0.1813 -0.0011 0.0078  0.0072  137 VAL   A CG1 
1007 C CG2 . VAL   A 131 ? 0.1570 0.1706 0.1768 -0.0082 0.0122  0.0021  137 VAL   A CG2 
1008 N N   . ARG   A 132 ? 0.1571 0.1916 0.1661 -0.0259 0.0102  0.0115  138 ARG   A N   
1009 C CA  . ARG   A 132 ? 0.1545 0.1916 0.1552 -0.0357 0.0136  0.0082  138 ARG   A CA  
1010 C C   . ARG   A 132 ? 0.1761 0.2200 0.1735 -0.0432 0.0125  0.0116  138 ARG   A C   
1011 O O   . ARG   A 132 ? 0.1922 0.2367 0.1820 -0.0523 0.0167  0.0070  138 ARG   A O   
1012 C CB  . ARG   A 132 ? 0.1664 0.2085 0.1617 -0.0405 0.0135  0.0092  138 ARG   A CB  
1013 C CG  . ARG   A 132 ? 0.1702 0.2047 0.1668 -0.0350 0.0157  0.0047  138 ARG   A CG  
1014 C CD  . ARG   A 132 ? 0.1804 0.2206 0.1717 -0.0403 0.0154  0.0062  138 ARG   A CD  
1015 N NE  . ARG   A 132 ? 0.1953 0.2443 0.1915 -0.0374 0.0099  0.0144  138 ARG   A NE  
1016 C CZ  . ARG   A 132 ? 0.2245 0.2806 0.2191 -0.0403 0.0084  0.0177  138 ARG   A CZ  
1017 N NH1 . ARG   A 132 ? 0.2218 0.2772 0.2079 -0.0475 0.0116  0.0133  138 ARG   A NH1 
1018 N NH2 . ARG   A 132 ? 0.2260 0.2899 0.2282 -0.0365 0.0042  0.0254  138 ARG   A NH2 
1019 N N   . ASP   A 133 ? 0.1642 0.2134 0.1674 -0.0405 0.0074  0.0197  139 ASP   A N   
1020 C CA  . ASP   A 133 ? 0.1754 0.2316 0.1758 -0.0480 0.0056  0.0243  139 ASP   A CA  
1021 C C   . ASP   A 133 ? 0.1832 0.2329 0.1856 -0.0460 0.0078  0.0205  139 ASP   A C   
1022 O O   . ASP   A 133 ? 0.1993 0.2538 0.1982 -0.0531 0.0072  0.0233  139 ASP   A O   
1023 C CB  . ASP   A 133 ? 0.1927 0.2579 0.2003 -0.0464 -0.0008 0.0364  139 ASP   A CB  
1024 C CG  . ASP   A 133 ? 0.2376 0.2962 0.2570 -0.0346 -0.0020 0.0383  139 ASP   A CG  
1025 O OD1 . ASP   A 133 ? 0.2090 0.2593 0.2307 -0.0273 0.0002  0.0324  139 ASP   A OD1 
1026 O OD2 . ASP   A 133 ? 0.2569 0.3186 0.2830 -0.0335 -0.0051 0.0458  139 ASP   A OD2 
1027 N N   . LEU   A 134 ? 0.1778 0.2175 0.1856 -0.0372 0.0100  0.0149  140 LEU   A N   
1028 C CA  . LEU   A 134 ? 0.1738 0.2082 0.1851 -0.0347 0.0116  0.0119  140 LEU   A CA  
1029 C C   . LEU   A 134 ? 0.1854 0.2166 0.1921 -0.0402 0.0179  0.0035  140 LEU   A C   
1030 O O   . LEU   A 134 ? 0.1838 0.2080 0.1945 -0.0353 0.0213  -0.0023 140 LEU   A O   
1031 C CB  . LEU   A 134 ? 0.1662 0.1933 0.1855 -0.0241 0.0105  0.0106  140 LEU   A CB  
1032 C CG  . LEU   A 134 ? 0.1713 0.2000 0.1961 -0.0187 0.0062  0.0174  140 LEU   A CG  
1033 C CD1 . LEU   A 134 ? 0.1761 0.1973 0.2061 -0.0105 0.0063  0.0144  140 LEU   A CD1 
1034 C CD2 . LEU   A 134 ? 0.1780 0.2106 0.2060 -0.0206 0.0035  0.0243  140 LEU   A CD2 
1035 N N   . LEU   A 135 ? 0.1814 0.2184 0.1801 -0.0510 0.0199  0.0033  141 LEU   A N   
1036 C CA  . LEU   A 135 ? 0.1927 0.2264 0.1867 -0.0577 0.0279  -0.0057 141 LEU   A CA  
1037 C C   . LEU   A 135 ? 0.1984 0.2258 0.1994 -0.0536 0.0318  -0.0108 141 LEU   A C   
1038 O O   . LEU   A 135 ? 0.2134 0.2353 0.2167 -0.0542 0.0391  -0.0186 141 LEU   A O   
1039 C CB  . LEU   A 135 ? 0.2119 0.2539 0.1939 -0.0724 0.0296  -0.0052 141 LEU   A CB  
1040 C CG  . LEU   A 135 ? 0.2404 0.2916 0.2159 -0.0779 0.0244  0.0020  141 LEU   A CG  
1041 C CD1 . LEU   A 135 ? 0.2666 0.3263 0.2288 -0.0944 0.0266  0.0016  141 LEU   A CD1 
1042 C CD2 . LEU   A 135 ? 0.2508 0.2983 0.2270 -0.0738 0.0257  -0.0009 141 LEU   A CD2 
1043 N N   . TRP   A 136 ? 0.1874 0.2158 0.1930 -0.0496 0.0275  -0.0062 142 TRP   A N   
1044 C CA  . TRP   A 136 ? 0.1840 0.2080 0.1965 -0.0463 0.0304  -0.0102 142 TRP   A CA  
1045 C C   . TRP   A 136 ? 0.1937 0.2109 0.2159 -0.0367 0.0316  -0.0135 142 TRP   A C   
1046 O O   . TRP   A 136 ? 0.1997 0.2140 0.2289 -0.0347 0.0351  -0.0174 142 TRP   A O   
1047 C CB  . TRP   A 136 ? 0.1843 0.2108 0.1989 -0.0449 0.0252  -0.0041 142 TRP   A CB  
1048 C CG  . TRP   A 136 ? 0.1763 0.2024 0.1948 -0.0374 0.0185  0.0027  142 TRP   A CG  
1049 C CD1 . TRP   A 136 ? 0.1877 0.2189 0.2038 -0.0390 0.0137  0.0105  142 TRP   A CD1 
1050 C CD2 . TRP   A 136 ? 0.1791 0.1995 0.2054 -0.0278 0.0164  0.0023  142 TRP   A CD2 
1051 N NE1 . TRP   A 136 ? 0.1973 0.2253 0.2202 -0.0303 0.0099  0.0141  142 TRP   A NE1 
1052 C CE2 . TRP   A 136 ? 0.1867 0.2079 0.2144 -0.0240 0.0116  0.0087  142 TRP   A CE2 
1053 C CE3 . TRP   A 136 ? 0.1944 0.2099 0.2270 -0.0227 0.0183  -0.0023 142 TRP   A CE3 
1054 C CZ2 . TRP   A 136 ? 0.1951 0.2112 0.2285 -0.0162 0.0095  0.0090  142 TRP   A CZ2 
1055 C CZ3 . TRP   A 136 ? 0.2041 0.2159 0.2415 -0.0155 0.0149  -0.0009 142 TRP   A CZ3 
1056 C CH2 . TRP   A 136 ? 0.1991 0.2107 0.2360 -0.0128 0.0110  0.0040  142 TRP   A CH2 
1057 N N   . LEU   A 137 ? 0.1876 0.2029 0.2107 -0.0312 0.0285  -0.0116 143 LEU   A N   
1058 C CA  . LEU   A 137 ? 0.2083 0.2181 0.2398 -0.0234 0.0292  -0.0138 143 LEU   A CA  
1059 C C   . LEU   A 137 ? 0.2418 0.2480 0.2773 -0.0255 0.0371  -0.0203 143 LEU   A C   
1060 O O   . LEU   A 137 ? 0.2429 0.2456 0.2885 -0.0198 0.0383  -0.0214 143 LEU   A O   
1061 C CB  . LEU   A 137 ? 0.1931 0.2019 0.2231 -0.0190 0.0253  -0.0109 143 LEU   A CB  
1062 C CG  . LEU   A 137 ? 0.1879 0.1981 0.2181 -0.0146 0.0189  -0.0053 143 LEU   A CG  
1063 C CD1 . LEU   A 137 ? 0.1916 0.2018 0.2195 -0.0120 0.0165  -0.0032 143 LEU   A CD1 
1064 C CD2 . LEU   A 137 ? 0.1992 0.2063 0.2365 -0.0089 0.0169  -0.0053 143 LEU   A CD2 
1065 N N   . ASP   A 138 ? 0.2790 0.2862 0.3070 -0.0344 0.0429  -0.0244 144 ASP   A N   
1066 C CA  . ASP   A 138 ? 0.3178 0.3202 0.3497 -0.0375 0.0526  -0.0318 144 ASP   A CA  
1067 C C   . ASP   A 138 ? 0.3695 0.3714 0.4071 -0.0404 0.0592  -0.0366 144 ASP   A C   
1068 O O   . ASP   A 138 ? 0.3753 0.3728 0.4178 -0.0433 0.0688  -0.0434 144 ASP   A O   
1069 C CB  . ASP   A 138 ? 0.3396 0.3429 0.3593 -0.0477 0.0573  -0.0355 144 ASP   A CB  
1070 C CG  . ASP   A 138 ? 0.4037 0.4077 0.4178 -0.0465 0.0527  -0.0320 144 ASP   A CG  
1071 O OD1 . ASP   A 138 ? 0.4006 0.4025 0.4211 -0.0372 0.0476  -0.0281 144 ASP   A OD1 
1072 O OD2 . ASP   A 138 ? 0.4824 0.4900 0.4852 -0.0557 0.0541  -0.0330 144 ASP   A OD2 
1073 N N   . GLU   A 139 ? 0.3977 0.4038 0.4354 -0.0403 0.0552  -0.0336 145 GLU   A N   
1074 C CA  . GLU   A 139 ? 0.4387 0.4453 0.4811 -0.0442 0.0617  -0.0383 145 GLU   A CA  
1075 C C   . GLU   A 139 ? 0.4681 0.4766 0.5192 -0.0379 0.0566  -0.0343 145 GLU   A C   
1076 O O   . GLU   A 139 ? 0.4651 0.4742 0.5170 -0.0314 0.0481  -0.0283 145 GLU   A O   
1077 C CB  . GLU   A 139 ? 0.4829 0.4942 0.5110 -0.0569 0.0643  -0.0402 145 GLU   A CB  
1078 C CG  . GLU   A 139 ? 0.5698 0.5871 0.5895 -0.0577 0.0542  -0.0317 145 GLU   A CG  
1079 C CD  . GLU   A 139 ? 0.6813 0.7052 0.6860 -0.0702 0.0538  -0.0302 145 GLU   A CD  
1080 O OE1 . GLU   A 139 ? 0.6881 0.7174 0.6888 -0.0722 0.0474  -0.0234 145 GLU   A OE1 
1081 O OE2 . GLU   A 139 ? 0.7280 0.7517 0.7250 -0.0785 0.0598  -0.0353 145 GLU   A OE2 
1082 N N   . GLU   A 140 ? 0.4988 0.5083 0.5558 -0.0408 0.0624  -0.0383 146 GLU   A N   
1083 C CA  . GLU   A 140 ? 0.5339 0.5460 0.5990 -0.0370 0.0592  -0.0357 146 GLU   A CA  
1084 C C   . GLU   A 140 ? 0.5493 0.5598 0.6304 -0.0271 0.0573  -0.0336 146 GLU   A C   
1085 O O   . GLU   A 140 ? 0.5564 0.5680 0.6504 -0.0257 0.0621  -0.0359 146 GLU   A O   
1086 C CB  . GLU   A 140 ? 0.5820 0.5974 0.6377 -0.0380 0.0503  -0.0294 146 GLU   A CB  
1087 C CG  . GLU   A 140 ? 0.6760 0.6929 0.7393 -0.0335 0.0459  -0.0263 146 GLU   A CG  
1088 C CD  . GLU   A 140 ? 0.7903 0.8105 0.8532 -0.0398 0.0495  -0.0285 146 GLU   A CD  
1089 O OE1 . GLU   A 140 ? 0.8140 0.8360 0.8712 -0.0417 0.0442  -0.0241 146 GLU   A OE1 
1090 O OE2 . GLU   A 140 ? 0.8275 0.8480 0.8963 -0.0431 0.0582  -0.0346 146 GLU   A OE2 
1091 N N   . SER   B 1   ? 0.2289 0.2355 0.2477 0.0062  -0.0041 0.0365  7   SER   C N   
1092 C CA  . SER   B 1   ? 0.2205 0.2293 0.2476 0.0047  -0.0050 0.0367  7   SER   C CA  
1093 C C   . SER   B 1   ? 0.2280 0.2353 0.2546 0.0037  -0.0049 0.0336  7   SER   C C   
1094 O O   . SER   B 1   ? 0.2489 0.2533 0.2686 0.0039  -0.0054 0.0314  7   SER   C O   
1095 C CB  . SER   B 1   ? 0.2622 0.2719 0.2903 0.0038  -0.0093 0.0390  7   SER   C CB  
1096 O OG  . SER   B 1   ? 0.3144 0.3213 0.3353 0.0031  -0.0129 0.0371  7   SER   C OG  
1097 N N   . GLY   B 2   ? 0.2185 0.2274 0.2524 0.0029  -0.0041 0.0337  8   GLY   C N   
1098 C CA  . GLY   B 2   ? 0.2075 0.2149 0.2411 0.0023  -0.0034 0.0316  8   GLY   C CA  
1099 C C   . GLY   B 2   ? 0.1928 0.2016 0.2328 0.0027  -0.0003 0.0315  8   GLY   C C   
1100 O O   . GLY   B 2   ? 0.1929 0.2032 0.2361 0.0037  0.0018  0.0316  8   GLY   C O   
1101 N N   . ALA   B 3   ? 0.1746 0.1825 0.2160 0.0020  0.0002  0.0310  9   ALA   C N   
1102 C CA  . ALA   B 3   ? 0.1662 0.1746 0.2120 0.0029  0.0037  0.0309  9   ALA   C CA  
1103 C C   . ALA   B 3   ? 0.1567 0.1623 0.1985 0.0033  0.0051  0.0294  9   ALA   C C   
1104 O O   . ALA   B 3   ? 0.1695 0.1731 0.2076 0.0024  0.0032  0.0290  9   ALA   C O   
1105 C CB  . ALA   B 3   ? 0.1820 0.1931 0.2368 0.0021  0.0039  0.0337  9   ALA   C CB  
1106 N N   . ILE   B 4   ? 0.1540 0.1590 0.1962 0.0049  0.0084  0.0286  10  ILE   C N   
1107 C CA  . ILE   B 4   ? 0.1514 0.1536 0.1900 0.0059  0.0106  0.0280  10  ILE   C CA  
1108 C C   . ILE   B 4   ? 0.1664 0.1697 0.2121 0.0056  0.0133  0.0306  10  ILE   C C   
1109 O O   . ILE   B 4   ? 0.1751 0.1804 0.2259 0.0063  0.0150  0.0313  10  ILE   C O   
1110 C CB  . ILE   B 4   ? 0.1603 0.1607 0.1933 0.0085  0.0123  0.0253  10  ILE   C CB  
1111 C CG1 . ILE   B 4   ? 0.1809 0.1813 0.2098 0.0088  0.0100  0.0229  10  ILE   C CG1 
1112 C CG2 . ILE   B 4   ? 0.1805 0.1776 0.2083 0.0098  0.0144  0.0252  10  ILE   C CG2 
1113 C CD1 . ILE   B 4   ? 0.1901 0.1898 0.2163 0.0112  0.0108  0.0200  10  ILE   C CD1 
1114 N N   . TYR   B 5   ? 0.1613 0.1630 0.2080 0.0048  0.0143  0.0322  11  TYR   C N   
1115 C CA  . TYR   B 5   ? 0.1659 0.1687 0.2205 0.0046  0.0175  0.0351  11  TYR   C CA  
1116 C C   . TYR   B 5   ? 0.1894 0.1886 0.2390 0.0068  0.0220  0.0353  11  TYR   C C   
1117 O O   . TYR   B 5   ? 0.2073 0.2040 0.2544 0.0062  0.0217  0.0358  11  TYR   C O   
1118 C CB  . TYR   B 5   ? 0.1699 0.1744 0.2326 0.0016  0.0147  0.0376  11  TYR   C CB  
1119 C CG  . TYR   B 5   ? 0.1765 0.1845 0.2436 0.0000  0.0103  0.0379  11  TYR   C CG  
1120 C CD1 . TYR   B 5   ? 0.1764 0.1880 0.2522 0.0002  0.0114  0.0399  11  TYR   C CD1 
1121 C CD2 . TYR   B 5   ? 0.1911 0.1985 0.2530 -0.0012 0.0055  0.0363  11  TYR   C CD2 
1122 C CE1 . TYR   B 5   ? 0.1881 0.2026 0.2670 -0.0008 0.0074  0.0406  11  TYR   C CE1 
1123 C CE2 . TYR   B 5   ? 0.2028 0.2128 0.2669 -0.0020 0.0019  0.0369  11  TYR   C CE2 
1124 C CZ  . TYR   B 5   ? 0.2070 0.2206 0.2797 -0.0018 0.0026  0.0392  11  TYR   C CZ  
1125 O OH  . TYR   B 5   ? 0.2243 0.2404 0.2987 -0.0022 -0.0010 0.0402  11  TYR   C OH  
1126 N N   . VAL   B 6   ? 0.1951 0.1935 0.2421 0.0097  0.0259  0.0346  12  VAL   C N   
1127 C CA  . VAL   B 6   ? 0.2042 0.1987 0.2444 0.0125  0.0304  0.0348  12  VAL   C CA  
1128 C C   . VAL   B 6   ? 0.2091 0.2039 0.2544 0.0142  0.0361  0.0372  12  VAL   C C   
1129 O O   . VAL   B 6   ? 0.1988 0.1955 0.2474 0.0149  0.0367  0.0363  12  VAL   C O   
1130 C CB  . VAL   B 6   ? 0.2266 0.2184 0.2553 0.0153  0.0292  0.0309  12  VAL   C CB  
1131 C CG1 . VAL   B 6   ? 0.2223 0.2160 0.2522 0.0161  0.0283  0.0283  12  VAL   C CG1 
1132 C CG2 . VAL   B 6   ? 0.2489 0.2363 0.2691 0.0188  0.0335  0.0313  12  VAL   C CG2 
1133 N N   . GLY   B 7   ? 0.2211 0.2141 0.2685 0.0147  0.0406  0.0406  13  GLY   C N   
1134 C CA  . GLY   B 7   ? 0.2170 0.2104 0.2703 0.0164  0.0469  0.0434  13  GLY   C CA  
1135 C C   . GLY   B 7   ? 0.2174 0.2162 0.2845 0.0141  0.0457  0.0449  13  GLY   C C   
1136 O O   . GLY   B 7   ? 0.2246 0.2264 0.2993 0.0105  0.0410  0.0459  13  GLY   C O   
1137 N N   . ASN   B 8   ? 0.2082 0.2077 0.2773 0.0162  0.0489  0.0445  14  ASN   C N   
1138 C CA  . ASN   B 8   ? 0.2058 0.2103 0.2877 0.0144  0.0475  0.0459  14  ASN   C CA  
1139 C C   . ASN   B 8   ? 0.1940 0.1995 0.2725 0.0145  0.0432  0.0423  14  ASN   C C   
1140 O O   . ASN   B 8   ? 0.1860 0.1937 0.2713 0.0150  0.0441  0.0426  14  ASN   C O   
1141 C CB  . ASN   B 8   ? 0.2273 0.2327 0.3176 0.0165  0.0545  0.0489  14  ASN   C CB  
1142 C CG  . ASN   B 8   ? 0.3100 0.3164 0.4099 0.0152  0.0578  0.0538  14  ASN   C CG  
1143 O OD1 . ASN   B 8   ? 0.3387 0.3498 0.4526 0.0120  0.0553  0.0566  14  ASN   C OD1 
1144 N ND2 . ASN   B 8   ? 0.3398 0.3419 0.4325 0.0175  0.0631  0.0548  14  ASN   C ND2 
1145 N N   . TYR   B 9   ? 0.1749 0.1788 0.2442 0.0137  0.0385  0.0392  15  TYR   C N   
1146 C CA  . TYR   B 9   ? 0.1763 0.1810 0.2431 0.0136  0.0346  0.0360  15  TYR   C CA  
1147 C C   . TYR   B 9   ? 0.1696 0.1765 0.2373 0.0104  0.0285  0.0361  15  TYR   C C   
1148 O O   . TYR   B 9   ? 0.1828 0.1885 0.2471 0.0091  0.0267  0.0364  15  TYR   C O   
1149 C CB  . TYR   B 9   ? 0.1848 0.1855 0.2393 0.0163  0.0348  0.0316  15  TYR   C CB  
1150 C CG  . TYR   B 9   ? 0.2157 0.2132 0.2664 0.0200  0.0404  0.0307  15  TYR   C CG  
1151 C CD1 . TYR   B 9   ? 0.2320 0.2304 0.2885 0.0213  0.0430  0.0304  15  TYR   C CD1 
1152 C CD2 . TYR   B 9   ? 0.2521 0.2453 0.2924 0.0227  0.0432  0.0299  15  TYR   C CD2 
1153 C CE1 . TYR   B 9   ? 0.2690 0.2638 0.3210 0.0251  0.0484  0.0293  15  TYR   C CE1 
1154 C CE2 . TYR   B 9   ? 0.2795 0.2691 0.3144 0.0267  0.0484  0.0289  15  TYR   C CE2 
1155 C CZ  . TYR   B 9   ? 0.3048 0.2950 0.3451 0.0279  0.0510  0.0282  15  TYR   C CZ  
1156 O OH  . TYR   B 9   ? 0.3704 0.3564 0.4044 0.0322  0.0564  0.0268  15  TYR   C OH  
1157 N N   . ARG   B 10  ? 0.1499 0.1593 0.2213 0.0095  0.0255  0.0357  16  ARG   C N   
1158 C CA  . ARG   B 10  ? 0.1485 0.1594 0.2188 0.0073  0.0202  0.0354  16  ARG   C CA  
1159 C C   . ARG   B 10  ? 0.1516 0.1615 0.2168 0.0086  0.0193  0.0322  16  ARG   C C   
1160 O O   . ARG   B 10  ? 0.1488 0.1595 0.2182 0.0096  0.0209  0.0319  16  ARG   C O   
1161 C CB  . ARG   B 10  ? 0.1659 0.1809 0.2461 0.0054  0.0176  0.0386  16  ARG   C CB  
1162 C CG  . ARG   B 10  ? 0.1548 0.1710 0.2328 0.0041  0.0127  0.0385  16  ARG   C CG  
1163 C CD  . ARG   B 10  ? 0.1476 0.1674 0.2345 0.0025  0.0097  0.0420  16  ARG   C CD  
1164 N NE  . ARG   B 10  ? 0.1741 0.1954 0.2611 0.0027  0.0073  0.0427  16  ARG   C NE  
1165 C CZ  . ARG   B 10  ? 0.2063 0.2274 0.2882 0.0018  0.0031  0.0428  16  ARG   C CZ  
1166 N NH1 . ARG   B 10  ? 0.2257 0.2451 0.3017 0.0005  0.0005  0.0416  16  ARG   C NH1 
1167 N NH2 . ARG   B 10  ? 0.2024 0.2247 0.2846 0.0024  0.0018  0.0441  16  ARG   C NH2 
1168 N N   . VAL   B 11  ? 0.1363 0.1445 0.1937 0.0084  0.0170  0.0299  17  VAL   C N   
1169 C CA  . VAL   B 11  ? 0.1392 0.1467 0.1932 0.0094  0.0160  0.0270  17  VAL   C CA  
1170 C C   . VAL   B 11  ? 0.1438 0.1532 0.1986 0.0077  0.0127  0.0280  17  VAL   C C   
1171 O O   . VAL   B 11  ? 0.1517 0.1606 0.2025 0.0066  0.0105  0.0284  17  VAL   C O   
1172 C CB  . VAL   B 11  ? 0.1591 0.1636 0.2041 0.0109  0.0160  0.0237  17  VAL   C CB  
1173 C CG1 . VAL   B 11  ? 0.1789 0.1831 0.2229 0.0119  0.0150  0.0204  17  VAL   C CG1 
1174 C CG2 . VAL   B 11  ? 0.1795 0.1814 0.2212 0.0128  0.0194  0.0234  17  VAL   C CG2 
1175 N N   . VAL   B 12  ? 0.1406 0.1516 0.2002 0.0078  0.0127  0.0284  18  VAL   C N   
1176 C CA  A VAL   B 12  ? 0.1327 0.1452 0.1925 0.0068  0.0102  0.0300  18  VAL   C CA  
1177 C CA  B VAL   B 12  ? 0.1580 0.1706 0.2182 0.0067  0.0103  0.0301  18  VAL   C CA  
1178 C C   . VAL   B 12  ? 0.1471 0.1595 0.2083 0.0076  0.0109  0.0284  18  VAL   C C   
1179 O O   . VAL   B 12  ? 0.1512 0.1628 0.2149 0.0087  0.0127  0.0262  18  VAL   C O   
1180 C CB  A VAL   B 12  ? 0.1229 0.1380 0.1891 0.0058  0.0092  0.0339  18  VAL   C CB  
1181 C CB  B VAL   B 12  ? 0.1969 0.2121 0.2645 0.0060  0.0097  0.0340  18  VAL   C CB  
1182 C CG1 A VAL   B 12  ? 0.1273 0.1428 0.1932 0.0045  0.0073  0.0356  18  VAL   C CG1 
1183 C CG1 B VAL   B 12  ? 0.2042 0.2205 0.2701 0.0051  0.0067  0.0363  18  VAL   C CG1 
1184 C CG2 A VAL   B 12  ? 0.0953 0.1115 0.1697 0.0067  0.0117  0.0349  18  VAL   C CG2 
1185 C CG2 B VAL   B 12  ? 0.2276 0.2436 0.2987 0.0053  0.0100  0.0357  18  VAL   C CG2 
1186 N N   . ASN   B 13  ? 0.1362 0.1492 0.1961 0.0071  0.0096  0.0297  19  ASN   C N   
1187 C CA  . ASN   B 13  ? 0.1290 0.1424 0.1925 0.0077  0.0107  0.0291  19  ASN   C CA  
1188 C C   . ASN   B 13  ? 0.1262 0.1408 0.1984 0.0079  0.0122  0.0313  19  ASN   C C   
1189 O O   . ASN   B 13  ? 0.1360 0.1520 0.2102 0.0074  0.0114  0.0348  19  ASN   C O   
1190 C CB  . ASN   B 13  ? 0.1453 0.1591 0.2062 0.0074  0.0100  0.0313  19  ASN   C CB  
1191 C CG  . ASN   B 13  ? 0.1409 0.1533 0.1940 0.0075  0.0089  0.0292  19  ASN   C CG  
1192 O OD1 . ASN   B 13  ? 0.1573 0.1689 0.2046 0.0070  0.0072  0.0298  19  ASN   C OD1 
1193 N ND2 . ASN   B 13  ? 0.1436 0.1556 0.1974 0.0082  0.0098  0.0266  19  ASN   C ND2 
1194 N N   . ARG   B 14  ? 0.1271 0.1410 0.2045 0.0086  0.0139  0.0291  20  ARG   C N   
1195 C CA  . ARG   B 14  ? 0.1273 0.1418 0.2133 0.0090  0.0156  0.0310  20  ARG   C CA  
1196 C C   . ARG   B 14  ? 0.1381 0.1544 0.2275 0.0086  0.0154  0.0359  20  ARG   C C   
1197 O O   . ARG   B 14  ? 0.1454 0.1630 0.2396 0.0087  0.0155  0.0392  20  ARG   C O   
1198 C CB  . ARG   B 14  ? 0.1305 0.1433 0.2215 0.0097  0.0171  0.0274  20  ARG   C CB  
1199 C CG  . ARG   B 14  ? 0.1334 0.1461 0.2334 0.0104  0.0192  0.0285  20  ARG   C CG  
1200 C CD  . ARG   B 14  ? 0.1457 0.1561 0.2504 0.0110  0.0201  0.0242  20  ARG   C CD  
1201 N NE  . ARG   B 14  ? 0.1538 0.1628 0.2663 0.0119  0.0222  0.0239  20  ARG   C NE  
1202 C CZ  . ARG   B 14  ? 0.1566 0.1661 0.2782 0.0117  0.0236  0.0272  20  ARG   C CZ  
1203 N NH1 . ARG   B 14  ? 0.1648 0.1763 0.2877 0.0108  0.0232  0.0316  20  ARG   C NH1 
1204 N NH2 . ARG   B 14  ? 0.1480 0.1556 0.2769 0.0127  0.0257  0.0262  20  ARG   C NH2 
1205 N N   . HIS   B 15  ? 0.1312 0.1475 0.2175 0.0084  0.0150  0.0367  21  HIS   C N   
1206 C CA  . HIS   B 15  ? 0.1390 0.1563 0.2270 0.0086  0.0152  0.0417  21  HIS   C CA  
1207 C C   . HIS   B 15  ? 0.1559 0.1742 0.2385 0.0084  0.0126  0.0451  21  HIS   C C   
1208 O O   . HIS   B 15  ? 0.1752 0.1944 0.2590 0.0089  0.0123  0.0495  21  HIS   C O   
1209 C CB  . HIS   B 15  ? 0.1450 0.1617 0.2319 0.0088  0.0166  0.0421  21  HIS   C CB  
1210 C CG  . HIS   B 15  ? 0.1515 0.1677 0.2286 0.0087  0.0152  0.0411  21  HIS   C CG  
1211 N ND1 . HIS   B 15  ? 0.1679 0.1834 0.2419 0.0085  0.0147  0.0366  21  HIS   C ND1 
1212 C CD2 . HIS   B 15  ? 0.1711 0.1872 0.2409 0.0092  0.0143  0.0441  21  HIS   C CD2 
1213 C CE1 . HIS   B 15  ? 0.1815 0.1964 0.2471 0.0087  0.0137  0.0370  21  HIS   C CE1 
1214 N NE2 . HIS   B 15  ? 0.1765 0.1915 0.2390 0.0091  0.0135  0.0413  21  HIS   C NE2 
1215 N N   . LEU   B 16  ? 0.1421 0.1604 0.2194 0.0076  0.0105  0.0430  22  LEU   C N   
1216 C CA  . LEU   B 16  ? 0.1566 0.1758 0.2301 0.0071  0.0072  0.0455  22  LEU   C CA  
1217 C C   . LEU   B 16  ? 0.1644 0.1851 0.2440 0.0067  0.0067  0.0460  22  LEU   C C   
1218 O O   . LEU   B 16  ? 0.1734 0.1952 0.2518 0.0059  0.0036  0.0476  22  LEU   C O   
1219 C CB  . LEU   B 16  ? 0.1640 0.1817 0.2279 0.0065  0.0052  0.0433  22  LEU   C CB  
1220 C CG  . LEU   B 16  ? 0.1729 0.1891 0.2306 0.0072  0.0060  0.0432  22  LEU   C CG  
1221 C CD1 . LEU   B 16  ? 0.1785 0.1928 0.2270 0.0068  0.0042  0.0407  22  LEU   C CD1 
1222 C CD2 . LEU   B 16  ? 0.1675 0.1841 0.2237 0.0082  0.0054  0.0478  22  LEU   C CD2 
1223 N N   . ALA   B 17  ? 0.1621 0.1827 0.2485 0.0072  0.0097  0.0444  23  ALA   C N   
1224 C CA  . ALA   B 17  ? 0.1620 0.1839 0.2543 0.0071  0.0102  0.0450  23  ALA   C CA  
1225 C C   . ALA   B 17  ? 0.1661 0.1907 0.2648 0.0072  0.0084  0.0499  23  ALA   C C   
1226 O O   . ALA   B 17  ? 0.1794 0.2044 0.2805 0.0080  0.0085  0.0526  23  ALA   C O   
1227 C CB  . ALA   B 17  ? 0.1660 0.1865 0.2632 0.0082  0.0141  0.0424  23  ALA   C CB  
1228 N N   . THR   B 18  ? 0.1694 0.1959 0.2717 0.0066  0.0069  0.0511  24  THR   C N   
1229 C CA  . THR   B 18  ? 0.1655 0.1951 0.2748 0.0066  0.0043  0.0557  24  THR   C CA  
1230 C C   . THR   B 18  ? 0.1671 0.1980 0.2878 0.0078  0.0079  0.0570  24  THR   C C   
1231 O O   . THR   B 18  ? 0.1741 0.2032 0.2960 0.0085  0.0122  0.0539  24  THR   C O   
1232 C CB  . THR   B 18  ? 0.1785 0.2097 0.2876 0.0050  0.0005  0.0562  24  THR   C CB  
1233 O OG1 . THR   B 18  ? 0.1841 0.2152 0.2972 0.0047  0.0035  0.0543  24  THR   C OG1 
1234 C CG2 . THR   B 18  ? 0.1935 0.2228 0.2913 0.0039  -0.0031 0.0544  24  THR   C CG2 
1235 N N   . HIS   B 19  ? 0.1654 0.1994 0.2946 0.0083  0.0060  0.0615  25  HIS   C N   
1236 C CA  . HIS   B 19  ? 0.1743 0.2098 0.3153 0.0096  0.0094  0.0630  25  HIS   C CA  
1237 C C   . HIS   B 19  ? 0.1676 0.2034 0.3114 0.0091  0.0119  0.0609  25  HIS   C C   
1238 O O   . HIS   B 19  ? 0.1862 0.2206 0.3341 0.0105  0.0170  0.0594  25  HIS   C O   
1239 C CB  . HIS   B 19  ? 0.1885 0.2279 0.3385 0.0101  0.0060  0.0685  25  HIS   C CB  
1240 C CG  . HIS   B 19  ? 0.2188 0.2604 0.3823 0.0114  0.0094  0.0704  25  HIS   C CG  
1241 N ND1 . HIS   B 19  ? 0.2553 0.2953 0.4245 0.0133  0.0142  0.0704  25  HIS   C ND1 
1242 C CD2 . HIS   B 19  ? 0.2430 0.2879 0.4153 0.0110  0.0090  0.0719  25  HIS   C CD2 
1243 C CE1 . HIS   B 19  ? 0.2563 0.2986 0.4370 0.0143  0.0166  0.0721  25  HIS   C CE1 
1244 N NE2 . HIS   B 19  ? 0.2493 0.2948 0.4326 0.0129  0.0139  0.0731  25  HIS   C NE2 
1245 N N   . ASN   B 20  ? 0.1645 0.2016 0.3059 0.0074  0.0087  0.0609  26  ASN   C N   
1246 C CA  . ASN   B 20  ? 0.1733 0.2104 0.3179 0.0070  0.0117  0.0597  26  ASN   C CA  
1247 C C   . ASN   B 20  ? 0.1674 0.2003 0.3038 0.0079  0.0164  0.0551  26  ASN   C C   
1248 O O   . ASN   B 20  ? 0.1604 0.1923 0.3000 0.0092  0.0213  0.0541  26  ASN   C O   
1249 C CB  . ASN   B 20  ? 0.1894 0.2283 0.3335 0.0047  0.0072  0.0604  26  ASN   C CB  
1250 C CG  . ASN   B 20  ? 0.2777 0.3169 0.4275 0.0045  0.0111  0.0601  26  ASN   C CG  
1251 O OD1 . ASN   B 20  ? 0.3175 0.3597 0.4797 0.0051  0.0133  0.0630  26  ASN   C OD1 
1252 N ND2 . ASN   B 20  ? 0.2967 0.3327 0.4378 0.0038  0.0126  0.0571  26  ASN   C ND2 
1253 N N   . ASP   B 21  ? 0.1556 0.1857 0.2810 0.0075  0.0149  0.0522  27  ASP   C N   
1254 C CA  . ASP   B 21  ? 0.1567 0.1829 0.2746 0.0085  0.0184  0.0477  27  ASP   C CA  
1255 C C   . ASP   B 21  ? 0.1597 0.1844 0.2822 0.0107  0.0229  0.0465  27  ASP   C C   
1256 O O   . ASP   B 21  ? 0.1704 0.1926 0.2911 0.0121  0.0270  0.0439  27  ASP   C O   
1257 C CB  . ASP   B 21  ? 0.1583 0.1823 0.2660 0.0078  0.0160  0.0453  27  ASP   C CB  
1258 C CG  . ASP   B 21  ? 0.1634 0.1873 0.2641 0.0061  0.0125  0.0449  27  ASP   C CG  
1259 O OD1 . ASP   B 21  ? 0.1730 0.1966 0.2736 0.0056  0.0133  0.0446  27  ASP   C OD1 
1260 O OD2 . ASP   B 21  ? 0.1728 0.1966 0.2683 0.0054  0.0092  0.0452  27  ASP   C OD2 
1261 N N   . TRP   B 22  ? 0.1548 0.1804 0.2826 0.0112  0.0223  0.0484  28  TRP   C N   
1262 C CA  . TRP   B 22  ? 0.1549 0.1785 0.2877 0.0132  0.0264  0.0470  28  TRP   C CA  
1263 C C   . TRP   B 22  ? 0.1432 0.1679 0.2848 0.0147  0.0302  0.0486  28  TRP   C C   
1264 O O   . TRP   B 22  ? 0.1483 0.1700 0.2906 0.0167  0.0347  0.0458  28  TRP   C O   
1265 C CB  . TRP   B 22  ? 0.1473 0.1716 0.2848 0.0133  0.0250  0.0493  28  TRP   C CB  
1266 C CG  . TRP   B 22  ? 0.1460 0.1679 0.2762 0.0127  0.0237  0.0466  28  TRP   C CG  
1267 C CD1 . TRP   B 22  ? 0.1519 0.1747 0.2767 0.0113  0.0201  0.0482  28  TRP   C CD1 
1268 C CD2 . TRP   B 22  ? 0.1420 0.1602 0.2700 0.0135  0.0259  0.0418  28  TRP   C CD2 
1269 N NE1 . TRP   B 22  ? 0.1647 0.1851 0.2855 0.0113  0.0207  0.0452  28  TRP   C NE1 
1270 C CE2 . TRP   B 22  ? 0.1593 0.1770 0.2824 0.0124  0.0237  0.0411  28  TRP   C CE2 
1271 C CE3 . TRP   B 22  ? 0.1714 0.1865 0.3016 0.0152  0.0295  0.0380  28  TRP   C CE3 
1272 C CZ2 . TRP   B 22  ? 0.1647 0.1794 0.2866 0.0127  0.0246  0.0369  28  TRP   C CZ2 
1273 C CZ3 . TRP   B 22  ? 0.1806 0.1922 0.3082 0.0155  0.0298  0.0333  28  TRP   C CZ3 
1274 C CH2 . TRP   B 22  ? 0.1709 0.1828 0.2954 0.0141  0.0272  0.0329  28  TRP   C CH2 
1275 N N   . ALA   B 23  ? 0.1388 0.1677 0.2874 0.0138  0.0284  0.0530  29  ALA   C N   
1276 C CA  . ALA   B 23  ? 0.1485 0.1792 0.3074 0.0151  0.0323  0.0553  29  ALA   C CA  
1277 C C   . ALA   B 23  ? 0.1757 0.2044 0.3305 0.0158  0.0364  0.0530  29  ALA   C C   
1278 O O   . ALA   B 23  ? 0.1861 0.2153 0.3484 0.0175  0.0413  0.0543  29  ALA   C O   
1279 C CB  . ALA   B 23  ? 0.1482 0.1843 0.3170 0.0138  0.0283  0.0607  29  ALA   C CB  
1280 N N   . ASN   B 24  ? 0.1703 0.1967 0.3135 0.0146  0.0348  0.0501  30  ASN   C N   
1281 C CA  . ASN   B 24  ? 0.1645 0.1885 0.3018 0.0154  0.0385  0.0482  30  ASN   C CA  
1282 C C   . ASN   B 24  ? 0.1747 0.1936 0.2983 0.0164  0.0388  0.0427  30  ASN   C C   
1283 O O   . ASN   B 24  ? 0.1735 0.1905 0.2884 0.0160  0.0386  0.0410  30  ASN   C O   
1284 C CB  . ASN   B 24  ? 0.1898 0.2165 0.3280 0.0129  0.0353  0.0507  30  ASN   C CB  
1285 C CG  . ASN   B 24  ? 0.1921 0.2237 0.3448 0.0121  0.0350  0.0556  30  ASN   C CG  
1286 O OD1 . ASN   B 24  ? 0.2184 0.2505 0.3781 0.0135  0.0403  0.0572  30  ASN   C OD1 
1287 N ND2 . ASN   B 24  ? 0.1908 0.2260 0.3483 0.0102  0.0290  0.0581  30  ASN   C ND2 
1288 N N   . LEU   B 25  ? 0.1730 0.1898 0.2957 0.0176  0.0391  0.0400  31  LEU   C N   
1289 C CA  . LEU   B 25  ? 0.1694 0.1820 0.2811 0.0182  0.0383  0.0348  31  LEU   C CA  
1290 C C   . LEU   B 25  ? 0.1899 0.1980 0.2931 0.0209  0.0423  0.0311  31  LEU   C C   
1291 O O   . LEU   B 25  ? 0.1997 0.2062 0.3059 0.0233  0.0473  0.0311  31  LEU   C O   
1292 C CB  . LEU   B 25  ? 0.1757 0.1872 0.2914 0.0188  0.0378  0.0331  31  LEU   C CB  
1293 C CG  . LEU   B 25  ? 0.1885 0.1964 0.2959 0.0191  0.0361  0.0279  31  LEU   C CG  
1294 C CD1 . LEU   B 25  ? 0.1853 0.1950 0.2877 0.0166  0.0314  0.0285  31  LEU   C CD1 
1295 C CD2 . LEU   B 25  ? 0.2083 0.2146 0.3218 0.0198  0.0365  0.0262  31  LEU   C CD2 
1296 N N   . VAL   B 26  ? 0.1823 0.1881 0.2744 0.0206  0.0402  0.0280  32  VAL   C N   
1297 C CA  . VAL   B 26  ? 0.1889 0.1897 0.2703 0.0235  0.0430  0.0241  32  VAL   C CA  
1298 C C   . VAL   B 26  ? 0.2069 0.2044 0.2825 0.0244  0.0405  0.0184  32  VAL   C C   
1299 O O   . VAL   B 26  ? 0.2275 0.2208 0.2992 0.0273  0.0430  0.0145  32  VAL   C O   
1300 C CB  . VAL   B 26  ? 0.1989 0.1994 0.2724 0.0229  0.0424  0.0250  32  VAL   C CB  
1301 C CG1 . VAL   B 26  ? 0.2276 0.2227 0.2883 0.0262  0.0446  0.0209  32  VAL   C CG1 
1302 C CG2 . VAL   B 26  ? 0.2045 0.2079 0.2851 0.0221  0.0452  0.0303  32  VAL   C CG2 
1303 N N   . TRP   B 27  ? 0.1917 0.1910 0.2672 0.0220  0.0356  0.0178  33  TRP   C N   
1304 C CA  . TRP   B 27  ? 0.1885 0.1853 0.2603 0.0225  0.0328  0.0127  33  TRP   C CA  
1305 C C   . TRP   B 27  ? 0.1929 0.1930 0.2693 0.0195  0.0287  0.0142  33  TRP   C C   
1306 O O   . TRP   B 27  ? 0.1845 0.1876 0.2610 0.0176  0.0272  0.0179  33  TRP   C O   
1307 C CB  . TRP   B 27  ? 0.2112 0.2046 0.2703 0.0242  0.0318  0.0090  33  TRP   C CB  
1308 C CG  . TRP   B 27  ? 0.2246 0.2163 0.2799 0.0243  0.0277  0.0039  33  TRP   C CG  
1309 C CD1 . TRP   B 27  ? 0.2497 0.2377 0.3036 0.0263  0.0271  -0.0015 33  TRP   C CD1 
1310 C CD2 . TRP   B 27  ? 0.2184 0.2119 0.2715 0.0225  0.0235  0.0037  33  TRP   C CD2 
1311 N NE1 . TRP   B 27  ? 0.2592 0.2470 0.3111 0.0256  0.0224  -0.0051 33  TRP   C NE1 
1312 C CE2 . TRP   B 27  ? 0.2350 0.2263 0.2865 0.0234  0.0204  -0.0018 33  TRP   C CE2 
1313 C CE3 . TRP   B 27  ? 0.2127 0.2094 0.2655 0.0202  0.0219  0.0073  33  TRP   C CE3 
1314 C CZ2 . TRP   B 27  ? 0.2325 0.2252 0.2830 0.0221  0.0163  -0.0031 33  TRP   C CZ2 
1315 C CZ3 . TRP   B 27  ? 0.2263 0.2237 0.2767 0.0193  0.0182  0.0057  33  TRP   C CZ3 
1316 C CH2 . TRP   B 27  ? 0.2300 0.2257 0.2799 0.0202  0.0157  0.0008  33  TRP   C CH2 
1317 N N   . GLU   B 28  ? 0.1773 0.1765 0.2578 0.0193  0.0272  0.0115  34  GLU   C N   
1318 C CA  . GLU   B 28  ? 0.1785 0.1805 0.2630 0.0170  0.0242  0.0130  34  GLU   C CA  
1319 C C   . GLU   B 28  ? 0.1785 0.1783 0.2637 0.0173  0.0222  0.0081  34  GLU   C C   
1320 O O   . GLU   B 28  ? 0.1784 0.1748 0.2649 0.0190  0.0232  0.0041  34  GLU   C O   
1321 C CB  . GLU   B 28  ? 0.1778 0.1827 0.2723 0.0157  0.0250  0.0181  34  GLU   C CB  
1322 C CG  . GLU   B 28  ? 0.1878 0.1913 0.2907 0.0169  0.0277  0.0177  34  GLU   C CG  
1323 C CD  . GLU   B 28  ? 0.2319 0.2336 0.3405 0.0167  0.0270  0.0149  34  GLU   C CD  
1324 O OE1 . GLU   B 28  ? 0.2481 0.2468 0.3611 0.0182  0.0290  0.0122  34  GLU   C OE1 
1325 O OE2 . GLU   B 28  ? 0.1972 0.2004 0.3068 0.0151  0.0247  0.0155  34  GLU   C OE2 
1326 N N   . ASP   B 29  ? 0.1601 0.1616 0.2453 0.0157  0.0194  0.0082  35  ASP   C N   
1327 C CA  . ASP   B 29  ? 0.1667 0.1669 0.2549 0.0157  0.0173  0.0039  35  ASP   C CA  
1328 C C   . ASP   B 29  ? 0.1624 0.1657 0.2564 0.0135  0.0163  0.0072  35  ASP   C C   
1329 O O   . ASP   B 29  ? 0.1683 0.1734 0.2572 0.0128  0.0150  0.0088  35  ASP   C O   
1330 C CB  . ASP   B 29  ? 0.1917 0.1897 0.2703 0.0171  0.0148  -0.0009 35  ASP   C CB  
1331 C CG  . ASP   B 29  ? 0.2497 0.2465 0.3318 0.0172  0.0117  -0.0061 35  ASP   C CG  
1332 O OD1 . ASP   B 29  ? 0.2602 0.2591 0.3513 0.0153  0.0111  -0.0047 35  ASP   C OD1 
1333 O OD2 . ASP   B 29  ? 0.2818 0.2754 0.3575 0.0192  0.0097  -0.0113 35  ASP   C OD2 
1334 N N   . SER   B 30  ? 0.1592 0.1629 0.2638 0.0128  0.0174  0.0086  36  SER   C N   
1335 C CA  A SER   B 30  ? 0.1561 0.1624 0.2665 0.0112  0.0175  0.0123  36  SER   C CA  
1336 C CA  B SER   B 30  ? 0.1620 0.1683 0.2718 0.0112  0.0175  0.0124  36  SER   C CA  
1337 C C   . SER   B 30  ? 0.1609 0.1677 0.2706 0.0107  0.0152  0.0093  36  SER   C C   
1338 O O   . SER   B 30  ? 0.1564 0.1654 0.2649 0.0099  0.0152  0.0125  36  SER   C O   
1339 C CB  A SER   B 30  ? 0.1602 0.1660 0.2826 0.0107  0.0195  0.0141  36  SER   C CB  
1340 C CB  B SER   B 30  ? 0.1843 0.1905 0.3057 0.0108  0.0197  0.0149  36  SER   C CB  
1341 O OG  A SER   B 30  ? 0.1479 0.1555 0.2763 0.0096  0.0200  0.0170  36  SER   C OG  
1342 O OG  B SER   B 30  ? 0.2115 0.2148 0.3393 0.0112  0.0192  0.0097  36  SER   C OG  
1343 N N   . SER   B 31  ? 0.1688 0.1733 0.2792 0.0114  0.0130  0.0032  37  SER   C N   
1344 C CA  . SER   B 31  ? 0.1752 0.1805 0.2867 0.0111  0.0103  0.0002  37  SER   C CA  
1345 C C   . SER   B 31  ? 0.1661 0.1727 0.2668 0.0115  0.0089  0.0010  37  SER   C C   
1346 O O   . SER   B 31  ? 0.1821 0.1905 0.2845 0.0110  0.0076  0.0007  37  SER   C O   
1347 C CB  . SER   B 31  ? 0.2298 0.2323 0.3433 0.0120  0.0072  -0.0069 37  SER   C CB  
1348 O OG  . SER   B 31  ? 0.2965 0.2966 0.3981 0.0140  0.0055  -0.0104 37  SER   C OG  
1349 N N   . ARG   B 32  ? 0.1524 0.1582 0.2432 0.0124  0.0096  0.0021  38  ARG   C N   
1350 C CA  . ARG   B 32  ? 0.1501 0.1566 0.2310 0.0127  0.0085  0.0030  38  ARG   C CA  
1351 C C   . ARG   B 32  ? 0.1489 0.1574 0.2277 0.0115  0.0104  0.0088  38  ARG   C C   
1352 O O   . ARG   B 32  ? 0.1474 0.1562 0.2188 0.0116  0.0096  0.0098  38  ARG   C O   
1353 C CB  . ARG   B 32  ? 0.1726 0.1764 0.2437 0.0145  0.0081  0.0006  38  ARG   C CB  
1354 C CG  . ARG   B 32  ? 0.1964 0.1975 0.2657 0.0163  0.0055  -0.0056 38  ARG   C CG  
1355 C CD  . ARG   B 32  ? 0.1761 0.1739 0.2343 0.0186  0.0058  -0.0074 38  ARG   C CD  
1356 N NE  . ARG   B 32  ? 0.1699 0.1681 0.2191 0.0191  0.0052  -0.0058 38  ARG   C NE  
1357 C CZ  . ARG   B 32  ? 0.2090 0.2044 0.2480 0.0215  0.0043  -0.0080 38  ARG   C CZ  
1358 N NH1 . ARG   B 32  ? 0.2157 0.2075 0.2507 0.0239  0.0037  -0.0122 38  ARG   C NH1 
1359 N NH2 . ARG   B 32  ? 0.1861 0.1817 0.2183 0.0218  0.0038  -0.0062 38  ARG   C NH2 
1360 N N   . ASP   B 33  ? 0.1363 0.1458 0.2213 0.0107  0.0125  0.0125  39  ASP   C N   
1361 C CA  . ASP   B 33  ? 0.1331 0.1442 0.2157 0.0099  0.0135  0.0177  39  ASP   C CA  
1362 C C   . ASP   B 33  ? 0.1391 0.1495 0.2140 0.0102  0.0132  0.0182  39  ASP   C C   
1363 O O   . ASP   B 33  ? 0.1402 0.1514 0.2101 0.0096  0.0126  0.0208  39  ASP   C O   
1364 C CB  . ASP   B 33  ? 0.1281 0.1406 0.2089 0.0094  0.0133  0.0200  39  ASP   C CB  
1365 C CG  . ASP   B 33  ? 0.1589 0.1724 0.2366 0.0088  0.0139  0.0251  39  ASP   C CG  
1366 O OD1 . ASP   B 33  ? 0.1657 0.1798 0.2477 0.0086  0.0149  0.0280  39  ASP   C OD1 
1367 O OD2 . ASP   B 33  ? 0.1370 0.1507 0.2082 0.0087  0.0132  0.0261  39  ASP   C OD2 
1368 N N   . LEU   B 34  ? 0.1342 0.1429 0.2084 0.0113  0.0138  0.0157  40  LEU   C N   
1369 C CA  . LEU   B 34  ? 0.1399 0.1479 0.2081 0.0117  0.0143  0.0166  40  LEU   C CA  
1370 C C   . LEU   B 34  ? 0.1429 0.1509 0.2158 0.0121  0.0166  0.0183  40  LEU   C C   
1371 O O   . LEU   B 34  ? 0.1429 0.1498 0.2212 0.0129  0.0178  0.0166  40  LEU   C O   
1372 C CB  . LEU   B 34  ? 0.1491 0.1545 0.2097 0.0133  0.0136  0.0125  40  LEU   C CB  
1373 C CG  . LEU   B 34  ? 0.1676 0.1729 0.2220 0.0132  0.0114  0.0113  40  LEU   C CG  
1374 C CD1 . LEU   B 34  ? 0.1721 0.1745 0.2186 0.0153  0.0107  0.0077  40  LEU   C CD1 
1375 C CD2 . LEU   B 34  ? 0.1664 0.1729 0.2176 0.0119  0.0111  0.0150  40  LEU   C CD2 
1376 N N   . LEU   B 35  ? 0.1363 0.1453 0.2078 0.0116  0.0171  0.0215  41  LEU   C N   
1377 C CA  . LEU   B 35  ? 0.1386 0.1480 0.2151 0.0122  0.0196  0.0234  41  LEU   C CA  
1378 C C   . LEU   B 35  ? 0.1495 0.1586 0.2214 0.0122  0.0202  0.0246  41  LEU   C C   
1379 O O   . LEU   B 35  ? 0.1636 0.1735 0.2316 0.0109  0.0181  0.0259  41  LEU   C O   
1380 C CB  . LEU   B 35  ? 0.1305 0.1429 0.2153 0.0110  0.0193  0.0279  41  LEU   C CB  
1381 C CG  . LEU   B 35  ? 0.1365 0.1497 0.2283 0.0118  0.0218  0.0303  41  LEU   C CG  
1382 C CD1 . LEU   B 35  ? 0.1536 0.1682 0.2545 0.0117  0.0222  0.0329  41  LEU   C CD1 
1383 C CD2 . LEU   B 35  ? 0.1428 0.1583 0.2348 0.0107  0.0210  0.0338  41  LEU   C CD2 
1384 N N   . VAL   B 36  ? 0.1451 0.1528 0.2175 0.0139  0.0234  0.0240  42  VAL   C N   
1385 C CA  . VAL   B 36  ? 0.1443 0.1515 0.2142 0.0142  0.0253  0.0257  42  VAL   C CA  
1386 C C   . VAL   B 36  ? 0.1505 0.1596 0.2293 0.0144  0.0282  0.0290  42  VAL   C C   
1387 O O   . VAL   B 36  ? 0.1707 0.1789 0.2535 0.0160  0.0308  0.0279  42  VAL   C O   
1388 C CB  . VAL   B 36  ? 0.1652 0.1684 0.2259 0.0166  0.0273  0.0222  42  VAL   C CB  
1389 C CG1 . VAL   B 36  ? 0.1787 0.1813 0.2376 0.0170  0.0301  0.0248  42  VAL   C CG1 
1390 C CG2 . VAL   B 36  ? 0.1767 0.1785 0.2296 0.0165  0.0239  0.0190  42  VAL   C CG2 
1391 N N   . SER   B 37  ? 0.1398 0.1515 0.2227 0.0127  0.0276  0.0328  43  SER   C N   
1392 C CA  . SER   B 37  ? 0.1478 0.1620 0.2410 0.0128  0.0301  0.0365  43  SER   C CA  
1393 C C   . SER   B 37  ? 0.1683 0.1819 0.2610 0.0130  0.0328  0.0381  43  SER   C C   
1394 O O   . SER   B 37  ? 0.1697 0.1814 0.2547 0.0125  0.0319  0.0370  43  SER   C O   
1395 C CB  . SER   B 37  ? 0.1538 0.1722 0.2550 0.0105  0.0262  0.0401  43  SER   C CB  
1396 O OG  . SER   B 37  ? 0.1718 0.1911 0.2695 0.0083  0.0220  0.0410  43  SER   C OG  
1397 N N   . SER   B 38  ? 0.1649 0.1801 0.2666 0.0139  0.0368  0.0410  44  SER   C N   
1398 C CA  . SER   B 38  ? 0.1836 0.1984 0.2870 0.0141  0.0404  0.0432  44  SER   C CA  
1399 C C   . SER   B 38  ? 0.2090 0.2280 0.3215 0.0108  0.0368  0.0471  44  SER   C C   
1400 O O   . SER   B 38  ? 0.2146 0.2373 0.3344 0.0092  0.0328  0.0488  44  SER   C O   
1401 C CB  . SER   B 38  ? 0.2077 0.2219 0.3166 0.0170  0.0473  0.0444  44  SER   C CB  
1402 O OG  . SER   B 38  ? 0.2491 0.2675 0.3710 0.0164  0.0467  0.0472  44  SER   C OG  
1403 N N   . THR   B 39  ? 0.2095 0.2276 0.3213 0.0099  0.0378  0.0484  45  THR   C N   
1404 C CA  . THR   B 39  ? 0.2142 0.2356 0.3346 0.0067  0.0340  0.0514  45  THR   C CA  
1405 C C   . THR   B 39  ? 0.2426 0.2652 0.3737 0.0070  0.0393  0.0552  45  THR   C C   
1406 O O   . THR   B 39  ? 0.2401 0.2596 0.3672 0.0097  0.0461  0.0552  45  THR   C O   
1407 C CB  . THR   B 39  ? 0.2229 0.2417 0.3339 0.0049  0.0299  0.0495  45  THR   C CB  
1408 O OG1 . THR   B 39  ? 0.2397 0.2544 0.3434 0.0066  0.0347  0.0489  45  THR   C OG1 
1409 C CG2 . THR   B 39  ? 0.2214 0.2390 0.3221 0.0047  0.0253  0.0460  45  THR   C CG2 
1410 N N   . THR   B 40  ? 0.2603 0.2874 0.4047 0.0042  0.0361  0.0585  46  THR   C N   
1411 C CA  . THR   B 40  ? 0.2819 0.3107 0.4390 0.0039  0.0408  0.0625  46  THR   C CA  
1412 C C   . THR   B 40  ? 0.2867 0.3121 0.4391 0.0026  0.0414  0.0625  46  THR   C C   
1413 O O   . THR   B 40  ? 0.3026 0.3259 0.4564 0.0043  0.0485  0.0646  46  THR   C O   
1414 C CB  . THR   B 40  ? 0.3272 0.3623 0.5019 0.0015  0.0364  0.0658  46  THR   C CB  
1415 O OG1 . THR   B 40  ? 0.3787 0.4147 0.5514 -0.0018 0.0274  0.0645  46  THR   C OG1 
1416 C CG2 . THR   B 40  ? 0.3237 0.3617 0.5032 0.0032  0.0364  0.0664  46  THR   C CG2 
1417 N N   . ALA   B 41  ? 0.2729 0.2973 0.4191 0.0000  0.0343  0.0602  47  ALA   C N   
1418 C CA  . ALA   B 41  ? 0.2756 0.2965 0.4176 -0.0013 0.0344  0.0600  47  ALA   C CA  
1419 C C   . ALA   B 41  ? 0.2680 0.2832 0.3919 0.0012  0.0366  0.0567  47  ALA   C C   
1420 O O   . ALA   B 41  ? 0.2662 0.2807 0.3806 0.0025  0.0345  0.0536  47  ALA   C O   
1421 C CB  . ALA   B 41  ? 0.2881 0.3102 0.4328 -0.0052 0.0257  0.0590  47  ALA   C CB  
1422 N N   . GLN   B 42  ? 0.2672 0.2784 0.3869 0.0018  0.0405  0.0576  48  GLN   C N   
1423 C CA  . GLN   B 42  ? 0.2762 0.2822 0.3792 0.0043  0.0419  0.0547  48  GLN   C CA  
1424 C C   . GLN   B 42  ? 0.2658 0.2704 0.3616 0.0020  0.0347  0.0516  48  GLN   C C   
1425 O O   . GLN   B 42  ? 0.2788 0.2842 0.3813 -0.0012 0.0307  0.0524  48  GLN   C O   
1426 C CB  . GLN   B 42  ? 0.3297 0.3315 0.4303 0.0062  0.0490  0.0574  48  GLN   C CB  
1427 C CG  . GLN   B 42  ? 0.4464 0.4478 0.5480 0.0100  0.0573  0.0596  48  GLN   C CG  
1428 C CD  . GLN   B 42  ? 0.5879 0.5846 0.6851 0.0124  0.0645  0.0625  48  GLN   C CD  
1429 O OE1 . GLN   B 42  ? 0.6219 0.6192 0.7307 0.0108  0.0676  0.0668  48  GLN   C OE1 
1430 N NE2 . GLN   B 42  ? 0.6293 0.6210 0.7099 0.0164  0.0670  0.0603  48  GLN   C NE2 
1431 N N   . GLY   B 43  ? 0.2450 0.2473 0.3275 0.0039  0.0332  0.0479  49  GLY   C N   
1432 C CA  . GLY   B 43  ? 0.2387 0.2393 0.3131 0.0026  0.0275  0.0449  49  GLY   C CA  
1433 C C   . GLY   B 43  ? 0.2419 0.2374 0.3072 0.0039  0.0295  0.0444  49  GLY   C C   
1434 O O   . GLY   B 43  ? 0.2586 0.2517 0.3216 0.0065  0.0354  0.0462  49  GLY   C O   
1435 N N   . CYS   B 44  ? 0.2269 0.2206 0.2869 0.0026  0.0248  0.0422  50  CYS   C N   
1436 C CA  . CYS   B 44  ? 0.2398 0.2287 0.2925 0.0036  0.0263  0.0421  50  CYS   C CA  
1437 C C   . CYS   B 44  ? 0.2463 0.2328 0.2863 0.0056  0.0242  0.0386  50  CYS   C C   
1438 O O   . CYS   B 44  ? 0.2720 0.2544 0.3060 0.0065  0.0246  0.0385  50  CYS   C O   
1439 C CB  . CYS   B 44  ? 0.2486 0.2364 0.3081 0.0002  0.0234  0.0432  50  CYS   C CB  
1440 S SG  . CYS   B 44  ? 0.3425 0.3330 0.4193 -0.0021 0.0263  0.0478  50  CYS   C SG  
1441 N N   . ASP   B 45  ? 0.2071 0.1961 0.2441 0.0063  0.0218  0.0359  51  ASP   C N   
1442 C CA  . ASP   B 45  ? 0.2092 0.1965 0.2360 0.0081  0.0198  0.0327  51  ASP   C CA  
1443 C C   . ASP   B 45  ? 0.2234 0.2082 0.2428 0.0120  0.0237  0.0324  51  ASP   C C   
1444 O O   . ASP   B 45  ? 0.2405 0.2258 0.2620 0.0134  0.0276  0.0338  51  ASP   C O   
1445 C CB  . ASP   B 45  ? 0.2146 0.2054 0.2419 0.0076  0.0165  0.0303  51  ASP   C CB  
1446 C CG  . ASP   B 45  ? 0.2684 0.2609 0.2997 0.0046  0.0122  0.0302  51  ASP   C CG  
1447 O OD1 . ASP   B 45  ? 0.2613 0.2513 0.2915 0.0032  0.0104  0.0302  51  ASP   C OD1 
1448 O OD2 . ASP   B 45  ? 0.2240 0.2198 0.2591 0.0038  0.0105  0.0301  51  ASP   C OD2 
1449 N N   . THR   B 46  ? 0.2097 0.1916 0.2202 0.0139  0.0226  0.0306  52  THR   C N   
1450 C CA  . THR   B 46  ? 0.2111 0.1903 0.2128 0.0180  0.0249  0.0297  52  THR   C CA  
1451 C C   . THR   B 46  ? 0.2105 0.1914 0.2082 0.0191  0.0212  0.0256  52  THR   C C   
1452 O O   . THR   B 46  ? 0.2160 0.1976 0.2136 0.0177  0.0176  0.0240  52  THR   C O   
1453 C CB  . THR   B 46  ? 0.2427 0.2174 0.2379 0.0195  0.0256  0.0309  52  THR   C CB  
1454 O OG1 . THR   B 46  ? 0.2724 0.2454 0.2727 0.0184  0.0294  0.0350  52  THR   C OG1 
1455 C CG2 . THR   B 46  ? 0.2652 0.2370 0.2495 0.0241  0.0266  0.0296  52  THR   C CG2 
1456 N N   . ILE   B 47  ? 0.2023 0.1833 0.1968 0.0216  0.0223  0.0238  53  ILE   C N   
1457 C CA  . ILE   B 47  ? 0.1901 0.1724 0.1820 0.0226  0.0188  0.0198  53  ILE   C CA  
1458 C C   . ILE   B 47  ? 0.1869 0.1661 0.1693 0.0258  0.0173  0.0182  53  ILE   C C   
1459 O O   . ILE   B 47  ? 0.2069 0.1825 0.1823 0.0288  0.0200  0.0194  53  ILE   C O   
1460 C CB  . ILE   B 47  ? 0.2034 0.1867 0.1962 0.0240  0.0201  0.0180  53  ILE   C CB  
1461 C CG1 . ILE   B 47  ? 0.2077 0.1939 0.2101 0.0215  0.0222  0.0202  53  ILE   C CG1 
1462 C CG2 . ILE   B 47  ? 0.2126 0.1973 0.2048 0.0247  0.0161  0.0137  53  ILE   C CG2 
1463 C CD1 . ILE   B 47  ? 0.2211 0.2110 0.2307 0.0179  0.0187  0.0203  53  ILE   C CD1 
1464 N N   . ALA   B 48  ? 0.1771 0.1577 0.1594 0.0255  0.0133  0.0157  54  ALA   C N   
1465 C CA  . ALA   B 48  ? 0.1739 0.1522 0.1485 0.0287  0.0111  0.0140  54  ALA   C CA  
1466 C C   . ALA   B 48  ? 0.1846 0.1619 0.1538 0.0320  0.0103  0.0111  54  ALA   C C   
1467 O O   . ALA   B 48  ? 0.1920 0.1717 0.1659 0.0311  0.0096  0.0088  54  ALA   C O   
1468 C CB  . ALA   B 48  ? 0.1780 0.1587 0.1557 0.0276  0.0072  0.0120  54  ALA   C CB  
1469 N N   . ARG   B 49  ? 0.1939 0.1674 0.1533 0.0359  0.0103  0.0110  55  ARG   C N   
1470 C CA  . ARG   B 49  ? 0.1969 0.1687 0.1492 0.0396  0.0085  0.0076  55  ARG   C CA  
1471 C C   . ARG   B 49  ? 0.2068 0.1777 0.1537 0.0421  0.0039  0.0058  55  ARG   C C   
1472 O O   . ARG   B 49  ? 0.2351 0.2023 0.1737 0.0450  0.0048  0.0081  55  ARG   C O   
1473 C CB  . ARG   B 49  ? 0.2053 0.1728 0.1492 0.0426  0.0133  0.0096  55  ARG   C CB  
1474 C CG  . ARG   B 49  ? 0.1940 0.1628 0.1450 0.0401  0.0181  0.0118  55  ARG   C CG  
1475 C CD  . ARG   B 49  ? 0.2200 0.1919 0.1779 0.0385  0.0166  0.0083  55  ARG   C CD  
1476 N NE  . ARG   B 49  ? 0.2284 0.2016 0.1933 0.0364  0.0214  0.0111  55  ARG   C NE  
1477 C CZ  . ARG   B 49  ? 0.2331 0.2097 0.2071 0.0339  0.0210  0.0098  55  ARG   C CZ  
1478 N NH1 . ARG   B 49  ? 0.2144 0.1932 0.1917 0.0331  0.0165  0.0059  55  ARG   C NH1 
1479 N NH2 . ARG   B 49  ? 0.2310 0.2089 0.2118 0.0322  0.0252  0.0128  55  ARG   C NH2 
1480 N N   . CYS   B 50  ? 0.2048 0.1794 0.1579 0.0409  -0.0009 0.0023  56  CYS   C N   
1481 C CA  . CYS   B 50  ? 0.2076 0.1827 0.1595 0.0426  -0.0054 0.0009  56  CYS   C CA  
1482 C C   . CYS   B 50  ? 0.2144 0.1939 0.1752 0.0412  -0.0100 -0.0032 56  CYS   C C   
1483 O O   . CYS   B 50  ? 0.2120 0.1940 0.1798 0.0388  -0.0094 -0.0047 56  CYS   C O   
1484 C CB  . CYS   B 50  ? 0.2125 0.1878 0.1675 0.0406  -0.0036 0.0046  56  CYS   C CB  
1485 S SG  . CYS   B 50  ? 0.2082 0.1882 0.1761 0.0352  -0.0026 0.0049  56  CYS   C SG  
1486 N N   . ASP   B 51  ? 0.2131 0.1940 0.1749 0.0427  -0.0145 -0.0047 57  ASP   C N   
1487 C CA  . ASP   B 51  ? 0.2240 0.2095 0.1965 0.0412  -0.0183 -0.0079 57  ASP   C CA  
1488 C C   . ASP   B 51  ? 0.2233 0.2113 0.2023 0.0396  -0.0179 -0.0058 57  ASP   C C   
1489 O O   . ASP   B 51  ? 0.2348 0.2259 0.2207 0.0398  -0.0214 -0.0078 57  ASP   C O   
1490 C CB  . ASP   B 51  ? 0.2544 0.2399 0.2247 0.0445  -0.0246 -0.0124 57  ASP   C CB  
1491 C CG  . ASP   B 51  ? 0.3321 0.3156 0.2948 0.0483  -0.0276 -0.0117 57  ASP   C CG  
1492 O OD1 . ASP   B 51  ? 0.3283 0.3097 0.2867 0.0486  -0.0242 -0.0075 57  ASP   C OD1 
1493 O OD2 . ASP   B 51  ? 0.3959 0.3798 0.3575 0.0511  -0.0337 -0.0154 57  ASP   C OD2 
1494 N N   . CYS   B 52  ? 0.2073 0.1938 0.1848 0.0379  -0.0136 -0.0020 58  CYS   C N   
1495 C CA  . CYS   B 52  ? 0.1790 0.1670 0.1616 0.0364  -0.0127 -0.0003 58  CYS   C CA  
1496 C C   . CYS   B 52  ? 0.1799 0.1727 0.1738 0.0340  -0.0133 -0.0018 58  CYS   C C   
1497 O O   . CYS   B 52  ? 0.1947 0.1892 0.1928 0.0320  -0.0125 -0.0027 58  CYS   C O   
1498 C CB  . CYS   B 52  ? 0.1862 0.1717 0.1663 0.0344  -0.0083 0.0034  58  CYS   C CB  
1499 S SG  . CYS   B 52  ? 0.2134 0.1931 0.1827 0.0370  -0.0067 0.0064  58  CYS   C SG  
1500 N N   . GLN   B 53  ? 0.1756 0.1703 0.1744 0.0344  -0.0142 -0.0018 59  GLN   C N   
1501 C CA  . GLN   B 53  ? 0.1747 0.1736 0.1842 0.0323  -0.0135 -0.0023 59  GLN   C CA  
1502 C C   . GLN   B 53  ? 0.1650 0.1632 0.1748 0.0313  -0.0102 0.0003  59  GLN   C C   
1503 O O   . GLN   B 53  ? 0.1686 0.1697 0.1861 0.0306  -0.0092 0.0004  59  GLN   C O   
1504 C CB  . GLN   B 53  ? 0.1893 0.1919 0.2072 0.0338  -0.0175 -0.0051 59  GLN   C CB  
1505 C CG  . GLN   B 53  ? 0.2417 0.2455 0.2620 0.0339  -0.0209 -0.0085 59  GLN   C CG  
1506 C CD  . GLN   B 53  ? 0.2870 0.2949 0.3181 0.0347  -0.0251 -0.0114 59  GLN   C CD  
1507 O OE1 . GLN   B 53  ? 0.3229 0.3304 0.3518 0.0374  -0.0303 -0.0141 59  GLN   C OE1 
1508 N NE2 . GLN   B 53  ? 0.2411 0.2529 0.2843 0.0326  -0.0230 -0.0107 59  GLN   C NE2 
1509 N N   . THR   B 54  ? 0.1652 0.1592 0.1668 0.0314  -0.0084 0.0024  60  THR   C N   
1510 C CA  . THR   B 54  ? 0.1774 0.1698 0.1784 0.0303  -0.0055 0.0043  60  THR   C CA  
1511 C C   . THR   B 54  ? 0.1769 0.1660 0.1722 0.0282  -0.0033 0.0061  60  THR   C C   
1512 O O   . THR   B 54  ? 0.1854 0.1724 0.1759 0.0287  -0.0036 0.0067  60  THR   C O   
1513 C CB  . THR   B 54  ? 0.2192 0.2095 0.2179 0.0327  -0.0058 0.0047  60  THR   C CB  
1514 O OG1 . THR   B 54  ? 0.2612 0.2475 0.2522 0.0343  -0.0066 0.0056  60  THR   C OG1 
1515 C CG2 . THR   B 54  ? 0.2208 0.2147 0.2264 0.0350  -0.0083 0.0031  60  THR   C CG2 
1516 N N   . GLY   B 55  ? 0.1652 0.1541 0.1616 0.0260  -0.0011 0.0072  61  GLY   C N   
1517 C CA  . GLY   B 55  ? 0.1631 0.1495 0.1558 0.0238  0.0003  0.0088  61  GLY   C CA  
1518 C C   . GLY   B 55  ? 0.1607 0.1465 0.1537 0.0221  0.0018  0.0094  61  GLY   C C   
1519 O O   . GLY   B 55  ? 0.1702 0.1563 0.1643 0.0231  0.0024  0.0088  61  GLY   C O   
1520 N N   . VAL   B 56  ? 0.1513 0.1360 0.1430 0.0197  0.0023  0.0106  62  VAL   C N   
1521 C CA  . VAL   B 56  ? 0.1483 0.1319 0.1387 0.0181  0.0030  0.0110  62  VAL   C CA  
1522 C C   . VAL   B 56  ? 0.1458 0.1320 0.1390 0.0160  0.0030  0.0120  62  VAL   C C   
1523 O O   . VAL   B 56  ? 0.1563 0.1429 0.1507 0.0150  0.0026  0.0128  62  VAL   C O   
1524 C CB  . VAL   B 56  ? 0.1638 0.1423 0.1495 0.0174  0.0026  0.0113  62  VAL   C CB  
1525 C CG1 . VAL   B 56  ? 0.1902 0.1669 0.1734 0.0157  0.0024  0.0112  62  VAL   C CG1 
1526 C CG2 . VAL   B 56  ? 0.1700 0.1455 0.1531 0.0198  0.0029  0.0105  62  VAL   C CG2 
1527 N N   . TYR   B 57  ? 0.1430 0.1307 0.1372 0.0155  0.0037  0.0124  63  TYR   C N   
1528 C CA  . TYR   B 57  ? 0.1367 0.1267 0.1335 0.0137  0.0035  0.0139  63  TYR   C CA  
1529 C C   . TYR   B 57  ? 0.1500 0.1379 0.1425 0.0127  0.0030  0.0146  63  TYR   C C   
1530 O O   . TYR   B 57  ? 0.1641 0.1495 0.1520 0.0138  0.0036  0.0138  63  TYR   C O   
1531 C CB  . TYR   B 57  ? 0.1395 0.1337 0.1424 0.0142  0.0047  0.0142  63  TYR   C CB  
1532 C CG  . TYR   B 57  ? 0.1392 0.1341 0.1421 0.0150  0.0066  0.0149  63  TYR   C CG  
1533 C CD1 . TYR   B 57  ? 0.1611 0.1558 0.1643 0.0170  0.0079  0.0138  63  TYR   C CD1 
1534 C CD2 . TYR   B 57  ? 0.1441 0.1401 0.1476 0.0142  0.0074  0.0169  63  TYR   C CD2 
1535 C CE1 . TYR   B 57  ? 0.1698 0.1650 0.1734 0.0180  0.0106  0.0149  63  TYR   C CE1 
1536 C CE2 . TYR   B 57  ? 0.1515 0.1480 0.1547 0.0154  0.0099  0.0181  63  TYR   C CE2 
1537 C CZ  . TYR   B 57  ? 0.1643 0.1604 0.1678 0.0173  0.0118  0.0171  63  TYR   C CZ  
1538 O OH  . TYR   B 57  ? 0.1846 0.1810 0.1881 0.0188  0.0152  0.0186  63  TYR   C OH  
1539 N N   . TYR   B 58  ? 0.1499 0.1389 0.1439 0.0108  0.0018  0.0161  64  TYR   C N   
1540 C CA  . TYR   B 58  ? 0.1561 0.1432 0.1457 0.0099  0.0004  0.0167  64  TYR   C CA  
1541 C C   . TYR   B 58  ? 0.1523 0.1419 0.1427 0.0106  0.0017  0.0184  64  TYR   C C   
1542 O O   . TYR   B 58  ? 0.1503 0.1435 0.1468 0.0102  0.0024  0.0199  64  TYR   C O   
1543 C CB  . TYR   B 58  ? 0.1643 0.1513 0.1558 0.0076  -0.0022 0.0177  64  TYR   C CB  
1544 C CG  . TYR   B 58  ? 0.1767 0.1616 0.1633 0.0069  -0.0049 0.0179  64  TYR   C CG  
1545 C CD1 . TYR   B 58  ? 0.1959 0.1761 0.1751 0.0075  -0.0059 0.0158  64  TYR   C CD1 
1546 C CD2 . TYR   B 58  ? 0.1790 0.1664 0.1679 0.0059  -0.0065 0.0199  64  TYR   C CD2 
1547 C CE1 . TYR   B 58  ? 0.2021 0.1797 0.1753 0.0071  -0.0089 0.0154  64  TYR   C CE1 
1548 C CE2 . TYR   B 58  ? 0.1893 0.1746 0.1727 0.0056  -0.0097 0.0200  64  TYR   C CE2 
1549 C CZ  . TYR   B 58  ? 0.2137 0.1939 0.1886 0.0062  -0.0110 0.0175  64  TYR   C CZ  
1550 O OH  . TYR   B 58  ? 0.2523 0.2298 0.2202 0.0063  -0.0146 0.0170  64  TYR   C OH  
1551 N N   . CYS   B 59  ? 0.1571 0.1443 0.1409 0.0119  0.0023  0.0182  65  CYS   C N   
1552 C CA  . CYS   B 59  ? 0.1646 0.1531 0.1474 0.0131  0.0043  0.0203  65  CYS   C CA  
1553 C C   . CYS   B 59  ? 0.1794 0.1654 0.1550 0.0126  0.0015  0.0211  65  CYS   C C   
1554 O O   . CYS   B 59  ? 0.1925 0.1741 0.1593 0.0136  0.0007  0.0194  65  CYS   C O   
1555 C CB  . CYS   B 59  ? 0.1763 0.1638 0.1568 0.0155  0.0078  0.0196  65  CYS   C CB  
1556 S SG  . CYS   B 59  ? 0.2051 0.1936 0.1840 0.0175  0.0115  0.0228  65  CYS   C SG  
1557 N N   . SER   B 60  ? 0.1781 0.1666 0.1572 0.0113  -0.0003 0.0233  66  SER   C N   
1558 C CA  A SER   B 60  ? 0.1971 0.1836 0.1700 0.0109  -0.0041 0.0240  66  SER   C CA  
1559 C CA  B SER   B 60  ? 0.1901 0.1767 0.1631 0.0109  -0.0041 0.0241  66  SER   C CA  
1560 C C   . SER   B 60  ? 0.2003 0.1841 0.1635 0.0135  -0.0027 0.0249  66  SER   C C   
1561 O O   . SER   B 60  ? 0.2287 0.2085 0.1827 0.0138  -0.0060 0.0236  66  SER   C O   
1562 C CB  A SER   B 60  ? 0.2313 0.2214 0.2110 0.0093  -0.0064 0.0265  66  SER   C CB  
1563 C CB  B SER   B 60  ? 0.2038 0.1942 0.1838 0.0095  -0.0059 0.0268  66  SER   C CB  
1564 O OG  A SER   B 60  ? 0.2633 0.2567 0.2478 0.0103  -0.0032 0.0294  66  SER   C OG  
1565 O OG  B SER   B 60  ? 0.2073 0.1960 0.1820 0.0090  -0.0105 0.0273  66  SER   C OG  
1566 N N   . SER   B 61  ? 0.2015 0.1871 0.1666 0.0154  0.0022  0.0270  67  SER   C N   
1567 C CA  . SER   B 61  ? 0.2123 0.1952 0.1680 0.0183  0.0048  0.0286  67  SER   C CA  
1568 C C   . SER   B 61  ? 0.2301 0.2081 0.1766 0.0202  0.0063  0.0256  67  SER   C C   
1569 O O   . SER   B 61  ? 0.2509 0.2256 0.1876 0.0230  0.0085  0.0265  67  SER   C O   
1570 C CB  . SER   B 61  ? 0.2175 0.2038 0.1796 0.0197  0.0102  0.0322  67  SER   C CB  
1571 O OG  . SER   B 61  ? 0.2368 0.2250 0.2063 0.0198  0.0138  0.0308  67  SER   C OG  
1572 N N   . ARG   B 62  ? 0.2098 0.1868 0.1588 0.0190  0.0052  0.0222  68  ARG   C N   
1573 C CA  . ARG   B 62  ? 0.2101 0.1818 0.1506 0.0207  0.0060  0.0191  68  ARG   C CA  
1574 C C   . ARG   B 62  ? 0.2309 0.1990 0.1682 0.0186  0.0005  0.0157  68  ARG   C C   
1575 O O   . ARG   B 62  ? 0.2545 0.2176 0.1854 0.0197  0.0006  0.0126  68  ARG   C O   
1576 C CB  . ARG   B 62  ? 0.2081 0.1815 0.1550 0.0218  0.0105  0.0184  68  ARG   C CB  
1577 C CG  . ARG   B 62  ? 0.2695 0.2464 0.2215 0.0237  0.0162  0.0216  68  ARG   C CG  
1578 C CD  . ARG   B 62  ? 0.2741 0.2469 0.2156 0.0272  0.0200  0.0223  68  ARG   C CD  
1579 N NE  . ARG   B 62  ? 0.2834 0.2594 0.2307 0.0292  0.0263  0.0258  68  ARG   C NE  
1580 C CZ  . ARG   B 62  ? 0.3308 0.3085 0.2784 0.0297  0.0281  0.0298  68  ARG   C CZ  
1581 N NH1 . ARG   B 62  ? 0.3471 0.3239 0.2892 0.0286  0.0238  0.0308  68  ARG   C NH1 
1582 N NH2 . ARG   B 62  ? 0.3343 0.3146 0.2880 0.0316  0.0344  0.0331  68  ARG   C NH2 
1583 N N   . ARG   B 63  ? 0.2370 0.2075 0.1804 0.0156  -0.0038 0.0162  69  ARG   C N   
1584 C CA  . ARG   B 63  ? 0.2562 0.2242 0.2002 0.0132  -0.0086 0.0135  69  ARG   C CA  
1585 C C   . ARG   B 63  ? 0.2634 0.2292 0.2092 0.0134  -0.0066 0.0110  69  ARG   C C   
1586 O O   . ARG   B 63  ? 0.2893 0.2498 0.2300 0.0132  -0.0086 0.0080  69  ARG   C O   
1587 C CB  . ARG   B 63  ? 0.2810 0.2434 0.2142 0.0134  -0.0132 0.0113  69  ARG   C CB  
1588 C CG  . ARG   B 63  ? 0.3351 0.2992 0.2658 0.0133  -0.0165 0.0137  69  ARG   C CG  
1589 C CD  . ARG   B 63  ? 0.4068 0.3749 0.3479 0.0100  -0.0205 0.0149  69  ARG   C CD  
1590 N NE  . ARG   B 63  ? 0.4589 0.4272 0.3965 0.0098  -0.0256 0.0162  69  ARG   C NE  
1591 C CZ  . ARG   B 63  ? 0.4807 0.4531 0.4205 0.0106  -0.0248 0.0201  69  ARG   C CZ  
1592 N NH1 . ARG   B 63  ? 0.4597 0.4361 0.4051 0.0116  -0.0190 0.0229  69  ARG   C NH1 
1593 N NH2 . ARG   B 63  ? 0.4762 0.4486 0.4128 0.0105  -0.0302 0.0213  69  ARG   C NH2 
1594 N N   . LYS   B 64  ? 0.2332 0.2029 0.1860 0.0141  -0.0026 0.0123  70  LYS   C N   
1595 C CA  . LYS   B 64  ? 0.2286 0.1966 0.1829 0.0149  -0.0007 0.0104  70  LYS   C CA  
1596 C C   . LYS   B 64  ? 0.2172 0.1898 0.1813 0.0140  0.0004  0.0116  70  LYS   C C   
1597 O O   . LYS   B 64  ? 0.2101 0.1876 0.1798 0.0138  0.0016  0.0137  70  LYS   C O   
1598 C CB  . LYS   B 64  ? 0.2831 0.2500 0.2334 0.0181  0.0038  0.0102  70  LYS   C CB  
1599 C CG  . LYS   B 64  ? 0.4253 0.3854 0.3642 0.0198  0.0034  0.0077  70  LYS   C CG  
1600 C CD  . LYS   B 64  ? 0.5306 0.4877 0.4679 0.0223  0.0068  0.0059  70  LYS   C CD  
1601 C CE  . LYS   B 64  ? 0.6212 0.5713 0.5462 0.0244  0.0070  0.0034  70  LYS   C CE  
1602 N NZ  . LYS   B 64  ? 0.6650 0.6154 0.5833 0.0259  0.0083  0.0052  70  LYS   C NZ  
1603 N N   . HIS   B 65  ? 0.2057 0.1764 0.1714 0.0138  0.0002  0.0102  71  HIS   C N   
1604 C CA  . HIS   B 65  ? 0.1940 0.1680 0.1667 0.0139  0.0013  0.0109  71  HIS   C CA  
1605 C C   . HIS   B 65  ? 0.2118 0.1859 0.1846 0.0166  0.0042  0.0100  71  HIS   C C   
1606 O O   . HIS   B 65  ? 0.2475 0.2171 0.2154 0.0180  0.0047  0.0084  71  HIS   C O   
1607 C CB  . HIS   B 65  ? 0.1897 0.1614 0.1639 0.0124  -0.0005 0.0105  71  HIS   C CB  
1608 C CG  . HIS   B 65  ? 0.1803 0.1527 0.1569 0.0096  -0.0030 0.0116  71  HIS   C CG  
1609 N ND1 . HIS   B 65  ? 0.2104 0.1866 0.1934 0.0085  -0.0028 0.0134  71  HIS   C ND1 
1610 C CD2 . HIS   B 65  ? 0.1948 0.1645 0.1686 0.0079  -0.0060 0.0110  71  HIS   C CD2 
1611 C CE1 . HIS   B 65  ? 0.2063 0.1824 0.1912 0.0062  -0.0052 0.0141  71  HIS   C CE1 
1612 N NE2 . HIS   B 65  ? 0.2264 0.1987 0.2063 0.0056  -0.0076 0.0127  71  HIS   C NE2 
1613 N N   . TYR   B 66  ? 0.1790 0.1578 0.1579 0.0175  0.0058  0.0110  72  TYR   C N   
1614 C CA  . TYR   B 66  ? 0.1744 0.1540 0.1553 0.0201  0.0082  0.0103  72  TYR   C CA  
1615 C C   . TYR   B 66  ? 0.1646 0.1463 0.1507 0.0206  0.0073  0.0099  72  TYR   C C   
1616 O O   . TYR   B 66  ? 0.1581 0.1430 0.1485 0.0195  0.0063  0.0105  72  TYR   C O   
1617 C CB  . TYR   B 66  ? 0.1820 0.1657 0.1673 0.0209  0.0108  0.0117  72  TYR   C CB  
1618 C CG  . TYR   B 66  ? 0.2070 0.1886 0.1863 0.0215  0.0126  0.0125  72  TYR   C CG  
1619 C CD1 . TYR   B 66  ? 0.2276 0.2058 0.2018 0.0238  0.0152  0.0116  72  TYR   C CD1 
1620 C CD2 . TYR   B 66  ? 0.2198 0.2026 0.1981 0.0200  0.0120  0.0142  72  TYR   C CD2 
1621 C CE1 . TYR   B 66  ? 0.2376 0.2134 0.2049 0.0250  0.0173  0.0124  72  TYR   C CE1 
1622 C CE2 . TYR   B 66  ? 0.2253 0.2060 0.1969 0.0211  0.0137  0.0153  72  TYR   C CE2 
1623 C CZ  . TYR   B 66  ? 0.2425 0.2195 0.2079 0.0237  0.0163  0.0143  72  TYR   C CZ  
1624 O OH  . TYR   B 66  ? 0.2745 0.2488 0.2316 0.0252  0.0182  0.0154  72  TYR   C OH  
1625 N N   . PRO   B 67  ? 0.1726 0.1523 0.1579 0.0227  0.0076  0.0089  73  PRO   C N   
1626 C CA  . PRO   B 67  ? 0.1682 0.1501 0.1579 0.0239  0.0065  0.0085  73  PRO   C CA  
1627 C C   . PRO   B 67  ? 0.1688 0.1559 0.1661 0.0250  0.0073  0.0085  73  PRO   C C   
1628 O O   . PRO   B 67  ? 0.1925 0.1805 0.1918 0.0261  0.0098  0.0087  73  PRO   C O   
1629 C CB  . PRO   B 67  ? 0.2013 0.1793 0.1880 0.0261  0.0067  0.0078  73  PRO   C CB  
1630 C CG  . PRO   B 67  ? 0.2281 0.2029 0.2107 0.0265  0.0088  0.0072  73  PRO   C CG  
1631 C CD  . PRO   B 67  ? 0.1884 0.1635 0.1686 0.0243  0.0091  0.0078  73  PRO   C CD  
1632 N N   . VAL   B 68  ? 0.1535 0.1439 0.1554 0.0247  0.0055  0.0083  74  VAL   C N   
1633 C CA  . VAL   B 68  ? 0.1643 0.1597 0.1750 0.0253  0.0057  0.0079  74  VAL   C CA  
1634 C C   . VAL   B 68  ? 0.1510 0.1483 0.1650 0.0265  0.0026  0.0064  74  VAL   C C   
1635 O O   . VAL   B 68  ? 0.1593 0.1546 0.1686 0.0264  0.0007  0.0061  74  VAL   C O   
1636 C CB  . VAL   B 68  ? 0.1866 0.1846 0.2007 0.0231  0.0066  0.0089  74  VAL   C CB  
1637 C CG1 . VAL   B 68  ? 0.2140 0.2112 0.2262 0.0227  0.0098  0.0106  74  VAL   C CG1 
1638 C CG2 . VAL   B 68  ? 0.1909 0.1879 0.2018 0.0213  0.0048  0.0091  74  VAL   C CG2 
1639 N N   . SER   B 69  ? 0.1479 0.1492 0.1707 0.0278  0.0020  0.0055  75  SER   C N   
1640 C CA  . SER   B 69  ? 0.1500 0.1540 0.1777 0.0287  -0.0017 0.0035  75  SER   C CA  
1641 C C   . SER   B 69  ? 0.1428 0.1498 0.1769 0.0266  -0.0016 0.0032  75  SER   C C   
1642 O O   . SER   B 69  ? 0.1501 0.1588 0.1891 0.0254  0.0015  0.0046  75  SER   C O   
1643 C CB  . SER   B 69  ? 0.1822 0.1892 0.2180 0.0309  -0.0028 0.0026  75  SER   C CB  
1644 O OG  . SER   B 69  ? 0.2630 0.2670 0.2932 0.0331  -0.0029 0.0030  75  SER   C OG  
1645 N N   . PHE   B 70  ? 0.1296 0.1366 0.1627 0.0264  -0.0044 0.0016  76  PHE   C N   
1646 C CA  . PHE   B 70  ? 0.1379 0.1472 0.1770 0.0245  -0.0043 0.0010  76  PHE   C CA  
1647 C C   . PHE   B 70  ? 0.1474 0.1584 0.1911 0.0255  -0.0086 -0.0023 76  PHE   C C   
1648 O O   . PHE   B 70  ? 0.1505 0.1599 0.1889 0.0276  -0.0119 -0.0040 76  PHE   C O   
1649 C CB  . PHE   B 70  ? 0.1439 0.1508 0.1767 0.0226  -0.0025 0.0026  76  PHE   C CB  
1650 C CG  . PHE   B 70  ? 0.1413 0.1447 0.1645 0.0234  -0.0039 0.0023  76  PHE   C CG  
1651 C CD1 . PHE   B 70  ? 0.1434 0.1435 0.1590 0.0237  -0.0027 0.0040  76  PHE   C CD1 
1652 C CD2 . PHE   B 70  ? 0.1613 0.1642 0.1831 0.0239  -0.0059 0.0005  76  PHE   C CD2 
1653 C CE1 . PHE   B 70  ? 0.1475 0.1443 0.1554 0.0245  -0.0034 0.0042  76  PHE   C CE1 
1654 C CE2 . PHE   B 70  ? 0.1659 0.1653 0.1785 0.0250  -0.0061 0.0008  76  PHE   C CE2 
1655 C CZ  . PHE   B 70  ? 0.1552 0.1517 0.1615 0.0252  -0.0047 0.0029  76  PHE   C CZ  
1656 N N   . SER   B 71  ? 0.1380 0.1519 0.1916 0.0241  -0.0087 -0.0033 77  SER   C N   
1657 C CA  . SER   B 71  ? 0.1530 0.1683 0.2124 0.0249  -0.0132 -0.0072 77  SER   C CA  
1658 C C   . SER   B 71  ? 0.1778 0.1901 0.2292 0.0252  -0.0153 -0.0092 77  SER   C C   
1659 O O   . SER   B 71  ? 0.1798 0.1894 0.2231 0.0244  -0.0125 -0.0071 77  SER   C O   
1660 C CB  . SER   B 71  ? 0.1536 0.1728 0.2279 0.0232  -0.0125 -0.0075 77  SER   C CB  
1661 O OG  . SER   B 71  ? 0.1795 0.1981 0.2544 0.0210  -0.0090 -0.0057 77  SER   C OG  
1662 N N   . LYS   B 72  ? 0.1952 0.2077 0.2487 0.0265  -0.0200 -0.0133 78  LYS   C N   
1663 C CA  . LYS   B 72  ? 0.2047 0.2138 0.2499 0.0274  -0.0216 -0.0155 78  LYS   C CA  
1664 C C   . LYS   B 72  ? 0.1965 0.2059 0.2477 0.0249  -0.0191 -0.0155 78  LYS   C C   
1665 O O   . LYS   B 72  ? 0.1932 0.2057 0.2567 0.0231  -0.0184 -0.0154 78  LYS   C O   
1666 C CB  . LYS   B 72  ? 0.2714 0.2801 0.3162 0.0300  -0.0281 -0.0205 78  LYS   C CB  
1667 C CG  . LYS   B 72  ? 0.3680 0.3761 0.4061 0.0329  -0.0308 -0.0202 78  LYS   C CG  
1668 C CD  . LYS   B 72  ? 0.4993 0.5049 0.5298 0.0363  -0.0370 -0.0244 78  LYS   C CD  
1669 C CE  . LYS   B 72  ? 0.5807 0.5842 0.6008 0.0396  -0.0385 -0.0228 78  LYS   C CE  
1670 N NZ  . LYS   B 72  ? 0.6337 0.6339 0.6433 0.0435  -0.0439 -0.0263 78  LYS   C NZ  
1671 N N   . PRO   B 73  ? 0.1919 0.1981 0.2351 0.0250  -0.0175 -0.0153 79  PRO   C N   
1672 C CA  . PRO   B 73  ? 0.1940 0.2004 0.2431 0.0229  -0.0148 -0.0149 79  PRO   C CA  
1673 C C   . PRO   B 73  ? 0.2039 0.2116 0.2638 0.0225  -0.0181 -0.0192 79  PRO   C C   
1674 O O   . PRO   B 73  ? 0.2301 0.2361 0.2870 0.0246  -0.0229 -0.0239 79  PRO   C O   
1675 C CB  . PRO   B 73  ? 0.2176 0.2200 0.2561 0.0240  -0.0134 -0.0150 79  PRO   C CB  
1676 C CG  . PRO   B 73  ? 0.2418 0.2420 0.2685 0.0264  -0.0142 -0.0142 79  PRO   C CG  
1677 C CD  . PRO   B 73  ? 0.2086 0.2109 0.2377 0.0273  -0.0173 -0.0150 79  PRO   C CD  
1678 N N   . SER   B 74  ? 0.1789 0.1893 0.2513 0.0201  -0.0159 -0.0177 80  SER   C N   
1679 C CA  . SER   B 74  ? 0.1812 0.1930 0.2665 0.0193  -0.0188 -0.0215 80  SER   C CA  
1680 C C   . SER   B 74  ? 0.1767 0.1894 0.2722 0.0168  -0.0148 -0.0191 80  SER   C C   
1681 O O   . SER   B 74  ? 0.1699 0.1824 0.2620 0.0158  -0.0101 -0.0144 80  SER   C O   
1682 C CB  . SER   B 74  ? 0.2195 0.2352 0.3145 0.0192  -0.0210 -0.0217 80  SER   C CB  
1683 O OG  . SER   B 74  ? 0.3126 0.3280 0.3988 0.0215  -0.0238 -0.0223 80  SER   C OG  
1684 N N   . LEU   B 75  ? 0.1768 0.1903 0.2853 0.0158  -0.0170 -0.0224 81  LEU   C N   
1685 C CA  . LEU   B 75  ? 0.1876 0.2017 0.3080 0.0135  -0.0133 -0.0202 81  LEU   C CA  
1686 C C   . LEU   B 75  ? 0.1966 0.2150 0.3290 0.0121  -0.0108 -0.0164 81  LEU   C C   
1687 O O   . LEU   B 75  ? 0.2073 0.2281 0.3498 0.0120  -0.0141 -0.0191 81  LEU   C O   
1688 C CB  . LEU   B 75  ? 0.2071 0.2192 0.3359 0.0133  -0.0171 -0.0261 81  LEU   C CB  
1689 C CG  . LEU   B 75  ? 0.2478 0.2597 0.3891 0.0111  -0.0135 -0.0243 81  LEU   C CG  
1690 C CD1 . LEU   B 75  ? 0.2464 0.2558 0.3792 0.0113  -0.0092 -0.0211 81  LEU   C CD1 
1691 C CD2 . LEU   B 75  ? 0.2711 0.2810 0.4223 0.0108  -0.0181 -0.0310 81  LEU   C CD2 
1692 N N   . ILE   B 76  ? 0.1992 0.2186 0.3298 0.0113  -0.0052 -0.0102 82  ILE   C N   
1693 C CA  . ILE   B 76  ? 0.2056 0.2283 0.3439 0.0106  -0.0016 -0.0059 82  ILE   C CA  
1694 C C   . ILE   B 76  ? 0.2022 0.2254 0.3499 0.0090  0.0036  -0.0014 82  ILE   C C   
1695 O O   . ILE   B 76  ? 0.1877 0.2088 0.3294 0.0087  0.0057  0.0008  82  ILE   C O   
1696 C CB  . ILE   B 76  ? 0.2369 0.2594 0.3612 0.0117  0.0006  -0.0023 82  ILE   C CB  
1697 C CG1 . ILE   B 76  ? 0.2683 0.2901 0.3829 0.0136  -0.0038 -0.0058 82  ILE   C CG1 
1698 C CG2 . ILE   B 76  ? 0.2617 0.2867 0.3908 0.0115  0.0056  0.0029  82  ILE   C CG2 
1699 C CD1 . ILE   B 76  ? 0.2816 0.3064 0.4043 0.0144  -0.0063 -0.0076 82  ILE   C CD1 
1700 N N   . PHE   B 77  ? 0.1987 0.2247 0.3610 0.0081  0.0059  0.0006  83  PHE   C N   
1701 C CA  . PHE   B 77  ? 0.2033 0.2296 0.3739 0.0070  0.0117  0.0060  83  PHE   C CA  
1702 C C   . PHE   B 77  ? 0.2046 0.2311 0.3645 0.0080  0.0166  0.0121  83  PHE   C C   
1703 O O   . PHE   B 77  ? 0.2268 0.2548 0.3832 0.0090  0.0173  0.0130  83  PHE   C O   
1704 C CB  . PHE   B 77  ? 0.2023 0.2313 0.3929 0.0058  0.0132  0.0065  83  PHE   C CB  
1705 C CG  . PHE   B 77  ? 0.2084 0.2368 0.4083 0.0048  0.0190  0.0118  83  PHE   C CG  
1706 C CD1 . PHE   B 77  ? 0.2222 0.2481 0.4264 0.0037  0.0181  0.0103  83  PHE   C CD1 
1707 C CD2 . PHE   B 77  ? 0.2238 0.2537 0.4263 0.0052  0.0257  0.0187  83  PHE   C CD2 
1708 C CE1 . PHE   B 77  ? 0.2359 0.2609 0.4479 0.0030  0.0236  0.0158  83  PHE   C CE1 
1709 C CE2 . PHE   B 77  ? 0.2323 0.2612 0.4419 0.0047  0.0312  0.0242  83  PHE   C CE2 
1710 C CZ  . PHE   B 77  ? 0.2303 0.2570 0.4451 0.0035  0.0301  0.0229  83  PHE   C CZ  
1711 N N   . VAL   B 78  ? 0.1730 0.1975 0.3267 0.0078  0.0195  0.0160  84  VAL   C N   
1712 C CA  . VAL   B 78  ? 0.1729 0.1969 0.3152 0.0088  0.0232  0.0213  84  VAL   C CA  
1713 C C   . VAL   B 78  ? 0.1724 0.1967 0.3222 0.0086  0.0291  0.0276  84  VAL   C C   
1714 O O   . VAL   B 78  ? 0.1734 0.1968 0.3306 0.0077  0.0298  0.0283  84  VAL   C O   
1715 C CB  . VAL   B 78  ? 0.1884 0.2101 0.3165 0.0090  0.0211  0.0209  84  VAL   C CB  
1716 C CG1 . VAL   B 78  ? 0.1980 0.2189 0.3143 0.0099  0.0238  0.0257  84  VAL   C CG1 
1717 C CG2 . VAL   B 78  ? 0.1972 0.2182 0.3183 0.0094  0.0159  0.0151  84  VAL   C CG2 
1718 N N   . GLU   B 79  ? 0.1660 0.1909 0.3131 0.0098  0.0336  0.0321  85  GLU   C N   
1719 C CA  . GLU   B 79  ? 0.1644 0.1890 0.3160 0.0103  0.0397  0.0388  85  GLU   C CA  
1720 C C   . GLU   B 79  ? 0.1706 0.1929 0.3119 0.0106  0.0399  0.0421  85  GLU   C C   
1721 O O   . GLU   B 79  ? 0.1641 0.1851 0.2933 0.0106  0.0360  0.0398  85  GLU   C O   
1722 C CB  . GLU   B 79  ? 0.2036 0.2288 0.3521 0.0122  0.0448  0.0429  85  GLU   C CB  
1723 C CG  . GLU   B 79  ? 0.2602 0.2884 0.4232 0.0120  0.0459  0.0411  85  GLU   C CG  
1724 C CD  . GLU   B 79  ? 0.3813 0.4111 0.5649 0.0103  0.0475  0.0416  85  GLU   C CD  
1725 O OE1 . GLU   B 79  ? 0.4148 0.4434 0.6028 0.0104  0.0524  0.0471  85  GLU   C OE1 
1726 O OE2 . GLU   B 79  ? 0.4295 0.4613 0.6250 0.0089  0.0435  0.0364  85  GLU   C OE2 
1727 N N   . ALA   B 80  ? 0.1721 0.1937 0.3190 0.0110  0.0445  0.0478  86  ALA   C N   
1728 C CA  . ALA   B 80  ? 0.1796 0.1992 0.3182 0.0115  0.0448  0.0517  86  ALA   C CA  
1729 C C   . ALA   B 80  ? 0.1858 0.2042 0.3058 0.0132  0.0439  0.0532  86  ALA   C C   
1730 O O   . ALA   B 80  ? 0.2127 0.2311 0.3272 0.0145  0.0462  0.0543  86  ALA   C O   
1731 C CB  . ALA   B 80  ? 0.1881 0.2071 0.3351 0.0123  0.0508  0.0586  86  ALA   C CB  
1732 N N   . SER   B 81  ? 0.1807 0.1981 0.2921 0.0129  0.0402  0.0527  87  SER   C N   
1733 C CA  . SER   B 81  ? 0.2028 0.2188 0.2981 0.0141  0.0386  0.0540  87  SER   C CA  
1734 C C   . SER   B 81  ? 0.2213 0.2362 0.3130 0.0149  0.0389  0.0592  87  SER   C C   
1735 O O   . SER   B 81  ? 0.2251 0.2403 0.3274 0.0146  0.0408  0.0617  87  SER   C O   
1736 C CB  . SER   B 81  ? 0.1938 0.2098 0.2825 0.0130  0.0331  0.0483  87  SER   C CB  
1737 O OG  . SER   B 81  ? 0.1897 0.2060 0.2825 0.0118  0.0305  0.0470  87  SER   C OG  
1738 N N   . GLU   B 82  ? 0.2358 0.2493 0.3135 0.0159  0.0365  0.0605  88  GLU   C N   
1739 C CA  . GLU   B 82  ? 0.2524 0.2653 0.3269 0.0169  0.0359  0.0654  88  GLU   C CA  
1740 C C   . GLU   B 82  ? 0.2466 0.2606 0.3282 0.0152  0.0325  0.0636  88  GLU   C C   
1741 O O   . GLU   B 82  ? 0.2613 0.2752 0.3453 0.0158  0.0328  0.0678  88  GLU   C O   
1742 C CB  . GLU   B 82  ? 0.3152 0.3261 0.3732 0.0185  0.0336  0.0670  88  GLU   C CB  
1743 C CG  . GLU   B 82  ? 0.4083 0.4194 0.4593 0.0171  0.0277  0.0624  88  GLU   C CG  
1744 C CD  . GLU   B 82  ? 0.4936 0.5026 0.5297 0.0186  0.0246  0.0641  88  GLU   C CD  
1745 O OE1 . GLU   B 82  ? 0.5019 0.5088 0.5297 0.0209  0.0274  0.0671  88  GLU   C OE1 
1746 O OE2 . GLU   B 82  ? 0.5060 0.5155 0.5392 0.0174  0.0195  0.0624  88  GLU   C OE2 
1747 N N   . TYR   B 83  ? 0.2132 0.2282 0.2987 0.0133  0.0301  0.0577  89  TYR   C N   
1748 C CA  . TYR   B 83  ? 0.1972 0.2129 0.2880 0.0121  0.0274  0.0556  89  TYR   C CA  
1749 C C   . TYR   B 83  ? 0.1994 0.2154 0.3033 0.0109  0.0285  0.0518  89  TYR   C C   
1750 O O   . TYR   B 83  ? 0.2146 0.2306 0.3233 0.0104  0.0272  0.0504  89  TYR   C O   
1751 C CB  . TYR   B 83  ? 0.1930 0.2088 0.2747 0.0114  0.0229  0.0521  89  TYR   C CB  
1752 C CG  . TYR   B 83  ? 0.1924 0.2078 0.2685 0.0110  0.0221  0.0476  89  TYR   C CG  
1753 C CD1 . TYR   B 83  ? 0.1903 0.2046 0.2562 0.0120  0.0221  0.0486  89  TYR   C CD1 
1754 C CD2 . TYR   B 83  ? 0.1870 0.2027 0.2676 0.0101  0.0212  0.0424  89  TYR   C CD2 
1755 C CE1 . TYR   B 83  ? 0.1840 0.1979 0.2456 0.0118  0.0215  0.0447  89  TYR   C CE1 
1756 C CE2 . TYR   B 83  ? 0.1927 0.2081 0.2683 0.0100  0.0201  0.0387  89  TYR   C CE2 
1757 C CZ  . TYR   B 83  ? 0.1842 0.1987 0.2510 0.0108  0.0205  0.0400  89  TYR   C CZ  
1758 O OH  . TYR   B 83  ? 0.1942 0.2083 0.2569 0.0110  0.0198  0.0366  89  TYR   C OH  
1759 N N   . TYR   B 84  ? 0.1775 0.1937 0.2876 0.0106  0.0307  0.0499  90  TYR   C N   
1760 C CA  . TYR   B 84  ? 0.1647 0.1809 0.2877 0.0096  0.0311  0.0462  90  TYR   C CA  
1761 C C   . TYR   B 84  ? 0.1653 0.1819 0.2981 0.0096  0.0351  0.0483  90  TYR   C C   
1762 O O   . TYR   B 84  ? 0.1739 0.1910 0.3020 0.0105  0.0370  0.0503  90  TYR   C O   
1763 C CB  . TYR   B 84  ? 0.1543 0.1707 0.2755 0.0087  0.0276  0.0390  90  TYR   C CB  
1764 C CG  . TYR   B 84  ? 0.1434 0.1592 0.2583 0.0086  0.0243  0.0361  90  TYR   C CG  
1765 C CD1 . TYR   B 84  ? 0.1462 0.1611 0.2666 0.0085  0.0243  0.0358  90  TYR   C CD1 
1766 C CD2 . TYR   B 84  ? 0.1498 0.1656 0.2540 0.0087  0.0217  0.0337  90  TYR   C CD2 
1767 C CE1 . TYR   B 84  ? 0.1521 0.1665 0.2673 0.0086  0.0221  0.0334  90  TYR   C CE1 
1768 C CE2 . TYR   B 84  ? 0.1508 0.1660 0.2499 0.0086  0.0195  0.0315  90  TYR   C CE2 
1769 C CZ  . TYR   B 84  ? 0.1645 0.1791 0.2693 0.0086  0.0198  0.0313  90  TYR   C CZ  
1770 O OH  . TYR   B 84  ? 0.1622 0.1762 0.2627 0.0088  0.0183  0.0294  90  TYR   C OH  
1771 N N   . PRO   B 85  ? 0.1696 0.1858 0.3165 0.0088  0.0365  0.0475  91  PRO   C N   
1772 C CA  . PRO   B 85  ? 0.1734 0.1902 0.3321 0.0085  0.0401  0.0487  91  PRO   C CA  
1773 C C   . PRO   B 85  ? 0.1739 0.1921 0.3341 0.0077  0.0375  0.0426  91  PRO   C C   
1774 O O   . PRO   B 85  ? 0.1735 0.1917 0.3253 0.0075  0.0330  0.0375  91  PRO   C O   
1775 C CB  . PRO   B 85  ? 0.1787 0.1942 0.3523 0.0075  0.0412  0.0485  91  PRO   C CB  
1776 C CG  . PRO   B 85  ? 0.1839 0.1984 0.3541 0.0070  0.0367  0.0430  91  PRO   C CG  
1777 C CD  . PRO   B 85  ? 0.1729 0.1878 0.3266 0.0080  0.0348  0.0445  91  PRO   C CD  
1778 N N   . ALA   B 86  ? 0.1643 0.1837 0.3359 0.0073  0.0403  0.0432  92  ALA   C N   
1779 C CA  . ALA   B 86  ? 0.1797 0.2007 0.3557 0.0066  0.0374  0.0374  92  ALA   C CA  
1780 C C   . ALA   B 86  ? 0.1905 0.2106 0.3730 0.0052  0.0325  0.0305  92  ALA   C C   
1781 O O   . ALA   B 86  ? 0.2133 0.2319 0.4061 0.0044  0.0335  0.0309  92  ALA   C O   
1782 C CB  . ALA   B 86  ? 0.1806 0.2035 0.3711 0.0063  0.0417  0.0400  92  ALA   C CB  
1783 N N   . ARG   B 87  ? 0.1825 0.2027 0.3574 0.0053  0.0274  0.0244  93  ARG   C N   
1784 C CA  . ARG   B 87  ? 0.1798 0.1983 0.3575 0.0047  0.0227  0.0177  93  ARG   C CA  
1785 C C   . ARG   B 87  ? 0.1858 0.2048 0.3554 0.0053  0.0175  0.0118  93  ARG   C C   
1786 O O   . ARG   B 87  ? 0.1854 0.2059 0.3462 0.0061  0.0177  0.0132  93  ARG   C O   
1787 C CB  . ARG   B 87  ? 0.1889 0.2050 0.3584 0.0052  0.0227  0.0187  93  ARG   C CB  
1788 C CG  . ARG   B 87  ? 0.1861 0.2024 0.3382 0.0063  0.0217  0.0199  93  ARG   C CG  
1789 C CD  . ARG   B 87  ? 0.1846 0.1991 0.3299 0.0067  0.0216  0.0209  93  ARG   C CD  
1790 N NE  . ARG   B 87  ? 0.1874 0.2019 0.3182 0.0075  0.0196  0.0203  93  ARG   C NE  
1791 C CZ  . ARG   B 87  ? 0.2129 0.2259 0.3370 0.0079  0.0180  0.0183  93  ARG   C CZ  
1792 N NH1 . ARG   B 87  ? 0.2037 0.2150 0.3335 0.0080  0.0184  0.0170  93  ARG   C NH1 
1793 N NH2 . ARG   B 87  ? 0.1988 0.2119 0.3112 0.0085  0.0164  0.0179  93  ARG   C NH2 
1794 N N   . TYR   B 88  ? 0.1919 0.2091 0.3628 0.0052  0.0129  0.0051  94  TYR   C N   
1795 C CA  . TYR   B 88  ? 0.2113 0.2283 0.3722 0.0063  0.0079  -0.0002 94  TYR   C CA  
1796 C C   . TYR   B 88  ? 0.1989 0.2138 0.3438 0.0075  0.0077  0.0003  94  TYR   C C   
1797 O O   . TYR   B 88  ? 0.2151 0.2279 0.3593 0.0074  0.0089  0.0007  94  TYR   C O   
1798 C CB  . TYR   B 88  ? 0.2408 0.2561 0.4085 0.0062  0.0027  -0.0077 94  TYR   C CB  
1799 C CG  . TYR   B 88  ? 0.2706 0.2886 0.4542 0.0051  0.0013  -0.0093 94  TYR   C CG  
1800 C CD1 . TYR   B 88  ? 0.2868 0.3074 0.4692 0.0058  -0.0014 -0.0108 94  TYR   C CD1 
1801 C CD2 . TYR   B 88  ? 0.2926 0.3105 0.4935 0.0034  0.0032  -0.0086 94  TYR   C CD2 
1802 C CE1 . TYR   B 88  ? 0.3083 0.3319 0.5070 0.0047  -0.0026 -0.0119 94  TYR   C CE1 
1803 C CE2 . TYR   B 88  ? 0.3018 0.3224 0.5193 0.0022  0.0023  -0.0096 94  TYR   C CE2 
1804 C CZ  . TYR   B 88  ? 0.3228 0.3465 0.5394 0.0028  -0.0008 -0.0114 94  TYR   C CZ  
1805 O OH  . TYR   B 88  ? 0.3611 0.3879 0.5962 0.0016  -0.0015 -0.0121 94  TYR   C OH  
1806 N N   . GLN   B 89  ? 0.1783 0.1940 0.3114 0.0085  0.0067  0.0007  95  GLN   C N   
1807 C CA  . GLN   B 89  ? 0.1677 0.1815 0.2865 0.0095  0.0064  0.0010  95  GLN   C CA  
1808 C C   . GLN   B 89  ? 0.1584 0.1709 0.2697 0.0109  0.0018  -0.0046 95  GLN   C C   
1809 O O   . GLN   B 89  ? 0.1670 0.1811 0.2798 0.0113  -0.0005 -0.0064 95  GLN   C O   
1810 C CB  . GLN   B 89  ? 0.1727 0.1878 0.2838 0.0094  0.0092  0.0065  95  GLN   C CB  
1811 C CG  . GLN   B 89  ? 0.1896 0.2030 0.2880 0.0101  0.0088  0.0071  95  GLN   C CG  
1812 C CD  . GLN   B 89  ? 0.1706 0.1847 0.2631 0.0098  0.0112  0.0125  95  GLN   C CD  
1813 O OE1 . GLN   B 89  ? 0.1805 0.1956 0.2778 0.0092  0.0140  0.0167  95  GLN   C OE1 
1814 N NE2 . GLN   B 89  ? 0.1631 0.1763 0.2449 0.0103  0.0102  0.0125  95  GLN   C NE2 
1815 N N   . SER   B 90  ? 0.1580 0.1676 0.2617 0.0120  0.0007  -0.0072 96  SER   C N   
1816 C CA  . SER   B 90  ? 0.1550 0.1626 0.2499 0.0139  -0.0033 -0.0122 96  SER   C CA  
1817 C C   . SER   B 90  ? 0.1525 0.1596 0.2338 0.0151  -0.0028 -0.0100 96  SER   C C   
1818 O O   . SER   B 90  ? 0.1475 0.1551 0.2256 0.0143  0.0005  -0.0054 96  SER   C O   
1819 C CB  . SER   B 90  ? 0.1741 0.1781 0.2679 0.0150  -0.0047 -0.0168 96  SER   C CB  
1820 O OG  . SER   B 90  ? 0.1925 0.1949 0.2807 0.0153  -0.0011 -0.0138 96  SER   C OG  
1821 N N   . HIS   B 91  ? 0.1530 0.1587 0.2265 0.0170  -0.0063 -0.0135 97  HIS   C N   
1822 C CA  . HIS   B 91  ? 0.1454 0.1499 0.2061 0.0184  -0.0059 -0.0119 97  HIS   C CA  
1823 C C   . HIS   B 91  ? 0.1531 0.1602 0.2139 0.0170  -0.0036 -0.0070 97  HIS   C C   
1824 O O   . HIS   B 91  ? 0.1696 0.1757 0.2227 0.0170  -0.0016 -0.0040 97  HIS   C O   
1825 C CB  . HIS   B 91  ? 0.1697 0.1713 0.2227 0.0192  -0.0035 -0.0111 97  HIS   C CB  
1826 C CG  . HIS   B 91  ? 0.2043 0.2025 0.2547 0.0212  -0.0054 -0.0162 97  HIS   C CG  
1827 N ND1 . HIS   B 91  ? 0.2320 0.2270 0.2708 0.0242  -0.0074 -0.0190 97  HIS   C ND1 
1828 C CD2 . HIS   B 91  ? 0.2150 0.2121 0.2725 0.0209  -0.0054 -0.0189 97  HIS   C CD2 
1829 C CE1 . HIS   B 91  ? 0.2338 0.2257 0.2718 0.0257  -0.0086 -0.0235 97  HIS   C CE1 
1830 N NE2 . HIS   B 91  ? 0.2330 0.2259 0.2823 0.0238  -0.0075 -0.0238 97  HIS   C NE2 
1831 N N   . LEU   B 92  ? 0.1400 0.1498 0.2095 0.0160  -0.0038 -0.0064 98  LEU   C N   
1832 C CA  . LEU   B 92  ? 0.1405 0.1523 0.2100 0.0151  -0.0012 -0.0021 98  LEU   C CA  
1833 C C   . LEU   B 92  ? 0.1409 0.1534 0.2082 0.0164  -0.0034 -0.0033 98  LEU   C C   
1834 O O   . LEU   B 92  ? 0.1446 0.1581 0.2169 0.0173  -0.0067 -0.0069 98  LEU   C O   
1835 C CB  . LEU   B 92  ? 0.1543 0.1685 0.2357 0.0135  0.0012  0.0003  98  LEU   C CB  
1836 C CG  . LEU   B 92  ? 0.1760 0.1916 0.2564 0.0129  0.0046  0.0050  98  LEU   C CG  
1837 C CD1 . LEU   B 92  ? 0.1854 0.1994 0.2575 0.0124  0.0065  0.0084  98  LEU   C CD1 
1838 C CD2 . LEU   B 92  ? 0.1832 0.2011 0.2759 0.0119  0.0074  0.0074  98  LEU   C CD2 
1839 N N   . MET   B 93  ? 0.1381 0.1502 0.1982 0.0166  -0.0018 -0.0005 99  MET   C N   
1840 C CA  . MET   B 93  ? 0.1320 0.1445 0.1897 0.0180  -0.0032 -0.0010 99  MET   C CA  
1841 C C   . MET   B 93  ? 0.1440 0.1581 0.2045 0.0173  0.0001  0.0025  99  MET   C C   
1842 O O   . MET   B 93  ? 0.1531 0.1662 0.2099 0.0162  0.0029  0.0056  99  MET   C O   
1843 C CB  . MET   B 93  ? 0.1589 0.1682 0.2041 0.0193  -0.0039 -0.0008 99  MET   C CB  
1844 C CG  . MET   B 93  ? 0.1950 0.2021 0.2354 0.0205  -0.0064 -0.0038 99  MET   C CG  
1845 S SD  . MET   B 93  ? 0.2064 0.2096 0.2332 0.0219  -0.0058 -0.0024 99  MET   C SD  
1846 C CE  . MET   B 93  ? 0.2176 0.2205 0.2439 0.0194  -0.0017 0.0017  99  MET   C CE  
1847 N N   . LEU   B 94  ? 0.1324 0.1486 0.1988 0.0181  0.0000  0.0021  100 LEU   C N   
1848 C CA  . LEU   B 94  ? 0.1446 0.1619 0.2133 0.0179  0.0040  0.0055  100 LEU   C CA  
1849 C C   . LEU   B 94  ? 0.1493 0.1654 0.2115 0.0195  0.0040  0.0057  100 LEU   C C   
1850 O O   . LEU   B 94  ? 0.1555 0.1715 0.2168 0.0210  0.0007  0.0031  100 LEU   C O   
1851 C CB  . LEU   B 94  ? 0.1502 0.1712 0.2335 0.0177  0.0052  0.0056  100 LEU   C CB  
1852 C CG  . LEU   B 94  ? 0.1689 0.1912 0.2618 0.0160  0.0060  0.0058  100 LEU   C CG  
1853 C CD1 . LEU   B 94  ? 0.2016 0.2275 0.3101 0.0158  0.0077  0.0064  100 LEU   C CD1 
1854 C CD2 . LEU   B 94  ? 0.1834 0.2040 0.2712 0.0148  0.0095  0.0096  100 LEU   C CD2 
1855 N N   . ALA   B 95  ? 0.1454 0.1603 0.2032 0.0195  0.0077  0.0087  101 ALA   C N   
1856 C CA  . ALA   B 95  ? 0.1456 0.1590 0.1983 0.0212  0.0085  0.0090  101 ALA   C CA  
1857 C C   . ALA   B 95  ? 0.1365 0.1506 0.1919 0.0216  0.0135  0.0120  101 ALA   C C   
1858 O O   . ALA   B 95  ? 0.1412 0.1559 0.1989 0.0204  0.0160  0.0143  101 ALA   C O   
1859 C CB  . ALA   B 95  ? 0.1576 0.1668 0.1973 0.0211  0.0077  0.0092  101 ALA   C CB  
1860 N N   . VAL   B 96  ? 0.1410 0.1547 0.1955 0.0235  0.0152  0.0121  102 VAL   C N   
1861 C CA  . VAL   B 96  ? 0.1592 0.1724 0.2135 0.0245  0.0205  0.0149  102 VAL   C CA  
1862 C C   . VAL   B 96  ? 0.1701 0.1784 0.2100 0.0244  0.0213  0.0160  102 VAL   C C   
1863 O O   . VAL   B 96  ? 0.1844 0.1895 0.2161 0.0250  0.0193  0.0144  102 VAL   C O   
1864 C CB  . VAL   B 96  ? 0.1764 0.1910 0.2361 0.0269  0.0220  0.0145  102 VAL   C CB  
1865 C CG1 . VAL   B 96  ? 0.1903 0.2036 0.2481 0.0286  0.0284  0.0174  102 VAL   C CG1 
1866 C CG2 . VAL   B 96  ? 0.1736 0.1933 0.2489 0.0268  0.0202  0.0132  102 VAL   C CG2 
1867 N N   . GLY   B 97  ? 0.1814 0.1890 0.2186 0.0236  0.0238  0.0185  103 GLY   C N   
1868 C CA  . GLY   B 97  ? 0.2069 0.2100 0.2309 0.0233  0.0235  0.0193  103 GLY   C CA  
1869 C C   . GLY   B 97  ? 0.2093 0.2125 0.2317 0.0225  0.0254  0.0223  103 GLY   C C   
1870 O O   . GLY   B 97  ? 0.2211 0.2276 0.2529 0.0220  0.0272  0.0241  103 GLY   C O   
1871 N N   . HIS   B 98  ? 0.1939 0.1932 0.2046 0.0225  0.0249  0.0229  104 HIS   C N   
1872 C CA  . HIS   B 98  ? 0.2009 0.1996 0.2083 0.0222  0.0262  0.0261  104 HIS   C CA  
1873 C C   . HIS   B 98  ? 0.2010 0.2011 0.2102 0.0197  0.0225  0.0264  104 HIS   C C   
1874 O O   . HIS   B 98  ? 0.1954 0.1943 0.2015 0.0183  0.0185  0.0242  104 HIS   C O   
1875 C CB  . HIS   B 98  ? 0.2355 0.2292 0.2290 0.0237  0.0267  0.0264  104 HIS   C CB  
1876 C CG  . HIS   B 98  ? 0.2818 0.2746 0.2705 0.0243  0.0283  0.0299  104 HIS   C CG  
1877 N ND1 . HIS   B 98  ? 0.3146 0.3091 0.3078 0.0260  0.0338  0.0335  104 HIS   C ND1 
1878 C CD2 . HIS   B 98  ? 0.3118 0.3027 0.2930 0.0233  0.0249  0.0307  104 HIS   C CD2 
1879 C CE1 . HIS   B 98  ? 0.3471 0.3402 0.3341 0.0263  0.0337  0.0365  104 HIS   C CE1 
1880 N NE2 . HIS   B 98  ? 0.3455 0.3366 0.3250 0.0248  0.0281  0.0348  104 HIS   C NE2 
1881 N N   . SER   B 99  ? 0.1987 0.2009 0.2130 0.0193  0.0242  0.0295  105 SER   C N   
1882 C CA  . SER   B 99  ? 0.2058 0.2091 0.2222 0.0173  0.0212  0.0302  105 SER   C CA  
1883 C C   . SER   B 99  ? 0.2234 0.2273 0.2409 0.0178  0.0237  0.0346  105 SER   C C   
1884 O O   . SER   B 99  ? 0.2552 0.2612 0.2811 0.0185  0.0276  0.0366  105 SER   C O   
1885 C CB  . SER   B 99  ? 0.2108 0.2173 0.2381 0.0159  0.0199  0.0282  105 SER   C CB  
1886 O OG  . SER   B 99  ? 0.2130 0.2205 0.2431 0.0143  0.0178  0.0289  105 SER   C OG  
1887 N N   . GLU   B 100 ? 0.2203 0.2225 0.2303 0.0175  0.0215  0.0363  106 GLU   C N   
1888 C CA  . GLU   B 100 ? 0.2161 0.2187 0.2260 0.0182  0.0230  0.0409  106 GLU   C CA  
1889 C C   . GLU   B 100 ? 0.1962 0.2009 0.2124 0.0160  0.0196  0.0410  106 GLU   C C   
1890 O O   . GLU   B 100 ? 0.1927 0.1978 0.2099 0.0144  0.0162  0.0378  106 GLU   C O   
1891 C CB  . GLU   B 100 ? 0.2673 0.2659 0.2626 0.0197  0.0214  0.0424  106 GLU   C CB  
1892 C CG  . GLU   B 100 ? 0.3917 0.3867 0.3768 0.0217  0.0228  0.0406  106 GLU   C CG  
1893 C CD  . GLU   B 100 ? 0.4750 0.4672 0.4515 0.0250  0.0272  0.0440  106 GLU   C CD  
1894 O OE1 . GLU   B 100 ? 0.5299 0.5232 0.5090 0.0260  0.0300  0.0486  106 GLU   C OE1 
1895 O OE2 . GLU   B 100 ? 0.4818 0.4705 0.4493 0.0268  0.0285  0.0421  106 GLU   C OE2 
1896 N N   . PRO   B 101 ? 0.1973 0.2032 0.2177 0.0162  0.0208  0.0450  107 PRO   C N   
1897 C CA  . PRO   B 101 ? 0.1910 0.1988 0.2178 0.0145  0.0180  0.0452  107 PRO   C CA  
1898 C C   . PRO   B 101 ? 0.1913 0.1983 0.2120 0.0132  0.0129  0.0434  107 PRO   C C   
1899 O O   . PRO   B 101 ? 0.2032 0.2117 0.2296 0.0116  0.0109  0.0414  107 PRO   C O   
1900 C CB  . PRO   B 101 ? 0.2126 0.2208 0.2413 0.0156  0.0199  0.0506  107 PRO   C CB  
1901 C CG  . PRO   B 101 ? 0.2428 0.2504 0.2717 0.0175  0.0253  0.0529  107 PRO   C CG  
1902 C CD  . PRO   B 101 ? 0.2180 0.2235 0.2383 0.0183  0.0255  0.0498  107 PRO   C CD  
1903 N N   . GLY   B 102 ? 0.1851 0.1894 0.1943 0.0142  0.0108  0.0438  108 GLY   C N   
1904 C CA  . GLY   B 102 ? 0.1966 0.1999 0.2014 0.0128  0.0054  0.0422  108 GLY   C CA  
1905 C C   . GLY   B 102 ? 0.1850 0.1877 0.1901 0.0113  0.0041  0.0377  108 GLY   C C   
1906 O O   . GLY   B 102 ? 0.1997 0.2020 0.2041 0.0098  0.0003  0.0363  108 GLY   C O   
1907 N N   . ASP   B 103 ? 0.1632 0.1656 0.1696 0.0119  0.0071  0.0356  109 ASP   C N   
1908 C CA  . ASP   B 103 ? 0.1628 0.1645 0.1692 0.0110  0.0061  0.0317  109 ASP   C CA  
1909 C C   . ASP   B 103 ? 0.1645 0.1686 0.1798 0.0097  0.0058  0.0306  109 ASP   C C   
1910 O O   . ASP   B 103 ? 0.1630 0.1663 0.1779 0.0090  0.0047  0.0280  109 ASP   C O   
1911 C CB  . ASP   B 103 ? 0.1638 0.1644 0.1686 0.0126  0.0092  0.0301  109 ASP   C CB  
1912 C CG  . ASP   B 103 ? 0.1932 0.1903 0.1873 0.0142  0.0095  0.0303  109 ASP   C CG  
1913 O OD1 . ASP   B 103 ? 0.2035 0.1979 0.1905 0.0136  0.0061  0.0296  109 ASP   C OD1 
1914 O OD2 . ASP   B 103 ? 0.2243 0.2210 0.2174 0.0161  0.0134  0.0312  109 ASP   C OD2 
1915 N N   . CYS   B 104 ? 0.1473 0.1541 0.1705 0.0095  0.0072  0.0326  110 CYS   C N   
1916 C CA  . CYS   B 104 ? 0.1522 0.1608 0.1832 0.0086  0.0072  0.0313  110 CYS   C CA  
1917 C C   . CYS   B 104 ? 0.1577 0.1657 0.1872 0.0073  0.0045  0.0306  110 CYS   C C   
1918 O O   . CYS   B 104 ? 0.1698 0.1776 0.1969 0.0067  0.0023  0.0325  110 CYS   C O   
1919 C CB  . CYS   B 104 ? 0.1530 0.1637 0.1920 0.0086  0.0088  0.0338  110 CYS   C CB  
1920 S SG  . CYS   B 104 ? 0.1772 0.1889 0.2225 0.0097  0.0126  0.0340  110 CYS   C SG  
1921 N N   . GLY   B 105 ? 0.1294 0.1372 0.1605 0.0071  0.0047  0.0280  111 GLY   C N   
1922 C CA  . GLY   B 105 ? 0.1385 0.1456 0.1692 0.0061  0.0032  0.0277  111 GLY   C CA  
1923 C C   . GLY   B 105 ? 0.1427 0.1471 0.1669 0.0059  0.0019  0.0258  111 GLY   C C   
1924 O O   . GLY   B 105 ? 0.1591 0.1626 0.1836 0.0052  0.0014  0.0254  111 GLY   C O   
1925 N N   . GLY   B 106 ? 0.1448 0.1475 0.1634 0.0068  0.0020  0.0249  112 GLY   C N   
1926 C CA  . GLY   B 106 ? 0.1604 0.1600 0.1729 0.0069  0.0011  0.0229  112 GLY   C CA  
1927 C C   . GLY   B 106 ? 0.1514 0.1507 0.1652 0.0076  0.0023  0.0210  112 GLY   C C   
1928 O O   . GLY   B 106 ? 0.1489 0.1498 0.1661 0.0086  0.0037  0.0201  112 GLY   C O   
1929 N N   . ILE   B 107 ? 0.1456 0.1423 0.1566 0.0072  0.0015  0.0203  113 ILE   C N   
1930 C CA  . ILE   B 107 ? 0.1539 0.1498 0.1647 0.0083  0.0026  0.0190  113 ILE   C CA  
1931 C C   . ILE   B 107 ? 0.1462 0.1406 0.1531 0.0101  0.0028  0.0170  113 ILE   C C   
1932 O O   . ILE   B 107 ? 0.1496 0.1419 0.1524 0.0102  0.0022  0.0165  113 ILE   C O   
1933 C CB  . ILE   B 107 ? 0.1959 0.1896 0.2063 0.0074  0.0025  0.0198  113 ILE   C CB  
1934 C CG1 . ILE   B 107 ? 0.2237 0.2199 0.2404 0.0064  0.0033  0.0218  113 ILE   C CG1 
1935 C CG2 . ILE   B 107 ? 0.1967 0.1879 0.2036 0.0090  0.0036  0.0187  113 ILE   C CG2 
1936 C CD1 . ILE   B 107 ? 0.2716 0.2666 0.2907 0.0051  0.0036  0.0234  113 ILE   C CD1 
1937 N N   . LEU   B 108 ? 0.1414 0.1367 0.1495 0.0117  0.0035  0.0155  114 LEU   C N   
1938 C CA  . LEU   B 108 ? 0.1310 0.1251 0.1363 0.0137  0.0032  0.0137  114 LEU   C CA  
1939 C C   . LEU   B 108 ? 0.1404 0.1318 0.1421 0.0146  0.0034  0.0137  114 LEU   C C   
1940 O O   . LEU   B 108 ? 0.1419 0.1339 0.1450 0.0148  0.0041  0.0139  114 LEU   C O   
1941 C CB  . LEU   B 108 ? 0.1284 0.1253 0.1381 0.0150  0.0031  0.0120  114 LEU   C CB  
1942 C CG  . LEU   B 108 ? 0.1507 0.1470 0.1589 0.0173  0.0021  0.0099  114 LEU   C CG  
1943 C CD1 . LEU   B 108 ? 0.1556 0.1510 0.1621 0.0179  0.0023  0.0100  114 LEU   C CD1 
1944 C CD2 . LEU   B 108 ? 0.1594 0.1587 0.1734 0.0181  0.0012  0.0080  114 LEU   C CD2 
1945 N N   . ARG   B 109 ? 0.1440 0.1323 0.1413 0.0154  0.0031  0.0136  115 ARG   C N   
1946 C CA  . ARG   B 109 ? 0.1492 0.1345 0.1429 0.0165  0.0038  0.0143  115 ARG   C CA  
1947 C C   . ARG   B 109 ? 0.1680 0.1513 0.1577 0.0191  0.0030  0.0131  115 ARG   C C   
1948 O O   . ARG   B 109 ? 0.1753 0.1586 0.1649 0.0195  0.0023  0.0122  115 ARG   C O   
1949 C CB  . ARG   B 109 ? 0.1950 0.1777 0.1884 0.0145  0.0044  0.0162  115 ARG   C CB  
1950 C CG  . ARG   B 109 ? 0.2727 0.2530 0.2639 0.0138  0.0033  0.0157  115 ARG   C CG  
1951 C CD  . ARG   B 109 ? 0.3732 0.3508 0.3654 0.0115  0.0032  0.0172  115 ARG   C CD  
1952 N NE  . ARG   B 109 ? 0.4647 0.4448 0.4609 0.0090  0.0022  0.0179  115 ARG   C NE  
1953 C CZ  . ARG   B 109 ? 0.5646 0.5458 0.5654 0.0075  0.0028  0.0198  115 ARG   C CZ  
1954 N NH1 . ARG   B 109 ? 0.5746 0.5545 0.5761 0.0082  0.0050  0.0213  115 ARG   C NH1 
1955 N NH2 . ARG   B 109 ? 0.5864 0.5701 0.5912 0.0055  0.0013  0.0205  115 ARG   C NH2 
1956 N N   . CYS   B 110 ? 0.1699 0.1515 0.1561 0.0212  0.0034  0.0134  116 CYS   C N   
1957 C CA  . CYS   B 110 ? 0.1818 0.1611 0.1635 0.0241  0.0025  0.0129  116 CYS   C CA  
1958 C C   . CYS   B 110 ? 0.2009 0.1755 0.1781 0.0247  0.0044  0.0154  116 CYS   C C   
1959 O O   . CYS   B 110 ? 0.1971 0.1709 0.1761 0.0225  0.0063  0.0173  116 CYS   C O   
1960 C CB  . CYS   B 110 ? 0.1838 0.1649 0.1646 0.0268  0.0007  0.0108  116 CYS   C CB  
1961 S SG  . CYS   B 110 ? 0.1836 0.1636 0.1607 0.0279  0.0022  0.0115  116 CYS   C SG  
1962 N N   . GLN   B 111 ? 0.2093 0.1810 0.1814 0.0278  0.0040  0.0158  117 GLN   C N   
1963 C CA  . GLN   B 111 ? 0.2393 0.2063 0.2074 0.0286  0.0065  0.0188  117 GLN   C CA  
1964 C C   . GLN   B 111 ? 0.2420 0.2087 0.2086 0.0289  0.0090  0.0205  117 GLN   C C   
1965 O O   . GLN   B 111 ? 0.2743 0.2377 0.2404 0.0285  0.0121  0.0237  117 GLN   C O   
1966 C CB  . GLN   B 111 ? 0.2753 0.2392 0.2376 0.0325  0.0056  0.0193  117 GLN   C CB  
1967 C CG  . GLN   B 111 ? 0.3164 0.2818 0.2742 0.0361  0.0036  0.0178  117 GLN   C CG  
1968 C CD  . GLN   B 111 ? 0.4417 0.4044 0.3939 0.0402  0.0018  0.0183  117 GLN   C CD  
1969 O OE1 . GLN   B 111 ? 0.4706 0.4357 0.4247 0.0415  -0.0015 0.0160  117 GLN   C OE1 
1970 N NE2 . GLN   B 111 ? 0.4495 0.4075 0.3952 0.0425  0.0042  0.0215  117 GLN   C NE2 
1971 N N   . HIS   B 112 ? 0.2145 0.1843 0.1812 0.0296  0.0082  0.0186  118 HIS   C N   
1972 C CA  . HIS   B 112 ? 0.2152 0.1841 0.1796 0.0306  0.0110  0.0200  118 HIS   C CA  
1973 C C   . HIS   B 112 ? 0.2221 0.1935 0.1936 0.0271  0.0129  0.0208  118 HIS   C C   
1974 O O   . HIS   B 112 ? 0.2380 0.2087 0.2091 0.0276  0.0161  0.0225  118 HIS   C O   
1975 C CB  . HIS   B 112 ? 0.2297 0.1996 0.1893 0.0338  0.0090  0.0171  118 HIS   C CB  
1976 C CG  . HIS   B 112 ? 0.2294 0.1974 0.1823 0.0375  0.0062  0.0161  118 HIS   C CG  
1977 N ND1 . HIS   B 112 ? 0.2361 0.2070 0.1916 0.0379  0.0018  0.0129  118 HIS   C ND1 
1978 C CD2 . HIS   B 112 ? 0.2553 0.2189 0.1995 0.0412  0.0073  0.0182  118 HIS   C CD2 
1979 C CE1 . HIS   B 112 ? 0.2518 0.2203 0.2008 0.0416  -0.0002 0.0130  118 HIS   C CE1 
1980 N NE2 . HIS   B 112 ? 0.2618 0.2256 0.2032 0.0438  0.0030  0.0163  118 HIS   C NE2 
1981 N N   . GLY   B 113 ? 0.2025 0.1768 0.1804 0.0239  0.0111  0.0198  119 GLY   C N   
1982 C CA  . GLY   B 113 ? 0.1934 0.1704 0.1783 0.0208  0.0121  0.0206  119 GLY   C CA  
1983 C C   . GLY   B 113 ? 0.1726 0.1538 0.1619 0.0192  0.0097  0.0183  119 GLY   C C   
1984 O O   . GLY   B 113 ? 0.1726 0.1547 0.1613 0.0195  0.0073  0.0163  119 GLY   C O   
1985 N N   . VAL   B 114 ? 0.1644 0.1482 0.1591 0.0175  0.0106  0.0188  120 VAL   C N   
1986 C CA  . VAL   B 114 ? 0.1610 0.1485 0.1604 0.0161  0.0088  0.0173  120 VAL   C CA  
1987 C C   . VAL   B 114 ? 0.1613 0.1501 0.1596 0.0183  0.0079  0.0145  120 VAL   C C   
1988 O O   . VAL   B 114 ? 0.1811 0.1690 0.1775 0.0201  0.0093  0.0139  120 VAL   C O   
1989 C CB  . VAL   B 114 ? 0.1705 0.1601 0.1763 0.0139  0.0101  0.0193  120 VAL   C CB  
1990 C CG1 . VAL   B 114 ? 0.1768 0.1700 0.1875 0.0128  0.0087  0.0183  120 VAL   C CG1 
1991 C CG2 . VAL   B 114 ? 0.1901 0.1787 0.1982 0.0115  0.0100  0.0217  120 VAL   C CG2 
1992 N N   . VAL   B 115 ? 0.1450 0.1355 0.1448 0.0182  0.0057  0.0127  121 VAL   C N   
1993 C CA  . VAL   B 115 ? 0.1541 0.1462 0.1549 0.0199  0.0040  0.0096  121 VAL   C CA  
1994 C C   . VAL   B 115 ? 0.1662 0.1613 0.1742 0.0184  0.0043  0.0092  121 VAL   C C   
1995 O O   . VAL   B 115 ? 0.1632 0.1588 0.1728 0.0195  0.0038  0.0070  121 VAL   C O   
1996 C CB  . VAL   B 115 ? 0.1731 0.1658 0.1738 0.0206  0.0019  0.0082  121 VAL   C CB  
1997 C CG1 . VAL   B 115 ? 0.1746 0.1696 0.1793 0.0217  -0.0003 0.0051  121 VAL   C CG1 
1998 C CG2 . VAL   B 115 ? 0.1821 0.1714 0.1759 0.0225  0.0015  0.0087  121 VAL   C CG2 
1999 N N   . GLY   B 116 ? 0.1477 0.1445 0.1597 0.0160  0.0048  0.0112  122 GLY   C N   
2000 C CA  . GLY   B 116 ? 0.1630 0.1626 0.1819 0.0147  0.0052  0.0116  122 GLY   C CA  
2001 C C   . GLY   B 116 ? 0.1365 0.1372 0.1574 0.0126  0.0054  0.0142  122 GLY   C C   
2002 O O   . GLY   B 116 ? 0.1494 0.1485 0.1665 0.0119  0.0051  0.0155  122 GLY   C O   
2003 N N   . ILE   B 117 ? 0.1311 0.1343 0.1580 0.0116  0.0058  0.0151  123 ILE   C N   
2004 C CA  . ILE   B 117 ? 0.1360 0.1401 0.1637 0.0101  0.0058  0.0177  123 ILE   C CA  
2005 C C   . ILE   B 117 ? 0.1350 0.1409 0.1664 0.0103  0.0063  0.0179  123 ILE   C C   
2006 O O   . ILE   B 117 ? 0.1378 0.1450 0.1745 0.0109  0.0067  0.0164  123 ILE   C O   
2007 C CB  . ILE   B 117 ? 0.1507 0.1559 0.1823 0.0089  0.0063  0.0202  123 ILE   C CB  
2008 C CG1 . ILE   B 117 ? 0.1566 0.1632 0.1944 0.0094  0.0075  0.0196  123 ILE   C CG1 
2009 C CG2 . ILE   B 117 ? 0.1675 0.1712 0.1965 0.0083  0.0061  0.0210  123 ILE   C CG2 
2010 C CD1 . ILE   B 117 ? 0.1503 0.1584 0.1932 0.0083  0.0082  0.0226  123 ILE   C CD1 
2011 N N   . VAL   B 118 ? 0.1272 0.1328 0.1558 0.0099  0.0063  0.0196  124 VAL   C N   
2012 C CA  . VAL   B 118 ? 0.1274 0.1345 0.1593 0.0103  0.0077  0.0206  124 VAL   C CA  
2013 C C   . VAL   B 118 ? 0.1289 0.1380 0.1683 0.0098  0.0088  0.0223  124 VAL   C C   
2014 O O   . VAL   B 118 ? 0.1375 0.1469 0.1776 0.0090  0.0084  0.0241  124 VAL   C O   
2015 C CB  . VAL   B 118 ? 0.1290 0.1347 0.1548 0.0104  0.0079  0.0225  124 VAL   C CB  
2016 C CG1 . VAL   B 118 ? 0.1421 0.1491 0.1708 0.0111  0.0103  0.0245  124 VAL   C CG1 
2017 C CG2 . VAL   B 118 ? 0.1462 0.1493 0.1651 0.0110  0.0070  0.0207  124 VAL   C CG2 
2018 N N   . SER   B 119 ? 0.1184 0.1291 0.1646 0.0103  0.0102  0.0216  125 SER   C N   
2019 C CA  . SER   B 119 ? 0.1285 0.1407 0.1829 0.0099  0.0116  0.0232  125 SER   C CA  
2020 C C   . SER   B 119 ? 0.1357 0.1491 0.1957 0.0103  0.0141  0.0251  125 SER   C C   
2021 O O   . SER   B 119 ? 0.1430 0.1573 0.2084 0.0100  0.0157  0.0279  125 SER   C O   
2022 C CB  . SER   B 119 ? 0.1530 0.1653 0.2124 0.0100  0.0108  0.0198  125 SER   C CB  
2023 O OG  . SER   B 119 ? 0.1683 0.1816 0.2367 0.0096  0.0121  0.0207  125 SER   C OG  
2024 N N   . THR   B 120 ? 0.1259 0.1396 0.1858 0.0111  0.0148  0.0239  126 THR   C N   
2025 C CA  . THR   B 120 ? 0.1223 0.1373 0.1889 0.0116  0.0180  0.0261  126 THR   C CA  
2026 C C   . THR   B 120 ? 0.1291 0.1432 0.1891 0.0128  0.0196  0.0273  126 THR   C C   
2027 O O   . THR   B 120 ? 0.1389 0.1515 0.1907 0.0132  0.0178  0.0254  126 THR   C O   
2028 C CB  . THR   B 120 ? 0.1232 0.1400 0.2013 0.0114  0.0177  0.0230  126 THR   C CB  
2029 O OG1 . THR   B 120 ? 0.1469 0.1639 0.2232 0.0122  0.0160  0.0198  126 THR   C OG1 
2030 C CG2 . THR   B 120 ? 0.1401 0.1568 0.2236 0.0106  0.0158  0.0207  126 THR   C CG2 
2031 N N   . GLY   B 121 ? 0.1506 0.1654 0.2143 0.0136  0.0235  0.0306  127 GLY   C N   
2032 C CA  . GLY   B 121 ? 0.1863 0.2000 0.2443 0.0153  0.0261  0.0318  127 GLY   C CA  
2033 C C   . GLY   B 121 ? 0.2248 0.2400 0.2912 0.0163  0.0312  0.0352  127 GLY   C C   
2034 O O   . GLY   B 121 ? 0.2431 0.2594 0.3175 0.0156  0.0329  0.0376  127 GLY   C O   
2035 N N   . GLY   B 122 ? 0.2588 0.2736 0.3231 0.0180  0.0342  0.0359  128 GLY   C N   
2036 C CA  . GLY   B 122 ? 0.2812 0.2973 0.3539 0.0192  0.0401  0.0395  128 GLY   C CA  
2037 C C   . GLY   B 122 ? 0.2779 0.2963 0.3596 0.0199  0.0413  0.0373  128 GLY   C C   
2038 O O   . GLY   B 122 ? 0.2682 0.2878 0.3527 0.0190  0.0369  0.0328  128 GLY   C O   
2039 N N   . ASN   B 123 ? 0.2683 0.2874 0.3549 0.0217  0.0474  0.0407  129 ASN   C N   
2040 C CA  . ASN   B 123 ? 0.2747 0.2964 0.3714 0.0226  0.0491  0.0393  129 ASN   C CA  
2041 C C   . ASN   B 123 ? 0.2544 0.2749 0.3422 0.0236  0.0460  0.0353  129 ASN   C C   
2042 O O   . ASN   B 123 ? 0.2808 0.3039 0.3777 0.0238  0.0447  0.0327  129 ASN   C O   
2043 C CB  . ASN   B 123 ? 0.3225 0.3484 0.4382 0.0205  0.0469  0.0371  129 ASN   C CB  
2044 C CG  . ASN   B 123 ? 0.4174 0.4456 0.5486 0.0206  0.0530  0.0414  129 ASN   C CG  
2045 O OD1 . ASN   B 123 ? 0.4425 0.4696 0.5711 0.0227  0.0600  0.0465  129 ASN   C OD1 
2046 N ND2 . ASN   B 123 ? 0.4437 0.4750 0.5916 0.0185  0.0509  0.0397  129 ASN   C ND2 
2047 N N   . GLY   B 124 ? 0.2298 0.2461 0.3006 0.0243  0.0446  0.0350  130 GLY   C N   
2048 C CA  . GLY   B 124 ? 0.2127 0.2270 0.2747 0.0252  0.0417  0.0315  130 GLY   C CA  
2049 C C   . GLY   B 124 ? 0.1982 0.2136 0.2619 0.0233  0.0350  0.0270  130 GLY   C C   
2050 O O   . GLY   B 124 ? 0.1988 0.2132 0.2588 0.0242  0.0327  0.0242  130 GLY   C O   
2051 N N   . LEU   B 125 ? 0.1825 0.1993 0.2510 0.0212  0.0320  0.0264  131 LEU   C N   
2052 C CA  . LEU   B 125 ? 0.1783 0.1955 0.2470 0.0197  0.0261  0.0224  131 LEU   C CA  
2053 C C   . LEU   B 125 ? 0.1778 0.1926 0.2375 0.0183  0.0237  0.0226  131 LEU   C C   
2054 O O   . LEU   B 125 ? 0.2073 0.2218 0.2662 0.0178  0.0257  0.0257  131 LEU   C O   
2055 C CB  . LEU   B 125 ? 0.1881 0.2091 0.2718 0.0186  0.0244  0.0206  131 LEU   C CB  
2056 C CG  . LEU   B 125 ? 0.2090 0.2332 0.3051 0.0198  0.0261  0.0203  131 LEU   C CG  
2057 C CD1 . LEU   B 125 ? 0.2499 0.2776 0.3628 0.0184  0.0259  0.0199  131 LEU   C CD1 
2058 C CD2 . LEU   B 125 ? 0.2157 0.2399 0.3090 0.0211  0.0226  0.0168  131 LEU   C CD2 
2059 N N   . VAL   B 126 ? 0.1427 0.1562 0.1965 0.0178  0.0194  0.0196  132 VAL   C N   
2060 C CA  . VAL   B 126 ? 0.1340 0.1457 0.1814 0.0164  0.0171  0.0197  132 VAL   C CA  
2061 C C   . VAL   B 126 ? 0.1362 0.1493 0.1889 0.0156  0.0137  0.0166  132 VAL   C C   
2062 O O   . VAL   B 126 ? 0.1349 0.1484 0.1890 0.0164  0.0115  0.0137  132 VAL   C O   
2063 C CB  . VAL   B 126 ? 0.1515 0.1596 0.1862 0.0166  0.0157  0.0193  132 VAL   C CB  
2064 C CG1 . VAL   B 126 ? 0.1708 0.1779 0.2032 0.0178  0.0141  0.0166  132 VAL   C CG1 
2065 C CG2 . VAL   B 126 ? 0.1503 0.1572 0.1808 0.0150  0.0131  0.0193  132 VAL   C CG2 
2066 N N   . GLY   B 127 ? 0.1289 0.1423 0.1841 0.0142  0.0132  0.0173  133 GLY   C N   
2067 C CA  . GLY   B 127 ? 0.1256 0.1395 0.1846 0.0138  0.0104  0.0141  133 GLY   C CA  
2068 C C   . GLY   B 127 ? 0.1351 0.1469 0.1865 0.0132  0.0088  0.0140  133 GLY   C C   
2069 O O   . GLY   B 127 ? 0.1348 0.1460 0.1832 0.0123  0.0099  0.0169  133 GLY   C O   
2070 N N   . PHE   B 128 ? 0.1166 0.1274 0.1652 0.0138  0.0063  0.0110  134 PHE   C N   
2071 C CA  . PHE   B 128 ? 0.1171 0.1259 0.1592 0.0135  0.0054  0.0110  134 PHE   C CA  
2072 C C   . PHE   B 128 ? 0.1353 0.1440 0.1808 0.0137  0.0045  0.0087  134 PHE   C C   
2073 O O   . PHE   B 128 ? 0.1384 0.1473 0.1864 0.0148  0.0026  0.0055  134 PHE   C O   
2074 C CB  . PHE   B 128 ? 0.1258 0.1322 0.1595 0.0146  0.0040  0.0098  134 PHE   C CB  
2075 C CG  . PHE   B 128 ? 0.1230 0.1288 0.1532 0.0148  0.0048  0.0111  134 PHE   C CG  
2076 C CD1 . PHE   B 128 ? 0.1276 0.1317 0.1524 0.0139  0.0055  0.0134  134 PHE   C CD1 
2077 C CD2 . PHE   B 128 ? 0.1400 0.1467 0.1724 0.0162  0.0045  0.0098  134 PHE   C CD2 
2078 C CE1 . PHE   B 128 ? 0.1342 0.1369 0.1548 0.0144  0.0062  0.0140  134 PHE   C CE1 
2079 C CE2 . PHE   B 128 ? 0.1503 0.1559 0.1791 0.0168  0.0057  0.0108  134 PHE   C CE2 
2080 C CZ  . PHE   B 128 ? 0.1360 0.1393 0.1584 0.0159  0.0066  0.0128  134 PHE   C CZ  
2081 N N   . ALA   B 129 ? 0.1365 0.1447 0.1816 0.0129  0.0055  0.0102  135 ALA   C N   
2082 C CA  . ALA   B 129 ? 0.1360 0.1434 0.1829 0.0134  0.0051  0.0080  135 ALA   C CA  
2083 C C   . ALA   B 129 ? 0.1450 0.1497 0.1832 0.0149  0.0042  0.0064  135 ALA   C C   
2084 O O   . ALA   B 129 ? 0.1518 0.1555 0.1849 0.0145  0.0052  0.0087  135 ALA   C O   
2085 C CB  . ALA   B 129 ? 0.1428 0.1506 0.1930 0.0123  0.0071  0.0107  135 ALA   C CB  
2086 N N   . ASP   B 130 ? 0.1469 0.1505 0.1835 0.0167  0.0022  0.0027  136 ASP   C N   
2087 C CA  . ASP   B 130 ? 0.1546 0.1554 0.1820 0.0187  0.0016  0.0014  136 ASP   C CA  
2088 C C   . ASP   B 130 ? 0.1692 0.1681 0.1941 0.0191  0.0039  0.0023  136 ASP   C C   
2089 O O   . ASP   B 130 ? 0.1634 0.1627 0.1934 0.0188  0.0048  0.0015  136 ASP   C O   
2090 C CB  . ASP   B 130 ? 0.1710 0.1709 0.1973 0.0209  -0.0017 -0.0031 136 ASP   C CB  
2091 C CG  . ASP   B 130 ? 0.2302 0.2268 0.2458 0.0236  -0.0027 -0.0042 136 ASP   C CG  
2092 O OD1 . ASP   B 130 ? 0.2270 0.2228 0.2375 0.0238  -0.0020 -0.0019 136 ASP   C OD1 
2093 O OD2 . ASP   B 130 ? 0.2636 0.2580 0.2756 0.0257  -0.0039 -0.0074 136 ASP   C OD2 
2094 N N   . VAL   B 131 ? 0.1493 0.1459 0.1667 0.0200  0.0051  0.0038  137 VAL   C N   
2095 C CA  . VAL   B 131 ? 0.1483 0.1429 0.1631 0.0210  0.0080  0.0047  137 VAL   C CA  
2096 C C   . VAL   B 131 ? 0.1680 0.1588 0.1727 0.0242  0.0081  0.0032  137 VAL   C C   
2097 O O   . VAL   B 131 ? 0.1786 0.1672 0.1798 0.0256  0.0112  0.0041  137 VAL   C O   
2098 C CB  . VAL   B 131 ? 0.1599 0.1554 0.1771 0.0189  0.0107  0.0092  137 VAL   C CB  
2099 C CG1 . VAL   B 131 ? 0.1647 0.1636 0.1907 0.0163  0.0105  0.0109  137 VAL   C CG1 
2100 C CG2 . VAL   B 131 ? 0.1604 0.1549 0.1729 0.0185  0.0103  0.0112  137 VAL   C CG2 
2101 N N   . ARG   B 132 ? 0.1671 0.1571 0.1670 0.0257  0.0051  0.0012  138 ARG   C N   
2102 C CA  . ARG   B 132 ? 0.1648 0.1509 0.1540 0.0290  0.0050  0.0006  138 ARG   C CA  
2103 C C   . ARG   B 132 ? 0.1855 0.1687 0.1694 0.0322  0.0048  -0.0030 138 ARG   C C   
2104 O O   . ARG   B 132 ? 0.2036 0.1830 0.1773 0.0353  0.0061  -0.0027 138 ARG   C O   
2105 C CB  . ARG   B 132 ? 0.1573 0.1435 0.1436 0.0300  0.0014  -0.0005 138 ARG   C CB  
2106 C CG  . ARG   B 132 ? 0.1737 0.1613 0.1626 0.0277  0.0021  0.0028  138 ARG   C CG  
2107 C CD  . ARG   B 132 ? 0.1869 0.1746 0.1737 0.0291  -0.0012 0.0015  138 ARG   C CD  
2108 N NE  . ARG   B 132 ? 0.1847 0.1758 0.1790 0.0283  -0.0043 -0.0015 138 ARG   C NE  
2109 C CZ  . ARG   B 132 ? 0.2035 0.1959 0.1995 0.0292  -0.0074 -0.0029 138 ARG   C CZ  
2110 N NH1 . ARG   B 132 ? 0.2000 0.1904 0.1898 0.0312  -0.0082 -0.0019 138 ARG   C NH1 
2111 N NH2 . ARG   B 132 ? 0.1988 0.1947 0.2037 0.0282  -0.0095 -0.0051 138 ARG   C NH2 
2112 N N   . ASP   B 133 ? 0.1823 0.1669 0.1724 0.0315  0.0032  -0.0062 139 ASP   C N   
2113 C CA  . ASP   B 133 ? 0.2009 0.1822 0.1860 0.0345  0.0027  -0.0103 139 ASP   C CA  
2114 C C   . ASP   B 133 ? 0.2189 0.1986 0.2039 0.0348  0.0081  -0.0085 139 ASP   C C   
2115 O O   . ASP   B 133 ? 0.2298 0.2057 0.2086 0.0378  0.0087  -0.0117 139 ASP   C O   
2116 C CB  . ASP   B 133 ? 0.2170 0.2000 0.2096 0.0337  -0.0016 -0.0152 139 ASP   C CB  
2117 C CG  . ASP   B 133 ? 0.2496 0.2360 0.2550 0.0301  0.0002  -0.0137 139 ASP   C CG  
2118 O OD1 . ASP   B 133 ? 0.2217 0.2109 0.2317 0.0275  0.0022  -0.0092 139 ASP   C OD1 
2119 O OD2 . ASP   B 133 ? 0.2713 0.2571 0.2818 0.0301  -0.0004 -0.0169 139 ASP   C OD2 
2120 N N   . LEU   B 134 ? 0.2113 0.1936 0.2032 0.0319  0.0117  -0.0037 140 LEU   C N   
2121 C CA  . LEU   B 134 ? 0.2015 0.1832 0.1961 0.0319  0.0168  -0.0016 140 LEU   C CA  
2122 C C   . LEU   B 134 ? 0.2026 0.1811 0.1886 0.0342  0.0210  0.0015  140 LEU   C C   
2123 O O   . LEU   B 134 ? 0.1979 0.1780 0.1875 0.0323  0.0238  0.0063  140 LEU   C O   
2124 C CB  . LEU   B 134 ? 0.1870 0.1733 0.1936 0.0278  0.0177  0.0021  140 LEU   C CB  
2125 C CG  . LEU   B 134 ? 0.2007 0.1899 0.2161 0.0257  0.0143  0.0000  140 LEU   C CG  
2126 C CD1 . LEU   B 134 ? 0.1984 0.1917 0.2233 0.0222  0.0153  0.0042  140 LEU   C CD1 
2127 C CD2 . LEU   B 134 ? 0.2118 0.1992 0.2295 0.0272  0.0143  -0.0043 140 LEU   C CD2 
2128 N N   . LEU   B 135 ? 0.2214 0.1951 0.1957 0.0386  0.0213  -0.0013 141 LEU   C N   
2129 C CA  . LEU   B 135 ? 0.2312 0.2013 0.1959 0.0413  0.0256  0.0021  141 LEU   C CA  
2130 C C   . LEU   B 135 ? 0.2312 0.2012 0.2002 0.0411  0.0325  0.0063  141 LEU   C C   
2131 O O   . LEU   B 135 ? 0.2457 0.2147 0.2125 0.0416  0.0365  0.0109  141 LEU   C O   
2132 C CB  . LEU   B 135 ? 0.2424 0.2069 0.1919 0.0467  0.0244  -0.0017 141 LEU   C CB  
2133 C CG  . LEU   B 135 ? 0.2690 0.2338 0.2153 0.0472  0.0167  -0.0064 141 LEU   C CG  
2134 C CD1 . LEU   B 135 ? 0.2885 0.2475 0.2189 0.0528  0.0150  -0.0099 141 LEU   C CD1 
2135 C CD2 . LEU   B 135 ? 0.2822 0.2502 0.2322 0.0446  0.0141  -0.0036 141 LEU   C CD2 
2136 N N   . TRP   B 136 ? 0.2181 0.1893 0.1942 0.0405  0.0340  0.0049  142 TRP   C N   
2137 C CA  . TRP   B 136 ? 0.2319 0.2035 0.2139 0.0405  0.0405  0.0087  142 TRP   C CA  
2138 C C   . TRP   B 136 ? 0.2341 0.2104 0.2273 0.0362  0.0415  0.0143  142 TRP   C C   
2139 O O   . TRP   B 136 ? 0.2550 0.2318 0.2533 0.0362  0.0470  0.0184  142 TRP   C O   
2140 C CB  . TRP   B 136 ? 0.2371 0.2089 0.2249 0.0408  0.0413  0.0057  142 TRP   C CB  
2141 C CG  . TRP   B 136 ? 0.2359 0.2118 0.2337 0.0371  0.0360  0.0037  142 TRP   C CG  
2142 C CD1 . TRP   B 136 ? 0.2406 0.2158 0.2367 0.0374  0.0308  -0.0017 142 TRP   C CD1 
2143 C CD2 . TRP   B 136 ? 0.2269 0.2082 0.2384 0.0329  0.0357  0.0072  142 TRP   C CD2 
2144 N NE1 . TRP   B 136 ? 0.2409 0.2207 0.2491 0.0335  0.0280  -0.0013 142 TRP   C NE1 
2145 C CE2 . TRP   B 136 ? 0.2364 0.2197 0.2531 0.0310  0.0309  0.0042  142 TRP   C CE2 
2146 C CE3 . TRP   B 136 ? 0.2297 0.2142 0.2496 0.0308  0.0389  0.0127  142 TRP   C CE3 
2147 C CZ2 . TRP   B 136 ? 0.2306 0.2186 0.2592 0.0274  0.0296  0.0068  142 TRP   C CZ2 
2148 C CZ3 . TRP   B 136 ? 0.2383 0.2276 0.2700 0.0272  0.0368  0.0148  142 TRP   C CZ3 
2149 C CH2 . TRP   B 136 ? 0.2332 0.2240 0.2682 0.0257  0.0324  0.0120  142 TRP   C CH2 
2150 N N   . LEU   B 137 ? 0.2237 0.2033 0.2211 0.0328  0.0364  0.0144  143 LEU   C N   
2151 C CA  . LEU   B 137 ? 0.2191 0.2024 0.2255 0.0290  0.0368  0.0192  143 LEU   C CA  
2152 C C   . LEU   B 137 ? 0.2677 0.2486 0.2702 0.0300  0.0408  0.0232  143 LEU   C C   
2153 O O   . LEU   B 137 ? 0.2840 0.2673 0.2953 0.0275  0.0426  0.0274  143 LEU   C O   
2154 C CB  . LEU   B 137 ? 0.2116 0.1977 0.2207 0.0259  0.0310  0.0183  143 LEU   C CB  
2155 C CG  . LEU   B 137 ? 0.2083 0.1976 0.2245 0.0240  0.0277  0.0161  143 LEU   C CG  
2156 C CD1 . LEU   B 137 ? 0.2092 0.2004 0.2254 0.0219  0.0226  0.0148  143 LEU   C CD1 
2157 C CD2 . LEU   B 137 ? 0.2138 0.2067 0.2415 0.0216  0.0294  0.0194  143 LEU   C CD2 
2158 N N   . ASP   B 138 ? 0.2699 0.2461 0.2597 0.0338  0.0418  0.0220  144 ASP   C N   
2159 C CA  . ASP   B 138 ? 0.2902 0.2633 0.2752 0.0352  0.0458  0.0260  144 ASP   C CA  
2160 C C   . ASP   B 138 ? 0.3270 0.2978 0.3116 0.0380  0.0537  0.0291  144 ASP   C C   
2161 O O   . ASP   B 138 ? 0.3373 0.3052 0.3181 0.0396  0.0580  0.0329  144 ASP   C O   
2162 C CB  . ASP   B 138 ? 0.2890 0.2577 0.2596 0.0387  0.0438  0.0239  144 ASP   C CB  
2163 C CG  . ASP   B 138 ? 0.3132 0.2838 0.2836 0.0366  0.0369  0.0215  144 ASP   C CG  
2164 O OD1 . ASP   B 138 ? 0.3093 0.2839 0.2896 0.0324  0.0342  0.0221  144 ASP   C OD1 
2165 O OD2 . ASP   B 138 ? 0.3350 0.3026 0.2947 0.0396  0.0341  0.0189  144 ASP   C OD2 
2166 N N   . GLU   B 139 ? 0.3463 0.3180 0.3349 0.0389  0.0561  0.0278  145 GLU   C N   
2167 C CA  . GLU   B 139 ? 0.4066 0.3755 0.3941 0.0423  0.0643  0.0306  145 GLU   C CA  
2168 C C   . GLU   B 139 ? 0.4540 0.4269 0.4553 0.0406  0.0669  0.0317  145 GLU   C C   
2169 O O   . GLU   B 139 ? 0.4510 0.4283 0.4615 0.0370  0.0620  0.0302  145 GLU   C O   
2170 C CB  . GLU   B 139 ? 0.4705 0.4333 0.4413 0.0480  0.0655  0.0264  145 GLU   C CB  
2171 C CG  . GLU   B 139 ? 0.5759 0.5393 0.5461 0.0481  0.0606  0.0201  145 GLU   C CG  
2172 C CD  . GLU   B 139 ? 0.7094 0.6672 0.6634 0.0529  0.0583  0.0145  145 GLU   C CD  
2173 O OE1 . GLU   B 139 ? 0.7267 0.6835 0.6803 0.0540  0.0568  0.0096  145 GLU   C OE1 
2174 O OE2 . GLU   B 139 ? 0.7566 0.7108 0.6984 0.0555  0.0576  0.0148  145 GLU   C OE2 
2175 N N   . GLU   B 140 ? 0.4918 0.4627 0.4942 0.0436  0.0750  0.0345  146 GLU   C N   
2176 C CA  . GLU   B 140 ? 0.5239 0.4977 0.5386 0.0432  0.0791  0.0360  146 GLU   C CA  
2177 C C   . GLU   B 140 ? 0.5503 0.5303 0.5831 0.0384  0.0788  0.0410  146 GLU   C C   
2178 O O   . GLU   B 140 ? 0.5659 0.5469 0.6075 0.0390  0.0855  0.0457  146 GLU   C O   
2179 C CB  . GLU   B 140 ? 0.5525 0.5266 0.5670 0.0436  0.0753  0.0304  146 GLU   C CB  
2180 C CG  . GLU   B 140 ? 0.6275 0.6054 0.6568 0.0424  0.0779  0.0320  146 GLU   C CG  
2181 C CD  . GLU   B 140 ? 0.7193 0.6932 0.7456 0.0473  0.0859  0.0316  146 GLU   C CD  
2182 O OE1 . GLU   B 140 ? 0.7468 0.7198 0.7740 0.0485  0.0851  0.0276  146 GLU   C OE1 
2183 O OE2 . GLU   B 140 ? 0.7485 0.7199 0.7717 0.0502  0.0933  0.0353  146 GLU   C OE2 
2184 N N1  . A1BRX C .   ? 0.5680 0.5416 0.6191 0.0138  0.0536  -0.0252 201 A1BRX A N1  
2185 N N3  . A1BRX C .   ? 0.5873 0.5760 0.6139 0.0072  0.0449  -0.0240 201 A1BRX A N3  
2186 C C4  . A1BRX C .   ? 0.5709 0.5296 0.6142 0.0067  0.0602  -0.0363 201 A1BRX A C4  
2187 C C5  . A1BRX C .   ? 0.5738 0.5407 0.6115 0.0069  0.0551  -0.0330 201 A1BRX A C5  
2188 C C6  . A1BRX C .   ? 0.5735 0.5534 0.6190 0.0129  0.0507  -0.0238 201 A1BRX A C6  
2189 C C7  . A1BRX C .   ? 0.5781 0.5664 0.6065 0.0093  0.0398  -0.0204 201 A1BRX A C7  
2190 C C8  . A1BRX C .   ? 0.5852 0.5699 0.6205 0.0082  0.0541  -0.0283 201 A1BRX A C8  
2191 C C10 . A1BRX C .   ? 0.5884 0.5687 0.6324 0.0063  0.0716  -0.0382 201 A1BRX A C10 
2192 C C13 . A1BRX C .   ? 0.5812 0.5610 0.6274 0.0114  0.0577  -0.0283 201 A1BRX A C13 
2193 O O   . A1BRX C .   ? 0.4924 0.4715 0.5874 0.0293  0.0499  -0.0020 201 A1BRX A O   
2194 C C   . A1BRX C .   ? 0.4924 0.4713 0.5744 0.0260  0.0439  -0.0036 201 A1BRX A C   
2195 N N   . A1BRX C .   ? 0.4558 0.4412 0.5359 0.0262  0.0363  0.0027  201 A1BRX A N   
2196 C C1  . A1BRX C .   ? 0.5234 0.4949 0.5911 0.0208  0.0452  -0.0128 201 A1BRX A C1  
2197 C C2  . A1BRX C .   ? 0.5478 0.5160 0.6119 0.0182  0.0521  -0.0200 201 A1BRX A C2  
2198 C C14 . A1BRX C .   ? 0.5542 0.5301 0.6115 0.0175  0.0479  -0.0183 201 A1BRX A C14 
2199 C C3  . A1BRX C .   ? 0.5658 0.5265 0.6166 0.0114  0.0542  -0.0289 201 A1BRX A C3  
2200 N N2  . A1BRX C .   ? 0.5782 0.5629 0.6149 0.0119  0.0417  -0.0199 201 A1BRX A N2  
2201 C C12 . A1BRX C .   ? 0.5842 0.5590 0.6413 0.0125  0.0687  -0.0329 201 A1BRX A C12 
2202 C C11 . A1BRX C .   ? 0.5879 0.5629 0.6442 0.0101  0.0757  -0.0381 201 A1BRX A C11 
2203 C C9  . A1BRX C .   ? 0.5875 0.5723 0.6213 0.0055  0.0608  -0.0331 201 A1BRX A C9  
# 
