data_7I4I
# 
_entry.id   7I4I 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7I4I         pdb_00007i4i 10.2210/pdb7i4i/pdb 
WWPDB D_1001408305 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I4I 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                 15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-(4-hydroxythiane-4-carbonyl)piperidine-3-carboxamide' 272.364   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    341 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-(4-hydroxythiane-4-carbonyl)piperidine-3-carboxamide' A1B2W 
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 
A1B2W non-polymer         . '(3S)-1-(4-hydroxythiane-4-carbonyl)piperidine-3-carboxamide' ? 'C12 H20 N2 O3 S' 272.364 
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        A1B2W 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B2W 
_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 A1B2W 1   201 201 A1B2W LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   201 1   DMS   DMS C . 
F 3 ZN    1   202 1   ZN    ZN  C . 
G 4 DMS   1   203 1   DMS   DMS C . 
H 5 HOH   1   301 237 HOH   HOH A . 
H 5 HOH   2   302 351 HOH   HOH A . 
H 5 HOH   3   303 350 HOH   HOH A . 
H 5 HOH   4   304 286 HOH   HOH A . 
H 5 HOH   5   305 161 HOH   HOH A . 
H 5 HOH   6   306 199 HOH   HOH A . 
H 5 HOH   7   307 247 HOH   HOH A . 
H 5 HOH   8   308 238 HOH   HOH A . 
H 5 HOH   9   309 133 HOH   HOH A . 
H 5 HOH   10  310 83  HOH   HOH A . 
H 5 HOH   11  311 102 HOH   HOH A . 
H 5 HOH   12  312 158 HOH   HOH A . 
H 5 HOH   13  313 251 HOH   HOH A . 
H 5 HOH   14  314 307 HOH   HOH A . 
H 5 HOH   15  315 77  HOH   HOH A . 
H 5 HOH   16  316 190 HOH   HOH A . 
H 5 HOH   17  317 26  HOH   HOH A . 
H 5 HOH   18  318 118 HOH   HOH A . 
H 5 HOH   19  319 80  HOH   HOH A . 
H 5 HOH   20  320 209 HOH   HOH A . 
H 5 HOH   21  321 113 HOH   HOH A . 
H 5 HOH   22  322 181 HOH   HOH A . 
H 5 HOH   23  323 87  HOH   HOH A . 
H 5 HOH   24  324 256 HOH   HOH A . 
H 5 HOH   25  325 148 HOH   HOH A . 
H 5 HOH   26  326 95  HOH   HOH A . 
H 5 HOH   27  327 137 HOH   HOH A . 
H 5 HOH   28  328 183 HOH   HOH A . 
H 5 HOH   29  329 177 HOH   HOH A . 
H 5 HOH   30  330 42  HOH   HOH A . 
H 5 HOH   31  331 35  HOH   HOH A . 
H 5 HOH   32  332 200 HOH   HOH A . 
H 5 HOH   33  333 169 HOH   HOH A . 
H 5 HOH   34  334 58  HOH   HOH A . 
H 5 HOH   35  335 27  HOH   HOH A . 
H 5 HOH   36  336 13  HOH   HOH A . 
H 5 HOH   37  337 308 HOH   HOH A . 
H 5 HOH   38  338 57  HOH   HOH A . 
H 5 HOH   39  339 68  HOH   HOH A . 
H 5 HOH   40  340 115 HOH   HOH A . 
H 5 HOH   41  341 29  HOH   HOH A . 
H 5 HOH   42  342 295 HOH   HOH A . 
H 5 HOH   43  343 5   HOH   HOH A . 
H 5 HOH   44  344 213 HOH   HOH A . 
H 5 HOH   45  345 257 HOH   HOH A . 
H 5 HOH   46  346 271 HOH   HOH A . 
H 5 HOH   47  347 287 HOH   HOH A . 
H 5 HOH   48  348 336 HOH   HOH A . 
H 5 HOH   49  349 51  HOH   HOH A . 
H 5 HOH   50  350 186 HOH   HOH A . 
H 5 HOH   51  351 50  HOH   HOH A . 
H 5 HOH   52  352 12  HOH   HOH A . 
H 5 HOH   53  353 309 HOH   HOH A . 
H 5 HOH   54  354 326 HOH   HOH A . 
H 5 HOH   55  355 38  HOH   HOH A . 
H 5 HOH   56  356 36  HOH   HOH A . 
H 5 HOH   57  357 208 HOH   HOH A . 
H 5 HOH   58  358 10  HOH   HOH A . 
H 5 HOH   59  359 86  HOH   HOH A . 
H 5 HOH   60  360 171 HOH   HOH A . 
H 5 HOH   61  361 39  HOH   HOH A . 
H 5 HOH   62  362 193 HOH   HOH A . 
H 5 HOH   63  363 65  HOH   HOH A . 
H 5 HOH   64  364 72  HOH   HOH A . 
H 5 HOH   65  365 142 HOH   HOH A . 
H 5 HOH   66  366 93  HOH   HOH A . 
H 5 HOH   67  367 344 HOH   HOH A . 
H 5 HOH   68  368 311 HOH   HOH A . 
H 5 HOH   69  369 4   HOH   HOH A . 
H 5 HOH   70  370 197 HOH   HOH A . 
H 5 HOH   71  371 60  HOH   HOH A . 
H 5 HOH   72  372 52  HOH   HOH A . 
H 5 HOH   73  373 226 HOH   HOH A . 
H 5 HOH   74  374 61  HOH   HOH A . 
H 5 HOH   75  375 70  HOH   HOH A . 
H 5 HOH   76  376 49  HOH   HOH A . 
H 5 HOH   77  377 153 HOH   HOH A . 
H 5 HOH   78  378 130 HOH   HOH A . 
H 5 HOH   79  379 147 HOH   HOH A . 
H 5 HOH   80  380 155 HOH   HOH A . 
H 5 HOH   81  381 23  HOH   HOH A . 
H 5 HOH   82  382 296 HOH   HOH A . 
H 5 HOH   83  383 300 HOH   HOH A . 
H 5 HOH   84  384 85  HOH   HOH A . 
H 5 HOH   85  385 119 HOH   HOH A . 
H 5 HOH   86  386 78  HOH   HOH A . 
H 5 HOH   87  387 88  HOH   HOH A . 
H 5 HOH   88  388 217 HOH   HOH A . 
H 5 HOH   89  389 312 HOH   HOH A . 
H 5 HOH   90  390 6   HOH   HOH A . 
H 5 HOH   91  391 185 HOH   HOH A . 
H 5 HOH   92  392 55  HOH   HOH A . 
H 5 HOH   93  393 2   HOH   HOH A . 
H 5 HOH   94  394 79  HOH   HOH A . 
H 5 HOH   95  395 159 HOH   HOH A . 
H 5 HOH   96  396 222 HOH   HOH A . 
H 5 HOH   97  397 73  HOH   HOH A . 
H 5 HOH   98  398 53  HOH   HOH A . 
H 5 HOH   99  399 92  HOH   HOH A . 
H 5 HOH   100 400 227 HOH   HOH A . 
H 5 HOH   101 401 120 HOH   HOH A . 
H 5 HOH   102 402 112 HOH   HOH A . 
H 5 HOH   103 403 187 HOH   HOH A . 
H 5 HOH   104 404 305 HOH   HOH A . 
H 5 HOH   105 405 210 HOH   HOH A . 
H 5 HOH   106 406 340 HOH   HOH A . 
H 5 HOH   107 407 141 HOH   HOH A . 
H 5 HOH   108 408 291 HOH   HOH A . 
H 5 HOH   109 409 310 HOH   HOH A . 
H 5 HOH   110 410 150 HOH   HOH A . 
H 5 HOH   111 411 1   HOH   HOH A . 
H 5 HOH   112 412 313 HOH   HOH A . 
H 5 HOH   113 413 332 HOH   HOH A . 
H 5 HOH   114 414 288 HOH   HOH A . 
H 5 HOH   115 415 34  HOH   HOH A . 
H 5 HOH   116 416 100 HOH   HOH A . 
H 5 HOH   117 417 32  HOH   HOH A . 
H 5 HOH   118 418 294 HOH   HOH A . 
H 5 HOH   119 419 221 HOH   HOH A . 
H 5 HOH   120 420 318 HOH   HOH A . 
H 5 HOH   121 421 134 HOH   HOH A . 
H 5 HOH   122 422 325 HOH   HOH A . 
H 5 HOH   123 423 132 HOH   HOH A . 
H 5 HOH   124 424 320 HOH   HOH A . 
H 5 HOH   125 425 116 HOH   HOH A . 
H 5 HOH   126 426 117 HOH   HOH A . 
H 5 HOH   127 427 8   HOH   HOH A . 
H 5 HOH   128 428 205 HOH   HOH A . 
H 5 HOH   129 429 111 HOH   HOH A . 
H 5 HOH   130 430 45  HOH   HOH A . 
H 5 HOH   131 431 292 HOH   HOH A . 
H 5 HOH   132 432 108 HOH   HOH A . 
H 5 HOH   133 433 343 HOH   HOH A . 
H 5 HOH   134 434 297 HOH   HOH A . 
H 5 HOH   135 435 299 HOH   HOH A . 
H 5 HOH   136 436 342 HOH   HOH A . 
H 5 HOH   137 437 337 HOH   HOH A . 
H 5 HOH   138 438 146 HOH   HOH A . 
H 5 HOH   139 439 229 HOH   HOH A . 
H 5 HOH   140 440 322 HOH   HOH A . 
H 5 HOH   141 441 269 HOH   HOH A . 
H 5 HOH   142 442 126 HOH   HOH A . 
H 5 HOH   143 443 54  HOH   HOH A . 
H 5 HOH   144 444 347 HOH   HOH A . 
H 5 HOH   145 445 245 HOH   HOH A . 
H 5 HOH   146 446 262 HOH   HOH A . 
H 5 HOH   147 447 338 HOH   HOH A . 
H 5 HOH   148 448 156 HOH   HOH A . 
H 5 HOH   149 449 314 HOH   HOH A . 
H 5 HOH   150 450 206 HOH   HOH A . 
H 5 HOH   151 451 233 HOH   HOH A . 
H 5 HOH   152 452 207 HOH   HOH A . 
H 5 HOH   153 453 345 HOH   HOH A . 
H 5 HOH   154 454 361 HOH   HOH A . 
H 5 HOH   155 455 265 HOH   HOH A . 
H 5 HOH   156 456 264 HOH   HOH A . 
H 5 HOH   157 457 330 HOH   HOH A . 
H 5 HOH   158 458 283 HOH   HOH A . 
H 5 HOH   159 459 232 HOH   HOH A . 
H 5 HOH   160 460 355 HOH   HOH A . 
H 5 HOH   161 461 352 HOH   HOH A . 
H 5 HOH   162 462 211 HOH   HOH A . 
H 5 HOH   163 463 176 HOH   HOH A . 
H 5 HOH   164 464 254 HOH   HOH A . 
H 5 HOH   165 465 225 HOH   HOH A . 
H 5 HOH   166 466 282 HOH   HOH A . 
I 5 HOH   1   301 358 HOH   HOH C . 
I 5 HOH   2   302 98  HOH   HOH C . 
I 5 HOH   3   303 103 HOH   HOH C . 
I 5 HOH   4   304 170 HOH   HOH C . 
I 5 HOH   5   305 252 HOH   HOH C . 
I 5 HOH   6   306 323 HOH   HOH C . 
I 5 HOH   7   307 298 HOH   HOH C . 
I 5 HOH   8   308 306 HOH   HOH C . 
I 5 HOH   9   309 128 HOH   HOH C . 
I 5 HOH   10  310 244 HOH   HOH C . 
I 5 HOH   11  311 64  HOH   HOH C . 
I 5 HOH   12  312 357 HOH   HOH C . 
I 5 HOH   13  313 19  HOH   HOH C . 
I 5 HOH   14  314 215 HOH   HOH C . 
I 5 HOH   15  315 76  HOH   HOH C . 
I 5 HOH   16  316 160 HOH   HOH C . 
I 5 HOH   17  317 62  HOH   HOH C . 
I 5 HOH   18  318 231 HOH   HOH C . 
I 5 HOH   19  319 224 HOH   HOH C . 
I 5 HOH   20  320 63  HOH   HOH C . 
I 5 HOH   21  321 328 HOH   HOH C . 
I 5 HOH   22  322 284 HOH   HOH C . 
I 5 HOH   23  323 136 HOH   HOH C . 
I 5 HOH   24  324 219 HOH   HOH C . 
I 5 HOH   25  325 228 HOH   HOH C . 
I 5 HOH   26  326 97  HOH   HOH C . 
I 5 HOH   27  327 140 HOH   HOH C . 
I 5 HOH   28  328 165 HOH   HOH C . 
I 5 HOH   29  329 164 HOH   HOH C . 
I 5 HOH   30  330 174 HOH   HOH C . 
I 5 HOH   31  331 331 HOH   HOH C . 
I 5 HOH   32  332 91  HOH   HOH C . 
I 5 HOH   33  333 216 HOH   HOH C . 
I 5 HOH   34  334 16  HOH   HOH C . 
I 5 HOH   35  335 22  HOH   HOH C . 
I 5 HOH   36  336 162 HOH   HOH C . 
I 5 HOH   37  337 281 HOH   HOH C . 
I 5 HOH   38  338 106 HOH   HOH C . 
I 5 HOH   39  339 261 HOH   HOH C . 
I 5 HOH   40  340 168 HOH   HOH C . 
I 5 HOH   41  341 293 HOH   HOH C . 
I 5 HOH   42  342 334 HOH   HOH C . 
I 5 HOH   43  343 175 HOH   HOH C . 
I 5 HOH   44  344 82  HOH   HOH C . 
I 5 HOH   45  345 9   HOH   HOH C . 
I 5 HOH   46  346 33  HOH   HOH C . 
I 5 HOH   47  347 59  HOH   HOH C . 
I 5 HOH   48  348 14  HOH   HOH C . 
I 5 HOH   49  349 30  HOH   HOH C . 
I 5 HOH   50  350 143 HOH   HOH C . 
I 5 HOH   51  351 151 HOH   HOH C . 
I 5 HOH   52  352 204 HOH   HOH C . 
I 5 HOH   53  353 69  HOH   HOH C . 
I 5 HOH   54  354 335 HOH   HOH C . 
I 5 HOH   55  355 7   HOH   HOH C . 
I 5 HOH   56  356 66  HOH   HOH C . 
I 5 HOH   57  357 135 HOH   HOH C . 
I 5 HOH   58  358 315 HOH   HOH C . 
I 5 HOH   59  359 18  HOH   HOH C . 
I 5 HOH   60  360 127 HOH   HOH C . 
I 5 HOH   61  361 333 HOH   HOH C . 
I 5 HOH   62  362 24  HOH   HOH C . 
I 5 HOH   63  363 114 HOH   HOH C . 
I 5 HOH   64  364 11  HOH   HOH C . 
I 5 HOH   65  365 172 HOH   HOH C . 
I 5 HOH   66  366 109 HOH   HOH C . 
I 5 HOH   67  367 41  HOH   HOH C . 
I 5 HOH   68  368 144 HOH   HOH C . 
I 5 HOH   69  369 101 HOH   HOH C . 
I 5 HOH   70  370 304 HOH   HOH C . 
I 5 HOH   71  371 360 HOH   HOH C . 
I 5 HOH   72  372 218 HOH   HOH C . 
I 5 HOH   73  373 316 HOH   HOH C . 
I 5 HOH   74  374 43  HOH   HOH C . 
I 5 HOH   75  375 44  HOH   HOH C . 
I 5 HOH   76  376 89  HOH   HOH C . 
I 5 HOH   77  377 56  HOH   HOH C . 
I 5 HOH   78  378 154 HOH   HOH C . 
I 5 HOH   79  379 242 HOH   HOH C . 
I 5 HOH   80  380 107 HOH   HOH C . 
I 5 HOH   81  381 20  HOH   HOH C . 
I 5 HOH   82  382 329 HOH   HOH C . 
I 5 HOH   83  383 339 HOH   HOH C . 
I 5 HOH   84  384 303 HOH   HOH C . 
I 5 HOH   85  385 75  HOH   HOH C . 
I 5 HOH   86  386 214 HOH   HOH C . 
I 5 HOH   87  387 48  HOH   HOH C . 
I 5 HOH   88  388 259 HOH   HOH C . 
I 5 HOH   89  389 243 HOH   HOH C . 
I 5 HOH   90  390 212 HOH   HOH C . 
I 5 HOH   91  391 302 HOH   HOH C . 
I 5 HOH   92  392 189 HOH   HOH C . 
I 5 HOH   93  393 46  HOH   HOH C . 
I 5 HOH   94  394 123 HOH   HOH C . 
I 5 HOH   95  395 319 HOH   HOH C . 
I 5 HOH   96  396 131 HOH   HOH C . 
I 5 HOH   97  397 180 HOH   HOH C . 
I 5 HOH   98  398 236 HOH   HOH C . 
I 5 HOH   99  399 17  HOH   HOH C . 
I 5 HOH   100 400 15  HOH   HOH C . 
I 5 HOH   101 401 149 HOH   HOH C . 
I 5 HOH   102 402 110 HOH   HOH C . 
I 5 HOH   103 403 129 HOH   HOH C . 
I 5 HOH   104 404 96  HOH   HOH C . 
I 5 HOH   105 405 234 HOH   HOH C . 
I 5 HOH   106 406 28  HOH   HOH C . 
I 5 HOH   107 407 145 HOH   HOH C . 
I 5 HOH   108 408 99  HOH   HOH C . 
I 5 HOH   109 409 290 HOH   HOH C . 
I 5 HOH   110 410 203 HOH   HOH C . 
I 5 HOH   111 411 321 HOH   HOH C . 
I 5 HOH   112 412 25  HOH   HOH C . 
I 5 HOH   113 413 263 HOH   HOH C . 
I 5 HOH   114 414 173 HOH   HOH C . 
I 5 HOH   115 415 289 HOH   HOH C . 
I 5 HOH   116 416 167 HOH   HOH C . 
I 5 HOH   117 417 230 HOH   HOH C . 
I 5 HOH   118 418 94  HOH   HOH C . 
I 5 HOH   119 419 124 HOH   HOH C . 
I 5 HOH   120 420 182 HOH   HOH C . 
I 5 HOH   121 421 179 HOH   HOH C . 
I 5 HOH   122 422 121 HOH   HOH C . 
I 5 HOH   123 423 194 HOH   HOH C . 
I 5 HOH   124 424 47  HOH   HOH C . 
I 5 HOH   125 425 138 HOH   HOH C . 
I 5 HOH   126 426 31  HOH   HOH C . 
I 5 HOH   127 427 40  HOH   HOH C . 
I 5 HOH   128 428 235 HOH   HOH C . 
I 5 HOH   129 429 74  HOH   HOH C . 
I 5 HOH   130 430 250 HOH   HOH C . 
I 5 HOH   131 431 139 HOH   HOH C . 
I 5 HOH   132 432 188 HOH   HOH C . 
I 5 HOH   133 433 246 HOH   HOH C . 
I 5 HOH   134 434 37  HOH   HOH C . 
I 5 HOH   135 435 67  HOH   HOH C . 
I 5 HOH   136 436 327 HOH   HOH C . 
I 5 HOH   137 437 125 HOH   HOH C . 
I 5 HOH   138 438 301 HOH   HOH C . 
I 5 HOH   139 439 324 HOH   HOH C . 
I 5 HOH   140 440 90  HOH   HOH C . 
I 5 HOH   141 441 163 HOH   HOH C . 
I 5 HOH   142 442 157 HOH   HOH C . 
I 5 HOH   143 443 152 HOH   HOH C . 
I 5 HOH   144 444 353 HOH   HOH C . 
I 5 HOH   145 445 273 HOH   HOH C . 
I 5 HOH   146 446 166 HOH   HOH C . 
I 5 HOH   147 447 198 HOH   HOH C . 
I 5 HOH   148 448 191 HOH   HOH C . 
I 5 HOH   149 449 84  HOH   HOH C . 
I 5 HOH   150 450 277 HOH   HOH C . 
I 5 HOH   151 451 105 HOH   HOH C . 
I 5 HOH   152 452 274 HOH   HOH C . 
I 5 HOH   153 453 356 HOH   HOH C . 
I 5 HOH   154 454 3   HOH   HOH C . 
I 5 HOH   155 455 278 HOH   HOH C . 
I 5 HOH   156 456 239 HOH   HOH C . 
I 5 HOH   157 457 359 HOH   HOH C . 
I 5 HOH   158 458 260 HOH   HOH C . 
I 5 HOH   159 459 195 HOH   HOH C . 
I 5 HOH   160 460 196 HOH   HOH C . 
I 5 HOH   161 461 354 HOH   HOH C . 
I 5 HOH   162 462 346 HOH   HOH C . 
I 5 HOH   163 463 275 HOH   HOH C . 
I 5 HOH   164 464 81  HOH   HOH C . 
I 5 HOH   165 465 192 HOH   HOH C . 
I 5 HOH   166 466 349 HOH   HOH C . 
I 5 HOH   167 467 241 HOH   HOH C . 
I 5 HOH   168 468 71  HOH   HOH C . 
I 5 HOH   169 469 122 HOH   HOH C . 
I 5 HOH   170 470 348 HOH   HOH C . 
I 5 HOH   171 471 249 HOH   HOH C . 
I 5 HOH   172 472 276 HOH   HOH C . 
I 5 HOH   173 473 220 HOH   HOH C . 
I 5 HOH   174 474 280 HOH   HOH C . 
I 5 HOH   175 475 240 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           7I4I 
_cell.length_a           86.634 
_cell.length_b           57.175 
_cell.length_c           64.780 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.67 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I4I 
_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          7I4I 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.52 
_exptl_crystal.density_percent_sol   51.10 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-01-17 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92201 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I4I 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             64.57 
_reflns.d_resolution_high            1.40 
_reflns.number_obs                   62150 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.075 
_reflns.pdbx_netI_over_sigmaI        19.9 
_reflns.pdbx_redundancy              6.3 
_reflns.pdbx_Rrim_I_all              0.082 
_reflns.pdbx_Rpim_I_all              0.032 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     389719 
_reflns.pdbx_chi_squared             0.87 
_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                  1.40 
_reflns_shell.d_res_low                   1.42 
_reflns_shell.number_measured_all         12694 
_reflns_shell.number_unique_obs           2997 
_reflns_shell.Rmerge_I_obs                0.961 
_reflns_shell.pdbx_chi_squared            0.19 
_reflns_shell.pdbx_redundancy             4.2 
_reflns_shell.percent_possible_obs        98.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.8 
_reflns_shell.pdbx_Rrim_I_all             1.131 
_reflns_shell.pdbx_Rpim_I_all             0.570 
_reflns_shell.pdbx_CC_half                0.253 
_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                                 7I4I 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     62084 
_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                             19.99 
_refine.ls_d_res_high                            1.400 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_R_factor_obs                          0.1822 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1815 
_refine.ls_R_factor_R_free                       0.1957 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.980 
_refine.ls_number_reflns_R_free                  3094 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.962 
_refine.B_iso_mean                               20.64 
_refine.aniso_B[1][1]                            -1.72090 
_refine.aniso_B[2][2]                            0.10150 
_refine.aniso_B[3][3]                            1.61940 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.37880 
_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             0.056 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.055 
_refine.pdbx_overall_SU_R_Blow_DPI               0.060 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.058 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I4I 
_refine_analyze.Luzzati_coordinate_error_obs    0.17 
_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         28 
_refine_hist.number_atoms_solvent             341 
_refine_hist.number_atoms_total               2535 
_refine_hist.d_res_high                       1.400 
_refine_hist.d_res_low                        19.99 
# 
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  2261 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.02  ? 2.00  3081 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  761  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  395  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2261 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.55  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.51 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  279  '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  2026 '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                       1.40 
_refine_ls_shell.d_res_low                        1.41 
_refine_ls_shell.number_reflns_R_work             1192 
_refine_ls_shell.R_factor_R_work                  0.2388 
_refine_ls_shell.percent_reflns_obs               99.14 
_refine_ls_shell.R_factor_R_free                  0.2822 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.03 
_refine_ls_shell.number_reflns_R_free             50 
_refine_ls_shell.number_reflns_all                1242 
_refine_ls_shell.R_factor_all                     0.2403 
# 
_struct.entry_id                  7I4I 
_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-0036619-001 (A71EV2A-x4708)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I4I 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I4I A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I4I 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,H   
2 1 B,E,F,G,I 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P6  AA6 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P7  AA7 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P8  AA8 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P9  AA9 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P10 AB1 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P11 AB2 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.451 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.238 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 1.995 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 202 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 202 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 202 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 202 1_555 ? ? ? ? ? ? ? 2.099 ? ? 
# 
_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_555 107.3 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 103.7 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.8 ? 
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_555 102.1 ? 
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_555 104.8 ? 
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_555 121.5 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 110.3 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.0 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 117.7 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 103.4 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 102.1 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 115.4 ? 
# 
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 ? THR A 120 ? GLY A 119 THR A 126 
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 SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
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                   7I4I 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 336 ? ? O A HOH 413 ? ? 1.62 
2 1 O C HOH 331 ? ? O C HOH 369 ? ? 1.97 
3 1 O A HOH 354 ? ? O A HOH 442 ? ? 2.07 
# 
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 14.9369 8.2631   14.3568 -0.0220 -0.0129 0.0041 0.0220 0.0026 0.0046 1.4156 0.8529 0.8167 0.9602  
-0.5176 -0.4714 -0.0082 0.0436 0.1352 0.0689 0.0622 0.0290 -0.0629 -0.1193 -0.0540 
'X-RAY DIFFRACTION' 2 ? refined 25.7497 -20.1815 17.7348 -0.0366 -0.0163 0.0118 0.0100 0.0020 0.0167 0.7302 0.9543 0.3016 -0.2528 
-0.1338 -0.0519 0.0074  0.0027 0.1196 0.0159 0.0369 0.0040 0.0471  -0.0036 -0.0443 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
5 1 Y 1 C ALA 147 ? B ALA 141 
6 1 Y 1 C MET 148 ? B MET 142 
7 1 Y 1 C GLU 149 ? B GLU 143 
8 1 Y 1 C GLN 150 ? B GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1B2W N1   N  N N 1   
A1B2W C4   C  N N 2   
A1B2W C5   C  N N 3   
A1B2W C6   C  N N 4   
A1B2W C7   C  N N 5   
A1B2W C8   C  N N 6   
A1B2W C10  C  N N 7   
A1B2W O1   O  N N 8   
A1B2W C3   C  N N 9   
A1B2W C2   C  N N 10  
A1B2W C11  C  N N 11  
A1B2W C1   C  N S 12  
A1B2W C    C  N N 13  
A1B2W O    O  N N 14  
A1B2W N    N  N N 15  
A1B2W O2   O  N N 16  
A1B2W C9   C  N N 17  
A1B2W S    S  N N 18  
A1B2W H8   H  N N 19  
A1B2W H7   H  N N 20  
A1B2W H10  H  N N 21  
A1B2W H11  H  N N 22  
A1B2W H12  H  N N 23  
A1B2W H13  H  N N 24  
A1B2W H16  H  N N 25  
A1B2W H17  H  N N 26  
A1B2W H6   H  N N 27  
A1B2W H5   H  N N 28  
A1B2W H4   H  N N 29  
A1B2W H3   H  N N 30  
A1B2W H19  H  N N 31  
A1B2W H18  H  N N 32  
A1B2W H    H  N N 33  
A1B2W H1   H  N N 34  
A1B2W H2   H  N N 35  
A1B2W H9   H  N N 36  
A1B2W H14  H  N N 37  
A1B2W H15  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 
A1B2W N   C    sing N N 1   
A1B2W O   C    doub N N 2   
A1B2W C   C1   sing N N 3   
A1B2W C1  C2   sing N N 4   
A1B2W C2  C3   sing N N 5   
A1B2W C3  C4   sing N N 6   
A1B2W C4  N1   sing N N 7   
A1B2W N1  C5   sing N N 8   
A1B2W C5  O1   doub N N 9   
A1B2W C6  C5   sing N N 10  
A1B2W O2  C6   sing N N 11  
A1B2W C6  C7   sing N N 12  
A1B2W C7  C8   sing N N 13  
A1B2W C8  S    sing N N 14  
A1B2W S   C9   sing N N 15  
A1B2W C9  C10  sing N N 16  
A1B2W C10 C6   sing N N 17  
A1B2W C11 N1   sing N N 18  
A1B2W C1  C11  sing N N 19  
A1B2W C4  H8   sing N N 20  
A1B2W C4  H7   sing N N 21  
A1B2W C7  H10  sing N N 22  
A1B2W C7  H11  sing N N 23  
A1B2W C8  H12  sing N N 24  
A1B2W C8  H13  sing N N 25  
A1B2W C10 H16  sing N N 26  
A1B2W C10 H17  sing N N 27  
A1B2W C3  H6   sing N N 28  
A1B2W C3  H5   sing N N 29  
A1B2W C2  H4   sing N N 30  
A1B2W C2  H3   sing N N 31  
A1B2W C11 H19  sing N N 32  
A1B2W C11 H18  sing N N 33  
A1B2W C1  H    sing N N 34  
A1B2W N   H1   sing N N 35  
A1B2W N   H2   sing N N 36  
A1B2W O2  H9   sing N N 37  
A1B2W C9  H14  sing N N 38  
A1B2W C9  H15  sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
DMS   S   O    doub N N 122 
DMS   S   C1   sing N N 123 
DMS   S   C2   sing N N 124 
DMS   C1  H11  sing N N 125 
DMS   C1  H12  sing N N 126 
DMS   C1  H13  sing N N 127 
DMS   C2  H21  sing N N 128 
DMS   C2  H22  sing N N 129 
DMS   C2  H23  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
HIS   N   CA   sing N N 177 
HIS   N   H    sing N N 178 
HIS   N   H2   sing N N 179 
HIS   CA  C    sing N N 180 
HIS   CA  CB   sing N N 181 
HIS   CA  HA   sing N N 182 
HIS   C   O    doub N N 183 
HIS   C   OXT  sing N N 184 
HIS   CB  CG   sing N N 185 
HIS   CB  HB2  sing N N 186 
HIS   CB  HB3  sing N N 187 
HIS   CG  ND1  sing Y N 188 
HIS   CG  CD2  doub Y N 189 
HIS   ND1 CE1  doub Y N 190 
HIS   ND1 HD1  sing N N 191 
HIS   CD2 NE2  sing Y N 192 
HIS   CD2 HD2  sing N N 193 
HIS   CE1 NE2  sing Y N 194 
HIS   CE1 HE1  sing N N 195 
HIS   NE2 HE2  sing N N 196 
HIS   OXT HXT  sing N N 197 
HOH   O   H1   sing N N 198 
HOH   O   H2   sing N N 199 
ILE   N   CA   sing N N 200 
ILE   N   H    sing N N 201 
ILE   N   H2   sing N N 202 
ILE   CA  C    sing N N 203 
ILE   CA  CB   sing N N 204 
ILE   CA  HA   sing N N 205 
ILE   C   O    doub N N 206 
ILE   C   OXT  sing N N 207 
ILE   CB  CG1  sing N N 208 
ILE   CB  CG2  sing N N 209 
ILE   CB  HB   sing N N 210 
ILE   CG1 CD1  sing N N 211 
ILE   CG1 HG12 sing N N 212 
ILE   CG1 HG13 sing N N 213 
ILE   CG2 HG21 sing N N 214 
ILE   CG2 HG22 sing N N 215 
ILE   CG2 HG23 sing N N 216 
ILE   CD1 HD11 sing N N 217 
ILE   CD1 HD12 sing N N 218 
ILE   CD1 HD13 sing N N 219 
ILE   OXT HXT  sing N N 220 
LEU   N   CA   sing N N 221 
LEU   N   H    sing N N 222 
LEU   N   H2   sing N N 223 
LEU   CA  C    sing N N 224 
LEU   CA  CB   sing N N 225 
LEU   CA  HA   sing N N 226 
LEU   C   O    doub N N 227 
LEU   C   OXT  sing N N 228 
LEU   CB  CG   sing N N 229 
LEU   CB  HB2  sing N N 230 
LEU   CB  HB3  sing N N 231 
LEU   CG  CD1  sing N N 232 
LEU   CG  CD2  sing N N 233 
LEU   CG  HG   sing N N 234 
LEU   CD1 HD11 sing N N 235 
LEU   CD1 HD12 sing N N 236 
LEU   CD1 HD13 sing N N 237 
LEU   CD2 HD21 sing N N 238 
LEU   CD2 HD22 sing N N 239 
LEU   CD2 HD23 sing N N 240 
LEU   OXT HXT  sing N N 241 
LYS   N   CA   sing N N 242 
LYS   N   H    sing N N 243 
LYS   N   H2   sing N N 244 
LYS   CA  C    sing N N 245 
LYS   CA  CB   sing N N 246 
LYS   CA  HA   sing N N 247 
LYS   C   O    doub N N 248 
LYS   C   OXT  sing N N 249 
LYS   CB  CG   sing N N 250 
LYS   CB  HB2  sing N N 251 
LYS   CB  HB3  sing N N 252 
LYS   CG  CD   sing N N 253 
LYS   CG  HG2  sing N N 254 
LYS   CG  HG3  sing N N 255 
LYS   CD  CE   sing N N 256 
LYS   CD  HD2  sing N N 257 
LYS   CD  HD3  sing N N 258 
LYS   CE  NZ   sing N N 259 
LYS   CE  HE2  sing N N 260 
LYS   CE  HE3  sing N N 261 
LYS   NZ  HZ1  sing N N 262 
LYS   NZ  HZ2  sing N N 263 
LYS   NZ  HZ3  sing N N 264 
LYS   OXT HXT  sing N N 265 
MET   N   CA   sing N N 266 
MET   N   H    sing N N 267 
MET   N   H2   sing N N 268 
MET   CA  C    sing N N 269 
MET   CA  CB   sing N N 270 
MET   CA  HA   sing N N 271 
MET   C   O    doub N N 272 
MET   C   OXT  sing N N 273 
MET   CB  CG   sing N N 274 
MET   CB  HB2  sing N N 275 
MET   CB  HB3  sing N N 276 
MET   CG  SD   sing N N 277 
MET   CG  HG2  sing N N 278 
MET   CG  HG3  sing N N 279 
MET   SD  CE   sing N N 280 
MET   CE  HE1  sing N N 281 
MET   CE  HE2  sing N N 282 
MET   CE  HE3  sing N N 283 
MET   OXT HXT  sing N N 284 
PHE   N   CA   sing N N 285 
PHE   N   H    sing N N 286 
PHE   N   H2   sing N N 287 
PHE   CA  C    sing N N 288 
PHE   CA  CB   sing N N 289 
PHE   CA  HA   sing N N 290 
PHE   C   O    doub N N 291 
PHE   C   OXT  sing N N 292 
PHE   CB  CG   sing N N 293 
PHE   CB  HB2  sing N N 294 
PHE   CB  HB3  sing N N 295 
PHE   CG  CD1  doub Y N 296 
PHE   CG  CD2  sing Y N 297 
PHE   CD1 CE1  sing Y N 298 
PHE   CD1 HD1  sing N N 299 
PHE   CD2 CE2  doub Y N 300 
PHE   CD2 HD2  sing N N 301 
PHE   CE1 CZ   doub Y N 302 
PHE   CE1 HE1  sing N N 303 
PHE   CE2 CZ   sing Y N 304 
PHE   CE2 HE2  sing N N 305 
PHE   CZ  HZ   sing N N 306 
PHE   OXT HXT  sing N N 307 
PRO   N   CA   sing N N 308 
PRO   N   CD   sing N N 309 
PRO   N   H    sing N N 310 
PRO   CA  C    sing N N 311 
PRO   CA  CB   sing N N 312 
PRO   CA  HA   sing N N 313 
PRO   C   O    doub N N 314 
PRO   C   OXT  sing N N 315 
PRO   CB  CG   sing N N 316 
PRO   CB  HB2  sing N N 317 
PRO   CB  HB3  sing N N 318 
PRO   CG  CD   sing N N 319 
PRO   CG  HG2  sing N N 320 
PRO   CG  HG3  sing N N 321 
PRO   CD  HD2  sing N N 322 
PRO   CD  HD3  sing N N 323 
PRO   OXT HXT  sing N N 324 
SER   N   CA   sing N N 325 
SER   N   H    sing N N 326 
SER   N   H2   sing N N 327 
SER   CA  C    sing N N 328 
SER   CA  CB   sing N N 329 
SER   CA  HA   sing N N 330 
SER   C   O    doub N N 331 
SER   C   OXT  sing N N 332 
SER   CB  OG   sing N N 333 
SER   CB  HB2  sing N N 334 
SER   CB  HB3  sing N N 335 
SER   OG  HG   sing N N 336 
SER   OXT HXT  sing N N 337 
THR   N   CA   sing N N 338 
THR   N   H    sing N N 339 
THR   N   H2   sing N N 340 
THR   CA  C    sing N N 341 
THR   CA  CB   sing N N 342 
THR   CA  HA   sing N N 343 
THR   C   O    doub N N 344 
THR   C   OXT  sing N N 345 
THR   CB  OG1  sing N N 346 
THR   CB  CG2  sing N N 347 
THR   CB  HB   sing N N 348 
THR   OG1 HG1  sing N N 349 
THR   CG2 HG21 sing N N 350 
THR   CG2 HG22 sing N N 351 
THR   CG2 HG23 sing N N 352 
THR   OXT HXT  sing N N 353 
TRP   N   CA   sing N N 354 
TRP   N   H    sing N N 355 
TRP   N   H2   sing N N 356 
TRP   CA  C    sing N N 357 
TRP   CA  CB   sing N N 358 
TRP   CA  HA   sing N N 359 
TRP   C   O    doub N N 360 
TRP   C   OXT  sing N N 361 
TRP   CB  CG   sing N N 362 
TRP   CB  HB2  sing N N 363 
TRP   CB  HB3  sing N N 364 
TRP   CG  CD1  doub Y N 365 
TRP   CG  CD2  sing Y N 366 
TRP   CD1 NE1  sing Y N 367 
TRP   CD1 HD1  sing N N 368 
TRP   CD2 CE2  doub Y N 369 
TRP   CD2 CE3  sing Y N 370 
TRP   NE1 CE2  sing Y N 371 
TRP   NE1 HE1  sing N N 372 
TRP   CE2 CZ2  sing Y N 373 
TRP   CE3 CZ3  doub Y N 374 
TRP   CE3 HE3  sing N N 375 
TRP   CZ2 CH2  doub Y N 376 
TRP   CZ2 HZ2  sing N N 377 
TRP   CZ3 CH2  sing Y N 378 
TRP   CZ3 HZ3  sing N N 379 
TRP   CH2 HH2  sing N N 380 
TRP   OXT HXT  sing N N 381 
TYR   N   CA   sing N N 382 
TYR   N   H    sing N N 383 
TYR   N   H2   sing N N 384 
TYR   CA  C    sing N N 385 
TYR   CA  CB   sing N N 386 
TYR   CA  HA   sing N N 387 
TYR   C   O    doub N N 388 
TYR   C   OXT  sing N N 389 
TYR   CB  CG   sing N N 390 
TYR   CB  HB2  sing N N 391 
TYR   CB  HB3  sing N N 392 
TYR   CG  CD1  doub Y N 393 
TYR   CG  CD2  sing Y N 394 
TYR   CD1 CE1  sing Y N 395 
TYR   CD1 HD1  sing N N 396 
TYR   CD2 CE2  doub Y N 397 
TYR   CD2 HD2  sing N N 398 
TYR   CE1 CZ   doub Y N 399 
TYR   CE1 HE1  sing N N 400 
TYR   CE2 CZ   sing Y N 401 
TYR   CE2 HE2  sing N N 402 
TYR   CZ  OH   sing N N 403 
TYR   OH  HH   sing N N 404 
TYR   OXT HXT  sing N N 405 
VAL   N   CA   sing N N 406 
VAL   N   H    sing N N 407 
VAL   N   H2   sing N N 408 
VAL   CA  C    sing N N 409 
VAL   CA  CB   sing N N 410 
VAL   CA  HA   sing N N 411 
VAL   C   O    doub N N 412 
VAL   C   OXT  sing N N 413 
VAL   CB  CG1  sing N N 414 
VAL   CB  CG2  sing N N 415 
VAL   CB  HB   sing N N 416 
VAL   CG1 HG11 sing N N 417 
VAL   CG1 HG12 sing N N 418 
VAL   CG1 HG13 sing N N 419 
VAL   CG2 HG21 sing N N 420 
VAL   CG2 HG22 sing N N 421 
VAL   CG2 HG23 sing N N 422 
VAL   OXT HXT  sing N N 423 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I4I 
_atom_sites.fract_transf_matrix[1][1]   0.011543 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000943 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017490 
_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]   0.015488 
_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   ? 17.658 8.142   24.795 1.00 17.53 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.896 8.239   24.009 1.00 17.48 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.044 7.020   23.095 1.00 16.68 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.330 6.018   23.259 1.00 17.11 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.091 8.338   24.962 1.00 21.22 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.214 7.113   25.664 1.00 24.37 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.960 7.101   22.131 1.00 15.27 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.207 5.990   21.227 1.00 14.59 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.590 6.455   19.839 1.00 13.51 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.259 7.564   19.430 1.00 15.26 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.281 5.608   19.129 1.00 12.58 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.764 5.945   17.799 1.00 12.85 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.735 4.726   16.900 1.00 12.84 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.658 3.573   17.358 1.00 13.59 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.205 6.495   17.921 1.00 14.28 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.810 4.971   15.587 1.00 12.19 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.042 3.922   14.573 1.00 11.26 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.518 3.990   14.195 1.00 11.75 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.017 5.098   13.893 1.00 12.21 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.192 4.115   13.300 1.00 11.82 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.710 4.287   13.657 1.00 13.16 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.413 2.914   12.354 1.00 14.11 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.903 4.828   12.404 1.00 13.67 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.226 2.845   14.178 1.00 12.07 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.634 2.846   13.769 1.00 13.94 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.747 2.014   12.490 1.00 14.75 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.735 0.773   12.552 1.00 14.32 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.514 2.256   14.893 1.00 14.73 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.563 3.144   16.115 1.00 14.07 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.433 4.230   16.182 1.00 14.72 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.716 2.927   17.192 1.00 15.66 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.439 5.091   17.284 1.00 15.46 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.739 3.763   18.313 1.00 16.48 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.555 4.884   18.320 1.00 16.79 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.590 5.737   19.418 1.00 19.34 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.822 2.680   11.337 1.00 14.65 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.904 2.037   10.034 1.00 15.06 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.143 2.536   9.324  1.00 15.73 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.371 3.756   9.264  1.00 14.80 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.608 2.296   9.196  1.00 15.40 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.269 3.791   9.103  1.00 16.56 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.754 1.707   7.808  1.00 17.06 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.011 1.622   8.861  1.00 16.86 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.249 2.039   8.210  1.00 16.56 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.085 2.917   9.128  1.00 15.99 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.181 2.623   10.333 1.00 16.08 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.531 4.074   8.616  1.00 14.70 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.218 5.062   9.448  1.00 14.28 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.326 6.251   9.761  1.00 13.76 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.807 7.392   9.891  1.00 14.78 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.561 5.506   8.859  1.00 16.11 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.632 4.460   8.999  1.00 21.31 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.373 4.405   10.000 1.00 23.98 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.700 3.587   8.032  1.00 19.88 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.051 5.958   10.010 1.00 13.17 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.073 6.981   10.365 1.00 13.22 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.406 6.668   11.711 1.00 12.98 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.127 5.486   12.019 1.00 13.34 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.958 7.064   9.280  1.00 14.11 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.469 7.467   7.910  1.00 15.08 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.113 8.686   7.712  1.00 16.24 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.285 6.639   6.809  1.00 17.24 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.598 9.051   6.455  1.00 17.37 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.720 7.020   5.542  1.00 17.47 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.350 8.237   5.366  1.00 18.56 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.829 8.629   4.120  1.00 21.81 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.053 7.728   12.439 1.00 12.39 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.257 7.671   13.665 1.00 11.82 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.021 8.537   13.407 1.00 11.95 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.167 9.750   13.132 1.00 12.99 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.074 8.232   14.865 1.00 12.56 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.271 8.529   16.130 1.00 13.31 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.189 8.917   17.303 1.00 15.08 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.622 9.982   18.135 1.00 16.35 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 25.954 9.775   19.268 1.00 17.94 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.688 8.537   19.673 1.00 18.59 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.484 10.803  19.964 1.00 17.75 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.827 7.936   13.439 1.00 11.55 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.555 8.663   13.202 1.00 11.64 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.870 8.866   14.548 1.00 12.77 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.563 7.877   15.245 1.00 13.55 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.620 7.861   12.271 1.00 12.46 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.387 8.706   11.899 1.00 12.58 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.344 7.365   11.020 1.00 13.27 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.631 10.127  14.916 1.00 11.52 ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 20.985 10.453  16.206 0.50 11.64 ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.027 10.439  16.217 0.50 13.52 ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.887 11.454  16.004 1.00 12.71 ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.730 12.054  14.910 1.00 13.96 ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 21.987 11.035  17.248 0.50 10.89 ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.166 11.044  17.110 0.50 16.53 ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 22.902 9.960   17.781 0.50 11.52 ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.714 11.377  18.521 0.50 17.38 ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.740 12.283  16.712 0.50 9.01  ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.371 10.134  17.175 0.50 18.09 ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.044 11.649  17.040 1.00 12.84 ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.012 12.696  16.984 1.00 13.02 ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.815 14.026  16.998 1.00 13.40 ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.726 14.211  17.829 1.00 14.23 ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.153 12.679  18.262 1.00 13.59 ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.301 11.442  18.371 1.00 14.21 ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.729 10.419  18.974 1.00 14.42 ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.148 11.475  17.700 1.00 14.57 ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.455 14.969  16.104 1.00 13.02 ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.189 16.252  16.054 1.00 13.40 ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.134 16.949  17.423 1.00 15.58 ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.131 17.509  17.869 1.00 17.50 ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.584 17.145  14.963 1.00 14.13 ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.374 18.447  14.736 1.00 15.05 ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.629 19.330  13.747 1.00 17.33 ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.369 20.517  13.310 1.00 18.30 ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.331 21.692  13.925 1.00 20.84 ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.777 21.802  15.126 1.00 20.76 ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 19.940 22.748  13.389 1.00 21.15 ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 17.986 16.831  18.118 1.00 15.70 ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 17.825 17.530  19.396 1.00 17.89 ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.680 16.936  20.531 1.00 18.76 ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 18.806 17.566  21.584 1.00 20.46 ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.330 17.678  19.794 1.00 19.08 ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.667 16.437  20.292 1.00 19.71 ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.051 15.554  19.425 1.00 19.87 ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.424 16.042  21.567 1.00 21.16 ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.523 14.609  20.187 1.00 20.05 ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 14.711 14.867  21.486 1.00 20.87 ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.217 15.716  20.342 1.00 18.13 ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.090 15.062  21.329 1.00 17.54 ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.564 14.993  20.893 1.00 19.02 ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.380 14.366  21.561 1.00 19.46 ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.569 13.669  21.654 1.00 17.28 ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.168 13.645  22.231 1.00 19.06 ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.726 12.187  22.440 1.00 19.01 ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.070 14.439  23.556 1.00 21.25 ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 21.913 15.602  19.729 1.00 17.42 ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.291 15.589  19.251 1.00 17.02 ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.260 16.226  20.252 1.00 18.44 ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 23.936 17.257  20.876 1.00 19.32 ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.378 16.297  17.889 1.00 16.29 ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.441 15.609  20.381 1.00 17.64 ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.494 16.122  21.290 1.00 17.86 ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.417 17.129  20.582 1.00 18.77 ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.357 17.267  19.342 1.00 17.61 ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.359 14.924  21.788 1.00 19.90 ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.106 14.382  20.681 1.00 21.25 ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.551 13.849  22.494 1.00 20.97 ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.333 17.802  21.325 1.00 19.30 ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.316 18.666  20.698 1.00 19.61 ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.197 17.863  19.737 1.00 19.02 ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.472 18.327  18.633 1.00 19.04 ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.217 19.344  21.772 1.00 21.54 ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.439 20.020  21.186 1.00 29.97 ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.346 21.241  20.536 1.00 34.19 ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.708 19.556  21.055 1.00 33.81 ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.564 21.526  20.107 1.00 35.12 ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.422 20.535  20.374 1.00 36.28 ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.573 16.610  20.118 1.00 17.80 ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.399 15.802  19.228 1.00 17.97 ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.641 15.513  17.916 1.00 15.96 ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.239 15.546  16.844 1.00 17.26 ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 31.861 14.494  19.863 1.00 20.38 ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.840 13.762  18.965 1.00 28.60 ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 33.991 14.203  18.765 1.00 32.08 ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.382 12.677  18.328 1.00 30.77 ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.303 15.281  18.004 1.00 15.44 ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.523 15.097  16.769 1.00 14.44 ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.585 16.356  15.855 1.00 14.58 ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.816 16.236  14.649 1.00 14.29 ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.055 14.825  17.085 1.00 15.06 ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.788 13.447  17.661 1.00 16.32 ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.474 12.484  17.239 1.00 16.33 ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 25.946 13.345  18.594 1.00 16.76 ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.386 17.548  16.415 1.00 14.73 ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.430 18.793  15.634 1.00 14.85 ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.834 19.073  15.080 1.00 15.61 ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 29.951 19.620  13.985 1.00 16.72 ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 27.948 19.978  16.508 1.00 15.69 ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.449 20.046  16.629 1.00 15.25 ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.687 19.739  17.719 1.00 16.32 ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.531 20.497  15.613 1.00 16.07 ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.354 19.966  17.445 1.00 16.20 ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.227 20.392  16.139 1.00 16.17 ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.693 20.945  14.290 1.00 17.65 ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.091 20.778  15.397 1.00 17.47 ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.578 21.278  13.557 1.00 18.01 ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.309 21.255  14.116 1.00 18.20 ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 30.891 18.661  15.822 1.00 15.26 ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.266 18.848  15.387 1.00 15.81 ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.707 17.838  14.323 1.00 16.79 ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.731 18.029  13.686 1.00 17.86 ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.197 18.812  16.611 1.00 16.37 ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 31.902 16.769  14.092 1.00 15.61 ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.195 15.731  13.073 1.00 15.80 ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 30.946 15.537  12.209 1.00 15.50 ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.575 14.415  11.855 1.00 15.93 ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.594 14.400  13.758 1.00 17.21 ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 33.939 14.581  14.430 1.00 19.96 ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 34.977 14.547  13.769 1.00 22.29 ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 33.946 14.857  15.750 1.00 20.55 ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.306 16.632  11.855 1.00 14.92 ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.017 16.605  11.173 1.00 14.19 ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.084 16.174  9.733  1.00 15.24 ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.947 16.639  8.969  1.00 17.04 ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.420 18.036  11.233 1.00 14.28 ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.013 18.180  10.633 1.00 15.43 ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 25.979 17.389  11.452 1.00 15.24 ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.585 19.659  10.568 1.00 17.10 ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.165 15.279  9.339  1.00 13.45 ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.007 14.863  7.944  1.00 13.74 ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.765 15.574  7.358  1.00 14.44 ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.823 16.129  6.257  1.00 16.17 ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.884 13.327  7.832  1.00 13.94 ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.527 12.908  6.388  1.00 15.49 ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.181 12.659  8.339  1.00 14.92 ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.607 15.508  8.067  1.00 14.35 ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.353 16.058  7.566  1.00 15.23 ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.370 16.257  8.696  1.00 14.88 ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.400 15.494  9.673  1.00 14.20 ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.758 15.073  6.517  1.00 15.89 ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.343 15.331  6.070  1.00 16.20 ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.933 16.145  5.049  1.00 18.59 ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.151 14.683  6.568  1.00 15.48 ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.560 16.060  4.902  1.00 19.80 ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.058 15.168  5.816  1.00 17.50 ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.897 13.764  7.592  1.00 15.92 ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.736 14.717  6.027  1.00 18.21 ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.598 13.315  7.787  1.00 17.30 ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.533 13.809  7.034  1.00 18.20 ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.556 17.326  8.617  1.00 14.76 ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.525 17.509  9.628  1.00 15.12 ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.299 18.146  8.993  1.00 16.65 ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.409 18.937  8.037  1.00 17.13 ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.031 18.344  10.805 1.00 15.95 ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.633 19.696  10.445 1.00 17.23 ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.681 20.868  10.235 1.00 19.86 ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.050 21.821  9.506  1.00 20.72 ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.566 20.854  10.808 1.00 17.97 ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.108 17.836  9.544  1.00 15.16 ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.871 18.407  9.021  1.00 15.12 ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.892 18.564  10.189 1.00 15.81 ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.374 17.567  10.732 1.00 15.98 ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.302 17.471  7.926  1.00 17.23 ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.044 17.951  7.256  1.00 20.27 ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.203 18.530  7.942  1.00 23.06 ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.883 17.692  6.044  1.00 24.26 ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.675 19.817  10.597 1.00 16.50 ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.787 20.143  11.700 0.50 17.16 ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.800 20.083  11.725 0.50 17.75 ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.346 19.689  11.430 1.00 18.21 ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.668 19.192  12.345 1.00 18.70 ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.835 21.651  11.954 0.50 18.13 ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 15.922 21.543  12.154 0.50 20.62 ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 14.810 22.052  12.843 0.50 19.32 ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.518 22.376  11.086 0.50 24.96 ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.869 19.838  10.177 1.00 18.41 ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.490 19.429  9.855  1.00 18.75 ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.243 17.939  10.060 1.00 17.56 ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.101 17.560  10.295 1.00 18.77 ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.087 19.834  8.438  1.00 21.09 ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.666 18.998  7.450  1.00 26.27 ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.294 17.109  10.031 1.00 15.54 ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.191 15.643  10.231 1.00 15.42 ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.655 15.193  11.630 1.00 15.05 ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.586 13.991  11.922 1.00 14.49 ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.076 14.928  9.183  1.00 15.82 ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.524 15.072  7.763  1.00 17.08 ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.411 14.406  6.723  1.00 16.94 ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.335 12.955  6.863  1.00 15.45 ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.485 12.094  5.866  1.00 17.96 ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.737 12.531  4.629  1.00 19.38 ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.354 10.783  6.082  1.00 16.05 ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.226 16.108  12.447 1.00 14.47 ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.845 15.768  13.724 1.00 13.40 ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 15.997 14.764  13.583 1.00 13.47 ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.207 13.934  14.473 1.00 13.87 ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.835 15.292  14.791 1.00 13.77 ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.436 15.086  16.174 1.00 15.71 ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.274 15.902  16.592 1.00 16.80 ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.079 14.093  16.829 1.00 16.25 ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.801 14.884  12.493 1.00 13.40 ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.903 13.936  12.309 1.00 12.19 ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.269 14.661  12.187 1.00 12.84 ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.345 15.784  11.635 1.00 13.65 ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.693 13.137  11.028 1.00 12.64 ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.619 12.020  11.063 1.00 14.59 ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.525 11.325  9.703  1.00 15.47 ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.911 10.998  12.174 1.00 14.97 ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.320 14.007  12.679 1.00 12.33 ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.684 14.498  12.488 1.00 12.09 ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.551 13.253  12.357 1.00 12.80 ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.345 12.226  13.026 1.00 13.37 ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.146 15.337  13.714 1.00 12.58 ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.583 15.919  13.622 1.00 13.39 ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.675 17.285  14.313 1.00 14.87 ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.617 14.971  14.261 1.00 13.45 ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.519 13.320  11.419 1.00 12.03 ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.471 12.235  11.163 1.00 11.73 ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.886 12.745  11.316 1.00 11.98 ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.196 13.834  10.789 1.00 12.53 ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.253 11.647  9.752  1.00 12.30 ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.280 10.540  9.487  1.00 13.68 ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.819 11.100  9.614  1.00 14.34 ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.690 12.071  12.152 1.00 11.95 ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.096 12.419  12.331 1.00 12.05 ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 28.976 11.237  11.882 1.00 13.61 ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.506 10.100  11.667 1.00 13.77 ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.373 12.763  13.799 1.00 13.87 ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.041 11.691  14.673 1.00 14.93 ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.269 11.521  11.682 1.00 14.93 ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.216 10.475  11.273 1.00 15.83 ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.833 9.755   12.482 1.00 17.31 ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 32.010 10.368  13.556 1.00 18.70 ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.299 11.069  10.380 1.00 18.63 ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 32.986 12.066  11.124 1.00 20.94 ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.169 8.454   12.298 1.00 17.34 ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.744 7.627   13.360 1.00 18.84 ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.086 7.035   12.915 1.00 20.88 ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.307 6.818   11.709 1.00 20.35 ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.811 6.448   13.719 1.00 19.86 ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.697 5.564   12.599 1.00 20.71 ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.416 6.913   14.124 1.00 20.57 ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 34.955 6.744   13.890 1.00 21.82 ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.231 6.127   13.570 1.00 23.96 ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 36.026 4.616   13.345 1.00 24.70 ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.573 4.054   12.382 1.00 26.72 ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.264 6.442   14.671 1.00 27.62 ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.783 5.940   15.908 1.00 31.64 ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.526 7.919   14.812 1.00 28.02 ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.226 3.978   14.202 1.00 24.59 ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.950 2.546   14.073 1.00 25.08 ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.726 2.268   13.174 1.00 23.96 ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.791 3.076   13.125 1.00 23.15 ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.708 1.940   15.446 1.00 26.75 ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.712 1.107   12.505 1.00 23.19 ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.593 0.697   11.662 1.00 23.25 ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.484 0.112   12.519 1.00 22.17 ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.742 -0.656  13.449 1.00 23.59 ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 33.026 -0.334  10.619 1.00 24.92 ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.902 0.270   9.520  1.00 30.27 ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.239 -0.773  8.493  1.00 36.61 ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.070 -1.660  8.724  1.00 37.74 ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.563 -0.715  7.350  1.00 38.19 ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.251 0.464   12.182 1.00 18.66 ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.071 -0.010  12.889 1.00 18.50 ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.477 -1.272  12.309 1.00 17.17 ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.789 -1.657  11.176 1.00 18.14 ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.530 -1.875  13.079 1.00 16.68 ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 26.937 -3.164  12.695 1.00 17.49 ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.492 -3.126  12.240 1.00 17.41 ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 24.948 -4.178  11.868 1.00 18.56 ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.093 -4.171  13.830 1.00 18.44 ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.799 -4.592  14.202 1.00 22.85 ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.837 -1.971  12.349 1.00 15.51 ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.446 -1.881  11.928 1.00 14.55 ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.355 -1.809  10.404 1.00 16.62 ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.245 -1.254  9.750  1.00 17.68 ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.804 -0.629  12.557 1.00 13.83 ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.686 -0.683  14.077 1.00 15.62 ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.325 -1.779  14.609 1.00 16.17 ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.879 0.377   14.733 1.00 15.86 ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.333 -2.402  9.853  1.00 17.16 ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 22.017 -2.385  8.415  1.00 18.60 ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.706 -1.606  8.243  1.00 17.06 ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.794 -1.764  9.069  1.00 17.57 ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 21.853 -3.817  7.916  1.00 24.17 ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 23.182 -4.416  7.888  1.00 28.34 ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 21.198 -3.903  6.534  1.00 27.39 ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.611 -0.744  7.217  1.00 16.25 ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.386 0.012   6.997  1.00 15.10 ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.421 -0.771  6.104  1.00 15.74 ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.810 -1.304  5.056  1.00 16.57 ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.700 1.395   6.359  1.00 14.62 ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.797 2.156   7.134  1.00 15.82 ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.404 2.246   6.231  1.00 14.74 ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.407 2.462   8.622  1.00 16.37 ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.145 -0.779  6.482  1.00 14.21 ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 16.090 -1.401  5.685  1.00 14.20 ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.834 -0.563  4.424  1.00 15.59 ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.830 0.688   4.468  1.00 16.03 ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.805 -1.449  6.503  1.00 14.00 ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.623 -1.257  3.276  1.00 17.44 ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.293 -0.583  2.033  1.00 18.36 ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 14.031 -1.321  1.559  1.00 20.73 ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 14.104 -2.269  0.775  1.00 22.17 ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.471 -0.674  1.025  1.00 18.54 ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.804 -0.099  1.537  1.00 19.02 ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.800 1.424   1.788  1.00 17.88 ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 19.105 1.898   2.293  1.00 17.00 ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.284 3.057   2.925  1.00 18.56 ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.276 3.903   3.071  1.00 17.57 ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.481 3.382   3.413  1.00 20.33 ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 12.884 -0.839  2.015  1.00 19.91 ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.583 -1.503  1.866  1.00 21.53 ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.420 -0.534  2.136  1.00 22.29 ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.609 0.620   2.490  1.00 23.23 ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.549 -2.634  2.880  1.00 20.74 ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.499 -2.023  4.589  1.00 20.29 ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 9.143  -1.060  2.044  1.00 25.36 ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 7.982  -0.248  2.398  1.00 27.56 ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 7.176  -0.948  3.536  1.00 26.30 ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 5.935  -0.834  3.611  1.00 27.00 ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 7.078  0.045   1.180  1.00 34.00 ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.460  -1.185  0.555  1.00 42.48 ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 6.841  -2.320  0.959  1.00 43.68 ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 5.603  -1.022  -0.354 1.00 46.63 ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 7.876  -1.662  4.444  1.00 23.64 ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 7.203  -2.281  5.602  1.00 21.86 ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.432  -1.202  6.426  1.00 21.43 ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 6.859  -0.045  6.575  1.00 21.46 ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 8.221  -3.001  6.491  1.00 21.34 ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 8.916  -4.572  5.865  1.00 20.41 ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.274  -1.594  6.931  1.00 18.11 ? 59  GLN   A N   1 
ATOM   411  C  CA  . GLN   A 1 53  ? 4.469  -0.801  7.858  1.00 18.56 ? 59  GLN   A CA  1 
ATOM   412  C  C   . GLN   A 1 53  ? 4.241  -1.541  9.182  1.00 15.83 ? 59  GLN   A C   1 
ATOM   413  O  O   . GLN   A 1 53  ? 3.377  -1.175  9.963  1.00 16.85 ? 59  GLN   A O   1 
ATOM   414  C  CB  . GLN   A 1 53  ? 3.133  -0.353  7.273  1.00 22.34 ? 59  GLN   A CB  1 
ATOM   415  C  CG  . GLN   A 1 53  ? 3.222  0.792   6.313  1.00 27.54 ? 59  GLN   A CG  1 
ATOM   416  C  CD  . GLN   A 1 53  ? 1.818  1.295   5.959  1.00 32.58 ? 59  GLN   A CD  1 
ATOM   417  O  OE1 . GLN   A 1 53  ? 1.309  1.097   4.848  1.00 35.01 ? 59  GLN   A OE1 1 
ATOM   418  N  NE2 . GLN   A 1 53  ? 1.120  1.953   6.887  1.00 30.52 ? 59  GLN   A NE2 1 
ATOM   419  N  N   . THR   A 1 54  ? 4.971  -2.656  9.404  1.00 14.36 ? 60  THR   A N   1 
ATOM   420  C  CA  . THR   A 1 54  ? 4.981  -3.352  10.674 1.00 14.83 ? 60  THR   A CA  1 
ATOM   421  C  C   . THR   A 1 54  ? 6.430  -3.631  11.077 1.00 14.22 ? 60  THR   A C   1 
ATOM   422  O  O   . THR   A 1 54  ? 7.300  -3.850  10.223 1.00 15.55 ? 60  THR   A O   1 
ATOM   423  C  CB  . THR   A 1 54  ? 4.187  -4.655  10.682 1.00 18.32 ? 60  THR   A CB  1 
ATOM   424  O  OG1 . THR   A 1 54  ? 4.799  -5.586  9.813  1.00 23.42 ? 60  THR   A OG1 1 
ATOM   425  C  CG2 . THR   A 1 54  ? 2.736  -4.477  10.279 1.00 18.97 ? 60  THR   A CG2 1 
ATOM   426  N  N   . GLY   A 1 55  ? 6.694  -3.533  12.353 1.00 12.33 ? 61  GLY   A N   1 
ATOM   427  C  CA  . GLY   A 1 55  ? 8.049  -3.751  12.860 1.00 12.15 ? 61  GLY   A CA  1 
ATOM   428  C  C   . GLY   A 1 55  ? 8.056  -3.783  14.370 1.00 11.50 ? 61  GLY   A C   1 
ATOM   429  O  O   . GLY   A 1 55  ? 7.021  -4.009  15.002 1.00 12.38 ? 61  GLY   A O   1 
ATOM   430  N  N   . VAL   A 1 56  ? 9.243  -3.589  14.959 1.00 10.90 ? 62  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 56  ? 9.416  -3.655  16.400 1.00 10.60 ? 62  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 56  ? 10.272 -2.481  16.828 1.00 11.00 ? 62  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 56  ? 11.266 -2.199  16.155 1.00 12.32 ? 62  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 56  ? 10.106 -5.008  16.737 1.00 12.53 ? 62  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 56  ? 10.485 -5.079  18.203 1.00 15.15 ? 62  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 56  ? 9.204  -6.202  16.360 1.00 12.62 ? 62  VAL   A CG2 1 
ATOM   437  N  N   . TYR   A 1 57  ? 9.917  -1.797  17.934 1.00 10.64 ? 63  TYR   A N   1 
ATOM   438  C  CA  . TYR   A 1 57  ? 10.769 -0.703  18.405 1.00 10.41 ? 63  TYR   A CA  1 
ATOM   439  C  C   . TYR   A 1 57  ? 11.213 -0.916  19.850 1.00 11.04 ? 63  TYR   A C   1 
ATOM   440  O  O   . TYR   A 1 57  ? 10.494 -1.533  20.644 1.00 11.53 ? 63  TYR   A O   1 
ATOM   441  C  CB  . TYR   A 1 57  ? 10.098 0.697   18.258 1.00 10.71 ? 63  TYR   A CB  1 
ATOM   442  C  CG  . TYR   A 1 57  ? 9.123  1.096   19.353 1.00 10.95 ? 63  TYR   A CG  1 
ATOM   443  C  CD1 . TYR   A 1 57  ? 7.838  0.568   19.392 1.00 12.89 ? 63  TYR   A CD1 1 
ATOM   444  C  CD2 . TYR   A 1 57  ? 9.477  2.025   20.333 1.00 12.24 ? 63  TYR   A CD2 1 
ATOM   445  C  CE1 . TYR   A 1 57  ? 6.926  0.952   20.370 1.00 13.66 ? 63  TYR   A CE1 1 
ATOM   446  C  CE2 . TYR   A 1 57  ? 8.570  2.412   21.324 1.00 12.95 ? 63  TYR   A CE2 1 
ATOM   447  C  CZ  . TYR   A 1 57  ? 7.306  1.858   21.343 1.00 13.80 ? 63  TYR   A CZ  1 
ATOM   448  O  OH  . TYR   A 1 57  ? 6.415  2.233   22.323 1.00 15.45 ? 63  TYR   A OH  1 
ATOM   449  N  N   . TYR   A 1 58  ? 12.343 -0.321  20.212 1.00 10.50 ? 64  TYR   A N   1 
ATOM   450  C  CA  . TYR   A 1 58  ? 12.811 -0.347  21.595 1.00 10.82 ? 64  TYR   A CA  1 
ATOM   451  C  C   . TYR   A 1 58  ? 12.335 0.858   22.382 1.00 11.41 ? 64  TYR   A C   1 
ATOM   452  O  O   . TYR   A 1 58  ? 12.582 2.018   21.987 1.00 11.66 ? 64  TYR   A O   1 
ATOM   453  C  CB  . TYR   A 1 58  ? 14.360 -0.436  21.645 1.00 11.24 ? 64  TYR   A CB  1 
ATOM   454  C  CG  . TYR   A 1 58  ? 14.827 -0.569  23.079 1.00 12.57 ? 64  TYR   A CG  1 
ATOM   455  C  CD1 . TYR   A 1 58  ? 14.491 -1.675  23.834 1.00 13.19 ? 64  TYR   A CD1 1 
ATOM   456  C  CD2 . TYR   A 1 58  ? 15.596 0.431   23.685 1.00 12.39 ? 64  TYR   A CD2 1 
ATOM   457  C  CE1 . TYR   A 1 58  ? 14.869 -1.775  25.165 1.00 14.58 ? 64  TYR   A CE1 1 
ATOM   458  C  CE2 . TYR   A 1 58  ? 15.972 0.346   25.018 1.00 13.10 ? 64  TYR   A CE2 1 
ATOM   459  C  CZ  . TYR   A 1 58  ? 15.657 -0.787  25.730 1.00 14.18 ? 64  TYR   A CZ  1 
ATOM   460  O  OH  . TYR   A 1 58  ? 16.027 -0.897  27.066 1.00 16.90 ? 64  TYR   A OH  1 
ATOM   461  N  N   . CYS   A 1 59  ? 11.731 0.585   23.558 1.00 11.41 ? 65  CYS   A N   1 
ATOM   462  C  CA  . CYS   A 1 59  ? 11.213 1.603   24.476 1.00 12.11 ? 65  CYS   A CA  1 
ATOM   463  C  C   . CYS   A 1 59  ? 12.027 1.566   25.778 1.00 13.10 ? 65  CYS   A C   1 
ATOM   464  O  O   . CYS   A 1 59  ? 11.852 0.642   26.616 1.00 13.05 ? 65  CYS   A O   1 
ATOM   465  C  CB  . CYS   A 1 59  ? 9.742  1.333   24.742 1.00 13.54 ? 65  CYS   A CB  1 
ATOM   466  S  SG  . CYS   A 1 59  ? 9.010  2.412   26.005 1.00 13.57 ? 65  CYS   A SG  1 
ATOM   467  N  N   . SER   A 1 60  ? 12.951 2.538   25.949 1.00 12.11 ? 66  SER   A N   1 
ATOM   468  C  CA  . SER   A 1 60  ? 13.847 2.503   27.119 1.00 13.03 ? 66  SER   A CA  1 
ATOM   469  C  C   . SER   A 1 60  ? 13.120 2.666   28.448 1.00 13.46 ? 66  SER   A C   1 
ATOM   470  O  O   . SER   A 1 60  ? 13.519 2.049   29.443 1.00 14.93 ? 66  SER   A O   1 
ATOM   471  C  CB  . SER   A 1 60  ? 14.965 3.527   26.969 1.00 15.48 ? 66  SER   A CB  1 
ATOM   472  O  OG  . SER   A 1 60  ? 14.527 4.866   27.097 1.00 18.89 ? 66  SER   A OG  1 
ATOM   473  N  N   . SER   A 1 61  ? 11.982 3.441   28.462 1.00 12.21 ? 67  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 61  ? 11.192 3.635   29.677 1.00 12.32 ? 67  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 61  ? 10.369 2.426   30.128 1.00 12.44 ? 67  SER   A C   1 
ATOM   476  O  O   . SER   A 1 61  ? 9.767  2.449   31.196 1.00 14.36 ? 67  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 61  ? 10.291 4.859   29.551 1.00 13.67 ? 67  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 61  ? 9.296  4.704   28.555 1.00 14.83 ? 67  SER   A OG  1 
ATOM   479  N  N   . ARG   A 1 62  ? 10.456 1.330   29.343 1.00 12.64 ? 68  ARG   A N   1 
ATOM   480  C  CA  . ARG   A 1 62  ? 9.861  0.041   29.694 1.00 13.22 ? 68  ARG   A CA  1 
ATOM   481  C  C   . ARG   A 1 62  ? 10.880 -1.104  29.634 1.00 14.83 ? 68  ARG   A C   1 
ATOM   482  O  O   . ARG   A 1 62  ? 10.511 -2.257  29.911 1.00 15.81 ? 68  ARG   A O   1 
ATOM   483  C  CB  . ARG   A 1 62  ? 8.657  -0.277  28.780 1.00 14.05 ? 68  ARG   A CB  1 
ATOM   484  C  CG  . ARG   A 1 62  ? 7.514  0.718   28.934 1.00 15.12 ? 68  ARG   A CG  1 
ATOM   485  C  CD  . ARG   A 1 62  ? 6.735  0.460   30.186 1.00 15.21 ? 68  ARG   A CD  1 
ATOM   486  N  NE  . ARG   A 1 62  ? 5.604  1.382   30.351 1.00 16.37 ? 68  ARG   A NE  1 
ATOM   487  C  CZ  . ARG   A 1 62  ? 5.663  2.545   30.987 1.00 16.76 ? 68  ARG   A CZ  1 
ATOM   488  N  NH1 . ARG   A 1 62  ? 6.811  2.959   31.538 1.00 18.06 ? 68  ARG   A NH1 1 
ATOM   489  N  NH2 . ARG   A 1 62  ? 4.559  3.292   31.133 1.00 18.88 ? 68  ARG   A NH2 1 
ATOM   490  N  N   . ARG   A 1 63  ? 12.118 -0.850  29.176 1.00 14.67 ? 69  ARG   A N   1 
ATOM   491  C  CA  . ARG   A 1 63  ? 13.109 -1.915  28.892 1.00 15.96 ? 69  ARG   A CA  1 
ATOM   492  C  C   . ARG   A 1 63  ? 12.482 -3.039  28.029 1.00 17.14 ? 69  ARG   A C   1 
ATOM   493  O  O   . ARG   A 1 63  ? 12.626 -4.247  28.331 1.00 19.07 ? 69  ARG   A O   1 
ATOM   494  C  CB  . ARG   A 1 63  ? 13.704 -2.509  30.161 1.00 18.01 ? 69  ARG   A CB  1 
ATOM   495  C  CG  . ARG   A 1 63  ? 14.658 -1.558  30.799 1.00 18.30 ? 69  ARG   A CG  1 
ATOM   496  C  CD  . ARG   A 1 63  ? 15.572 -2.346  31.736 1.00 19.64 ? 69  ARG   A CD  1 
ATOM   497  N  NE  . ARG   A 1 63  ? 16.341 -1.389  32.517 1.00 21.85 ? 69  ARG   A NE  1 
ATOM   498  C  CZ  . ARG   A 1 63  ? 16.041 -1.015  33.757 1.00 19.62 ? 69  ARG   A CZ  1 
ATOM   499  N  NH1 . ARG   A 1 63  ? 14.977 -1.523  34.378 1.00 21.44 ? 69  ARG   A NH1 1 
ATOM   500  N  NH2 . ARG   A 1 63  ? 16.792 -0.120  34.384 1.00 21.64 ? 69  ARG   A NH2 1 
ATOM   501  N  N   . LYS   A 1 64  ? 11.740 -2.645  27.013 1.00 15.57 ? 70  LYS   A N   1 
ATOM   502  C  CA  . LYS   A 1 64  ? 11.005 -3.609  26.212 1.00 15.77 ? 70  LYS   A CA  1 
ATOM   503  C  C   . LYS   A 1 64  ? 10.995 -3.250  24.756 1.00 14.90 ? 70  LYS   A C   1 
ATOM   504  O  O   . LYS   A 1 64  ? 10.938 -2.071  24.399 1.00 14.69 ? 70  LYS   A O   1 
ATOM   505  C  CB  . LYS   A 1 64  ? 9.545  -3.666  26.704 1.00 19.39 ? 70  LYS   A CB  1 
ATOM   506  C  CG  . LYS   A 1 64  ? 9.336  -4.592  27.900 1.00 29.29 ? 70  LYS   A CG  1 
ATOM   507  C  CD  . LYS   A 1 64  ? 7.861  -4.934  28.079 1.00 38.48 ? 70  LYS   A CD  1 
ATOM   508  C  CE  . LYS   A 1 64  ? 7.631  -5.729  29.351 1.00 44.79 ? 70  LYS   A CE  1 
ATOM   509  N  NZ  . LYS   A 1 64  ? 8.396  -5.164  30.502 1.00 48.87 ? 70  LYS   A NZ  1 
ATOM   510  N  N   . HIS   A 1 65  ? 10.973 -4.268  23.912 1.00 13.59 ? 71  HIS   A N   1 
ATOM   511  C  CA  . HIS   A 1 65  ? 10.782 -4.130  22.462 1.00 12.98 ? 71  HIS   A CA  1 
ATOM   512  C  C   . HIS   A 1 65  ? 9.303  -4.458  22.192 1.00 14.62 ? 71  HIS   A C   1 
ATOM   513  O  O   . HIS   A 1 65  ? 8.811  -5.519  22.605 1.00 17.29 ? 71  HIS   A O   1 
ATOM   514  C  CB  . HIS   A 1 65  ? 11.685 -5.122  21.703 1.00 12.26 ? 71  HIS   A CB  1 
ATOM   515  C  CG  . HIS   A 1 65  ? 13.139 -4.789  21.827 1.00 13.67 ? 71  HIS   A CG  1 
ATOM   516  N  ND1 . HIS   A 1 65  ? 13.849 -4.135  20.825 1.00 17.16 ? 71  HIS   A ND1 1 
ATOM   517  C  CD2 . HIS   A 1 65  ? 13.989 -5.077  22.841 1.00 12.69 ? 71  HIS   A CD2 1 
ATOM   518  C  CE1 . HIS   A 1 65  ? 15.108 -4.068  21.260 1.00 15.82 ? 71  HIS   A CE1 1 
ATOM   519  N  NE2 . HIS   A 1 65  ? 15.227 -4.610  22.458 1.00 17.06 ? 71  HIS   A NE2 1 
ATOM   520  N  N   . TYR   A 1 66  ? 8.600  -3.568  21.459 1.00 12.40 ? 72  TYR   A N   1 
ATOM   521  C  CA  . TYR   A 1 66  ? 7.174  -3.767  21.191 1.00 13.08 ? 72  TYR   A CA  1 
ATOM   522  C  C   . TYR   A 1 66  ? 6.912  -3.871  19.706 1.00 12.28 ? 72  TYR   A C   1 
ATOM   523  O  O   . TYR   A 1 66  ? 7.433  -3.060  18.920 1.00 12.18 ? 72  TYR   A O   1 
ATOM   524  C  CB  . TYR   A 1 66  ? 6.380  -2.500  21.664 1.00 13.26 ? 72  TYR   A CB  1 
ATOM   525  C  CG  . TYR   A 1 66  ? 6.284  -2.311  23.164 1.00 13.63 ? 72  TYR   A CG  1 
ATOM   526  C  CD1 . TYR   A 1 66  ? 5.431  -3.095  23.931 1.00 14.98 ? 72  TYR   A CD1 1 
ATOM   527  C  CD2 . TYR   A 1 66  ? 7.039  -1.349  23.811 1.00 13.39 ? 72  TYR   A CD2 1 
ATOM   528  C  CE1 . TYR   A 1 66  ? 5.306  -2.902  25.300 1.00 15.74 ? 72  TYR   A CE1 1 
ATOM   529  C  CE2 . TYR   A 1 66  ? 6.939  -1.154  25.189 1.00 14.43 ? 72  TYR   A CE2 1 
ATOM   530  C  CZ  . TYR   A 1 66  ? 6.056  -1.926  25.926 1.00 16.17 ? 72  TYR   A CZ  1 
ATOM   531  O  OH  . TYR   A 1 66  ? 5.956  -1.757  27.295 1.00 19.12 ? 72  TYR   A OH  1 
ATOM   532  N  N   . PRO   A 1 67  ? 6.108  -4.869  19.294 1.00 12.44 ? 73  PRO   A N   1 
ATOM   533  C  CA  . PRO   A 1 67  ? 5.689  -4.923  17.877 1.00 12.07 ? 73  PRO   A CA  1 
ATOM   534  C  C   . PRO   A 1 67  ? 4.654  -3.829  17.600 1.00 13.03 ? 73  PRO   A C   1 
ATOM   535  O  O   . PRO   A 1 67  ? 3.699  -3.666  18.400 1.00 15.41 ? 73  PRO   A O   1 
ATOM   536  C  CB  . PRO   A 1 67  ? 5.034  -6.315  17.730 1.00 14.08 ? 73  PRO   A CB  1 
ATOM   537  C  CG  . PRO   A 1 67  ? 4.674  -6.720  19.128 1.00 15.55 ? 73  PRO   A CG  1 
ATOM   538  C  CD  . PRO   A 1 67  ? 5.515  -5.939  20.122 1.00 13.33 ? 73  PRO   A CD  1 
ATOM   539  N  N   . VAL   A 1 68  ? 4.792  -3.161  16.468 1.00 12.31 ? 74  VAL   A N   1 
ATOM   540  C  CA  . VAL   A 1 68  ? 3.849  -2.084  16.124 1.00 13.70 ? 74  VAL   A CA  1 
ATOM   541  C  C   . VAL   A 1 68  ? 3.532  -2.073  14.661 1.00 12.93 ? 74  VAL   A C   1 
ATOM   542  O  O   . VAL   A 1 68  ? 4.356  -2.420  13.819 1.00 13.19 ? 74  VAL   A O   1 
ATOM   543  C  CB  . VAL   A 1 68  ? 4.409  -0.695  16.509 1.00 15.51 ? 74  VAL   A CB  1 
ATOM   544  C  CG1 . VAL   A 1 68  ? 4.366  -0.482  18.029 1.00 16.12 ? 74  VAL   A CG1 1 
ATOM   545  C  CG2 . VAL   A 1 68  ? 5.807  -0.457  15.944 1.00 16.82 ? 74  VAL   A CG2 1 
ATOM   546  N  N   . SER   A 1 69  ? 2.343  -1.526  14.317 1.00 13.74 ? 75  SER   A N   1 
ATOM   547  C  CA  . SER   A 1 69  ? 1.947  -1.129  12.971 1.00 14.95 ? 75  SER   A CA  1 
ATOM   548  C  C   . SER   A 1 69  ? 2.168  0.397   12.931 1.00 14.58 ? 75  SER   A C   1 
ATOM   549  O  O   . SER   A 1 69  ? 1.807  1.092   13.902 1.00 14.98 ? 75  SER   A O   1 
ATOM   550  C  CB  . SER   A 1 69  ? 0.459  -1.370  12.762 1.00 19.43 ? 75  SER   A CB  1 
ATOM   551  O  OG  . SER   A 1 69  ? 0.219  -2.763  12.798 1.00 27.37 ? 75  SER   A OG  1 
ATOM   552  N  N   . PHE   A 1 70  ? 2.771  0.916   11.854 1.00 14.10 ? 76  PHE   A N   1 
ATOM   553  C  CA  . PHE   A 1 70  ? 3.095  2.341   11.782 1.00 14.83 ? 76  PHE   A CA  1 
ATOM   554  C  C   . PHE   A 1 70  ? 2.708  2.912   10.442 1.00 15.59 ? 76  PHE   A C   1 
ATOM   555  O  O   . PHE   A 1 70  ? 2.630  2.202   9.435  1.00 17.57 ? 76  PHE   A O   1 
ATOM   556  C  CB  . PHE   A 1 70  ? 4.584  2.614   12.131 1.00 14.86 ? 76  PHE   A CB  1 
ATOM   557  C  CG  . PHE   A 1 70  ? 5.610  1.805   11.356 1.00 14.45 ? 76  PHE   A CG  1 
ATOM   558  C  CD1 . PHE   A 1 70  ? 6.009  0.545   11.789 1.00 13.86 ? 76  PHE   A CD1 1 
ATOM   559  C  CD2 . PHE   A 1 70  ? 6.170  2.298   10.189 1.00 14.54 ? 76  PHE   A CD2 1 
ATOM   560  C  CE1 . PHE   A 1 70  ? 6.965  -0.185  11.073 1.00 14.58 ? 76  PHE   A CE1 1 
ATOM   561  C  CE2 . PHE   A 1 70  ? 7.137  1.564   9.486  1.00 15.60 ? 76  PHE   A CE2 1 
ATOM   562  C  CZ  . PHE   A 1 70  ? 7.476  0.303   9.898  1.00 15.01 ? 76  PHE   A CZ  1 
ATOM   563  N  N   . SER   A 1 71  ? 2.388  4.213   10.432 1.00 15.68 ? 77  SER   A N   1 
ATOM   564  C  CA  . SER   A 1 71  ? 1.971  4.894   9.215  1.00 16.65 ? 77  SER   A CA  1 
ATOM   565  C  C   . SER   A 1 71  ? 3.151  5.154   8.271  1.00 15.89 ? 77  SER   A C   1 
ATOM   566  O  O   . SER   A 1 71  ? 4.317  5.019   8.652  1.00 15.86 ? 77  SER   A O   1 
ATOM   567  C  CB  . SER   A 1 71  ? 1.250  6.206   9.572  1.00 18.87 ? 77  SER   A CB  1 
ATOM   568  O  OG  . SER   A 1 71  ? 2.103  7.133   10.237 1.00 20.79 ? 77  SER   A OG  1 
ATOM   569  N  N   . LYS   A 1 72  ? 2.850  5.497   7.024  1.00 16.72 ? 78  LYS   A N   1 
ATOM   570  C  CA  . LYS   A 1 72  ? 3.880  5.812   6.050  1.00 16.81 ? 78  LYS   A CA  1 
ATOM   571  C  C   . LYS   A 1 72  ? 4.533  7.154   6.387  1.00 18.32 ? 78  LYS   A C   1 
ATOM   572  O  O   . LYS   A 1 72  ? 3.858  8.028   6.938  1.00 19.26 ? 78  LYS   A O   1 
ATOM   573  C  CB  . LYS   A 1 72  ? 3.304  5.810   4.627  1.00 19.87 ? 78  LYS   A CB  1 
ATOM   574  C  CG  . LYS   A 1 72  ? 2.858  4.421   4.210  1.00 24.01 ? 78  LYS   A CG  1 
ATOM   575  C  CD  . LYS   A 1 72  ? 2.600  4.330   2.700  1.00 30.12 ? 78  LYS   A CD  1 
ATOM   576  C  CE  . LYS   A 1 72  ? 2.317  2.894   2.289  1.00 35.64 ? 78  LYS   A CE  1 
ATOM   577  N  NZ  . LYS   A 1 72  ? 2.531  2.671   0.828  1.00 39.45 ? 78  LYS   A NZ  1 
ATOM   578  N  N   . PRO   A 1 73  ? 5.801  7.384   6.028  1.00 17.88 ? 79  PRO   A N   1 
ATOM   579  C  CA  . PRO   A 1 73  ? 6.441  8.672   6.349  1.00 18.17 ? 79  PRO   A CA  1 
ATOM   580  C  C   . PRO   A 1 73  ? 5.661  9.849   5.781  1.00 19.21 ? 79  PRO   A C   1 
ATOM   581  O  O   . PRO   A 1 73  ? 5.312  9.845   4.594  1.00 21.33 ? 79  PRO   A O   1 
ATOM   582  C  CB  . PRO   A 1 73  ? 7.836  8.554   5.700  1.00 20.65 ? 79  PRO   A CB  1 
ATOM   583  C  CG  . PRO   A 1 73  ? 8.060  7.091   5.471  1.00 22.66 ? 79  PRO   A CG  1 
ATOM   584  C  CD  . PRO   A 1 73  ? 6.730  6.449   5.339  1.00 19.00 ? 79  PRO   A CD  1 
ATOM   585  N  N   . SER   A 1 74  ? 5.354  10.817  6.636  1.00 18.46 ? 80  SER   A N   1 
ATOM   586  C  CA  . SER   A 1 74  ? 4.521  11.937  6.222  1.00 20.09 ? 80  SER   A CA  1 
ATOM   587  C  C   . SER   A 1 74  ? 4.856  13.202  7.012  1.00 19.21 ? 80  SER   A C   1 
ATOM   588  O  O   . SER   A 1 74  ? 5.682  13.180  7.926  1.00 18.92 ? 80  SER   A O   1 
ATOM   589  C  CB  . SER   A 1 74  ? 3.041  11.573  6.354  1.00 25.39 ? 80  SER   A CB  1 
ATOM   590  O  OG  . SER   A 1 74  ? 2.695  11.400  7.701  1.00 32.08 ? 80  SER   A OG  1 
ATOM   591  N  N   . LEU   A 1 75  ? 4.168  14.317  6.655  1.00 21.00 ? 81  LEU   A N   1 
ATOM   592  C  CA  . LEU   A 1 75  ? 4.341  15.614  7.296  1.00 23.05 ? 81  LEU   A CA  1 
ATOM   593  C  C   . LEU   A 1 75  ? 3.245  15.691  8.369  1.00 24.41 ? 81  LEU   A C   1 
ATOM   594  O  O   . LEU   A 1 75  ? 2.039  15.748  8.053  1.00 26.45 ? 81  LEU   A O   1 
ATOM   595  C  CB  . LEU   A 1 75  ? 4.146  16.721  6.225  1.00 24.78 ? 81  LEU   A CB  1 
ATOM   596  C  CG  . LEU   A 1 75  ? 4.494  18.148  6.620  1.00 28.45 ? 81  LEU   A CG  1 
ATOM   597  C  CD1 . LEU   A 1 75  ? 5.966  18.276  6.926  1.00 29.61 ? 81  LEU   A CD1 1 
ATOM   598  C  CD2 . LEU   A 1 75  ? 4.186  19.120  5.470  1.00 29.23 ? 81  LEU   A CD2 1 
ATOM   599  N  N   . ILE   A 1 76  ? 3.657  15.604  9.630  1.00 23.47 ? 82  ILE   A N   1 
ATOM   600  C  CA  . ILE   A 1 76  ? 2.769  15.547  10.797 1.00 24.91 ? 82  ILE   A CA  1 
ATOM   601  C  C   . ILE   A 1 76  ? 2.995  16.731  11.725 1.00 25.47 ? 82  ILE   A C   1 
ATOM   602  O  O   . ILE   A 1 76  ? 4.143  17.085  12.012 1.00 24.43 ? 82  ILE   A O   1 
ATOM   603  C  CB  . ILE   A 1 76  ? 3.074  14.240  11.579 1.00 26.63 ? 82  ILE   A CB  1 
ATOM   604  C  CG1 . ILE   A 1 76  ? 2.859  12.949  10.726 1.00 29.38 ? 82  ILE   A CG1 1 
ATOM   605  C  CG2 . ILE   A 1 76  ? 2.305  14.165  12.931 1.00 28.19 ? 82  ILE   A CG2 1 
ATOM   606  C  CD1 . ILE   A 1 76  ? 1.391  12.595  10.445 1.00 32.69 ? 82  ILE   A CD1 1 
ATOM   607  N  N   . PHE   A 1 77  ? 1.914  17.305  12.259 1.00 26.49 ? 83  PHE   A N   1 
ATOM   608  C  CA  . PHE   A 1 77  ? 2.009  18.395  13.222 1.00 27.29 ? 83  PHE   A CA  1 
ATOM   609  C  C   . PHE   A 1 77  ? 2.420  17.813  14.584 1.00 28.12 ? 83  PHE   A C   1 
ATOM   610  O  O   . PHE   A 1 77  ? 1.837  16.834  15.069 1.00 30.15 ? 83  PHE   A O   1 
ATOM   611  C  CB  . PHE   A 1 77  ? 0.653  19.127  13.376 1.00 28.70 ? 83  PHE   A CB  1 
ATOM   612  C  CG  . PHE   A 1 77  ? 0.849  20.449  14.059 1.00 31.63 ? 83  PHE   A CG  1 
ATOM   613  C  CD1 . PHE   A 1 77  ? 1.477  21.493  13.406 1.00 34.13 ? 83  PHE   A CD1 1 
ATOM   614  C  CD2 . PHE   A 1 77  ? 0.454  20.634  15.375 1.00 34.14 ? 83  PHE   A CD2 1 
ATOM   615  C  CE1 . PHE   A 1 77  ? 1.674  22.706  14.037 1.00 36.36 ? 83  PHE   A CE1 1 
ATOM   616  C  CE2 . PHE   A 1 77  ? 0.644  21.857  16.001 1.00 35.14 ? 83  PHE   A CE2 1 
ATOM   617  C  CZ  . PHE   A 1 77  ? 1.239  22.885  15.325 1.00 36.29 ? 83  PHE   A CZ  1 
ATOM   618  N  N   . VAL   A 1 78  ? 3.506  18.348  15.151 1.00 25.40 ? 84  VAL   A N   1 
ATOM   619  C  CA  . VAL   A 1 78  ? 4.002  17.908  16.444 1.00 24.60 ? 84  VAL   A CA  1 
ATOM   620  C  C   . VAL   A 1 78  ? 3.897  19.076  17.449 1.00 25.61 ? 84  VAL   A C   1 
ATOM   621  O  O   . VAL   A 1 78  ? 4.341  20.167  17.126 1.00 25.81 ? 84  VAL   A O   1 
ATOM   622  C  CB  . VAL   A 1 78  ? 5.470  17.416  16.318 1.00 23.00 ? 84  VAL   A CB  1 
ATOM   623  C  CG1 . VAL   A 1 78  ? 6.026  17.059  17.694 1.00 23.20 ? 84  VAL   A CG1 1 
ATOM   624  C  CG2 . VAL   A 1 78  ? 5.556  16.217  15.380 1.00 22.64 ? 84  VAL   A CG2 1 
ATOM   625  N  N   . GLU   A 1 79  ? 3.365  18.829  18.646 1.00 26.62 ? 85  GLU   A N   1 
ATOM   626  C  CA  . GLU   A 1 79  ? 3.203  19.875  19.667 1.00 29.60 ? 85  GLU   A CA  1 
ATOM   627  C  C   . GLU   A 1 79  ? 4.544  20.357  20.205 1.00 30.90 ? 85  GLU   A C   1 
ATOM   628  O  O   . GLU   A 1 79  ? 5.517  19.601  20.191 1.00 29.77 ? 85  GLU   A O   1 
ATOM   629  C  CB  . GLU   A 1 79  ? 2.346  19.361  20.831 1.00 33.21 ? 85  GLU   A CB  1 
ATOM   630  C  CG  . GLU   A 1 79  ? 1.736  20.459  21.693 1.00 42.64 ? 85  GLU   A CG  1 
ATOM   631  C  CD  . GLU   A 1 79  ? 1.029  21.593  20.969 1.00 49.57 ? 85  GLU   A CD  1 
ATOM   632  O  OE1 . GLU   A 1 79  ? 1.561  22.729  20.988 1.00 48.19 ? 85  GLU   A OE1 1 
ATOM   633  O  OE2 . GLU   A 1 79  ? -0.042 21.342  20.371 1.00 52.93 ? 85  GLU   A OE2 1 
ATOM   634  N  N   . ALA   A 1 80  ? 4.570  21.597  20.738 1.00 32.74 ? 86  ALA   A N   1 
ATOM   635  C  CA  . ALA   A 1 80  ? 5.749  22.225  21.330 1.00 35.19 ? 86  ALA   A CA  1 
ATOM   636  C  C   . ALA   A 1 80  ? 6.339  21.368  22.415 1.00 37.31 ? 86  ALA   A C   1 
ATOM   637  O  O   . ALA   A 1 80  ? 5.618  20.747  23.203 1.00 38.59 ? 86  ALA   A O   1 
ATOM   638  C  CB  . ALA   A 1 80  ? 5.398  23.584  21.912 1.00 35.92 ? 86  ALA   A CB  1 
ATOM   639  N  N   . SER   A 1 81  ? 7.658  21.274  22.419 1.00 36.70 ? 87  SER   A N   1 
ATOM   640  C  CA  . SER   A 1 81  ? 8.390  20.536  23.438 1.00 36.19 ? 87  SER   A CA  1 
ATOM   641  C  C   . SER   A 1 81  ? 9.511  21.468  23.974 1.00 35.41 ? 87  SER   A C   1 
ATOM   642  O  O   . SER   A 1 81  ? 9.587  22.624  23.567 1.00 36.04 ? 87  SER   A O   1 
ATOM   643  C  CB  . SER   A 1 81  ? 9.000  19.285  22.823 1.00 37.66 ? 87  SER   A CB  1 
ATOM   644  O  OG  . SER   A 1 81  ? 10.045 19.630  21.924 1.00 38.12 ? 87  SER   A OG  1 
ATOM   645  N  N   . GLU   A 1 82  ? 10.421 20.952  24.822 1.00 34.78 ? 88  GLU   A N   1 
ATOM   646  C  CA  . GLU   A 1 82  ? 11.568 21.767  25.253 1.00 33.86 ? 88  GLU   A CA  1 
ATOM   647  C  C   . GLU   A 1 82  ? 12.593 21.938  24.097 1.00 29.53 ? 88  GLU   A C   1 
ATOM   648  O  O   . GLU   A 1 82  ? 13.415 22.844  24.156 1.00 28.87 ? 88  GLU   A O   1 
ATOM   649  C  CB  . GLU   A 1 82  ? 12.239 21.158  26.493 1.00 38.29 ? 88  GLU   A CB  1 
ATOM   650  C  CG  . GLU   A 1 82  ? 11.702 21.784  27.765 1.00 46.75 ? 88  GLU   A CG  1 
ATOM   651  C  CD  . GLU   A 1 82  ? 11.393 20.805  28.877 1.00 57.64 ? 88  GLU   A CD  1 
ATOM   652  O  OE1 . GLU   A 1 82  ? 10.603 21.167  29.782 1.00 60.05 ? 88  GLU   A OE1 1 
ATOM   653  O  OE2 . GLU   A 1 82  ? 11.940 19.677  28.843 1.00 60.30 ? 88  GLU   A OE2 1 
ATOM   654  N  N   . TYR   A 1 83  ? 12.490 21.130  23.018 1.00 27.11 ? 89  TYR   A N   1 
ATOM   655  C  CA  . TYR   A 1 83  ? 13.463 21.157  21.913 1.00 24.77 ? 89  TYR   A CA  1 
ATOM   656  C  C   . TYR   A 1 83  ? 12.999 21.827  20.641 1.00 23.17 ? 89  TYR   A C   1 
ATOM   657  O  O   . TYR   A 1 83  ? 13.835 22.270  19.840 1.00 22.41 ? 89  TYR   A O   1 
ATOM   658  C  CB  . TYR   A 1 83  ? 13.856 19.725  21.593 1.00 24.68 ? 89  TYR   A CB  1 
ATOM   659  C  CG  . TYR   A 1 83  ? 14.498 19.046  22.776 1.00 25.45 ? 89  TYR   A CG  1 
ATOM   660  C  CD1 . TYR   A 1 83  ? 13.764 18.213  23.610 1.00 28.77 ? 89  TYR   A CD1 1 
ATOM   661  C  CD2 . TYR   A 1 83  ? 15.816 19.307  23.118 1.00 26.70 ? 89  TYR   A CD2 1 
ATOM   662  C  CE1 . TYR   A 1 83  ? 14.358 17.572  24.692 1.00 30.23 ? 89  TYR   A CE1 1 
ATOM   663  C  CE2 . TYR   A 1 83  ? 16.424 18.667  24.190 1.00 28.58 ? 89  TYR   A CE2 1 
ATOM   664  C  CZ  . TYR   A 1 83  ? 15.677 17.838  25.007 1.00 31.00 ? 89  TYR   A CZ  1 
ATOM   665  O  OH  . TYR   A 1 83  ? 16.289 17.171  26.050 1.00 33.54 ? 89  TYR   A OH  1 
ATOM   666  N  N   . TYR   A 1 84  ? 11.674 21.850  20.398 1.00 23.77 ? 90  TYR   A N   1 
ATOM   667  C  CA  . TYR   A 1 84  ? 11.152 22.479  19.175 1.00 23.54 ? 90  TYR   A CA  1 
ATOM   668  C  C   . TYR   A 1 84  ? 9.845  23.187  19.497 1.00 26.60 ? 90  TYR   A C   1 
ATOM   669  O  O   . TYR   A 1 84  ? 9.086  22.674  20.325 1.00 27.89 ? 90  TYR   A O   1 
ATOM   670  C  CB  . TYR   A 1 84  ? 10.818 21.426  18.069 1.00 22.26 ? 90  TYR   A CB  1 
ATOM   671  C  CG  . TYR   A 1 84  ? 11.995 20.641  17.521 1.00 19.70 ? 90  TYR   A CG  1 
ATOM   672  C  CD1 . TYR   A 1 84  ? 12.930 21.238  16.689 1.00 19.27 ? 90  TYR   A CD1 1 
ATOM   673  C  CD2 . TYR   A 1 84  ? 12.155 19.292  17.818 1.00 19.11 ? 90  TYR   A CD2 1 
ATOM   674  C  CE1 . TYR   A 1 84  ? 14.008 20.512  16.191 1.00 17.90 ? 90  TYR   A CE1 1 
ATOM   675  C  CE2 . TYR   A 1 84  ? 13.238 18.573  17.361 1.00 18.69 ? 90  TYR   A CE2 1 
ATOM   676  C  CZ  . TYR   A 1 84  ? 14.175 19.190  16.572 1.00 17.27 ? 90  TYR   A CZ  1 
ATOM   677  O  OH  . TYR   A 1 84  ? 15.240 18.465  16.115 1.00 17.15 ? 90  TYR   A OH  1 
ATOM   678  N  N   . PRO   A 1 85  ? 9.506  24.253  18.764 1.00 28.26 ? 91  PRO   A N   1 
ATOM   679  C  CA  . PRO   A 1 85  ? 8.149  24.822  18.901 1.00 29.39 ? 91  PRO   A CA  1 
ATOM   680  C  C   . PRO   A 1 85  ? 7.137  23.866  18.232 1.00 30.96 ? 91  PRO   A C   1 
ATOM   681  O  O   . PRO   A 1 85  ? 7.536  22.879  17.572 1.00 30.78 ? 91  PRO   A O   1 
ATOM   682  C  CB  . PRO   A 1 85  ? 8.250  26.138  18.110 1.00 30.75 ? 91  PRO   A CB  1 
ATOM   683  C  CG  . PRO   A 1 85  ? 9.253  25.854  17.055 1.00 31.32 ? 91  PRO   A CG  1 
ATOM   684  C  CD  . PRO   A 1 85  ? 10.277 24.925  17.689 1.00 28.45 ? 91  PRO   A CD  1 
ATOM   685  N  N   . ALA   A 1 86  ? 5.830  24.159  18.327 1.00 31.96 ? 92  ALA   A N   1 
ATOM   686  C  CA  . ALA   A 1 86  ? 4.821  23.348  17.624 1.00 31.83 ? 92  ALA   A CA  1 
ATOM   687  C  C   . ALA   A 1 86  ? 5.062  23.586  16.108 1.00 31.05 ? 92  ALA   A C   1 
ATOM   688  O  O   . ALA   A 1 86  ? 5.305  24.713  15.712 1.00 32.84 ? 92  ALA   A O   1 
ATOM   689  C  CB  . ALA   A 1 86  ? 3.421  23.799  18.029 1.00 32.12 ? 92  ALA   A CB  1 
ATOM   690  N  N   . ARG   A 1 87  ? 5.196  22.515  15.304 1.00 28.95 ? 93  ARG   A N   1 
ATOM   691  C  CA  . ARG   A 1 87  ? 5.566  22.666  13.895 1.00 27.74 ? 93  ARG   A CA  1 
ATOM   692  C  C   . ARG   A 1 87  ? 5.215  21.390  13.104 1.00 27.23 ? 93  ARG   A C   1 
ATOM   693  O  O   . ARG   A 1 87  ? 4.792  20.397  13.700 1.00 27.90 ? 93  ARG   A O   1 
ATOM   694  C  CB  . ARG   A 1 87  ? 7.093  22.900  13.819 1.00 28.02 ? 93  ARG   A CB  1 
ATOM   695  C  CG  . ARG   A 1 87  ? 7.905  21.558  13.970 1.00 28.37 ? 93  ARG   A CG  1 
ATOM   696  C  CD  . ARG   A 1 87  ? 9.293  21.734  14.499 1.00 27.68 ? 93  ARG   A CD  1 
ATOM   697  N  NE  . ARG   A 1 87  ? 10.232 20.665  14.110 1.00 27.11 ? 93  ARG   A NE  1 
ATOM   698  C  CZ  . ARG   A 1 87  ? 10.283 19.440  14.610 1.00 28.54 ? 93  ARG   A CZ  1 
ATOM   699  N  NH1 . ARG   A 1 87  ? 9.378  19.038  15.513 1.00 28.46 ? 93  ARG   A NH1 1 
ATOM   700  N  NH2 . ARG   A 1 87  ? 11.229 18.596  14.209 1.00 22.00 ? 93  ARG   A NH2 1 
ATOM   701  N  N   . TYR   A 1 88  ? 5.475  21.399  11.781 1.00 26.65 ? 94  TYR   A N   1 
ATOM   702  C  CA  . TYR   A 1 88  ? 5.304  20.214  10.980 1.00 27.38 ? 94  TYR   A CA  1 
ATOM   703  C  C   . TYR   A 1 88  ? 6.634  19.501  10.871 1.00 24.50 ? 94  TYR   A C   1 
ATOM   704  O  O   . TYR   A 1 88  ? 7.630  20.077  10.402 1.00 25.03 ? 94  TYR   A O   1 
ATOM   705  C  CB  . TYR   A 1 88  ? 4.773  20.545  9.596  1.00 28.67 ? 94  TYR   A CB  1 
ATOM   706  C  CG  . TYR   A 1 88  ? 3.303  20.859  9.656  1.00 30.12 ? 94  TYR   A CG  1 
ATOM   707  C  CD1 . TYR   A 1 88  ? 2.357  19.844  9.687  1.00 30.86 ? 94  TYR   A CD1 1 
ATOM   708  C  CD2 . TYR   A 1 88  ? 2.856  22.168  9.783  1.00 32.18 ? 94  TYR   A CD2 1 
ATOM   709  C  CE1 . TYR   A 1 88  ? 1.006  20.122  9.784  1.00 33.07 ? 94  TYR   A CE1 1 
ATOM   710  C  CE2 . TYR   A 1 88  ? 1.504  22.457  9.885  1.00 33.68 ? 94  TYR   A CE2 1 
ATOM   711  C  CZ  . TYR   A 1 88  ? 0.584  21.429  9.898  1.00 34.90 ? 94  TYR   A CZ  1 
ATOM   712  O  OH  . TYR   A 1 88  ? -0.752 21.701  9.999  1.00 38.28 ? 94  TYR   A OH  1 
ATOM   713  N  N   . GLN   A 1 89  ? 6.672  18.240  11.327 1.00 21.45 ? 95  GLN   A N   1 
ATOM   714  C  CA  . GLN   A 1 89  ? 7.891  17.431  11.190 1.00 19.60 ? 95  GLN   A CA  1 
ATOM   715  C  C   . GLN   A 1 89  ? 7.713  16.531  9.966  1.00 19.31 ? 95  GLN   A C   1 
ATOM   716  O  O   . GLN   A 1 89  ? 6.648  15.918  9.799  1.00 19.54 ? 95  GLN   A O   1 
ATOM   717  C  CB  . GLN   A 1 89  ? 8.159  16.594  12.446 1.00 18.97 ? 95  GLN   A CB  1 
ATOM   718  C  CG  . GLN   A 1 89  ? 9.417  15.762  12.307 1.00 18.01 ? 95  GLN   A CG  1 
ATOM   719  C  CD  . GLN   A 1 89  ? 9.964  15.276  13.641 1.00 17.81 ? 95  GLN   A CD  1 
ATOM   720  O  OE1 . GLN   A 1 89  ? 9.975  15.986  14.649 1.00 19.46 ? 95  GLN   A OE1 1 
ATOM   721  N  NE2 . GLN   A 1 89  ? 10.429 14.038  13.652 1.00 17.52 ? 95  GLN   A NE2 1 
ATOM   722  N  N   . SER   A 1 90  ? 8.718  16.478  9.083  1.00 17.46 ? 96  SER   A N   1 
ATOM   723  C  CA  . SER   A 1 90  ? 8.612  15.680  7.890  1.00 17.27 ? 96  SER   A CA  1 
ATOM   724  C  C   . SER   A 1 90  ? 9.216  14.275  8.088  1.00 16.40 ? 96  SER   A C   1 
ATOM   725  O  O   . SER   A 1 90  ? 9.983  14.045  9.039  1.00 17.59 ? 96  SER   A O   1 
ATOM   726  C  CB  . SER   A 1 90  ? 9.300  16.396  6.737  1.00 20.41 ? 96  SER   A CB  1 
ATOM   727  O  OG  . SER   A 1 90  ? 10.688 16.526  7.012  1.00 23.72 ? 96  SER   A OG  1 
ATOM   728  N  N   . HIS   A 1 91  ? 8.806  13.344  7.192  1.00 16.70 ? 97  HIS   A N   1 
ATOM   729  C  CA  . HIS   A 1 91  ? 9.319  11.967  7.164  1.00 16.11 ? 97  HIS   A CA  1 
ATOM   730  C  C   . HIS   A 1 91  ? 9.081  11.271  8.527  1.00 15.15 ? 97  HIS   A C   1 
ATOM   731  O  O   . HIS   A 1 91  ? 9.886  10.407  8.917  1.00 15.73 ? 97  HIS   A O   1 
ATOM   732  C  CB  . HIS   A 1 91  ? 10.828 11.933  6.760  1.00 17.32 ? 97  HIS   A CB  1 
ATOM   733  C  CG  . HIS   A 1 91  ? 11.110 12.508  5.393  1.00 19.80 ? 97  HIS   A CG  1 
ATOM   734  N  ND1 . HIS   A 1 91  ? 11.211 11.700  4.277  1.00 23.15 ? 97  HIS   A ND1 1 
ATOM   735  C  CD2 . HIS   A 1 91  ? 11.253 13.794  5.014  1.00 21.35 ? 97  HIS   A CD2 1 
ATOM   736  C  CE1 . HIS   A 1 91  ? 11.458 12.515  3.257  1.00 23.54 ? 97  HIS   A CE1 1 
ATOM   737  N  NE2 . HIS   A 1 91  ? 11.488 13.786  3.646  1.00 23.04 ? 97  HIS   A NE2 1 
ATOM   738  N  N   . LEU   A 1 92  ? 7.943  11.560  9.156  1.00 14.56 ? 98  LEU   A N   1 
ATOM   739  C  CA  . LEU   A 1 92  ? 7.589  11.017  10.471 1.00 15.74 ? 98  LEU   A CA  1 
ATOM   740  C  C   . LEU   A 1 92  ? 6.506  9.932   10.298 1.00 14.99 ? 98  LEU   A C   1 
ATOM   741  O  O   . LEU   A 1 92  ? 5.589  10.086  9.485  1.00 15.79 ? 98  LEU   A O   1 
ATOM   742  C  CB  . LEU   A 1 92  ? 7.042  12.151  11.367 1.00 17.35 ? 98  LEU   A CB  1 
ATOM   743  C  CG  . LEU   A 1 92  ? 6.789  11.739  12.857 1.00 19.08 ? 98  LEU   A CG  1 
ATOM   744  C  CD1 . LEU   A 1 92  ? 8.073  11.454  13.552 1.00 18.64 ? 98  LEU   A CD1 1 
ATOM   745  C  CD2 . LEU   A 1 92  ? 6.056  12.846  13.637 1.00 20.57 ? 98  LEU   A CD2 1 
ATOM   746  N  N   . MET   A 1 93  ? 6.652  8.821   11.036 1.00 14.98 ? 99  MET   A N   1 
ATOM   747  C  CA  . MET   A 1 93  ? 5.685  7.714   11.016 1.00 14.71 ? 99  MET   A CA  1 
ATOM   748  C  C   . MET   A 1 93  ? 5.111  7.562   12.424 1.00 15.27 ? 99  MET   A C   1 
ATOM   749  O  O   . MET   A 1 93  ? 5.876  7.597   13.394 1.00 15.42 ? 99  MET   A O   1 
ATOM   750  C  CB  . MET   A 1 93  ? 6.434  6.445   10.665 1.00 15.02 ? 99  MET   A CB  1 
ATOM   751  C  CG  . MET   A 1 93  ? 7.057  6.534   9.249  1.00 15.85 ? 99  MET   A CG  1 
ATOM   752  S  SD  . MET   A 1 93  ? 8.157  5.160   8.761  1.00 19.46 ? 99  MET   A SD  1 
ATOM   753  C  CE  . MET   A 1 93  ? 9.386  5.305   10.041 1.00 23.05 ? 99  MET   A CE  1 
ATOM   754  N  N   . LEU   A 1 94  ? 3.797  7.374   12.571 1.00 14.83 ? 100 LEU   A N   1 
ATOM   755  C  CA  . LEU   A 1 94  ? 3.179  7.247   13.885 1.00 15.59 ? 100 LEU   A CA  1 
ATOM   756  C  C   . LEU   A 1 94  ? 2.713  5.825   14.150 1.00 14.22 ? 100 LEU   A C   1 
ATOM   757  O  O   . LEU   A 1 94  ? 2.241  5.137   13.227 1.00 15.90 ? 100 LEU   A O   1 
ATOM   758  C  CB  . LEU   A 1 94  ? 1.956  8.188   14.059 1.00 17.80 ? 100 LEU   A CB  1 
ATOM   759  C  CG  . LEU   A 1 94  ? 2.198  9.664   13.994 1.00 21.79 ? 100 LEU   A CG  1 
ATOM   760  C  CD1 . LEU   A 1 94  ? 0.915  10.427  14.350 1.00 23.39 ? 100 LEU   A CD1 1 
ATOM   761  C  CD2 . LEU   A 1 94  ? 3.253  10.117  15.010 1.00 23.75 ? 100 LEU   A CD2 1 
ATOM   762  N  N   . ALA   A 1 95  ? 2.741  5.438   15.431 1.00 14.46 ? 101 ALA   A N   1 
ATOM   763  C  CA  . ALA   A 1 95  ? 2.185  4.163   15.881 1.00 13.47 ? 101 ALA   A CA  1 
ATOM   764  C  C   . ALA   A 1 95  ? 1.585  4.380   17.289 1.00 13.55 ? 101 ALA   A C   1 
ATOM   765  O  O   . ALA   A 1 95  ? 1.874  5.383   17.949 1.00 14.34 ? 101 ALA   A O   1 
ATOM   766  C  CB  . ALA   A 1 95  ? 3.302  3.104   15.979 1.00 14.17 ? 101 ALA   A CB  1 
ATOM   767  N  N   . VAL   A 1 96  ? 0.776  3.422   17.746 1.00 13.08 ? 102 VAL   A N   1 
ATOM   768  C  CA  . VAL   A 1 96  ? 0.256  3.437   19.091 1.00 13.30 ? 102 VAL   A CA  1 
ATOM   769  C  C   . VAL   A 1 96  ? 1.287  2.730   19.969 1.00 15.45 ? 102 VAL   A C   1 
ATOM   770  O  O   . VAL   A 1 96  ? 1.634  1.581   19.714 1.00 16.04 ? 102 VAL   A O   1 
ATOM   771  C  CB  . VAL   A 1 96  ? -1.096 2.696   19.148 1.00 14.13 ? 102 VAL   A CB  1 
ATOM   772  C  CG1 . VAL   A 1 96  ? -1.603 2.548   20.586 1.00 15.15 ? 102 VAL   A CG1 1 
ATOM   773  C  CG2 . VAL   A 1 96  ? -2.108 3.427   18.242 1.00 15.07 ? 102 VAL   A CG2 1 
ATOM   774  N  N   . GLY   A 1 97  ? 1.800  3.435   20.968 1.00 15.88 ? 103 GLY   A N   1 
ATOM   775  C  CA  . GLY   A 1 97  ? 2.805  2.859   21.852 1.00 16.09 ? 103 GLY   A CA  1 
ATOM   776  C  C   . GLY   A 1 97  ? 3.284  3.863   22.859 1.00 16.28 ? 103 GLY   A C   1 
ATOM   777  O  O   . GLY   A 1 97  ? 2.982  5.057   22.758 1.00 17.73 ? 103 GLY   A O   1 
ATOM   778  N  N   . HIS   A 1 98  ? 4.019  3.377   23.871 1.00 16.53 ? 104 HIS   A N   1 
ATOM   779  C  CA  . HIS   A 1 98  ? 4.549  4.258   24.896 1.00 17.35 ? 104 HIS   A CA  1 
ATOM   780  C  C   . HIS   A 1 98  ? 5.840  4.969   24.489 1.00 15.70 ? 104 HIS   A C   1 
ATOM   781  O  O   . HIS   A 1 98  ? 6.770  4.315   23.967 1.00 16.23 ? 104 HIS   A O   1 
ATOM   782  C  CB  . HIS   A 1 98  ? 4.775  3.450   26.194 1.00 18.17 ? 104 HIS   A CB  1 
ATOM   783  C  CG  . HIS   A 1 98  ? 5.131  4.331   27.338 1.00 19.16 ? 104 HIS   A CG  1 
ATOM   784  N  ND1 . HIS   A 1 98  ? 4.219  5.202   27.879 1.00 20.90 ? 104 HIS   A ND1 1 
ATOM   785  C  CD2 . HIS   A 1 98  ? 6.306  4.463   27.991 1.00 20.04 ? 104 HIS   A CD2 1 
ATOM   786  C  CE1 . HIS   A 1 98  ? 4.867  5.839   28.844 1.00 21.26 ? 104 HIS   A CE1 1 
ATOM   787  N  NE2 . HIS   A 1 98  ? 6.122  5.408   28.947 1.00 20.10 ? 104 HIS   A NE2 1 
ATOM   788  N  N   . SER   A 1 99  ? 5.940  6.286   24.726 1.00 15.76 ? 105 SER   A N   1 
ATOM   789  C  CA  . SER   A 1 99  ? 7.121  7.071   24.363 1.00 16.46 ? 105 SER   A CA  1 
ATOM   790  C  C   . SER   A 1 99  ? 7.123  8.273   25.245 1.00 20.77 ? 105 SER   A C   1 
ATOM   791  O  O   . SER   A 1 99  ? 6.277  9.170   25.077 1.00 22.33 ? 105 SER   A O   1 
ATOM   792  C  CB  . SER   A 1 99  ? 7.062  7.476   22.873 1.00 17.12 ? 105 SER   A CB  1 
ATOM   793  O  OG  . SER   A 1 99  ? 8.126  8.314   22.426 1.00 18.58 ? 105 SER   A OG  1 
ATOM   794  N  N   . GLU   A 1 100 ? 8.021  8.297   26.214 1.00 19.98 ? 106 GLU   A N   1 
ATOM   795  C  CA  . GLU   A 1 100 ? 8.113  9.445   27.089 1.00 22.89 ? 106 GLU   A CA  1 
ATOM   796  C  C   . GLU   A 1 100 ? 9.503  10.087  26.843 1.00 25.18 ? 106 GLU   A C   1 
ATOM   797  O  O   . GLU   A 1 100 ? 10.314 9.645   25.971 1.00 24.72 ? 106 GLU   A O   1 
ATOM   798  C  CB  . GLU   A 1 100 ? 7.696  9.071   28.576 1.00 26.19 ? 106 GLU   A CB  1 
ATOM   799  C  CG  . GLU   A 1 100 ? 8.528  7.975   29.163 1.00 26.65 ? 106 GLU   A CG  1 
ATOM   800  C  CD  . GLU   A 1 100 ? 8.240  7.592   30.596 1.00 24.77 ? 106 GLU   A CD  1 
ATOM   801  O  OE1 . GLU   A 1 100 ? 8.830  8.208   31.512 1.00 27.65 ? 106 GLU   A OE1 1 
ATOM   802  O  OE2 . GLU   A 1 100 ? 7.436  6.658   30.801 1.00 22.19 ? 106 GLU   A OE2 1 
ATOM   803  N  N   . PRO   A 1 101 ? 9.688  11.286  27.430 1.00 29.41 ? 107 PRO   A N   1 
ATOM   804  C  CA  . PRO   A 1 101 ? 10.954 11.965  27.288 1.00 29.75 ? 107 PRO   A CA  1 
ATOM   805  C  C   . PRO   A 1 101 ? 12.084 11.178  27.966 1.00 27.20 ? 107 PRO   A C   1 
ATOM   806  O  O   . PRO   A 1 101 ? 12.207 11.066  29.237 1.00 28.91 ? 107 PRO   A O   1 
ATOM   807  C  CB  . PRO   A 1 101 ? 10.699 13.335  27.942 1.00 31.85 ? 107 PRO   A CB  1 
ATOM   808  C  CG  . PRO   A 1 101 ? 9.230  13.426  28.094 1.00 32.92 ? 107 PRO   A CG  1 
ATOM   809  C  CD  . PRO   A 1 101 ? 8.793  12.034  28.327 1.00 30.66 ? 107 PRO   A CD  1 
ATOM   810  N  N   . GLY   A 1 102 ? 12.945 10.743  27.052 1.00 21.19 ? 108 GLY   A N   1 
ATOM   811  C  CA  . GLY   A 1 102 ? 14.119 9.885   27.197 1.00 19.67 ? 108 GLY   A CA  1 
ATOM   812  C  C   . GLY   A 1 102 ? 14.092 8.696   26.238 1.00 16.66 ? 108 GLY   A C   1 
ATOM   813  O  O   . GLY   A 1 102 ? 15.123 8.073   26.027 1.00 15.96 ? 108 GLY   A O   1 
ATOM   814  N  N   . ASP   A 1 103 ? 12.918 8.353   25.653 1.00 15.13 ? 109 ASP   A N   1 
ATOM   815  C  CA  . ASP   A 1 103 ? 12.830 7.249   24.702 1.00 14.60 ? 109 ASP   A CA  1 
ATOM   816  C  C   . ASP   A 1 103 ? 13.338 7.579   23.306 1.00 14.00 ? 109 ASP   A C   1 
ATOM   817  O  O   . ASP   A 1 103 ? 13.568 6.653   22.507 1.00 14.39 ? 109 ASP   A O   1 
ATOM   818  C  CB  . ASP   A 1 103 ? 11.393 6.697   24.618 1.00 13.16 ? 109 ASP   A CB  1 
ATOM   819  C  CG  . ASP   A 1 103 ? 11.029 5.958   25.904 1.00 15.06 ? 109 ASP   A CG  1 
ATOM   820  O  OD1 . ASP   A 1 103 ? 11.896 5.275   26.441 1.00 14.78 ? 109 ASP   A OD1 1 
ATOM   821  O  OD2 . ASP   A 1 103 ? 9.846  6.062   26.358 1.00 14.31 ? 109 ASP   A OD2 1 
ATOM   822  N  N   . CYS   A 1 104 ? 13.557 8.893   23.011 1.00 13.41 ? 110 CYS   A N   1 
ATOM   823  C  CA  . CYS   A 1 104 ? 14.094 9.198   21.645 1.00 14.01 ? 110 CYS   A CA  1 
ATOM   824  C  C   . CYS   A 1 104 ? 15.428 8.492   21.418 1.00 13.81 ? 110 CYS   A C   1 
ATOM   825  O  O   . CYS   A 1 104 ? 16.249 8.394   22.321 1.00 13.67 ? 110 CYS   A O   1 
ATOM   826  C  CB  . CYS   A 1 104 ? 14.245 10.696  21.449 1.00 14.79 ? 110 CYS   A CB  1 
ATOM   827  S  SG  . CYS   A 1 104 ? 12.675 11.578  21.257 1.00 18.63 ? 110 CYS   A SG  1 
ATOM   828  N  N   . GLY   A 1 105 ? 15.615 7.987   20.209 1.00 13.07 ? 111 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 105 ? 16.845 7.283   19.858 1.00 12.25 ? 111 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 105 ? 16.672 5.772   19.783 1.00 12.22 ? 111 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 105 ? 17.513 5.072   19.210 1.00 13.02 ? 111 GLY   A O   1 
ATOM   832  N  N   . GLY   A 1 106 ? 15.569 5.258   20.353 1.00 12.24 ? 112 GLY   A N   1 
ATOM   833  C  CA  . GLY   A 1 106 ? 15.309 3.829   20.273 1.00 11.27 ? 112 GLY   A CA  1 
ATOM   834  C  C   . GLY   A 1 106 ? 15.079 3.413   18.818 1.00 10.74 ? 112 GLY   A C   1 
ATOM   835  O  O   . GLY   A 1 106 ? 14.395 4.115   18.071 1.00 11.66 ? 112 GLY   A O   1 
ATOM   836  N  N   . ILE   A 1 107 ? 15.592 2.228   18.430 1.00 11.00 ? 113 ILE   A N   1 
ATOM   837  C  CA  . ILE   A 1 107 ? 15.424 1.787   17.028 1.00 10.55 ? 113 ILE   A CA  1 
ATOM   838  C  C   . ILE   A 1 107 ? 14.092 1.133   16.753 1.00 10.33 ? 113 ILE   A C   1 
ATOM   839  O  O   . ILE   A 1 107 ? 13.615 0.307   17.544 1.00 11.38 ? 113 ILE   A O   1 
ATOM   840  C  CB  . ILE   A 1 107 ? 16.595 0.836   16.685 1.00 10.95 ? 113 ILE   A CB  1 
ATOM   841  C  CG1 . ILE   A 1 107 ? 17.869 1.698   16.455 1.00 12.63 ? 113 ILE   A CG1 1 
ATOM   842  C  CG2 . ILE   A 1 107 ? 16.314 -0.076  15.452 1.00 12.45 ? 113 ILE   A CG2 1 
ATOM   843  C  CD1 . ILE   A 1 107 ? 19.152 0.873   16.266 1.00 15.68 ? 113 ILE   A CD1 1 
ATOM   844  N  N   . LEU   A 1 108 ? 13.517 1.485   15.572 1.00 10.19 ? 114 LEU   A N   1 
ATOM   845  C  CA  . LEU   A 1 108 ? 12.397 0.773   14.969 1.00 10.32 ? 114 LEU   A CA  1 
ATOM   846  C  C   . LEU   A 1 108 ? 13.022 -0.093  13.846 1.00 10.48 ? 114 LEU   A C   1 
ATOM   847  O  O   . LEU   A 1 108 ? 13.807 0.425   13.028 1.00 11.54 ? 114 LEU   A O   1 
ATOM   848  C  CB  . LEU   A 1 108 ? 11.401 1.774   14.353 1.00 10.76 ? 114 LEU   A CB  1 
ATOM   849  C  CG  . LEU   A 1 108 ? 10.301 1.141   13.453 1.00 11.81 ? 114 LEU   A CG  1 
ATOM   850  C  CD1 . LEU   A 1 108 ? 9.313  0.335   14.312 1.00 13.05 ? 114 LEU   A CD1 1 
ATOM   851  C  CD2 . LEU   A 1 108 ? 9.490  2.240   12.683 1.00 13.93 ? 114 LEU   A CD2 1 
ATOM   852  N  N   . ARG   A 1 109 ? 12.719 -1.397  13.820 1.00 11.09 ? 115 ARG   A N   1 
ATOM   853  C  CA  . ARG   A 1 109 ? 13.299 -2.296  12.800 1.00 11.72 ? 115 ARG   A CA  1 
ATOM   854  C  C   . ARG   A 1 109 ? 12.242 -3.223  12.238 1.00 12.24 ? 115 ARG   A C   1 
ATOM   855  O  O   . ARG   A 1 109 ? 11.208 -3.487  12.876 1.00 12.42 ? 115 ARG   A O   1 
ATOM   856  C  CB  . ARG   A 1 109 ? 14.441 -3.134  13.422 1.00 13.27 ? 115 ARG   A CB  1 
ATOM   857  C  CG  . ARG   A 1 109 ? 13.976 -4.096  14.511 1.00 13.36 ? 115 ARG   A CG  1 
ATOM   858  C  CD  . ARG   A 1 109 ? 15.233 -4.817  15.004 1.00 14.87 ? 115 ARG   A CD  1 
ATOM   859  N  NE  . ARG   A 1 109 ? 16.008 -3.968  15.897 1.00 16.52 ? 115 ARG   A NE  1 
ATOM   860  C  CZ  . ARG   A 1 109 ? 17.306 -3.723  15.766 1.00 16.50 ? 115 ARG   A CZ  1 
ATOM   861  N  NH1 . ARG   A 1 109 ? 17.969 -4.148  14.691 1.00 16.10 ? 115 ARG   A NH1 1 
ATOM   862  N  NH2 . ARG   A 1 109 ? 17.949 -2.996  16.677 1.00 16.86 ? 115 ARG   A NH2 1 
ATOM   863  N  N   . CYS   A 1 110 ? 12.515 -3.709  11.030 1.00 14.68 ? 116 CYS   A N   1 
ATOM   864  C  CA  . CYS   A 1 110 ? 11.652 -4.695  10.391 1.00 17.78 ? 116 CYS   A CA  1 
ATOM   865  C  C   . CYS   A 1 110 ? 12.535 -5.890  9.972  1.00 20.95 ? 116 CYS   A C   1 
ATOM   866  O  O   . CYS   A 1 110 ? 13.717 -5.946  10.321 1.00 20.73 ? 116 CYS   A O   1 
ATOM   867  C  CB  . CYS   A 1 110 ? 10.961 -4.056  9.196  1.00 17.02 ? 116 CYS   A CB  1 
ATOM   868  S  SG  . CYS   A 1 110 ? 12.109 -3.655  7.842  1.00 17.51 ? 116 CYS   A SG  1 
ATOM   869  N  N   . GLN   A 1 111 ? 11.961 -6.858  9.180  1.00 24.07 ? 117 GLN   A N   1 
ATOM   870  C  CA  . GLN   A 1 111 ? 12.761 -7.991  8.741  1.00 26.56 ? 117 GLN   A CA  1 
ATOM   871  C  C   . GLN   A 1 111 ? 13.966 -7.586  7.860  1.00 26.29 ? 117 GLN   A C   1 
ATOM   872  O  O   . GLN   A 1 111 ? 14.928 -8.350  7.754  1.00 28.47 ? 117 GLN   A O   1 
ATOM   873  C  CB  . GLN   A 1 111 ? 11.883 -9.032  8.000  1.00 30.65 ? 117 GLN   A CB  1 
ATOM   874  C  CG  . GLN   A 1 111 ? 11.403 -8.536  6.642  1.00 35.97 ? 117 GLN   A CG  1 
ATOM   875  C  CD  . GLN   A 1 111 ? 10.414 -9.444  5.953  1.00 42.08 ? 117 GLN   A CD  1 
ATOM   876  O  OE1 . GLN   A 1 111 ? 9.196  -9.342  6.155  1.00 44.22 ? 117 GLN   A OE1 1 
ATOM   877  N  NE2 . GLN   A 1 111 ? 10.908 -10.321 5.098  1.00 41.74 ? 117 GLN   A NE2 1 
ATOM   878  N  N   . HIS   A 1 112 ? 13.938 -6.387  7.265  1.00 22.69 ? 118 HIS   A N   1 
ATOM   879  C  CA  . HIS   A 1 112 ? 15.017 -5.939  6.361  1.00 20.97 ? 118 HIS   A CA  1 
ATOM   880  C  C   . HIS   A 1 112 ? 16.143 -5.148  7.035  1.00 20.61 ? 118 HIS   A C   1 
ATOM   881  O  O   . HIS   A 1 112 ? 17.183 -4.885  6.415  1.00 21.87 ? 118 HIS   A O   1 
ATOM   882  C  CB  . HIS   A 1 112 ? 14.410 -5.124  5.207  1.00 20.53 ? 118 HIS   A CB  1 
ATOM   883  C  CG  . HIS   A 1 112 ? 13.299 -5.851  4.494  1.00 24.95 ? 118 HIS   A CG  1 
ATOM   884  N  ND1 . HIS   A 1 112 ? 11.984 -5.459  4.620  1.00 27.12 ? 118 HIS   A ND1 1 
ATOM   885  C  CD2 . HIS   A 1 112 ? 13.360 -6.884  3.613  1.00 27.20 ? 118 HIS   A CD2 1 
ATOM   886  C  CE1 . HIS   A 1 112 ? 11.269 -6.314  3.903  1.00 28.84 ? 118 HIS   A CE1 1 
ATOM   887  N  NE2 . HIS   A 1 112 ? 12.061 -7.171  3.247  1.00 28.52 ? 118 HIS   A NE2 1 
ATOM   888  N  N   . GLY   A 1 113 ? 15.921 -4.721  8.287  1.00 18.64 ? 119 GLY   A N   1 
ATOM   889  C  CA  . GLY   A 1 113 ? 16.920 -3.921  8.973  1.00 17.07 ? 119 GLY   A CA  1 
ATOM   890  C  C   . GLY   A 1 113 ? 16.291 -2.750  9.717  1.00 14.41 ? 119 GLY   A C   1 
ATOM   891  O  O   . GLY   A 1 113 ? 15.103 -2.757  10.060 1.00 14.42 ? 119 GLY   A O   1 
ATOM   892  N  N   . VAL   A 1 114 ? 17.117 -1.720  9.984  1.00 13.58 ? 120 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 114 ? 16.680 -0.513  10.726 1.00 13.49 ? 120 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 114 ? 15.821 0.403   9.861  1.00 11.92 ? 120 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 114 ? 16.238 0.756   8.737  1.00 12.38 ? 120 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 114 ? 17.893 0.256   11.314 1.00 13.05 ? 120 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 114 ? 17.451 1.561   11.996 1.00 13.80 ? 120 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 114 ? 18.675 -0.620  12.277 1.00 13.86 ? 120 VAL   A CG2 1 
ATOM   899  N  N   . VAL   A 1 115 ? 14.655 0.787   10.371 1.00 12.20 ? 121 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 115 ? 13.693 1.612   9.652  1.00 12.09 ? 121 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 115 ? 13.840 3.067   10.075 1.00 12.09 ? 121 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 115 ? 13.700 3.977   9.273  1.00 13.34 ? 121 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 115 ? 12.243 1.113   9.968  1.00 13.45 ? 121 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 115 ? 11.168 2.073   9.426  1.00 14.60 ? 121 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 115 ? 12.033 -0.288  9.438  1.00 14.33 ? 121 VAL   A CG2 1 
ATOM   906  N  N   . GLY   A 1 116 ? 14.038 3.300   11.384 1.00 12.20 ? 122 GLY   A N   1 
ATOM   907  C  CA  . GLY   A 1 116 ? 14.166 4.670   11.887 1.00 12.44 ? 122 GLY   A CA  1 
ATOM   908  C  C   . GLY   A 1 116 ? 14.352 4.708   13.389 1.00 11.83 ? 122 GLY   A C   1 
ATOM   909  O  O   . GLY   A 1 116 ? 14.710 3.673   13.959 1.00 11.85 ? 122 GLY   A O   1 
ATOM   910  N  N   . ILE   A 1 117 ? 14.245 5.884   13.990 1.00 11.64 ? 123 ILE   A N   1 
ATOM   911  C  CA  . ILE   A 1 117 ? 14.457 6.022   15.441 1.00 10.98 ? 123 ILE   A CA  1 
ATOM   912  C  C   . ILE   A 1 117 ? 13.299 6.770   16.063 1.00 10.97 ? 123 ILE   A C   1 
ATOM   913  O  O   . ILE   A 1 117 ? 12.706 7.652   15.424 1.00 12.11 ? 123 ILE   A O   1 
ATOM   914  C  CB  . ILE   A 1 117 ? 15.795 6.712   15.816 1.00 12.19 ? 123 ILE   A CB  1 
ATOM   915  C  CG1 . ILE   A 1 117 ? 15.953 8.051   15.096 1.00 13.71 ? 123 ILE   A CG1 1 
ATOM   916  C  CG2 . ILE   A 1 117 ? 16.960 5.759   15.599 1.00 13.30 ? 123 ILE   A CG2 1 
ATOM   917  C  CD1 . ILE   A 1 117 ? 17.236 8.846   15.576 1.00 15.43 ? 123 ILE   A CD1 1 
ATOM   918  N  N   . VAL   A 1 118 ? 13.028 6.509   17.354 1.00 11.46 ? 124 VAL   A N   1 
ATOM   919  C  CA  . VAL   A 1 118 ? 11.980 7.233   18.075 1.00 11.64 ? 124 VAL   A CA  1 
ATOM   920  C  C   . VAL   A 1 118 ? 12.337 8.741   18.070 1.00 11.92 ? 124 VAL   A C   1 
ATOM   921  O  O   . VAL   A 1 118 ? 13.497 9.097   18.364 1.00 12.67 ? 124 VAL   A O   1 
ATOM   922  C  CB  . VAL   A 1 118 ? 11.865 6.754   19.537 1.00 12.22 ? 124 VAL   A CB  1 
ATOM   923  C  CG1 . VAL   A 1 118 ? 10.865 7.632   20.329 1.00 13.12 ? 124 VAL   A CG1 1 
ATOM   924  C  CG2 . VAL   A 1 118 ? 11.427 5.277   19.588 1.00 12.64 ? 124 VAL   A CG2 1 
ATOM   925  N  N   . SER   A 1 119 ? 11.357 9.602   17.750 1.00 12.94 ? 125 SER   A N   1 
ATOM   926  C  CA  . SER   A 1 119 ? 11.541 11.054  17.679 1.00 14.17 ? 125 SER   A CA  1 
ATOM   927  C  C   . SER   A 1 119 ? 10.453 11.824  18.422 1.00 16.01 ? 125 SER   A C   1 
ATOM   928  O  O   . SER   A 1 119 ? 10.735 12.921  18.895 1.00 18.63 ? 125 SER   A O   1 
ATOM   929  C  CB  . SER   A 1 119 ? 11.655 11.481  16.219 1.00 16.11 ? 125 SER   A CB  1 
ATOM   930  O  OG  . SER   A 1 119 ? 11.729 12.884  16.024 1.00 16.92 ? 125 SER   A OG  1 
ATOM   931  N  N   . THR   A 1 120 ? 9.223  11.273  18.549 1.00 15.76 ? 126 THR   A N   1 
ATOM   932  C  CA  . THR   A 1 120 ? 8.126  11.989  19.248 1.00 17.22 ? 126 THR   A CA  1 
ATOM   933  C  C   . THR   A 1 120 ? 7.339  11.013  20.183 1.00 17.25 ? 126 THR   A C   1 
ATOM   934  O  O   . THR   A 1 120 ? 7.479  9.796   20.056 1.00 16.28 ? 126 THR   A O   1 
ATOM   935  C  CB  . THR   A 1 120 ? 7.160  12.666  18.214 1.00 18.66 ? 126 THR   A CB  1 
ATOM   936  O  OG1 . THR   A 1 120 ? 6.339  11.696  17.582 1.00 19.71 ? 126 THR   A OG1 1 
ATOM   937  C  CG2 . THR   A 1 120 ? 7.869  13.529  17.181 1.00 19.26 ? 126 THR   A CG2 1 
ATOM   938  N  N   . GLY   A 1 121 ? 6.485  11.541  21.078 1.00 18.58 ? 127 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 121 ? 5.695  10.676  21.960 1.00 20.51 ? 127 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 121 ? 4.456  11.325  22.566 1.00 23.51 ? 127 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 121 ? 3.905  12.234  21.980 1.00 26.20 ? 127 GLY   A O   1 
ATOM   942  N  N   . GLY   A 1 122 ? 4.006  10.815  23.705 1.00 22.89 ? 128 GLY   A N   1 
ATOM   943  C  CA  . GLY   A 1 122 ? 2.849  11.339  24.423 1.00 23.79 ? 128 GLY   A CA  1 
ATOM   944  C  C   . GLY   A 1 122 ? 1.520  10.845  23.900 1.00 25.22 ? 128 GLY   A C   1 
ATOM   945  O  O   . GLY   A 1 122 ? 1.387  10.436  22.735 1.00 24.66 ? 128 GLY   A O   1 
ATOM   946  N  N   . ASN   A 1 123 ? 0.517  10.929  24.756 1.00 26.05 ? 129 ASN   A N   1 
ATOM   947  C  CA  . ASN   A 1 123 ? -0.862 10.606  24.377 1.00 27.43 ? 129 ASN   A CA  1 
ATOM   948  C  C   . ASN   A 1 123 ? -1.043 9.140   23.939 1.00 24.86 ? 129 ASN   A C   1 
ATOM   949  O  O   . ASN   A 1 123 ? -2.064 8.818   23.309 1.00 24.11 ? 129 ASN   A O   1 
ATOM   950  C  CB  . ASN   A 1 123 ? -1.350 11.573  23.271 1.00 30.05 ? 129 ASN   A CB  1 
ATOM   951  C  CG  . ASN   A 1 123 ? -1.535 13.017  23.715 1.00 36.18 ? 129 ASN   A CG  1 
ATOM   952  O  OD1 . ASN   A 1 123 ? -1.680 13.319  24.905 1.00 38.48 ? 129 ASN   A OD1 1 
ATOM   953  N  ND2 . ASN   A 1 123 ? -1.541 13.935  22.760 1.00 36.58 ? 129 ASN   A ND2 1 
ATOM   954  N  N   . GLY   A 1 124 ? -0.125 8.249   24.308 1.00 22.27 ? 130 GLY   A N   1 
ATOM   955  C  CA  . GLY   A 1 124 ? -0.224 6.864   23.897 1.00 20.15 ? 130 GLY   A CA  1 
ATOM   956  C  C   . GLY   A 1 124 ? 0.187  6.678   22.436 1.00 17.72 ? 130 GLY   A C   1 
ATOM   957  O  O   . GLY   A 1 124 ? -0.028 5.605   21.885 1.00 17.68 ? 130 GLY   A O   1 
ATOM   958  N  N   . LEU   A 1 125 ? 0.905  7.656   21.853 1.00 16.00 ? 131 LEU   A N   1 
ATOM   959  C  CA  . LEU   A 1 125 ? 1.458  7.581   20.485 1.00 15.82 ? 131 LEU   A CA  1 
ATOM   960  C  C   . LEU   A 1 125 ? 2.981  7.648   20.520 1.00 17.02 ? 131 LEU   A C   1 
ATOM   961  O  O   . LEU   A 1 125 ? 3.562  8.213   21.467 1.00 18.51 ? 131 LEU   A O   1 
ATOM   962  C  CB  . LEU   A 1 125 ? 0.949  8.764   19.641 1.00 16.83 ? 131 LEU   A CB  1 
ATOM   963  C  CG  . LEU   A 1 125 ? -0.572 8.749   19.407 1.00 17.91 ? 131 LEU   A CG  1 
ATOM   964  C  CD1 . LEU   A 1 125 ? -1.069 10.120  18.974 1.00 20.13 ? 131 LEU   A CD1 1 
ATOM   965  C  CD2 . LEU   A 1 125 ? -0.976 7.645   18.409 1.00 18.22 ? 131 LEU   A CD2 1 
ATOM   966  N  N   . VAL   A 1 126 ? 3.612  7.028   19.543 1.00 14.87 ? 132 VAL   A N   1 
ATOM   967  C  CA  . VAL   A 1 126 ? 5.072  7.105   19.388 1.00 14.38 ? 132 VAL   A CA  1 
ATOM   968  C  C   . VAL   A 1 126 ? 5.320  7.444   17.915 1.00 14.28 ? 132 VAL   A C   1 
ATOM   969  O  O   . VAL   A 1 126 ? 4.715  6.857   17.018 1.00 15.14 ? 132 VAL   A O   1 
ATOM   970  C  CB  . VAL   A 1 126 ? 5.767  5.782   19.807 1.00 14.47 ? 132 VAL   A CB  1 
ATOM   971  C  CG1 . VAL   A 1 126 ? 5.166  4.576   19.096 1.00 15.61 ? 132 VAL   A CG1 1 
ATOM   972  C  CG2 . VAL   A 1 126 ? 7.299  5.859   19.592 1.00 14.61 ? 132 VAL   A CG2 1 
ATOM   973  N  N   . GLY   A 1 127 ? 6.216  8.398   17.655 1.00 13.78 ? 133 GLY   A N   1 
ATOM   974  C  CA  . GLY   A 1 127 ? 6.562  8.780   16.284 1.00 13.44 ? 133 GLY   A CA  1 
ATOM   975  C  C   . GLY   A 1 127 ? 8.016  8.464   16.002 1.00 13.51 ? 133 GLY   A C   1 
ATOM   976  O  O   . GLY   A 1 127 ? 8.886  8.606   16.875 1.00 14.88 ? 133 GLY   A O   1 
ATOM   977  N  N   . PHE   A 1 128 ? 8.262  7.980   14.800 1.00 12.64 ? 134 PHE   A N   1 
ATOM   978  C  CA  . PHE   A 1 128 ? 9.606  7.564   14.365 1.00 13.00 ? 134 PHE   A CA  1 
ATOM   979  C  C   . PHE   A 1 128 ? 10.070 8.386   13.169 1.00 13.28 ? 134 PHE   A C   1 
ATOM   980  O  O   . PHE   A 1 128 ? 9.318  8.559   12.200 1.00 13.59 ? 134 PHE   A O   1 
ATOM   981  C  CB  . PHE   A 1 128 ? 9.582  6.082   13.930 1.00 13.67 ? 134 PHE   A CB  1 
ATOM   982  C  CG  . PHE   A 1 128 ? 8.959  5.158   14.959 1.00 13.45 ? 134 PHE   A CG  1 
ATOM   983  C  CD1 . PHE   A 1 128 ? 9.703  4.673   16.025 1.00 13.02 ? 134 PHE   A CD1 1 
ATOM   984  C  CD2 . PHE   A 1 128 ? 7.633  4.762   14.842 1.00 14.40 ? 134 PHE   A CD2 1 
ATOM   985  C  CE1 . PHE   A 1 128 ? 9.120  3.827   16.970 1.00 13.44 ? 134 PHE   A CE1 1 
ATOM   986  C  CE2 . PHE   A 1 128 ? 7.058  3.915   15.779 1.00 14.59 ? 134 PHE   A CE2 1 
ATOM   987  C  CZ  . PHE   A 1 128 ? 7.817  3.440   16.833 1.00 13.57 ? 134 PHE   A CZ  1 
ATOM   988  N  N   . ALA   A 1 129 ? 11.312 8.854   13.247 1.00 13.03 ? 135 ALA   A N   1 
ATOM   989  C  CA  . ALA   A 1 129 ? 11.944 9.516   12.110 1.00 13.32 ? 135 ALA   A CA  1 
ATOM   990  C  C   . ALA   A 1 129 ? 12.437 8.437   11.154 1.00 12.65 ? 135 ALA   A C   1 
ATOM   991  O  O   . ALA   A 1 129 ? 13.311 7.645   11.528 1.00 12.92 ? 135 ALA   A O   1 
ATOM   992  C  CB  . ALA   A 1 129 ? 13.082 10.392  12.613 1.00 12.92 ? 135 ALA   A CB  1 
ATOM   993  N  N   . ASP   A 1 130 ? 11.895 8.380   9.913  1.00 13.23 ? 136 ASP   A N   1 
ATOM   994  C  CA  . ASP   A 1 130 ? 12.317 7.400   8.911  1.00 13.83 ? 136 ASP   A CA  1 
ATOM   995  C  C   . ASP   A 1 130 ? 13.722 7.699   8.394  1.00 13.63 ? 136 ASP   A C   1 
ATOM   996  O  O   . ASP   A 1 130 ? 14.110 8.871   8.258  1.00 15.25 ? 136 ASP   A O   1 
ATOM   997  C  CB  . ASP   A 1 130 ? 11.358 7.483   7.694  1.00 15.37 ? 136 ASP   A CB  1 
ATOM   998  C  CG  . ASP   A 1 130 ? 11.624 6.455   6.626  1.00 23.44 ? 136 ASP   A CG  1 
ATOM   999  O  OD1 . ASP   A 1 130 ? 11.742 5.256   6.964  1.00 18.75 ? 136 ASP   A OD1 1 
ATOM   1000 O  OD2 . ASP   A 1 130 ? 11.771 6.858   5.430  1.00 29.85 ? 136 ASP   A OD2 1 
ATOM   1001 N  N   . VAL   A 1 131 ? 14.490 6.637   8.129  1.00 11.96 ? 137 VAL   A N   1 
ATOM   1002 C  CA  . VAL   A 1 131 ? 15.806 6.788   7.490  1.00 11.75 ? 137 VAL   A CA  1 
ATOM   1003 C  C   . VAL   A 1 131 ? 15.921 5.957   6.190  1.00 12.88 ? 137 VAL   A C   1 
ATOM   1004 O  O   . VAL   A 1 131 ? 16.994 5.975   5.584  1.00 13.22 ? 137 VAL   A O   1 
ATOM   1005 C  CB  . VAL   A 1 131 ? 16.973 6.439   8.454  1.00 12.12 ? 137 VAL   A CB  1 
ATOM   1006 C  CG1 . VAL   A 1 131 ? 17.025 7.366   9.680  1.00 13.16 ? 137 VAL   A CG1 1 
ATOM   1007 C  CG2 . VAL   A 1 131 ? 16.970 4.952   8.840  1.00 13.43 ? 137 VAL   A CG2 1 
ATOM   1008 N  N   . ARG   A 1 132 ? 14.867 5.250   5.769  1.00 13.57 ? 138 ARG   A N   1 
ATOM   1009 C  CA  . ARG   A 1 132 ? 14.956 4.347   4.618  1.00 13.59 ? 138 ARG   A CA  1 
ATOM   1010 C  C   . ARG   A 1 132 ? 15.212 5.033   3.308  1.00 15.27 ? 138 ARG   A C   1 
ATOM   1011 O  O   . ARG   A 1 132 ? 15.676 4.373   2.359  1.00 16.22 ? 138 ARG   A O   1 
ATOM   1012 C  CB  . ARG   A 1 132 ? 13.697 3.471   4.532  1.00 14.32 ? 138 ARG   A CB  1 
ATOM   1013 C  CG  . ARG   A 1 132 ? 13.576 2.510   5.734  1.00 13.97 ? 138 ARG   A CG  1 
ATOM   1014 C  CD  . ARG   A 1 132 ? 12.274 1.718   5.623  1.00 14.53 ? 138 ARG   A CD  1 
ATOM   1015 N  NE  . ARG   A 1 132 ? 11.119 2.607   5.834  1.00 14.44 ? 138 ARG   A NE  1 
ATOM   1016 C  CZ  . ARG   A 1 132 ? 9.863  2.194   5.937  1.00 17.01 ? 138 ARG   A CZ  1 
ATOM   1017 N  NH1 . ARG   A 1 132 ? 9.555  0.919   5.700  1.00 17.34 ? 138 ARG   A NH1 1 
ATOM   1018 N  NH2 . ARG   A 1 132 ? 8.891  3.073   6.179  1.00 19.12 ? 138 ARG   A NH2 1 
ATOM   1019 N  N   . ASP   A 1 133 ? 14.910 6.356   3.209  1.00 14.66 ? 139 ASP   A N   1 
ATOM   1020 C  CA  . ASP   A 1 133 ? 15.166 7.053   1.946  1.00 15.87 ? 139 ASP   A CA  1 
ATOM   1021 C  C   . ASP   A 1 133 ? 16.605 7.592   1.852  1.00 15.58 ? 139 ASP   A C   1 
ATOM   1022 O  O   . ASP   A 1 133 ? 16.991 8.078   0.795  1.00 17.15 ? 139 ASP   A O   1 
ATOM   1023 C  CB  . ASP   A 1 133 ? 14.168 8.233   1.791  1.00 17.87 ? 139 ASP   A CB  1 
ATOM   1024 C  CG  . ASP   A 1 133 ? 14.375 9.298   2.878  1.00 21.50 ? 139 ASP   A CG  1 
ATOM   1025 O  OD1 . ASP   A 1 133 ? 14.505 8.926   4.085  1.00 20.35 ? 139 ASP   A OD1 1 
ATOM   1026 O  OD2 . ASP   A 1 133 ? 14.396 10.485  2.547  1.00 23.27 ? 139 ASP   A OD2 1 
ATOM   1027 N  N   . LEU   A 1 134 ? 17.402 7.532   2.957  1.00 13.71 ? 140 LEU   A N   1 
ATOM   1028 C  CA  . LEU   A 1 134 ? 18.765 8.081   2.994  1.00 13.90 ? 140 LEU   A CA  1 
ATOM   1029 C  C   . LEU   A 1 134 ? 19.738 7.027   2.457  1.00 14.24 ? 140 LEU   A C   1 
ATOM   1030 O  O   . LEU   A 1 134 ? 20.423 6.334   3.211  1.00 14.77 ? 140 LEU   A O   1 
ATOM   1031 C  CB  . LEU   A 1 134 ? 19.111 8.485   4.455  1.00 14.02 ? 140 LEU   A CB  1 
ATOM   1032 C  CG  . LEU   A 1 134 ? 18.135 9.510   5.079  1.00 15.84 ? 140 LEU   A CG  1 
ATOM   1033 C  CD1 . LEU   A 1 134 ? 18.521 9.773   6.529  1.00 16.25 ? 140 LEU   A CD1 1 
ATOM   1034 C  CD2 . LEU   A 1 134 ? 18.144 10.823  4.300  1.00 17.56 ? 140 LEU   A CD2 1 
ATOM   1035 N  N   . LEU   A 1 135 ? 19.757 6.881   1.116  1.00 14.46 ? 141 LEU   A N   1 
ATOM   1036 C  CA  . LEU   A 1 135 ? 20.519 5.795   0.507  1.00 15.47 ? 141 LEU   A CA  1 
ATOM   1037 C  C   . LEU   A 1 135 ? 22.008 5.928   0.705  1.00 15.38 ? 141 LEU   A C   1 
ATOM   1038 O  O   . LEU   A 1 135 ? 22.727 4.913   0.749  1.00 17.19 ? 141 LEU   A O   1 
ATOM   1039 C  CB  . LEU   A 1 135 ? 20.187 5.659   -1.013 1.00 16.80 ? 141 LEU   A CB  1 
ATOM   1040 C  CG  . LEU   A 1 135 ? 18.667 5.637   -1.337 1.00 18.61 ? 141 LEU   A CG  1 
ATOM   1041 C  CD1 . LEU   A 1 135 ? 18.437 5.301   -2.836 1.00 20.49 ? 141 LEU   A CD1 1 
ATOM   1042 C  CD2 . LEU   A 1 135 ? 17.861 4.646   -0.480 1.00 19.84 ? 141 LEU   A CD2 1 
ATOM   1043 N  N   . TRP   A 1 136 ? 22.482 7.172   0.872  1.00 14.20 ? 142 TRP   A N   1 
ATOM   1044 C  CA  . TRP   A 1 136 ? 23.897 7.422   1.048  1.00 14.81 ? 142 TRP   A CA  1 
ATOM   1045 C  C   . TRP   A 1 136 ? 24.439 6.837   2.349  1.00 14.96 ? 142 TRP   A C   1 
ATOM   1046 O  O   . TRP   A 1 136 ? 25.666 6.737   2.477  1.00 16.29 ? 142 TRP   A O   1 
ATOM   1047 C  CB  . TRP   A 1 136 ? 24.196 8.936   0.919  1.00 15.16 ? 142 TRP   A CB  1 
ATOM   1048 C  CG  . TRP   A 1 136 ? 23.385 9.779   1.861  1.00 14.76 ? 142 TRP   A CG  1 
ATOM   1049 C  CD1 . TRP   A 1 136 ? 22.220 10.434  1.577  1.00 16.28 ? 142 TRP   A CD1 1 
ATOM   1050 C  CD2 . TRP   A 1 136 ? 23.712 10.105  3.231  1.00 15.09 ? 142 TRP   A CD2 1 
ATOM   1051 N  NE1 . TRP   A 1 136 ? 21.758 11.093  2.712  1.00 17.03 ? 142 TRP   A NE1 1 
ATOM   1052 C  CE2 . TRP   A 1 136 ? 22.682 10.937  3.720  1.00 15.86 ? 142 TRP   A CE2 1 
ATOM   1053 C  CE3 . TRP   A 1 136 ? 24.785 9.794   4.076  1.00 16.14 ? 142 TRP   A CE3 1 
ATOM   1054 C  CZ2 . TRP   A 1 136 ? 22.697 11.434  5.030  1.00 16.80 ? 142 TRP   A CZ2 1 
ATOM   1055 C  CZ3 . TRP   A 1 136 ? 24.817 10.321  5.353  1.00 17.47 ? 142 TRP   A CZ3 1 
ATOM   1056 C  CH2 . TRP   A 1 136 ? 23.785 11.133  5.813  1.00 16.74 ? 142 TRP   A CH2 1 
ATOM   1057 N  N   . LEU   A 1 137 ? 23.573 6.472   3.328  1.00 14.28 ? 143 LEU   A N   1 
ATOM   1058 C  CA  . LEU   A 1 137 ? 24.083 5.834   4.548  1.00 15.68 ? 143 LEU   A CA  1 
ATOM   1059 C  C   . LEU   A 1 137 ? 24.783 4.500   4.234  1.00 18.51 ? 143 LEU   A C   1 
ATOM   1060 O  O   . LEU   A 1 137 ? 25.610 4.056   5.031  1.00 19.64 ? 143 LEU   A O   1 
ATOM   1061 C  CB  . LEU   A 1 137 ? 22.952 5.574   5.550  1.00 15.34 ? 143 LEU   A CB  1 
ATOM   1062 C  CG  . LEU   A 1 137 ? 22.378 6.807   6.211  1.00 15.19 ? 143 LEU   A CG  1 
ATOM   1063 C  CD1 . LEU   A 1 137 ? 21.102 6.449   6.974  1.00 15.89 ? 143 LEU   A CD1 1 
ATOM   1064 C  CD2 . LEU   A 1 137 ? 23.451 7.449   7.185  1.00 15.74 ? 143 LEU   A CD2 1 
ATOM   1065 N  N   . ASP   A 1 138 ? 24.463 3.870   3.082  1.00 20.89 ? 144 ASP   A N   1 
ATOM   1066 C  CA  . ASP   A 1 138 ? 25.045 2.562   2.692  1.00 23.37 ? 144 ASP   A CA  1 
ATOM   1067 C  C   . ASP   A 1 138 ? 26.385 2.655   1.973  1.00 27.22 ? 144 ASP   A C   1 
ATOM   1068 O  O   . ASP   A 1 138 ? 26.943 1.610   1.609  1.00 28.31 ? 144 ASP   A O   1 
ATOM   1069 C  CB  . ASP   A 1 138 ? 24.086 1.797   1.741  1.00 24.39 ? 144 ASP   A CB  1 
ATOM   1070 C  CG  . ASP   A 1 138 ? 22.723 1.497   2.296  1.00 27.76 ? 144 ASP   A CG  1 
ATOM   1071 O  OD1 . ASP   A 1 138 ? 22.558 1.571   3.530  1.00 29.08 ? 144 ASP   A OD1 1 
ATOM   1072 O  OD2 . ASP   A 1 138 ? 21.805 1.191   1.499  1.00 32.46 ? 144 ASP   A OD2 1 
ATOM   1073 N  N   . GLU   A 1 139 ? 26.900 3.865   1.722  1.00 28.81 ? 145 GLU   A N   1 
ATOM   1074 C  CA  . GLU   A 1 139 ? 28.141 4.012   0.950  1.00 32.37 ? 145 GLU   A CA  1 
ATOM   1075 C  C   . GLU   A 1 139 ? 29.137 4.994   1.590  1.00 35.00 ? 145 GLU   A C   1 
ATOM   1076 O  O   . GLU   A 1 139 ? 28.796 5.651   2.571  1.00 34.77 ? 145 GLU   A O   1 
ATOM   1077 C  CB  . GLU   A 1 139 ? 27.772 4.456   -0.480 1.00 36.15 ? 145 GLU   A CB  1 
ATOM   1078 C  CG  . GLU   A 1 139 ? 26.967 5.743   -0.498 1.00 43.02 ? 145 GLU   A CG  1 
ATOM   1079 C  CD  . GLU   A 1 139 ? 26.227 6.068   -1.782 1.00 50.12 ? 145 GLU   A CD  1 
ATOM   1080 O  OE1 . GLU   A 1 139 ? 26.045 7.275   -2.066 1.00 50.12 ? 145 GLU   A OE1 1 
ATOM   1081 O  OE2 . GLU   A 1 139 ? 25.827 5.122   -2.501 1.00 53.21 ? 145 GLU   A OE2 1 
ATOM   1082 N  N   . GLU   A 1 140 ? 30.357 5.095   1.013  1.00 37.75 ? 146 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 140 ? 31.458 5.987   1.401  1.00 41.00 ? 146 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 140 ? 32.217 5.463   2.609  1.00 42.97 ? 146 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 140 ? 33.434 5.296   2.523  1.00 44.05 ? 146 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 140 ? 30.991 7.447   1.581  1.00 44.37 ? 146 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 140 ? 31.973 8.379   2.280  1.00 51.14 ? 146 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 140 ? 32.873 9.189   1.367  1.00 59.35 ? 146 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 140 ? 32.422 10.248  0.875  1.00 61.27 ? 146 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 140 ? 34.031 8.766   1.147  1.00 61.06 ? 146 GLU   A OE2 1 
ATOM   1091 N  N   . SER   B 1 1   ? 21.873 -21.292 7.602  1.00 18.73 ? 7   SER   C N   1 
ATOM   1092 C  CA  . SER   B 1 1   ? 20.719 -21.120 8.505  1.00 18.24 ? 7   SER   C CA  1 
ATOM   1093 C  C   . SER   B 1 1   ? 20.695 -22.211 9.592  1.00 18.10 ? 7   SER   C C   1 
ATOM   1094 O  O   . SER   B 1 1   ? 21.366 -23.247 9.453  1.00 19.18 ? 7   SER   C O   1 
ATOM   1095 C  CB  . SER   B 1 1   ? 19.428 -21.197 7.692  1.00 21.78 ? 7   SER   C CB  1 
ATOM   1096 O  OG  . SER   B 1 1   ? 19.280 -22.499 7.150  1.00 25.44 ? 7   SER   C OG  1 
ATOM   1097 N  N   . GLY   B 1 2   ? 19.920 -21.978 10.659 1.00 17.79 ? 8   GLY   C N   1 
ATOM   1098 C  CA  . GLY   B 1 2   ? 19.763 -22.970 11.718 1.00 16.85 ? 8   GLY   C CA  1 
ATOM   1099 C  C   . GLY   B 1 2   ? 19.474 -22.354 13.075 1.00 15.13 ? 8   GLY   C C   1 
ATOM   1100 O  O   . GLY   B 1 2   ? 19.859 -21.210 13.329 1.00 16.16 ? 8   GLY   C O   1 
ATOM   1101 N  N   . ALA   B 1 3   ? 18.784 -23.092 13.939 1.00 13.98 ? 9   ALA   C N   1 
ATOM   1102 C  CA  . ALA   B 1 3   ? 18.472 -22.605 15.282 1.00 14.75 ? 9   ALA   C CA  1 
ATOM   1103 C  C   . ALA   B 1 3   ? 18.605 -23.731 16.311 1.00 13.49 ? 9   ALA   C C   1 
ATOM   1104 O  O   . ALA   B 1 3   ? 18.646 -24.924 15.948 1.00 14.95 ? 9   ALA   C O   1 
ATOM   1105 C  CB  . ALA   B 1 3   ? 17.030 -22.049 15.295 1.00 17.33 ? 9   ALA   C CB  1 
ATOM   1106 N  N   . ILE   B 1 4   ? 18.629 -23.355 17.607 1.00 13.22 ? 10  ILE   C N   1 
ATOM   1107 C  CA  . ILE   B 1 4   ? 18.545 -24.274 18.734 1.00 13.70 ? 10  ILE   C CA  1 
ATOM   1108 C  C   . ILE   B 1 4   ? 17.142 -24.103 19.339 1.00 13.81 ? 10  ILE   C C   1 
ATOM   1109 O  O   . ILE   B 1 4   ? 16.700 -22.964 19.549 1.00 15.04 ? 10  ILE   C O   1 
ATOM   1110 C  CB  . ILE   B 1 4   ? 19.586 -23.970 19.819 1.00 13.93 ? 10  ILE   C CB  1 
ATOM   1111 C  CG1 . ILE   B 1 4   ? 21.012 -23.817 19.217 1.00 14.56 ? 10  ILE   C CG1 1 
ATOM   1112 C  CG2 . ILE   B 1 4   ? 19.497 -25.052 20.905 1.00 15.34 ? 10  ILE   C CG2 1 
ATOM   1113 C  CD1 . ILE   B 1 4   ? 21.997 -23.206 20.246 1.00 15.07 ? 10  ILE   C CD1 1 
ATOM   1114 N  N   . TYR   B 1 5   ? 16.439 -25.206 19.631 1.00 13.34 ? 11  TYR   C N   1 
ATOM   1115 C  CA  . TYR   B 1 5   ? 15.098 -25.141 20.214 1.00 14.14 ? 11  TYR   C CA  1 
ATOM   1116 C  C   . TYR   B 1 5   ? 15.150 -25.814 21.586 1.00 15.83 ? 11  TYR   C C   1 
ATOM   1117 O  O   . TYR   B 1 5   ? 15.215 -27.043 21.656 1.00 17.25 ? 11  TYR   C O   1 
ATOM   1118 C  CB  . TYR   B 1 5   ? 14.058 -25.837 19.286 1.00 14.97 ? 11  TYR   C CB  1 
ATOM   1119 C  CG  . TYR   B 1 5   ? 13.858 -25.089 17.982 1.00 15.62 ? 11  TYR   C CG  1 
ATOM   1120 C  CD1 . TYR   B 1 5   ? 13.034 -23.969 17.916 1.00 15.52 ? 11  TYR   C CD1 1 
ATOM   1121 C  CD2 . TYR   B 1 5   ? 14.578 -25.430 16.844 1.00 16.63 ? 11  TYR   C CD2 1 
ATOM   1122 C  CE1 . TYR   B 1 5   ? 12.891 -23.249 16.735 1.00 17.64 ? 11  TYR   C CE1 1 
ATOM   1123 C  CE2 . TYR   B 1 5   ? 14.427 -24.732 15.653 1.00 18.56 ? 11  TYR   C CE2 1 
ATOM   1124 C  CZ  . TYR   B 1 5   ? 13.613 -23.622 15.615 1.00 18.95 ? 11  TYR   C CZ  1 
ATOM   1125 O  OH  . TYR   B 1 5   ? 13.510 -22.902 14.447 1.00 20.60 ? 11  TYR   C OH  1 
ATOM   1126 N  N   . VAL   B 1 6   ? 15.199 -25.041 22.673 1.00 15.98 ? 12  VAL   C N   1 
ATOM   1127 C  CA  . VAL   B 1 6   ? 15.280 -25.574 24.029 1.00 16.86 ? 12  VAL   C CA  1 
ATOM   1128 C  C   . VAL   B 1 6   ? 14.135 -24.980 24.863 1.00 16.66 ? 12  VAL   C C   1 
ATOM   1129 O  O   . VAL   B 1 6   ? 13.949 -23.770 24.855 1.00 16.05 ? 12  VAL   C O   1 
ATOM   1130 C  CB  . VAL   B 1 6   ? 16.677 -25.301 24.645 1.00 17.11 ? 12  VAL   C CB  1 
ATOM   1131 C  CG1 . VAL   B 1 6   ? 17.047 -23.805 24.542 1.00 17.03 ? 12  VAL   C CG1 1 
ATOM   1132 C  CG2 . VAL   B 1 6   ? 16.711 -25.789 26.090 1.00 18.62 ? 12  VAL   C CG2 1 
ATOM   1133 N  N   . GLY   B 1 7   ? 13.332 -25.808 25.545 1.00 17.92 ? 13  GLY   C N   1 
ATOM   1134 C  CA  . GLY   B 1 7   ? 12.196 -25.277 26.300 1.00 18.07 ? 13  GLY   C CA  1 
ATOM   1135 C  C   . GLY   B 1 7   ? 11.247 -24.455 25.430 1.00 17.92 ? 13  GLY   C C   1 
ATOM   1136 O  O   . GLY   B 1 7   ? 10.979 -24.833 24.284 1.00 19.37 ? 13  GLY   C O   1 
ATOM   1137 N  N   . ASN   B 1 8   ? 10.916 -23.246 25.866 1.00 17.61 ? 14  ASN   C N   1 
ATOM   1138 C  CA  . ASN   B 1 8   ? 10.125 -22.335 25.031 1.00 18.18 ? 14  ASN   C CA  1 
ATOM   1139 C  C   . ASN   B 1 8   ? 11.002 -21.233 24.461 1.00 17.11 ? 14  ASN   C C   1 
ATOM   1140 O  O   . ASN   B 1 8   ? 10.552 -20.096 24.299 1.00 17.46 ? 14  ASN   C O   1 
ATOM   1141 C  CB  . ASN   B 1 8   ? 8.891  -21.768 25.765 1.00 19.95 ? 14  ASN   C CB  1 
ATOM   1142 C  CG  . ASN   B 1 8   ? 7.797  -22.808 25.897 1.00 26.59 ? 14  ASN   C CG  1 
ATOM   1143 O  OD1 . ASN   B 1 8   ? 6.934  -22.945 25.023 1.00 29.95 ? 14  ASN   C OD1 1 
ATOM   1144 N  ND2 . ASN   B 1 8   ? 7.867  -23.588 26.955 1.00 28.51 ? 14  ASN   C ND2 1 
ATOM   1145 N  N   . TYR   B 1 9   ? 12.225 -21.605 24.055 1.00 14.93 ? 15  TYR   C N   1 
ATOM   1146 C  CA  . TYR   B 1 9   ? 13.191 -20.651 23.485 1.00 15.50 ? 15  TYR   C CA  1 
ATOM   1147 C  C   . TYR   B 1 9   ? 13.679 -21.115 22.113 1.00 15.14 ? 15  TYR   C C   1 
ATOM   1148 O  O   . TYR   B 1 9   ? 13.870 -22.320 21.890 1.00 16.40 ? 15  TYR   C O   1 
ATOM   1149 C  CB  . TYR   B 1 9   ? 14.422 -20.496 24.406 1.00 16.03 ? 15  TYR   C CB  1 
ATOM   1150 C  CG  . TYR   B 1 9   ? 14.093 -19.965 25.800 1.00 17.62 ? 15  TYR   C CG  1 
ATOM   1151 C  CD1 . TYR   B 1 9   ? 13.549 -18.703 25.971 1.00 19.43 ? 15  TYR   C CD1 1 
ATOM   1152 C  CD2 . TYR   B 1 9   ? 14.404 -20.699 26.941 1.00 19.21 ? 15  TYR   C CD2 1 
ATOM   1153 C  CE1 . TYR   B 1 9   ? 13.235 -18.218 27.243 1.00 21.88 ? 15  TYR   C CE1 1 
ATOM   1154 C  CE2 . TYR   B 1 9   ? 14.137 -20.202 28.219 1.00 21.55 ? 15  TYR   C CE2 1 
ATOM   1155 C  CZ  . TYR   B 1 9   ? 13.588 -18.944 28.361 1.00 24.34 ? 15  TYR   C CZ  1 
ATOM   1156 O  OH  . TYR   B 1 9   ? 13.284 -18.435 29.613 1.00 29.66 ? 15  TYR   C OH  1 
ATOM   1157 N  N   . ARG   B 1 10  ? 13.917 -20.154 21.216 1.00 13.62 ? 16  ARG   C N   1 
ATOM   1158 C  CA  . ARG   B 1 10  ? 14.532 -20.372 19.898 1.00 13.07 ? 16  ARG   C CA  1 
ATOM   1159 C  C   . ARG   B 1 10  ? 15.808 -19.506 19.882 1.00 13.23 ? 16  ARG   C C   1 
ATOM   1160 O  O   . ARG   B 1 10  ? 15.731 -18.286 20.084 1.00 13.53 ? 16  ARG   C O   1 
ATOM   1161 C  CB  . ARG   B 1 10  ? 13.564 -19.921 18.759 1.00 14.75 ? 16  ARG   C CB  1 
ATOM   1162 C  CG  . ARG   B 1 10  ? 14.203 -19.775 17.370 1.00 15.56 ? 16  ARG   C CG  1 
ATOM   1163 C  CD  . ARG   B 1 10  ? 13.143 -19.496 16.304 1.00 16.30 ? 16  ARG   C CD  1 
ATOM   1164 N  NE  . ARG   B 1 10  ? 13.596 -18.540 15.284 1.00 17.07 ? 16  ARG   C NE  1 
ATOM   1165 C  CZ  . ARG   B 1 10  ? 14.095 -18.863 14.092 1.00 19.00 ? 16  ARG   C CZ  1 
ATOM   1166 N  NH1 . ARG   B 1 10  ? 14.313 -20.141 13.775 1.00 19.27 ? 16  ARG   C NH1 1 
ATOM   1167 N  NH2 . ARG   B 1 10  ? 14.451 -17.913 13.236 1.00 19.33 ? 16  ARG   C NH2 1 
ATOM   1168 N  N   . VAL   B 1 11  ? 16.986 -20.118 19.695 1.00 12.48 ? 17  VAL   C N   1 
ATOM   1169 C  CA  . VAL   B 1 11  ? 18.270 -19.391 19.655 1.00 12.08 ? 17  VAL   C CA  1 
ATOM   1170 C  C   . VAL   B 1 11  ? 18.750 -19.340 18.212 1.00 12.83 ? 17  VAL   C C   1 
ATOM   1171 O  O   . VAL   B 1 11  ? 18.923 -20.410 17.584 1.00 13.21 ? 17  VAL   C O   1 
ATOM   1172 C  CB  . VAL   B 1 11  ? 19.346 -20.110 20.517 1.00 13.52 ? 17  VAL   C CB  1 
ATOM   1173 C  CG1 . VAL   B 1 11  ? 20.597 -19.249 20.613 1.00 14.87 ? 17  VAL   C CG1 1 
ATOM   1174 C  CG2 . VAL   B 1 11  ? 18.800 -20.474 21.912 1.00 14.83 ? 17  VAL   C CG2 1 
ATOM   1175 N  N   . VAL   B 1 12  ? 18.985 -18.139 17.675 1.00 12.49 ? 18  VAL   C N   1 
ATOM   1176 C  CA  A VAL   B 1 12  ? 19.447 -17.970 16.292 0.50 11.94 ? 18  VAL   C CA  1 
ATOM   1177 C  CA  B VAL   B 1 12  ? 19.404 -17.984 16.289 0.50 13.46 ? 18  VAL   C CA  1 
ATOM   1178 C  C   . VAL   B 1 12  ? 20.576 -16.969 16.218 1.00 12.80 ? 18  VAL   C C   1 
ATOM   1179 O  O   . VAL   B 1 12  ? 20.835 -16.216 17.180 1.00 13.37 ? 18  VAL   C O   1 
ATOM   1180 C  CB  A VAL   B 1 12  ? 18.301 -17.482 15.344 0.50 12.07 ? 18  VAL   C CB  1 
ATOM   1181 C  CB  B VAL   B 1 12  ? 18.140 -17.456 15.512 0.50 16.53 ? 18  VAL   C CB  1 
ATOM   1182 C  CG1 A VAL   B 1 12  ? 17.323 -18.608 15.066 0.50 12.70 ? 18  VAL   C CG1 1 
ATOM   1183 C  CG1 B VAL   B 1 12  ? 18.393 -17.284 14.034 0.50 16.65 ? 18  VAL   C CG1 1 
ATOM   1184 C  CG2 A VAL   B 1 12  ? 17.634 -16.176 15.850 0.50 10.17 ? 18  VAL   C CG2 1 
ATOM   1185 C  CG2 B VAL   B 1 12  ? 16.943 -18.374 15.715 0.50 18.69 ? 18  VAL   C CG2 1 
ATOM   1186 N  N   . ASN   B 1 13  ? 21.268 -16.914 15.065 1.00 11.68 ? 19  ASN   C N   1 
ATOM   1187 C  CA  . ASN   B 1 13  ? 22.269 -15.875 14.840 1.00 11.27 ? 19  ASN   C CA  1 
ATOM   1188 C  C   . ASN   B 1 13  ? 21.460 -14.524 14.785 1.00 12.43 ? 19  ASN   C C   1 
ATOM   1189 O  O   . ASN   B 1 13  ? 20.443 -14.431 14.088 1.00 13.32 ? 19  ASN   C O   1 
ATOM   1190 C  CB  . ASN   B 1 13  ? 22.962 -16.027 13.476 1.00 12.22 ? 19  ASN   C CB  1 
ATOM   1191 C  CG  . ASN   B 1 13  ? 23.829 -17.286 13.411 1.00 12.58 ? 19  ASN   C CG  1 
ATOM   1192 O  OD1 . ASN   B 1 13  ? 23.370 -18.362 13.011 1.00 14.00 ? 19  ASN   C OD1 1 
ATOM   1193 N  ND2 . ASN   B 1 13  ? 25.068 -17.166 13.890 1.00 13.33 ? 19  ASN   C ND2 1 
ATOM   1194 N  N   . ARG   B 1 14  ? 21.959 -13.482 15.496 1.00 12.84 ? 20  ARG   C N   1 
ATOM   1195 C  CA  . ARG   B 1 14  ? 21.213 -12.204 15.531 1.00 12.30 ? 20  ARG   C CA  1 
ATOM   1196 C  C   . ARG   B 1 14  ? 21.065 -11.649 14.100 1.00 13.70 ? 20  ARG   C C   1 
ATOM   1197 O  O   . ARG   B 1 14  ? 20.013 -11.087 13.751 1.00 14.36 ? 20  ARG   C O   1 
ATOM   1198 C  CB  . ARG   B 1 14  ? 21.961 -11.202 16.406 1.00 12.26 ? 20  ARG   C CB  1 
ATOM   1199 C  CG  . ARG   B 1 14  ? 21.170 -9.873  16.611 1.00 13.20 ? 20  ARG   C CG  1 
ATOM   1200 C  CD  . ARG   B 1 14  ? 22.041 -8.903  17.398 1.00 14.59 ? 20  ARG   C CD  1 
ATOM   1201 N  NE  . ARG   B 1 14  ? 21.373 -7.664  17.834 1.00 15.38 ? 20  ARG   C NE  1 
ATOM   1202 C  CZ  . ARG   B 1 14  ? 21.299 -6.557  17.106 1.00 15.16 ? 20  ARG   C CZ  1 
ATOM   1203 N  NH1 . ARG   B 1 14  ? 21.642 -6.572  15.820 1.00 15.92 ? 20  ARG   C NH1 1 
ATOM   1204 N  NH2 . ARG   B 1 14  ? 20.784 -5.447  17.625 1.00 15.92 ? 20  ARG   C NH2 1 
ATOM   1205 N  N   . HIS   B 1 15  ? 22.096 -11.866 13.241 1.00 13.20 ? 21  HIS   C N   1 
ATOM   1206 C  CA  . HIS   B 1 15  ? 22.029 -11.317 11.874 1.00 14.05 ? 21  HIS   C CA  1 
ATOM   1207 C  C   . HIS   B 1 15  ? 21.005 -12.034 10.971 1.00 14.99 ? 21  HIS   C C   1 
ATOM   1208 O  O   . HIS   B 1 15  ? 20.702 -11.531 9.890  1.00 17.22 ? 21  HIS   C O   1 
ATOM   1209 C  CB  . HIS   B 1 15  ? 23.432 -11.234 11.197 1.00 13.78 ? 21  HIS   C CB  1 
ATOM   1210 C  CG  . HIS   B 1 15  ? 24.020 -12.553 10.762 1.00 14.39 ? 21  HIS   C CG  1 
ATOM   1211 N  ND1 . HIS   B 1 15  ? 24.744 -13.366 11.635 1.00 15.44 ? 21  HIS   C ND1 1 
ATOM   1212 C  CD2 . HIS   B 1 15  ? 24.024 -13.116 9.527  1.00 14.96 ? 21  HIS   C CD2 1 
ATOM   1213 C  CE1 . HIS   B 1 15  ? 25.143 -14.407 10.907 1.00 15.98 ? 21  HIS   C CE1 1 
ATOM   1214 N  NE2 . HIS   B 1 15  ? 24.729 -14.298 9.632  1.00 15.46 ? 21  HIS   C NE2 1 
ATOM   1215 N  N   . LEU   B 1 16  ? 20.493 -13.203 11.406 1.00 14.23 ? 22  LEU   C N   1 
ATOM   1216 C  CA  . LEU   B 1 16  ? 19.477 -13.950 10.646 1.00 14.60 ? 22  LEU   C CA  1 
ATOM   1217 C  C   . LEU   B 1 16  ? 18.089 -13.907 11.321 1.00 15.42 ? 22  LEU   C C   1 
ATOM   1218 O  O   . LEU   B 1 16  ? 17.174 -14.632 10.887 1.00 16.65 ? 22  LEU   C O   1 
ATOM   1219 C  CB  . LEU   B 1 16  ? 19.938 -15.391 10.446 1.00 14.61 ? 22  LEU   C CB  1 
ATOM   1220 C  CG  . LEU   B 1 16  ? 21.224 -15.544 9.652  1.00 14.97 ? 22  LEU   C CG  1 
ATOM   1221 C  CD1 . LEU   B 1 16  ? 21.633 -17.010 9.608  1.00 14.95 ? 22  LEU   C CD1 1 
ATOM   1222 C  CD2 . LEU   B 1 16  ? 21.108 -14.924 8.245  1.00 15.56 ? 22  LEU   C CD2 1 
ATOM   1223 N  N   . ALA   B 1 17  ? 17.936 -13.149 12.432 1.00 15.43 ? 23  ALA   C N   1 
ATOM   1224 C  CA  . ALA   B 1 17  ? 16.655 -13.078 13.138 1.00 15.74 ? 23  ALA   C CA  1 
ATOM   1225 C  C   . ALA   B 1 17  ? 15.541 -12.521 12.252 1.00 17.57 ? 23  ALA   C C   1 
ATOM   1226 O  O   . ALA   B 1 17  ? 15.780 -11.602 11.451 1.00 18.44 ? 23  ALA   C O   1 
ATOM   1227 C  CB  . ALA   B 1 17  ? 16.796 -12.234 14.406 1.00 16.98 ? 23  ALA   C CB  1 
ATOM   1228 N  N   . THR   B 1 18  ? 14.341 -13.106 12.388 1.00 16.88 ? 24  THR   C N   1 
ATOM   1229 C  CA  . THR   B 1 18  ? 13.178 -12.688 11.603 1.00 17.60 ? 24  THR   C CA  1 
ATOM   1230 C  C   . THR   B 1 18  ? 12.362 -11.609 12.366 1.00 17.77 ? 24  THR   C C   1 
ATOM   1231 O  O   . THR   B 1 18  ? 12.603 -11.340 13.544 1.00 18.19 ? 24  THR   C O   1 
ATOM   1232 C  CB  . THR   B 1 18  ? 12.251 -13.934 11.363 1.00 18.80 ? 24  THR   C CB  1 
ATOM   1233 O  OG1 . THR   B 1 18  ? 11.728 -14.362 12.613 1.00 19.17 ? 24  THR   C OG1 1 
ATOM   1234 C  CG2 . THR   B 1 18  ? 12.958 -15.094 10.636 1.00 19.71 ? 24  THR   C CG2 1 
ATOM   1235 N  N   . HIS   B 1 19  ? 11.324 -11.020 11.700 1.00 18.74 ? 25  HIS   C N   1 
ATOM   1236 C  CA  . HIS   B 1 19  ? 10.416 -10.101 12.387 1.00 19.50 ? 25  HIS   C CA  1 
ATOM   1237 C  C   . HIS   B 1 19  ? 9.713  -10.840 13.530 1.00 18.14 ? 25  HIS   C C   1 
ATOM   1238 O  O   . HIS   B 1 19  ? 9.638  -10.281 14.618 1.00 19.14 ? 25  HIS   C O   1 
ATOM   1239 C  CB  . HIS   B 1 19  ? 9.334  -9.571  11.422 1.00 21.42 ? 25  HIS   C CB  1 
ATOM   1240 C  CG  . HIS   B 1 19  ? 8.201  -8.859  12.121 1.00 24.55 ? 25  HIS   C CG  1 
ATOM   1241 N  ND1 . HIS   B 1 19  ? 8.356  -7.582  12.630 1.00 27.65 ? 25  HIS   C ND1 1 
ATOM   1242 C  CD2 . HIS   B 1 19  ? 6.981  -9.320  12.478 1.00 26.43 ? 25  HIS   C CD2 1 
ATOM   1243 C  CE1 . HIS   B 1 19  ? 7.194  -7.268  13.183 1.00 27.75 ? 25  HIS   C CE1 1 
ATOM   1244 N  NE2 . HIS   B 1 19  ? 6.340  -8.290  13.138 1.00 27.59 ? 25  HIS   C NE2 1 
ATOM   1245 N  N   . ASN   B 1 20  ? 9.299  -12.108 13.328 1.00 18.27 ? 26  ASN   C N   1 
ATOM   1246 C  CA  . ASN   B 1 20  ? 8.653  -12.851 14.413 1.00 18.91 ? 26  ASN   C CA  1 
ATOM   1247 C  C   . ASN   B 1 20  ? 9.596  -13.003 15.602 1.00 17.05 ? 26  ASN   C C   1 
ATOM   1248 O  O   . ASN   B 1 20  ? 9.170  -12.889 16.750 1.00 16.99 ? 26  ASN   C O   1 
ATOM   1249 C  CB  . ASN   B 1 20  ? 8.129  -14.220 13.965 1.00 20.37 ? 26  ASN   C CB  1 
ATOM   1250 C  CG  . ASN   B 1 20  ? 7.326  -14.902 15.074 1.00 26.33 ? 26  ASN   C CG  1 
ATOM   1251 O  OD1 . ASN   B 1 20  ? 6.208  -14.480 15.410 1.00 29.69 ? 26  ASN   C OD1 1 
ATOM   1252 N  ND2 . ASN   B 1 20  ? 7.909  -15.917 15.720 1.00 27.43 ? 26  ASN   C ND2 1 
ATOM   1253 N  N   . ASP   B 1 21  ? 10.919 -13.215 15.332 1.00 15.88 ? 27  ASP   C N   1 
ATOM   1254 C  CA  . ASP   B 1 21  ? 11.867 -13.293 16.442 1.00 15.56 ? 27  ASP   C CA  1 
ATOM   1255 C  C   . ASP   B 1 21  ? 11.915 -11.975 17.247 1.00 15.93 ? 27  ASP   C C   1 
ATOM   1256 O  O   . ASP   B 1 21  ? 11.849 -11.999 18.477 1.00 16.99 ? 27  ASP   C O   1 
ATOM   1257 C  CB  . ASP   B 1 21  ? 13.282 -13.608 15.937 1.00 15.46 ? 27  ASP   C CB  1 
ATOM   1258 C  CG  . ASP   B 1 21  ? 13.489 -15.036 15.469 1.00 16.07 ? 27  ASP   C CG  1 
ATOM   1259 O  OD1 . ASP   B 1 21  ? 12.890 -15.950 16.072 1.00 17.34 ? 27  ASP   C OD1 1 
ATOM   1260 O  OD2 . ASP   B 1 21  ? 14.193 -15.230 14.442 1.00 16.28 ? 27  ASP   C OD2 1 
ATOM   1261 N  N   . TRP   B 1 22  ? 12.007 -10.819 16.554 1.00 16.82 ? 28  TRP   C N   1 
ATOM   1262 C  CA  . TRP   B 1 22  ? 12.056 -9.530  17.235 1.00 16.78 ? 28  TRP   C CA  1 
ATOM   1263 C  C   . TRP   B 1 22  ? 10.726 -9.202  17.953 1.00 16.47 ? 28  TRP   C C   1 
ATOM   1264 O  O   . TRP   B 1 22  ? 10.739 -8.563  19.020 1.00 16.75 ? 28  TRP   C O   1 
ATOM   1265 C  CB  . TRP   B 1 22  ? 12.419 -8.429  16.239 1.00 17.00 ? 28  TRP   C CB  1 
ATOM   1266 C  CG  . TRP   B 1 22  ? 13.902 -8.397  15.953 1.00 17.27 ? 28  TRP   C CG  1 
ATOM   1267 C  CD1 . TRP   B 1 22  ? 14.542 -8.880  14.846 1.00 18.43 ? 28  TRP   C CD1 1 
ATOM   1268 C  CD2 . TRP   B 1 22  ? 14.918 -7.828  16.789 1.00 16.72 ? 28  TRP   C CD2 1 
ATOM   1269 N  NE1 . TRP   B 1 22  ? 15.896 -8.616  14.927 1.00 18.63 ? 28  TRP   C NE1 1 
ATOM   1270 C  CE2 . TRP   B 1 22  ? 16.155 -7.995  16.119 1.00 17.87 ? 28  TRP   C CE2 1 
ATOM   1271 C  CE3 . TRP   B 1 22  ? 14.900 -7.156  18.017 1.00 18.75 ? 28  TRP   C CE3 1 
ATOM   1272 C  CZ2 . TRP   B 1 22  ? 17.339 -7.474  16.606 1.00 18.05 ? 28  TRP   C CZ2 1 
ATOM   1273 C  CZ3 . TRP   B 1 22  ? 16.109 -6.694  18.525 1.00 18.99 ? 28  TRP   C CZ3 1 
ATOM   1274 C  CH2 . TRP   B 1 22  ? 17.303 -6.841  17.806 1.00 18.31 ? 28  TRP   C CH2 1 
ATOM   1275 N  N   . ALA   B 1 23  ? 9.612  -9.655  17.390 1.00 16.75 ? 29  ALA   C N   1 
ATOM   1276 C  CA  . ALA   B 1 23  ? 8.270  -9.435  17.983 1.00 17.22 ? 29  ALA   C CA  1 
ATOM   1277 C  C   . ALA   B 1 23  ? 8.026  -10.332 19.217 1.00 18.63 ? 29  ALA   C C   1 
ATOM   1278 O  O   . ALA   B 1 23  ? 7.067  -10.122 19.958 1.00 19.26 ? 29  ALA   C O   1 
ATOM   1279 C  CB  . ALA   B 1 23  ? 7.180  -9.679  16.942 1.00 17.82 ? 29  ALA   C CB  1 
ATOM   1280 N  N   . ASN   B 1 24  ? 8.875  -11.352 19.429 1.00 18.07 ? 30  ASN   C N   1 
ATOM   1281 C  CA  . ASN   B 1 24  ? 8.769  -12.255 20.586 1.00 18.11 ? 30  ASN   C CA  1 
ATOM   1282 C  C   . ASN   B 1 24  ? 10.139 -12.337 21.287 1.00 17.89 ? 30  ASN   C C   1 
ATOM   1283 O  O   . ASN   B 1 24  ? 10.562 -13.400 21.731 1.00 17.16 ? 30  ASN   C O   1 
ATOM   1284 C  CB  . ASN   B 1 24  ? 8.292  -13.642 20.099 1.00 19.29 ? 30  ASN   C CB  1 
ATOM   1285 C  CG  . ASN   B 1 24  ? 6.873  -13.575 19.613 1.00 20.25 ? 30  ASN   C CG  1 
ATOM   1286 O  OD1 . ASN   B 1 24  ? 5.926  -13.575 20.430 1.00 22.12 ? 30  ASN   C OD1 1 
ATOM   1287 N  ND2 . ASN   B 1 24  ? 6.689  -13.477 18.297 1.00 20.78 ? 30  ASN   C ND2 1 
ATOM   1288 N  N   . LEU   B 1 25  ? 10.840 -11.222 21.372 1.00 17.47 ? 31  LEU   C N   1 
ATOM   1289 C  CA  . LEU   B 1 25  ? 12.213 -11.180 21.880 1.00 16.95 ? 31  LEU   C CA  1 
ATOM   1290 C  C   . LEU   B 1 25  ? 12.356 -11.477 23.354 1.00 18.45 ? 31  LEU   C C   1 
ATOM   1291 O  O   . LEU   B 1 25  ? 11.581 -10.978 24.173 1.00 19.67 ? 31  LEU   C O   1 
ATOM   1292 C  CB  . LEU   B 1 25  ? 12.780 -9.780  21.593 1.00 17.47 ? 31  LEU   C CB  1 
ATOM   1293 C  CG  . LEU   B 1 25  ? 14.259 -9.612  21.953 1.00 18.04 ? 31  LEU   C CG  1 
ATOM   1294 C  CD1 . LEU   B 1 25  ? 15.161 -10.497 21.075 1.00 17.71 ? 31  LEU   C CD1 1 
ATOM   1295 C  CD2 . LEU   B 1 25  ? 14.681 -8.153  21.850 1.00 19.51 ? 31  LEU   C CD2 1 
ATOM   1296 N  N   . VAL   B 1 26  ? 13.333 -12.312 23.686 1.00 17.38 ? 32  VAL   C N   1 
ATOM   1297 C  CA  . VAL   B 1 26  ? 13.692 -12.604 25.075 1.00 17.93 ? 32  VAL   C CA  1 
ATOM   1298 C  C   . VAL   B 1 26  ? 15.016 -11.885 25.398 1.00 18.77 ? 32  VAL   C C   1 
ATOM   1299 O  O   . VAL   B 1 26  ? 15.132 -11.182 26.419 1.00 20.58 ? 32  VAL   C O   1 
ATOM   1300 C  CB  . VAL   B 1 26  ? 13.831 -14.125 25.306 1.00 18.14 ? 32  VAL   C CB  1 
ATOM   1301 C  CG1 . VAL   B 1 26  ? 14.362 -14.414 26.714 1.00 19.28 ? 32  VAL   C CG1 1 
ATOM   1302 C  CG2 . VAL   B 1 26  ? 12.486 -14.820 25.093 1.00 18.37 ? 32  VAL   C CG2 1 
ATOM   1303 N  N   . TRP   B 1 27  ? 16.035 -12.043 24.526 1.00 16.84 ? 33  TRP   C N   1 
ATOM   1304 C  CA  . TRP   B 1 27  ? 17.358 -11.466 24.772 1.00 16.61 ? 33  TRP   C CA  1 
ATOM   1305 C  C   . TRP   B 1 27  ? 18.153 -11.418 23.477 1.00 16.46 ? 33  TRP   C C   1 
ATOM   1306 O  O   . TRP   B 1 27  ? 17.968 -12.290 22.609 1.00 16.00 ? 33  TRP   C O   1 
ATOM   1307 C  CB  . TRP   B 1 27  ? 18.086 -12.332 25.831 1.00 17.32 ? 33  TRP   C CB  1 
ATOM   1308 C  CG  . TRP   B 1 27  ? 19.565 -12.072 26.009 1.00 17.60 ? 33  TRP   C CG  1 
ATOM   1309 C  CD1 . TRP   B 1 27  ? 20.144 -11.152 26.838 1.00 19.40 ? 33  TRP   C CD1 1 
ATOM   1310 C  CD2 . TRP   B 1 27  ? 20.648 -12.795 25.391 1.00 17.22 ? 33  TRP   C CD2 1 
ATOM   1311 N  NE1 . TRP   B 1 27  ? 21.526 -11.262 26.782 1.00 20.65 ? 33  TRP   C NE1 1 
ATOM   1312 C  CE2 . TRP   B 1 27  ? 21.857 -12.254 25.892 1.00 18.56 ? 33  TRP   C CE2 1 
ATOM   1313 C  CE3 . TRP   B 1 27  ? 20.715 -13.823 24.433 1.00 17.03 ? 33  TRP   C CE3 1 
ATOM   1314 C  CZ2 . TRP   B 1 27  ? 23.112 -12.742 25.507 1.00 18.69 ? 33  TRP   C CZ2 1 
ATOM   1315 C  CZ3 . TRP   B 1 27  ? 21.961 -14.303 24.060 1.00 18.25 ? 33  TRP   C CZ3 1 
ATOM   1316 C  CH2 . TRP   B 1 27  ? 23.132 -13.735 24.565 1.00 18.41 ? 33  TRP   C CH2 1 
ATOM   1317 N  N   . GLU   B 1 28  ? 18.992 -10.394 23.321 1.00 15.11 ? 34  GLU   C N   1 
ATOM   1318 C  CA  . GLU   B 1 28  ? 19.856 -10.317 22.152 1.00 15.74 ? 34  GLU   C CA  1 
ATOM   1319 C  C   . GLU   B 1 28  ? 21.160 -9.630  22.504 1.00 16.09 ? 34  GLU   C C   1 
ATOM   1320 O  O   . GLU   B 1 28  ? 21.189 -8.745  23.396 1.00 17.15 ? 34  GLU   C O   1 
ATOM   1321 C  CB  . GLU   B 1 28  ? 19.169 -9.618  20.977 1.00 15.95 ? 34  GLU   C CB  1 
ATOM   1322 C  CG  . GLU   B 1 28  ? 18.611 -8.241  21.257 1.00 16.94 ? 34  GLU   C CG  1 
ATOM   1323 C  CD  . GLU   B 1 28  ? 19.585 -7.079  21.195 1.00 20.02 ? 34  GLU   C CD  1 
ATOM   1324 O  OE1 . GLU   B 1 28  ? 19.320 -6.057  21.866 1.00 22.78 ? 34  GLU   C OE1 1 
ATOM   1325 O  OE2 . GLU   B 1 28  ? 20.597 -7.165  20.454 1.00 18.27 ? 34  GLU   C OE2 1 
ATOM   1326 N  N   . ASP   B 1 29  ? 22.246 -9.996  21.801 1.00 14.51 ? 35  ASP   C N   1 
ATOM   1327 C  CA  . ASP   B 1 29  ? 23.536 -9.361  22.042 1.00 14.65 ? 35  ASP   C CA  1 
ATOM   1328 C  C   . ASP   B 1 29  ? 24.312 -9.321  20.713 1.00 15.16 ? 35  ASP   C C   1 
ATOM   1329 O  O   . ASP   B 1 29  ? 24.749 -10.368 20.223 1.00 15.29 ? 35  ASP   C O   1 
ATOM   1330 C  CB  . ASP   B 1 29  ? 24.275 -10.134 23.146 1.00 15.81 ? 35  ASP   C CB  1 
ATOM   1331 C  CG  . ASP   B 1 29  ? 25.608 -9.567  23.545 1.00 20.60 ? 35  ASP   C CG  1 
ATOM   1332 O  OD1 . ASP   B 1 29  ? 26.345 -9.104  22.658 1.00 21.13 ? 35  ASP   C OD1 1 
ATOM   1333 O  OD2 . ASP   B 1 29  ? 25.971 -9.693  24.731 1.00 23.86 ? 35  ASP   C OD2 1 
ATOM   1334 N  N   . SER   B 1 30  ? 24.464 -8.125  20.134 1.00 14.79 ? 36  SER   C N   1 
ATOM   1335 C  CA  A SER   B 1 30  ? 25.162 -7.950  18.864 0.50 14.59 ? 36  SER   C CA  1 
ATOM   1336 C  CA  B SER   B 1 30  ? 25.143 -8.009  18.853 0.50 15.03 ? 36  SER   C CA  1 
ATOM   1337 C  C   . SER   B 1 30  ? 26.625 -8.405  18.954 1.00 15.35 ? 36  SER   C C   1 
ATOM   1338 O  O   . SER   B 1 30  ? 27.147 -8.996  17.994 1.00 14.61 ? 36  SER   C O   1 
ATOM   1339 C  CB  A SER   B 1 30  ? 25.095 -6.491  18.410 0.50 15.58 ? 36  SER   C CB  1 
ATOM   1340 C  CB  B SER   B 1 30  ? 24.967 -6.613  18.273 0.50 17.27 ? 36  SER   C CB  1 
ATOM   1341 O  OG  A SER   B 1 30  ? 26.018 -6.225  17.359 0.50 15.82 ? 36  SER   C OG  1 
ATOM   1342 O  OG  B SER   B 1 30  ? 25.515 -5.667  19.170 0.50 19.47 ? 36  SER   C OG  1 
ATOM   1343 N  N   . SER   B 1 31  ? 27.300 -8.111  20.098 1.00 15.25 ? 37  SER   C N   1 
ATOM   1344 C  CA  . SER   B 1 31  ? 28.711 -8.503  20.206 1.00 15.93 ? 37  SER   C CA  1 
ATOM   1345 C  C   . SER   B 1 31  ? 28.907 -10.024 20.162 1.00 14.33 ? 37  SER   C C   1 
ATOM   1346 O  O   . SER   B 1 31  ? 30.009 -10.470 19.808 1.00 15.78 ? 37  SER   C O   1 
ATOM   1347 C  CB  . SER   B 1 31  ? 29.335 -7.948  21.476 1.00 19.39 ? 37  SER   C CB  1 
ATOM   1348 O  OG  . SER   B 1 31  ? 28.929 -8.640  22.642 1.00 23.97 ? 37  SER   C OG  1 
ATOM   1349 N  N   . ARG   B 1 32  ? 27.861 -10.823 20.484 1.00 13.89 ? 38  ARG   C N   1 
ATOM   1350 C  CA  . ARG   B 1 32  ? 27.940 -12.296 20.435 1.00 13.91 ? 38  ARG   C CA  1 
ATOM   1351 C  C   . ARG   B 1 32  ? 27.294 -12.873 19.157 1.00 13.56 ? 38  ARG   C C   1 
ATOM   1352 O  O   . ARG   B 1 32  ? 27.323 -14.090 18.967 1.00 12.99 ? 38  ARG   C O   1 
ATOM   1353 C  CB  . ARG   B 1 32  ? 27.194 -12.876 21.656 1.00 15.88 ? 38  ARG   C CB  1 
ATOM   1354 C  CG  . ARG   B 1 32  ? 27.886 -12.547 22.971 1.00 17.34 ? 38  ARG   C CG  1 
ATOM   1355 C  CD  . ARG   B 1 32  ? 27.118 -13.097 24.175 1.00 15.23 ? 38  ARG   C CD  1 
ATOM   1356 N  NE  . ARG   B 1 32  ? 27.165 -14.574 24.213 1.00 14.80 ? 38  ARG   C NE  1 
ATOM   1357 C  CZ  . ARG   B 1 32  ? 27.132 -15.309 25.323 1.00 15.66 ? 38  ARG   C CZ  1 
ATOM   1358 N  NH1 . ARG   B 1 32  ? 27.018 -14.731 26.512 1.00 16.42 ? 38  ARG   C NH1 1 
ATOM   1359 N  NH2 . ARG   B 1 32  ? 27.284 -16.637 25.255 1.00 15.35 ? 38  ARG   C NH2 1 
ATOM   1360 N  N   . ASP   B 1 33  ? 26.613 -12.037 18.331 1.00 12.60 ? 39  ASP   C N   1 
ATOM   1361 C  CA  . ASP   B 1 33  ? 25.821 -12.508 17.201 1.00 12.74 ? 39  ASP   C CA  1 
ATOM   1362 C  C   . ASP   B 1 33  ? 24.723 -13.466 17.630 1.00 12.94 ? 39  ASP   C C   1 
ATOM   1363 O  O   . ASP   B 1 33  ? 24.423 -14.389 16.876 1.00 12.76 ? 39  ASP   C O   1 
ATOM   1364 C  CB  . ASP   B 1 33  ? 26.679 -13.089 16.067 1.00 12.37 ? 39  ASP   C CB  1 
ATOM   1365 C  CG  . ASP   B 1 33  ? 25.891 -13.431 14.799 1.00 13.98 ? 39  ASP   C CG  1 
ATOM   1366 O  OD1 . ASP   B 1 33  ? 24.999 -12.646 14.425 1.00 14.72 ? 39  ASP   C OD1 1 
ATOM   1367 O  OD2 . ASP   B 1 33  ? 26.193 -14.463 14.172 1.00 13.73 ? 39  ASP   C OD2 1 
ATOM   1368 N  N   . LEU   B 1 34  ? 24.069 -13.234 18.800 1.00 11.82 ? 40  LEU   C N   1 
ATOM   1369 C  CA  . LEU   B 1 34  ? 22.990 -14.130 19.250 1.00 12.20 ? 40  LEU   C CA  1 
ATOM   1370 C  C   . LEU   B 1 34  ? 21.689 -13.379 19.504 1.00 12.94 ? 40  LEU   C C   1 
ATOM   1371 O  O   . LEU   B 1 34  ? 21.708 -12.224 19.961 1.00 13.84 ? 40  LEU   C O   1 
ATOM   1372 C  CB  . LEU   B 1 34  ? 23.381 -14.832 20.566 1.00 12.57 ? 40  LEU   C CB  1 
ATOM   1373 C  CG  . LEU   B 1 34  ? 24.456 -15.945 20.476 1.00 13.41 ? 40  LEU   C CG  1 
ATOM   1374 C  CD1 . LEU   B 1 34  ? 24.725 -16.528 21.885 1.00 14.46 ? 40  LEU   C CD1 1 
ATOM   1375 C  CD2 . LEU   B 1 34  ? 24.020 -17.069 19.521 1.00 14.53 ? 40  LEU   C CD2 1 
ATOM   1376 N  N   . LEU   B 1 35  ? 20.577 -14.074 19.278 1.00 11.91 ? 41  LEU   C N   1 
ATOM   1377 C  CA  . LEU   B 1 35  ? 19.255 -13.549 19.624 1.00 12.48 ? 41  LEU   C CA  1 
ATOM   1378 C  C   . LEU   B 1 35  ? 18.417 -14.768 20.034 1.00 13.42 ? 41  LEU   C C   1 
ATOM   1379 O  O   . LEU   B 1 35  ? 18.528 -15.841 19.441 1.00 14.15 ? 41  LEU   C O   1 
ATOM   1380 C  CB  . LEU   B 1 35  ? 18.606 -12.821 18.403 1.00 12.52 ? 41  LEU   C CB  1 
ATOM   1381 C  CG  . LEU   B 1 35  ? 17.212 -12.229 18.673 1.00 13.46 ? 41  LEU   C CG  1 
ATOM   1382 C  CD1 . LEU   B 1 35  ? 17.015 -10.918 17.924 1.00 16.10 ? 41  LEU   C CD1 1 
ATOM   1383 C  CD2 . LEU   B 1 35  ? 16.111 -13.251 18.326 1.00 14.17 ? 41  LEU   C CD2 1 
ATOM   1384 N  N   . VAL   B 1 36  ? 17.621 -14.599 21.093 1.00 13.31 ? 42  VAL   C N   1 
ATOM   1385 C  CA  . VAL   B 1 36  ? 16.708 -15.616 21.612 1.00 13.47 ? 42  VAL   C CA  1 
ATOM   1386 C  C   . VAL   B 1 36  ? 15.289 -15.079 21.623 1.00 14.44 ? 42  VAL   C C   1 
ATOM   1387 O  O   . VAL   B 1 36  ? 15.074 -13.935 22.074 1.00 15.33 ? 42  VAL   C O   1 
ATOM   1388 C  CB  . VAL   B 1 36  ? 17.115 -16.058 23.035 1.00 14.50 ? 42  VAL   C CB  1 
ATOM   1389 C  CG1 . VAL   B 1 36  ? 16.143 -17.118 23.574 1.00 15.78 ? 42  VAL   C CG1 1 
ATOM   1390 C  CG2 . VAL   B 1 36  ? 18.550 -16.618 23.019 1.00 15.16 ? 42  VAL   C CG2 1 
ATOM   1391 N  N   . SER   B 1 37  ? 14.367 -15.826 21.031 1.00 13.95 ? 43  SER   C N   1 
ATOM   1392 C  CA  . SER   B 1 37  ? 12.952 -15.473 21.015 1.00 14.10 ? 43  SER   C CA  1 
ATOM   1393 C  C   . SER   B 1 37  ? 12.147 -16.580 21.702 1.00 15.43 ? 43  SER   C C   1 
ATOM   1394 O  O   . SER   B 1 37  ? 12.635 -17.701 21.945 1.00 15.63 ? 43  SER   C O   1 
ATOM   1395 C  CB  . SER   B 1 37  ? 12.470 -15.285 19.574 1.00 15.43 ? 43  SER   C CB  1 
ATOM   1396 O  OG  . SER   B 1 37  ? 12.645 -16.456 18.782 1.00 17.08 ? 43  SER   C OG  1 
ATOM   1397 N  N   . SER   B 1 38  ? 10.901 -16.256 22.076 1.00 15.86 ? 44  SER   C N   1 
ATOM   1398 C  CA  . SER   B 1 38  ? 10.016 -17.226 22.718 1.00 16.93 ? 44  SER   C CA  1 
ATOM   1399 C  C   . SER   B 1 38  ? 9.203  -18.015 21.679 1.00 19.13 ? 44  SER   C C   1 
ATOM   1400 O  O   . SER   B 1 38  ? 8.892  -17.504 20.601 1.00 19.75 ? 44  SER   C O   1 
ATOM   1401 C  CB  . SER   B 1 38  ? 9.099  -16.535 23.727 1.00 19.41 ? 44  SER   C CB  1 
ATOM   1402 O  OG  . SER   B 1 38  ? 8.293  -15.581 23.060 1.00 23.17 ? 44  SER   C OG  1 
ATOM   1403 N  N   . THR   B 1 39  ? 8.857  -19.264 22.009 1.00 19.04 ? 45  THR   C N   1 
ATOM   1404 C  CA  . THR   B 1 39  ? 8.109  -20.156 21.122 1.00 19.91 ? 45  THR   C CA  1 
ATOM   1405 C  C   . THR   B 1 39  ? 6.812  -20.631 21.824 1.00 22.48 ? 45  THR   C C   1 
ATOM   1406 O  O   . THR   B 1 39  ? 6.759  -20.713 23.044 1.00 21.46 ? 45  THR   C O   1 
ATOM   1407 C  CB  . THR   B 1 39  ? 8.954  -21.411 20.770 1.00 20.65 ? 45  THR   C CB  1 
ATOM   1408 O  OG1 . THR   B 1 39  ? 9.198  -22.150 21.962 1.00 21.51 ? 45  THR   C OG1 1 
ATOM   1409 C  CG2 . THR   B 1 39  ? 10.324 -21.058 20.122 1.00 20.06 ? 45  THR   C CG2 1 
ATOM   1410 N  N   . THR   B 1 40  ? 5.814  -21.000 21.033 1.00 24.58 ? 46  THR   C N   1 
ATOM   1411 C  CA  . THR   B 1 40  ? 4.569  -21.544 21.591 1.00 26.45 ? 46  THR   C CA  1 
ATOM   1412 C  C   . THR   B 1 40  ? 4.781  -23.024 21.947 1.00 26.99 ? 46  THR   C C   1 
ATOM   1413 O  O   . THR   B 1 40  ? 4.381  -23.472 23.029 1.00 28.60 ? 46  THR   C O   1 
ATOM   1414 C  CB  . THR   B 1 40  ? 3.402  -21.303 20.628 1.00 30.55 ? 46  THR   C CB  1 
ATOM   1415 O  OG1 . THR   B 1 40  ? 3.715  -21.931 19.388 1.00 34.80 ? 46  THR   C OG1 1 
ATOM   1416 C  CG2 . THR   B 1 40  ? 3.169  -19.834 20.373 1.00 29.69 ? 46  THR   C CG2 1 
ATOM   1417 N  N   . ALA   B 1 41  ? 5.445  -23.773 21.045 1.00 25.61 ? 47  ALA   C N   1 
ATOM   1418 C  CA  . ALA   B 1 41  ? 5.712  -25.187 21.284 1.00 25.68 ? 47  ALA   C CA  1 
ATOM   1419 C  C   . ALA   B 1 41  ? 7.033  -25.413 22.026 1.00 23.73 ? 47  ALA   C C   1 
ATOM   1420 O  O   . ALA   B 1 41  ? 7.957  -24.620 21.885 1.00 22.62 ? 47  ALA   C O   1 
ATOM   1421 C  CB  . ALA   B 1 41  ? 5.745  -25.935 19.956 1.00 27.04 ? 47  ALA   C CB  1 
ATOM   1422 N  N   . GLN   B 1 42  ? 7.141  -26.496 22.788 1.00 23.57 ? 48  GLN   C N   1 
ATOM   1423 C  CA  . GLN   B 1 42  ? 8.370  -26.844 23.487 1.00 24.10 ? 48  GLN   C CA  1 
ATOM   1424 C  C   . GLN   B 1 42  ? 9.356  -27.508 22.525 1.00 23.58 ? 48  GLN   C C   1 
ATOM   1425 O  O   . GLN   B 1 42  ? 8.967  -28.331 21.697 1.00 24.91 ? 48  GLN   C O   1 
ATOM   1426 C  CB  . GLN   B 1 42  ? 8.083  -27.781 24.664 1.00 28.26 ? 48  GLN   C CB  1 
ATOM   1427 C  CG  . GLN   B 1 42  ? 7.426  -27.060 25.833 1.00 36.82 ? 48  GLN   C CG  1 
ATOM   1428 C  CD  . GLN   B 1 42  ? 7.288  -28.010 26.987 1.00 47.22 ? 48  GLN   C CD  1 
ATOM   1429 O  OE1 . GLN   B 1 42  ? 6.414  -28.887 27.002 1.00 50.73 ? 48  GLN   C OE1 1 
ATOM   1430 N  NE2 . GLN   B 1 42  ? 8.157  -27.870 27.978 1.00 49.69 ? 48  GLN   C NE2 1 
ATOM   1431 N  N   . GLY   B 1 43  ? 10.624 -27.140 22.651 1.00 21.12 ? 49  GLY   C N   1 
ATOM   1432 C  CA  . GLY   B 1 43  ? 11.726 -27.693 21.867 1.00 20.42 ? 49  GLY   C CA  1 
ATOM   1433 C  C   . GLY   B 1 43  ? 12.376 -28.862 22.578 1.00 19.72 ? 49  GLY   C C   1 
ATOM   1434 O  O   . GLY   B 1 43  ? 12.151 -29.067 23.785 1.00 21.53 ? 49  GLY   C O   1 
ATOM   1435 N  N   . CYS   B 1 44  ? 13.201 -29.593 21.870 1.00 18.94 ? 50  CYS   C N   1 
ATOM   1436 C  CA  . CYS   B 1 44  ? 13.787 -30.812 22.443 1.00 19.91 ? 50  CYS   C CA  1 
ATOM   1437 C  C   . CYS   B 1 44  ? 15.287 -30.843 22.521 1.00 19.78 ? 50  CYS   C C   1 
ATOM   1438 O  O   . CYS   B 1 44  ? 15.840 -31.885 22.905 1.00 22.21 ? 50  CYS   C O   1 
ATOM   1439 C  CB  . CYS   B 1 44  ? 13.271 -32.026 21.682 1.00 21.16 ? 50  CYS   C CB  1 
ATOM   1440 S  SG  . CYS   B 1 44  ? 11.456 -32.131 21.665 1.00 28.91 ? 50  CYS   C SG  1 
ATOM   1441 N  N   . ASP   B 1 45  ? 15.970 -29.756 22.170 1.00 16.87 ? 51  ASP   C N   1 
ATOM   1442 C  CA  . ASP   B 1 45  ? 17.427 -29.736 22.230 1.00 16.72 ? 51  ASP   C CA  1 
ATOM   1443 C  C   . ASP   B 1 45  ? 17.832 -29.527 23.691 1.00 17.13 ? 51  ASP   C C   1 
ATOM   1444 O  O   . ASP   B 1 45  ? 17.103 -28.887 24.482 1.00 18.84 ? 51  ASP   C O   1 
ATOM   1445 C  CB  . ASP   B 1 45  ? 18.000 -28.581 21.370 1.00 17.04 ? 51  ASP   C CB  1 
ATOM   1446 C  CG  . ASP   B 1 45  ? 17.848 -28.766 19.872 1.00 21.13 ? 51  ASP   C CG  1 
ATOM   1447 O  OD1 . ASP   B 1 45  ? 17.901 -29.928 19.405 1.00 21.79 ? 51  ASP   C OD1 1 
ATOM   1448 O  OD2 . ASP   B 1 45  ? 17.696 -27.737 19.151 1.00 18.64 ? 51  ASP   C OD2 1 
ATOM   1449 N  N   . THR   B 1 46  ? 18.960 -30.128 24.040 1.00 15.42 ? 52  THR   C N   1 
ATOM   1450 C  CA  . THR   B 1 46  ? 19.562 -29.981 25.362 1.00 15.72 ? 52  THR   C CA  1 
ATOM   1451 C  C   . THR   B 1 46  ? 20.833 -29.135 25.199 1.00 15.23 ? 52  THR   C C   1 
ATOM   1452 O  O   . THR   B 1 46  ? 21.637 -29.406 24.287 1.00 16.03 ? 52  THR   C O   1 
ATOM   1453 C  CB  . THR   B 1 46  ? 19.934 -31.351 25.919 1.00 18.12 ? 52  THR   C CB  1 
ATOM   1454 O  OG1 . THR   B 1 46  ? 18.728 -32.097 26.125 1.00 19.91 ? 52  THR   C OG1 1 
ATOM   1455 C  CG2 . THR   B 1 46  ? 20.692 -31.232 27.261 1.00 19.63 ? 52  THR   C CG2 1 
ATOM   1456 N  N   . ILE   B 1 47  ? 21.012 -28.102 26.040 1.00 15.28 ? 53  ILE   C N   1 
ATOM   1457 C  CA  . ILE   B 1 47  ? 22.221 -27.293 25.968 1.00 14.43 ? 53  ILE   C CA  1 
ATOM   1458 C  C   . ILE   B 1 47  ? 23.315 -27.956 26.817 1.00 13.71 ? 53  ILE   C C   1 
ATOM   1459 O  O   . ILE   B 1 47  ? 23.059 -28.399 27.948 1.00 15.44 ? 53  ILE   C O   1 
ATOM   1460 C  CB  . ILE   B 1 47  ? 21.970 -25.884 26.533 1.00 15.06 ? 53  ILE   C CB  1 
ATOM   1461 C  CG1 . ILE   B 1 47  ? 20.755 -25.207 25.897 1.00 15.96 ? 53  ILE   C CG1 1 
ATOM   1462 C  CG2 . ILE   B 1 47  ? 23.229 -25.035 26.430 1.00 15.76 ? 53  ILE   C CG2 1 
ATOM   1463 C  CD1 . ILE   B 1 47  ? 20.957 -25.065 24.338 1.00 18.36 ? 53  ILE   C CD1 1 
ATOM   1464 N  N   . ALA   B 1 48  ? 24.533 -28.021 26.272 1.00 12.93 ? 54  ALA   C N   1 
ATOM   1465 C  CA  . ALA   B 1 48  ? 25.658 -28.586 27.031 1.00 13.49 ? 54  ALA   C CA  1 
ATOM   1466 C  C   . ALA   B 1 48  ? 26.025 -27.671 28.186 1.00 13.09 ? 54  ALA   C C   1 
ATOM   1467 O  O   . ALA   B 1 48  ? 25.981 -26.435 28.036 1.00 13.68 ? 54  ALA   C O   1 
ATOM   1468 C  CB  . ALA   B 1 48  ? 26.857 -28.707 26.097 1.00 12.92 ? 54  ALA   C CB  1 
ATOM   1469 N  N   . ARG   B 1 49  ? 26.371 -28.254 29.359 1.00 12.51 ? 55  ARG   C N   1 
ATOM   1470 C  CA  . ARG   B 1 49  ? 26.828 -27.477 30.515 1.00 12.79 ? 55  ARG   C CA  1 
ATOM   1471 C  C   . ARG   B 1 49  ? 28.143 -28.156 30.883 1.00 14.66 ? 55  ARG   C C   1 
ATOM   1472 O  O   . ARG   B 1 49  ? 28.160 -29.201 31.554 1.00 15.60 ? 55  ARG   C O   1 
ATOM   1473 C  CB  . ARG   B 1 49  ? 25.793 -27.484 31.665 1.00 14.09 ? 55  ARG   C CB  1 
ATOM   1474 C  CG  . ARG   B 1 49  ? 24.435 -26.951 31.202 1.00 13.49 ? 55  ARG   C CG  1 
ATOM   1475 C  CD  . ARG   B 1 49  ? 24.430 -25.463 30.867 1.00 15.39 ? 55  ARG   C CD  1 
ATOM   1476 N  NE  . ARG   B 1 49  ? 23.085 -25.035 30.462 1.00 16.10 ? 55  ARG   C NE  1 
ATOM   1477 C  CZ  . ARG   B 1 49  ? 22.835 -23.941 29.745 1.00 16.39 ? 55  ARG   C CZ  1 
ATOM   1478 N  NH1 . ARG   B 1 49  ? 23.825 -23.121 29.401 1.00 15.76 ? 55  ARG   C NH1 1 
ATOM   1479 N  NH2 . ARG   B 1 49  ? 21.586 -23.648 29.377 1.00 16.43 ? 55  ARG   C NH2 1 
ATOM   1480 N  N   . CYS   B 1 50  ? 29.238 -27.599 30.340 1.00 13.96 ? 56  CYS   C N   1 
ATOM   1481 C  CA  . CYS   B 1 50  ? 30.561 -28.256 30.393 1.00 14.35 ? 56  CYS   C CA  1 
ATOM   1482 C  C   . CYS   B 1 50  ? 31.646 -27.303 29.909 1.00 14.54 ? 56  CYS   C C   1 
ATOM   1483 O  O   . CYS   B 1 50  ? 31.336 -26.195 29.450 1.00 14.48 ? 56  CYS   C O   1 
ATOM   1484 C  CB  . CYS   B 1 50  ? 30.520 -29.470 29.463 1.00 14.62 ? 56  CYS   C CB  1 
ATOM   1485 S  SG  . CYS   B 1 50  ? 30.380 -29.011 27.704 1.00 13.92 ? 56  CYS   C SG  1 
ATOM   1486 N  N   . ASP   B 1 51  ? 32.933 -27.772 29.944 1.00 15.40 ? 57  ASP   C N   1 
ATOM   1487 C  CA  . ASP   B 1 51  ? 34.058 -27.030 29.356 1.00 16.00 ? 57  ASP   C CA  1 
ATOM   1488 C  C   . ASP   B 1 51  ? 34.730 -27.894 28.241 1.00 15.92 ? 57  ASP   C C   1 
ATOM   1489 O  O   . ASP   B 1 51  ? 35.931 -27.783 28.000 1.00 16.63 ? 57  ASP   C O   1 
ATOM   1490 C  CB  . ASP   B 1 51  ? 35.063 -26.598 30.432 1.00 18.98 ? 57  ASP   C CB  1 
ATOM   1491 C  CG  . ASP   B 1 51  ? 35.751 -27.738 31.128 1.00 22.60 ? 57  ASP   C CG  1 
ATOM   1492 O  OD1 . ASP   B 1 51  ? 35.401 -28.900 30.863 1.00 20.75 ? 57  ASP   C OD1 1 
ATOM   1493 O  OD2 . ASP   B 1 51  ? 36.665 -27.467 31.957 1.00 27.75 ? 57  ASP   C OD2 1 
ATOM   1494 N  N   . CYS   B 1 52  ? 33.941 -28.746 27.534 1.00 14.31 ? 58  CYS   C N   1 
ATOM   1495 C  CA  . CYS   B 1 52  ? 34.500 -29.534 26.403 1.00 13.88 ? 58  CYS   C CA  1 
ATOM   1496 C  C   . CYS   B 1 52  ? 35.176 -28.631 25.370 1.00 13.47 ? 58  CYS   C C   1 
ATOM   1497 O  O   . CYS   B 1 52  ? 34.747 -27.467 25.139 1.00 13.90 ? 58  CYS   C O   1 
ATOM   1498 C  CB  . CYS   B 1 52  ? 33.408 -30.335 25.700 1.00 14.92 ? 58  CYS   C CB  1 
ATOM   1499 S  SG  . CYS   B 1 52  ? 32.804 -31.780 26.600 1.00 14.51 ? 58  CYS   C SG  1 
ATOM   1500 N  N   . GLN   B 1 53  ? 36.233 -29.145 24.785 1.00 13.32 ? 59  GLN   C N   1 
ATOM   1501 C  CA  . GLN   B 1 53  ? 36.921 -28.505 23.666 1.00 13.87 ? 59  GLN   C CA  1 
ATOM   1502 C  C   . GLN   B 1 53  ? 36.982 -29.430 22.463 1.00 12.90 ? 59  GLN   C C   1 
ATOM   1503 O  O   . GLN   B 1 53  ? 37.766 -29.209 21.517 1.00 13.18 ? 59  GLN   C O   1 
ATOM   1504 C  CB  . GLN   B 1 53  ? 38.336 -28.019 24.039 1.00 14.58 ? 59  GLN   C CB  1 
ATOM   1505 C  CG  . GLN   B 1 53  ? 38.328 -26.748 24.901 1.00 18.85 ? 59  GLN   C CG  1 
ATOM   1506 C  CD  . GLN   B 1 53  ? 39.701 -26.186 25.104 1.00 21.61 ? 59  GLN   C CD  1 
ATOM   1507 O  OE1 . GLN   B 1 53  ? 40.225 -26.245 26.231 1.00 23.14 ? 59  GLN   C OE1 1 
ATOM   1508 N  NE2 . GLN   B 1 53  ? 40.318 -25.671 24.026 1.00 18.86 ? 59  GLN   C NE2 1 
ATOM   1509 N  N   . THR   B 1 54  ? 36.217 -30.542 22.466 1.00 12.99 ? 60  THR   C N   1 
ATOM   1510 C  CA  . THR   B 1 54  ? 36.085 -31.389 21.278 1.00 13.45 ? 60  THR   C CA  1 
ATOM   1511 C  C   . THR   B 1 54  ? 34.607 -31.686 21.038 1.00 13.09 ? 60  THR   C C   1 
ATOM   1512 O  O   . THR   B 1 54  ? 33.818 -31.780 21.980 1.00 14.17 ? 60  THR   C O   1 
ATOM   1513 C  CB  . THR   B 1 54  ? 36.856 -32.698 21.346 1.00 16.91 ? 60  THR   C CB  1 
ATOM   1514 O  OG1 . THR   B 1 54  ? 36.331 -33.486 22.387 1.00 20.52 ? 60  THR   C OG1 1 
ATOM   1515 C  CG2 . THR   B 1 54  ? 38.353 -32.486 21.589 1.00 17.25 ? 60  THR   C CG2 1 
ATOM   1516 N  N   . GLY   B 1 55  ? 34.218 -31.739 19.765 1.00 11.96 ? 61  GLY   C N   1 
ATOM   1517 C  CA  . GLY   B 1 55  ? 32.821 -31.971 19.413 1.00 12.37 ? 61  GLY   C CA  1 
ATOM   1518 C  C   . GLY   B 1 55  ? 32.678 -32.175 17.923 1.00 11.62 ? 61  GLY   C C   1 
ATOM   1519 O  O   . GLY   B 1 55  ? 33.666 -32.511 17.240 1.00 12.49 ? 61  GLY   C O   1 
ATOM   1520 N  N   . VAL   B 1 56  ? 31.440 -32.071 17.441 1.00 10.89 ? 62  VAL   C N   1 
ATOM   1521 C  CA  . VAL   B 1 56  ? 31.144 -32.266 16.026 1.00 9.72  ? 62  VAL   C CA  1 
ATOM   1522 C  C   . VAL   B 1 56  ? 30.253 -31.125 15.586 1.00 10.34 ? 62  VAL   C C   1 
ATOM   1523 O  O   . VAL   B 1 56  ? 29.299 -30.805 16.297 1.00 12.16 ? 62  VAL   C O   1 
ATOM   1524 C  CB  . VAL   B 1 56  ? 30.411 -33.639 15.873 1.00 11.11 ? 62  VAL   C CB  1 
ATOM   1525 C  CG1 . VAL   B 1 56  ? 29.907 -33.835 14.432 1.00 12.73 ? 62  VAL   C CG1 1 
ATOM   1526 C  CG2 . VAL   B 1 56  ? 31.321 -34.814 16.282 1.00 12.26 ? 62  VAL   C CG2 1 
ATOM   1527 N  N   . TYR   B 1 57  ? 30.500 -30.568 14.391 1.00 10.47 ? 63  TYR   C N   1 
ATOM   1528 C  CA  . TYR   B 1 57  ? 29.613 -29.488 13.892 1.00 9.69  ? 63  TYR   C CA  1 
ATOM   1529 C  C   . TYR   B 1 57  ? 29.051 -29.842 12.525 1.00 10.72 ? 63  TYR   C C   1 
ATOM   1530 O  O   . TYR   B 1 57  ? 29.717 -30.522 11.741 1.00 11.97 ? 63  TYR   C O   1 
ATOM   1531 C  CB  . TYR   B 1 57  ? 30.273 -28.075 13.865 1.00 10.58 ? 63  TYR   C CB  1 
ATOM   1532 C  CG  . TYR   B 1 57  ? 31.153 -27.769 12.658 1.00 11.22 ? 63  TYR   C CG  1 
ATOM   1533 C  CD1 . TYR   B 1 57  ? 32.433 -28.293 12.551 1.00 12.21 ? 63  TYR   C CD1 1 
ATOM   1534 C  CD2 . TYR   B 1 57  ? 30.696 -26.932 11.627 1.00 12.11 ? 63  TYR   C CD2 1 
ATOM   1535 C  CE1 . TYR   B 1 57  ? 33.266 -27.969 11.476 1.00 12.95 ? 63  TYR   C CE1 1 
ATOM   1536 C  CE2 . TYR   B 1 57  ? 31.512 -26.613 10.545 1.00 12.60 ? 63  TYR   C CE2 1 
ATOM   1537 C  CZ  . TYR   B 1 57  ? 32.795 -27.128 10.469 1.00 12.72 ? 63  TYR   C CZ  1 
ATOM   1538 O  OH  . TYR   B 1 57  ? 33.654 -26.803 9.400  1.00 14.36 ? 63  TYR   C OH  1 
ATOM   1539 N  N   . TYR   B 1 58  ? 27.895 -29.277 12.239 1.00 10.65 ? 64  TYR   C N   1 
ATOM   1540 C  CA  . TYR   B 1 58  ? 27.291 -29.447 10.916 1.00 11.17 ? 64  TYR   C CA  1 
ATOM   1541 C  C   . TYR   B 1 58  ? 27.677 -28.300 9.986  1.00 11.96 ? 64  TYR   C C   1 
ATOM   1542 O  O   . TYR   B 1 58  ? 27.425 -27.105 10.284 1.00 11.97 ? 64  TYR   C O   1 
ATOM   1543 C  CB  . TYR   B 1 58  ? 25.757 -29.558 10.994 1.00 11.63 ? 64  TYR   C CB  1 
ATOM   1544 C  CG  . TYR   B 1 58  ? 25.165 -29.831 9.619  1.00 12.82 ? 64  TYR   C CG  1 
ATOM   1545 C  CD1 . TYR   B 1 58  ? 25.504 -30.982 8.912  1.00 14.20 ? 64  TYR   C CD1 1 
ATOM   1546 C  CD2 . TYR   B 1 58  ? 24.289 -28.942 9.035  1.00 13.01 ? 64  TYR   C CD2 1 
ATOM   1547 C  CE1 . TYR   B 1 58  ? 25.008 -31.220 7.623  1.00 14.16 ? 64  TYR   C CE1 1 
ATOM   1548 C  CE2 . TYR   B 1 58  ? 23.778 -29.175 7.747  1.00 13.62 ? 64  TYR   C CE2 1 
ATOM   1549 C  CZ  . TYR   B 1 58  ? 24.114 -30.338 7.075  1.00 14.65 ? 64  TYR   C CZ  1 
ATOM   1550 O  OH  . TYR   B 1 58  ? 23.652 -30.601 5.791  1.00 17.61 ? 64  TYR   C OH  1 
ATOM   1551 N  N   . CYS   B 1 59  ? 28.190 -28.665 8.799  1.00 11.64 ? 65  CYS   C N   1 
ATOM   1552 C  CA  . CYS   B 1 59  ? 28.597 -27.719 7.749  1.00 12.54 ? 65  CYS   C CA  1 
ATOM   1553 C  C   . CYS   B 1 59  ? 27.665 -27.909 6.518  1.00 13.51 ? 65  CYS   C C   1 
ATOM   1554 O  O   . CYS   B 1 59  ? 27.820 -28.876 5.753  1.00 13.97 ? 65  CYS   C O   1 
ATOM   1555 C  CB  . CYS   B 1 59  ? 30.051 -27.967 7.384  1.00 13.23 ? 65  CYS   C CB  1 
ATOM   1556 S  SG  . CYS   B 1 59  ? 30.640 -26.945 5.999  1.00 14.66 ? 65  CYS   C SG  1 
ATOM   1557 N  N   . SER   B 1 60  ? 26.667 -27.011 6.372  1.00 13.11 ? 66  SER   C N   1 
ATOM   1558 C  CA  . SER   B 1 60  ? 25.683 -27.179 5.303  1.00 14.03 ? 66  SER   C CA  1 
ATOM   1559 C  C   . SER   B 1 60  ? 26.292 -27.124 3.922  1.00 14.19 ? 66  SER   C C   1 
ATOM   1560 O  O   . SER   B 1 60  ? 25.848 -27.873 3.045  1.00 16.14 ? 66  SER   C O   1 
ATOM   1561 C  CB  . SER   B 1 60  ? 24.558 -26.169 5.441  1.00 16.38 ? 66  SER   C CB  1 
ATOM   1562 O  OG  . SER   B 1 60  ? 23.624 -26.424 4.410  1.00 20.66 ? 66  SER   C OG  1 
ATOM   1563 N  N   . SER   B 1 61  ? 27.305 -26.276 3.720  1.00 13.73 ? 67  SER   C N   1 
ATOM   1564 C  CA  . SER   B 1 61  ? 27.931 -26.166 2.399  1.00 14.00 ? 67  SER   C CA  1 
ATOM   1565 C  C   . SER   B 1 61  ? 28.715 -27.392 1.962  1.00 16.52 ? 67  SER   C C   1 
ATOM   1566 O  O   . SER   B 1 61  ? 29.099 -27.484 0.786  1.00 18.48 ? 67  SER   C O   1 
ATOM   1567 C  CB  . SER   B 1 61  ? 28.797 -24.924 2.339  1.00 14.74 ? 67  SER   C CB  1 
ATOM   1568 O  OG  . SER   B 1 61  ? 29.901 -24.990 3.220  1.00 16.27 ? 67  SER   C OG  1 
ATOM   1569 N  N   . ARG   B 1 62  ? 28.971 -28.334 2.881  1.00 15.25 ? 68  ARG   C N   1 
ATOM   1570 C  CA  . ARG   B 1 62  ? 29.594 -29.604 2.535  1.00 15.12 ? 68  ARG   C CA  1 
ATOM   1571 C  C   . ARG   B 1 62  ? 28.658 -30.799 2.762  1.00 15.34 ? 68  ARG   C C   1 
ATOM   1572 O  O   . ARG   B 1 62  ? 29.060 -31.950 2.553  1.00 16.69 ? 68  ARG   C O   1 
ATOM   1573 C  CB  . ARG   B 1 62  ? 30.893 -29.802 3.328  1.00 15.48 ? 68  ARG   C CB  1 
ATOM   1574 C  CG  . ARG   B 1 62  ? 31.944 -28.716 3.071  1.00 19.87 ? 68  ARG   C CG  1 
ATOM   1575 C  CD  . ARG   B 1 62  ? 32.600 -28.965 1.752  1.00 19.65 ? 68  ARG   C CD  1 
ATOM   1576 N  NE  . ARG   B 1 62  ? 33.620 -27.946 1.435  1.00 23.10 ? 68  ARG   C NE  1 
ATOM   1577 C  CZ  . ARG   B 1 62  ? 33.388 -26.796 0.806  1.00 27.68 ? 68  ARG   C CZ  1 
ATOM   1578 N  NH1 . ARG   B 1 62  ? 32.165 -26.498 0.377  1.00 27.89 ? 68  ARG   C NH1 1 
ATOM   1579 N  NH2 . ARG   B 1 62  ? 34.398 -25.969 0.517  1.00 28.96 ? 68  ARG   C NH2 1 
ATOM   1580 N  N   . ARG   B 1 63  ? 27.450 -30.551 3.309  1.00 15.89 ? 69  ARG   C N   1 
ATOM   1581 C  CA  . ARG   B 1 63  ? 26.489 -31.603 3.741  1.00 17.16 ? 69  ARG   C CA  1 
ATOM   1582 C  C   . ARG   B 1 63  ? 27.204 -32.638 4.617  1.00 18.05 ? 69  ARG   C C   1 
ATOM   1583 O  O   . ARG   B 1 63  ? 27.084 -33.856 4.403  1.00 20.19 ? 69  ARG   C O   1 
ATOM   1584 C  CB  . ARG   B 1 63  ? 25.844 -32.288 2.524  1.00 17.68 ? 69  ARG   C CB  1 
ATOM   1585 C  CG  . ARG   B 1 63  ? 24.970 -31.408 1.678  1.00 21.49 ? 69  ARG   C CG  1 
ATOM   1586 C  CD  . ARG   B 1 63  ? 23.693 -31.039 2.362  1.00 26.86 ? 69  ARG   C CD  1 
ATOM   1587 N  NE  . ARG   B 1 63  ? 22.732 -30.541 1.384  1.00 28.60 ? 69  ARG   C NE  1 
ATOM   1588 C  CZ  . ARG   B 1 63  ? 22.575 -29.263 1.072  1.00 29.18 ? 69  ARG   C CZ  1 
ATOM   1589 N  NH1 . ARG   B 1 63  ? 23.341 -28.332 1.635  1.00 27.45 ? 69  ARG   C NH1 1 
ATOM   1590 N  NH2 . ARG   B 1 63  ? 21.660 -28.901 0.187  1.00 29.87 ? 69  ARG   C NH2 1 
ATOM   1591 N  N   . LYS   B 1 64  ? 28.021 -32.137 5.559  1.00 16.14 ? 70  LYS   C N   1 
ATOM   1592 C  CA  . LYS   B 1 64  ? 28.830 -33.021 6.364  1.00 16.11 ? 70  LYS   C CA  1 
ATOM   1593 C  C   . LYS   B 1 64  ? 28.915 -32.565 7.806  1.00 15.11 ? 70  LYS   C C   1 
ATOM   1594 O  O   . LYS   B 1 64  ? 28.942 -31.358 8.080  1.00 14.99 ? 70  LYS   C O   1 
ATOM   1595 C  CB  . LYS   B 1 64  ? 30.253 -33.051 5.785  1.00 19.92 ? 70  LYS   C CB  1 
ATOM   1596 C  CG  . LYS   B 1 64  ? 30.435 -34.048 4.652  1.00 29.84 ? 70  LYS   C CG  1 
ATOM   1597 C  CD  . LYS   B 1 64  ? 31.910 -34.373 4.430  1.00 37.26 ? 70  LYS   C CD  1 
ATOM   1598 C  CE  . LYS   B 1 64  ? 32.079 -35.281 3.236  1.00 42.29 ? 70  LYS   C CE  1 
ATOM   1599 N  NZ  . LYS   B 1 64  ? 31.268 -34.810 2.082  1.00 46.23 ? 70  LYS   C NZ  1 
ATOM   1600 N  N   . HIS   B 1 65  ? 29.031 -33.519 8.703  1.00 14.21 ? 71  HIS   C N   1 
ATOM   1601 C  CA  . HIS   B 1 65  ? 29.315 -33.260 10.109 1.00 14.40 ? 71  HIS   C CA  1 
ATOM   1602 C  C   . HIS   B 1 65  ? 30.794 -33.534 10.296 1.00 15.93 ? 71  HIS   C C   1 
ATOM   1603 O  O   . HIS   B 1 65  ? 31.276 -34.627 9.951  1.00 18.50 ? 71  HIS   C O   1 
ATOM   1604 C  CB  . HIS   B 1 65  ? 28.492 -34.192 11.022 1.00 14.49 ? 71  HIS   C CB  1 
ATOM   1605 C  CG  . HIS   B 1 65  ? 27.023 -33.903 10.983 1.00 14.20 ? 71  HIS   C CG  1 
ATOM   1606 N  ND1 . HIS   B 1 65  ? 26.381 -33.146 11.964 1.00 17.07 ? 71  HIS   C ND1 1 
ATOM   1607 C  CD2 . HIS   B 1 65  ? 26.110 -34.294 10.062 1.00 14.05 ? 71  HIS   C CD2 1 
ATOM   1608 C  CE1 . HIS   B 1 65  ? 25.091 -33.147 11.643 1.00 15.28 ? 71  HIS   C CE1 1 
ATOM   1609 N  NE2 . HIS   B 1 65  ? 24.875 -33.824 10.510 1.00 16.54 ? 71  HIS   C NE2 1 
ATOM   1610 N  N   . TYR   B 1 66  ? 31.539 -32.567 10.877 1.00 13.83 ? 72  TYR   C N   1 
ATOM   1611 C  CA  . TYR   B 1 66  ? 32.984 -32.752 11.038 1.00 12.98 ? 72  TYR   C CA  1 
ATOM   1612 C  C   . TYR   B 1 66  ? 33.356 -32.779 12.526 1.00 12.47 ? 72  TYR   C C   1 
ATOM   1613 O  O   . TYR   B 1 66  ? 32.921 -31.909 13.286 1.00 12.79 ? 72  TYR   C O   1 
ATOM   1614 C  CB  . TYR   B 1 66  ? 33.722 -31.511 10.460 1.00 13.78 ? 72  TYR   C CB  1 
ATOM   1615 C  CG  . TYR   B 1 66  ? 33.709 -31.412 8.940  1.00 14.26 ? 72  TYR   C CG  1 
ATOM   1616 C  CD1 . TYR   B 1 66  ? 34.571 -32.170 8.172  1.00 16.45 ? 72  TYR   C CD1 1 
ATOM   1617 C  CD2 . TYR   B 1 66  ? 32.886 -30.504 8.286  1.00 14.71 ? 72  TYR   C CD2 1 
ATOM   1618 C  CE1 . TYR   B 1 66  ? 34.585 -32.068 6.783  1.00 17.32 ? 72  TYR   C CE1 1 
ATOM   1619 C  CE2 . TYR   B 1 66  ? 32.898 -30.378 6.898  1.00 15.43 ? 72  TYR   C CE2 1 
ATOM   1620 C  CZ  . TYR   B 1 66  ? 33.763 -31.151 6.152  1.00 16.07 ? 72  TYR   C CZ  1 
ATOM   1621 O  OH  . TYR   B 1 66  ? 33.736 -30.996 4.777  1.00 19.05 ? 72  TYR   C OH  1 
ATOM   1622 N  N   . PRO   B 1 67  ? 34.159 -33.761 12.937 1.00 12.69 ? 73  PRO   C N   1 
ATOM   1623 C  CA  . PRO   B 1 67  ? 34.696 -33.725 14.315 1.00 11.73 ? 73  PRO   C CA  1 
ATOM   1624 C  C   . PRO   B 1 67  ? 35.784 -32.657 14.406 1.00 13.20 ? 73  PRO   C C   1 
ATOM   1625 O  O   . PRO   B 1 67  ? 36.673 -32.596 13.520 1.00 14.89 ? 73  PRO   C O   1 
ATOM   1626 C  CB  . PRO   B 1 67  ? 35.292 -35.140 14.517 1.00 14.62 ? 73  PRO   C CB  1 
ATOM   1627 C  CG  . PRO   B 1 67  ? 35.487 -35.684 13.157 1.00 17.33 ? 73  PRO   C CG  1 
ATOM   1628 C  CD  . PRO   B 1 67  ? 34.691 -34.899 12.142 1.00 14.27 ? 73  PRO   C CD  1 
ATOM   1629 N  N   . VAL   B 1 68  ? 35.756 -31.854 15.461 1.00 12.14 ? 74  VAL   C N   1 
ATOM   1630 C  CA  . VAL   B 1 68  ? 36.722 -30.760 15.593 1.00 12.94 ? 74  VAL   C CA  1 
ATOM   1631 C  C   . VAL   B 1 68  ? 37.140 -30.577 17.025 1.00 12.46 ? 74  VAL   C C   1 
ATOM   1632 O  O   . VAL   B 1 68  ? 36.393 -30.852 17.963 1.00 12.62 ? 74  VAL   C O   1 
ATOM   1633 C  CB  . VAL   B 1 68  ? 36.132 -29.393 15.101 1.00 14.32 ? 74  VAL   C CB  1 
ATOM   1634 C  CG1 . VAL   B 1 68  ? 36.057 -29.319 13.570 1.00 15.79 ? 74  VAL   C CG1 1 
ATOM   1635 C  CG2 . VAL   B 1 68  ? 34.789 -29.065 15.769 1.00 15.11 ? 74  VAL   C CG2 1 
ATOM   1636 N  N   . SER   B 1 69  ? 38.349 -29.991 17.201 1.00 12.42 ? 75  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 69  ? 38.827 -29.402 18.456 1.00 12.64 ? 75  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 69  ? 38.544 -27.887 18.339 1.00 12.99 ? 75  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 69  ? 38.682 -27.302 17.246 1.00 13.55 ? 75  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 69  ? 40.335 -29.595 18.603 1.00 15.19 ? 75  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 69  ? 40.613 -30.981 18.685 1.00 20.95 ? 75  SER   C OG  1 
ATOM   1642 N  N   . PHE   B 1 70  ? 38.045 -27.270 19.405 1.00 11.96 ? 76  PHE   C N   1 
ATOM   1643 C  CA  . PHE   B 1 70  ? 37.697 -25.840 19.355 1.00 11.86 ? 76  PHE   C CA  1 
ATOM   1644 C  C   . PHE   B 1 70  ? 38.194 -25.118 20.602 1.00 12.70 ? 76  PHE   C C   1 
ATOM   1645 O  O   . PHE   B 1 70  ? 38.361 -25.717 21.669 1.00 12.80 ? 76  PHE   C O   1 
ATOM   1646 C  CB  . PHE   B 1 70  ? 36.180 -25.603 19.126 1.00 12.74 ? 76  PHE   C CB  1 
ATOM   1647 C  CG  . PHE   B 1 70  ? 35.275 -26.316 20.110 1.00 11.80 ? 76  PHE   C CG  1 
ATOM   1648 C  CD1 . PHE   B 1 70  ? 34.863 -27.628 19.886 1.00 11.55 ? 76  PHE   C CD1 1 
ATOM   1649 C  CD2 . PHE   B 1 70  ? 34.852 -25.683 21.263 1.00 12.91 ? 76  PHE   C CD2 1 
ATOM   1650 C  CE1 . PHE   B 1 70  ? 34.032 -28.274 20.788 1.00 12.08 ? 76  PHE   C CE1 1 
ATOM   1651 C  CE2 . PHE   B 1 70  ? 33.998 -26.330 22.154 1.00 12.93 ? 76  PHE   C CE2 1 
ATOM   1652 C  CZ  . PHE   B 1 70  ? 33.631 -27.635 21.943 1.00 12.74 ? 76  PHE   C CZ  1 
ATOM   1653 N  N   . SER   B 1 71  ? 38.452 -23.828 20.459 1.00 11.98 ? 77  SER   C N   1 
ATOM   1654 C  CA  . SER   B 1 71  ? 39.056 -23.033 21.522 1.00 13.15 ? 77  SER   C CA  1 
ATOM   1655 C  C   . SER   B 1 71  ? 38.067 -22.647 22.591 1.00 14.25 ? 77  SER   C C   1 
ATOM   1656 O  O   . SER   B 1 71  ? 36.866 -22.869 22.464 1.00 15.91 ? 77  SER   C O   1 
ATOM   1657 C  CB  . SER   B 1 71  ? 39.784 -21.823 20.932 1.00 14.33 ? 77  SER   C CB  1 
ATOM   1658 O  OG  . SER   B 1 71  ? 38.876 -20.941 20.286 1.00 16.09 ? 77  SER   C OG  1 
ATOM   1659 N  N   . LYS   B 1 72  ? 38.566 -22.046 23.683 1.00 15.87 ? 78  LYS   C N   1 
ATOM   1660 C  CA  . LYS   B 1 72  ? 37.673 -21.626 24.769 1.00 16.11 ? 78  LYS   C CA  1 
ATOM   1661 C  C   . LYS   B 1 72  ? 36.943 -20.321 24.355 1.00 16.42 ? 78  LYS   C C   1 
ATOM   1662 O  O   . LYS   B 1 72  ? 37.512 -19.515 23.617 1.00 17.53 ? 78  LYS   C O   1 
ATOM   1663 C  CB  . LYS   B 1 72  ? 38.509 -21.386 26.041 1.00 21.77 ? 78  LYS   C CB  1 
ATOM   1664 C  CG  . LYS   B 1 72  ? 39.201 -22.662 26.515 1.00 26.63 ? 78  LYS   C CG  1 
ATOM   1665 C  CD  . LYS   B 1 72  ? 39.336 -22.704 28.056 1.00 37.64 ? 78  LYS   C CD  1 
ATOM   1666 C  CE  . LYS   B 1 72  ? 39.582 -24.100 28.591 1.00 44.25 ? 78  LYS   C CE  1 
ATOM   1667 N  NZ  . LYS   B 1 72  ? 39.667 -24.103 30.079 1.00 48.44 ? 78  LYS   C NZ  1 
ATOM   1668 N  N   . PRO   B 1 73  ? 35.720 -20.065 24.842 1.00 15.64 ? 79  PRO   C N   1 
ATOM   1669 C  CA  . PRO   B 1 73  ? 34.996 -18.822 24.436 1.00 15.31 ? 79  PRO   C CA  1 
ATOM   1670 C  C   . PRO   B 1 73  ? 35.770 -17.572 24.803 1.00 16.07 ? 79  PRO   C C   1 
ATOM   1671 O  O   . PRO   B 1 73  ? 36.231 -17.442 25.952 1.00 18.51 ? 79  PRO   C O   1 
ATOM   1672 C  CB  . PRO   B 1 73  ? 33.690 -18.863 25.229 1.00 17.27 ? 79  PRO   C CB  1 
ATOM   1673 C  CG  . PRO   B 1 73  ? 33.540 -20.271 25.656 1.00 19.42 ? 79  PRO   C CG  1 
ATOM   1674 C  CD  . PRO   B 1 73  ? 34.914 -20.913 25.745 1.00 16.81 ? 79  PRO   C CD  1 
ATOM   1675 N  N   . SER   B 1 74  ? 36.012 -16.700 23.821 1.00 14.46 ? 80  SER   C N   1 
ATOM   1676 C  CA  . SER   B 1 74  ? 36.889 -15.549 24.039 1.00 15.55 ? 80  SER   C CA  1 
ATOM   1677 C  C   . SER   B 1 74  ? 36.481 -14.379 23.136 1.00 15.44 ? 80  SER   C C   1 
ATOM   1678 O  O   . SER   B 1 74  ? 35.597 -14.526 22.285 1.00 15.17 ? 80  SER   C O   1 
ATOM   1679 C  CB  . SER   B 1 74  ? 38.339 -15.943 23.720 1.00 19.09 ? 80  SER   C CB  1 
ATOM   1680 O  OG  . SER   B 1 74  ? 38.798 -17.108 24.389 1.00 24.00 ? 80  SER   C OG  1 
ATOM   1681 N  N   . LEU   B 1 75  ? 37.160 -13.231 23.306 1.00 16.28 ? 81  LEU   C N   1 
ATOM   1682 C  CA  . LEU   B 1 75  ? 36.969 -12.016 22.509 1.00 17.83 ? 81  LEU   C CA  1 
ATOM   1683 C  C   . LEU   B 1 75  ? 37.988 -12.103 21.352 1.00 18.09 ? 81  LEU   C C   1 
ATOM   1684 O  O   . LEU   B 1 75  ? 39.216 -12.042 21.580 1.00 20.25 ? 81  LEU   C O   1 
ATOM   1685 C  CB  . LEU   B 1 75  ? 37.227 -10.772 23.390 1.00 19.50 ? 81  LEU   C CB  1 
ATOM   1686 C  CG  . LEU   B 1 75  ? 36.926 -9.416  22.777 1.00 22.31 ? 81  LEU   C CG  1 
ATOM   1687 C  CD1 . LEU   B 1 75  ? 35.430 -9.260  22.509 1.00 21.75 ? 81  LEU   C CD1 1 
ATOM   1688 C  CD2 . LEU   B 1 75  ? 37.428 -8.267  23.711 1.00 24.24 ? 81  LEU   C CD2 1 
ATOM   1689 N  N   . ILE   B 1 76  ? 37.492 -12.362 20.134 1.00 18.63 ? 82  ILE   C N   1 
ATOM   1690 C  CA  . ILE   B 1 76  ? 38.318 -12.626 18.950 1.00 19.93 ? 82  ILE   C CA  1 
ATOM   1691 C  C   . ILE   B 1 76  ? 38.065 -11.554 17.885 1.00 19.89 ? 82  ILE   C C   1 
ATOM   1692 O  O   . ILE   B 1 76  ? 36.887 -11.231 17.619 1.00 18.46 ? 82  ILE   C O   1 
ATOM   1693 C  CB  . ILE   B 1 76  ? 37.914 -14.015 18.366 1.00 22.09 ? 82  ILE   C CB  1 
ATOM   1694 C  CG1 . ILE   B 1 76  ? 38.166 -15.185 19.341 1.00 24.17 ? 82  ILE   C CG1 1 
ATOM   1695 C  CG2 . ILE   B 1 76  ? 38.585 -14.294 17.010 1.00 23.73 ? 82  ILE   C CG2 1 
ATOM   1696 C  CD1 . ILE   B 1 76  ? 39.632 -15.540 19.550 1.00 26.45 ? 82  ILE   C CD1 1 
ATOM   1697 N  N   . PHE   B 1 77  ? 39.136 -11.058 17.228 1.00 20.32 ? 83  PHE   C N   1 
ATOM   1698 C  CA  . PHE   B 1 77  ? 38.942 -10.104 16.133 1.00 20.77 ? 83  PHE   C CA  1 
ATOM   1699 C  C   . PHE   B 1 77  ? 38.552 -10.939 14.902 1.00 21.07 ? 83  PHE   C C   1 
ATOM   1700 O  O   . PHE   B 1 77  ? 39.230 -11.927 14.567 1.00 22.89 ? 83  PHE   C O   1 
ATOM   1701 C  CB  . PHE   B 1 77  ? 40.233 -9.309  15.839 1.00 21.46 ? 83  PHE   C CB  1 
ATOM   1702 C  CG  . PHE   B 1 77  ? 39.966 -8.141  14.911 1.00 22.51 ? 83  PHE   C CG  1 
ATOM   1703 C  CD1 . PHE   B 1 77  ? 39.272 -7.029  15.353 1.00 23.68 ? 83  PHE   C CD1 1 
ATOM   1704 C  CD2 . PHE   B 1 77  ? 40.338 -8.195  13.571 1.00 24.03 ? 83  PHE   C CD2 1 
ATOM   1705 C  CE1 . PHE   B 1 77  ? 38.981 -5.977  14.485 1.00 25.26 ? 83  PHE   C CE1 1 
ATOM   1706 C  CE2 . PHE   B 1 77  ? 40.051 -7.138  12.711 1.00 24.41 ? 83  PHE   C CE2 1 
ATOM   1707 C  CZ  . PHE   B 1 77  ? 39.399 -6.030  13.178 1.00 24.93 ? 83  PHE   C CZ  1 
ATOM   1708 N  N   . VAL   B 1 78  ? 37.439 -10.555 14.246 1.00 18.92 ? 84  VAL   C N   1 
ATOM   1709 C  CA  . VAL   B 1 78  ? 36.920 -11.266 13.088 1.00 18.90 ? 84  VAL   C CA  1 
ATOM   1710 C  C   . VAL   B 1 78  ? 36.995 -10.355 11.880 1.00 18.67 ? 84  VAL   C C   1 
ATOM   1711 O  O   . VAL   B 1 78  ? 36.535 -9.216  11.965 1.00 18.56 ? 84  VAL   C O   1 
ATOM   1712 C  CB  . VAL   B 1 78  ? 35.436 -11.652 13.379 1.00 19.43 ? 84  VAL   C CB  1 
ATOM   1713 C  CG1 . VAL   B 1 78  ? 34.851 -12.432 12.212 1.00 20.83 ? 84  VAL   C CG1 1 
ATOM   1714 C  CG2 . VAL   B 1 78  ? 35.310 -12.454 14.696 1.00 19.85 ? 84  VAL   C CG2 1 
ATOM   1715 N  N   . GLU   B 1 79  ? 37.523 -10.832 10.738 1.00 18.14 ? 85  GLU   C N   1 
ATOM   1716 C  CA  . GLU   B 1 79  ? 37.536 -10.023 9.518  1.00 18.35 ? 85  GLU   C CA  1 
ATOM   1717 C  C   . GLU   B 1 79  ? 36.128 -9.772  8.986  1.00 18.37 ? 85  GLU   C C   1 
ATOM   1718 O  O   . GLU   B 1 79  ? 35.160 -10.429 9.397  1.00 17.57 ? 85  GLU   C O   1 
ATOM   1719 C  CB  . GLU   B 1 79  ? 38.402 -10.691 8.433  1.00 20.95 ? 85  GLU   C CB  1 
ATOM   1720 C  CG  . GLU   B 1 79  ? 39.883 -10.717 8.790  1.00 25.71 ? 85  GLU   C CG  1 
ATOM   1721 C  CD  . GLU   B 1 79  ? 40.488 -9.338  9.016  1.00 34.99 ? 85  GLU   C CD  1 
ATOM   1722 O  OE1 . GLU   B 1 79  ? 40.150 -8.398  8.259  1.00 38.85 ? 85  GLU   C OE1 1 
ATOM   1723 O  OE2 . GLU   B 1 79  ? 41.280 -9.185  9.973  1.00 37.40 ? 85  GLU   C OE2 1 
ATOM   1724 N  N   . ALA   B 1 80  ? 35.978 -8.739  8.146  1.00 18.93 ? 86  ALA   C N   1 
ATOM   1725 C  CA  . ALA   B 1 80  ? 34.702 -8.387  7.563  1.00 19.53 ? 86  ALA   C CA  1 
ATOM   1726 C  C   . ALA   B 1 80  ? 34.085 -9.583  6.838  1.00 20.37 ? 86  ALA   C C   1 
ATOM   1727 O  O   . ALA   B 1 80  ? 34.797 -10.380 6.225  1.00 21.83 ? 86  ALA   C O   1 
ATOM   1728 C  CB  . ALA   B 1 80  ? 34.917 -7.238  6.577  1.00 20.12 ? 86  ALA   C CB  1 
ATOM   1729 N  N   . SER   B 1 81  ? 32.785 -9.736  7.004  1.00 19.24 ? 87  SER   C N   1 
ATOM   1730 C  CA  . SER   B 1 81  ? 32.057 -10.765 6.317  1.00 20.19 ? 87  SER   C CA  1 
ATOM   1731 C  C   . SER   B 1 81  ? 30.932 -10.104 5.516  1.00 20.98 ? 87  SER   C C   1 
ATOM   1732 O  O   . SER   B 1 81  ? 30.784 -8.861  5.524  1.00 21.72 ? 87  SER   C O   1 
ATOM   1733 C  CB  . SER   B 1 81  ? 31.490 -11.746 7.333  1.00 19.10 ? 87  SER   C CB  1 
ATOM   1734 O  OG  . SER   B 1 81  ? 30.434 -11.125 8.061  1.00 19.73 ? 87  SER   C OG  1 
ATOM   1735 N  N   . GLU   B 1 82  ? 30.112 -10.925 4.847  1.00 22.35 ? 88  GLU   C N   1 
ATOM   1736 C  CA  . GLU   B 1 82  ? 28.997 -10.320 4.115  1.00 22.96 ? 88  GLU   C CA  1 
ATOM   1737 C  C   . GLU   B 1 82  ? 27.941 -9.691  5.056  1.00 22.92 ? 88  GLU   C C   1 
ATOM   1738 O  O   . GLU   B 1 82  ? 27.185 -8.828  4.608  1.00 24.94 ? 88  GLU   C O   1 
ATOM   1739 C  CB  . GLU   B 1 82  ? 28.389 -11.300 3.109  1.00 27.37 ? 88  GLU   C CB  1 
ATOM   1740 C  CG  . GLU   B 1 82  ? 27.599 -12.446 3.692  1.00 34.95 ? 88  GLU   C CG  1 
ATOM   1741 C  CD  . GLU   B 1 82  ? 26.900 -13.217 2.587  1.00 41.48 ? 88  GLU   C CD  1 
ATOM   1742 O  OE1 . GLU   B 1 82  ? 27.537 -13.430 1.529  1.00 43.26 ? 88  GLU   C OE1 1 
ATOM   1743 O  OE2 . GLU   B 1 82  ? 25.717 -13.592 2.772  1.00 42.15 ? 88  GLU   C OE2 1 
ATOM   1744 N  N   . TYR   B 1 83  ? 27.982 -9.992  6.370  1.00 20.09 ? 89  TYR   C N   1 
ATOM   1745 C  CA  . TYR   B 1 83  ? 26.958 -9.518  7.292  1.00 19.75 ? 89  TYR   C CA  1 
ATOM   1746 C  C   . TYR   B 1 83  ? 27.454 -8.655  8.496  1.00 20.01 ? 89  TYR   C C   1 
ATOM   1747 O  O   . TYR   B 1 83  ? 26.619 -8.069  9.180  1.00 20.29 ? 89  TYR   C O   1 
ATOM   1748 C  CB  . TYR   B 1 83  ? 26.108 -10.713 7.791  1.00 19.21 ? 89  TYR   C CB  1 
ATOM   1749 C  CG  . TYR   B 1 83  ? 26.915 -11.933 8.236  1.00 18.07 ? 89  TYR   C CG  1 
ATOM   1750 C  CD1 . TYR   B 1 83  ? 27.327 -12.899 7.317  1.00 18.41 ? 89  TYR   C CD1 1 
ATOM   1751 C  CD2 . TYR   B 1 83  ? 27.365 -12.058 9.545  1.00 17.51 ? 89  TYR   C CD2 1 
ATOM   1752 C  CE1 . TYR   B 1 83  ? 28.092 -14.000 7.708  1.00 17.62 ? 89  TYR   C CE1 1 
ATOM   1753 C  CE2 . TYR   B 1 83  ? 28.100 -13.168 9.955  1.00 18.19 ? 89  TYR   C CE2 1 
ATOM   1754 C  CZ  . TYR   B 1 83  ? 28.499 -14.119 9.027  1.00 17.58 ? 89  TYR   C CZ  1 
ATOM   1755 O  OH  . TYR   B 1 83  ? 29.296 -15.184 9.412  1.00 18.57 ? 89  TYR   C OH  1 
ATOM   1756 N  N   . TYR   B 1 84  ? 28.767 -8.529  8.741  1.00 18.59 ? 90  TYR   C N   1 
ATOM   1757 C  CA  . TYR   B 1 84  ? 29.306 -7.598  9.762  1.00 18.15 ? 90  TYR   C CA  1 
ATOM   1758 C  C   . TYR   B 1 84  ? 30.630 -7.005  9.228  1.00 17.88 ? 90  TYR   C C   1 
ATOM   1759 O  O   . TYR   B 1 84  ? 31.344 -7.654  8.473  1.00 18.12 ? 90  TYR   C O   1 
ATOM   1760 C  CB  . TYR   B 1 84  ? 29.665 -8.323  11.095 1.00 16.99 ? 90  TYR   C CB  1 
ATOM   1761 C  CG  . TYR   B 1 84  ? 28.497 -8.761  11.956 1.00 15.71 ? 90  TYR   C CG  1 
ATOM   1762 C  CD1 . TYR   B 1 84  ? 27.575 -7.838  12.459 1.00 15.95 ? 90  TYR   C CD1 1 
ATOM   1763 C  CD2 . TYR   B 1 84  ? 28.291 -10.083 12.231 1.00 14.94 ? 90  TYR   C CD2 1 
ATOM   1764 C  CE1 . TYR   B 1 84  ? 26.507 -8.244  13.280 1.00 15.50 ? 90  TYR   C CE1 1 
ATOM   1765 C  CE2 . TYR   B 1 84  ? 27.221 -10.508 13.033 1.00 14.46 ? 90  TYR   C CE2 1 
ATOM   1766 C  CZ  . TYR   B 1 84  ? 26.330 -9.586  13.569 1.00 15.38 ? 90  TYR   C CZ  1 
ATOM   1767 O  OH  . TYR   B 1 84  ? 25.254 -10.019 14.345 1.00 15.09 ? 90  TYR   C OH  1 
ATOM   1768 N  N   . PRO   B 1 85  ? 31.011 -5.797  9.683  1.00 18.14 ? 91  PRO   C N   1 
ATOM   1769 C  CA  . PRO   B 1 85  ? 32.364 -5.302  9.373  1.00 17.79 ? 91  PRO   C CA  1 
ATOM   1770 C  C   . PRO   B 1 85  ? 33.405 -6.073  10.201 1.00 18.15 ? 91  PRO   C C   1 
ATOM   1771 O  O   . PRO   B 1 85  ? 33.057 -6.896  11.082 1.00 17.64 ? 91  PRO   C O   1 
ATOM   1772 C  CB  . PRO   B 1 85  ? 32.280 -3.824  9.812  1.00 18.41 ? 91  PRO   C CB  1 
ATOM   1773 C  CG  . PRO   B 1 85  ? 31.357 -3.870  10.998 1.00 18.57 ? 91  PRO   C CG  1 
ATOM   1774 C  CD  . PRO   B 1 85  ? 30.297 -4.923  10.650 1.00 18.68 ? 91  PRO   C CD  1 
ATOM   1775 N  N   . ALA   B 1 86  ? 34.703 -5.776  9.982  1.00 17.66 ? 92  ALA   C N   1 
ATOM   1776 C  CA  . ALA   B 1 86  ? 35.772 -6.336  10.818 1.00 18.92 ? 92  ALA   C CA  1 
ATOM   1777 C  C   . ALA   B 1 86  ? 35.582 -5.766  12.230 1.00 19.97 ? 92  ALA   C C   1 
ATOM   1778 O  O   . ALA   B 1 86  ? 35.304 -4.561  12.378 1.00 21.81 ? 92  ALA   C O   1 
ATOM   1779 C  CB  . ALA   B 1 86  ? 37.146 -5.946  10.269 1.00 18.93 ? 92  ALA   C CB  1 
ATOM   1780 N  N   . ARG   B 1 87  ? 35.579 -6.649  13.231 1.00 18.75 ? 93  ARG   C N   1 
ATOM   1781 C  CA  . ARG   B 1 87  ? 35.275 -6.213  14.592 1.00 18.83 ? 93  ARG   C CA  1 
ATOM   1782 C  C   . ARG   B 1 87  ? 35.668 -7.311  15.580 1.00 19.30 ? 93  ARG   C C   1 
ATOM   1783 O  O   . ARG   B 1 87  ? 35.876 -8.456  15.200 1.00 18.93 ? 93  ARG   C O   1 
ATOM   1784 C  CB  . ARG   B 1 87  ? 33.751 -5.928  14.742 1.00 18.76 ? 93  ARG   C CB  1 
ATOM   1785 C  CG  . ARG   B 1 87  ? 32.912 -7.209  14.599 1.00 18.03 ? 93  ARG   C CG  1 
ATOM   1786 C  CD  . ARG   B 1 87  ? 31.440 -6.947  14.845 1.00 17.84 ? 93  ARG   C CD  1 
ATOM   1787 N  NE  . ARG   B 1 87  ? 30.722 -8.220  15.025 1.00 17.53 ? 93  ARG   C NE  1 
ATOM   1788 C  CZ  . ARG   B 1 87  ? 29.625 -8.392  15.751 1.00 18.76 ? 93  ARG   C CZ  1 
ATOM   1789 N  NH1 . ARG   B 1 87  ? 29.033 -7.350  16.338 1.00 19.79 ? 93  ARG   C NH1 1 
ATOM   1790 N  NH2 . ARG   B 1 87  ? 29.115 -9.605  15.904 1.00 19.13 ? 93  ARG   C NH2 1 
ATOM   1791 N  N   . TYR   B 1 88  ? 35.636 -6.985  16.880 1.00 20.76 ? 94  TYR   C N   1 
ATOM   1792 C  CA  . TYR   B 1 88  ? 35.793 -7.993  17.916 1.00 21.59 ? 94  TYR   C CA  1 
ATOM   1793 C  C   . TYR   B 1 88  ? 34.391 -8.636  18.165 1.00 19.09 ? 94  TYR   C C   1 
ATOM   1794 O  O   . TYR   B 1 88  ? 33.384 -7.931  18.246 1.00 20.21 ? 94  TYR   C O   1 
ATOM   1795 C  CB  . TYR   B 1 88  ? 36.226 -7.313  19.228 1.00 24.05 ? 94  TYR   C CB  1 
ATOM   1796 C  CG  . TYR   B 1 88  ? 37.674 -6.889  19.192 1.00 26.55 ? 94  TYR   C CG  1 
ATOM   1797 C  CD1 . TYR   B 1 88  ? 38.686 -7.798  19.432 1.00 27.77 ? 94  TYR   C CD1 1 
ATOM   1798 C  CD2 . TYR   B 1 88  ? 38.029 -5.583  18.860 1.00 27.97 ? 94  TYR   C CD2 1 
ATOM   1799 C  CE1 . TYR   B 1 88  ? 40.026 -7.422  19.363 1.00 29.01 ? 94  TYR   C CE1 1 
ATOM   1800 C  CE2 . TYR   B 1 88  ? 39.355 -5.197  18.785 1.00 29.17 ? 94  TYR   C CE2 1 
ATOM   1801 C  CZ  . TYR   B 1 88  ? 40.352 -6.116  19.042 1.00 30.27 ? 94  TYR   C CZ  1 
ATOM   1802 O  OH  . TYR   B 1 88  ? 41.664 -5.713  18.989 1.00 32.81 ? 94  TYR   C OH  1 
ATOM   1803 N  N   . GLN   B 1 89  ? 34.343 -9.955  18.274 1.00 16.67 ? 95  GLN   C N   1 
ATOM   1804 C  CA  . GLN   B 1 89  ? 33.122 -10.685 18.628 1.00 15.76 ? 95  GLN   C CA  1 
ATOM   1805 C  C   . GLN   B 1 89  ? 33.436 -11.412 19.943 1.00 15.49 ? 95  GLN   C C   1 
ATOM   1806 O  O   . GLN   B 1 89  ? 34.508 -12.037 20.072 1.00 16.15 ? 95  GLN   C O   1 
ATOM   1807 C  CB  . GLN   B 1 89  ? 32.743 -11.655 17.496 1.00 15.53 ? 95  GLN   C CB  1 
ATOM   1808 C  CG  . GLN   B 1 89  ? 31.445 -12.394 17.768 1.00 16.79 ? 95  GLN   C CG  1 
ATOM   1809 C  CD  . GLN   B 1 89  ? 30.790 -12.968 16.528 1.00 16.65 ? 95  GLN   C CD  1 
ATOM   1810 O  OE1 . GLN   B 1 89  ? 30.771 -12.380 15.456 1.00 17.41 ? 95  GLN   C OE1 1 
ATOM   1811 N  NE2 . GLN   B 1 89  ? 30.202 -14.131 16.698 1.00 15.12 ? 95  GLN   C NE2 1 
ATOM   1812 N  N   . SER   B 1 90  ? 32.518 -11.367 20.888 1.00 15.05 ? 96  SER   C N   1 
ATOM   1813 C  CA  . SER   B 1 90  ? 32.717 -11.994 22.190 1.00 15.31 ? 96  SER   C CA  1 
ATOM   1814 C  C   . SER   B 1 90  ? 32.108 -13.411 22.255 1.00 14.32 ? 96  SER   C C   1 
ATOM   1815 O  O   . SER   B 1 90  ? 31.259 -13.757 21.434 1.00 14.44 ? 96  SER   C O   1 
ATOM   1816 C  CB  . SER   B 1 90  ? 32.166 -11.113 23.317 1.00 17.05 ? 96  SER   C CB  1 
ATOM   1817 O  OG  . SER   B 1 90  ? 30.762 -11.041 23.187 1.00 17.88 ? 96  SER   C OG  1 
ATOM   1818 N  N   . HIS   B 1 91  ? 32.564 -14.199 23.245 1.00 13.77 ? 97  HIS   C N   1 
ATOM   1819 C  CA  . HIS   B 1 91  ? 32.073 -15.565 23.489 1.00 13.49 ? 97  HIS   C CA  1 
ATOM   1820 C  C   . HIS   B 1 91  ? 32.158 -16.437 22.224 1.00 13.56 ? 97  HIS   C C   1 
ATOM   1821 O  O   . HIS   B 1 91  ? 31.282 -17.287 21.994 1.00 14.35 ? 97  HIS   C O   1 
ATOM   1822 C  CB  . HIS   B 1 91  ? 30.639 -15.538 24.078 1.00 14.70 ? 97  HIS   C CB  1 
ATOM   1823 C  CG  . HIS   B 1 91  ? 30.507 -14.778 25.372 1.00 16.39 ? 97  HIS   C CG  1 
ATOM   1824 N  ND1 . HIS   B 1 91  ? 30.515 -15.424 26.591 1.00 18.75 ? 97  HIS   C ND1 1 
ATOM   1825 C  CD2 . HIS   B 1 91  ? 30.406 -13.433 25.586 1.00 16.86 ? 97  HIS   C CD2 1 
ATOM   1826 C  CE1 . HIS   B 1 91  ? 30.374 -14.471 27.511 1.00 18.66 ? 97  HIS   C CE1 1 
ATOM   1827 N  NE2 . HIS   B 1 91  ? 30.298 -13.254 26.955 1.00 18.41 ? 97  HIS   C NE2 1 
ATOM   1828 N  N   . LEU   B 1 92  ? 33.243 -16.284 21.481 1.00 12.95 ? 98  LEU   C N   1 
ATOM   1829 C  CA  . LEU   B 1 92  ? 33.463 -16.976 20.218 1.00 13.49 ? 98  LEU   C CA  1 
ATOM   1830 C  C   . LEU   B 1 92  ? 34.550 -18.035 20.407 1.00 12.60 ? 98  LEU   C C   1 
ATOM   1831 O  O   . LEU   B 1 92  ? 35.535 -17.818 21.132 1.00 13.53 ? 98  LEU   C O   1 
ATOM   1832 C  CB  . LEU   B 1 92  ? 33.940 -15.965 19.132 1.00 14.90 ? 98  LEU   C CB  1 
ATOM   1833 C  CG  . LEU   B 1 92  ? 34.014 -16.541 17.713 1.00 16.10 ? 98  LEU   C CG  1 
ATOM   1834 C  CD1 . LEU   B 1 92  ? 32.619 -16.858 17.179 1.00 16.44 ? 98  LEU   C CD1 1 
ATOM   1835 C  CD2 . LEU   B 1 92  ? 34.710 -15.549 16.749 1.00 16.52 ? 98  LEU   C CD2 1 
ATOM   1836 N  N   . MET   B 1 93  ? 34.343 -19.218 19.794 1.00 12.07 ? 99  MET   C N   1 
ATOM   1837 C  CA  . MET   B 1 93  ? 35.292 -20.331 19.851 1.00 11.65 ? 99  MET   C CA  1 
ATOM   1838 C  C   . MET   B 1 93  ? 35.702 -20.639 18.404 1.00 12.03 ? 99  MET   C C   1 
ATOM   1839 O  O   . MET   B 1 93  ? 34.825 -20.679 17.547 1.00 13.62 ? 99  MET   C O   1 
ATOM   1840 C  CB  . MET   B 1 93  ? 34.568 -21.543 20.423 1.00 13.69 ? 99  MET   C CB  1 
ATOM   1841 C  CG  . MET   B 1 93  ? 34.118 -21.294 21.856 1.00 15.65 ? 99  MET   C CG  1 
ATOM   1842 S  SD  . MET   B 1 93  ? 33.064 -22.590 22.495 1.00 15.90 ? 99  MET   C SD  1 
ATOM   1843 C  CE  . MET   B 1 93  ? 31.702 -22.538 21.382 1.00 17.12 ? 99  MET   C CE  1 
ATOM   1844 N  N   . LEU   B 1 94  ? 36.981 -20.911 18.126 1.00 11.96 ? 100 LEU   C N   1 
ATOM   1845 C  CA  . LEU   B 1 94  ? 37.407 -21.185 16.758 1.00 12.56 ? 100 LEU   C CA  1 
ATOM   1846 C  C   . LEU   B 1 94  ? 37.845 -22.646 16.628 1.00 12.76 ? 100 LEU   C C   1 
ATOM   1847 O  O   . LEU   B 1 94  ? 38.381 -23.225 17.574 1.00 13.92 ? 100 LEU   C O   1 
ATOM   1848 C  CB  . LEU   B 1 94  ? 38.662 -20.340 16.355 1.00 14.07 ? 100 LEU   C CB  1 
ATOM   1849 C  CG  . LEU   B 1 94  ? 38.498 -18.843 16.309 1.00 15.68 ? 100 LEU   C CG  1 
ATOM   1850 C  CD1 . LEU   B 1 94  ? 39.794 -18.194 15.859 1.00 18.88 ? 100 LEU   C CD1 1 
ATOM   1851 C  CD2 . LEU   B 1 94  ? 37.333 -18.423 15.384 1.00 16.80 ? 100 LEU   C CD2 1 
ATOM   1852 N  N   . ALA   B 1 95  ? 37.696 -23.182 15.407 1.00 13.08 ? 101 ALA   C N   1 
ATOM   1853 C  CA  . ALA   B 1 95  ? 38.241 -24.473 15.034 1.00 12.51 ? 101 ALA   C CA  1 
ATOM   1854 C  C   . ALA   B 1 95  ? 38.819 -24.378 13.611 1.00 12.65 ? 101 ALA   C C   1 
ATOM   1855 O  O   . ALA   B 1 95  ? 38.452 -23.458 12.875 1.00 12.92 ? 101 ALA   C O   1 
ATOM   1856 C  CB  . ALA   B 1 95  ? 37.140 -25.550 15.098 1.00 13.21 ? 101 ALA   C CB  1 
ATOM   1857 N  N   . VAL   B 1 96  ? 39.653 -25.326 13.208 1.00 12.90 ? 102 VAL   C N   1 
ATOM   1858 C  CA  . VAL   B 1 96  ? 40.122 -25.373 11.827 1.00 14.01 ? 102 VAL   C CA  1 
ATOM   1859 C  C   . VAL   B 1 96  ? 39.062 -26.114 11.030 1.00 14.24 ? 102 VAL   C C   1 
ATOM   1860 O  O   . VAL   B 1 96  ? 38.734 -27.283 11.335 1.00 15.38 ? 102 VAL   C O   1 
ATOM   1861 C  CB  . VAL   B 1 96  ? 41.478 -26.103 11.779 1.00 15.87 ? 102 VAL   C CB  1 
ATOM   1862 C  CG1 . VAL   B 1 96  ? 41.945 -26.261 10.331 1.00 17.06 ? 102 VAL   C CG1 1 
ATOM   1863 C  CG2 . VAL   B 1 96  ? 42.498 -25.338 12.604 1.00 16.98 ? 102 VAL   C CG2 1 
ATOM   1864 N  N   . GLY   B 1 97  ? 38.476 -25.426 10.062 1.00 14.85 ? 103 GLY   C N   1 
ATOM   1865 C  CA  . GLY   B 1 97  ? 37.405 -26.036 9.286  1.00 15.90 ? 103 GLY   C CA  1 
ATOM   1866 C  C   . GLY   B 1 97  ? 36.723 -25.067 8.363  1.00 16.07 ? 103 GLY   C C   1 
ATOM   1867 O  O   . GLY   B 1 97  ? 36.992 -23.854 8.369  1.00 18.03 ? 103 GLY   C O   1 
ATOM   1868 N  N   . HIS   B 1 98  ? 35.852 -25.623 7.533  1.00 16.08 ? 104 HIS   C N   1 
ATOM   1869 C  CA  . HIS   B 1 98  ? 35.143 -24.838 6.551  1.00 16.20 ? 104 HIS   C CA  1 
ATOM   1870 C  C   . HIS   B 1 98  ? 33.872 -24.147 7.066  1.00 15.34 ? 104 HIS   C C   1 
ATOM   1871 O  O   . HIS   B 1 98  ? 33.047 -24.768 7.758  1.00 15.58 ? 104 HIS   C O   1 
ATOM   1872 C  CB  . HIS   B 1 98  ? 34.820 -25.695 5.338  1.00 19.10 ? 104 HIS   C CB  1 
ATOM   1873 C  CG  . HIS   B 1 98  ? 34.302 -24.887 4.203  1.00 22.99 ? 104 HIS   C CG  1 
ATOM   1874 N  ND1 . HIS   B 1 98  ? 35.112 -23.970 3.531  1.00 24.98 ? 104 HIS   C ND1 1 
ATOM   1875 C  CD2 . HIS   B 1 98  ? 33.058 -24.846 3.678  1.00 25.71 ? 104 HIS   C CD2 1 
ATOM   1876 C  CE1 . HIS   B 1 98  ? 34.328 -23.404 2.621  1.00 27.23 ? 104 HIS   C CE1 1 
ATOM   1877 N  NE2 . HIS   B 1 98  ? 33.087 -23.908 2.665  1.00 27.27 ? 104 HIS   C NE2 1 
ATOM   1878 N  N   . SER   B 1 99  ? 33.686 -22.867 6.698  1.00 15.17 ? 105 SER   C N   1 
ATOM   1879 C  CA  . SER   B 1 99  ? 32.475 -22.111 7.070  1.00 15.75 ? 105 SER   C CA  1 
ATOM   1880 C  C   . SER   B 1 99  ? 32.208 -20.966 6.061  1.00 17.57 ? 105 SER   C C   1 
ATOM   1881 O  O   . SER   B 1 99  ? 33.041 -20.047 5.943  1.00 20.07 ? 105 SER   C O   1 
ATOM   1882 C  CB  . SER   B 1 99  ? 32.683 -21.536 8.462  1.00 17.07 ? 105 SER   C CB  1 
ATOM   1883 O  OG  . SER   B 1 99  ? 31.595 -20.693 8.827  1.00 17.67 ? 105 SER   C OG  1 
ATOM   1884 N  N   . GLU   B 1 100 ? 31.115 -21.108 5.279  1.00 16.83 ? 106 GLU   C N   1 
ATOM   1885 C  CA  . GLU   B 1 100 ? 30.604 -20.109 4.309  1.00 16.71 ? 106 GLU   C CA  1 
ATOM   1886 C  C   . GLU   B 1 100 ? 29.508 -19.307 5.084  1.00 15.76 ? 106 GLU   C C   1 
ATOM   1887 O  O   . GLU   B 1 100 ? 28.960 -19.776 6.109  1.00 15.43 ? 106 GLU   C O   1 
ATOM   1888 C  CB  . GLU   B 1 100 ? 29.861 -20.828 3.127  1.00 19.77 ? 106 GLU   C CB  1 
ATOM   1889 C  CG  . GLU   B 1 100 ? 30.614 -21.831 2.272  1.00 25.35 ? 106 GLU   C CG  1 
ATOM   1890 C  CD  . GLU   B 1 100 ? 31.572 -21.242 1.266  1.00 30.16 ? 106 GLU   C CD  1 
ATOM   1891 O  OE1 . GLU   B 1 100 ? 32.269 -22.031 0.596  1.00 30.60 ? 106 GLU   C OE1 1 
ATOM   1892 O  OE2 . GLU   B 1 100 ? 31.633 -19.997 1.151  1.00 32.01 ? 106 GLU   C OE2 1 
ATOM   1893 N  N   . PRO   B 1 101 ? 29.104 -18.103 4.593  1.00 16.57 ? 107 PRO   C N   1 
ATOM   1894 C  CA  . PRO   B 1 101 ? 28.020 -17.377 5.296  1.00 16.03 ? 107 PRO   C CA  1 
ATOM   1895 C  C   . PRO   B 1 101 ? 26.756 -18.222 5.487  1.00 16.12 ? 107 PRO   C C   1 
ATOM   1896 O  O   . PRO   B 1 101 ? 26.116 -18.161 6.543  1.00 15.77 ? 107 PRO   C O   1 
ATOM   1897 C  CB  . PRO   B 1 101 ? 27.759 -16.149 4.383  1.00 18.41 ? 107 PRO   C CB  1 
ATOM   1898 C  CG  . PRO   B 1 101 ? 28.974 -16.030 3.517  1.00 20.71 ? 107 PRO   C CG  1 
ATOM   1899 C  CD  . PRO   B 1 101 ? 29.673 -17.337 3.453  1.00 18.53 ? 107 PRO   C CD  1 
ATOM   1900 N  N   . GLY   B 1 102 ? 26.402 -19.038 4.494  1.00 15.34 ? 108 GLY   C N   1 
ATOM   1901 C  CA  . GLY   B 1 102 ? 25.193 -19.875 4.595  1.00 14.95 ? 108 GLY   C CA  1 
ATOM   1902 C  C   . GLY   B 1 102 ? 25.277 -20.978 5.646  1.00 14.45 ? 108 GLY   C C   1 
ATOM   1903 O  O   . GLY   B 1 102 ? 24.274 -21.616 5.984  1.00 15.77 ? 108 GLY   C O   1 
ATOM   1904 N  N   . ASP   B 1 103 ? 26.501 -21.238 6.149  1.00 13.27 ? 109 ASP   C N   1 
ATOM   1905 C  CA  . ASP   B 1 103 ? 26.693 -22.231 7.193  1.00 12.75 ? 109 ASP   C CA  1 
ATOM   1906 C  C   . ASP   B 1 103 ? 26.303 -21.753 8.579  1.00 12.79 ? 109 ASP   C C   1 
ATOM   1907 O  O   . ASP   B 1 103 ? 26.184 -22.560 9.503  1.00 13.47 ? 109 ASP   C O   1 
ATOM   1908 C  CB  . ASP   B 1 103 ? 28.160 -22.727 7.217  1.00 13.87 ? 109 ASP   C CB  1 
ATOM   1909 C  CG  . ASP   B 1 103 ? 28.459 -23.554 5.997  1.00 15.03 ? 109 ASP   C CG  1 
ATOM   1910 O  OD1 . ASP   B 1 103 ? 27.588 -24.319 5.582  1.00 16.18 ? 109 ASP   C OD1 1 
ATOM   1911 O  OD2 . ASP   B 1 103 ? 29.583 -23.440 5.457  1.00 16.41 ? 109 ASP   C OD2 1 
ATOM   1912 N  N   . CYS   B 1 104 ? 26.084 -20.433 8.758  1.00 12.19 ? 110 CYS   C N   1 
ATOM   1913 C  CA  . CYS   B 1 104 ? 25.678 -19.902 10.069 1.00 12.26 ? 110 CYS   C CA  1 
ATOM   1914 C  C   . CYS   B 1 104 ? 24.428 -20.611 10.574 1.00 12.30 ? 110 CYS   C C   1 
ATOM   1915 O  O   . CYS   B 1 104 ? 23.489 -20.829 9.804  1.00 13.67 ? 110 CYS   C O   1 
ATOM   1916 C  CB  . CYS   B 1 104 ? 25.462 -18.389 10.007 1.00 12.22 ? 110 CYS   C CB  1 
ATOM   1917 S  SG  . CYS   B 1 104 ? 26.985 -17.416 9.897  1.00 14.70 ? 110 CYS   C SG  1 
ATOM   1918 N  N   . GLY   B 1 105 ? 24.439 -20.936 11.854 1.00 10.64 ? 111 GLY   C N   1 
ATOM   1919 C  CA  . GLY   B 1 105 ? 23.302 -21.609 12.477 1.00 11.74 ? 111 GLY   C CA  1 
ATOM   1920 C  C   . GLY   B 1 105 ? 23.505 -23.114 12.624 1.00 11.95 ? 111 GLY   C C   1 
ATOM   1921 O  O   . GLY   B 1 105 ? 22.751 -23.752 13.345 1.00 13.63 ? 111 GLY   C O   1 
ATOM   1922 N  N   . GLY   B 1 106 ? 24.529 -23.694 11.971 1.00 12.49 ? 112 GLY   C N   1 
ATOM   1923 C  CA  . GLY   B 1 106 ? 24.830 -25.126 12.130 1.00 12.41 ? 112 GLY   C CA  1 
ATOM   1924 C  C   . GLY   B 1 106 ? 25.236 -25.406 13.575 1.00 12.01 ? 112 GLY   C C   1 
ATOM   1925 O  O   . GLY   B 1 106 ? 25.954 -24.613 14.195 1.00 12.17 ? 112 GLY   C O   1 
ATOM   1926 N  N   . ILE   B 1 107 ? 24.773 -26.542 14.102 1.00 11.30 ? 113 ILE   C N   1 
ATOM   1927 C  CA  . ILE   B 1 107 ? 25.057 -26.871 15.510 1.00 11.00 ? 113 ILE   C CA  1 
ATOM   1928 C  C   . ILE   B 1 107 ? 26.419 -27.501 15.700 1.00 10.95 ? 113 ILE   C C   1 
ATOM   1929 O  O   . ILE   B 1 107 ? 26.843 -28.371 14.935 1.00 11.33 ? 113 ILE   C O   1 
ATOM   1930 C  CB  . ILE   B 1 107 ? 23.901 -27.795 16.044 1.00 14.05 ? 113 ILE   C CB  1 
ATOM   1931 C  CG1 . ILE   B 1 107 ? 22.661 -26.854 16.403 1.00 17.52 ? 113 ILE   C CG1 1 
ATOM   1932 C  CG2 . ILE   B 1 107 ? 24.349 -28.612 17.294 1.00 14.40 ? 113 ILE   C CG2 1 
ATOM   1933 C  CD1 . ILE   B 1 107 ? 21.358 -27.558 16.866 1.00 20.83 ? 113 ILE   C CD1 1 
ATOM   1934 N  N   . LEU   B 1 108 ? 27.102 -27.039 16.800 1.00 10.15 ? 114 LEU   C N   1 
ATOM   1935 C  CA  . LEU   B 1 108 ? 28.284 -27.705 17.350 1.00 10.34 ? 114 LEU   C CA  1 
ATOM   1936 C  C   . LEU   B 1 108 ? 27.775 -28.463 18.608 1.00 11.16 ? 114 LEU   C C   1 
ATOM   1937 O  O   . LEU   B 1 108 ? 27.109 -27.863 19.457 1.00 10.96 ? 114 LEU   C O   1 
ATOM   1938 C  CB  . LEU   B 1 108 ? 29.332 -26.650 17.743 1.00 10.44 ? 114 LEU   C CB  1 
ATOM   1939 C  CG  . LEU   B 1 108 ? 30.521 -27.180 18.556 1.00 11.78 ? 114 LEU   C CG  1 
ATOM   1940 C  CD1 . LEU   B 1 108 ? 31.412 -28.081 17.674 1.00 13.03 ? 114 LEU   C CD1 1 
ATOM   1941 C  CD2 . LEU   B 1 108 ? 31.370 -26.008 19.082 1.00 12.87 ? 114 LEU   C CD2 1 
ATOM   1942 N  N   . ARG   B 1 109 ? 28.063 -29.779 18.685 1.00 10.40 ? 115 ARG   C N   1 
ATOM   1943 C  CA  . ARG   B 1 109 ? 27.595 -30.564 19.845 1.00 12.32 ? 115 ARG   C CA  1 
ATOM   1944 C  C   . ARG   B 1 109 ? 28.712 -31.410 20.400 1.00 12.69 ? 115 ARG   C C   1 
ATOM   1945 O  O   . ARG   B 1 109 ? 29.648 -31.809 19.682 1.00 12.30 ? 115 ARG   C O   1 
ATOM   1946 C  CB  . ARG   B 1 109 ? 26.435 -31.481 19.431 1.00 15.87 ? 115 ARG   C CB  1 
ATOM   1947 C  CG  . ARG   B 1 109 ? 26.817 -32.503 18.381 1.00 19.70 ? 115 ARG   C CG  1 
ATOM   1948 C  CD  . ARG   B 1 109 ? 25.585 -33.344 18.016 1.00 26.84 ? 115 ARG   C CD  1 
ATOM   1949 N  NE  . ARG   B 1 109 ? 24.682 -32.640 17.092 1.00 32.73 ? 115 ARG   C NE  1 
ATOM   1950 C  CZ  . ARG   B 1 109 ? 23.426 -32.283 17.380 1.00 40.63 ? 115 ARG   C CZ  1 
ATOM   1951 N  NH1 . ARG   B 1 109 ? 22.917 -32.522 18.590 1.00 42.01 ? 115 ARG   C NH1 1 
ATOM   1952 N  NH2 . ARG   B 1 109 ? 22.684 -31.652 16.476 1.00 42.18 ? 115 ARG   C NH2 1 
ATOM   1953 N  N   . CYS   B 1 110 ? 28.605 -31.666 21.696 1.00 12.13 ? 116 CYS   C N   1 
ATOM   1954 C  CA  . CYS   B 1 110 ? 29.549 -32.552 22.403 1.00 12.86 ? 116 CYS   C CA  1 
ATOM   1955 C  C   . CYS   B 1 110 ? 28.713 -33.657 23.085 1.00 14.99 ? 116 CYS   C C   1 
ATOM   1956 O  O   . CYS   B 1 110 ? 27.481 -33.739 22.877 1.00 14.78 ? 116 CYS   C O   1 
ATOM   1957 C  CB  . CYS   B 1 110 ? 30.361 -31.751 23.411 1.00 11.76 ? 116 CYS   C CB  1 
ATOM   1958 S  SG  . CYS   B 1 110 ? 29.356 -31.108 24.782 1.00 13.03 ? 116 CYS   C SG  1 
ATOM   1959 N  N   . GLN   B 1 111 ? 29.356 -34.489 23.962 1.00 15.68 ? 117 GLN   C N   1 
ATOM   1960 C  CA  . GLN   B 1 111 ? 28.582 -35.537 24.637 1.00 17.62 ? 117 GLN   C CA  1 
ATOM   1961 C  C   . GLN   B 1 111 ? 27.502 -34.970 25.576 1.00 17.29 ? 117 GLN   C C   1 
ATOM   1962 O  O   . GLN   B 1 111 ? 26.545 -35.682 25.921 1.00 18.59 ? 117 GLN   C O   1 
ATOM   1963 C  CB  . GLN   B 1 111 ? 29.521 -36.484 25.437 1.00 19.20 ? 117 GLN   C CB  1 
ATOM   1964 C  CG  . GLN   B 1 111 ? 30.136 -35.803 26.662 1.00 23.96 ? 117 GLN   C CG  1 
ATOM   1965 C  CD  . GLN   B 1 111 ? 31.157 -36.641 27.396 1.00 33.79 ? 117 GLN   C CD  1 
ATOM   1966 O  OE1 . GLN   B 1 111 ? 32.351 -36.618 27.071 1.00 36.93 ? 117 GLN   C OE1 1 
ATOM   1967 N  NE2 . GLN   B 1 111 ? 30.708 -37.354 28.419 1.00 33.99 ? 117 GLN   C NE2 1 
ATOM   1968 N  N   . HIS   B 1 112 ? 27.603 -33.675 25.962 1.00 15.40 ? 118 HIS   C N   1 
ATOM   1969 C  CA  . HIS   B 1 112 ? 26.634 -33.103 26.898 1.00 15.45 ? 118 HIS   C CA  1 
ATOM   1970 C  C   . HIS   B 1 112 ? 25.462 -32.398 26.216 1.00 15.82 ? 118 HIS   C C   1 
ATOM   1971 O  O   . HIS   B 1 112 ? 24.514 -32.024 26.899 1.00 16.71 ? 118 HIS   C O   1 
ATOM   1972 C  CB  . HIS   B 1 112 ? 27.354 -32.149 27.861 1.00 15.86 ? 118 HIS   C CB  1 
ATOM   1973 C  CG  . HIS   B 1 112 ? 28.537 -32.776 28.543 1.00 14.64 ? 118 HIS   C CG  1 
ATOM   1974 N  ND1 . HIS   B 1 112 ? 29.835 -32.430 28.221 1.00 15.48 ? 118 HIS   C ND1 1 
ATOM   1975 C  CD2 . HIS   B 1 112 ? 28.573 -33.618 29.603 1.00 17.63 ? 118 HIS   C CD2 1 
ATOM   1976 C  CE1 . HIS   B 1 112 ? 30.616 -33.174 28.967 1.00 17.26 ? 118 HIS   C CE1 1 
ATOM   1977 N  NE2 . HIS   B 1 112 ? 29.901 -33.863 29.858 1.00 17.85 ? 118 HIS   C NE2 1 
ATOM   1978 N  N   . GLY   B 1 113 ? 25.542 -32.173 24.905 1.00 14.61 ? 119 GLY   C N   1 
ATOM   1979 C  CA  . GLY   B 1 113 ? 24.471 -31.483 24.205 1.00 14.59 ? 119 GLY   C CA  1 
ATOM   1980 C  C   . GLY   B 1 113 ? 25.005 -30.410 23.263 1.00 12.45 ? 119 GLY   C C   1 
ATOM   1981 O  O   . GLY   B 1 113 ? 26.123 -30.506 22.748 1.00 12.93 ? 119 GLY   C O   1 
ATOM   1982 N  N   . VAL   B 1 114 ? 24.156 -29.399 22.979 1.00 12.16 ? 120 VAL   C N   1 
ATOM   1983 C  CA  . VAL   B 1 114 ? 24.493 -28.325 22.047 1.00 12.41 ? 120 VAL   C CA  1 
ATOM   1984 C  C   . VAL   B 1 114 ? 25.426 -27.304 22.709 1.00 12.21 ? 120 VAL   C C   1 
ATOM   1985 O  O   . VAL   B 1 114 ? 25.128 -26.761 23.794 1.00 13.35 ? 120 VAL   C O   1 
ATOM   1986 C  CB  . VAL   B 1 114 ? 23.198 -27.631 21.553 1.00 13.76 ? 120 VAL   C CB  1 
ATOM   1987 C  CG1 . VAL   B 1 114 ? 23.552 -26.415 20.678 1.00 15.19 ? 120 VAL   C CG1 1 
ATOM   1988 C  CG2 . VAL   B 1 114 ? 22.280 -28.625 20.807 1.00 14.72 ? 120 VAL   C CG2 1 
ATOM   1989 N  N   . VAL   B 1 115 ? 26.598 -27.086 22.090 1.00 11.07 ? 121 VAL   C N   1 
ATOM   1990 C  CA  . VAL   B 1 115 ? 27.625 -26.152 22.588 1.00 11.40 ? 121 VAL   C CA  1 
ATOM   1991 C  C   . VAL   B 1 115 ? 27.402 -24.755 22.071 1.00 12.20 ? 121 VAL   C C   1 
ATOM   1992 O  O   . VAL   B 1 115 ? 27.626 -23.766 22.778 1.00 12.85 ? 121 VAL   C O   1 
ATOM   1993 C  CB  . VAL   B 1 115 ? 29.020 -26.691 22.184 1.00 11.82 ? 121 VAL   C CB  1 
ATOM   1994 C  CG1 . VAL   B 1 115 ? 30.106 -25.686 22.537 1.00 12.99 ? 121 VAL   C CG1 1 
ATOM   1995 C  CG2 . VAL   B 1 115 ? 29.279 -28.051 22.811 1.00 13.47 ? 121 VAL   C CG2 1 
ATOM   1996 N  N   . GLY   B 1 116 ? 27.070 -24.669 20.791 1.00 11.56 ? 122 GLY   C N   1 
ATOM   1997 C  CA  . GLY   B 1 116 ? 26.838 -23.364 20.171 1.00 12.45 ? 122 GLY   C CA  1 
ATOM   1998 C  C   . GLY   B 1 116 ? 26.493 -23.517 18.712 1.00 11.19 ? 122 GLY   C C   1 
ATOM   1999 O  O   . GLY   B 1 116 ? 26.171 -24.628 18.284 1.00 11.68 ? 122 GLY   C O   1 
ATOM   2000 N  N   . ILE   B 1 117 ? 26.464 -22.377 17.987 1.00 10.68 ? 123 ILE   C N   1 
ATOM   2001 C  CA  . ILE   B 1 117 ? 26.117 -22.417 16.564 1.00 10.85 ? 123 ILE   C CA  1 
ATOM   2002 C  C   . ILE   B 1 117 ? 27.172 -21.686 15.747 1.00 10.64 ? 123 ILE   C C   1 
ATOM   2003 O  O   . ILE   B 1 117 ? 27.794 -20.714 16.204 1.00 11.63 ? 123 ILE   C O   1 
ATOM   2004 C  CB  . ILE   B 1 117 ? 24.718 -21.791 16.294 1.00 12.39 ? 123 ILE   C CB  1 
ATOM   2005 C  CG1 . ILE   B 1 117 ? 24.603 -20.376 16.910 1.00 13.78 ? 123 ILE   C CG1 1 
ATOM   2006 C  CG2 . ILE   B 1 117 ? 23.596 -22.731 16.743 1.00 13.26 ? 123 ILE   C CG2 1 
ATOM   2007 C  CD1 . ILE   B 1 117 ? 23.252 -19.592 16.535 1.00 14.28 ? 123 ILE   C CD1 1 
ATOM   2008 N  N   . VAL   B 1 118 ? 27.334 -22.116 14.476 1.00 10.68 ? 124 VAL   C N   1 
ATOM   2009 C  CA  . VAL   B 1 118 ? 28.269 -21.440 13.572 1.00 11.41 ? 124 VAL   C CA  1 
ATOM   2010 C  C   . VAL   B 1 118 ? 27.901 -19.948 13.442 1.00 11.60 ? 124 VAL   C C   1 
ATOM   2011 O  O   . VAL   B 1 118 ? 26.710 -19.612 13.288 1.00 11.38 ? 124 VAL   C O   1 
ATOM   2012 C  CB  . VAL   B 1 118 ? 28.266 -22.098 12.182 1.00 11.53 ? 124 VAL   C CB  1 
ATOM   2013 C  CG1 . VAL   B 1 118 ? 29.135 -21.310 11.193 1.00 12.23 ? 124 VAL   C CG1 1 
ATOM   2014 C  CG2 . VAL   B 1 118 ? 28.732 -23.572 12.247 1.00 11.71 ? 124 VAL   C CG2 1 
ATOM   2015 N  N   . SER   B 1 119 ? 28.910 -19.062 13.532 1.00 11.60 ? 125 SER   C N   1 
ATOM   2016 C  CA  . SER   B 1 119 ? 28.706 -17.610 13.434 1.00 11.71 ? 125 SER   C CA  1 
ATOM   2017 C  C   . SER   B 1 119 ? 29.725 -16.919 12.530 1.00 12.51 ? 125 SER   C C   1 
ATOM   2018 O  O   . SER   B 1 119 ? 29.400 -15.853 11.987 1.00 13.20 ? 125 SER   C O   1 
ATOM   2019 C  CB  . SER   B 1 119 ? 28.767 -17.009 14.840 1.00 12.97 ? 125 SER   C CB  1 
ATOM   2020 O  OG  . SER   B 1 119 ? 28.627 -15.582 14.788 1.00 13.76 ? 125 SER   C OG  1 
ATOM   2021 N  N   . THR   B 1 120 ? 30.971 -17.466 12.399 1.00 12.63 ? 126 THR   C N   1 
ATOM   2022 C  CA  . THR   B 1 120 ? 32.016 -16.808 11.590 1.00 12.69 ? 126 THR   C CA  1 
ATOM   2023 C  C   . THR   B 1 120 ? 32.700 -17.824 10.681 1.00 12.57 ? 126 THR   C C   1 
ATOM   2024 O  O   . THR   B 1 120 ? 32.621 -19.053 10.913 1.00 12.10 ? 126 THR   C O   1 
ATOM   2025 C  CB  . THR   B 1 120 ? 33.075 -16.065 12.459 1.00 13.11 ? 126 THR   C CB  1 
ATOM   2026 O  OG1 . THR   B 1 120 ? 33.920 -17.027 13.094 1.00 14.23 ? 126 THR   C OG1 1 
ATOM   2027 C  CG2 . THR   B 1 120 ? 32.452 -15.120 13.459 1.00 14.40 ? 126 THR   C CG2 1 
ATOM   2028 N  N   . GLY   B 1 121 ? 33.394 -17.319 9.669  1.00 14.35 ? 127 GLY   C N   1 
ATOM   2029 C  CA  . GLY   B 1 121 ? 34.143 -18.160 8.736  1.00 15.96 ? 127 GLY   C CA  1 
ATOM   2030 C  C   . GLY   B 1 121 ? 35.189 -17.386 7.974  1.00 19.69 ? 127 GLY   C C   1 
ATOM   2031 O  O   . GLY   B 1 121 ? 35.081 -16.180 7.814  1.00 21.06 ? 127 GLY   C O   1 
ATOM   2032 N  N   . GLY   B 1 122 ? 36.112 -18.100 7.373  1.00 21.95 ? 128 GLY   C N   1 
ATOM   2033 C  CA  . GLY   B 1 122 ? 37.190 -17.476 6.604  1.00 23.71 ? 128 GLY   C CA  1 
ATOM   2034 C  C   . GLY   B 1 122 ? 38.580 -17.854 7.092  1.00 24.13 ? 128 GLY   C C   1 
ATOM   2035 O  O   . GLY   B 1 122 ? 38.770 -18.259 8.232  1.00 24.22 ? 128 GLY   C O   1 
ATOM   2036 N  N   . ASN   B 1 123 ? 39.578 -17.732 6.215  1.00 23.41 ? 129 ASN   C N   1 
ATOM   2037 C  CA  . ASN   B 1 123 ? 40.968 -18.080 6.551  1.00 24.89 ? 129 ASN   C CA  1 
ATOM   2038 C  C   . ASN   B 1 123 ? 41.124 -19.561 6.985  1.00 22.78 ? 129 ASN   C C   1 
ATOM   2039 O  O   . ASN   B 1 123 ? 42.092 -19.888 7.682  1.00 25.30 ? 129 ASN   C O   1 
ATOM   2040 C  CB  . ASN   B 1 123 ? 41.500 -17.168 7.676  1.00 29.62 ? 129 ASN   C CB  1 
ATOM   2041 C  CG  . ASN   B 1 123 ? 42.099 -15.861 7.226  1.00 38.06 ? 129 ASN   C CG  1 
ATOM   2042 O  OD1 . ASN   B 1 123 ? 42.933 -15.816 6.311  1.00 39.18 ? 129 ASN   C OD1 1 
ATOM   2043 N  ND2 . ASN   B 1 123 ? 41.720 -14.761 7.884  1.00 42.00 ? 129 ASN   C ND2 1 
ATOM   2044 N  N   . GLY   B 1 124 ? 40.207 -20.434 6.561  1.00 20.09 ? 130 GLY   C N   1 
ATOM   2045 C  CA  . GLY   B 1 124 ? 40.255 -21.846 6.951  1.00 18.77 ? 130 GLY   C CA  1 
ATOM   2046 C  C   . GLY   B 1 124 ? 39.861 -22.116 8.390  1.00 17.22 ? 130 GLY   C C   1 
ATOM   2047 O  O   . GLY   B 1 124 ? 40.111 -23.221 8.889  1.00 17.50 ? 130 GLY   C O   1 
ATOM   2048 N  N   . LEU   B 1 125 ? 39.208 -21.121 9.037  1.00 16.13 ? 131 LEU   C N   1 
ATOM   2049 C  CA  . LEU   B 1 125 ? 38.726 -21.255 10.409 1.00 15.99 ? 131 LEU   C CA  1 
ATOM   2050 C  C   . LEU   B 1 125 ? 37.208 -21.108 10.443 1.00 16.25 ? 131 LEU   C C   1 
ATOM   2051 O  O   . LEU   B 1 125 ? 36.606 -20.406 9.608  1.00 18.38 ? 131 LEU   C O   1 
ATOM   2052 C  CB  . LEU   B 1 125 ? 39.344 -20.183 11.315 1.00 17.79 ? 131 LEU   C CB  1 
ATOM   2053 C  CG  . LEU   B 1 125 ? 40.886 -20.208 11.338 1.00 20.37 ? 131 LEU   C CG  1 
ATOM   2054 C  CD1 . LEU   B 1 125 ? 41.468 -18.860 11.748 1.00 24.00 ? 131 LEU   C CD1 1 
ATOM   2055 C  CD2 . LEU   B 1 125 ? 41.387 -21.384 12.144 1.00 20.88 ? 131 LEU   C CD2 1 
ATOM   2056 N  N   . VAL   B 1 126 ? 36.580 -21.810 11.370 1.00 13.03 ? 132 VAL   C N   1 
ATOM   2057 C  CA  . VAL   B 1 126 ? 35.140 -21.693 11.599 1.00 11.97 ? 132 VAL   C CA  1 
ATOM   2058 C  C   . VAL   B 1 126 ? 34.986 -21.212 13.070 1.00 11.97 ? 132 VAL   C C   1 
ATOM   2059 O  O   . VAL   B 1 126 ? 35.670 -21.700 13.981 1.00 12.16 ? 132 VAL   C O   1 
ATOM   2060 C  CB  . VAL   B 1 126 ? 34.381 -23.030 11.367 1.00 12.35 ? 132 VAL   C CB  1 
ATOM   2061 C  CG1 . VAL   B 1 126 ? 35.022 -24.211 12.062 1.00 14.53 ? 132 VAL   C CG1 1 
ATOM   2062 C  CG2 . VAL   B 1 126 ? 32.897 -22.909 11.759 1.00 12.69 ? 132 VAL   C CG2 1 
ATOM   2063 N  N   . GLY   B 1 127 ? 34.108 -20.239 13.273 1.00 11.62 ? 133 GLY   C N   1 
ATOM   2064 C  CA  . GLY   B 1 127 ? 33.855 -19.728 14.626 1.00 11.39 ? 133 GLY   C CA  1 
ATOM   2065 C  C   . GLY   B 1 127 ? 32.434 -20.029 15.070 1.00 11.36 ? 133 GLY   C C   1 
ATOM   2066 O  O   . GLY   B 1 127 ? 31.482 -19.873 14.284 1.00 11.71 ? 133 GLY   C O   1 
ATOM   2067 N  N   . PHE   B 1 128 ? 32.303 -20.415 16.328 1.00 10.40 ? 134 PHE   C N   1 
ATOM   2068 C  CA  . PHE   B 1 128 ? 31.021 -20.769 16.939 1.00 10.80 ? 134 PHE   C CA  1 
ATOM   2069 C  C   . PHE   B 1 128 ? 30.690 -19.829 18.079 1.00 11.31 ? 134 PHE   C C   1 
ATOM   2070 O  O   . PHE   B 1 128 ? 31.537 -19.577 18.949 1.00 11.81 ? 134 PHE   C O   1 
ATOM   2071 C  CB  . PHE   B 1 128 ? 31.081 -22.213 17.519 1.00 11.15 ? 134 PHE   C CB  1 
ATOM   2072 C  CG  . PHE   B 1 128 ? 31.615 -23.241 16.540 1.00 11.03 ? 134 PHE   C CG  1 
ATOM   2073 C  CD1 . PHE   B 1 128 ? 30.773 -23.845 15.618 1.00 11.39 ? 134 PHE   C CD1 1 
ATOM   2074 C  CD2 . PHE   B 1 128 ? 32.955 -23.609 16.553 1.00 11.98 ? 134 PHE   C CD2 1 
ATOM   2075 C  CE1 . PHE   B 1 128 ? 31.252 -24.807 14.748 1.00 12.07 ? 134 PHE   C CE1 1 
ATOM   2076 C  CE2 . PHE   B 1 128 ? 33.451 -24.564 15.654 1.00 12.41 ? 134 PHE   C CE2 1 
ATOM   2077 C  CZ  . PHE   B 1 128 ? 32.606 -25.156 14.752 1.00 12.01 ? 134 PHE   C CZ  1 
ATOM   2078 N  N   . ALA   B 1 129 ? 29.434 -19.341 18.102 1.00 11.47 ? 135 ALA   C N   1 
ATOM   2079 C  CA  . ALA   B 1 129 ? 28.931 -18.555 19.237 1.00 11.26 ? 135 ALA   C CA  1 
ATOM   2080 C  C   . ALA   B 1 129 ? 28.526 -19.527 20.367 1.00 12.35 ? 135 ALA   C C   1 
ATOM   2081 O  O   . ALA   B 1 129 ? 27.633 -20.372 20.182 1.00 12.49 ? 135 ALA   C O   1 
ATOM   2082 C  CB  . ALA   B 1 129 ? 27.700 -17.728 18.796 1.00 12.16 ? 135 ALA   C CB  1 
ATOM   2083 N  N   . ASP   B 1 130 ? 29.219 -19.448 21.501 1.00 11.92 ? 136 ASP   C N   1 
ATOM   2084 C  CA  . ASP   B 1 130 ? 28.946 -20.303 22.644 1.00 12.37 ? 136 ASP   C CA  1 
ATOM   2085 C  C   . ASP   B 1 130 ? 27.603 -19.976 23.257 1.00 12.86 ? 136 ASP   C C   1 
ATOM   2086 O  O   . ASP   B 1 130 ? 27.207 -18.797 23.315 1.00 13.53 ? 136 ASP   C O   1 
ATOM   2087 C  CB  . ASP   B 1 130 ? 30.025 -20.083 23.708 1.00 13.97 ? 136 ASP   C CB  1 
ATOM   2088 C  CG  . ASP   B 1 130 ? 29.912 -20.994 24.895 1.00 17.44 ? 136 ASP   C CG  1 
ATOM   2089 O  OD1 . ASP   B 1 130 ? 29.784 -22.216 24.699 1.00 15.79 ? 136 ASP   C OD1 1 
ATOM   2090 O  OD2 . ASP   B 1 130 ? 29.920 -20.475 26.048 1.00 20.91 ? 136 ASP   C OD2 1 
ATOM   2091 N  N   . VAL   B 1 131 ? 26.882 -20.998 23.728 1.00 12.41 ? 137 VAL   C N   1 
ATOM   2092 C  CA  . VAL   B 1 131 ? 25.648 -20.782 24.500 1.00 12.52 ? 137 VAL   C CA  1 
ATOM   2093 C  C   . VAL   B 1 131 ? 25.718 -21.452 25.880 1.00 13.45 ? 137 VAL   C C   1 
ATOM   2094 O  O   . VAL   B 1 131 ? 24.733 -21.405 26.627 1.00 13.57 ? 137 VAL   C O   1 
ATOM   2095 C  CB  . VAL   B 1 131 ? 24.383 -21.246 23.742 1.00 13.11 ? 137 VAL   C CB  1 
ATOM   2096 C  CG1 . VAL   B 1 131 ? 24.189 -20.437 22.434 1.00 13.26 ? 137 VAL   C CG1 1 
ATOM   2097 C  CG2 . VAL   B 1 131 ? 24.431 -22.742 23.465 1.00 13.23 ? 137 VAL   C CG2 1 
ATOM   2098 N  N   . ARG   B 1 132 ? 26.832 -22.112 26.225 1.00 12.74 ? 138 ARG   C N   1 
ATOM   2099 C  CA  . ARG   B 1 132 ? 26.906 -22.889 27.487 1.00 12.34 ? 138 ARG   C CA  1 
ATOM   2100 C  C   . ARG   B 1 132 ? 26.846 -22.056 28.743 1.00 13.71 ? 138 ARG   C C   1 
ATOM   2101 O  O   . ARG   B 1 132 ? 26.534 -22.617 29.802 1.00 15.09 ? 138 ARG   C O   1 
ATOM   2102 C  CB  . ARG   B 1 132 ? 28.171 -23.740 27.479 1.00 12.39 ? 138 ARG   C CB  1 
ATOM   2103 C  CG  . ARG   B 1 132 ? 28.158 -24.793 26.374 1.00 12.15 ? 138 ARG   C CG  1 
ATOM   2104 C  CD  . ARG   B 1 132 ? 29.457 -25.580 26.391 1.00 12.70 ? 138 ARG   C CD  1 
ATOM   2105 N  NE  . ARG   B 1 132 ? 30.569 -24.698 25.993 1.00 12.53 ? 138 ARG   C NE  1 
ATOM   2106 C  CZ  . ARG   B 1 132 ? 31.811 -25.105 25.811 1.00 14.08 ? 138 ARG   C CZ  1 
ATOM   2107 N  NH1 . ARG   B 1 132 ? 32.169 -26.349 26.134 1.00 14.15 ? 138 ARG   C NH1 1 
ATOM   2108 N  NH2 . ARG   B 1 132 ? 32.730 -24.260 25.370 1.00 15.09 ? 138 ARG   C NH2 1 
ATOM   2109 N  N   . ASP   B 1 133 ? 27.136 -20.746 28.665 1.00 13.34 ? 139 ASP   C N   1 
ATOM   2110 C  CA  . ASP   B 1 133 ? 27.071 -19.884 29.843 1.00 14.13 ? 139 ASP   C CA  1 
ATOM   2111 C  C   . ASP   B 1 133 ? 25.638 -19.335 30.070 1.00 15.13 ? 139 ASP   C C   1 
ATOM   2112 O  O   . ASP   B 1 133 ? 25.400 -18.717 31.113 1.00 16.54 ? 139 ASP   C O   1 
ATOM   2113 C  CB  . ASP   B 1 133 ? 28.046 -18.693 29.710 1.00 15.57 ? 139 ASP   C CB  1 
ATOM   2114 C  CG  . ASP   B 1 133 ? 27.682 -17.768 28.557 1.00 18.19 ? 139 ASP   C CG  1 
ATOM   2115 O  OD1 . ASP   B 1 133 ? 27.340 -18.281 27.469 1.00 16.71 ? 139 ASP   C OD1 1 
ATOM   2116 O  OD2 . ASP   B 1 133 ? 27.687 -16.510 28.757 1.00 20.13 ? 139 ASP   C OD2 1 
ATOM   2117 N  N   . LEU   B 1 134 ? 24.701 -19.541 29.107 1.00 14.67 ? 140 LEU   C N   1 
ATOM   2118 C  CA  . LEU   B 1 134 ? 23.342 -18.989 29.200 1.00 14.33 ? 140 LEU   C CA  1 
ATOM   2119 C  C   . LEU   B 1 134 ? 22.466 -19.975 29.981 1.00 14.53 ? 140 LEU   C C   1 
ATOM   2120 O  O   . LEU   B 1 134 ? 21.646 -20.713 29.417 1.00 14.65 ? 140 LEU   C O   1 
ATOM   2121 C  CB  . LEU   B 1 134 ? 22.798 -18.752 27.771 1.00 13.92 ? 140 LEU   C CB  1 
ATOM   2122 C  CG  . LEU   B 1 134 ? 23.663 -17.806 26.918 1.00 14.89 ? 140 LEU   C CG  1 
ATOM   2123 C  CD1 . LEU   B 1 134 ? 23.088 -17.698 25.481 1.00 15.54 ? 140 LEU   C CD1 1 
ATOM   2124 C  CD2 . LEU   B 1 134 ? 23.764 -16.412 27.556 1.00 16.09 ? 140 LEU   C CD2 1 
ATOM   2125 N  N   . LEU   B 1 135 ? 22.686 -20.027 31.320 1.00 15.28 ? 141 LEU   C N   1 
ATOM   2126 C  CA  . LEU   B 1 135 ? 22.033 -21.047 32.137 1.00 15.98 ? 141 LEU   C CA  1 
ATOM   2127 C  C   . LEU   B 1 135 ? 20.524 -20.918 32.179 1.00 16.15 ? 141 LEU   C C   1 
ATOM   2128 O  O   . LEU   B 1 135 ? 19.828 -21.923 32.372 1.00 17.09 ? 141 LEU   C O   1 
ATOM   2129 C  CB  . LEU   B 1 135 ? 22.618 -21.088 33.575 1.00 16.01 ? 141 LEU   C CB  1 
ATOM   2130 C  CG  . LEU   B 1 135 ? 24.172 -21.069 33.665 1.00 19.10 ? 141 LEU   C CG  1 
ATOM   2131 C  CD1 . LEU   B 1 135 ? 24.654 -21.223 35.134 1.00 19.94 ? 141 LEU   C CD1 1 
ATOM   2132 C  CD2 . LEU   B 1 135 ? 24.837 -22.130 32.807 1.00 19.49 ? 141 LEU   C CD2 1 
ATOM   2133 N  N   . TRP   B 1 136 ? 20.032 -19.684 31.994 1.00 16.07 ? 142 TRP   C N   1 
ATOM   2134 C  CA  . TRP   B 1 136 ? 18.593 -19.408 32.034 1.00 16.87 ? 142 TRP   C CA  1 
ATOM   2135 C  C   . TRP   B 1 136 ? 17.850 -20.106 30.886 1.00 17.55 ? 142 TRP   C C   1 
ATOM   2136 O  O   . TRP   B 1 136 ? 16.623 -20.211 30.960 1.00 19.40 ? 142 TRP   C O   1 
ATOM   2137 C  CB  . TRP   B 1 136 ? 18.342 -17.891 32.030 1.00 16.91 ? 142 TRP   C CB  1 
ATOM   2138 C  CG  . TRP   B 1 136 ? 19.016 -17.153 30.913 1.00 16.59 ? 142 TRP   C CG  1 
ATOM   2139 C  CD1 . TRP   B 1 136 ? 20.217 -16.501 30.958 1.00 17.54 ? 142 TRP   C CD1 1 
ATOM   2140 C  CD2 . TRP   B 1 136 ? 18.499 -16.956 29.577 1.00 16.57 ? 142 TRP   C CD2 1 
ATOM   2141 N  NE1 . TRP   B 1 136 ? 20.498 -15.937 29.719 1.00 18.47 ? 142 TRP   C NE1 1 
ATOM   2142 C  CE2 . TRP   B 1 136 ? 19.448 -16.189 28.866 1.00 17.72 ? 142 TRP   C CE2 1 
ATOM   2143 C  CE3 . TRP   B 1 136 ? 17.324 -17.339 28.936 1.00 17.25 ? 142 TRP   C CE3 1 
ATOM   2144 C  CZ2 . TRP   B 1 136 ? 19.256 -15.811 27.532 1.00 17.24 ? 142 TRP   C CZ2 1 
ATOM   2145 C  CZ3 . TRP   B 1 136 ? 17.107 -16.917 27.637 1.00 18.13 ? 142 TRP   C CZ3 1 
ATOM   2146 C  CH2 . TRP   B 1 136 ? 18.080 -16.187 26.941 1.00 17.72 ? 142 TRP   C CH2 1 
ATOM   2147 N  N   . LEU   B 1 137 ? 18.550 -20.593 29.831 1.00 16.63 ? 143 LEU   C N   1 
ATOM   2148 C  CA  . LEU   B 1 137 ? 17.862 -21.343 28.773 1.00 17.36 ? 143 LEU   C CA  1 
ATOM   2149 C  C   . LEU   B 1 137 ? 17.234 -22.639 29.328 1.00 19.67 ? 143 LEU   C C   1 
ATOM   2150 O  O   . LEU   B 1 137 ? 16.298 -23.162 28.722 1.00 21.09 ? 143 LEU   C O   1 
ATOM   2151 C  CB  . LEU   B 1 137 ? 18.811 -21.700 27.618 1.00 16.90 ? 143 LEU   C CB  1 
ATOM   2152 C  CG  . LEU   B 1 137 ? 19.272 -20.533 26.745 1.00 16.16 ? 143 LEU   C CG  1 
ATOM   2153 C  CD1 . LEU   B 1 137 ? 20.441 -20.953 25.832 1.00 17.02 ? 143 LEU   C CD1 1 
ATOM   2154 C  CD2 . LEU   B 1 137 ? 18.117 -19.980 25.887 1.00 17.49 ? 143 LEU   C CD2 1 
ATOM   2155 N  N   . ASP   B 1 138 ? 17.752 -23.162 30.467 1.00 19.70 ? 144 ASP   C N   1 
ATOM   2156 C  CA  . ASP   B 1 138 ? 17.256 -24.408 31.067 1.00 21.62 ? 144 ASP   C CA  1 
ATOM   2157 C  C   . ASP   B 1 138 ? 16.038 -24.230 31.977 1.00 24.42 ? 144 ASP   C C   1 
ATOM   2158 O  O   . ASP   B 1 138 ? 15.557 -25.234 32.499 1.00 25.39 ? 144 ASP   C O   1 
ATOM   2159 C  CB  . ASP   B 1 138 ? 18.350 -25.099 31.903 1.00 21.59 ? 144 ASP   C CB  1 
ATOM   2160 C  CG  . ASP   B 1 138 ? 19.609 -25.469 31.132 1.00 22.43 ? 144 ASP   C CG  1 
ATOM   2161 O  OD1 . ASP   B 1 138 ? 19.557 -25.507 29.889 1.00 22.84 ? 144 ASP   C OD1 1 
ATOM   2162 O  OD2 . ASP   B 1 138 ? 20.643 -25.721 31.783 1.00 24.94 ? 144 ASP   C OD2 1 
ATOM   2163 N  N   . GLU   B 1 139 ? 15.549 -23.006 32.169 1.00 26.03 ? 145 GLU   C N   1 
ATOM   2164 C  CA  . GLU   B 1 139 ? 14.443 -22.767 33.096 1.00 30.18 ? 145 GLU   C CA  1 
ATOM   2165 C  C   . GLU   B 1 139 ? 13.361 -21.828 32.524 1.00 34.27 ? 145 GLU   C C   1 
ATOM   2166 O  O   . GLU   B 1 139 ? 13.536 -21.269 31.446 1.00 34.47 ? 145 GLU   C O   1 
ATOM   2167 C  CB  . GLU   B 1 139 ? 15.033 -22.196 34.408 1.00 34.20 ? 145 GLU   C CB  1 
ATOM   2168 C  CG  . GLU   B 1 139 ? 15.817 -20.914 34.180 1.00 41.79 ? 145 GLU   C CG  1 
ATOM   2169 C  CD  . GLU   B 1 139 ? 16.737 -20.455 35.295 1.00 49.78 ? 145 GLU   C CD  1 
ATOM   2170 O  OE1 . GLU   B 1 139 ? 16.958 -19.226 35.412 1.00 50.53 ? 145 GLU   C OE1 1 
ATOM   2171 O  OE2 . GLU   B 1 139 ? 17.235 -21.320 36.050 1.00 52.09 ? 145 GLU   C OE2 1 
ATOM   2172 N  N   . GLU   B 1 140 ? 12.256 -21.638 33.285 1.00 37.20 ? 146 GLU   C N   1 
ATOM   2173 C  CA  . GLU   B 1 140 ? 11.118 -20.755 32.987 1.00 40.45 ? 146 GLU   C CA  1 
ATOM   2174 C  C   . GLU   B 1 140 ? 10.156 -21.385 31.994 1.00 43.37 ? 146 GLU   C C   1 
ATOM   2175 O  O   . GLU   B 1 140 ? 8.967  -21.504 32.314 1.00 44.98 ? 146 GLU   C O   1 
ATOM   2176 C  CB  . GLU   B 1 140 ? 11.556 -19.339 32.567 1.00 42.53 ? 146 GLU   C CB  1 
ATOM   2177 C  CG  . GLU   B 1 140 ? 10.480 -18.451 31.962 1.00 48.95 ? 146 GLU   C CG  1 
ATOM   2178 C  CD  . GLU   B 1 140 ? 9.779  -17.538 32.955 1.00 57.02 ? 146 GLU   C CD  1 
ATOM   2179 O  OE1 . GLU   B 1 140 ? 10.324 -16.449 33.247 1.00 58.36 ? 146 GLU   C OE1 1 
ATOM   2180 O  OE2 . GLU   B 1 140 ? 8.682  -17.907 33.434 1.00 59.65 ? 146 GLU   C OE2 1 
HETATM 2181 N  N1  . A1B2W C 2 .   ? 8.762  15.679  21.638 1.00 31.81 ? 201 A1B2W A N1  1 
HETATM 2182 C  C4  . A1B2W C 2 .   ? 9.747  16.394  22.467 1.00 31.87 ? 201 A1B2W A C4  1 
HETATM 2183 C  C5  . A1B2W C 2 .   ? 7.876  14.800  22.144 1.00 31.73 ? 201 A1B2W A C5  1 
HETATM 2184 C  C6  . A1B2W C 2 .   ? 7.680  14.516  23.654 1.00 33.28 ? 201 A1B2W A C6  1 
HETATM 2185 C  C7  . A1B2W C 2 .   ? 6.722  15.559  24.243 1.00 33.61 ? 201 A1B2W A C7  1 
HETATM 2186 C  C8  . A1B2W C 2 .   ? 6.397  15.380  25.717 1.00 34.09 ? 201 A1B2W A C8  1 
HETATM 2187 C  C10 . A1B2W C 2 .   ? 7.142  13.096  23.873 1.00 33.59 ? 201 A1B2W A C10 1 
HETATM 2188 O  O1  . A1B2W C 2 .   ? 7.076  14.260  21.410 1.00 31.06 ? 201 A1B2W A O1  1 
HETATM 2189 C  C3  . A1B2W C 2 .   ? 11.149 16.301  21.882 1.00 31.68 ? 201 A1B2W A C3  1 
HETATM 2190 C  C2  . A1B2W C 2 .   ? 11.152 16.752  20.425 1.00 30.32 ? 201 A1B2W A C2  1 
HETATM 2191 C  C11 . A1B2W C 2 .   ? 8.744  16.075  20.225 1.00 30.66 ? 201 A1B2W A C11 1 
HETATM 2192 C  C1  . A1B2W C 2 .   ? 10.136 15.936  19.606 1.00 29.38 ? 201 A1B2W A C1  1 
HETATM 2193 C  C   . A1B2W C 2 .   ? 10.188 16.306  18.134 1.00 28.34 ? 201 A1B2W A C   1 
HETATM 2194 O  O   . A1B2W C 2 .   ? 9.666  17.345  17.723 1.00 28.97 ? 201 A1B2W A O   1 
HETATM 2195 N  N   . A1B2W C 2 .   ? 10.834 15.462  17.344 1.00 25.61 ? 201 A1B2W A N   1 
HETATM 2196 O  O2  . A1B2W C 2 .   ? 8.930  14.585  24.337 1.00 34.07 ? 201 A1B2W A O2  1 
HETATM 2197 C  C9  . A1B2W C 2 .   ? 6.844  12.726  25.317 1.00 33.22 ? 201 A1B2W A C9  1 
HETATM 2198 S  S   . A1B2W C 2 .   ? 5.594  13.799  26.065 1.00 34.54 ? 201 A1B2W A S   1 
HETATM 2199 ZN ZN  . ZN    D 3 .   ? 11.193 -4.102  5.850  1.00 21.35 2 202 ZN    A ZN  1 
HETATM 2200 S  S   . DMS   E 4 .   ? 18.815 -2.779  24.646 1.00 79.71 ? 201 DMS   C S   1 
HETATM 2201 O  O   . DMS   E 4 .   ? 18.748 -2.173  23.274 1.00 79.60 ? 201 DMS   C O   1 
HETATM 2202 C  C1  . DMS   E 4 .   ? 18.009 -4.405  24.588 1.00 79.73 ? 201 DMS   C C1  1 
HETATM 2203 C  C2  . DMS   E 4 .   ? 20.498 -3.402  24.906 1.00 79.70 ? 201 DMS   C C2  1 
HETATM 2204 ZN ZN  . ZN    F 3 .   ? 30.569 -31.148 26.730 1.00 14.24 2 202 ZN    C ZN  1 
HETATM 2205 S  S   . DMS   G 4 .   ? 20.971 -32.863 10.176 1.00 53.11 ? 203 DMS   C S   1 
HETATM 2206 O  O   . DMS   G 4 .   ? 21.402 -32.046 8.984  1.00 53.00 ? 203 DMS   C O   1 
HETATM 2207 C  C1  . DMS   G 4 .   ? 21.956 -32.297 11.596 1.00 53.05 ? 203 DMS   C C1  1 
HETATM 2208 C  C2  . DMS   G 4 .   ? 19.419 -32.098 10.758 1.00 53.33 ? 203 DMS   C C2  1 
HETATM 2209 O  O   . HOH   H 5 .   ? 5.296  18.657  23.873 1.00 42.11 ? 301 HOH   A O   1 
HETATM 2210 O  O   . HOH   H 5 .   ? 35.322 -3.789  7.864  1.00 24.10 ? 302 HOH   A O   1 
HETATM 2211 O  O   . HOH   H 5 .   ? 11.200 8.797   4.236  1.00 21.84 ? 303 HOH   A O   1 
HETATM 2212 O  O   . HOH   H 5 .   ? 7.354  20.474  17.277 1.00 26.03 ? 304 HOH   A O   1 
HETATM 2213 O  O   . HOH   H 5 .   ? 2.948  9.377   9.070  1.00 33.67 ? 305 HOH   A O   1 
HETATM 2214 O  O   . HOH   H 5 .   ? 5.876  17.493  21.438 1.00 40.43 ? 306 HOH   A O   1 
HETATM 2215 O  O   . HOH   H 5 .   ? 13.381 11.417  24.653 1.00 23.41 ? 307 HOH   A O   1 
HETATM 2216 O  O   . HOH   H 5 .   ? 14.093 17.378  4.241  1.00 36.43 ? 308 HOH   A O   1 
HETATM 2217 O  O   . HOH   H 5 .   ? 23.094 11.912  21.959 1.00 36.74 ? 309 HOH   A O   1 
HETATM 2218 O  O   . HOH   H 5 .   ? 13.925 2.811   1.196  1.00 27.80 ? 310 HOH   A O   1 
HETATM 2219 O  O   . HOH   H 5 .   ? 27.763 8.096   1.677  1.00 31.82 ? 311 HOH   A O   1 
HETATM 2220 O  O   . HOH   H 5 .   ? 10.711 12.687  23.985 1.00 39.74 ? 312 HOH   A O   1 
HETATM 2221 O  O   . HOH   H 5 .   ? 20.031 20.119  5.712  1.00 40.51 ? 313 HOH   A O   1 
HETATM 2222 O  O   . HOH   H 5 .   ? 28.132 3.276   4.915  1.00 33.60 ? 314 HOH   A O   1 
HETATM 2223 O  O   . HOH   H 5 .   ? 4.626  -3.491  28.792 1.00 29.35 ? 315 HOH   A O   1 
HETATM 2224 O  O   . HOH   H 5 .   ? 17.468 1.052   28.143 1.00 25.52 ? 316 HOH   A O   1 
HETATM 2225 O  O   . HOH   H 5 .   ? 19.302 10.114  19.619 1.00 14.43 ? 317 HOH   A O   1 
HETATM 2226 O  O   . HOH   H 5 .   ? 30.384 10.516  15.671 1.00 30.48 ? 318 HOH   A O   1 
HETATM 2227 O  O   . HOH   H 5 .   ? 10.418 10.350  31.340 1.00 24.10 ? 319 HOH   A O   1 
HETATM 2228 O  O   . HOH   H 5 .   ? 6.880  26.318  14.259 1.00 43.66 ? 320 HOH   A O   1 
HETATM 2229 O  O   . HOH   H 5 .   ? 23.449 21.732  7.225  1.00 23.96 ? 321 HOH   A O   1 
HETATM 2230 O  O   . HOH   H 5 .   ? 21.610 5.052   24.654 1.00 45.67 ? 322 HOH   A O   1 
HETATM 2231 O  O   . HOH   H 5 .   ? 0.496  -0.848  19.385 1.00 21.73 ? 323 HOH   A O   1 
HETATM 2232 O  O   . HOH   H 5 .   ? -1.082 -4.398  11.082 1.00 56.19 ? 324 HOH   A O   1 
HETATM 2233 O  O   . HOH   H 5 .   ? 3.875  -8.133  9.799  1.00 50.38 ? 325 HOH   A O   1 
HETATM 2234 O  O   . HOH   H 5 .   ? 2.643  -2.833  20.755 1.00 25.09 ? 326 HOH   A O   1 
HETATM 2235 O  O   . HOH   H 5 .   ? 33.936 -2.248  13.551 1.00 35.16 ? 327 HOH   A O   1 
HETATM 2236 O  O   . HOH   H 5 .   ? 33.644 11.089  15.602 1.00 42.29 ? 328 HOH   A O   1 
HETATM 2237 O  O   . HOH   H 5 .   ? 21.893 2.423   -0.920 1.00 32.78 ? 329 HOH   A O   1 
HETATM 2238 O  O   . HOH   H 5 .   ? 16.586 3.965   23.625 1.00 19.64 ? 330 HOH   A O   1 
HETATM 2239 O  O   . HOH   H 5 .   ? 29.862 11.663  18.461 1.00 29.94 ? 331 HOH   A O   1 
HETATM 2240 O  O   . HOH   H 5 .   ? 18.994 16.979  26.313 1.00 42.51 ? 332 HOH   A O   1 
HETATM 2241 O  O   . HOH   H 5 .   ? 24.829 5.175   21.420 1.00 31.90 ? 333 HOH   A O   1 
HETATM 2242 O  O   . HOH   H 5 .   ? 22.620 0.919   17.394 1.00 16.95 ? 334 HOH   A O   1 
HETATM 2243 O  O   . HOH   H 5 .   ? -0.069 1.331   15.869 1.00 13.35 ? 335 HOH   A O   1 
HETATM 2244 O  O   . HOH   H 5 .   ? 6.025  2.308   5.471  1.00 25.30 ? 336 HOH   A O   1 
HETATM 2245 O  O   . HOH   H 5 .   ? 33.819 14.280  9.756  1.00 35.11 ? 337 HOH   A O   1 
HETATM 2246 O  O   . HOH   H 5 .   ? 11.261 12.675  11.031 1.00 17.57 ? 338 HOH   A O   1 
HETATM 2247 O  O   . HOH   H 5 .   ? 31.569 20.021  11.813 1.00 24.18 ? 339 HOH   A O   1 
HETATM 2248 O  O   . HOH   H 5 .   ? 26.825 -1.245  8.809  1.00 27.03 ? 340 HOH   A O   1 
HETATM 2249 O  O   . HOH   H 5 .   ? 13.592 13.800  23.764 1.00 24.28 ? 341 HOH   A O   1 
HETATM 2250 O  O   . HOH   H 5 .   ? 20.914 -4.102  14.136 1.00 17.41 ? 342 HOH   A O   1 
HETATM 2251 O  O   . HOH   H 5 .   ? 13.711 4.052   23.485 1.00 13.42 ? 343 HOH   A O   1 
HETATM 2252 O  O   . HOH   H 5 .   ? 11.556 17.970  4.815  1.00 35.75 ? 344 HOH   A O   1 
HETATM 2253 O  O   . HOH   H 5 .   ? 36.412 18.028  14.379 1.00 32.68 ? 345 HOH   A O   1 
HETATM 2254 O  O   . HOH   H 5 .   ? 15.050 11.386  0.009  1.00 34.18 ? 346 HOH   A O   1 
HETATM 2255 O  O   . HOH   H 5 .   ? 4.687  15.451  20.664 1.00 46.59 ? 347 HOH   A O   1 
HETATM 2256 O  O   . HOH   H 5 .   ? 35.928 15.240  11.258 1.00 41.61 ? 348 HOH   A O   1 
HETATM 2257 O  O   . HOH   H 5 .   ? 18.366 21.917  9.495  1.00 19.97 ? 349 HOH   A O   1 
HETATM 2258 O  O   . HOH   H 5 .   ? 35.214 8.058   9.398  1.00 44.34 ? 350 HOH   A O   1 
HETATM 2259 O  O   . HOH   H 5 .   ? 8.596  19.260  19.426 1.00 24.04 ? 351 HOH   A O   1 
HETATM 2260 O  O   . HOH   H 5 .   ? 28.915 3.423   12.672 1.00 17.25 ? 352 HOH   A O   1 
HETATM 2261 O  O   . HOH   H 5 .   ? 29.371 11.965  21.268 1.00 37.27 ? 353 HOH   A O   1 
HETATM 2262 O  O   . HOH   H 5 .   ? 1.624  5.495   26.891 1.00 34.23 ? 354 HOH   A O   1 
HETATM 2263 O  O   . HOH   H 5 .   ? 9.708  4.069   33.482 1.00 14.67 ? 355 HOH   A O   1 
HETATM 2264 O  O   . HOH   H 5 .   ? 3.220  7.472   24.177 1.00 25.89 ? 356 HOH   A O   1 
HETATM 2265 O  O   . HOH   H 5 .   ? 16.933 -3.446  27.845 1.00 34.98 ? 357 HOH   A O   1 
HETATM 2266 O  O   . HOH   H 5 .   ? 2.555  16.189  19.202 1.00 33.73 ? 358 HOH   A O   1 
HETATM 2267 O  O   . HOH   H 5 .   ? 5.632  5.547   32.660 1.00 22.72 ? 359 HOH   A O   1 
HETATM 2268 O  O   . HOH   H 5 .   ? 36.740 2.525   10.019 1.00 37.20 ? 360 HOH   A O   1 
HETATM 2269 O  O   . HOH   H 5 .   ? 13.218 11.403  9.122  1.00 14.60 ? 361 HOH   A O   1 
HETATM 2270 O  O   . HOH   H 5 .   ? 20.710 -1.062  2.985  1.00 30.30 ? 362 HOH   A O   1 
HETATM 2271 O  O   . HOH   H 5 .   ? 6.633  -6.925  23.732 1.00 26.97 ? 363 HOH   A O   1 
HETATM 2272 O  O   . HOH   H 5 .   ? 20.794 -2.515  16.872 1.00 15.72 ? 364 HOH   A O   1 
HETATM 2273 O  O   . HOH   H 5 .   ? 28.828 15.781  4.282  1.00 32.97 ? 365 HOH   A O   1 
HETATM 2274 O  O   . HOH   H 5 .   ? 8.285  -2.708  31.920 1.00 25.78 ? 366 HOH   A O   1 
HETATM 2275 O  O   . HOH   H 5 .   ? 32.760 16.598  9.349  1.00 33.61 ? 367 HOH   A O   1 
HETATM 2276 O  O   . HOH   H 5 .   ? 9.231  3.085   2.805  1.00 36.44 ? 368 HOH   A O   1 
HETATM 2277 O  O   . HOH   H 5 .   ? 10.642 5.300   3.333  1.00 27.34 ? 369 HOH   A O   1 
HETATM 2278 O  O   . HOH   H 5 .   ? 8.484  -6.391  9.725  1.00 32.59 ? 370 HOH   A O   1 
HETATM 2279 O  O   . HOH   H 5 .   ? 19.412 2.957   19.400 1.00 19.93 ? 371 HOH   A O   1 
HETATM 2280 O  O   . HOH   H 5 .   ? 17.523 20.037  16.986 1.00 17.55 ? 372 HOH   A O   1 
HETATM 2281 O  O   . HOH   H 5 .   ? 35.187 10.875  12.502 1.00 48.06 ? 373 HOH   A O   1 
HETATM 2282 O  O   . HOH   H 5 .   ? 11.462 -6.950  24.767 1.00 32.12 ? 374 HOH   A O   1 
HETATM 2283 O  O   . HOH   H 5 .   ? 8.460  6.569   33.824 1.00 19.91 ? 375 HOH   A O   1 
HETATM 2284 O  O   . HOH   H 5 .   ? 22.865 -0.626  5.333  1.00 22.88 ? 376 HOH   A O   1 
HETATM 2285 O  O   . HOH   H 5 .   ? 16.271 2.334   30.172 1.00 28.52 ? 377 HOH   A O   1 
HETATM 2286 O  O   . HOH   H 5 .   ? 9.738  10.563  23.170 1.00 26.02 ? 378 HOH   A O   1 
HETATM 2287 O  O   . HOH   H 5 .   ? 3.237  0.644   28.906 1.00 37.85 ? 379 HOH   A O   1 
HETATM 2288 O  O   . HOH   H 5 .   ? 0.622  -1.150  9.155  1.00 33.58 ? 380 HOH   A O   1 
HETATM 2289 O  O   . HOH   H 5 .   ? 14.466 -2.413  17.928 1.00 18.97 ? 381 HOH   A O   1 
HETATM 2290 O  O   . HOH   H 5 .   ? 30.365 4.640   5.798  1.00 24.60 ? 382 HOH   A O   1 
HETATM 2291 O  O   . HOH   H 5 .   ? 17.142 6.049   26.794 1.00 27.30 ? 383 HOH   A O   1 
HETATM 2292 O  O   . HOH   H 5 .   ? 16.431 21.227  19.130 1.00 24.20 ? 384 HOH   A O   1 
HETATM 2293 O  O   . HOH   H 5 .   ? 15.116 21.823  8.280  1.00 32.92 ? 385 HOH   A O   1 
HETATM 2294 O  O   . HOH   H 5 .   ? 16.280 9.451   -1.645 1.00 22.42 ? 386 HOH   A O   1 
HETATM 2295 O  O   . HOH   H 5 .   ? 30.094 -1.365  8.606  1.00 33.70 ? 387 HOH   A O   1 
HETATM 2296 O  O   . HOH   H 5 .   ? 3.140  -0.579  2.888  1.00 52.15 ? 388 HOH   A O   1 
HETATM 2297 O  O   . HOH   H 5 .   ? 24.120 -3.418  16.190 1.00 34.95 ? 389 HOH   A O   1 
HETATM 2298 O  O   . HOH   H 5 .   ? 3.915  -3.987  6.007  1.00 29.96 ? 390 HOH   A O   1 
HETATM 2299 O  O   . HOH   H 5 .   ? 17.183 -5.402  12.188 1.00 40.29 ? 391 HOH   A O   1 
HETATM 2300 O  O   . HOH   H 5 .   ? 25.213 17.875  4.579  1.00 36.57 ? 392 HOH   A O   1 
HETATM 2301 O  O   . HOH   H 5 .   ? 30.461 2.934   14.862 1.00 22.89 ? 393 HOH   A O   1 
HETATM 2302 O  O   . HOH   H 5 .   ? 4.201  0.471   23.909 1.00 18.84 ? 394 HOH   A O   1 
HETATM 2303 O  O   . HOH   H 5 .   ? 17.587 10.773  26.046 1.00 30.53 ? 395 HOH   A O   1 
HETATM 2304 O  O   . HOH   H 5 .   ? 0.145  5.673   5.940  1.00 27.50 ? 396 HOH   A O   1 
HETATM 2305 O  O   . HOH   H 5 .   ? 33.877 18.723  10.848 1.00 27.07 ? 397 HOH   A O   1 
HETATM 2306 O  O   . HOH   H 5 .   ? 32.037 8.798   7.639  1.00 24.44 ? 398 HOH   A O   1 
HETATM 2307 O  O   . HOH   H 5 .   ? 36.260 -0.334  12.323 1.00 34.37 ? 399 HOH   A O   1 
HETATM 2308 O  O   . HOH   H 5 .   ? 30.632 15.781  22.935 1.00 28.09 ? 400 HOH   A O   1 
HETATM 2309 O  O   . HOH   H 5 .   ? 14.977 15.059  3.152  1.00 31.70 ? 401 HOH   A O   1 
HETATM 2310 O  O   . HOH   H 5 .   ? 15.275 -4.961  0.481  1.00 39.16 ? 402 HOH   A O   1 
HETATM 2311 O  O   . HOH   H 5 .   ? 3.718  11.655  18.950 1.00 32.92 ? 403 HOH   A O   1 
HETATM 2312 O  O   . HOH   H 5 .   ? 27.817 17.678  24.234 1.00 26.69 ? 404 HOH   A O   1 
HETATM 2313 O  O   . HOH   H 5 .   ? 18.190 17.901  4.205  1.00 32.03 ? 405 HOH   A O   1 
HETATM 2314 O  O   . HOH   H 5 .   ? 4.934  8.007   2.307  1.00 34.06 ? 406 HOH   A O   1 
HETATM 2315 O  O   . HOH   H 5 .   ? 27.173 -1.296  15.969 1.00 28.09 ? 407 HOH   A O   1 
HETATM 2316 O  O   . HOH   H 5 .   ? 17.468 0.731   20.183 1.00 19.86 ? 408 HOH   A O   1 
HETATM 2317 O  O   . HOH   H 5 .   ? 5.176  26.727  19.674 1.00 37.44 ? 409 HOH   A O   1 
HETATM 2318 O  O   . HOH   H 5 .   ? 3.337  -0.227  21.353 1.00 20.51 ? 410 HOH   A O   1 
HETATM 2319 O  O   . HOH   H 5 .   ? 2.189  14.500  16.884 1.00 32.55 ? 411 HOH   A O   1 
HETATM 2320 O  O   . HOH   H 5 .   ? 22.431 19.554  19.702 1.00 31.64 ? 412 HOH   A O   1 
HETATM 2321 O  O   . HOH   H 5 .   ? 5.706  3.066   6.863  1.00 44.87 ? 413 HOH   A O   1 
HETATM 2322 O  O   . HOH   H 5 .   ? 9.047  18.918  26.549 1.00 94.72 ? 414 HOH   A O   1 
HETATM 2323 O  O   . HOH   H 5 .   ? 32.166 2.056   5.954  1.00 36.72 ? 415 HOH   A O   1 
HETATM 2324 O  O   . HOH   H 5 .   ? 16.752 -4.015  2.816  1.00 26.94 ? 416 HOH   A O   1 
HETATM 2325 O  O   . HOH   H 5 .   ? 0.456  -1.255  16.668 1.00 17.89 ? 417 HOH   A O   1 
HETATM 2326 O  O   . HOH   H 5 .   ? 7.222  13.796  4.648  1.00 23.63 ? 418 HOH   A O   1 
HETATM 2327 O  O   . HOH   H 5 .   ? 19.785 13.344  2.206  1.00 34.82 ? 419 HOH   A O   1 
HETATM 2328 O  O   . HOH   H 5 .   ? 19.518 -0.473  33.089 1.00 38.65 ? 420 HOH   A O   1 
HETATM 2329 O  O   . HOH   H 5 .   ? 1.837  8.204   26.633 1.00 49.06 ? 421 HOH   A O   1 
HETATM 2330 O  O   . HOH   H 5 .   ? 14.290 24.424  17.732 1.00 36.61 ? 422 HOH   A O   1 
HETATM 2331 O  O   . HOH   H 5 .   ? 33.919 5.221   16.676 1.00 33.56 ? 423 HOH   A O   1 
HETATM 2332 O  O   . HOH   H 5 .   ? 1.135  -5.013  17.440 1.00 35.99 ? 424 HOH   A O   1 
HETATM 2333 O  O   . HOH   H 5 .   ? 22.673 3.472   20.810 1.00 21.37 ? 425 HOH   A O   1 
HETATM 2334 O  O   . HOH   H 5 .   ? 15.113 14.355  26.295 1.00 33.25 ? 426 HOH   A O   1 
HETATM 2335 O  O   . HOH   H 5 .   ? 23.254 19.164  6.262  1.00 21.07 ? 427 HOH   A O   1 
HETATM 2336 O  O   . HOH   H 5 .   ? 17.110 23.829  16.748 1.00 56.68 ? 428 HOH   A O   1 
HETATM 2337 O  O   . HOH   H 5 .   ? 34.090 7.770   16.669 1.00 33.61 ? 429 HOH   A O   1 
HETATM 2338 O  O   . HOH   H 5 .   ? 20.993 10.003  21.900 1.00 19.24 ? 430 HOH   A O   1 
HETATM 2339 O  O   . HOH   H 5 .   ? 17.159 -2.447  19.619 1.00 19.42 ? 431 HOH   A O   1 
HETATM 2340 O  O   . HOH   H 5 .   ? 23.346 8.278   21.689 1.00 27.17 ? 432 HOH   A O   1 
HETATM 2341 O  O   . HOH   H 5 .   ? 24.888 10.790  23.032 1.00 40.96 ? 433 HOH   A O   1 
HETATM 2342 O  O   . HOH   H 5 .   ? 20.652 -4.582  11.364 1.00 32.13 ? 434 HOH   A O   1 
HETATM 2343 O  O   . HOH   H 5 .   ? 19.660 9.361   -0.859 1.00 28.77 ? 435 HOH   A O   1 
HETATM 2344 O  O   . HOH   H 5 .   ? 8.455  21.109  7.486  1.00 46.74 ? 436 HOH   A O   1 
HETATM 2345 O  O   . HOH   H 5 .   ? 7.480  -4.791  2.896  1.00 39.79 ? 437 HOH   A O   1 
HETATM 2346 O  O   . HOH   H 5 .   ? 35.890 4.064   18.447 1.00 56.54 ? 438 HOH   A O   1 
HETATM 2347 O  O   . HOH   H 5 .   ? 10.669 17.016  25.828 1.00 36.41 ? 439 HOH   A O   1 
HETATM 2348 O  O   . HOH   H 5 .   ? 20.419 20.854  18.611 1.00 50.73 ? 440 HOH   A O   1 
HETATM 2349 O  O   . HOH   H 5 .   ? -0.027 13.955  19.579 1.00 38.44 ? 441 HOH   A O   1 
HETATM 2350 O  O   . HOH   H 5 .   ? 1.166  3.646   26.073 1.00 32.89 ? 442 HOH   A O   1 
HETATM 2351 O  O   . HOH   H 5 .   ? 31.866 7.115   5.465  1.00 33.49 ? 443 HOH   A O   1 
HETATM 2352 O  O   . HOH   H 5 .   ? 2.068  -5.443  14.555 1.00 40.53 ? 444 HOH   A O   1 
HETATM 2353 O  O   . HOH   H 5 .   ? 19.175 -3.414  33.807 1.00 39.46 ? 445 HOH   A O   1 
HETATM 2354 O  O   . HOH   H 5 .   ? 21.634 19.622  4.115  1.00 41.28 ? 446 HOH   A O   1 
HETATM 2355 O  O   . HOH   H 5 .   ? 30.615 13.051  23.214 1.00 44.63 ? 447 HOH   A O   1 
HETATM 2356 O  O   . HOH   H 5 .   ? 6.535  3.278   3.197  1.00 38.19 ? 448 HOH   A O   1 
HETATM 2357 O  O   . HOH   H 5 .   ? 18.504 2.170   22.637 1.00 37.76 ? 449 HOH   A O   1 
HETATM 2358 O  O   . HOH   H 5 .   ? 16.981 -4.881  34.255 1.00 34.78 ? 450 HOH   A O   1 
HETATM 2359 O  O   . HOH   H 5 .   ? 18.487 3.199   26.000 1.00 40.81 ? 451 HOH   A O   1 
HETATM 2360 O  O   . HOH   H 5 .   ? 29.649 0.722   16.580 1.00 33.90 ? 452 HOH   A O   1 
HETATM 2361 O  O   . HOH   H 5 .   ? 13.218 24.864  15.306 1.00 41.11 ? 453 HOH   A O   1 
HETATM 2362 O  O   . HOH   H 5 .   ? 0.148  0.226   23.299 1.00 32.46 ? 454 HOH   A O   1 
HETATM 2363 O  O   . HOH   H 5 .   ? 23.033 -8.507  7.064  1.00 48.25 ? 455 HOH   A O   1 
HETATM 2364 O  O   . HOH   H 5 .   ? 8.675  12.384  31.760 1.00 41.91 ? 456 HOH   A O   1 
HETATM 2365 O  O   . HOH   H 5 .   ? 21.378 3.041   23.203 1.00 38.24 ? 457 HOH   A O   1 
HETATM 2366 O  O   . HOH   H 5 .   ? 8.815  16.718  28.886 1.00 52.69 ? 458 HOH   A O   1 
HETATM 2367 O  O   . HOH   H 5 .   ? 37.638 -4.471  6.630  1.00 31.17 ? 459 HOH   A O   1 
HETATM 2368 O  O   . HOH   H 5 .   ? 12.487 -4.959  33.052 1.00 28.83 ? 460 HOH   A O   1 
HETATM 2369 O  O   . HOH   H 5 .   ? 31.205 4.566   17.043 1.00 26.36 ? 461 HOH   A O   1 
HETATM 2370 O  O   . HOH   H 5 .   ? 5.861  -10.735 8.837  1.00 61.85 ? 462 HOH   A O   1 
HETATM 2371 O  O   . HOH   H 5 .   ? 2.358  -5.081  22.470 1.00 32.37 ? 463 HOH   A O   1 
HETATM 2372 O  O   . HOH   H 5 .   ? 32.262 11.282  6.559  1.00 36.49 ? 464 HOH   A O   1 
HETATM 2373 O  O   . HOH   H 5 .   ? 4.029  -6.810  23.407 1.00 45.68 ? 465 HOH   A O   1 
HETATM 2374 O  O   . HOH   H 5 .   ? 26.398 0.405   19.997 1.00 44.10 ? 466 HOH   A O   1 
HETATM 2375 O  O   . HOH   I 5 .   ? 31.052 -32.771 0.791  1.00 35.73 ? 301 HOH   C O   1 
HETATM 2376 O  O   . HOH   I 5 .   ? 17.517 -33.260 24.060 1.00 37.38 ? 302 HOH   C O   1 
HETATM 2377 O  O   . HOH   I 5 .   ? 38.282 -7.367  7.003  1.00 22.66 ? 303 HOH   C O   1 
HETATM 2378 O  O   . HOH   I 5 .   ? 31.482 -17.878 -0.124 1.00 41.43 ? 304 HOH   C O   1 
HETATM 2379 O  O   . HOH   I 5 .   ? 16.346 -16.996 11.135 1.00 44.65 ? 305 HOH   C O   1 
HETATM 2380 O  O   . HOH   I 5 .   ? 16.497 -15.850 8.699  1.00 48.08 ? 306 HOH   C O   1 
HETATM 2381 O  O   . HOH   I 5 .   ? 19.713 -4.130  20.170 1.00 23.23 ? 307 HOH   C O   1 
HETATM 2382 O  O   . HOH   I 5 .   ? 38.902 -18.653 21.516 1.00 27.67 ? 308 HOH   C O   1 
HETATM 2383 O  O   . HOH   I 5 .   ? 14.703 -28.806 25.499 1.00 35.76 ? 309 HOH   C O   1 
HETATM 2384 O  O   . HOH   I 5 .   ? 18.882 -32.329 19.753 1.00 40.24 ? 310 HOH   C O   1 
HETATM 2385 O  O   . HOH   I 5 .   ? 30.710 -18.110 26.867 1.00 20.46 ? 311 HOH   C O   1 
HETATM 2386 O  O   . HOH   I 5 .   ? 14.653 -18.541 31.871 1.00 36.54 ? 312 HOH   C O   1 
HETATM 2387 O  O   . HOH   I 5 .   ? 20.715 -18.755 12.789 1.00 14.71 ? 313 HOH   C O   1 
HETATM 2388 O  O   . HOH   I 5 .   ? 24.418 -9.512  26.878 1.00 40.54 ? 314 HOH   C O   1 
HETATM 2389 O  O   . HOH   I 5 .   ? 22.032 -28.745 4.790  1.00 25.98 ? 315 HOH   C O   1 
HETATM 2390 O  O   . HOH   I 5 .   ? 14.697 -23.871 12.262 1.00 32.65 ? 316 HOH   C O   1 
HETATM 2391 O  O   . HOH   I 5 .   ? 22.891 -5.947  21.083 1.00 20.25 ? 317 HOH   C O   1 
HETATM 2392 O  O   . HOH   I 5 .   ? 36.291 -2.508  10.974 1.00 29.67 ? 318 HOH   C O   1 
HETATM 2393 O  O   . HOH   I 5 .   ? 24.582 -5.824  15.135 1.00 30.60 ? 319 HOH   C O   1 
HETATM 2394 O  O   . HOH   I 5 .   ? 37.336 -31.986 10.991 1.00 26.44 ? 320 HOH   C O   1 
HETATM 2395 O  O   . HOH   I 5 .   ? 44.218 -20.680 6.245  1.00 40.49 ? 321 HOH   C O   1 
HETATM 2396 O  O   . HOH   I 5 .   ? 17.856 -27.549 16.474 1.00 19.14 ? 322 HOH   C O   1 
HETATM 2397 O  O   . HOH   I 5 .   ? 10.200 -17.488 18.250 1.00 26.68 ? 323 HOH   C O   1 
HETATM 2398 O  O   . HOH   I 5 .   ? 28.197 -5.130  18.499 1.00 38.43 ? 324 HOH   C O   1 
HETATM 2399 O  O   . HOH   I 5 .   ? 36.147 -26.122 34.232 1.00 39.65 ? 325 HOH   C O   1 
HETATM 2400 O  O   . HOH   I 5 .   ? 9.880  -8.884  23.913 1.00 29.90 ? 326 HOH   C O   1 
HETATM 2401 O  O   . HOH   I 5 .   ? 37.123 -18.725 28.167 1.00 29.79 ? 327 HOH   C O   1 
HETATM 2402 O  O   . HOH   I 5 .   ? 35.239 -32.770 3.369  1.00 36.78 ? 328 HOH   C O   1 
HETATM 2403 O  O   . HOH   I 5 .   ? 13.255 -11.106 28.385 1.00 40.14 ? 329 HOH   C O   1 
HETATM 2404 O  O   . HOH   I 5 .   ? 18.603 -8.763  13.649 1.00 28.38 ? 330 HOH   C O   1 
HETATM 2405 O  O   . HOH   I 5 .   ? 36.030 -17.721 11.522 1.00 29.20 ? 331 HOH   C O   1 
HETATM 2406 O  O   . HOH   I 5 .   ? 26.520 -5.477  10.004 1.00 22.75 ? 332 HOH   C O   1 
HETATM 2407 O  O   . HOH   I 5 .   ? 25.742 -35.722 2.941  1.00 45.06 ? 333 HOH   C O   1 
HETATM 2408 O  O   . HOH   I 5 .   ? 40.514 -27.253 15.229 1.00 13.38 ? 334 HOH   C O   1 
HETATM 2409 O  O   . HOH   I 5 .   ? 30.925 -21.474 28.376 1.00 17.44 ? 335 HOH   C O   1 
HETATM 2410 O  O   . HOH   I 5 .   ? 26.269 -15.218 30.699 1.00 35.86 ? 336 HOH   C O   1 
HETATM 2411 O  O   . HOH   I 5 .   ? 21.351 -24.988 3.926  1.00 43.31 ? 337 HOH   C O   1 
HETATM 2412 O  O   . HOH   I 5 .   ? 23.898 -8.119  9.420  1.00 26.09 ? 338 HOH   C O   1 
HETATM 2413 O  O   . HOH   I 5 .   ? 4.637  -24.963 25.313 1.00 50.30 ? 339 HOH   C O   1 
HETATM 2414 O  O   . HOH   I 5 .   ? 13.831 -24.187 29.338 1.00 32.69 ? 340 HOH   C O   1 
HETATM 2415 O  O   . HOH   I 5 .   ? 40.051 -29.626 11.879 1.00 23.07 ? 341 HOH   C O   1 
HETATM 2416 O  O   . HOH   I 5 .   ? 37.093 -10.539 4.733  1.00 40.40 ? 342 HOH   C O   1 
HETATM 2417 O  O   . HOH   I 5 .   ? 17.542 -24.054 8.611  1.00 37.44 ? 343 HOH   C O   1 
HETATM 2418 O  O   . HOH   I 5 .   ? 24.814 -15.745 7.289  1.00 19.37 ? 344 HOH   C O   1 
HETATM 2419 O  O   . HOH   I 5 .   ? 25.691 -37.764 24.311 1.00 37.99 ? 345 HOH   C O   1 
HETATM 2420 O  O   . HOH   I 5 .   ? 29.886 -15.236 19.539 1.00 16.05 ? 346 HOH   C O   1 
HETATM 2421 O  O   . HOH   I 5 .   ? 34.022 -33.630 24.035 1.00 34.90 ? 347 HOH   C O   1 
HETATM 2422 O  O   . HOH   I 5 .   ? 26.003 -25.289 8.741  1.00 13.25 ? 348 HOH   C O   1 
HETATM 2423 O  O   . HOH   I 5 .   ? 32.445 -23.672 29.119 1.00 17.55 ? 349 HOH   C O   1 
HETATM 2424 O  O   . HOH   I 5 .   ? 9.194  -7.982  21.253 1.00 24.32 ? 350 HOH   C O   1 
HETATM 2425 O  O   . HOH   I 5 .   ? 41.328 -25.067 7.207  1.00 34.81 ? 351 HOH   C O   1 
HETATM 2426 O  O   . HOH   I 5 .   ? 22.835 -7.520  25.291 1.00 43.64 ? 352 HOH   C O   1 
HETATM 2427 O  O   . HOH   I 5 .   ? 19.145 -27.675 28.174 1.00 19.60 ? 353 HOH   C O   1 
HETATM 2428 O  O   . HOH   I 5 .   ? 16.810 -9.244  27.535 1.00 35.60 ? 354 HOH   C O   1 
HETATM 2429 O  O   . HOH   I 5 .   ? 11.887 -24.287 21.639 1.00 18.48 ? 355 HOH   C O   1 
HETATM 2430 O  O   . HOH   I 5 .   ? 29.734 -13.110 12.954 1.00 16.95 ? 356 HOH   C O   1 
HETATM 2431 O  O   . HOH   I 5 .   ? 10.504 -16.873 12.352 1.00 34.72 ? 357 HOH   C O   1 
HETATM 2432 O  O   . HOH   I 5 .   ? 35.915 -28.608 2.915  1.00 42.63 ? 358 HOH   C O   1 
HETATM 2433 O  O   . HOH   I 5 .   ? 26.967 -35.589 20.825 1.00 26.41 ? 359 HOH   C O   1 
HETATM 2434 O  O   . HOH   I 5 .   ? 10.427 -16.928 14.986 1.00 29.86 ? 360 HOH   C O   1 
HETATM 2435 O  O   . HOH   I 5 .   ? 36.249 -32.732 25.100 1.00 45.28 ? 361 HOH   C O   1 
HETATM 2436 O  O   . HOH   I 5 .   ? 35.081 -13.146 8.625  1.00 20.18 ? 362 HOH   C O   1 
HETATM 2437 O  O   . HOH   I 5 .   ? 31.992 -10.427 13.790 1.00 20.30 ? 363 HOH   C O   1 
HETATM 2438 O  O   . HOH   I 5 .   ? 22.888 -8.512  13.969 1.00 16.18 ? 364 HOH   C O   1 
HETATM 2439 O  O   . HOH   I 5 .   ? 20.733 -25.685 13.798 1.00 22.01 ? 365 HOH   C O   1 
HETATM 2440 O  O   . HOH   I 5 .   ? 4.260  -10.403 19.677 1.00 29.68 ? 366 HOH   C O   1 
HETATM 2441 O  O   . HOH   I 5 .   ? 37.739 -31.282 25.909 1.00 28.63 ? 367 HOH   C O   1 
HETATM 2442 O  O   . HOH   I 5 .   ? 23.511 -33.556 29.086 1.00 29.50 ? 368 HOH   C O   1 
HETATM 2443 O  O   . HOH   I 5 .   ? 36.564 -16.115 12.532 1.00 31.53 ? 369 HOH   C O   1 
HETATM 2444 O  O   . HOH   I 5 .   ? 31.103 -23.831 -1.287 1.00 23.63 ? 370 HOH   C O   1 
HETATM 2445 O  O   . HOH   I 5 .   ? 13.098 -29.503 19.019 1.00 36.74 ? 371 HOH   C O   1 
HETATM 2446 O  O   . HOH   I 5 .   ? 29.981 -15.834 30.321 1.00 35.27 ? 372 HOH   C O   1 
HETATM 2447 O  O   . HOH   I 5 .   ? 6.786  -9.181  22.650 1.00 37.62 ? 373 HOH   C O   1 
HETATM 2448 O  O   . HOH   I 5 .   ? 28.072 -16.367 22.056 1.00 14.13 ? 374 HOH   C O   1 
HETATM 2449 O  O   . HOH   I 5 .   ? 23.178 -25.402 8.890  1.00 20.24 ? 375 HOH   C O   1 
HETATM 2450 O  O   . HOH   I 5 .   ? 22.900 -28.142 12.618 1.00 20.19 ? 376 HOH   C O   1 
HETATM 2451 O  O   . HOH   I 5 .   ? 32.943 -9.798  11.117 1.00 16.03 ? 377 HOH   C O   1 
HETATM 2452 O  O   . HOH   I 5 .   ? 34.943 -34.908 18.193 1.00 33.88 ? 378 HOH   C O   1 
HETATM 2453 O  O   . HOH   I 5 .   ? 20.054 -32.144 15.410 1.00 41.21 ? 379 HOH   C O   1 
HETATM 2454 O  O   . HOH   I 5 .   ? 43.158 -25.232 23.813 1.00 24.27 ? 380 HOH   C O   1 
HETATM 2455 O  O   . HOH   I 5 .   ? 33.010 -30.283 31.686 1.00 20.98 ? 381 HOH   C O   1 
HETATM 2456 O  O   . HOH   I 5 .   ? 14.752 -18.457 10.420 1.00 38.41 ? 382 HOH   C O   1 
HETATM 2457 O  O   . HOH   I 5 .   ? 10.950 -21.804 13.695 1.00 44.82 ? 383 HOH   C O   1 
HETATM 2458 O  O   . HOH   I 5 .   ? 30.252 -18.178 8.382  1.00 24.99 ? 384 HOH   C O   1 
HETATM 2459 O  O   . HOH   I 5 .   ? 29.916 -10.500 27.746 1.00 43.83 ? 385 HOH   C O   1 
HETATM 2460 O  O   . HOH   I 5 .   ? 5.812  -16.795 22.203 1.00 47.57 ? 386 HOH   C O   1 
HETATM 2461 O  O   . HOH   I 5 .   ? 31.219 -12.176 10.640 1.00 16.43 ? 387 HOH   C O   1 
HETATM 2462 O  O   . HOH   I 5 .   ? 23.712 -3.391  19.106 1.00 37.01 ? 388 HOH   C O   1 
HETATM 2463 O  O   . HOH   I 5 .   ? 41.047 -15.368 10.645 1.00 62.13 ? 389 HOH   C O   1 
HETATM 2464 O  O   . HOH   I 5 .   ? 22.498 -13.828 29.734 1.00 35.86 ? 390 HOH   C O   1 
HETATM 2465 O  O   . HOH   I 5 .   ? 11.414 -22.469 28.630 1.00 27.99 ? 391 HOH   C O   1 
HETATM 2466 O  O   . HOH   I 5 .   ? 10.664 -11.988 9.031  1.00 28.98 ? 392 HOH   C O   1 
HETATM 2467 O  O   . HOH   I 5 .   ? 34.322 -13.437 25.442 1.00 21.41 ? 393 HOH   C O   1 
HETATM 2468 O  O   . HOH   I 5 .   ? 22.286 -23.797 6.166  1.00 34.33 ? 394 HOH   C O   1 
HETATM 2469 O  O   . HOH   I 5 .   ? 32.128 -34.507 24.872 1.00 29.94 ? 395 HOH   C O   1 
HETATM 2470 O  O   . HOH   I 5 .   ? 8.757  -13.333 10.732 1.00 24.32 ? 396 HOH   C O   1 
HETATM 2471 O  O   . HOH   I 5 .   ? 4.724  -28.100 23.136 1.00 35.73 ? 397 HOH   C O   1 
HETATM 2472 O  O   . HOH   I 5 .   ? 4.931  -12.012 14.500 1.00 46.48 ? 398 HOH   C O   1 
HETATM 2473 O  O   . HOH   I 5 .   ? 25.926 -30.957 30.862 1.00 19.16 ? 399 HOH   C O   1 
HETATM 2474 O  O   . HOH   I 5 .   ? 31.566 -13.377 4.190  1.00 33.47 ? 400 HOH   C O   1 
HETATM 2475 O  O   . HOH   I 5 .   ? 10.986 -6.431  13.199 1.00 27.12 ? 401 HOH   C O   1 
HETATM 2476 O  O   . HOH   I 5 .   ? 36.261 -21.307 6.841  1.00 25.23 ? 402 HOH   C O   1 
HETATM 2477 O  O   . HOH   I 5 .   ? 9.712  -18.511 26.623 1.00 30.25 ? 403 HOH   C O   1 
HETATM 2478 O  O   . HOH   I 5 .   ? 26.367 -31.271 14.882 1.00 20.59 ? 404 HOH   C O   1 
HETATM 2479 O  O   . HOH   I 5 .   ? 4.523  -16.286 17.006 1.00 48.76 ? 405 HOH   C O   1 
HETATM 2480 O  O   . HOH   I 5 .   ? 35.577 -24.614 24.718 1.00 20.56 ? 406 HOH   C O   1 
HETATM 2481 O  O   . HOH   I 5 .   ? 36.913 -29.276 10.157 1.00 21.25 ? 407 HOH   C O   1 
HETATM 2482 O  O   . HOH   I 5 .   ? 26.611 -11.974 27.467 1.00 28.32 ? 408 HOH   C O   1 
HETATM 2483 O  O   . HOH   I 5 .   ? 28.937 -36.352 7.888  1.00 21.58 ? 409 HOH   C O   1 
HETATM 2484 O  O   . HOH   I 5 .   ? 31.592 -35.287 31.812 1.00 43.97 ? 410 HOH   C O   1 
HETATM 2485 O  O   . HOH   I 5 .   ? 38.863 -14.630 13.428 1.00 35.25 ? 411 HOH   C O   1 
HETATM 2486 O  O   . HOH   I 5 .   ? 9.993  -24.857 19.753 1.00 21.62 ? 412 HOH   C O   1 
HETATM 2487 O  O   . HOH   I 5 .   ? 5.794  -12.449 23.169 1.00 46.38 ? 413 HOH   C O   1 
HETATM 2488 O  O   . HOH   I 5 .   ? 37.837 -20.471 4.771  1.00 35.79 ? 414 HOH   C O   1 
HETATM 2489 O  O   . HOH   I 5 .   ? 41.707 -12.380 17.935 1.00 26.37 ? 415 HOH   C O   1 
HETATM 2490 O  O   . HOH   I 5 .   ? 3.797  -8.304  14.687 1.00 25.74 ? 416 HOH   C O   1 
HETATM 2491 O  O   . HOH   I 5 .   ? 33.569 -36.135 8.788  1.00 46.98 ? 417 HOH   C O   1 
HETATM 2492 O  O   . HOH   I 5 .   ? 22.950 -33.474 5.400  1.00 31.98 ? 418 HOH   C O   1 
HETATM 2493 O  O   . HOH   I 5 .   ? 35.745 -28.598 7.802  1.00 19.64 ? 419 HOH   C O   1 
HETATM 2494 O  O   . HOH   I 5 .   ? 21.671 -18.867 5.861  1.00 29.36 ? 420 HOH   C O   1 
HETATM 2495 O  O   . HOH   I 5 .   ? 38.903 -13.082 25.743 1.00 28.85 ? 421 HOH   C O   1 
HETATM 2496 O  O   . HOH   I 5 .   ? 26.528 -6.019  22.112 1.00 31.53 ? 422 HOH   C O   1 
HETATM 2497 O  O   . HOH   I 5 .   ? 35.018 -4.144  17.645 1.00 31.96 ? 423 HOH   C O   1 
HETATM 2498 O  O   . HOH   I 5 .   ? 35.266 -13.714 6.082  1.00 35.55 ? 424 HOH   C O   1 
HETATM 2499 O  O   . HOH   I 5 .   ? 34.604 -23.207 -0.914 1.00 40.12 ? 425 HOH   C O   1 
HETATM 2500 O  O   . HOH   I 5 .   ? 32.742 -14.385 9.350  1.00 16.63 ? 426 HOH   C O   1 
HETATM 2501 O  O   . HOH   I 5 .   ? 18.596 -8.280  25.450 1.00 21.73 ? 427 HOH   C O   1 
HETATM 2502 O  O   . HOH   I 5 .   ? 38.685 -16.545 3.578  1.00 47.32 ? 428 HOH   C O   1 
HETATM 2503 O  O   . HOH   I 5 .   ? 17.183 -25.387 12.724 1.00 24.59 ? 429 HOH   C O   1 
HETATM 2504 O  O   . HOH   I 5 .   ? 3.950  -12.833 17.118 1.00 39.50 ? 430 HOH   C O   1 
HETATM 2505 O  O   . HOH   I 5 .   ? 24.349 -16.297 3.130  1.00 40.22 ? 431 HOH   C O   1 
HETATM 2506 O  O   . HOH   I 5 .   ? 16.372 -20.498 11.548 1.00 26.92 ? 432 HOH   C O   1 
HETATM 2507 O  O   . HOH   I 5 .   ? 31.095 -37.551 9.082  1.00 44.01 ? 433 HOH   C O   1 
HETATM 2508 O  O   . HOH   I 5 .   ? 40.020 -29.923 14.643 1.00 17.88 ? 434 HOH   C O   1 
HETATM 2509 O  O   . HOH   I 5 .   ? 18.782 -19.137 10.802 1.00 20.29 ? 435 HOH   C O   1 
HETATM 2510 O  O   . HOH   I 5 .   ? 6.595  -17.159 18.587 1.00 47.37 ? 436 HOH   C O   1 
HETATM 2511 O  O   . HOH   I 5 .   ? 20.332 -32.185 22.197 1.00 32.07 ? 437 HOH   C O   1 
HETATM 2512 O  O   . HOH   I 5 .   ? 15.225 -30.075 17.842 1.00 41.76 ? 438 HOH   C O   1 
HETATM 2513 O  O   . HOH   I 5 .   ? 20.437 -23.732 34.822 1.00 33.57 ? 439 HOH   C O   1 
HETATM 2514 O  O   . HOH   I 5 .   ? 6.501  -22.872 18.265 1.00 30.41 ? 440 HOH   C O   1 
HETATM 2515 O  O   . HOH   I 5 .   ? 6.449  -20.070 18.133 1.00 34.95 ? 441 HOH   C O   1 
HETATM 2516 O  O   . HOH   I 5 .   ? 34.012 -15.527 27.057 1.00 33.26 ? 442 HOH   C O   1 
HETATM 2517 O  O   . HOH   I 5 .   ? 6.339  -18.627 25.474 1.00 52.62 ? 443 HOH   C O   1 
HETATM 2518 O  O   . HOH   I 5 .   ? 23.267 -17.499 33.271 1.00 27.58 ? 444 HOH   C O   1 
HETATM 2519 O  O   . HOH   I 5 .   ? 31.540 -15.702 7.116  1.00 28.51 ? 445 HOH   C O   1 
HETATM 2520 O  O   . HOH   I 5 .   ? 20.173 -19.396 35.901 1.00 35.13 ? 446 HOH   C O   1 
HETATM 2521 O  O   . HOH   I 5 .   ? 41.890 -31.493 15.711 1.00 30.89 ? 447 HOH   C O   1 
HETATM 2522 O  O   . HOH   I 5 .   ? 36.474 -24.576 27.185 1.00 41.18 ? 448 HOH   C O   1 
HETATM 2523 O  O   . HOH   I 5 .   ? 34.151 -31.840 29.553 1.00 26.53 ? 449 HOH   C O   1 
HETATM 2524 O  O   . HOH   I 5 .   ? 23.701 -15.715 31.449 1.00 35.52 ? 450 HOH   C O   1 
HETATM 2525 O  O   . HOH   I 5 .   ? 37.370 -14.167 9.735  1.00 36.48 ? 451 HOH   C O   1 
HETATM 2526 O  O   . HOH   I 5 .   ? 21.205 -17.470 34.476 1.00 37.70 ? 452 HOH   C O   1 
HETATM 2527 O  O   . HOH   I 5 .   ? 26.228 -35.508 7.460  1.00 26.19 ? 453 HOH   C O   1 
HETATM 2528 O  O   . HOH   I 5 .   ? 10.168 -20.079 28.931 1.00 33.64 ? 454 HOH   C O   1 
HETATM 2529 O  O   . HOH   I 5 .   ? 38.565 -13.776 6.433  1.00 46.95 ? 455 HOH   C O   1 
HETATM 2530 O  O   . HOH   I 5 .   ? 8.790  -19.258 16.893 1.00 38.00 ? 456 HOH   C O   1 
HETATM 2531 O  O   . HOH   I 5 .   ? 22.866 -16.613 5.424  1.00 37.95 ? 457 HOH   C O   1 
HETATM 2532 O  O   . HOH   I 5 .   ? 21.522 -26.974 10.260 1.00 32.75 ? 458 HOH   C O   1 
HETATM 2533 O  O   . HOH   I 5 .   ? 38.651 -8.522  4.689  1.00 45.82 ? 459 HOH   C O   1 
HETATM 2534 O  O   . HOH   I 5 .   ? 20.740 -7.221  27.016 1.00 54.87 ? 460 HOH   C O   1 
HETATM 2535 O  O   . HOH   I 5 .   ? 16.301 -27.628 14.139 1.00 32.83 ? 461 HOH   C O   1 
HETATM 2536 O  O   . HOH   I 5 .   ? 10.038 -21.425 16.165 1.00 32.69 ? 462 HOH   C O   1 
HETATM 2537 O  O   . HOH   I 5 .   ? 41.439 -15.285 13.352 1.00 41.58 ? 463 HOH   C O   1 
HETATM 2538 O  O   . HOH   I 5 .   ? 32.528 -19.356 29.155 1.00 31.78 ? 464 HOH   C O   1 
HETATM 2539 O  O   . HOH   I 5 .   ? 18.163 -17.984 8.214  1.00 39.33 ? 465 HOH   C O   1 
HETATM 2540 O  O   . HOH   I 5 .   ? 8.919  -23.501 17.673 1.00 35.48 ? 466 HOH   C O   1 
HETATM 2541 O  O   . HOH   I 5 .   ? 18.404 -16.366 38.536 1.00 37.76 ? 467 HOH   C O   1 
HETATM 2542 O  O   . HOH   I 5 .   ? 35.128 -23.021 28.954 1.00 30.58 ? 468 HOH   C O   1 
HETATM 2543 O  O   . HOH   I 5 .   ? 35.253 -20.155 29.396 1.00 40.07 ? 469 HOH   C O   1 
HETATM 2544 O  O   . HOH   I 5 .   ? 37.194 -23.182 -1.696 1.00 33.98 ? 470 HOH   C O   1 
HETATM 2545 O  O   . HOH   I 5 .   ? 3.205  -8.772  21.940 1.00 48.88 ? 471 HOH   C O   1 
HETATM 2546 O  O   . HOH   I 5 .   ? 39.187 -2.589  10.791 1.00 36.79 ? 472 HOH   C O   1 
HETATM 2547 O  O   . HOH   I 5 .   ? 34.338 -10.677 26.453 1.00 43.30 ? 473 HOH   C O   1 
HETATM 2548 O  O   . HOH   I 5 .   ? 19.299 -17.530 5.772  1.00 37.51 ? 474 HOH   C O   1 
HETATM 2549 O  O   . HOH   I 5 .   ? 36.182 -35.683 8.482  1.00 53.51 ? 475 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   ? 0.2357 0.2226 0.2078 -0.0041 -0.0032 -0.0157 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2329 0.2197 0.2117 -0.0032 -0.0073 -0.0127 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2178 0.2095 0.2065 0.0012  -0.0104 -0.0069 7   SER   A C   
4    O O   . SER   A 1   ? 0.2219 0.2173 0.2110 0.0021  -0.0106 -0.0047 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2815 0.2703 0.2543 -0.0114 -0.0122 -0.0114 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3192 0.3155 0.2914 -0.0147 -0.0172 -0.0056 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1974 0.1888 0.1939 0.0032  -0.0122 -0.0049 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1846 0.1794 0.1905 0.0064  -0.0135 -0.0008 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1693 0.1622 0.1818 0.0097  -0.0118 -0.0016 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1932 0.1827 0.2039 0.0110  -0.0092 -0.0046 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1540 0.1491 0.1748 0.0106  -0.0128 0.0012  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1558 0.1501 0.1824 0.0123  -0.0110 0.0004  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1528 0.1489 0.1862 0.0133  -0.0088 0.0015  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1610 0.1583 0.1971 0.0131  -0.0091 0.0038  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1728 0.1669 0.2029 0.0103  -0.0138 0.0015  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1436 0.1396 0.1797 0.0137  -0.0061 -0.0001 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1296 0.1264 0.1719 0.0130  -0.0026 -0.0006 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1331 0.1296 0.1838 0.0127  -0.0025 0.0000  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1393 0.1357 0.1889 0.0124  -0.0038 -0.0006 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1372 0.1358 0.1760 0.0116  0.0007  -0.0028 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1558 0.1565 0.1877 0.0123  0.0002  -0.0023 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1648 0.1634 0.2079 0.0089  0.0055  -0.0048 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1617 0.1667 0.1911 0.0104  0.0019  -0.0022 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1339 0.1303 0.1943 0.0129  -0.0004 0.0015  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1539 0.1510 0.2249 0.0130  0.0006  0.0026  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1628 0.1582 0.2394 0.0117  0.0082  -0.0011 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1557 0.1489 0.2394 0.0122  0.0122  -0.0007 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1599 0.1592 0.2408 0.0143  -0.0027 0.0087  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1531 0.1548 0.2268 0.0131  -0.0098 0.0117  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1609 0.1643 0.2340 0.0116  -0.0130 0.0121  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1756 0.1775 0.2417 0.0125  -0.0128 0.0132  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1728 0.1774 0.2373 0.0089  -0.0184 0.0134  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1883 0.1920 0.2460 0.0098  -0.0181 0.0145  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1924 0.1968 0.2486 0.0078  -0.0205 0.0139  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2277 0.2328 0.2741 0.0036  -0.0247 0.0140  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1625 0.1584 0.2355 0.0093  0.0106  -0.0049 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1673 0.1622 0.2426 0.0058  0.0184  -0.0096 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1731 0.1693 0.2552 0.0048  0.0204  -0.0106 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1620 0.1605 0.2397 0.0046  0.0159  -0.0094 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1753 0.1719 0.2378 0.0015  0.0195  -0.0127 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1916 0.1914 0.2463 0.0017  0.0139  -0.0107 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.1965 0.1928 0.2588 -0.0045 0.0275  -0.0181 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1840 0.1784 0.2782 0.0044  0.0276  -0.0125 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1769 0.1733 0.2791 0.0035  0.0303  -0.0134 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1669 0.1668 0.2738 0.0070  0.0224  -0.0073 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1661 0.1667 0.2780 0.0105  0.0177  -0.0019 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1511 0.1537 0.2538 0.0048  0.0201  -0.0080 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1445 0.1499 0.2483 0.0064  0.0125  -0.0031 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1433 0.1474 0.2320 0.0055  0.0064  -0.0031 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1569 0.1618 0.2429 0.0045  0.0022  -0.0017 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1635 0.1725 0.2763 0.0049  0.0142  -0.0029 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2221 0.2335 0.3542 0.0074  0.0189  -0.0002 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2511 0.2668 0.3932 0.0099  0.0140  0.0066  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.2027 0.2118 0.3410 0.0064  0.0286  -0.0051 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1394 0.1411 0.2198 0.0062  0.0060  -0.0040 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1445 0.1446 0.2130 0.0063  0.0016  -0.0037 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1430 0.1417 0.2083 0.0087  -0.0019 -0.0016 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1464 0.1451 0.2153 0.0099  -0.0001 -0.0012 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1583 0.1589 0.2191 0.0039  0.0046  -0.0061 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1695 0.1726 0.2309 -0.0002 0.0077  -0.0079 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1842 0.1875 0.2452 -0.0010 0.0049  -0.0064 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1963 0.2013 0.2574 -0.0044 0.0138  -0.0113 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1975 0.2037 0.2586 -0.0055 0.0076  -0.0076 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.1986 0.2066 0.2584 -0.0097 0.0168  -0.0132 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2120 0.2211 0.2719 -0.0101 0.0134  -0.0109 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2524 0.2652 0.3110 -0.0160 0.0162  -0.0122 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1387 0.1355 0.1966 0.0090  -0.0060 -0.0010 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1340 0.1293 0.1859 0.0101  -0.0086 -0.0002 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1392 0.1319 0.1827 0.0108  -0.0077 -0.0019 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1540 0.1444 0.1953 0.0102  -0.0082 -0.0024 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1437 0.1389 0.1946 0.0084  -0.0133 0.0018  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1569 0.1500 0.1987 0.0077  -0.0154 0.0013  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1795 0.1741 0.2193 0.0035  -0.0200 0.0033  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2012 0.1907 0.2294 0.0009  -0.0201 -0.0001 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2239 0.2132 0.2447 -0.0010 -0.0209 -0.0007 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2295 0.2235 0.2532 -0.0001 -0.0222 0.0027  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2267 0.2104 0.2373 -0.0040 -0.0192 -0.0052 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1349 0.1284 0.1753 0.0121  -0.0061 -0.0022 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1379 0.1309 0.1732 0.0133  -0.0051 -0.0023 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1549 0.1453 0.1851 0.0146  -0.0060 -0.0028 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1646 0.1564 0.1937 0.0146  -0.0064 -0.0026 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1469 0.1444 0.1820 0.0125  -0.0025 -0.0019 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1485 0.1481 0.1812 0.0137  -0.0020 0.0002  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1551 0.1551 0.1939 0.0094  -0.0003 -0.0028 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1415 0.1276 0.1687 0.0153  -0.0056 -0.0037 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1460 0.1287 0.1676 0.0157  -0.0048 -0.0057 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1698 0.1525 0.1914 0.0156  -0.0049 -0.0057 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1603 0.1404 0.1822 0.0185  -0.0012 -0.0057 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1742 0.1552 0.2009 0.0200  -0.0002 -0.0032 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1394 0.1177 0.1568 0.0121  -0.0067 -0.0078 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.2105 0.1890 0.2287 0.0120  -0.0071 -0.0076 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1455 0.1283 0.1640 0.0094  -0.0107 -0.0059 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.2251 0.2000 0.2353 0.0097  -0.0060 -0.0106 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.1166 0.0903 0.1355 0.0112  -0.0063 -0.0086 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2275 0.2105 0.2494 0.0096  -0.0109 -0.0053 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1642 0.1416 0.1820 0.0193  0.0014  -0.0079 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1666 0.1407 0.1874 0.0227  0.0063  -0.0079 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1742 0.1396 0.1953 0.0215  0.0077  -0.0100 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1885 0.1492 0.2031 0.0171  0.0066  -0.0140 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1763 0.1479 0.1921 0.0227  0.0099  -0.0115 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1819 0.1613 0.1969 0.0235  0.0088  -0.0095 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1855 0.1673 0.1951 0.0203  0.0055  -0.0103 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1825 0.1670 0.2040 0.0274  0.0111  -0.0058 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1674 0.1313 0.1961 0.0248  0.0102  -0.0067 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1750 0.1296 0.2046 0.0236  0.0120  -0.0084 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.2082 0.1523 0.2315 0.0214  0.0172  -0.0154 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.2366 0.1740 0.2543 0.0166  0.0169  -0.0195 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1804 0.1353 0.2211 0.0279  0.0144  -0.0023 20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1946 0.1399 0.2374 0.0267  0.0162  -0.0030 20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.2189 0.1649 0.2745 0.0314  0.0188  0.0048  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.2328 0.1705 0.2919 0.0302  0.0199  0.0059  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.2688 0.1928 0.3303 0.0311  0.0266  0.0024  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2714 0.1878 0.3296 0.0318  0.0329  -0.0044 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2735 0.1904 0.3396 0.0301  0.0276  0.0046  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.2099 0.1536 0.2331 0.0238  0.0220  -0.0172 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.2433 0.1765 0.2600 0.0208  0.0287  -0.0250 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.2590 0.1924 0.2615 0.0126  0.0251  -0.0304 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.2862 0.2110 0.2802 0.0072  0.0300  -0.0375 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.2568 0.1892 0.2788 0.0257  0.0363  -0.0255 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.2632 0.2050 0.2807 0.0255  0.0340  -0.0251 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.2591 0.2126 0.2833 0.0297  0.0298  -0.0179 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.2855 0.2260 0.2926 0.0211  0.0364  -0.0312 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.2618 0.2202 0.2798 0.0281  0.0293  -0.0197 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.2779 0.2292 0.2859 0.0231  0.0331  -0.0272 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.2484 0.1919 0.2487 0.0111  0.0170  -0.0267 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.2434 0.1898 0.2333 0.0035  0.0122  -0.0288 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.2611 0.2101 0.2516 0.0000  0.0057  -0.0262 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.2667 0.2208 0.2519 -0.0057 0.0005  -0.0253 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.2374 0.1932 0.2260 0.0043  0.0088  -0.0259 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.2609 0.2156 0.2479 0.0066  0.0149  -0.0285 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.2573 0.2217 0.2433 0.0070  0.0108  -0.0248 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.2948 0.2414 0.2711 0.0001  0.0208  -0.0364 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.2389 0.1858 0.2372 0.0035  0.0058  -0.0237 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.2324 0.1821 0.2323 0.0004  0.0005  -0.0214 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.2549 0.2002 0.2457 -0.0083 -0.0004 -0.0255 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.2714 0.2066 0.2559 -0.0114 0.0053  -0.0314 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.2209 0.1684 0.2295 0.0045  0.0017  -0.0187 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.2421 0.1952 0.2329 -0.0127 -0.0071 -0.0222 24  THR   A N   
139  C CA  . THR   A 18  ? 0.2480 0.2002 0.2303 -0.0226 -0.0097 -0.0244 24  THR   A CA  
140  C C   . THR   A 18  ? 0.2602 0.2079 0.2452 -0.0243 -0.0097 -0.0248 24  THR   A C   
141  O O   . THR   A 18  ? 0.2425 0.1896 0.2369 -0.0178 -0.0088 -0.0222 24  THR   A O   
142  C CB  . THR   A 18  ? 0.2690 0.2343 0.2527 -0.0264 -0.0176 -0.0183 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.2798 0.2516 0.2760 -0.0217 -0.0211 -0.0125 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2817 0.2521 0.2630 -0.0254 -0.0184 -0.0167 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.2703 0.2160 0.2469 -0.0342 -0.0111 -0.0275 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.2745 0.2172 0.2536 -0.0368 -0.0119 -0.0273 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.2591 0.2135 0.2503 -0.0330 -0.0180 -0.0196 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.2577 0.2098 0.2558 -0.0294 -0.0170 -0.0185 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.3035 0.2446 0.2704 -0.0500 -0.0135 -0.0309 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.4091 0.3507 0.3791 -0.0540 -0.0162 -0.0292 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.4666 0.3952 0.4372 -0.0528 -0.0105 -0.0332 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.4517 0.4061 0.4268 -0.0578 -0.0238 -0.0227 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.4758 0.4091 0.4493 -0.0571 -0.0149 -0.0301 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.4841 0.4334 0.4611 -0.0599 -0.0229 -0.0237 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.2381 0.2050 0.2331 -0.0334 -0.0237 -0.0142 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.2325 0.2095 0.2407 -0.0295 -0.0276 -0.0076 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.2052 0.1797 0.2215 -0.0199 -0.0237 -0.0074 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.2181 0.1952 0.2426 -0.0177 -0.0238 -0.0053 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.2571 0.2468 0.2706 -0.0307 -0.0331 -0.0010 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.3528 0.3518 0.3820 -0.0271 -0.0355 0.0053  26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.3942 0.3974 0.4274 -0.0311 -0.0381 0.0076  26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.3764 0.3779 0.4149 -0.0195 -0.0336 0.0075  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.2011 0.1712 0.2144 -0.0152 -0.0200 -0.0098 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1866 0.1556 0.2064 -0.0078 -0.0167 -0.0091 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1904 0.1524 0.2112 -0.0073 -0.0138 -0.0104 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1833 0.1486 0.2110 -0.0048 -0.0138 -0.0078 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1967 0.1626 0.2130 -0.0038 -0.0133 -0.0109 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.2101 0.1830 0.2270 -0.0029 -0.0156 -0.0087 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.2052 0.1855 0.2298 -0.0021 -0.0182 -0.0048 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.2186 0.1893 0.2288 -0.0036 -0.0142 -0.0109 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1979 0.1500 0.2119 -0.0102 -0.0110 -0.0143 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.2012 0.1455 0.2173 -0.0097 -0.0080 -0.0148 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.2088 0.1566 0.2277 -0.0139 -0.0115 -0.0128 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.2215 0.1681 0.2455 -0.0123 -0.0104 -0.0106 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.2187 0.1498 0.2275 -0.0125 -0.0027 -0.0203 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.2144 0.1406 0.2245 -0.0065 0.0028  -0.0214 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.2307 0.1549 0.2347 -0.0070 0.0055  -0.0253 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.2225 0.1464 0.2415 0.0004  0.0063  -0.0176 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.2285 0.1490 0.2379 -0.0003 0.0110  -0.0246 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.2246 0.1458 0.2439 0.0045  0.0111  -0.0191 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.2393 0.1648 0.2665 0.0028  0.0055  -0.0121 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.2382 0.1585 0.2672 0.0114  0.0150  -0.0145 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.2411 0.1663 0.2767 0.0089  0.0087  -0.0074 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.2440 0.1663 0.2812 0.0133  0.0134  -0.0082 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.2032 0.1570 0.2197 -0.0197 -0.0159 -0.0126 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.2070 0.1661 0.2275 -0.0239 -0.0193 -0.0102 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.2121 0.1820 0.2438 -0.0198 -0.0210 -0.0056 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.2226 0.1967 0.2595 -0.0221 -0.0224 -0.0036 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.2145 0.1779 0.2294 -0.0324 -0.0236 -0.0104 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1947 0.1684 0.2299 -0.0142 -0.0199 -0.0045 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1910 0.1732 0.2361 -0.0108 -0.0195 -0.0016 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1881 0.1680 0.2329 -0.0060 -0.0159 -0.0021 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1905 0.1754 0.2393 -0.0031 -0.0147 -0.0014 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.2043 0.1947 0.2549 -0.0103 -0.0219 0.0011  30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.2364 0.2324 0.2898 -0.0157 -0.0263 0.0038  30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2611 0.2627 0.3230 -0.0168 -0.0266 0.0061  30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.2467 0.2418 0.2922 -0.0204 -0.0296 0.0037  30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1843 0.1572 0.2253 -0.0055 -0.0140 -0.0029 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1754 0.1472 0.2164 -0.0015 -0.0112 -0.0018 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1848 0.1635 0.2306 -0.0017 -0.0103 0.0006  31  LEU   A C   
201  O O   . LEU   A 25  ? 0.2063 0.1866 0.2545 -0.0047 -0.0106 0.0016  31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1806 0.1429 0.2190 -0.0011 -0.0092 -0.0017 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1945 0.1567 0.2351 0.0033  -0.0066 0.0013  31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1926 0.1556 0.2308 0.0066  -0.0056 -0.0003 31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.2183 0.1711 0.2605 0.0042  -0.0039 0.0029  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1606 0.1436 0.2068 0.0006  -0.0088 0.0012  32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1614 0.1511 0.2096 -0.0012 -0.0072 0.0029  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1706 0.1604 0.2175 -0.0002 -0.0067 0.0070  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1911 0.1842 0.2391 -0.0032 -0.0067 0.0105  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1616 0.1567 0.2114 -0.0011 -0.0053 0.0009  32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1792 0.1809 0.2285 -0.0048 -0.0026 0.0016  32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1719 0.1681 0.2269 -0.0016 -0.0054 -0.0011 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1708 0.1582 0.2163 0.0037  -0.0063 0.0075  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1808 0.1701 0.2278 0.0053  -0.0057 0.0128  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1783 0.1621 0.2250 0.0103  -0.0044 0.0121  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1713 0.1534 0.2147 0.0114  -0.0043 0.0077  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1859 0.1860 0.2320 0.0023  -0.0055 0.0149  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1872 0.1929 0.2353 0.0034  -0.0056 0.0215  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.2145 0.2258 0.2661 0.0012  -0.0068 0.0293  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1774 0.1859 0.2250 0.0062  -0.0049 0.0220  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2266 0.2447 0.2810 0.0027  -0.0071 0.0354  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.1990 0.2154 0.2506 0.0057  -0.0058 0.0305  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1848 0.1907 0.2294 0.0087  -0.0039 0.0169  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.2056 0.2279 0.2585 0.0077  -0.0055 0.0336  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.2006 0.2113 0.2454 0.0105  -0.0034 0.0193  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.2079 0.2267 0.2570 0.0102  -0.0040 0.0274  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1764 0.1571 0.2275 0.0131  -0.0030 0.0167  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1821 0.1581 0.2342 0.0179  -0.0002 0.0158  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1973 0.1773 0.2579 0.0210  0.0011  0.0241  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.2009 0.1830 0.2670 0.0199  0.0002  0.0306  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.1977 0.1608 0.2474 0.0186  0.0022  0.0103  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.2154 0.1708 0.2686 0.0176  0.0033  0.0121  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.2472 0.1976 0.3098 0.0219  0.0074  0.0177  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2572 0.2048 0.3250 0.0209  0.0073  0.0223  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.2226 0.1716 0.2886 0.0263  0.0111  0.0180  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1771 0.1591 0.2398 0.0249  0.0033  0.0250  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1712 0.1587 0.2445 0.0284  0.0047  0.0343  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1808 0.1627 0.2573 0.0340  0.0098  0.0318  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1831 0.1693 0.2547 0.0343  0.0097  0.0286  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1926 0.1965 0.2655 0.0247  0.0008  0.0405  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2240 0.2380 0.3084 0.0268  0.0006  0.0524  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2578 0.2676 0.3508 0.0331  0.0047  0.0545  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2700 0.2970 0.3547 0.0215  -0.0033 0.0597  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1902 0.1618 0.2749 0.0382  0.0150  0.0329  36  SER   A N   
245  C CA  A SER   A 30  ? 0.1996 0.1641 0.2884 0.0433  0.0219  0.0297  36  SER   A CA  
246  C CA  B SER   A 30  ? 0.2072 0.1719 0.2954 0.0431  0.0218  0.0293  36  SER   A CA  
247  C C   . SER   A 30  ? 0.2057 0.1829 0.3035 0.0471  0.0223  0.0375  36  SER   A C   
248  O O   . SER   A 30  ? 0.2128 0.1895 0.3081 0.0491  0.0256  0.0329  36  SER   A O   
249  C CB  A SER   A 30  ? 0.2134 0.1639 0.3117 0.0467  0.0287  0.0301  36  SER   A CB  
250  C CB  B SER   A 30  ? 0.2461 0.1954 0.3419 0.0461  0.0289  0.0279  36  SER   A CB  
251  O OG  A SER   A 30  ? 0.2280 0.1724 0.3338 0.0520  0.0371  0.0283  36  SER   A OG  
252  O OG  B SER   A 30  ? 0.2947 0.2481 0.4057 0.0491  0.0288  0.0399  36  SER   A OG  
253  N N   . SER   A 31  ? 0.2006 0.1904 0.3084 0.0471  0.0186  0.0498  37  SER   A N   
254  C CA  . SER   A 31  ? 0.1971 0.2013 0.3141 0.0496  0.0182  0.0588  37  SER   A CA  
255  C C   . SER   A 31  ? 0.1831 0.1963 0.2880 0.0458  0.0148  0.0541  37  SER   A C   
256  O O   . SER   A 31  ? 0.1939 0.2152 0.3041 0.0484  0.0163  0.0577  37  SER   A O   
257  C CB  . SER   A 31  ? 0.2181 0.2366 0.3469 0.0483  0.0137  0.0740  37  SER   A CB  
258  O OG  . SER   A 31  ? 0.2838 0.3129 0.4014 0.0399  0.0063  0.0749  37  SER   A OG  
259  N N   . ARG   A 32  ? 0.1631 0.1742 0.2532 0.0401  0.0109  0.0462  38  ARG   A N   
260  C CA  . ARG   A 32  ? 0.1632 0.1807 0.2422 0.0362  0.0082  0.0412  38  ARG   A CA  
261  C C   . ARG   A 32  ? 0.1655 0.1716 0.2348 0.0370  0.0107  0.0298  38  ARG   A C   
262  O O   . ARG   A 32  ? 0.1598 0.1698 0.2210 0.0344  0.0089  0.0259  38  ARG   A O   
263  C CB  . ARG   A 32  ? 0.1690 0.1923 0.2398 0.0289  0.0030  0.0408  38  ARG   A CB  
264  C CG  . ARG   A 32  ? 0.1780 0.2161 0.2548 0.0251  -0.0004 0.0521  38  ARG   A CG  
265  C CD  . ARG   A 32  ? 0.1776 0.2207 0.2452 0.0166  -0.0040 0.0503  38  ARG   A CD  
266  N NE  . ARG   A 32  ? 0.1609 0.2074 0.2187 0.0124  -0.0043 0.0441  38  ARG   A NE  
267  C CZ  . ARG   A 32  ? 0.1921 0.2473 0.2431 0.0040  -0.0060 0.0440  38  ARG   A CZ  
268  N NH1 . ARG   A 32  ? 0.2072 0.2702 0.2588 -0.0020 -0.0083 0.0499  38  ARG   A NH1 
269  N NH2 . ARG   A 32  ? 0.1701 0.2263 0.2133 0.0007  -0.0050 0.0380  38  ARG   A NH2 
270  N N   . ASP   A 33  ? 0.1627 0.1552 0.2319 0.0393  0.0146  0.0244  39  ASP   A N   
271  C CA  . ASP   A 33  ? 0.1559 0.1387 0.2144 0.0378  0.0160  0.0142  39  ASP   A CA  
272  C C   . ASP   A 33  ? 0.1596 0.1440 0.2081 0.0325  0.0106  0.0103  39  ASP   A C   
273  O O   . ASP   A 33  ? 0.1677 0.1508 0.2084 0.0307  0.0099  0.0050  39  ASP   A O   
274  C CB  . ASP   A 33  ? 0.1609 0.1444 0.2177 0.0399  0.0197  0.0111  39  ASP   A CB  
275  C CG  . ASP   A 33  ? 0.1924 0.1666 0.2380 0.0371  0.0213  0.0015  39  ASP   A CG  
276  O OD1 . ASP   A 33  ? 0.2107 0.1745 0.2533 0.0354  0.0231  -0.0030 39  ASP   A OD1 
277  O OD2 . ASP   A 33  ? 0.2000 0.1782 0.2394 0.0356  0.0204  -0.0010 39  ASP   A OD2 
278  N N   . LEU   A 34  ? 0.1574 0.1445 0.2071 0.0298  0.0072  0.0132  40  LEU   A N   
279  C CA  . LEU   A 34  ? 0.1439 0.1326 0.1868 0.0254  0.0034  0.0096  40  LEU   A CA  
280  C C   . LEU   A 34  ? 0.1547 0.1365 0.1966 0.0232  0.0023  0.0074  40  LEU   A C   
281  O O   . LEU   A 34  ? 0.1642 0.1432 0.2113 0.0240  0.0033  0.0107  40  LEU   A O   
282  C CB  . LEU   A 34  ? 0.1456 0.1452 0.1894 0.0223  0.0010  0.0139  40  LEU   A CB  
283  C CG  . LEU   A 34  ? 0.1682 0.1758 0.2104 0.0220  0.0011  0.0150  40  LEU   A CG  
284  C CD1 . LEU   A 34  ? 0.1762 0.1940 0.2176 0.0167  -0.0007 0.0183  40  LEU   A CD1 
285  C CD2 . LEU   A 34  ? 0.1764 0.1801 0.2123 0.0217  0.0011  0.0089  40  LEU   A CD2 
286  N N   . LEU   A 35  ? 0.1506 0.1306 0.1872 0.0203  0.0002  0.0028  41  LEU   A N   
287  C CA  . LEU   A 35  ? 0.1490 0.1252 0.1852 0.0175  -0.0015 0.0013  41  LEU   A CA  
288  C C   . LEU   A 35  ? 0.1567 0.1380 0.1917 0.0147  -0.0040 -0.0001 41  LEU   A C   
289  O O   . LEU   A 35  ? 0.1640 0.1472 0.1968 0.0149  -0.0045 -0.0016 41  LEU   A O   
290  C CB  . LEU   A 35  ? 0.1598 0.1262 0.1920 0.0166  -0.0003 -0.0031 41  LEU   A CB  
291  C CG  . LEU   A 35  ? 0.1715 0.1344 0.2028 0.0127  -0.0023 -0.0045 41  LEU   A CG  
292  C CD1 . LEU   A 35  ? 0.1948 0.1466 0.2236 0.0117  0.0008  -0.0075 41  LEU   A CD1 
293  C CD2 . LEU   A 35  ? 0.1721 0.1385 0.2003 0.0093  -0.0059 -0.0065 41  LEU   A CD2 
294  N N   . VAL   A 36  ? 0.1454 0.1289 0.1830 0.0122  -0.0051 0.0008  42  VAL   A N   
295  C CA  . VAL   A 36  ? 0.1395 0.1271 0.1790 0.0099  -0.0060 -0.0005 42  VAL   A CA  
296  C C   . VAL   A 36  ? 0.1428 0.1282 0.1841 0.0076  -0.0077 -0.0014 42  VAL   A C   
297  O O   . VAL   A 36  ? 0.1504 0.1334 0.1921 0.0064  -0.0077 -0.0004 42  VAL   A O   
298  C CB  . VAL   A 36  ? 0.1439 0.1381 0.1853 0.0077  -0.0043 0.0008  42  VAL   A CB  
299  C CG1 . VAL   A 36  ? 0.1593 0.1561 0.2044 0.0056  -0.0032 -0.0014 42  VAL   A CG1 
300  C CG2 . VAL   A 36  ? 0.1693 0.1673 0.2085 0.0088  -0.0032 0.0023  42  VAL   A CG2 
301  N N   . SER   A 37  ? 0.1417 0.1280 0.1843 0.0068  -0.0094 -0.0023 43  SER   A N   
302  C CA  . SER   A 37  ? 0.1419 0.1285 0.1875 0.0041  -0.0116 -0.0020 43  SER   A CA  
303  C C   . SER   A 37  ? 0.1566 0.1495 0.2109 0.0037  -0.0109 -0.0010 43  SER   A C   
304  O O   . SER   A 37  ? 0.1571 0.1523 0.2139 0.0053  -0.0086 -0.0012 43  SER   A O   
305  C CB  . SER   A 37  ? 0.1674 0.1512 0.2085 0.0023  -0.0145 -0.0026 43  SER   A CB  
306  O OG  . SER   A 37  ? 0.1799 0.1665 0.2207 0.0032  -0.0156 -0.0018 43  SER   A OG  
307  N N   . SER   A 38  ? 0.1708 0.1660 0.2304 0.0014  -0.0119 0.0000  44  SER   A N   
308  C CA  . SER   A 38  ? 0.1765 0.1775 0.2473 0.0015  -0.0101 0.0012  44  SER   A CA  
309  C C   . SER   A 38  ? 0.1920 0.1968 0.2690 0.0020  -0.0133 0.0049  44  SER   A C   
310  O O   . SER   A 38  ? 0.2115 0.2157 0.2834 -0.0002 -0.0180 0.0064  44  SER   A O   
311  C CB  . SER   A 38  ? 0.2097 0.2131 0.2852 -0.0012 -0.0091 0.0011  44  SER   A CB  
312  O OG  . SER   A 38  ? 0.2399 0.2425 0.3130 -0.0037 -0.0137 0.0027  44  SER   A OG  
313  N N   . THR   A 39  ? 0.1873 0.1958 0.2756 0.0041  -0.0103 0.0066  45  THR   A N   
314  C CA  . THR   A 39  ? 0.2017 0.2151 0.2992 0.0049  -0.0133 0.0122  45  THR   A CA  
315  C C   . THR   A 39  ? 0.2195 0.2392 0.3348 0.0056  -0.0108 0.0158  45  THR   A C   
316  O O   . THR   A 39  ? 0.2114 0.2301 0.3319 0.0062  -0.0044 0.0121  45  THR   A O   
317  C CB  . THR   A 39  ? 0.2149 0.2266 0.3130 0.0078  -0.0114 0.0126  45  THR   A CB  
318  O OG1 . THR   A 39  ? 0.2239 0.2339 0.3290 0.0097  -0.0039 0.0095  45  THR   A OG1 
319  C CG2 . THR   A 39  ? 0.2309 0.2373 0.3132 0.0076  -0.0129 0.0093  45  THR   A CG2 
320  N N   . THR   A 40  ? 0.2256 0.2525 0.3508 0.0050  -0.0155 0.0233  46  THR   A N   
321  C CA  . THR   A 40  ? 0.2435 0.2778 0.3892 0.0065  -0.0130 0.0283  46  THR   A CA  
322  C C   . THR   A 40  ? 0.2487 0.2817 0.4083 0.0113  -0.0064 0.0296  46  THR   A C   
323  O O   . THR   A 40  ? 0.2698 0.3027 0.4428 0.0134  0.0016  0.0277  46  THR   A O   
324  C CB  . THR   A 40  ? 0.2843 0.3288 0.4365 0.0033  -0.0211 0.0375  46  THR   A CB  
325  O OG1 . THR   A 40  ? 0.3353 0.3820 0.4849 0.0027  -0.0264 0.0429  46  THR   A OG1 
326  C CG2 . THR   A 40  ? 0.2940 0.3383 0.4325 -0.0025 -0.0262 0.0351  46  THR   A CG2 
327  N N   . ALA   A 41  ? 0.2490 0.2803 0.4050 0.0126  -0.0089 0.0322  47  ALA   A N   
328  C CA  . ALA   A 41  ? 0.2519 0.2806 0.4204 0.0168  -0.0026 0.0335  47  ALA   A CA  
329  C C   . ALA   A 41  ? 0.2450 0.2637 0.4015 0.0171  0.0043  0.0236  47  ALA   A C   
330  O O   . ALA   A 41  ? 0.2423 0.2574 0.3798 0.0148  0.0015  0.0185  47  ALA   A O   
331  C CB  . ALA   A 41  ? 0.2709 0.3035 0.4420 0.0172  -0.0090 0.0422  47  ALA   A CB  
332  N N   . GLN   A 42  ? 0.2328 0.2474 0.4010 0.0196  0.0136  0.0214  48  GLN   A N   
333  C CA  . GLN   A 42  ? 0.2399 0.2463 0.3973 0.0183  0.0205  0.0125  48  GLN   A CA  
334  C C   . GLN   A 42  ? 0.2295 0.2331 0.3797 0.0192  0.0174  0.0144  48  GLN   A C   
335  O O   . GLN   A 42  ? 0.2429 0.2486 0.4047 0.0219  0.0152  0.0221  48  GLN   A O   
336  C CB  . GLN   A 42  ? 0.2576 0.2598 0.4293 0.0189  0.0330  0.0081  48  GLN   A CB  
337  C CG  . GLN   A 42  ? 0.3236 0.3279 0.4985 0.0166  0.0379  0.0035  48  GLN   A CG  
338  C CD  . GLN   A 42  ? 0.4015 0.4005 0.5889 0.0161  0.0520  -0.0025 48  GLN   A CD  
339  O OE1 . GLN   A 42  ? 0.4082 0.4074 0.6183 0.0202  0.0576  0.0020  48  GLN   A OE1 
340  N NE2 . GLN   A 42  ? 0.4278 0.4220 0.6011 0.0104  0.0585  -0.0125 48  GLN   A NE2 
341  N N   . GLY   A 43  ? 0.1925 0.1921 0.3244 0.0167  0.0172  0.0082  49  GLY   A N   
342  C CA  . GLY   A 43  ? 0.1941 0.1913 0.3174 0.0170  0.0148  0.0090  49  GLY   A CA  
343  C C   . GLY   A 43  ? 0.1784 0.1695 0.3047 0.0166  0.0235  0.0049  49  GLY   A C   
344  O O   . GLY   A 43  ? 0.1900 0.1778 0.3212 0.0148  0.0323  -0.0008 49  GLY   A O   
345  N N   . CYS   A 44  ? 0.1744 0.1637 0.2957 0.0171  0.0212  0.0070  50  CYS   A N   
346  C CA  . CYS   A 44  ? 0.1858 0.1686 0.3102 0.0162  0.0292  0.0038  50  CYS   A CA  
347  C C   . CYS   A 44  ? 0.1914 0.1721 0.2980 0.0121  0.0303  -0.0024 50  CYS   A C   
348  O O   . CYS   A 44  ? 0.2076 0.1828 0.3147 0.0100  0.0372  -0.0058 50  CYS   A O   
349  C CB  . CYS   A 44  ? 0.1938 0.1761 0.3306 0.0196  0.0274  0.0121  50  CYS   A CB  
350  S SG  . CYS   A 44  ? 0.2396 0.2253 0.4034 0.0242  0.0284  0.0213  50  CYS   A SG  
351  N N   . ASP   A 45  ? 0.1707 0.1558 0.2627 0.0110  0.0237  -0.0031 51  ASP   A N   
352  C CA  . ASP   A 45  ? 0.1634 0.1487 0.2406 0.0074  0.0242  -0.0073 51  ASP   A CA  
353  C C   . ASP   A 45  ? 0.1913 0.1761 0.2640 0.0020  0.0309  -0.0141 51  ASP   A C   
354  O O   . ASP   A 45  ? 0.2031 0.1890 0.2796 0.0014  0.0324  -0.0156 51  ASP   A O   
355  C CB  . ASP   A 45  ? 0.1564 0.1465 0.2224 0.0086  0.0160  -0.0050 51  ASP   A CB  
356  C CG  . ASP   A 45  ? 0.1787 0.1699 0.2450 0.0117  0.0099  0.0006  51  ASP   A CG  
357  O OD1 . ASP   A 45  ? 0.1852 0.1744 0.2546 0.0119  0.0111  0.0026  51  ASP   A OD1 
358  O OD2 . ASP   A 45  ? 0.1821 0.1760 0.2445 0.0129  0.0041  0.0027  51  ASP   A OD2 
359  N N   . THR   A 46  ? 0.2011 0.1850 0.2657 -0.0029 0.0349  -0.0180 52  THR   A N   
360  C CA  . THR   A 46  ? 0.2215 0.2067 0.2784 -0.0107 0.0407  -0.0243 52  THR   A CA  
361  C C   . THR   A 46  ? 0.2042 0.1970 0.2470 -0.0136 0.0350  -0.0227 52  THR   A C   
362  O O   . THR   A 46  ? 0.2116 0.2055 0.2506 -0.0114 0.0311  -0.0197 52  THR   A O   
363  C CB  . THR   A 46  ? 0.2937 0.2721 0.3525 -0.0159 0.0507  -0.0299 52  THR   A CB  
364  O OG1 . THR   A 46  ? 0.3433 0.3150 0.4183 -0.0129 0.0575  -0.0312 52  THR   A OG1 
365  C CG2 . THR   A 46  ? 0.3378 0.3189 0.3841 -0.0267 0.0562  -0.0366 52  THR   A CG2 
366  N N   . ILE   A 47  ? 0.1943 0.1928 0.2304 -0.0182 0.0344  -0.0238 53  ILE   A N   
367  C CA  . ILE   A 47  ? 0.1803 0.1873 0.2062 -0.0207 0.0292  -0.0204 53  ILE   A CA  
368  C C   . ILE   A 47  ? 0.1901 0.2008 0.2070 -0.0305 0.0337  -0.0237 53  ILE   A C   
369  O O   . ILE   A 47  ? 0.2019 0.2113 0.2165 -0.0385 0.0407  -0.0295 53  ILE   A O   
370  C CB  . ILE   A 47  ? 0.1728 0.1856 0.1972 -0.0211 0.0254  -0.0178 53  ILE   A CB  
371  C CG1 . ILE   A 47  ? 0.1866 0.1952 0.2191 -0.0132 0.0219  -0.0157 53  ILE   A CG1 
372  C CG2 . ILE   A 47  ? 0.1734 0.1956 0.1911 -0.0221 0.0198  -0.0121 53  ILE   A CG2 
373  C CD1 . ILE   A 47  ? 0.1937 0.2005 0.2278 -0.0056 0.0162  -0.0116 53  ILE   A CD1 
374  N N   . ALA   A 48  ? 0.1708 0.1870 0.1821 -0.0308 0.0299  -0.0201 54  ALA   A N   
375  C CA  . ALA   A 48  ? 0.1718 0.1941 0.1735 -0.0410 0.0325  -0.0217 54  ALA   A CA  
376  C C   . ALA   A 48  ? 0.1879 0.2214 0.1830 -0.0490 0.0308  -0.0195 54  ALA   A C   
377  O O   . ALA   A 48  ? 0.1907 0.2299 0.1883 -0.0443 0.0247  -0.0133 54  ALA   A O   
378  C CB  . ALA   A 48  ? 0.1685 0.1958 0.1677 -0.0382 0.0278  -0.0167 54  ALA   A CB  
379  N N   . ARG   A 49  ? 0.2133 0.2499 0.1996 -0.0620 0.0366  -0.0244 55  ARG   A N   
380  C CA  . ARG   A 49  ? 0.2233 0.2726 0.2017 -0.0721 0.0347  -0.0215 55  ARG   A CA  
381  C C   . ARG   A 49  ? 0.2539 0.3119 0.2216 -0.0837 0.0357  -0.0214 55  ARG   A C   
382  O O   . ARG   A 49  ? 0.2758 0.3315 0.2351 -0.0960 0.0434  -0.0293 55  ARG   A O   
383  C CB  . ARG   A 49  ? 0.2275 0.2726 0.2043 -0.0790 0.0416  -0.0287 55  ARG   A CB  
384  C CG  . ARG   A 49  ? 0.2327 0.2690 0.2211 -0.0680 0.0414  -0.0293 55  ARG   A CG  
385  C CD  . ARG   A 49  ? 0.2146 0.2575 0.2071 -0.0605 0.0320  -0.0200 55  ARG   A CD  
386  N NE  . ARG   A 49  ? 0.2030 0.2373 0.2054 -0.0515 0.0321  -0.0213 55  ARG   A NE  
387  C CZ  . ARG   A 49  ? 0.2207 0.2556 0.2288 -0.0425 0.0253  -0.0151 55  ARG   A CZ  
388  N NH1 . ARG   A 49  ? 0.2061 0.2490 0.2125 -0.0406 0.0187  -0.0072 55  ARG   A NH1 
389  N NH2 . ARG   A 49  ? 0.2430 0.2704 0.2591 -0.0357 0.0256  -0.0166 55  ARG   A NH2 
390  N N   . CYS   A 50  ? 0.2399 0.3083 0.2082 -0.0804 0.0282  -0.0123 56  CYS   A N   
391  C CA  . CYS   A 50  ? 0.2600 0.3375 0.2205 -0.0890 0.0276  -0.0104 56  CYS   A CA  
392  C C   . CYS   A 50  ? 0.2631 0.3563 0.2275 -0.0848 0.0184  0.0024  56  CYS   A C   
393  O O   . CYS   A 50  ? 0.2715 0.3664 0.2448 -0.0748 0.0133  0.0090  56  CYS   A O   
394  C CB  . CYS   A 50  ? 0.2537 0.3180 0.2162 -0.0840 0.0321  -0.0164 56  CYS   A CB  
395  S SG  . CYS   A 50  ? 0.2455 0.3046 0.2207 -0.0650 0.0258  -0.0105 56  CYS   A SG  
396  N N   . ASP   A 51  ? 0.3003 0.4045 0.2589 -0.0923 0.0169  0.0060  57  ASP   A N   
397  C CA  . ASP   A 51  ? 0.3210 0.4401 0.2861 -0.0873 0.0092  0.0185  57  ASP   A CA  
398  C C   . ASP   A 51  ? 0.3055 0.4213 0.2723 -0.0818 0.0096  0.0178  57  ASP   A C   
399  O O   . ASP   A 51  ? 0.3092 0.4396 0.2773 -0.0838 0.0055  0.0261  57  ASP   A O   
400  C CB  . ASP   A 51  ? 0.3971 0.5385 0.3564 -0.1014 0.0050  0.0277  57  ASP   A CB  
401  C CG  . ASP   A 51  ? 0.5073 0.6543 0.4524 -0.1183 0.0086  0.0229  57  ASP   A CG  
402  O OD1 . ASP   A 51  ? 0.5296 0.6608 0.4692 -0.1195 0.0158  0.0110  57  ASP   A OD1 
403  O OD2 . ASP   A 51  ? 0.5549 0.7223 0.4946 -0.1312 0.0044  0.0314  57  ASP   A OD2 
404  N N   . CYS   A 52  ? 0.2775 0.3752 0.2456 -0.0748 0.0142  0.0089  58  CYS   A N   
405  C CA  . CYS   A 52  ? 0.2555 0.3495 0.2255 -0.0692 0.0143  0.0087  58  CYS   A CA  
406  C C   . CYS   A 52  ? 0.2439 0.3465 0.2239 -0.0580 0.0083  0.0184  58  CYS   A C   
407  O O   . CYS   A 52  ? 0.2417 0.3439 0.2297 -0.0496 0.0056  0.0224  58  CYS   A O   
408  C CB  . CYS   A 52  ? 0.2548 0.3289 0.2272 -0.0622 0.0190  0.0000  58  CYS   A CB  
409  S SG  . CYS   A 52  ? 0.2500 0.3109 0.2145 -0.0734 0.0288  -0.0119 58  CYS   A SG  
410  N N   . GLN   A 53  ? 0.1993 0.3096 0.1791 -0.0587 0.0070  0.0221  59  GLN   A N   
411  C CA  . GLN   A 53  ? 0.1996 0.3163 0.1891 -0.0483 0.0035  0.0296  59  GLN   A CA  
412  C C   . GLN   A 53  ? 0.1683 0.2758 0.1573 -0.0428 0.0056  0.0253  59  GLN   A C   
413  O O   . GLN   A 53  ? 0.1773 0.2910 0.1721 -0.0369 0.0040  0.0303  59  GLN   A O   
414  C CB  . GLN   A 53  ? 0.2391 0.3777 0.2321 -0.0532 -0.0005 0.0409  59  GLN   A CB  
415  C CG  . GLN   A 53  ? 0.2993 0.4490 0.2982 -0.0544 -0.0040 0.0492  59  GLN   A CG  
416  C CD  . GLN   A 53  ? 0.3527 0.5255 0.3596 -0.0568 -0.0084 0.0631  59  GLN   A CD  
417  O OE1 . GLN   A 53  ? 0.3796 0.5688 0.3817 -0.0697 -0.0112 0.0691  59  GLN   A OE1 
418  N NE2 . GLN   A 53  ? 0.3213 0.4972 0.3412 -0.0454 -0.0089 0.0690  59  GLN   A NE2 
419  N N   . THR   A 54  ? 0.1566 0.2499 0.1391 -0.0457 0.0095  0.0165  60  THR   A N   
420  C CA  . THR   A 54  ? 0.1659 0.2491 0.1486 -0.0405 0.0111  0.0130  60  THR   A CA  
421  C C   . THR   A 54  ? 0.1635 0.2292 0.1475 -0.0359 0.0136  0.0064  60  THR   A C   
422  O O   . THR   A 54  ? 0.1829 0.2431 0.1650 -0.0403 0.0163  0.0021  60  THR   A O   
423  C CB  . THR   A 54  ? 0.2119 0.2969 0.1872 -0.0492 0.0133  0.0111  60  THR   A CB  
424  O OG1 . THR   A 54  ? 0.2813 0.3586 0.2498 -0.0587 0.0179  0.0044  60  THR   A OG1 
425  C CG2 . THR   A 54  ? 0.2142 0.3183 0.1884 -0.0549 0.0106  0.0183  60  THR   A CG2 
426  N N   . GLY   A 55  ? 0.1408 0.1993 0.1286 -0.0274 0.0127  0.0062  61  GLY   A N   
427  C CA  . GLY   A 55  ? 0.1422 0.1866 0.1330 -0.0228 0.0140  0.0020  61  GLY   A CA  
428  C C   . GLY   A 55  ? 0.1347 0.1746 0.1277 -0.0161 0.0122  0.0032  61  GLY   A C   
429  O O   . GLY   A 55  ? 0.1448 0.1902 0.1355 -0.0163 0.0114  0.0054  61  GLY   A O   
430  N N   . VAL   A 56  ? 0.1288 0.1594 0.1258 -0.0109 0.0115  0.0018  62  VAL   A N   
431  C CA  . VAL   A 56  ? 0.1261 0.1527 0.1240 -0.0063 0.0095  0.0032  62  VAL   A CA  
432  C C   . VAL   A 56  ? 0.1309 0.1550 0.1321 -0.0006 0.0071  0.0034  62  VAL   A C   
433  O O   . VAL   A 56  ? 0.1477 0.1680 0.1523 -0.0001 0.0075  0.0019  62  VAL   A O   
434  C CB  . VAL   A 56  ? 0.1528 0.1702 0.1529 -0.0083 0.0113  0.0022  62  VAL   A CB  
435  C CG1 . VAL   A 56  ? 0.1867 0.2010 0.1881 -0.0047 0.0082  0.0050  62  VAL   A CG1 
436  C CG2 . VAL   A 56  ? 0.1551 0.1734 0.1511 -0.0149 0.0145  0.0013  62  VAL   A CG2 
437  N N   . TYR   A 57  ? 0.1262 0.1522 0.1258 0.0030  0.0052  0.0047  63  TYR   A N   
438  C CA  . TYR   A 57  ? 0.1238 0.1463 0.1253 0.0070  0.0036  0.0040  63  TYR   A CA  
439  C C   . TYR   A 57  ? 0.1339 0.1527 0.1330 0.0073  0.0015  0.0046  63  TYR   A C   
440  O O   . TYR   A 57  ? 0.1405 0.1616 0.1359 0.0056  0.0014  0.0057  63  TYR   A O   
441  C CB  . TYR   A 57  ? 0.1259 0.1531 0.1280 0.0102  0.0044  0.0043  63  TYR   A CB  
442  C CG  . TYR   A 57  ? 0.1288 0.1592 0.1282 0.0118  0.0056  0.0044  63  TYR   A CG  
443  C CD1 . TYR   A 57  ? 0.1513 0.1891 0.1495 0.0102  0.0070  0.0062  63  TYR   A CD1 
444  C CD2 . TYR   A 57  ? 0.1470 0.1733 0.1448 0.0140  0.0060  0.0023  63  TYR   A CD2 
445  C CE1 . TYR   A 57  ? 0.1603 0.2015 0.1570 0.0117  0.0091  0.0060  63  TYR   A CE1 
446  C CE2 . TYR   A 57  ? 0.1561 0.1848 0.1511 0.0147  0.0087  0.0012  63  TYR   A CE2 
447  C CZ  . TYR   A 57  ? 0.1644 0.2005 0.1594 0.0139  0.0104  0.0031  63  TYR   A CZ  
448  O OH  . TYR   A 57  ? 0.1850 0.2238 0.1781 0.0146  0.0140  0.0017  63  TYR   A OH  
449  N N   . TYR   A 58  ? 0.1279 0.1425 0.1286 0.0087  -0.0005 0.0042  64  TYR   A N   
450  C CA  . TYR   A 58  ? 0.1335 0.1467 0.1309 0.0075  -0.0032 0.0055  64  TYR   A CA  
451  C C   . TYR   A 58  ? 0.1426 0.1568 0.1342 0.0081  -0.0022 0.0028  64  TYR   A C   
452  O O   . TYR   A 58  ? 0.1459 0.1583 0.1388 0.0104  -0.0009 0.0004  64  TYR   A O   
453  C CB  . TYR   A 58  ? 0.1384 0.1477 0.1410 0.0073  -0.0062 0.0074  64  TYR   A CB  
454  C CG  . TYR   A 58  ? 0.1562 0.1663 0.1551 0.0043  -0.0100 0.0103  64  TYR   A CG  
455  C CD1 . TYR   A 58  ? 0.1638 0.1759 0.1616 0.0016  -0.0115 0.0143  64  TYR   A CD1 
456  C CD2 . TYR   A 58  ? 0.1550 0.1647 0.1510 0.0029  -0.0123 0.0095  64  TYR   A CD2 
457  C CE1 . TYR   A 58  ? 0.1818 0.1967 0.1754 -0.0026 -0.0156 0.0181  64  TYR   A CE1 
458  C CE2 . TYR   A 58  ? 0.1650 0.1772 0.1556 -0.0020 -0.0161 0.0124  64  TYR   A CE2 
459  C CZ  . TYR   A 58  ? 0.1778 0.1932 0.1678 -0.0048 -0.0181 0.0173  64  TYR   A CZ  
460  O OH  . TYR   A 58  ? 0.2127 0.2324 0.1970 -0.0110 -0.0226 0.0215  64  TYR   A OH  
461  N N   . CYS   A 59  ? 0.1439 0.1605 0.1291 0.0054  -0.0023 0.0030  65  CYS   A N   
462  C CA  . CYS   A 59  ? 0.1548 0.1718 0.1335 0.0046  0.0004  -0.0006 65  CYS   A CA  
463  C C   . CYS   A 59  ? 0.1700 0.1859 0.1417 -0.0008 -0.0029 -0.0001 65  CYS   A C   
464  O O   . CYS   A 59  ? 0.1697 0.1888 0.1373 -0.0050 -0.0053 0.0031  65  CYS   A O   
465  C CB  . CYS   A 59  ? 0.1721 0.1942 0.1483 0.0047  0.0039  -0.0011 65  CYS   A CB  
466  S SG  . CYS   A 59  ? 0.1749 0.1971 0.1437 0.0030  0.0094  -0.0065 65  CYS   A SG  
467  N N   . SER   A 60  ? 0.1592 0.1713 0.1295 -0.0018 -0.0036 -0.0024 66  SER   A N   
468  C CA  . SER   A 60  ? 0.1729 0.1858 0.1364 -0.0087 -0.0078 -0.0008 66  SER   A CA  
469  C C   . SER   A 60  ? 0.1815 0.1967 0.1331 -0.0148 -0.0055 -0.0038 66  SER   A C   
470  O O   . SER   A 60  ? 0.2007 0.2202 0.1465 -0.0217 -0.0101 0.0003  66  SER   A O   
471  C CB  . SER   A 60  ? 0.2052 0.2140 0.1690 -0.0095 -0.0088 -0.0029 66  SER   A CB  
472  O OG  . SER   A 60  ? 0.2517 0.2557 0.2106 -0.0092 -0.0028 -0.0103 66  SER   A OG  
473  N N   . SER   A 61  ? 0.1671 0.1806 0.1161 -0.0125 0.0020  -0.0102 67  SER   A N   
474  C CA  . SER   A 61  ? 0.1715 0.1869 0.1096 -0.0182 0.0062  -0.0144 67  SER   A CA  
475  C C   . SER   A 61  ? 0.1716 0.1937 0.1075 -0.0203 0.0047  -0.0103 67  SER   A C   
476  O O   . SER   A 61  ? 0.1982 0.2230 0.1243 -0.0262 0.0077  -0.0132 67  SER   A O   
477  C CB  . SER   A 61  ? 0.1898 0.2007 0.1288 -0.0145 0.0159  -0.0221 67  SER   A CB  
478  O OG  . SER   A 61  ? 0.2002 0.2134 0.1498 -0.0062 0.0189  -0.0204 67  SER   A OG  
479  N N   . ARG   A 62  ? 0.1704 0.1948 0.1148 -0.0165 0.0002  -0.0038 68  ARG   A N   
480  C CA  . ARG   A 62  ? 0.1764 0.2060 0.1197 -0.0188 -0.0021 0.0012  68  ARG   A CA  
481  C C   . ARG   A 62  ? 0.1948 0.2252 0.1432 -0.0205 -0.0097 0.0096  68  ARG   A C   
482  O O   . ARG   A 62  ? 0.2060 0.2397 0.1549 -0.0226 -0.0118 0.0148  68  ARG   A O   
483  C CB  . ARG   A 62  ? 0.1842 0.2157 0.1340 -0.0129 0.0019  0.0007  68  ARG   A CB  
484  C CG  . ARG   A 62  ? 0.1979 0.2307 0.1458 -0.0108 0.0097  -0.0056 68  ARG   A CG  
485  C CD  . ARG   A 62  ? 0.2008 0.2381 0.1390 -0.0168 0.0122  -0.0071 68  ARG   A CD  
486  N NE  . ARG   A 62  ? 0.2150 0.2536 0.1536 -0.0144 0.0212  -0.0132 68  ARG   A NE  
487  C CZ  . ARG   A 62  ? 0.2229 0.2573 0.1567 -0.0162 0.0274  -0.0203 68  ARG   A CZ  
488  N NH1 . ARG   A 62  ? 0.2436 0.2729 0.1698 -0.0216 0.0247  -0.0223 68  ARG   A NH1 
489  N NH2 . ARG   A 62  ? 0.2484 0.2838 0.1853 -0.0133 0.0369  -0.0253 68  ARG   A NH2 
490  N N   . ARG   A 63  ? 0.1919 0.2192 0.1462 -0.0190 -0.0130 0.0116  69  ARG   A N   
491  C CA  . ARG   A 63  ? 0.2051 0.2325 0.1689 -0.0186 -0.0187 0.0199  69  ARG   A CA  
492  C C   . ARG   A 63  ? 0.2179 0.2439 0.1895 -0.0144 -0.0169 0.0221  69  ARG   A C   
493  O O   . ARG   A 63  ? 0.2405 0.2677 0.2163 -0.0164 -0.0198 0.0290  69  ARG   A O   
494  C CB  . ARG   A 63  ? 0.2305 0.2634 0.1904 -0.0263 -0.0249 0.0275  69  ARG   A CB  
495  C CG  . ARG   A 63  ? 0.2355 0.2701 0.1898 -0.0315 -0.0278 0.0268  69  ARG   A CG  
496  C CD  . ARG   A 63  ? 0.2494 0.2913 0.2054 -0.0386 -0.0359 0.0381  69  ARG   A CD  
497  N NE  . ARG   A 63  ? 0.2793 0.3247 0.2260 -0.0464 -0.0389 0.0371  69  ARG   A NE  
498  C CZ  . ARG   A 63  ? 0.2547 0.3053 0.1855 -0.0569 -0.0395 0.0352  69  ARG   A CZ  
499  N NH1 . ARG   A 63  ? 0.2795 0.3327 0.2025 -0.0601 -0.0375 0.0346  69  ARG   A NH1 
500  N NH2 . ARG   A 63  ? 0.2825 0.3357 0.2042 -0.0652 -0.0417 0.0335  69  ARG   A NH2 
501  N N   . LYS   A 64  ? 0.1980 0.2220 0.1714 -0.0096 -0.0120 0.0166  70  LYS   A N   
502  C CA  . LYS   A 64  ? 0.1992 0.2228 0.1771 -0.0076 -0.0097 0.0175  70  LYS   A CA  
503  C C   . LYS   A 64  ? 0.1871 0.2079 0.1711 -0.0030 -0.0066 0.0141  70  LYS   A C   
504  O O   . LYS   A 64  ? 0.1848 0.2056 0.1677 -0.0004 -0.0048 0.0100  70  LYS   A O   
505  C CB  . LYS   A 64  ? 0.2459 0.2745 0.2163 -0.0095 -0.0068 0.0155  70  LYS   A CB  
506  C CG  . LYS   A 64  ? 0.3720 0.4037 0.3373 -0.0152 -0.0097 0.0204  70  LYS   A CG  
507  C CD  . LYS   A 64  ? 0.4886 0.5251 0.4486 -0.0168 -0.0063 0.0188  70  LYS   A CD  
508  C CE  . LYS   A 64  ? 0.5693 0.6095 0.5230 -0.0232 -0.0092 0.0236  70  LYS   A CE  
509  N NZ  . LYS   A 64  ? 0.6226 0.6645 0.5698 -0.0279 -0.0126 0.0248  70  LYS   A NZ  
510  N N   . HIS   A 65  ? 0.1693 0.1879 0.1592 -0.0027 -0.0054 0.0156  71  HIS   A N   
511  C CA  . HIS   A 65  ? 0.1607 0.1781 0.1544 -0.0006 -0.0020 0.0123  71  HIS   A CA  
512  C C   . HIS   A 65  ? 0.1812 0.2038 0.1706 -0.0024 0.0007  0.0112  71  HIS   A C   
513  O O   . HIS   A 65  ? 0.2154 0.2383 0.2030 -0.0055 0.0008  0.0134  71  HIS   A O   
514  C CB  . HIS   A 65  ? 0.1508 0.1620 0.1529 -0.0009 -0.0010 0.0138  71  HIS   A CB  
515  C CG  . HIS   A 65  ? 0.1677 0.1753 0.1764 0.0012  -0.0034 0.0156  71  HIS   A CG  
516  N ND1 . HIS   A 65  ? 0.2112 0.2167 0.2242 0.0034  -0.0021 0.0127  71  HIS   A ND1 
517  C CD2 . HIS   A 65  ? 0.1543 0.1616 0.1664 0.0005  -0.0074 0.0210  71  HIS   A CD2 
518  C CE1 . HIS   A 65  ? 0.1927 0.1962 0.2120 0.0045  -0.0049 0.0160  71  HIS   A CE1 
519  N NE2 . HIS   A 65  ? 0.2080 0.2130 0.2272 0.0027  -0.0084 0.0214  71  HIS   A NE2 
520  N N   . TYR   A 66  ? 0.1517 0.1790 0.1404 -0.0006 0.0028  0.0088  72  TYR   A N   
521  C CA  . TYR   A 66  ? 0.1586 0.1935 0.1447 -0.0024 0.0049  0.0090  72  TYR   A CA  
522  C C   . TYR   A 66  ? 0.1469 0.1844 0.1354 -0.0040 0.0066  0.0084  72  TYR   A C   
523  O O   . TYR   A 66  ? 0.1446 0.1816 0.1365 -0.0019 0.0067  0.0074  72  TYR   A O   
524  C CB  . TYR   A 66  ? 0.1592 0.2003 0.1442 0.0009  0.0063  0.0082  72  TYR   A CB  
525  C CG  . TYR   A 66  ? 0.1658 0.2064 0.1457 0.0005  0.0061  0.0076  72  TYR   A CG  
526  C CD1 . TYR   A 66  ? 0.1830 0.2277 0.1583 -0.0029 0.0065  0.0089  72  TYR   A CD1 
527  C CD2 . TYR   A 66  ? 0.1646 0.2010 0.1432 0.0023  0.0057  0.0054  72  TYR   A CD2 
528  C CE1 . TYR   A 66  ? 0.1946 0.2397 0.1638 -0.0046 0.0066  0.0081  72  TYR   A CE1 
529  C CE2 . TYR   A 66  ? 0.1799 0.2164 0.1518 0.0000  0.0060  0.0041  72  TYR   A CE2 
530  C CZ  . TYR   A 66  ? 0.2020 0.2432 0.1691 -0.0035 0.0066  0.0054  72  TYR   A CZ  
531  O OH  . TYR   A 66  ? 0.2417 0.2838 0.2009 -0.0073 0.0071  0.0040  72  TYR   A OH  
532  N N   . PRO   A 67  ? 0.1485 0.1893 0.1347 -0.0090 0.0081  0.0090  73  PRO   A N   
533  C CA  . PRO   A 67  ? 0.1420 0.1880 0.1284 -0.0129 0.0097  0.0086  73  PRO   A CA  
534  C C   . PRO   A 67  ? 0.1496 0.2078 0.1377 -0.0109 0.0093  0.0114  73  PRO   A C   
535  O O   . PRO   A 67  ? 0.1778 0.2424 0.1654 -0.0095 0.0095  0.0133  73  PRO   A O   
536  C CB  . PRO   A 67  ? 0.1688 0.2150 0.1510 -0.0200 0.0116  0.0084  73  PRO   A CB  
537  C CG  . PRO   A 67  ? 0.1885 0.2338 0.1687 -0.0186 0.0105  0.0102  73  PRO   A CG  
538  C CD  . PRO   A 67  ? 0.1610 0.2019 0.1434 -0.0124 0.0082  0.0104  73  PRO   A CD  
539  N N   . VAL   A 68  ? 0.1381 0.2003 0.1291 -0.0113 0.0092  0.0122  74  VAL   A N   
540  C CA  . VAL   A 68  ? 0.1501 0.2247 0.1458 -0.0089 0.0087  0.0168  74  VAL   A CA  
541  C C   . VAL   A 68  ? 0.1372 0.2209 0.1333 -0.0149 0.0081  0.0196  74  VAL   A C   
542  O O   . VAL   A 68  ? 0.1432 0.2216 0.1364 -0.0192 0.0085  0.0167  74  VAL   A O   
543  C CB  . VAL   A 68  ? 0.1723 0.2432 0.1739 -0.0009 0.0085  0.0168  74  VAL   A CB  
544  C CG1 . VAL   A 68  ? 0.1820 0.2479 0.1825 0.0036  0.0096  0.0147  74  VAL   A CG1 
545  C CG2 . VAL   A 68  ? 0.1919 0.2535 0.1936 -0.0004 0.0077  0.0139  74  VAL   A CG2 
546  N N   . SER   A 69  ? 0.1408 0.2396 0.1415 -0.0154 0.0073  0.0262  75  SER   A N   
547  C CA  . SER   A 69  ? 0.1512 0.2627 0.1544 -0.0205 0.0055  0.0318  75  SER   A CA  
548  C C   . SER   A 69  ? 0.1424 0.2555 0.1561 -0.0120 0.0048  0.0360  75  SER   A C   
549  O O   . SER   A 69  ? 0.1454 0.2578 0.1659 -0.0039 0.0064  0.0372  75  SER   A O   
550  C CB  . SER   A 69  ? 0.2013 0.3305 0.2064 -0.0252 0.0046  0.0387  75  SER   A CB  
551  O OG  . SER   A 69  ? 0.3059 0.4331 0.3009 -0.0337 0.0056  0.0347  75  SER   A OG  
552  N N   . PHE   A 70  ? 0.1355 0.2499 0.1504 -0.0143 0.0032  0.0378  76  PHE   A N   
553  C CA  . PHE   A 70  ? 0.1415 0.2556 0.1666 -0.0066 0.0028  0.0417  76  PHE   A CA  
554  C C   . PHE   A 70  ? 0.1445 0.2734 0.1746 -0.0114 -0.0001 0.0508  76  PHE   A C   
555  O O   . PHE   A 70  ? 0.1696 0.3057 0.1922 -0.0222 -0.0019 0.0515  76  PHE   A O   
556  C CB  . PHE   A 70  ? 0.1486 0.2452 0.1709 -0.0024 0.0037  0.0341  76  PHE   A CB  
557  C CG  . PHE   A 70  ? 0.1485 0.2384 0.1620 -0.0095 0.0035  0.0286  76  PHE   A CG  
558  C CD1 . PHE   A 70  ? 0.1467 0.2277 0.1524 -0.0129 0.0052  0.0217  76  PHE   A CD1 
559  C CD2 . PHE   A 70  ? 0.1485 0.2412 0.1627 -0.0131 0.0021  0.0305  76  PHE   A CD2 
560  C CE1 . PHE   A 70  ? 0.1599 0.2339 0.1600 -0.0189 0.0067  0.0164  76  PHE   A CE1 
561  C CE2 . PHE   A 70  ? 0.1667 0.2528 0.1734 -0.0199 0.0034  0.0244  76  PHE   A CE2 
562  C CZ  . PHE   A 70  ? 0.1644 0.2414 0.1646 -0.0228 0.0061  0.0173  76  PHE   A CZ  
563  N N   . SER   A 71  ? 0.1393 0.2736 0.1829 -0.0042 -0.0004 0.0584  77  SER   A N   
564  C CA  . SER   A 71  ? 0.1437 0.2939 0.1951 -0.0080 -0.0038 0.0698  77  SER   A CA  
565  C C   . SER   A 71  ? 0.1377 0.2823 0.1839 -0.0122 -0.0056 0.0675  77  SER   A C   
566  O O   . SER   A 71  ? 0.1451 0.2727 0.1848 -0.0098 -0.0037 0.0577  77  SER   A O   
567  C CB  . SER   A 71  ? 0.1633 0.3199 0.2337 0.0023  -0.0025 0.0795  77  SER   A CB  
568  O OG  . SER   A 71  ? 0.1917 0.3318 0.2666 0.0118  0.0008  0.0744  77  SER   A OG  
569  N N   . LYS   A 72  ? 0.1421 0.3021 0.1910 -0.0194 -0.0095 0.0772  78  LYS   A N   
570  C CA  . LYS   A 72  ? 0.1458 0.3028 0.1901 -0.0244 -0.0111 0.0762  78  LYS   A CA  
571  C C   . LYS   A 72  ? 0.1644 0.3116 0.2199 -0.0134 -0.0102 0.0779  78  LYS   A C   
572  O O   . LYS   A 72  ? 0.1705 0.3207 0.2406 -0.0042 -0.0092 0.0849  78  LYS   A O   
573  C CB  . LYS   A 72  ? 0.1779 0.3561 0.2210 -0.0370 -0.0159 0.0871  78  LYS   A CB  
574  C CG  . LYS   A 72  ? 0.2328 0.4181 0.2613 -0.0506 -0.0158 0.0828  78  LYS   A CG  
575  C CD  . LYS   A 72  ? 0.3060 0.5103 0.3282 -0.0666 -0.0201 0.0907  78  LYS   A CD  
576  C CE  . LYS   A 72  ? 0.3805 0.5882 0.3854 -0.0816 -0.0184 0.0835  78  LYS   A CE  
577  N NZ  . LYS   A 72  ? 0.4290 0.6482 0.4218 -0.0994 -0.0203 0.0851  78  LYS   A NZ  
578  N N   . PRO   A 73  ? 0.1645 0.3005 0.2146 -0.0144 -0.0100 0.0720  79  PRO   A N   
579  C CA  . PRO   A 73  ? 0.1680 0.2943 0.2281 -0.0048 -0.0090 0.0733  79  PRO   A CA  
580  C C   . PRO   A 73  ? 0.1712 0.3114 0.2475 -0.0021 -0.0114 0.0887  79  PRO   A C   
581  O O   . PRO   A 73  ? 0.1925 0.3493 0.2689 -0.0112 -0.0158 0.0982  79  PRO   A O   
582  C CB  . PRO   A 73  ? 0.2056 0.3230 0.2560 -0.0100 -0.0094 0.0663  79  PRO   A CB  
583  C CG  . PRO   A 73  ? 0.2364 0.3527 0.2721 -0.0193 -0.0083 0.0575  79  PRO   A CG  
584  C CD  . PRO   A 73  ? 0.1852 0.3163 0.2203 -0.0245 -0.0096 0.0631  79  PRO   A CD  
585  N N   . SER   A 74  ? 0.1590 0.2931 0.2494 0.0095  -0.0082 0.0914  80  SER   A N   
586  C CA  . SER   A 74  ? 0.1689 0.3155 0.2788 0.0139  -0.0092 0.1071  80  SER   A CA  
587  C C   . SER   A 74  ? 0.1587 0.2899 0.2814 0.0261  -0.0039 0.1059  80  SER   A C   
588  O O   . SER   A 74  ? 0.1639 0.2762 0.2789 0.0302  0.0001  0.0928  80  SER   A O   
589  C CB  . SER   A 74  ? 0.2275 0.3912 0.3461 0.0138  -0.0095 0.1159  80  SER   A CB  
590  O OG  . SER   A 74  ? 0.3152 0.4683 0.4353 0.0222  -0.0036 0.1079  80  SER   A OG  
591  N N   . LEU   A 75  ? 0.1713 0.3116 0.3150 0.0313  -0.0035 0.1206  81  LEU   A N   
592  C CA  . LEU   A 75  ? 0.1969 0.3231 0.3557 0.0425  0.0028  0.1211  81  LEU   A CA  
593  C C   . LEU   A 75  ? 0.2102 0.3364 0.3810 0.0510  0.0095  0.1212  81  LEU   A C   
594  O O   . LEU   A 75  ? 0.2248 0.3693 0.4111 0.0522  0.0087  0.1347  81  LEU   A O   
595  C CB  . LEU   A 75  ? 0.2090 0.3462 0.3862 0.0431  -0.0003 0.1386  81  LEU   A CB  
596  C CG  . LEU   A 75  ? 0.2555 0.3770 0.4486 0.0533  0.0061  0.1401  81  LEU   A CG  
597  C CD1 . LEU   A 75  ? 0.2826 0.3830 0.4596 0.0520  0.0073  0.1252  81  LEU   A CD1 
598  C CD2 . LEU   A 75  ? 0.2541 0.3895 0.4670 0.0531  0.0022  0.1602  81  LEU   A CD2 
599  N N   . ILE   A 76  ? 0.2071 0.3145 0.3700 0.0557  0.0160  0.1062  82  ILE   A N   
600  C CA  . ILE   A 76  ? 0.2242 0.3288 0.3936 0.0624  0.0235  0.1024  82  ILE   A CA  
601  C C   . ILE   A 76  ? 0.2341 0.3197 0.4137 0.0716  0.0335  0.0968  82  ILE   A C   
602  O O   . ILE   A 76  ? 0.2302 0.2985 0.3997 0.0710  0.0347  0.0868  82  ILE   A O   
603  C CB  . ILE   A 76  ? 0.2553 0.3541 0.4025 0.0574  0.0227  0.0880  82  ILE   A CB  
604  C CG1 . ILE   A 76  ? 0.2886 0.4037 0.4239 0.0472  0.0143  0.0913  82  ILE   A CG1 
605  C CG2 . ILE   A 76  ? 0.2755 0.3693 0.4262 0.0632  0.0309  0.0818  82  ILE   A CG2 
606  C CD1 . ILE   A 76  ? 0.3196 0.4561 0.4662 0.0464  0.0131  0.1032  82  ILE   A CD1 
607  N N   . PHE   A 77  ? 0.2397 0.3281 0.4389 0.0796  0.0415  0.1020  83  PHE   A N   
608  C CA  . PHE   A 77  ? 0.2528 0.3222 0.4619 0.0877  0.0533  0.0953  83  PHE   A CA  
609  C C   . PHE   A 77  ? 0.2751 0.3293 0.4639 0.0856  0.0582  0.0764  83  PHE   A C   
610  O O   . PHE   A 77  ? 0.3010 0.3628 0.4817 0.0831  0.0573  0.0731  83  PHE   A O   
611  C CB  . PHE   A 77  ? 0.2579 0.3363 0.4961 0.0968  0.0615  0.1072  83  PHE   A CB  
612  C CG  . PHE   A 77  ? 0.2989 0.3562 0.5469 0.1046  0.0760  0.0983  83  PHE   A CG  
613  C CD1 . PHE   A 77  ? 0.3304 0.3749 0.5916 0.1092  0.0809  0.1013  83  PHE   A CD1 
614  C CD2 . PHE   A 77  ? 0.3355 0.3845 0.5771 0.1059  0.0852  0.0854  83  PHE   A CD2 
615  C CE1 . PHE   A 77  ? 0.3622 0.3863 0.6330 0.1156  0.0959  0.0924  83  PHE   A CE1 
616  C CE2 . PHE   A 77  ? 0.3523 0.3814 0.6015 0.1115  0.0998  0.0759  83  PHE   A CE2 
617  C CZ  . PHE   A 77  ? 0.3662 0.3825 0.6300 0.1163  0.1055  0.0791  83  PHE   A CZ  
618  N N   . VAL   A 78  ? 0.2510 0.2846 0.4296 0.0851  0.0620  0.0645  84  VAL   A N   
619  C CA  . VAL   A 78  ? 0.2519 0.2716 0.4113 0.0818  0.0661  0.0478  84  VAL   A CA  
620  C C   . VAL   A 78  ? 0.2678 0.2695 0.4357 0.0870  0.0803  0.0400  84  VAL   A C   
621  O O   . VAL   A 78  ? 0.2707 0.2620 0.4479 0.0899  0.0839  0.0418  84  VAL   A O   
622  C CB  . VAL   A 78  ? 0.2415 0.2534 0.3787 0.0742  0.0580  0.0396  84  VAL   A CB  
623  C CG1 . VAL   A 78  ? 0.2549 0.2532 0.3735 0.0701  0.0619  0.0240  84  VAL   A CG1 
624  C CG2 . VAL   A 78  ? 0.2346 0.2623 0.3632 0.0685  0.0463  0.0454  84  VAL   A CG2 
625  N N   . GLU   A 79  ? 0.2836 0.2809 0.4467 0.0870  0.0884  0.0306  85  GLU   A N   
626  C CA  . GLU   A 79  ? 0.3251 0.3050 0.4948 0.0905  0.1037  0.0213  85  GLU   A CA  
627  C C   . GLU   A 79  ? 0.3539 0.3137 0.5066 0.0848  0.1053  0.0085  85  GLU   A C   
628  O O   . GLU   A 79  ? 0.3465 0.3065 0.4781 0.0773  0.0953  0.0037  85  GLU   A O   
629  C CB  . GLU   A 79  ? 0.3719 0.3531 0.5367 0.0897  0.1114  0.0133  85  GLU   A CB  
630  C CG  . GLU   A 79  ? 0.4912 0.4588 0.6701 0.0948  0.1297  0.0066  85  GLU   A CG  
631  C CD  . GLU   A 79  ? 0.5677 0.5363 0.7795 0.1056  0.1377  0.0191  85  GLU   A CD  
632  O OE1 . GLU   A 79  ? 0.5538 0.5049 0.7724 0.1077  0.1457  0.0156  85  GLU   A OE1 
633  O OE2 . GLU   A 79  ? 0.5975 0.5848 0.8288 0.1116  0.1358  0.0332  85  GLU   A OE2 
634  N N   . ALA   A 80  ? 0.3798 0.3222 0.5421 0.0880  0.1188  0.0027  86  ALA   A N   
635  C CA  . ALA   A 80  ? 0.4225 0.3445 0.5699 0.0819  0.1227  -0.0101 86  ALA   A CA  
636  C C   . ALA   A 80  ? 0.4598 0.3784 0.5793 0.0716  0.1202  -0.0239 86  ALA   A C   
637  O O   . ALA   A 80  ? 0.4761 0.3994 0.5907 0.0703  0.1243  -0.0285 86  ALA   A O   
638  C CB  . ALA   A 80  ? 0.4328 0.3366 0.5953 0.0863  0.1408  -0.0158 86  ALA   A CB  
639  N N   . SER   A 81  ? 0.4602 0.3726 0.5616 0.0640  0.1125  -0.0291 87  SER   A N   
640  C CA  . SER   A 81  ? 0.4633 0.3729 0.5387 0.0533  0.1090  -0.0406 87  SER   A CA  
641  C C   . SER   A 81  ? 0.4634 0.3544 0.5277 0.0462  0.1138  -0.0512 87  SER   A C   
642  O O   . SER   A 81  ? 0.4707 0.3506 0.5482 0.0504  0.1208  -0.0500 87  SER   A O   
643  C CB  . SER   A 81  ? 0.4808 0.4047 0.5454 0.0500  0.0925  -0.0345 87  SER   A CB  
644  O OG  . SER   A 81  ? 0.4872 0.4090 0.5520 0.0494  0.0850  -0.0304 87  SER   A OG  
645  N N   . GLU   A 82  ? 0.4640 0.3526 0.5048 0.0350  0.1093  -0.0603 88  GLU   A N   
646  C CA  . GLU   A 82  ? 0.4614 0.3350 0.4903 0.0266  0.1119  -0.0693 88  GLU   A CA  
647  C C   . GLU   A 82  ? 0.4049 0.2807 0.4365 0.0278  0.1006  -0.0614 88  GLU   A C   
648  O O   . GLU   A 82  ? 0.4021 0.2652 0.4295 0.0232  0.1035  -0.0664 88  GLU   A O   
649  C CB  . GLU   A 82  ? 0.5263 0.3988 0.5298 0.0131  0.1103  -0.0800 88  GLU   A CB  
650  C CG  . GLU   A 82  ? 0.6380 0.5009 0.6372 0.0091  0.1260  -0.0918 88  GLU   A CG  
651  C CD  . GLU   A 82  ? 0.7799 0.6508 0.7594 -0.0007 0.1234  -0.0974 88  GLU   A CD  
652  O OE1 . GLU   A 82  ? 0.8140 0.6785 0.7892 -0.0046 0.1365  -0.1072 88  GLU   A OE1 
653  O OE2 . GLU   A 82  ? 0.8128 0.6964 0.7820 -0.0047 0.1087  -0.0919 88  GLU   A OE2 
654  N N   . TYR   A 83  ? 0.3665 0.2578 0.4059 0.0337  0.0892  -0.0494 89  TYR   A N   
655  C CA  . TYR   A 83  ? 0.3351 0.2297 0.3764 0.0341  0.0789  -0.0424 89  TYR   A CA  
656  C C   . TYR   A 83  ? 0.3072 0.2035 0.3697 0.0435  0.0799  -0.0315 89  TYR   A C   
657  O O   . TYR   A 83  ? 0.2976 0.1917 0.3623 0.0430  0.0751  -0.0277 89  TYR   A O   
658  C CB  . TYR   A 83  ? 0.3315 0.2418 0.3644 0.0318  0.0656  -0.0375 89  TYR   A CB  
659  C CG  . TYR   A 83  ? 0.3479 0.2581 0.3610 0.0220  0.0627  -0.0456 89  TYR   A CG  
660  C CD1 . TYR   A 83  ? 0.3901 0.3063 0.3968 0.0203  0.0638  -0.0481 89  TYR   A CD1 
661  C CD2 . TYR   A 83  ? 0.3696 0.2740 0.3707 0.0137  0.0590  -0.0503 89  TYR   A CD2 
662  C CE1 . TYR   A 83  ? 0.4140 0.3317 0.4030 0.0105  0.0602  -0.0538 89  TYR   A CE1 
663  C CE2 . TYR   A 83  ? 0.3984 0.3053 0.3825 0.0038  0.0551  -0.0556 89  TYR   A CE2 
664  C CZ  . TYR   A 83  ? 0.4290 0.3421 0.4069 0.0021  0.0560  -0.0574 89  TYR   A CZ  
665  O OH  . TYR   A 83  ? 0.4651 0.3824 0.4268 -0.0082 0.0511  -0.0608 89  TYR   A OH  
666  N N   . TYR   A 84  ? 0.3073 0.2096 0.3861 0.0517  0.0851  -0.0252 90  TYR   A N   
667  C CA  . TYR   A 84  ? 0.2956 0.2023 0.3965 0.0602  0.0853  -0.0123 90  TYR   A CA  
668  C C   . TYR   A 84  ? 0.3292 0.2320 0.4493 0.0681  0.0985  -0.0104 90  TYR   A C   
669  O O   . TYR   A 84  ? 0.3456 0.2514 0.4626 0.0681  0.1033  -0.0152 90  TYR   A O   
670  C CB  . TYR   A 84  ? 0.2711 0.1986 0.3758 0.0625  0.0733  -0.0002 90  TYR   A CB  
671  C CG  . TYR   A 84  ? 0.2416 0.1749 0.3319 0.0562  0.0609  0.0000  90  TYR   A CG  
672  C CD1 . TYR   A 84  ? 0.2367 0.1665 0.3289 0.0549  0.0569  0.0034  90  TYR   A CD1 
673  C CD2 . TYR   A 84  ? 0.2358 0.1783 0.3122 0.0517  0.0538  -0.0029 90  TYR   A CD2 
674  C CE1 . TYR   A 84  ? 0.2214 0.1569 0.3019 0.0494  0.0467  0.0033  90  TYR   A CE1 
675  C CE2 . TYR   A 84  ? 0.2325 0.1794 0.2981 0.0465  0.0441  -0.0030 90  TYR   A CE2 
676  C CZ  . TYR   A 84  ? 0.2151 0.1585 0.2828 0.0454  0.0409  -0.0003 90  TYR   A CZ  
677  O OH  . TYR   A 84  ? 0.2150 0.1632 0.2735 0.0405  0.0324  -0.0005 90  TYR   A OH  
678  N N   . PRO   A 85  ? 0.3443 0.2433 0.4862 0.0752  0.1035  -0.0014 91  PRO   A N   
679  C CA  . PRO   A 85  ? 0.3506 0.2498 0.5162 0.0843  0.1153  0.0041  91  PRO   A CA  
680  C C   . PRO   A 85  ? 0.3595 0.2824 0.5345 0.0888  0.1075  0.0171  91  PRO   A C   
681  O O   . PRO   A 85  ? 0.3563 0.2932 0.5199 0.0846  0.0936  0.0215  91  PRO   A O   
682  C CB  . PRO   A 85  ? 0.3636 0.2543 0.5503 0.0901  0.1198  0.0131  91  PRO   A CB  
683  C CG  . PRO   A 85  ? 0.3712 0.2697 0.5491 0.0857  0.1050  0.0196  91  PRO   A CG  
684  C CD  . PRO   A 85  ? 0.3453 0.2421 0.4934 0.0756  0.0980  0.0064  91  PRO   A CD  
685  N N   . ALA   A 86  ? 0.3631 0.2912 0.5602 0.0970  0.1163  0.0239  92  ALA   A N   
686  C CA  . ALA   A 86  ? 0.3498 0.3020 0.5577 0.1006  0.1087  0.0379  92  ALA   A CA  
687  C C   . ALA   A 86  ? 0.3323 0.2959 0.5517 0.1020  0.0982  0.0543  92  ALA   A C   
688  O O   . ALA   A 86  ? 0.3532 0.3072 0.5872 0.1058  0.1028  0.0593  92  ALA   A O   
689  C CB  . ALA   A 86  ? 0.3440 0.2995 0.5767 0.1095  0.1213  0.0430  92  ALA   A CB  
690  N N   . ARG   A 87  ? 0.3032 0.2848 0.5121 0.0970  0.0841  0.0607  93  ARG   A N   
691  C CA  . ARG   A 87  ? 0.2823 0.2746 0.4970 0.0956  0.0738  0.0743  93  ARG   A CA  
692  C C   . ARG   A 87  ? 0.2707 0.2861 0.4777 0.0905  0.0615  0.0819  93  ARG   A C   
693  O O   . ARG   A 87  ? 0.2809 0.3017 0.4773 0.0884  0.0609  0.0758  93  ARG   A O   
694  C CB  . ARG   A 87  ? 0.2968 0.2745 0.4934 0.0895  0.0700  0.0649  93  ARG   A CB  
695  C CG  . ARG   A 87  ? 0.3092 0.2907 0.4781 0.0805  0.0605  0.0549  93  ARG   A CG  
696  C CD  . ARG   A 87  ? 0.3122 0.2767 0.4630 0.0751  0.0605  0.0416  93  ARG   A CD  
697  N NE  . ARG   A 87  ? 0.3092 0.2801 0.4407 0.0675  0.0495  0.0382  93  ARG   A NE  
698  C CZ  . ARG   A 87  ? 0.3307 0.3067 0.4471 0.0633  0.0456  0.0317  93  ARG   A CZ  
699  N NH1 . ARG   A 87  ? 0.3291 0.3066 0.4455 0.0654  0.0507  0.0280  93  ARG   A NH1 
700  N NH2 . ARG   A 87  ? 0.2513 0.2311 0.3534 0.0571  0.0370  0.0291  93  ARG   A NH2 
701  N N   . TYR   A 88  ? 0.2581 0.2861 0.4685 0.0873  0.0518  0.0944  94  TYR   A N   
702  C CA  . TYR   A 88  ? 0.2641 0.3120 0.4643 0.0802  0.0407  0.0998  94  TYR   A CA  
703  C C   . TYR   A 88  ? 0.2383 0.2794 0.4132 0.0719  0.0341  0.0884  94  TYR   A C   
704  O O   . TYR   A 88  ? 0.2488 0.2817 0.4207 0.0699  0.0320  0.0877  94  TYR   A O   
705  C CB  . TYR   A 88  ? 0.2683 0.3358 0.4854 0.0795  0.0341  0.1199  94  TYR   A CB  
706  C CG  . TYR   A 88  ? 0.2739 0.3546 0.5160 0.0867  0.0388  0.1331  94  TYR   A CG  
707  C CD1 . TYR   A 88  ? 0.2781 0.3764 0.5180 0.0842  0.0356  0.1362  94  TYR   A CD1 
708  C CD2 . TYR   A 88  ? 0.2932 0.3675 0.5618 0.0964  0.0476  0.1415  94  TYR   A CD2 
709  C CE1 . TYR   A 88  ? 0.2937 0.4053 0.5577 0.0908  0.0401  0.1486  94  TYR   A CE1 
710  C CE2 . TYR   A 88  ? 0.2996 0.3861 0.5939 0.1038  0.0530  0.1539  94  TYR   A CE2 
711  C CZ  . TYR   A 88  ? 0.3095 0.4153 0.6013 0.1010  0.0490  0.1575  94  TYR   A CZ  
712  O OH  . TYR   A 88  ? 0.3389 0.4584 0.6572 0.1083  0.0541  0.1704  94  TYR   A OH  
713  N N   . GLN   A 89  ? 0.2046 0.2485 0.3620 0.0671  0.0312  0.0794  95  GLN   A N   
714  C CA  . GLN   A 89  ? 0.1899 0.2292 0.3257 0.0595  0.0251  0.0698  95  GLN   A CA  
715  C C   . GLN   A 89  ? 0.1815 0.2395 0.3128 0.0522  0.0162  0.0778  95  GLN   A C   
716  O O   . GLN   A 89  ? 0.1782 0.2509 0.3132 0.0512  0.0147  0.0840  95  GLN   A O   
717  C CB  . GLN   A 89  ? 0.1904 0.2203 0.3102 0.0581  0.0275  0.0554  95  GLN   A CB  
718  C CG  . GLN   A 89  ? 0.1857 0.2115 0.2869 0.0511  0.0216  0.0472  95  GLN   A CG  
719  C CD  . GLN   A 89  ? 0.1918 0.2055 0.2795 0.0500  0.0242  0.0340  95  GLN   A CD  
720  O OE1 . GLN   A 89  ? 0.2163 0.2180 0.3052 0.0533  0.0309  0.0281  95  GLN   A OE1 
721  N NE2 . GLN   A 89  ? 0.1914 0.2083 0.2660 0.0447  0.0193  0.0295  95  GLN   A NE2 
722  N N   . SER   A 90  ? 0.1607 0.2187 0.2840 0.0462  0.0108  0.0778  96  SER   A N   
723  C CA  . SER   A 90  ? 0.1546 0.2292 0.2721 0.0376  0.0036  0.0841  96  SER   A CA  
724  C C   . SER   A 90  ? 0.1510 0.2233 0.2489 0.0310  0.0014  0.0725  96  SER   A C   
725  O O   . SER   A 90  ? 0.1739 0.2315 0.2631 0.0329  0.0041  0.0606  96  SER   A O   
726  C CB  . SER   A 90  ? 0.1926 0.2699 0.3130 0.0338  -0.0002 0.0913  96  SER   A CB  
727  O OG  . SER   A 90  ? 0.2432 0.3047 0.3532 0.0329  0.0006  0.0803  96  SER   A OG  
728  N N   . HIS   A 91  ? 0.1515 0.2391 0.2437 0.0227  -0.0031 0.0767  97  HIS   A N   
729  C CA  . HIS   A 91  ? 0.1502 0.2364 0.2256 0.0155  -0.0044 0.0669  97  HIS   A CA  
730  C C   . HIS   A 91  ? 0.1424 0.2200 0.2131 0.0199  -0.0009 0.0578  97  HIS   A C   
731  O O   . HIS   A 91  ? 0.1566 0.2256 0.2157 0.0173  -0.0006 0.0478  97  HIS   A O   
732  C CB  . HIS   A 91  ? 0.1717 0.2482 0.2381 0.0116  -0.0053 0.0596  97  HIS   A CB  
733  C CG  . HIS   A 91  ? 0.1993 0.2848 0.2681 0.0057  -0.0088 0.0679  97  HIS   A CG  
734  N ND1 . HIS   A 91  ? 0.2413 0.3376 0.3008 -0.0056 -0.0114 0.0685  97  HIS   A ND1 
735  C CD2 . HIS   A 91  ? 0.2156 0.3009 0.2949 0.0089  -0.0096 0.0759  97  HIS   A CD2 
736  C CE1 . HIS   A 91  ? 0.2425 0.3456 0.3061 -0.0094 -0.0143 0.0768  97  HIS   A CE1 
737  N NE2 . HIS   A 91  ? 0.2340 0.3310 0.3102 -0.0007 -0.0136 0.0821  97  HIS   A NE2 
738  N N   . LEU   A 92  ? 0.1304 0.2122 0.2104 0.0255  0.0016  0.0623  98  LEU   A N   
739  C CA  . LEU   A 92  ? 0.1489 0.2239 0.2251 0.0293  0.0052  0.0547  98  LEU   A CA  
740  C C   . LEU   A 92  ? 0.1357 0.2247 0.2092 0.0246  0.0036  0.0579  98  LEU   A C   
741  O O   . LEU   A 92  ? 0.1378 0.2427 0.2193 0.0223  0.0014  0.0689  98  LEU   A O   
742  C CB  . LEU   A 92  ? 0.1670 0.2362 0.2560 0.0386  0.0110  0.0564  98  LEU   A CB  
743  C CG  . LEU   A 92  ? 0.1936 0.2541 0.2773 0.0418  0.0157  0.0472  98  LEU   A CG  
744  C CD1 . LEU   A 92  ? 0.1974 0.2429 0.2678 0.0401  0.0156  0.0358  98  LEU   A CD1 
745  C CD2 . LEU   A 92  ? 0.2093 0.2655 0.3067 0.0500  0.0232  0.0489  98  LEU   A CD2 
746  N N   . MET   A 93  ? 0.1412 0.2247 0.2033 0.0225  0.0044  0.0491  99  MET   A N   
747  C CA  . MET   A 93  ? 0.1356 0.2298 0.1935 0.0177  0.0034  0.0506  99  MET   A CA  
748  C C   . MET   A 93  ? 0.1441 0.2334 0.2028 0.0233  0.0074  0.0464  99  MET   A C   
749  O O   . MET   A 93  ? 0.1525 0.2275 0.2058 0.0263  0.0096  0.0379  99  MET   A O   
750  C CB  . MET   A 93  ? 0.1455 0.2359 0.1894 0.0097  0.0016  0.0435  99  MET   A CB  
751  C CG  . MET   A 93  ? 0.1553 0.2503 0.1967 0.0026  -0.0012 0.0461  99  MET   A CG  
752  S SD  . MET   A 93  ? 0.2084 0.2958 0.2352 -0.0064 -0.0008 0.0361  99  MET   A SD  
753  C CE  . MET   A 93  ? 0.2605 0.3288 0.2866 0.0017  0.0013  0.0272  99  MET   A CE  
754  N N   . LEU   A 94  ? 0.1324 0.2338 0.1971 0.0237  0.0084  0.0522  100 LEU   A N   
755  C CA  . LEU   A 94  ? 0.1430 0.2409 0.2085 0.0284  0.0128  0.0482  100 LEU   A CA  
756  C C   . LEU   A 94  ? 0.1276 0.2300 0.1827 0.0223  0.0114  0.0454  100 LEU   A C   
757  O O   . LEU   A 94  ? 0.1455 0.2602 0.1984 0.0152  0.0080  0.0503  100 LEU   A O   
758  C CB  . LEU   A 94  ? 0.1619 0.2695 0.2449 0.0350  0.0169  0.0568  100 LEU   A CB  
759  C CG  . LEU   A 94  ? 0.2098 0.3117 0.3063 0.0423  0.0204  0.0601  100 LEU   A CG  
760  C CD1 . LEU   A 94  ? 0.2210 0.3314 0.3364 0.0495  0.0263  0.0678  100 LEU   A CD1 
761  C CD2 . LEU   A 94  ? 0.2439 0.3253 0.3332 0.0457  0.0245  0.0485  100 LEU   A CD2 
762  N N   . ALA   A 95  ? 0.1355 0.2293 0.1848 0.0243  0.0144  0.0381  101 ALA   A N   
763  C CA  . ALA   A 95  ? 0.1245 0.2220 0.1654 0.0195  0.0138  0.0359  101 ALA   A CA  
764  C C   . ALA   A 95  ? 0.1258 0.2205 0.1684 0.0242  0.0188  0.0327  101 ALA   A C   
765  O O   . ALA   A 95  ? 0.1371 0.2236 0.1840 0.0300  0.0229  0.0298  101 ALA   A O   
766  C CB  . ALA   A 95  ? 0.1414 0.2279 0.1690 0.0144  0.0113  0.0286  101 ALA   A CB  
767  N N   . VAL   A 96  ? 0.1193 0.2203 0.1574 0.0207  0.0190  0.0327  102 VAL   A N   
768  C CA  . VAL   A 96  ? 0.1233 0.2218 0.1602 0.0233  0.0237  0.0289  102 VAL   A CA  
769  C C   . VAL   A 96  ? 0.1597 0.2446 0.1827 0.0203  0.0222  0.0207  102 VAL   A C   
770  O O   . VAL   A 96  ? 0.1703 0.2540 0.1850 0.0147  0.0183  0.0199  102 VAL   A O   
771  C CB  . VAL   A 96  ? 0.1284 0.2413 0.1671 0.0203  0.0241  0.0335  102 VAL   A CB  
772  C CG1 . VAL   A 96  ? 0.1433 0.2537 0.1786 0.0215  0.0290  0.0288  102 VAL   A CG1 
773  C CG2 . VAL   A 96  ? 0.1296 0.2585 0.1844 0.0230  0.0247  0.0438  102 VAL   A CG2 
774  N N   . GLY   A 97  ? 0.1692 0.2440 0.1903 0.0235  0.0257  0.0152  103 GLY   A N   
775  C CA  . GLY   A 97  ? 0.1795 0.2434 0.1884 0.0200  0.0236  0.0091  103 GLY   A CA  
776  C C   . GLY   A 97  ? 0.1856 0.2403 0.1927 0.0223  0.0279  0.0034  103 GLY   A C   
777  O O   . GLY   A 97  ? 0.2012 0.2553 0.2171 0.0273  0.0330  0.0033  103 GLY   A O   
778  N N   . HIS   A 98  ? 0.1948 0.2425 0.1906 0.0180  0.0261  -0.0010 104 HIS   A N   
779  C CA  . HIS   A 98  ? 0.2096 0.2489 0.2007 0.0176  0.0299  -0.0071 104 HIS   A CA  
780  C C   . HIS   A 98  ? 0.1915 0.2219 0.1830 0.0186  0.0276  -0.0087 104 HIS   A C   
781  O O   . HIS   A 98  ? 0.1994 0.2282 0.1889 0.0168  0.0212  -0.0066 104 HIS   A O   
782  C CB  . HIS   A 98  ? 0.2248 0.2626 0.2029 0.0108  0.0281  -0.0098 104 HIS   A CB  
783  C CG  . HIS   A 98  ? 0.2420 0.2730 0.2130 0.0080  0.0328  -0.0166 104 HIS   A CG  
784  N ND1 . HIS   A 98  ? 0.2632 0.2943 0.2366 0.0097  0.0422  -0.0211 104 HIS   A ND1 
785  C CD2 . HIS   A 98  ? 0.2584 0.2828 0.2202 0.0029  0.0298  -0.0195 104 HIS   A CD2 
786  C CE1 . HIS   A 98  ? 0.2735 0.2967 0.2375 0.0049  0.0451  -0.0278 104 HIS   A CE1 
787  N NE2 . HIS   A 98  ? 0.2625 0.2824 0.2188 0.0002  0.0372  -0.0265 104 HIS   A NE2 
788  N N   . SER   A 99  ? 0.1934 0.2176 0.1879 0.0213  0.0334  -0.0127 105 SER   A N   
789  C CA  . SER   A 99  ? 0.2048 0.2205 0.1999 0.0219  0.0318  -0.0145 105 SER   A CA  
790  C C   . SER   A 99  ? 0.2629 0.2704 0.2558 0.0215  0.0397  -0.0214 105 SER   A C   
791  O O   . SER   A 99  ? 0.2795 0.2865 0.2823 0.0267  0.0474  -0.0218 105 SER   A O   
792  C CB  . SER   A 99  ? 0.2081 0.2267 0.2154 0.0275  0.0305  -0.0089 105 SER   A CB  
793  O OG  . SER   A 99  ? 0.2286 0.2395 0.2376 0.0284  0.0294  -0.0101 105 SER   A OG  
794  N N   . GLU   A 100 ? 0.2592 0.2604 0.2397 0.0149  0.0384  -0.0266 106 GLU   A N   
795  C CA  . GLU   A 100 ? 0.3005 0.2926 0.2765 0.0123  0.0465  -0.0346 106 GLU   A CA  
796  C C   . GLU   A 100 ? 0.3332 0.3171 0.3064 0.0102  0.0431  -0.0362 106 GLU   A C   
797  O O   . GLU   A 100 ? 0.3256 0.3117 0.3021 0.0116  0.0349  -0.0308 106 GLU   A O   
798  C CB  . GLU   A 100 ? 0.3465 0.3397 0.3090 0.0044  0.0502  -0.0403 106 GLU   A CB  
799  C CG  . GLU   A 100 ? 0.3550 0.3524 0.3052 -0.0036 0.0407  -0.0378 106 GLU   A CG  
800  C CD  . GLU   A 100 ? 0.3351 0.3349 0.2710 -0.0129 0.0428  -0.0420 106 GLU   A CD  
801  O OE1 . GLU   A 100 ? 0.3774 0.3716 0.3016 -0.0212 0.0455  -0.0484 106 GLU   A OE1 
802  O OE2 . GLU   A 100 ? 0.3000 0.3077 0.2355 -0.0131 0.0417  -0.0387 106 GLU   A OE2 
803  N N   . PRO   A 101 ? 0.3912 0.3649 0.3613 0.0078  0.0510  -0.0439 107 PRO   A N   
804  C CA  . PRO   A 101 ? 0.3993 0.3652 0.3659 0.0047  0.0484  -0.0460 107 PRO   A CA  
805  C C   . PRO   A 101 ? 0.3706 0.3396 0.3233 -0.0048 0.0395  -0.0455 107 PRO   A C   
806  O O   . PRO   A 101 ? 0.3971 0.3658 0.3356 -0.0145 0.0409  -0.0506 107 PRO   A O   
807  C CB  . PRO   A 101 ? 0.4303 0.3841 0.3958 0.0032  0.0607  -0.0552 107 PRO   A CB  
808  C CG  . PRO   A 101 ? 0.4405 0.3966 0.4138 0.0083  0.0700  -0.0563 107 PRO   A CG  
809  C CD  . PRO   A 101 ? 0.4094 0.3778 0.3778 0.0065  0.0633  -0.0517 107 PRO   A CD  
810  N N   . GLY   A 102 ? 0.2916 0.2638 0.2496 -0.0023 0.0308  -0.0390 108 GLY   A N   
811  C CA  . GLY   A 102 ? 0.2726 0.2496 0.2253 -0.0076 0.0208  -0.0345 108 GLY   A CA  
812  C C   . GLY   A 102 ? 0.2288 0.2135 0.1906 -0.0021 0.0142  -0.0264 108 GLY   A C   
813  O O   . GLY   A 102 ? 0.2188 0.2064 0.1814 -0.0040 0.0069  -0.0218 108 GLY   A O   
814  N N   . ASP   A 103 ? 0.2058 0.1942 0.1748 0.0041  0.0171  -0.0244 109 ASP   A N   
815  C CA  . ASP   A 103 ? 0.1946 0.1894 0.1707 0.0079  0.0120  -0.0178 109 ASP   A CA  
816  C C   . ASP   A 103 ? 0.1842 0.1778 0.1697 0.0127  0.0104  -0.0151 109 ASP   A C   
817  O O   . ASP   A 103 ? 0.1863 0.1841 0.1763 0.0139  0.0062  -0.0107 109 ASP   A O   
818  C CB  . ASP   A 103 ? 0.1735 0.1742 0.1523 0.0108  0.0152  -0.0164 109 ASP   A CB  
819  C CG  . ASP   A 103 ? 0.1997 0.2035 0.1688 0.0051  0.0148  -0.0174 109 ASP   A CG  
820  O OD1 . ASP   A 103 ? 0.1977 0.2024 0.1614 0.0000  0.0091  -0.0153 109 ASP   A OD1 
821  O OD2 . ASP   A 103 ? 0.1898 0.1960 0.1578 0.0058  0.0203  -0.0196 109 ASP   A OD2 
822  N N   . CYS   A 104 ? 0.1780 0.1653 0.1663 0.0146  0.0140  -0.0179 110 CYS   A N   
823  C CA  . CYS   A 104 ? 0.1828 0.1699 0.1797 0.0183  0.0119  -0.0147 110 CYS   A CA  
824  C C   . CYS   A 104 ? 0.1803 0.1683 0.1761 0.0153  0.0053  -0.0125 110 CYS   A C   
825  O O   . CYS   A 104 ? 0.1811 0.1675 0.1707 0.0104  0.0027  -0.0139 110 CYS   A O   
826  C CB  . CYS   A 104 ? 0.1941 0.1737 0.1941 0.0203  0.0165  -0.0174 110 CYS   A CB  
827  S SG  . CYS   A 104 ? 0.2398 0.2191 0.2487 0.0265  0.0250  -0.0170 110 CYS   A SG  
828  N N   . GLY   A 105 ? 0.1675 0.1590 0.1699 0.0176  0.0031  -0.0088 111 GLY   A N   
829  C CA  . GLY   A 105 ? 0.1562 0.1487 0.1606 0.0156  -0.0016 -0.0068 111 GLY   A CA  
830  C C   . GLY   A 105 ? 0.1538 0.1509 0.1595 0.0149  -0.0035 -0.0039 111 GLY   A C   
831  O O   . GLY   A 105 ? 0.1621 0.1599 0.1726 0.0143  -0.0056 -0.0019 111 GLY   A O   
832  N N   . GLY   A 106 ? 0.1544 0.1543 0.1565 0.0147  -0.0021 -0.0039 112 GLY   A N   
833  C CA  . GLY   A 106 ? 0.1405 0.1439 0.1438 0.0137  -0.0033 -0.0012 112 GLY   A CA  
834  C C   . GLY   A 106 ? 0.1312 0.1368 0.1400 0.0149  -0.0019 -0.0002 112 GLY   A C   
835  O O   . GLY   A 106 ? 0.1418 0.1496 0.1518 0.0167  0.0002  -0.0004 112 GLY   A O   
836  N N   . ILE   A 107 ? 0.1334 0.1388 0.1456 0.0134  -0.0025 0.0012  113 ILE   A N   
837  C CA  . ILE   A 107 ? 0.1261 0.1331 0.1416 0.0125  -0.0001 0.0008  113 ILE   A CA  
838  C C   . ILE   A 107 ? 0.1228 0.1344 0.1353 0.0109  0.0018  0.0012  113 ILE   A C   
839  O O   . ILE   A 107 ? 0.1367 0.1487 0.1469 0.0099  0.0016  0.0020  113 ILE   A O   
840  C CB  . ILE   A 107 ? 0.1303 0.1338 0.1519 0.0113  0.0003  0.0010  113 ILE   A CB  
841  C CG1 . ILE   A 107 ? 0.1510 0.1522 0.1767 0.0125  -0.0012 0.0008  113 ILE   A CG1 
842  C CG2 . ILE   A 107 ? 0.1486 0.1525 0.1718 0.0082  0.0044  -0.0006 113 ILE   A CG2 
843  C CD1 . ILE   A 107 ? 0.1876 0.1859 0.2221 0.0121  -0.0005 0.0018  113 ILE   A CD1 
844  N N   . LEU   A 108 ? 0.1194 0.1356 0.1321 0.0097  0.0034  0.0013  114 LEU   A N   
845  C CA  . LEU   A 108 ? 0.1198 0.1421 0.1301 0.0061  0.0052  0.0021  114 LEU   A CA  
846  C C   . LEU   A 108 ? 0.1223 0.1424 0.1335 0.0012  0.0077  -0.0002 114 LEU   A C   
847  O O   . LEU   A 108 ? 0.1353 0.1544 0.1489 0.0008  0.0081  -0.0012 114 LEU   A O   
848  C CB  . LEU   A 108 ? 0.1225 0.1532 0.1333 0.0067  0.0050  0.0051  114 LEU   A CB  
849  C CG  . LEU   A 108 ? 0.1335 0.1734 0.1420 0.0011  0.0061  0.0071  114 LEU   A CG  
850  C CD1 . LEU   A 108 ? 0.1494 0.1916 0.1547 0.0005  0.0066  0.0076  114 LEU   A CD1 
851  C CD2 . LEU   A 108 ? 0.1557 0.2061 0.1676 0.0015  0.0051  0.0125  114 LEU   A CD2 
852  N N   . ARG   A 109 ? 0.1311 0.1497 0.1406 -0.0027 0.0101  -0.0015 115 ARG   A N   
853  C CA  . ARG   A 109 ? 0.1400 0.1547 0.1504 -0.0080 0.0146  -0.0051 115 ARG   A CA  
854  C C   . ARG   A 109 ? 0.1474 0.1658 0.1520 -0.0152 0.0176  -0.0063 115 ARG   A C   
855  O O   . ARG   A 109 ? 0.1494 0.1719 0.1508 -0.0152 0.0161  -0.0040 115 ARG   A O   
856  C CB  . ARG   A 109 ? 0.1607 0.1656 0.1780 -0.0057 0.0163  -0.0061 115 ARG   A CB  
857  C CG  . ARG   A 109 ? 0.1627 0.1650 0.1798 -0.0051 0.0158  -0.0041 115 ARG   A CG  
858  C CD  . ARG   A 109 ? 0.1813 0.1753 0.2083 -0.0026 0.0171  -0.0031 115 ARG   A CD  
859  N NE  . ARG   A 109 ? 0.2007 0.1956 0.2312 0.0026  0.0118  0.0004  115 ARG   A NE  
860  C CZ  . ARG   A 109 ? 0.1988 0.1908 0.2375 0.0049  0.0118  0.0009  115 ARG   A CZ  
861  N NH1 . ARG   A 109 ? 0.1931 0.1810 0.2376 0.0031  0.0174  -0.0024 115 ARG   A NH1 
862  N NH2 . ARG   A 109 ? 0.2022 0.1957 0.2427 0.0081  0.0065  0.0045  115 ARG   A NH2 
863  N N   . CYS   A 110 ? 0.1793 0.1966 0.1820 -0.0222 0.0223  -0.0103 116 CYS   A N   
864  C CA  . CYS   A 110 ? 0.2200 0.2397 0.2159 -0.0314 0.0262  -0.0127 116 CYS   A CA  
865  C C   . CYS   A 110 ? 0.2631 0.2709 0.2618 -0.0356 0.0341  -0.0191 116 CYS   A C   
866  O O   . CYS   A 110 ? 0.2603 0.2596 0.2679 -0.0300 0.0355  -0.0200 116 CYS   A O   
867  C CB  . CYS   A 110 ? 0.2085 0.2404 0.1979 -0.0385 0.0251  -0.0114 116 CYS   A CB  
868  S SG  . CYS   A 110 ? 0.2152 0.2452 0.2047 -0.0434 0.0287  -0.0156 116 CYS   A SG  
869  N N   . GLN   A 111 ? 0.3053 0.3126 0.2969 -0.0461 0.0399  -0.0237 117 GLN   A N   
870  C CA  . GLN   A 111 ? 0.3399 0.3343 0.3349 -0.0505 0.0495  -0.0307 117 GLN   A CA  
871  C C   . GLN   A 111 ? 0.3363 0.3272 0.3355 -0.0512 0.0537  -0.0350 117 GLN   A C   
872  O O   . GLN   A 111 ? 0.3651 0.3440 0.3726 -0.0507 0.0615  -0.0397 117 GLN   A O   
873  C CB  . GLN   A 111 ? 0.3951 0.3894 0.3799 -0.0636 0.0559  -0.0360 117 GLN   A CB  
874  C CG  . GLN   A 111 ? 0.4627 0.4683 0.4357 -0.0751 0.0562  -0.0382 117 GLN   A CG  
875  C CD  . GLN   A 111 ? 0.5433 0.5517 0.5039 -0.0898 0.0611  -0.0425 117 GLN   A CD  
876  O OE1 . GLN   A 111 ? 0.5686 0.5890 0.5225 -0.0930 0.0555  -0.0374 117 GLN   A OE1 
877  N NE2 . GLN   A 111 ? 0.5435 0.5416 0.5009 -0.0997 0.0722  -0.0522 117 GLN   A NE2 
878  N N   . HIS   A 112 ? 0.2886 0.2897 0.2837 -0.0518 0.0488  -0.0326 118 HIS   A N   
879  C CA  . HIS   A 112 ? 0.2666 0.2659 0.2643 -0.0537 0.0525  -0.0364 118 HIS   A CA  
880  C C   . HIS   A 112 ? 0.2593 0.2553 0.2684 -0.0421 0.0484  -0.0329 118 HIS   A C   
881  O O   . HIS   A 112 ? 0.2748 0.2680 0.2883 -0.0425 0.0521  -0.0360 118 HIS   A O   
882  C CB  . HIS   A 112 ? 0.2603 0.2731 0.2469 -0.0627 0.0497  -0.0354 118 HIS   A CB  
883  C CG  . HIS   A 112 ? 0.3184 0.3369 0.2925 -0.0761 0.0529  -0.0381 118 HIS   A CG  
884  N ND1 . HIS   A 112 ? 0.3436 0.3756 0.3114 -0.0783 0.0458  -0.0312 118 HIS   A ND1 
885  C CD2 . HIS   A 112 ? 0.3511 0.3641 0.3182 -0.0887 0.0629  -0.0470 118 HIS   A CD2 
886  C CE1 . HIS   A 112 ? 0.3680 0.4029 0.3249 -0.0919 0.0505  -0.0354 118 HIS   A CE1 
887  N NE2 . HIS   A 112 ? 0.3684 0.3916 0.3235 -0.0993 0.0612  -0.0455 118 HIS   A NE2 
888  N N   . GLY   A 113 ? 0.2325 0.2299 0.2457 -0.0327 0.0410  -0.0265 119 GLY   A N   
889  C CA  . GLY   A 113 ? 0.2103 0.2058 0.2324 -0.0234 0.0366  -0.0230 119 GLY   A CA  
890  C C   . GLY   A 113 ? 0.1750 0.1782 0.1942 -0.0178 0.0277  -0.0168 119 GLY   A C   
891  O O   . GLY   A 113 ? 0.1753 0.1839 0.1886 -0.0187 0.0249  -0.0143 119 GLY   A O   
892  N N   . VAL   A 114 ? 0.1630 0.1662 0.1869 -0.0122 0.0239  -0.0146 120 VAL   A N   
893  C CA  . VAL   A 114 ? 0.1608 0.1689 0.1830 -0.0068 0.0170  -0.0098 120 VAL   A CA  
894  C C   . VAL   A 114 ? 0.1398 0.1570 0.1561 -0.0100 0.0151  -0.0077 120 VAL   A C   
895  O O   . VAL   A 114 ? 0.1452 0.1648 0.1606 -0.0143 0.0167  -0.0090 120 VAL   A O   
896  C CB  . VAL   A 114 ? 0.1544 0.1586 0.1830 -0.0010 0.0141  -0.0084 120 VAL   A CB  
897  C CG1 . VAL   A 114 ? 0.1636 0.1712 0.1896 0.0033  0.0087  -0.0050 120 VAL   A CG1 
898  C CG2 . VAL   A 114 ? 0.1642 0.1623 0.2002 0.0021  0.0146  -0.0078 120 VAL   A CG2 
899  N N   . VAL   A 115 ? 0.1425 0.1654 0.1558 -0.0081 0.0119  -0.0039 121 VAL   A N   
900  C CA  . VAL   A 115 ? 0.1384 0.1717 0.1491 -0.0105 0.0098  0.0003  121 VAL   A CA  
901  C C   . VAL   A 115 ? 0.1368 0.1705 0.1520 -0.0038 0.0063  0.0041  121 VAL   A C   
902  O O   . VAL   A 115 ? 0.1503 0.1898 0.1667 -0.0050 0.0050  0.0077  121 VAL   A O   
903  C CB  . VAL   A 115 ? 0.1545 0.1948 0.1617 -0.0123 0.0093  0.0030  121 VAL   A CB  
904  C CG1 . VAL   A 115 ? 0.1645 0.2175 0.1726 -0.0132 0.0065  0.0099  121 VAL   A CG1 
905  C CG2 . VAL   A 115 ? 0.1676 0.2073 0.1695 -0.0205 0.0133  -0.0010 121 VAL   A CG2 
906  N N   . GLY   A 116 ? 0.1396 0.1672 0.1568 0.0026  0.0051  0.0035  122 GLY   A N   
907  C CA  . GLY   A 116 ? 0.1422 0.1681 0.1626 0.0082  0.0032  0.0057  122 GLY   A CA  
908  C C   . GLY   A 116 ? 0.1367 0.1561 0.1567 0.0127  0.0025  0.0038  122 GLY   A C   
909  O O   . GLY   A 116 ? 0.1386 0.1546 0.1570 0.0116  0.0027  0.0016  122 GLY   A O   
910  N N   . ILE   A 117 ? 0.1345 0.1517 0.1561 0.0168  0.0022  0.0046  123 ILE   A N   
911  C CA  . ILE   A 117 ? 0.1290 0.1403 0.1480 0.0191  0.0020  0.0021  123 ILE   A CA  
912  C C   . ILE   A 117 ? 0.1281 0.1410 0.1476 0.0222  0.0042  0.0031  123 ILE   A C   
913  O O   . ILE   A 117 ? 0.1397 0.1560 0.1644 0.0243  0.0056  0.0063  123 ILE   A O   
914  C CB  . ILE   A 117 ? 0.1465 0.1507 0.1658 0.0195  0.0007  -0.0001 123 ILE   A CB  
915  C CG1 . ILE   A 117 ? 0.1650 0.1680 0.1881 0.0212  0.0014  0.0011  123 ILE   A CG1 
916  C CG2 . ILE   A 117 ? 0.1607 0.1634 0.1811 0.0171  -0.0010 -0.0008 123 ILE   A CG2 
917  C CD1 . ILE   A 117 ? 0.1894 0.1850 0.2118 0.0209  0.0003  -0.0014 123 ILE   A CD1 
918  N N   . VAL   A 118 ? 0.1366 0.1471 0.1517 0.0223  0.0050  0.0007  124 VAL   A N   
919  C CA  . VAL   A 118 ? 0.1386 0.1495 0.1543 0.0251  0.0087  0.0003  124 VAL   A CA  
920  C C   . VAL   A 118 ? 0.1429 0.1476 0.1624 0.0278  0.0112  -0.0009 124 VAL   A C   
921  O O   . VAL   A 118 ? 0.1557 0.1536 0.1720 0.0262  0.0098  -0.0039 124 VAL   A O   
922  C CB  . VAL   A 118 ? 0.1491 0.1576 0.1575 0.0231  0.0093  -0.0032 124 VAL   A CB  
923  C CG1 . VAL   A 118 ? 0.1607 0.1682 0.1697 0.0255  0.0149  -0.0052 124 VAL   A CG1 
924  C CG2 . VAL   A 118 ? 0.1536 0.1675 0.1592 0.0206  0.0072  -0.0014 124 VAL   A CG2 
925  N N   . SER   A 119 ? 0.1524 0.1597 0.1795 0.0318  0.0152  0.0020  125 SER   A N   
926  C CA  . SER   A 119 ? 0.1683 0.1689 0.2013 0.0349  0.0189  0.0017  125 SER   A CA  
927  C C   . SER   A 119 ? 0.1904 0.1891 0.2287 0.0388  0.0262  0.0007  125 SER   A C   
928  O O   . SER   A 119 ? 0.2264 0.2153 0.2661 0.0402  0.0311  -0.0031 125 SER   A O   
929  C CB  . SER   A 119 ? 0.1885 0.1939 0.2298 0.0362  0.0166  0.0082  125 SER   A CB  
930  O OG  . SER   A 119 ? 0.1980 0.1975 0.2473 0.0396  0.0202  0.0097  125 SER   A OG  
931  N N   . THR   A 120 ? 0.1833 0.1908 0.2247 0.0403  0.0278  0.0036  126 THR   A N   
932  C CA  . THR   A 120 ? 0.1997 0.2062 0.2483 0.0445  0.0361  0.0028  126 THR   A CA  
933  C C   . THR   A 120 ? 0.2007 0.2122 0.2426 0.0424  0.0373  0.0001  126 THR   A C   
934  O O   . THR   A 120 ? 0.1889 0.2062 0.2233 0.0385  0.0313  0.0011  126 THR   A O   
935  C CB  . THR   A 120 ? 0.2092 0.2242 0.2755 0.0503  0.0382  0.0126  126 THR   A CB  
936  O OG1 . THR   A 120 ? 0.2168 0.2468 0.2853 0.0491  0.0339  0.0194  126 THR   A OG1 
937  C CG2 . THR   A 120 ? 0.2155 0.2276 0.2887 0.0517  0.0360  0.0171  126 THR   A CG2 
938  N N   . GLY   A 121 ? 0.2171 0.2263 0.2625 0.0448  0.0457  -0.0031 127 GLY   A N   
939  C CA  . GLY   A 121 ? 0.2418 0.2564 0.2810 0.0424  0.0472  -0.0054 127 GLY   A CA  
940  C C   . GLY   A 121 ? 0.2762 0.2921 0.3251 0.0466  0.0576  -0.0063 127 GLY   A C   
941  O O   . GLY   A 121 ? 0.3042 0.3218 0.3695 0.0530  0.0624  -0.0012 127 GLY   A O   
942  N N   . GLY   A 122 ? 0.2711 0.2874 0.3112 0.0431  0.0611  -0.0119 128 GLY   A N   
943  C CA  . GLY   A 122 ? 0.2795 0.2968 0.3276 0.0463  0.0722  -0.0144 128 GLY   A CA  
944  C C   . GLY   A 122 ? 0.2882 0.3213 0.3489 0.0503  0.0721  -0.0054 128 GLY   A C   
945  O O   . GLY   A 122 ? 0.2754 0.3187 0.3429 0.0520  0.0647  0.0040  128 GLY   A O   
946  N N   . ASN   A 123 ? 0.2966 0.3323 0.3608 0.0513  0.0810  -0.0085 129 ASN   A N   
947  C CA  . ASN   A 123 ? 0.3039 0.3556 0.3826 0.0555  0.0827  0.0001  129 ASN   A CA  
948  C C   . ASN   A 123 ? 0.2701 0.3345 0.3401 0.0505  0.0717  0.0056  129 ASN   A C   
949  O O   . ASN   A 123 ? 0.2516 0.3312 0.3332 0.0529  0.0704  0.0148  129 ASN   A O   
950  C CB  . ASN   A 123 ? 0.3272 0.3845 0.4302 0.0642  0.0852  0.0106  129 ASN   A CB  
951  C CG  . ASN   A 123 ? 0.4038 0.4499 0.5212 0.0706  0.0989  0.0067  129 ASN   A CG  
952  O OD1 . ASN   A 123 ? 0.4380 0.4746 0.5497 0.0689  0.1092  -0.0040 129 ASN   A OD1 
953  N ND2 . ASN   A 123 ? 0.4022 0.4489 0.5386 0.0774  0.0999  0.0154  129 ASN   A ND2 
954  N N   . GLY   A 124 ? 0.2455 0.3045 0.2961 0.0433  0.0646  0.0005  130 GLY   A N   
955  C CA  . GLY   A 124 ? 0.2181 0.2864 0.2609 0.0385  0.0555  0.0049  130 GLY   A CA  
956  C C   . GLY   A 124 ? 0.1842 0.2572 0.2318 0.0391  0.0474  0.0125  130 GLY   A C   
957  O O   . GLY   A 124 ? 0.1822 0.2638 0.2259 0.0350  0.0411  0.0168  130 GLY   A O   
958  N N   . LEU   A 125 ? 0.1628 0.2288 0.2165 0.0427  0.0476  0.0131  131 LEU   A N   
959  C CA  . LEU   A 125 ? 0.1584 0.2277 0.2150 0.0422  0.0403  0.0193  131 LEU   A CA  
960  C C   . LEU   A 125 ? 0.1816 0.2374 0.2275 0.0397  0.0366  0.0133  131 LEU   A C   
961  O O   . LEU   A 125 ? 0.2062 0.2502 0.2468 0.0399  0.0407  0.0059  131 LEU   A O   
962  C CB  . LEU   A 125 ? 0.1630 0.2378 0.2388 0.0487  0.0435  0.0274  131 LEU   A CB  
963  C CG  . LEU   A 125 ? 0.1662 0.2577 0.2567 0.0516  0.0464  0.0364  131 LEU   A CG  
964  C CD1 . LEU   A 125 ? 0.1861 0.2804 0.2985 0.0595  0.0521  0.0438  131 LEU   A CD1 
965  C CD2 . LEU   A 125 ? 0.1660 0.2729 0.2534 0.0456  0.0379  0.0439  131 LEU   A CD2 
966  N N   . VAL   A 126 ? 0.1549 0.2130 0.1972 0.0364  0.0295  0.0162  132 VAL   A N   
967  C CA  . VAL   A 126 ? 0.1547 0.2018 0.1897 0.0344  0.0259  0.0121  132 VAL   A CA  
968  C C   . VAL   A 126 ? 0.1494 0.2014 0.1917 0.0350  0.0223  0.0184  132 VAL   A C   
969  O O   . VAL   A 126 ? 0.1556 0.2191 0.2004 0.0324  0.0193  0.0244  132 VAL   A O   
970  C CB  . VAL   A 126 ? 0.1614 0.2053 0.1832 0.0286  0.0212  0.0082  132 VAL   A CB  
971  C CG1 . VAL   A 126 ? 0.1729 0.2267 0.1935 0.0248  0.0177  0.0125  132 VAL   A CG1 
972  C CG2 . VAL   A 126 ? 0.1679 0.2023 0.1850 0.0270  0.0175  0.0051  132 VAL   A CG2 
973  N N   . GLY   A 127 ? 0.1450 0.1887 0.1898 0.0371  0.0226  0.0172  133 GLY   A N   
974  C CA  . GLY   A 127 ? 0.1373 0.1852 0.1880 0.0368  0.0192  0.0231  133 GLY   A CA  
975  C C   . GLY   A 127 ? 0.1439 0.1836 0.1860 0.0332  0.0152  0.0186  133 GLY   A C   
976  O O   . GLY   A 127 ? 0.1669 0.1956 0.2027 0.0332  0.0160  0.0120  133 GLY   A O   
977  N N   . PHE   A 128 ? 0.1309 0.1768 0.1724 0.0292  0.0111  0.0222  134 PHE   A N   
978  C CA  . PHE   A 128 ? 0.1398 0.1795 0.1748 0.0255  0.0080  0.0184  134 PHE   A CA  
979  C C   . PHE   A 128 ? 0.1408 0.1825 0.1812 0.0251  0.0065  0.0227  134 PHE   A C   
980  O O   . PHE   A 128 ? 0.1392 0.1921 0.1851 0.0236  0.0054  0.0300  134 PHE   A O   
981  C CB  . PHE   A 128 ? 0.1489 0.1932 0.1771 0.0194  0.0058  0.0174  134 PHE   A CB  
982  C CG  . PHE   A 128 ? 0.1478 0.1921 0.1712 0.0190  0.0069  0.0149  134 PHE   A CG  
983  C CD1 . PHE   A 128 ? 0.1472 0.1825 0.1650 0.0191  0.0067  0.0096  134 PHE   A CD1 
984  C CD2 . PHE   A 128 ? 0.1557 0.2106 0.1808 0.0177  0.0075  0.0190  134 PHE   A CD2 
985  C CE1 . PHE   A 128 ? 0.1538 0.1898 0.1671 0.0180  0.0073  0.0082  134 PHE   A CE1 
986  C CE2 . PHE   A 128 ? 0.1596 0.2148 0.1801 0.0169  0.0085  0.0169  134 PHE   A CE2 
987  C CZ  . PHE   A 128 ? 0.1520 0.1973 0.1663 0.0169  0.0084  0.0114  134 PHE   A CZ  
988  N N   . ALA   A 129 ? 0.1415 0.1736 0.1800 0.0256  0.0060  0.0187  135 ALA   A N   
989  C CA  . ALA   A 129 ? 0.1436 0.1768 0.1856 0.0241  0.0043  0.0220  135 ALA   A CA  
990  C C   . ALA   A 129 ? 0.1356 0.1733 0.1718 0.0172  0.0020  0.0209  135 ALA   A C   
991  O O   . ALA   A 129 ? 0.1431 0.1742 0.1736 0.0155  0.0019  0.0150  135 ALA   A O   
992  C CB  . ALA   A 129 ? 0.1427 0.1639 0.1845 0.0266  0.0050  0.0178  135 ALA   A CB  
993  N N   . ASP   A 130 ? 0.1386 0.1876 0.1763 0.0126  0.0005  0.0269  136 ASP   A N   
994  C CA  . ASP   A 130 ? 0.1471 0.2001 0.1783 0.0044  -0.0002 0.0249  136 ASP   A CA  
995  C C   . ASP   A 130 ? 0.1471 0.1936 0.1771 0.0027  -0.0003 0.0215  136 ASP   A C   
996  O O   . ASP   A 130 ? 0.1668 0.2110 0.2018 0.0058  -0.0012 0.0244  136 ASP   A O   
997  C CB  . ASP   A 130 ? 0.1610 0.2295 0.1936 -0.0018 -0.0021 0.0332  136 ASP   A CB  
998  C CG  . ASP   A 130 ? 0.2645 0.3379 0.2883 -0.0125 -0.0017 0.0303  136 ASP   A CG  
999  O OD1 . ASP   A 130 ? 0.2087 0.2774 0.2262 -0.0151 0.0007  0.0235  136 ASP   A OD1 
1000 O OD2 . ASP   A 130 ? 0.3432 0.4246 0.3665 -0.0188 -0.0032 0.0347  136 ASP   A OD2 
1001 N N   . VAL   A 131 ? 0.1289 0.1719 0.1535 -0.0020 0.0013  0.0154  137 VAL   A N   
1002 C CA  . VAL   A 131 ? 0.1279 0.1665 0.1521 -0.0046 0.0020  0.0122  137 VAL   A CA  
1003 C C   . VAL   A 131 ? 0.1421 0.1866 0.1608 -0.0146 0.0042  0.0102  137 VAL   A C   
1004 O O   . VAL   A 131 ? 0.1475 0.1890 0.1659 -0.0177 0.0059  0.0068  137 VAL   A O   
1005 C CB  . VAL   A 131 ? 0.1361 0.1631 0.1614 -0.0005 0.0031  0.0061  137 VAL   A CB  
1006 C CG1 . VAL   A 131 ? 0.1502 0.1713 0.1786 0.0069  0.0012  0.0070  137 VAL   A CG1 
1007 C CG2 . VAL   A 131 ? 0.1544 0.1786 0.1771 -0.0024 0.0057  0.0015  137 VAL   A CG2 
1008 N N   . ARG   A 132 ? 0.1495 0.2023 0.1636 -0.0205 0.0048  0.0117  138 ARG   A N   
1009 C CA  . ARG   A 132 ? 0.1507 0.2080 0.1576 -0.0318 0.0082  0.0081  138 ARG   A CA  
1010 C C   . ARG   A 132 ? 0.1700 0.2355 0.1747 -0.0392 0.0071  0.0116  138 ARG   A C   
1011 O O   . ARG   A 132 ? 0.1839 0.2503 0.1820 -0.0491 0.0113  0.0063  138 ARG   A O   
1012 C CB  . ARG   A 132 ? 0.1593 0.2241 0.1606 -0.0375 0.0087  0.0092  138 ARG   A CB  
1013 C CG  . ARG   A 132 ? 0.1577 0.2133 0.1597 -0.0322 0.0108  0.0045  138 ARG   A CG  
1014 C CD  . ARG   A 132 ? 0.1639 0.2278 0.1604 -0.0384 0.0111  0.0061  138 ARG   A CD  
1015 N NE  . ARG   A 132 ? 0.1576 0.2329 0.1580 -0.0349 0.0060  0.0156  138 ARG   A NE  
1016 C CZ  . ARG   A 132 ? 0.1877 0.2725 0.1862 -0.0380 0.0048  0.0195  138 ARG   A CZ  
1017 N NH1 . ARG   A 132 ? 0.1946 0.2793 0.1849 -0.0464 0.0081  0.0145  138 ARG   A NH1 
1018 N NH2 . ARG   A 132 ? 0.2088 0.3038 0.2140 -0.0333 0.0009  0.0287  138 ARG   A NH2 
1019 N N   . ASP   A 133 ? 0.1584 0.2299 0.1687 -0.0353 0.0022  0.0205  139 ASP   A N   
1020 C CA  . ASP   A 133 ? 0.1713 0.2516 0.1800 -0.0429 0.0005  0.0253  139 ASP   A CA  
1021 C C   . ASP   A 133 ? 0.1699 0.2410 0.1811 -0.0403 0.0019  0.0211  139 ASP   A C   
1022 O O   . ASP   A 133 ? 0.1885 0.2657 0.1975 -0.0474 0.0012  0.0238  139 ASP   A O   
1023 C CB  . ASP   A 133 ? 0.1903 0.2821 0.2063 -0.0403 -0.0052 0.0386  139 ASP   A CB  
1024 C CG  . ASP   A 133 ? 0.2361 0.3181 0.2627 -0.0268 -0.0066 0.0408  139 ASP   A CG  
1025 O OD1 . ASP   A 133 ? 0.2248 0.2959 0.2525 -0.0191 -0.0046 0.0346  139 ASP   A OD1 
1026 O OD2 . ASP   A 133 ? 0.2552 0.3402 0.2887 -0.0245 -0.0093 0.0487  139 ASP   A OD2 
1027 N N   . LEU   A 134 ? 0.1492 0.2068 0.1650 -0.0310 0.0034  0.0153  140 LEU   A N   
1028 C CA  . LEU   A 134 ? 0.1531 0.2027 0.1722 -0.0282 0.0041  0.0121  140 LEU   A CA  
1029 C C   . LEU   A 134 ? 0.1599 0.2058 0.1754 -0.0345 0.0101  0.0032  140 LEU   A C   
1030 O O   . LEU   A 134 ? 0.1686 0.2052 0.1873 -0.0300 0.0131  -0.0028 140 LEU   A O   
1031 C CB  . LEU   A 134 ? 0.1561 0.1949 0.1815 -0.0169 0.0027  0.0109  140 LEU   A CB  
1032 C CG  . LEU   A 134 ? 0.1772 0.2175 0.2070 -0.0104 -0.0009 0.0181  140 LEU   A CG  
1033 C CD1 . LEU   A 134 ? 0.1850 0.2142 0.2182 -0.0018 -0.0010 0.0149  140 LEU   A CD1 
1034 C CD2 . LEU   A 134 ? 0.1961 0.2412 0.2298 -0.0114 -0.0036 0.0257  140 LEU   A CD2 
1035 N N   . LEU   A 135 ? 0.1622 0.2162 0.1712 -0.0458 0.0122  0.0029  141 LEU   A N   
1036 C CA  . LEU   A 135 ? 0.1773 0.2279 0.1824 -0.0532 0.0199  -0.0066 141 LEU   A CA  
1037 C C   . LEU   A 135 ? 0.1769 0.2187 0.1888 -0.0489 0.0230  -0.0115 141 LEU   A C   
1038 O O   . LEU   A 135 ? 0.2013 0.2363 0.2157 -0.0499 0.0301  -0.0194 141 LEU   A O   
1039 C CB  . LEU   A 135 ? 0.1938 0.2558 0.1885 -0.0685 0.0222  -0.0065 141 LEU   A CB  
1040 C CG  . LEU   A 135 ? 0.2148 0.2894 0.2030 -0.0745 0.0179  0.0008  141 LEU   A CG  
1041 C CD1 . LEU   A 135 ? 0.2388 0.3252 0.2146 -0.0924 0.0208  -0.0003 141 LEU   A CD1 
1042 C CD2 . LEU   A 135 ? 0.2318 0.3024 0.2196 -0.0710 0.0193  -0.0020 141 LEU   A CD2 
1043 N N   . TRP   A 136 ? 0.1605 0.2022 0.1770 -0.0439 0.0180  -0.0063 142 TRP   A N   
1044 C CA  . TRP   A 136 ? 0.1681 0.2033 0.1911 -0.0405 0.0199  -0.0098 142 TRP   A CA  
1045 C C   . TRP   A 136 ? 0.1705 0.1961 0.2016 -0.0312 0.0209  -0.0130 142 TRP   A C   
1046 O O   . TRP   A 136 ? 0.1866 0.2078 0.2246 -0.0293 0.0236  -0.0162 142 TRP   A O   
1047 C CB  . TRP   A 136 ? 0.1712 0.2085 0.1963 -0.0383 0.0141  -0.0031 142 TRP   A CB  
1048 C CG  . TRP   A 136 ? 0.1658 0.2016 0.1936 -0.0302 0.0078  0.0037  142 TRP   A CG  
1049 C CD1 . TRP   A 136 ? 0.1833 0.2261 0.2092 -0.0311 0.0037  0.0115  142 TRP   A CD1 
1050 C CD2 . TRP   A 136 ? 0.1710 0.1978 0.2045 -0.0204 0.0055  0.0033  142 TRP   A CD2 
1051 N NE1 . TRP   A 136 ? 0.1929 0.2304 0.2237 -0.0217 0.0003  0.0151  142 TRP   A NE1 
1052 C CE2 . TRP   A 136 ? 0.1803 0.2078 0.2144 -0.0159 0.0013  0.0096  142 TRP   A CE2 
1053 C CE3 . TRP   A 136 ? 0.1851 0.2044 0.2237 -0.0159 0.0067  -0.0012 142 TRP   A CE3 
1054 C CZ2 . TRP   A 136 ? 0.1938 0.2133 0.2314 -0.0079 -0.0007 0.0097  142 TRP   A CZ2 
1055 C CZ3 . TRP   A 136 ? 0.2030 0.2162 0.2444 -0.0087 0.0033  0.0002  142 TRP   A CZ3 
1056 C CH2 . TRP   A 136 ? 0.1945 0.2072 0.2345 -0.0052 0.0001  0.0047  142 TRP   A CH2 
1057 N N   . LEU   A 137 ? 0.1628 0.1860 0.1939 -0.0259 0.0185  -0.0114 143 LEU   A N   
1058 C CA  . LEU   A 137 ? 0.1807 0.1963 0.2190 -0.0186 0.0191  -0.0136 143 LEU   A CA  
1059 C C   . LEU   A 137 ? 0.2162 0.2281 0.2590 -0.0215 0.0272  -0.0201 143 LEU   A C   
1060 O O   . LEU   A 137 ? 0.2291 0.2358 0.2814 -0.0161 0.0283  -0.0208 143 LEU   A O   
1061 C CB  . LEU   A 137 ? 0.1774 0.1920 0.2134 -0.0141 0.0159  -0.0111 143 LEU   A CB  
1062 C CG  . LEU   A 137 ? 0.1757 0.1911 0.2106 -0.0091 0.0095  -0.0055 143 LEU   A CG  
1063 C CD1 . LEU   A 137 ? 0.1852 0.2013 0.2172 -0.0063 0.0079  -0.0037 143 LEU   A CD1 
1064 C CD2 . LEU   A 137 ? 0.1827 0.1920 0.2233 -0.0033 0.0068  -0.0052 143 LEU   A CD2 
1065 N N   . ASP   A 138 ? 0.2474 0.2622 0.2842 -0.0306 0.0334  -0.0246 144 ASP   A N   
1066 C CA  . ASP   A 138 ? 0.2790 0.2887 0.3203 -0.0343 0.0435  -0.0321 144 ASP   A CA  
1067 C C   . ASP   A 138 ? 0.3259 0.3347 0.3736 -0.0369 0.0494  -0.0361 144 ASP   A C   
1068 O O   . ASP   A 138 ? 0.3395 0.3433 0.3930 -0.0397 0.0594  -0.0427 144 ASP   A O   
1069 C CB  . ASP   A 138 ? 0.2948 0.3073 0.3248 -0.0451 0.0490  -0.0366 144 ASP   A CB  
1070 C CG  . ASP   A 138 ? 0.3388 0.3533 0.3627 -0.0442 0.0448  -0.0335 144 ASP   A CG  
1071 O OD1 . ASP   A 138 ? 0.3548 0.3659 0.3841 -0.0347 0.0396  -0.0293 144 ASP   A OD1 
1072 O OD2 . ASP   A 138 ? 0.4001 0.4203 0.4130 -0.0540 0.0466  -0.0349 144 ASP   A OD2 
1073 N N   . GLU   A 139 ? 0.3447 0.3577 0.3921 -0.0364 0.0445  -0.0325 145 GLU   A N   
1074 C CA  . GLU   A 139 ? 0.3879 0.4014 0.4406 -0.0399 0.0502  -0.0362 145 GLU   A CA  
1075 C C   . GLU   A 139 ? 0.4183 0.4319 0.4797 -0.0327 0.0441  -0.0313 145 GLU   A C   
1076 O O   . GLU   A 139 ? 0.4157 0.4287 0.4768 -0.0262 0.0356  -0.0254 145 GLU   A O   
1077 C CB  . GLU   A 139 ? 0.4376 0.4585 0.4776 -0.0520 0.0521  -0.0381 145 GLU   A CB  
1078 C CG  . GLU   A 139 ? 0.5249 0.5528 0.5567 -0.0520 0.0416  -0.0297 145 GLU   A CG  
1079 C CD  . GLU   A 139 ? 0.6160 0.6536 0.6346 -0.0643 0.0414  -0.0285 145 GLU   A CD  
1080 O OE1 . GLU   A 139 ? 0.6149 0.6589 0.6305 -0.0651 0.0343  -0.0210 145 GLU   A OE1 
1081 O OE2 . GLU   A 139 ? 0.6571 0.6962 0.6685 -0.0738 0.0486  -0.0346 145 GLU   A OE2 
1082 N N   . GLU   A 140 ? 0.4505 0.4648 0.5189 -0.0349 0.0492  -0.0341 146 GLU   A N   
1083 C CA  . GLU   A 140 ? 0.4886 0.5042 0.5652 -0.0304 0.0448  -0.0302 146 GLU   A CA  
1084 C C   . GLU   A 140 ? 0.5096 0.5216 0.6015 -0.0216 0.0442  -0.0279 146 GLU   A C   
1085 O O   . GLU   A 140 ? 0.5188 0.5317 0.6232 -0.0204 0.0484  -0.0286 146 GLU   A O   
1086 C CB  . GLU   A 140 ? 0.5333 0.5517 0.6011 -0.0297 0.0345  -0.0238 146 GLU   A CB  
1087 C CG  . GLU   A 140 ? 0.6167 0.6348 0.6916 -0.0247 0.0289  -0.0196 146 GLU   A CG  
1088 C CD  . GLU   A 140 ? 0.7194 0.7415 0.7940 -0.0300 0.0299  -0.0197 146 GLU   A CD  
1089 O OE1 . GLU   A 140 ? 0.7459 0.7703 0.8116 -0.0332 0.0251  -0.0162 146 GLU   A OE1 
1090 O OE2 . GLU   A 140 ? 0.7373 0.7607 0.8219 -0.0309 0.0357  -0.0228 146 GLU   A OE2 
1091 N N   . SER   B 1   ? 0.2220 0.2446 0.2451 0.0079  -0.0109 0.0378  7   SER   C N   
1092 C CA  . SER   B 1   ? 0.2119 0.2373 0.2439 0.0061  -0.0123 0.0378  7   SER   C CA  
1093 C C   . SER   B 1   ? 0.2110 0.2342 0.2426 0.0043  -0.0122 0.0339  7   SER   C C   
1094 O O   . SER   B 1   ? 0.2284 0.2480 0.2524 0.0043  -0.0125 0.0314  7   SER   C O   
1095 C CB  . SER   B 1   ? 0.2560 0.2835 0.2881 0.0053  -0.0172 0.0398  7   SER   C CB  
1096 O OG  . SER   B 1   ? 0.3061 0.3308 0.3297 0.0042  -0.0209 0.0372  7   SER   C OG  
1097 N N   . GLY   B 2   ? 0.2037 0.2288 0.2435 0.0031  -0.0115 0.0338  8   GLY   C N   
1098 C CA  . GLY   B 2   ? 0.1926 0.2155 0.2320 0.0018  -0.0110 0.0310  8   GLY   C CA  
1099 C C   . GLY   B 2   ? 0.1679 0.1923 0.2148 0.0018  -0.0079 0.0308  8   GLY   C C   
1100 O O   . GLY   B 2   ? 0.1790 0.2049 0.2301 0.0031  -0.0055 0.0315  8   GLY   C O   
1101 N N   . ALA   B 3   ? 0.1531 0.1765 0.2015 0.0005  -0.0075 0.0298  9   ALA   C N   
1102 C CA  . ALA   B 3   ? 0.1609 0.1850 0.2146 0.0009  -0.0040 0.0294  9   ALA   C CA  
1103 C C   . ALA   B 3   ? 0.1476 0.1680 0.1969 0.0006  -0.0026 0.0275  9   ALA   C C   
1104 O O   . ALA   B 3   ? 0.1686 0.1863 0.2131 -0.0005 -0.0044 0.0268  9   ALA   C O   
1105 C CB  . ALA   B 3   ? 0.1891 0.2168 0.2524 -0.0001 -0.0041 0.0320  9   ALA   C CB  
1106 N N   . ILE   B 4   ? 0.1439 0.1638 0.1945 0.0017  0.0009  0.0266  10  ILE   C N   
1107 C CA  . ILE   B 4   ? 0.1524 0.1690 0.1992 0.0019  0.0030  0.0257  10  ILE   C CA  
1108 C C   . ILE   B 4   ? 0.1508 0.1690 0.2050 0.0010  0.0055  0.0276  10  ILE   C C   
1109 O O   . ILE   B 4   ? 0.1633 0.1844 0.2237 0.0017  0.0072  0.0283  10  ILE   C O   
1110 C CB  . ILE   B 4   ? 0.1577 0.1723 0.1994 0.0044  0.0050  0.0233  10  ILE   C CB  
1111 C CG1 . ILE   B 4   ? 0.1671 0.1814 0.2047 0.0055  0.0028  0.0215  10  ILE   C CG1 
1112 C CG2 . ILE   B 4   ? 0.1788 0.1894 0.2148 0.0051  0.0070  0.0231  10  ILE   C CG2 
1113 C CD1 . ILE   B 4   ? 0.1745 0.1882 0.2100 0.0079  0.0040  0.0188  10  ILE   C CD1 
1114 N N   . TYR   B 5   ? 0.1454 0.1617 0.1999 -0.0004 0.0063  0.0286  11  TYR   C N   
1115 C CA  . TYR   B 5   ? 0.1523 0.1701 0.2149 -0.0013 0.0094  0.0308  11  TYR   C CA  
1116 C C   . TYR   B 5   ? 0.1768 0.1905 0.2342 0.0001  0.0140  0.0307  11  TYR   C C   
1117 O O   . TYR   B 5   ? 0.1972 0.2073 0.2509 -0.0008 0.0139  0.0311  11  TYR   C O   
1118 C CB  . TYR   B 5   ? 0.1596 0.1794 0.2296 -0.0045 0.0064  0.0326  11  TYR   C CB  
1119 C CG  . TYR   B 5   ? 0.1649 0.1891 0.2396 -0.0053 0.0019  0.0332  11  TYR   C CG  
1120 C CD1 . TYR   B 5   ? 0.1588 0.1878 0.2432 -0.0050 0.0027  0.0351  11  TYR   C CD1 
1121 C CD2 . TYR   B 5   ? 0.1801 0.2033 0.2486 -0.0057 -0.0028 0.0319  11  TYR   C CD2 
1122 C CE1 . TYR   B 5   ? 0.1832 0.2159 0.2711 -0.0052 -0.0015 0.0362  11  TYR   C CE1 
1123 C CE2 . TYR   B 5   ? 0.2024 0.2292 0.2735 -0.0059 -0.0067 0.0329  11  TYR   C CE2 
1124 C CZ  . TYR   B 5   ? 0.2026 0.2342 0.2832 -0.0055 -0.0061 0.0352  11  TYR   C CZ  
1125 O OH  . TYR   B 5   ? 0.2218 0.2566 0.3042 -0.0052 -0.0099 0.0367  11  TYR   C OH  
1126 N N   . VAL   B 6   ? 0.1793 0.1926 0.2352 0.0025  0.0180  0.0301  12  VAL   C N   
1127 C CA  . VAL   B 6   ? 0.1942 0.2033 0.2432 0.0045  0.0225  0.0302  12  VAL   C CA  
1128 C C   . VAL   B 6   ? 0.1891 0.1995 0.2444 0.0053  0.0281  0.0319  12  VAL   C C   
1129 O O   . VAL   B 6   ? 0.1788 0.1921 0.2388 0.0061  0.0288  0.0310  12  VAL   C O   
1130 C CB  . VAL   B 6   ? 0.2020 0.2084 0.2398 0.0076  0.0217  0.0270  12  VAL   C CB  
1131 C CG1 . VAL   B 6   ? 0.1989 0.2085 0.2396 0.0087  0.0208  0.0246  12  VAL   C CG1 
1132 C CG2 . VAL   B 6   ? 0.2254 0.2274 0.2547 0.0103  0.0261  0.0273  12  VAL   C CG2 
1133 N N   . GLY   B 7   ? 0.2054 0.2135 0.2619 0.0050  0.0327  0.0346  13  GLY   C N   
1134 C CA  . GLY   B 7   ? 0.2046 0.2141 0.2681 0.0058  0.0388  0.0365  13  GLY   C CA  
1135 C C   . GLY   B 7   ? 0.1957 0.2113 0.2739 0.0037  0.0374  0.0377  13  GLY   C C   
1136 O O   . GLY   B 7   ? 0.2108 0.2293 0.2960 0.0007  0.0326  0.0386  13  GLY   C O   
1137 N N   . ASN   B 8   ? 0.1898 0.2075 0.2718 0.0056  0.0405  0.0371  14  ASN   C N   
1138 C CA  . ASN   B 8   ? 0.1904 0.2140 0.2862 0.0042  0.0389  0.0383  14  ASN   C CA  
1139 C C   . ASN   B 8   ? 0.1772 0.2022 0.2707 0.0052  0.0348  0.0355  14  ASN   C C   
1140 O O   . ASN   B 8   ? 0.1777 0.2060 0.2796 0.0058  0.0357  0.0358  14  ASN   C O   
1141 C CB  . ASN   B 8   ? 0.2090 0.2344 0.3148 0.0053  0.0458  0.0404  14  ASN   C CB  
1142 C CG  . ASN   B 8   ? 0.2900 0.3161 0.4043 0.0032  0.0490  0.0442  14  ASN   C CG  
1143 O OD1 . ASN   B 8   ? 0.3262 0.3573 0.4543 0.0004  0.0461  0.0466  14  ASN   C OD1 
1144 N ND2 . ASN   B 8   ? 0.3187 0.3397 0.4248 0.0046  0.0544  0.0449  14  ASN   C ND2 
1145 N N   . TYR   B 9   ? 0.1536 0.1764 0.2373 0.0050  0.0302  0.0333  15  TYR   C N   
1146 C CA  . TYR   B 9   ? 0.1612 0.1850 0.2428 0.0058  0.0266  0.0309  15  TYR   C CA  
1147 C C   . TYR   B 9   ? 0.1563 0.1816 0.2374 0.0037  0.0203  0.0315  15  TYR   C C   
1148 O O   . TYR   B 9   ? 0.1746 0.1978 0.2508 0.0023  0.0185  0.0317  15  TYR   C O   
1149 C CB  . TYR   B 9   ? 0.1733 0.1929 0.2428 0.0084  0.0274  0.0270  15  TYR   C CB  
1150 C CG  . TYR   B 9   ? 0.1951 0.2123 0.2621 0.0112  0.0332  0.0255  15  TYR   C CG  
1151 C CD1 . TYR   B 9   ? 0.2147 0.2339 0.2896 0.0122  0.0359  0.0250  15  TYR   C CD1 
1152 C CD2 . TYR   B 9   ? 0.2205 0.2331 0.2764 0.0132  0.0360  0.0244  15  TYR   C CD2 
1153 C CE1 . TYR   B 9   ? 0.2477 0.2642 0.3194 0.0150  0.0416  0.0232  15  TYR   C CE1 
1154 C CE2 . TYR   B 9   ? 0.2525 0.2624 0.3039 0.0162  0.0413  0.0228  15  TYR   C CE2 
1155 C CZ  . TYR   B 9   ? 0.2846 0.2964 0.3437 0.0171  0.0441  0.0218  15  TYR   C CZ  
1156 O OH  . TYR   B 9   ? 0.3546 0.3633 0.4089 0.0203  0.0497  0.0198  15  TYR   C OH  
1157 N N   . ARG   B 10  ? 0.1346 0.1629 0.2201 0.0036  0.0175  0.0316  16  ARG   C N   
1158 C CA  . ARG   B 10  ? 0.1280 0.1573 0.2113 0.0024  0.0121  0.0319  16  ARG   C CA  
1159 C C   . ARG   B 10  ? 0.1318 0.1600 0.2108 0.0042  0.0117  0.0295  16  ARG   C C   
1160 O O   . ARG   B 10  ? 0.1333 0.1630 0.2179 0.0054  0.0136  0.0293  16  ARG   C O   
1161 C CB  . ARG   B 10  ? 0.1442 0.1784 0.2378 0.0010  0.0094  0.0352  16  ARG   C CB  
1162 C CG  . ARG   B 10  ? 0.1551 0.1903 0.2458 0.0007  0.0044  0.0359  16  ARG   C CG  
1163 C CD  . ARG   B 10  ? 0.1600 0.1999 0.2594 -0.0004 0.0010  0.0393  16  ARG   C CD  
1164 N NE  . ARG   B 10  ? 0.1692 0.2108 0.2688 0.0008  -0.0012 0.0409  16  ARG   C NE  
1165 C CZ  . ARG   B 10  ? 0.1957 0.2371 0.2892 0.0005  -0.0055 0.0415  16  ARG   C CZ  
1166 N NH1 . ARG   B 10  ? 0.2024 0.2415 0.2883 -0.0009 -0.0082 0.0398  16  ARG   C NH1 
1167 N NH2 . ARG   B 10  ? 0.1993 0.2420 0.2933 0.0020  -0.0065 0.0436  16  ARG   C NH2 
1168 N N   . VAL   B 11  ? 0.1261 0.1518 0.1962 0.0044  0.0096  0.0276  17  VAL   C N   
1169 C CA  . VAL   B 11  ? 0.1222 0.1472 0.1896 0.0058  0.0091  0.0252  17  VAL   C CA  
1170 C C   . VAL   B 11  ? 0.1312 0.1576 0.1986 0.0051  0.0058  0.0268  17  VAL   C C   
1171 O O   . VAL   B 11  ? 0.1382 0.1635 0.2002 0.0041  0.0033  0.0273  17  VAL   C O   
1172 C CB  . VAL   B 11  ? 0.1449 0.1661 0.2027 0.0070  0.0092  0.0220  17  VAL   C CB  
1173 C CG1 . VAL   B 11  ? 0.1621 0.1832 0.2197 0.0085  0.0087  0.0192  17  VAL   C CG1 
1174 C CG2 . VAL   B 11  ? 0.1633 0.1822 0.2181 0.0080  0.0125  0.0210  17  VAL   C CG2 
1175 N N   . VAL   B 12  ? 0.1243 0.1527 0.1974 0.0058  0.0060  0.0278  18  VAL   C N   
1176 C CA  A VAL   B 12  ? 0.1171 0.1467 0.1897 0.0056  0.0037  0.0300  18  VAL   C CA  
1177 C CA  B VAL   B 12  ? 0.1364 0.1660 0.2090 0.0056  0.0036  0.0300  18  VAL   C CA  
1178 C C   . VAL   B 12  ? 0.1274 0.1568 0.2022 0.0069  0.0050  0.0289  18  VAL   C C   
1179 O O   . VAL   B 12  ? 0.1335 0.1623 0.2121 0.0078  0.0072  0.0265  18  VAL   C O   
1180 C CB  A VAL   B 12  ? 0.1155 0.1484 0.1946 0.0050  0.0023  0.0341  18  VAL   C CB  
1181 C CB  B VAL   B 12  ? 0.1716 0.2047 0.2516 0.0050  0.0026  0.0341  18  VAL   C CB  
1182 C CG1 A VAL   B 12  ? 0.1239 0.1574 0.2012 0.0033  -0.0003 0.0352  18  VAL   C CG1 
1183 C CG1 B VAL   B 12  ? 0.1734 0.2077 0.2517 0.0052  0.0000  0.0370  18  VAL   C CG1 
1184 C CG2 A VAL   B 12  ? 0.0874 0.1223 0.1768 0.0059  0.0050  0.0352  18  VAL   C CG2 
1185 C CG2 B VAL   B 12  ? 0.1985 0.2323 0.2793 0.0034  0.0014  0.0348  18  VAL   C CG2 
1186 N N   . ASN   B 13  ? 0.1138 0.1434 0.1865 0.0072  0.0039  0.0307  19  ASN   C N   
1187 C CA  . ASN   B 13  ? 0.1070 0.1368 0.1843 0.0083  0.0057  0.0307  19  ASN   C CA  
1188 C C   . ASN   B 13  ? 0.1177 0.1495 0.2051 0.0087  0.0074  0.0332  19  ASN   C C   
1189 O O   . ASN   B 13  ? 0.1278 0.1614 0.2171 0.0085  0.0062  0.0370  19  ASN   C O   
1190 C CB  . ASN   B 13  ? 0.1204 0.1501 0.1938 0.0087  0.0050  0.0334  19  ASN   C CB  
1191 C CG  . ASN   B 13  ? 0.1287 0.1562 0.1930 0.0087  0.0038  0.0310  19  ASN   C CG  
1192 O OD1 . ASN   B 13  ? 0.1494 0.1759 0.2066 0.0080  0.0016  0.0313  19  ASN   C OD1 
1193 N ND2 . ASN   B 13  ? 0.1382 0.1648 0.2035 0.0094  0.0052  0.0283  19  ASN   C ND2 
1194 N N   . ARG   B 14  ? 0.1207 0.1520 0.2151 0.0093  0.0099  0.0310  20  ARG   C N   
1195 C CA  . ARG   B 14  ? 0.1101 0.1426 0.2147 0.0099  0.0119  0.0330  20  ARG   C CA  
1196 C C   . ARG   B 14  ? 0.1263 0.1604 0.2340 0.0105  0.0118  0.0389  20  ARG   C C   
1197 O O   . ARG   B 14  ? 0.1321 0.1681 0.2454 0.0109  0.0119  0.0425  20  ARG   C O   
1198 C CB  . ARG   B 14  ? 0.1078 0.1388 0.2191 0.0104  0.0143  0.0291  20  ARG   C CB  
1199 C CG  . ARG   B 14  ? 0.1159 0.1473 0.2383 0.0111  0.0170  0.0305  20  ARG   C CG  
1200 C CD  . ARG   B 14  ? 0.1319 0.1613 0.2610 0.0114  0.0190  0.0259  20  ARG   C CD  
1201 N NE  . ARG   B 14  ? 0.1388 0.1675 0.2782 0.0122  0.0218  0.0256  20  ARG   C NE  
1202 C CZ  . ARG   B 14  ? 0.1326 0.1615 0.2821 0.0127  0.0239  0.0294  20  ARG   C CZ  
1203 N NH1 . ARG   B 14  ? 0.1417 0.1719 0.2913 0.0128  0.0234  0.0349  20  ARG   C NH1 
1204 N NH2 . ARG   B 14  ? 0.1393 0.1670 0.2986 0.0135  0.0266  0.0284  20  ARG   C NH2 
1205 N N   . HIS   B 15  ? 0.1216 0.1549 0.2250 0.0108  0.0116  0.0401  21  HIS   C N   
1206 C CA  . HIS   B 15  ? 0.1316 0.1659 0.2363 0.0119  0.0120  0.0461  21  HIS   C CA  
1207 C C   . HIS   B 15  ? 0.1452 0.1811 0.2432 0.0119  0.0084  0.0497  21  HIS   C C   
1208 O O   . HIS   B 15  ? 0.1729 0.2098 0.2715 0.0132  0.0081  0.0549  21  HIS   C O   
1209 C CB  . HIS   B 15  ? 0.1293 0.1622 0.2321 0.0126  0.0140  0.0468  21  HIS   C CB  
1210 C CG  . HIS   B 15  ? 0.1413 0.1731 0.2322 0.0124  0.0121  0.0455  21  HIS   C CG  
1211 N ND1 . HIS   B 15  ? 0.1561 0.1868 0.2436 0.0115  0.0114  0.0402  21  HIS   C ND1 
1212 C CD2 . HIS   B 15  ? 0.1515 0.1831 0.2337 0.0132  0.0109  0.0490  21  HIS   C CD2 
1213 C CE1 . HIS   B 15  ? 0.1666 0.1963 0.2441 0.0118  0.0101  0.0407  21  HIS   C CE1 
1214 N NE2 . HIS   B 15  ? 0.1613 0.1913 0.2350 0.0127  0.0098  0.0456  21  HIS   C NE2 
1215 N N   . LEU   B 16  ? 0.1376 0.1736 0.2294 0.0105  0.0056  0.0469  22  LEU   C N   
1216 C CA  . LEU   B 16  ? 0.1434 0.1810 0.2302 0.0101  0.0015  0.0493  22  LEU   C CA  
1217 C C   . LEU   B 16  ? 0.1508 0.1908 0.2445 0.0092  0.0005  0.0493  22  LEU   C C   
1218 O O   . LEU   B 16  ? 0.1665 0.2082 0.2579 0.0083  -0.0032 0.0504  22  LEU   C O   
1219 C CB  . LEU   B 16  ? 0.1480 0.1836 0.2234 0.0091  -0.0008 0.0466  22  LEU   C CB  
1220 C CG  . LEU   B 16  ? 0.1557 0.1891 0.2240 0.0103  0.0003  0.0469  22  LEU   C CG  
1221 C CD1 . LEU   B 16  ? 0.1597 0.1907 0.2176 0.0094  -0.0017 0.0436  22  LEU   C CD1 
1222 C CD2 . LEU   B 16  ? 0.1635 0.1977 0.2301 0.0121  -0.0001 0.0524  22  LEU   C CD2 
1223 N N   . ALA   B 17  ? 0.1480 0.1880 0.2502 0.0093  0.0039  0.0475  23  ALA   C N   
1224 C CA  . ALA   B 17  ? 0.1489 0.1910 0.2581 0.0088  0.0041  0.0475  23  ALA   C CA  
1225 C C   . ALA   B 17  ? 0.1686 0.2144 0.2847 0.0096  0.0020  0.0529  23  ALA   C C   
1226 O O   . ALA   B 17  ? 0.1786 0.2248 0.2974 0.0112  0.0024  0.0566  23  ALA   C O   
1227 C CB  . ALA   B 17  ? 0.1628 0.2036 0.2789 0.0094  0.0085  0.0445  23  ALA   C CB  
1228 N N   . THR   B 18  ? 0.1580 0.2064 0.2770 0.0085  -0.0003 0.0534  24  THR   C N   
1229 C CA  . THR   B 18  ? 0.1632 0.2159 0.2897 0.0091  -0.0033 0.0583  24  THR   C CA  
1230 C C   . THR   B 18  ? 0.1600 0.2147 0.3003 0.0102  0.0005  0.0595  24  THR   C C   
1231 O O   . THR   B 18  ? 0.1653 0.2177 0.3081 0.0102  0.0052  0.0560  24  THR   C O   
1232 C CB  . THR   B 18  ? 0.1781 0.2332 0.3029 0.0071  -0.0081 0.0580  24  THR   C CB  
1233 O OG1 . THR   B 18  ? 0.1813 0.2362 0.3108 0.0058  -0.0051 0.0551  24  THR   C OG1 
1234 C CG2 . THR   B 18  ? 0.1950 0.2476 0.3062 0.0060  -0.0119 0.0562  24  THR   C CG2 
1235 N N   . HIS   B 19  ? 0.1679 0.2268 0.3173 0.0114  -0.0017 0.0645  25  HIS   C N   
1236 C CA  . HIS   B 19  ? 0.1722 0.2332 0.3357 0.0125  0.0019  0.0658  25  HIS   C CA  
1237 C C   . HIS   B 19  ? 0.1537 0.2152 0.3202 0.0109  0.0039  0.0624  25  HIS   C C   
1238 O O   . HIS   B 19  ? 0.1652 0.2251 0.3371 0.0116  0.0095  0.0601  25  HIS   C O   
1239 C CB  . HIS   B 19  ? 0.1916 0.2578 0.3643 0.0140  -0.0019 0.0719  25  HIS   C CB  
1240 C CG  . HIS   B 19  ? 0.2250 0.2942 0.4135 0.0151  0.0013  0.0734  25  HIS   C CG  
1241 N ND1 . HIS   B 19  ? 0.2623 0.3296 0.4588 0.0172  0.0069  0.0738  25  HIS   C ND1 
1242 C CD2 . HIS   B 19  ? 0.2445 0.3179 0.4419 0.0141  0.0004  0.0738  25  HIS   C CD2 
1243 C CE1 . HIS   B 19  ? 0.2581 0.3286 0.4676 0.0178  0.0091  0.0749  25  HIS   C CE1 
1244 N NE2 . HIS   B 19  ? 0.2543 0.3287 0.4652 0.0160  0.0055  0.0750  25  HIS   C NE2 
1245 N N   . ASN   B 20  ? 0.1562 0.2193 0.3186 0.0087  0.0000  0.0616  26  ASN   C N   
1246 C CA  . ASN   B 20  ? 0.1632 0.2265 0.3289 0.0071  0.0027  0.0590  26  ASN   C CA  
1247 C C   . ASN   B 20  ? 0.1442 0.2019 0.3017 0.0071  0.0079  0.0540  26  ASN   C C   
1248 O O   . ASN   B 20  ? 0.1422 0.1991 0.3042 0.0075  0.0130  0.0522  26  ASN   C O   
1249 C CB  . ASN   B 20  ? 0.1819 0.2471 0.3449 0.0045  -0.0025 0.0589  26  ASN   C CB  
1250 C CG  . ASN   B 20  ? 0.2553 0.3209 0.4242 0.0031  0.0012  0.0573  26  ASN   C CG  
1251 O OD1 . ASN   B 20  ? 0.2920 0.3615 0.4746 0.0035  0.0033  0.0596  26  ASN   C OD1 
1252 N ND2 . ASN   B 20  ? 0.2739 0.3352 0.4330 0.0016  0.0028  0.0537  26  ASN   C ND2 
1253 N N   . ASP   B 21  ? 0.1345 0.1885 0.2802 0.0070  0.0068  0.0518  27  ASP   C N   
1254 C CA  . ASP   B 21  ? 0.1345 0.1837 0.2730 0.0073  0.0109  0.0470  27  ASP   C CA  
1255 C C   . ASP   B 21  ? 0.1373 0.1852 0.2827 0.0094  0.0161  0.0457  27  ASP   C C   
1256 O O   . ASP   B 21  ? 0.1517 0.1973 0.2964 0.0098  0.0204  0.0424  27  ASP   C O   
1257 C CB  . ASP   B 21  ? 0.1381 0.1842 0.2652 0.0071  0.0087  0.0451  27  ASP   C CB  
1258 C CG  . ASP   B 21  ? 0.1492 0.1947 0.2669 0.0053  0.0048  0.0445  27  ASP   C CG  
1259 O OD1 . ASP   B 21  ? 0.1654 0.2107 0.2827 0.0040  0.0052  0.0434  27  ASP   C OD1 
1260 O OD2 . ASP   B 21  ? 0.1541 0.1991 0.2654 0.0052  0.0015  0.0453  27  ASP   C OD2 
1261 N N   . TRP   B 22  ? 0.1460 0.1951 0.2980 0.0108  0.0159  0.0485  28  TRP   C N   
1262 C CA  . TRP   B 22  ? 0.1436 0.1910 0.3032 0.0126  0.0207  0.0472  28  TRP   C CA  
1263 C C   . TRP   B 22  ? 0.1353 0.1848 0.3055 0.0135  0.0244  0.0481  28  TRP   C C   
1264 O O   . TRP   B 22  ? 0.1390 0.1857 0.3118 0.0149  0.0295  0.0447  28  TRP   C O   
1265 C CB  . TRP   B 22  ? 0.1443 0.1923 0.3094 0.0139  0.0199  0.0508  28  TRP   C CB  
1266 C CG  . TRP   B 22  ? 0.1515 0.1962 0.3084 0.0136  0.0191  0.0487  28  TRP   C CG  
1267 C CD1 . TRP   B 22  ? 0.1684 0.2135 0.3181 0.0131  0.0154  0.0511  28  TRP   C CD1 
1268 C CD2 . TRP   B 22  ? 0.1463 0.1868 0.3023 0.0140  0.0224  0.0437  28  TRP   C CD2 
1269 N NE1 . TRP   B 22  ? 0.1735 0.2153 0.3191 0.0131  0.0167  0.0483  28  TRP   C NE1 
1270 C CE2 . TRP   B 22  ? 0.1634 0.2025 0.3131 0.0135  0.0205  0.0437  28  TRP   C CE2 
1271 C CE3 . TRP   B 22  ? 0.1715 0.2093 0.3316 0.0149  0.0266  0.0391  28  TRP   C CE3 
1272 C CZ2 . TRP   B 22  ? 0.1669 0.2027 0.3164 0.0136  0.0224  0.0395  28  TRP   C CZ2 
1273 C CZ3 . TRP   B 22  ? 0.1764 0.2105 0.3345 0.0150  0.0278  0.0343  28  TRP   C CZ3 
1274 C CH2 . TRP   B 22  ? 0.1695 0.2029 0.3233 0.0142  0.0255  0.0347  28  TRP   C CH2 
1275 N N   . ALA   B 23  ? 0.1353 0.1895 0.3115 0.0129  0.0218  0.0522  29  ALA   C N   
1276 C CA  . ALA   B 23  ? 0.1363 0.1933 0.3245 0.0136  0.0253  0.0537  29  ALA   C CA  
1277 C C   . ALA   B 23  ? 0.1565 0.2115 0.3399 0.0128  0.0291  0.0501  29  ALA   C C   
1278 O O   . ALA   B 23  ? 0.1613 0.2174 0.3532 0.0138  0.0339  0.0504  29  ALA   C O   
1279 C CB  . ALA   B 23  ? 0.1387 0.2021 0.3360 0.0130  0.0205  0.0593  29  ALA   C CB  
1280 N N   . ASN   B 24  ? 0.1550 0.2068 0.3249 0.0113  0.0275  0.0470  30  ASN   C N   
1281 C CA  . ASN   B 24  ? 0.1585 0.2076 0.3221 0.0108  0.0311  0.0439  30  ASN   C CA  
1282 C C   . ASN   B 24  ? 0.1622 0.2056 0.3120 0.0114  0.0321  0.0387  30  ASN   C C   
1283 O O   . ASN   B 24  ? 0.1571 0.1980 0.2967 0.0105  0.0317  0.0367  30  ASN   C O   
1284 C CB  . ASN   B 24  ? 0.1731 0.2247 0.3352 0.0082  0.0273  0.0460  30  ASN   C CB  
1285 C CG  . ASN   B 24  ? 0.1783 0.2358 0.3554 0.0076  0.0264  0.0505  30  ASN   C CG  
1286 O OD1 . ASN   B 24  ? 0.1989 0.2575 0.3842 0.0082  0.0317  0.0512  30  ASN   C OD1 
1287 N ND2 . ASN   B 24  ? 0.1822 0.2438 0.3636 0.0068  0.0201  0.0538  30  ASN   C ND2 
1288 N N   . LEU   B 25  ? 0.1574 0.1986 0.3077 0.0130  0.0331  0.0366  31  LEU   C N   
1289 C CA  . LEU   B 25  ? 0.1560 0.1926 0.2953 0.0134  0.0328  0.0316  31  LEU   C CA  
1290 C C   . LEU   B 25  ? 0.1791 0.2115 0.3104 0.0147  0.0370  0.0269  31  LEU   C C   
1291 O O   . LEU   B 25  ? 0.1933 0.2249 0.3292 0.0164  0.0422  0.0261  31  LEU   C O   
1292 C CB  . LEU   B 25  ? 0.1609 0.1966 0.3063 0.0146  0.0333  0.0306  31  LEU   C CB  
1293 C CG  . LEU   B 25  ? 0.1723 0.2040 0.3093 0.0148  0.0322  0.0255  31  LEU   C CG  
1294 C CD1 . LEU   B 25  ? 0.1704 0.2028 0.2997 0.0131  0.0272  0.0267  31  LEU   C CD1 
1295 C CD2 . LEU   B 25  ? 0.1886 0.2189 0.3338 0.0160  0.0337  0.0242  31  LEU   C CD2 
1296 N N   . VAL   B 26  ? 0.1707 0.2003 0.2895 0.0143  0.0349  0.0239  32  VAL   C N   
1297 C CA  . VAL   B 26  ? 0.1826 0.2075 0.2910 0.0160  0.0379  0.0193  32  VAL   C CA  
1298 C C   . VAL   B 26  ? 0.1959 0.2178 0.2996 0.0170  0.0362  0.0139  32  VAL   C C   
1299 O O   . VAL   B 26  ? 0.2205 0.2391 0.3223 0.0191  0.0393  0.0094  32  VAL   C O   
1300 C CB  . VAL   B 26  ? 0.1891 0.2130 0.2872 0.0151  0.0366  0.0200  32  VAL   C CB  
1301 C CG1 . VAL   B 26  ? 0.2094 0.2282 0.2949 0.0173  0.0391  0.0155  32  VAL   C CG1 
1302 C CG2 . VAL   B 26  ? 0.1890 0.2157 0.2934 0.0138  0.0387  0.0248  32  VAL   C CG2 
1303 N N   . TRP   B 27  ? 0.1716 0.1944 0.2738 0.0156  0.0314  0.0142  33  TRP   C N   
1304 C CA  . TRP   B 27  ? 0.1704 0.1909 0.2697 0.0162  0.0294  0.0093  33  TRP   C CA  
1305 C C   . TRP   B 27  ? 0.1666 0.1895 0.2694 0.0145  0.0254  0.0117  33  TRP   C C   
1306 O O   . TRP   B 27  ? 0.1606 0.1857 0.2616 0.0131  0.0232  0.0158  33  TRP   C O   
1307 C CB  . TRP   B 27  ? 0.1852 0.2023 0.2707 0.0173  0.0284  0.0050  33  TRP   C CB  
1308 C CG  . TRP   B 27  ? 0.1904 0.2060 0.2723 0.0176  0.0248  0.0002  33  TRP   C CG  
1309 C CD1 . TRP   B 27  ? 0.2140 0.2270 0.2961 0.0191  0.0250  -0.0057 33  TRP   C CD1 
1310 C CD2 . TRP   B 27  ? 0.1866 0.2031 0.2646 0.0165  0.0204  0.0007  33  TRP   C CD2 
1311 N NE1 . TRP   B 27  ? 0.2309 0.2436 0.3103 0.0188  0.0206  -0.0090 33  TRP   C NE1 
1312 C CE2 . TRP   B 27  ? 0.2044 0.2194 0.2815 0.0173  0.0181  -0.0049 33  TRP   C CE2 
1313 C CE3 . TRP   B 27  ? 0.1842 0.2027 0.2600 0.0149  0.0183  0.0050  33  TRP   C CE3 
1314 C CZ2 . TRP   B 27  ? 0.2066 0.2223 0.2812 0.0167  0.0141  -0.0058 33  TRP   C CZ2 
1315 C CZ3 . TRP   B 27  ? 0.2009 0.2195 0.2731 0.0145  0.0147  0.0038  33  TRP   C CZ3 
1316 C CH2 . TRP   B 27  ? 0.2032 0.2208 0.2756 0.0154  0.0128  -0.0012 33  TRP   C CH2 
1317 N N   . GLU   B 28  ? 0.1480 0.1701 0.2561 0.0148  0.0248  0.0092  34  GLU   C N   
1318 C CA  . GLU   B 28  ? 0.1544 0.1783 0.2655 0.0135  0.0219  0.0115  34  GLU   C CA  
1319 C C   . GLU   B 28  ? 0.1589 0.1808 0.2718 0.0138  0.0209  0.0065  34  GLU   C C   
1320 O O   . GLU   B 28  ? 0.1719 0.1915 0.2882 0.0149  0.0227  0.0019  34  GLU   C O   
1321 C CB  . GLU   B 28  ? 0.1527 0.1793 0.2741 0.0130  0.0228  0.0173  34  GLU   C CB  
1322 C CG  . GLU   B 28  ? 0.1618 0.1878 0.2942 0.0141  0.0262  0.0169  34  GLU   C CG  
1323 C CD  . GLU   B 28  ? 0.1990 0.2231 0.3387 0.0143  0.0268  0.0143  34  GLU   C CD  
1324 O OE1 . GLU   B 28  ? 0.2323 0.2543 0.3788 0.0154  0.0296  0.0113  34  GLU   C OE1 
1325 O OE2 . GLU   B 28  ? 0.1765 0.2013 0.3162 0.0135  0.0247  0.0153  34  GLU   C OE2 
1326 N N   . ASP   B 29  ? 0.1390 0.1619 0.2505 0.0129  0.0182  0.0072  35  ASP   C N   
1327 C CA  . ASP   B 29  ? 0.1397 0.1615 0.2552 0.0129  0.0170  0.0028  35  ASP   C CA  
1328 C C   . ASP   B 29  ? 0.1440 0.1678 0.2642 0.0119  0.0162  0.0068  35  ASP   C C   
1329 O O   . ASP   B 29  ? 0.1477 0.1725 0.2608 0.0115  0.0142  0.0086  35  ASP   C O   
1330 C CB  . ASP   B 29  ? 0.1584 0.1785 0.2639 0.0137  0.0143  -0.0029 35  ASP   C CB  
1331 C CG  . ASP   B 29  ? 0.2179 0.2372 0.3276 0.0138  0.0121  -0.0083 35  ASP   C CG  
1332 O OD1 . ASP   B 29  ? 0.2212 0.2420 0.3397 0.0127  0.0120  -0.0065 35  ASP   C OD1 
1333 O OD2 . ASP   B 29  ? 0.2618 0.2792 0.3656 0.0150  0.0102  -0.0143 35  ASP   C OD2 
1334 N N   . SER   B 30  ? 0.1353 0.1593 0.2673 0.0116  0.0182  0.0085  36  SER   C N   
1335 C CA  A SER   B 30  ? 0.1307 0.1561 0.2675 0.0110  0.0186  0.0130  36  SER   C CA  
1336 C CA  B SER   B 30  ? 0.1365 0.1620 0.2728 0.0110  0.0185  0.0131  36  SER   C CA  
1337 C C   . SER   B 30  ? 0.1407 0.1664 0.2760 0.0106  0.0166  0.0098  36  SER   C C   
1338 O O   . SER   B 30  ? 0.1319 0.1589 0.2644 0.0104  0.0163  0.0134  36  SER   C O   
1339 C CB  A SER   B 30  ? 0.1388 0.1637 0.2895 0.0111  0.0218  0.0152  36  SER   C CB  
1340 C CB  B SER   B 30  ? 0.1604 0.1857 0.3099 0.0112  0.0217  0.0162  36  SER   C CB  
1341 O OG  A SER   B 30  ? 0.1397 0.1655 0.2958 0.0108  0.0228  0.0188  36  SER   C OG  
1342 O OG  B SER   B 30  ? 0.1863 0.2094 0.3442 0.0111  0.0224  0.0103  36  SER   C OG  
1343 N N   . SER   B 31  ? 0.1393 0.1636 0.2766 0.0107  0.0150  0.0028  37  SER   C N   
1344 C CA  . SER   B 31  ? 0.1475 0.1726 0.2852 0.0104  0.0126  -0.0004 37  SER   C CA  
1345 C C   . SER   B 31  ? 0.1313 0.1572 0.2560 0.0108  0.0100  0.0004  37  SER   C C   
1346 O O   . SER   B 31  ? 0.1490 0.1762 0.2744 0.0107  0.0088  0.0002  37  SER   C O   
1347 C CB  . SER   B 31  ? 0.1905 0.2142 0.3321 0.0106  0.0103  -0.0084 37  SER   C CB  
1348 O OG  . SER   B 31  ? 0.2530 0.2752 0.3827 0.0118  0.0078  -0.0127 37  SER   C OG  
1349 N N   . ARG   B 32  ? 0.1295 0.1547 0.2434 0.0113  0.0096  0.0015  38  ARG   C N   
1350 C CA  . ARG   B 32  ? 0.1338 0.1591 0.2357 0.0117  0.0076  0.0025  38  ARG   C CA  
1351 C C   . ARG   B 32  ? 0.1301 0.1563 0.2286 0.0111  0.0088  0.0090  38  ARG   C C   
1352 O O   . ARG   B 32  ? 0.1261 0.1521 0.2155 0.0112  0.0074  0.0100  38  ARG   C O   
1353 C CB  . ARG   B 32  ? 0.1625 0.1859 0.2550 0.0126  0.0066  -0.0004 38  ARG   C CB  
1354 C CG  . ARG   B 32  ? 0.1816 0.2036 0.2735 0.0137  0.0045  -0.0073 38  ARG   C CG  
1355 C CD  . ARG   B 32  ? 0.1593 0.1790 0.2404 0.0152  0.0043  -0.0095 38  ARG   C CD  
1356 N NE  . ARG   B 32  ? 0.1577 0.1769 0.2276 0.0157  0.0028  -0.0076 38  ARG   C NE  
1357 C CZ  . ARG   B 32  ? 0.1729 0.1899 0.2321 0.0175  0.0015  -0.0102 38  ARG   C CZ  
1358 N NH1 . ARG   B 32  ? 0.1841 0.1991 0.2408 0.0190  0.0014  -0.0149 38  ARG   C NH1 
1359 N NH2 . ARG   B 32  ? 0.1721 0.1885 0.2228 0.0179  0.0003  -0.0080 38  ARG   C NH2 
1360 N N   . ASP   B 33  ? 0.1156 0.1426 0.2207 0.0107  0.0112  0.0132  39  ASP   C N   
1361 C CA  . ASP   B 33  ? 0.1183 0.1462 0.2195 0.0104  0.0116  0.0190  39  ASP   C CA  
1362 C C   . ASP   B 33  ? 0.1237 0.1513 0.2167 0.0102  0.0103  0.0191  39  ASP   C C   
1363 O O   . ASP   B 33  ? 0.1235 0.1514 0.2100 0.0097  0.0091  0.0220  39  ASP   C O   
1364 C CB  . ASP   B 33  ? 0.1146 0.1430 0.2125 0.0104  0.0113  0.0217  39  ASP   C CB  
1365 C CG  . ASP   B 33  ? 0.1361 0.1652 0.2297 0.0104  0.0113  0.0273  39  ASP   C CG  
1366 O OD1 . ASP   B 33  ? 0.1436 0.1736 0.2422 0.0105  0.0124  0.0306  39  ASP   C OD1 
1367 O OD2 . ASP   B 33  ? 0.1359 0.1646 0.2213 0.0105  0.0101  0.0283  39  ASP   C OD2 
1368 N N   . LEU   B 34  ? 0.1097 0.1363 0.2030 0.0105  0.0109  0.0162  40  LEU   C N   
1369 C CA  . LEU   B 34  ? 0.1168 0.1430 0.2036 0.0103  0.0106  0.0168  40  LEU   C CA  
1370 C C   . LEU   B 34  ? 0.1239 0.1509 0.2169 0.0104  0.0129  0.0183  40  LEU   C C   
1371 O O   . LEU   B 34  ? 0.1331 0.1596 0.2333 0.0110  0.0148  0.0165  40  LEU   C O   
1372 C CB  . LEU   B 34  ? 0.1250 0.1488 0.2039 0.0111  0.0098  0.0121  40  LEU   C CB  
1373 C CG  . LEU   B 34  ? 0.1385 0.1615 0.2097 0.0112  0.0073  0.0109  40  LEU   C CG  
1374 C CD1 . LEU   B 34  ? 0.1550 0.1757 0.2186 0.0126  0.0065  0.0068  40  LEU   C CD1 
1375 C CD2 . LEU   B 34  ? 0.1543 0.1775 0.2203 0.0102  0.0064  0.0148  40  LEU   C CD2 
1376 N N   . LEU   B 35  ? 0.1113 0.1392 0.2020 0.0097  0.0127  0.0213  41  LEU   C N   
1377 C CA  . LEU   B 35  ? 0.1162 0.1452 0.2130 0.0099  0.0150  0.0229  41  LEU   C CA  
1378 C C   . LEU   B 35  ? 0.1300 0.1588 0.2212 0.0093  0.0148  0.0235  41  LEU   C C   
1379 O O   . LEU   B 35  ? 0.1411 0.1700 0.2266 0.0082  0.0123  0.0250  41  LEU   C O   
1380 C CB  . LEU   B 35  ? 0.1127 0.1447 0.2181 0.0096  0.0147  0.0280  41  LEU   C CB  
1381 C CG  . LEU   B 35  ? 0.1212 0.1550 0.2351 0.0101  0.0170  0.0301  41  LEU   C CG  
1382 C CD1 . LEU   B 35  ? 0.1506 0.1861 0.2750 0.0109  0.0179  0.0334  41  LEU   C CD1 
1383 C CD2 . LEU   B 35  ? 0.1299 0.1660 0.2425 0.0089  0.0153  0.0332  41  LEU   C CD2 
1384 N N   . VAL   B 36  ? 0.1284 0.1563 0.2210 0.0101  0.0180  0.0223  42  VAL   C N   
1385 C CA  . VAL   B 36  ? 0.1316 0.1592 0.2210 0.0096  0.0192  0.0234  42  VAL   C CA  
1386 C C   . VAL   B 36  ? 0.1397 0.1699 0.2391 0.0096  0.0220  0.0263  42  VAL   C C   
1387 O O   . VAL   B 36  ? 0.1489 0.1790 0.2544 0.0110  0.0249  0.0251  42  VAL   C O   
1388 C CB  . VAL   B 36  ? 0.1490 0.1727 0.2293 0.0111  0.0214  0.0194  42  VAL   C CB  
1389 C CG1 . VAL   B 36  ? 0.1664 0.1893 0.2438 0.0108  0.0236  0.0213  42  VAL   C CG1 
1390 C CG2 . VAL   B 36  ? 0.1610 0.1826 0.2323 0.0113  0.0181  0.0166  42  VAL   C CG2 
1391 N N   . SER   B 37  ? 0.1316 0.1642 0.2340 0.0080  0.0207  0.0299  43  SER   C N   
1392 C CA  . SER   B 37  ? 0.1288 0.1647 0.2422 0.0078  0.0229  0.0331  43  SER   C CA  
1393 C C   . SER   B 37  ? 0.1464 0.1816 0.2584 0.0070  0.0252  0.0338  43  SER   C C   
1394 O O   . SER   B 37  ? 0.1529 0.1854 0.2556 0.0063  0.0242  0.0326  43  SER   C O   
1395 C CB  . SER   B 37  ? 0.1417 0.1820 0.2626 0.0066  0.0186  0.0372  43  SER   C CB  
1396 O OG  . SER   B 37  ? 0.1644 0.2050 0.2796 0.0046  0.0141  0.0382  43  SER   C OG  
1397 N N   . SER   B 38  ? 0.1476 0.1852 0.2697 0.0074  0.0289  0.0359  44  SER   C N   
1398 C CA  . SER   B 38  ? 0.1608 0.1981 0.2842 0.0066  0.0321  0.0373  44  SER   C CA  
1399 C C   . SER   B 38  ? 0.1847 0.2262 0.3158 0.0037  0.0279  0.0409  44  SER   C C   
1400 O O   . SER   B 38  ? 0.1886 0.2343 0.3274 0.0030  0.0237  0.0431  44  SER   C O   
1401 C CB  . SER   B 38  ? 0.1898 0.2273 0.3204 0.0086  0.0392  0.0377  44  SER   C CB  
1402 O OG  . SER   B 38  ? 0.2311 0.2735 0.3758 0.0087  0.0386  0.0403  44  SER   C OG  
1403 N N   . THR   B 39  ? 0.1848 0.2249 0.3138 0.0021  0.0288  0.0416  45  THR   C N   
1404 C CA  . THR   B 39  ? 0.1923 0.2356 0.3286 -0.0009 0.0245  0.0442  45  THR   C CA  
1405 C C   . THR   B 39  ? 0.2208 0.2657 0.3678 -0.0017 0.0297  0.0467  45  THR   C C   
1406 O O   . THR   B 39  ? 0.2102 0.2516 0.3536 0.0000  0.0365  0.0462  45  THR   C O   
1407 C CB  . THR   B 39  ? 0.2068 0.2464 0.3316 -0.0026 0.0206  0.0425  45  THR   C CB  
1408 O OG1 . THR   B 39  ? 0.2218 0.2564 0.3390 -0.0018 0.0258  0.0415  45  THR   C OG1 
1409 C CG2 . THR   B 39  ? 0.2036 0.2413 0.3175 -0.0017 0.0163  0.0401  45  THR   C CG2 
1410 N N   . THR   B 40  ? 0.2415 0.2912 0.4012 -0.0043 0.0261  0.0493  46  THR   C N   
1411 C CA  . THR   B 40  ? 0.2602 0.3120 0.4326 -0.0056 0.0307  0.0520  46  THR   C CA  
1412 C C   . THR   B 40  ? 0.2708 0.3180 0.4366 -0.0075 0.0315  0.0515  46  THR   C C   
1413 O O   . THR   B 40  ? 0.2918 0.3364 0.4586 -0.0069 0.0389  0.0527  46  THR   C O   
1414 C CB  . THR   B 40  ? 0.3037 0.3631 0.4941 -0.0075 0.0261  0.0549  46  THR   C CB  
1415 O OG1 . THR   B 40  ? 0.3582 0.4186 0.5454 -0.0101 0.0170  0.0540  46  THR   C OG1 
1416 C CG2 . THR   B 40  ? 0.2891 0.3526 0.4862 -0.0051 0.0261  0.0560  46  THR   C CG2 
1417 N N   . ALA   B 41  ? 0.2562 0.3019 0.4147 -0.0096 0.0244  0.0498  47  ALA   C N   
1418 C CA  . ALA   B 41  ? 0.2608 0.3016 0.4133 -0.0114 0.0248  0.0492  47  ALA   C CA  
1419 C C   . ALA   B 41  ? 0.2446 0.2785 0.3787 -0.0089 0.0274  0.0468  47  ALA   C C   
1420 O O   . ALA   B 41  ? 0.2336 0.2668 0.3588 -0.0068 0.0257  0.0446  47  ALA   C O   
1421 C CB  . ALA   B 41  ? 0.2771 0.3192 0.4310 -0.0147 0.0159  0.0481  47  ALA   C CB  
1422 N N   . GLN   B 42  ? 0.2459 0.2747 0.3750 -0.0092 0.0314  0.0473  48  GLN   C N   
1423 C CA  . GLN   B 42  ? 0.2605 0.2828 0.3724 -0.0067 0.0332  0.0453  48  GLN   C CA  
1424 C C   . GLN   B 42  ? 0.2574 0.2775 0.3610 -0.0081 0.0261  0.0428  48  GLN   C C   
1425 O O   . GLN   B 42  ? 0.2722 0.2929 0.3814 -0.0113 0.0219  0.0430  48  GLN   C O   
1426 C CB  . GLN   B 42  ? 0.3156 0.3329 0.4251 -0.0060 0.0404  0.0475  48  GLN   C CB  
1427 C CG  . GLN   B 42  ? 0.4230 0.4407 0.5353 -0.0033 0.0488  0.0494  48  GLN   C CG  
1428 C CD  . GLN   B 42  ? 0.5584 0.5703 0.6653 -0.0020 0.0561  0.0519  48  GLN   C CD  
1429 O OE1 . GLN   B 42  ? 0.5994 0.6113 0.7167 -0.0044 0.0589  0.0551  48  GLN   C OE1 
1430 N NE2 . GLN   B 42  ? 0.5968 0.6036 0.6875 0.0020  0.0592  0.0506  48  GLN   C NE2 
1431 N N   . GLY   B 43  ? 0.2315 0.2491 0.3220 -0.0056 0.0248  0.0402  49  GLY   C N   
1432 C CA  . GLY   B 43  ? 0.2265 0.2415 0.3077 -0.0061 0.0193  0.0378  49  GLY   C CA  
1433 C C   . GLY   B 43  ? 0.2232 0.2317 0.2945 -0.0052 0.0215  0.0376  49  GLY   C C   
1434 O O   . GLY   B 43  ? 0.2477 0.2534 0.3168 -0.0035 0.0275  0.0392  49  GLY   C O   
1435 N N   . CYS   B 44  ? 0.2162 0.2221 0.2812 -0.0059 0.0171  0.0357  50  CYS   C N   
1436 C CA  . CYS   B 44  ? 0.2334 0.2329 0.2901 -0.0052 0.0189  0.0359  50  CYS   C CA  
1437 C C   . CYS   B 44  ? 0.2369 0.2335 0.2810 -0.0025 0.0170  0.0334  50  CYS   C C   
1438 O O   . CYS   B 44  ? 0.2718 0.2631 0.3091 -0.0016 0.0179  0.0336  50  CYS   C O   
1439 C CB  . CYS   B 44  ? 0.2480 0.2456 0.3104 -0.0087 0.0163  0.0362  50  CYS   C CB  
1440 S SG  . CYS   B 44  ? 0.3390 0.3404 0.4191 -0.0122 0.0185  0.0392  50  CYS   C SG  
1441 N N   . ASP   B 45  ? 0.1999 0.1997 0.2414 -0.0011 0.0145  0.0313  51  ASP   C N   
1442 C CA  . ASP   B 45  ? 0.2021 0.1997 0.2334 0.0014  0.0126  0.0290  51  ASP   C CA  
1443 C C   . ASP   B 45  ? 0.2104 0.2057 0.2347 0.0049  0.0166  0.0290  51  ASP   C C   
1444 O O   . ASP   B 45  ? 0.2308 0.2274 0.2579 0.0057  0.0204  0.0301  51  ASP   C O   
1445 C CB  . ASP   B 45  ? 0.2044 0.2063 0.2369 0.0017  0.0092  0.0270  51  ASP   C CB  
1446 C CG  . ASP   B 45  ? 0.2544 0.2581 0.2903 -0.0008 0.0048  0.0266  51  ASP   C CG  
1447 O OD1 . ASP   B 45  ? 0.2646 0.2650 0.2983 -0.0022 0.0032  0.0264  51  ASP   C OD1 
1448 O OD2 . ASP   B 45  ? 0.2200 0.2280 0.2603 -0.0012 0.0030  0.0266  51  ASP   C OD2 
1449 N N   . THR   B 46  ? 0.1931 0.1847 0.2082 0.0071  0.0156  0.0279  52  THR   C N   
1450 C CA  . THR   B 46  ? 0.2005 0.1898 0.2070 0.0109  0.0178  0.0275  52  THR   C CA  
1451 C C   . THR   B 46  ? 0.1947 0.1863 0.1978 0.0128  0.0142  0.0239  52  THR   C C   
1452 O O   . THR   B 46  ? 0.2047 0.1966 0.2077 0.0121  0.0106  0.0227  52  THR   C O   
1453 C CB  . THR   B 46  ? 0.2353 0.2187 0.2345 0.0124  0.0190  0.0292  52  THR   C CB  
1454 O OG1 . THR   B 46  ? 0.2571 0.2383 0.2610 0.0105  0.0230  0.0327  52  THR   C OG1 
1455 C CG2 . THR   B 46  ? 0.2589 0.2398 0.2474 0.0169  0.0203  0.0287  52  THR   C CG2 
1456 N N   . ILE   B 47  ? 0.1956 0.1885 0.1965 0.0150  0.0152  0.0222  53  ILE   C N   
1457 C CA  . ILE   B 47  ? 0.1846 0.1797 0.1838 0.0166  0.0117  0.0186  53  ILE   C CA  
1458 C C   . ILE   B 47  ? 0.1799 0.1716 0.1692 0.0200  0.0103  0.0175  53  ILE   C C   
1459 O O   . ILE   B 47  ? 0.2054 0.1937 0.1874 0.0224  0.0129  0.0188  53  ILE   C O   
1460 C CB  . ILE   B 47  ? 0.1910 0.1886 0.1927 0.0176  0.0130  0.0165  53  ILE   C CB  
1461 C CG1 . ILE   B 47  ? 0.1979 0.1987 0.2097 0.0149  0.0151  0.0181  53  ILE   C CG1 
1462 C CG2 . ILE   B 47  ? 0.1991 0.1989 0.2010 0.0188  0.0093  0.0126  53  ILE   C CG2 
1463 C CD1 . ILE   B 47  ? 0.2249 0.2289 0.2437 0.0121  0.0117  0.0185  53  ILE   C CD1 
1464 N N   . ALA   B 48  ? 0.1698 0.1626 0.1589 0.0205  0.0064  0.0155  54  ALA   C N   
1465 C CA  . ALA   B 48  ? 0.1803 0.1708 0.1614 0.0239  0.0042  0.0144  54  ALA   C CA  
1466 C C   . ALA   B 48  ? 0.1765 0.1678 0.1533 0.0269  0.0034  0.0114  54  ALA   C C   
1467 O O   . ALA   B 48  ? 0.1809 0.1756 0.1633 0.0260  0.0029  0.0088  54  ALA   C O   
1468 C CB  . ALA   B 48  ? 0.1714 0.1638 0.1558 0.0237  0.0005  0.0128  54  ALA   C CB  
1469 N N   . ARG   B 49  ? 0.1737 0.1615 0.1402 0.0305  0.0032  0.0117  55  ARG   C N   
1470 C CA  . ARG   B 49  ? 0.1793 0.1673 0.1396 0.0339  0.0015  0.0082  55  ARG   C CA  
1471 C C   . ARG   B 49  ? 0.2052 0.1923 0.1597 0.0371  -0.0031 0.0072  55  ARG   C C   
1472 O O   . ARG   B 49  ? 0.2215 0.2043 0.1668 0.0398  -0.0023 0.0101  55  ARG   C O   
1473 C CB  . ARG   B 49  ? 0.1997 0.1840 0.1516 0.0358  0.0062  0.0098  55  ARG   C CB  
1474 C CG  . ARG   B 49  ? 0.1890 0.1746 0.1489 0.0325  0.0111  0.0114  55  ARG   C CG  
1475 C CD  . ARG   B 49  ? 0.2090 0.1989 0.1770 0.0311  0.0099  0.0074  55  ARG   C CD  
1476 N NE  . ARG   B 49  ? 0.2150 0.2060 0.1905 0.0284  0.0146  0.0096  55  ARG   C NE  
1477 C CZ  . ARG   B 49  ? 0.2140 0.2089 0.1999 0.0260  0.0143  0.0080  55  ARG   C CZ  
1478 N NH1 . ARG   B 49  ? 0.2037 0.2014 0.1935 0.0259  0.0101  0.0041  55  ARG   C NH1 
1479 N NH2 . ARG   B 49  ? 0.2117 0.2078 0.2048 0.0238  0.0183  0.0105  55  ARG   C NH2 
1480 N N   . CYS   B 50  ? 0.1926 0.1838 0.1539 0.0366  -0.0077 0.0037  56  CYS   C N   
1481 C CA  . CYS   B 50  ? 0.1980 0.1896 0.1577 0.0391  -0.0123 0.0030  56  CYS   C CA  
1482 C C   . CYS   B 50  ? 0.1954 0.1924 0.1648 0.0383  -0.0167 -0.0014 56  CYS   C C   
1483 O O   . CYS   B 50  ? 0.1911 0.1909 0.1683 0.0357  -0.0158 -0.0035 56  CYS   C O   
1484 C CB  . CYS   B 50  ? 0.2014 0.1910 0.1631 0.0376  -0.0106 0.0071  56  CYS   C CB  
1485 S SG  . CYS   B 50  ? 0.1869 0.1802 0.1618 0.0326  -0.0094 0.0069  56  CYS   C SG  
1486 N N   . ASP   B 51  ? 0.2055 0.2039 0.1758 0.0406  -0.0211 -0.0024 57  ASP   C N   
1487 C CA  . ASP   B 51  ? 0.2075 0.2112 0.1892 0.0397  -0.0248 -0.0060 57  ASP   C CA  
1488 C C   . ASP   B 51  ? 0.2043 0.2087 0.1919 0.0390  -0.0244 -0.0035 57  ASP   C C   
1489 O O   . ASP   B 51  ? 0.2098 0.2176 0.2045 0.0399  -0.0278 -0.0054 57  ASP   C O   
1490 C CB  . ASP   B 51  ? 0.2452 0.2509 0.2251 0.0431  -0.0310 -0.0105 57  ASP   C CB  
1491 C CG  . ASP   B 51  ? 0.2944 0.2982 0.2661 0.0474  -0.0343 -0.0090 57  ASP   C CG  
1492 O OD1 . ASP   B 51  ? 0.2738 0.2738 0.2406 0.0478  -0.0312 -0.0042 57  ASP   C OD1 
1493 O OD2 . ASP   B 51  ? 0.3593 0.3652 0.3298 0.0505  -0.0403 -0.0126 57  ASP   C OD2 
1494 N N   . CYS   B 52  ? 0.1859 0.1868 0.1709 0.0372  -0.0201 0.0006  58  CYS   C N   
1495 C CA  . CYS   B 52  ? 0.1789 0.1797 0.1687 0.0365  -0.0192 0.0025  58  CYS   C CA  
1496 C C   . CYS   B 52  ? 0.1680 0.1738 0.1698 0.0344  -0.0195 0.0004  58  CYS   C C   
1497 O O   . CYS   B 52  ? 0.1710 0.1793 0.1778 0.0321  -0.0186 -0.0011 58  CYS   C O   
1498 C CB  . CYS   B 52  ? 0.1946 0.1912 0.1811 0.0341  -0.0148 0.0061  58  CYS   C CB  
1499 S SG  . CYS   B 52  ? 0.1956 0.1853 0.1705 0.0364  -0.0133 0.0098  58  CYS   C SG  
1500 N N   . GLN   B 53  ? 0.1643 0.1713 0.1707 0.0355  -0.0204 0.0006  59  GLN   C N   
1501 C CA  . GLN   B 53  ? 0.1662 0.1772 0.1837 0.0339  -0.0194 -0.0003 59  GLN   C CA  
1502 C C   . GLN   B 53  ? 0.1548 0.1633 0.1720 0.0333  -0.0161 0.0023  59  GLN   C C   
1503 O O   . GLN   B 53  ? 0.1549 0.1659 0.1798 0.0330  -0.0148 0.0021  59  GLN   C O   
1504 C CB  . GLN   B 53  ? 0.1704 0.1864 0.1970 0.0359  -0.0233 -0.0033 59  GLN   C CB  
1505 C CG  . GLN   B 53  ? 0.2224 0.2416 0.2524 0.0356  -0.0264 -0.0070 59  GLN   C CG  
1506 C CD  . GLN   B 53  ? 0.2516 0.2762 0.2931 0.0369  -0.0305 -0.0104 59  GLN   C CD  
1507 O OE1 . GLN   B 53  ? 0.2714 0.2970 0.3107 0.0397  -0.0358 -0.0130 59  GLN   C OE1 
1508 N NE2 . GLN   B 53  ? 0.2116 0.2396 0.2655 0.0352  -0.0281 -0.0101 59  GLN   C NE2 
1509 N N   . THR   B 54  ? 0.1607 0.1639 0.1690 0.0333  -0.0145 0.0047  60  THR   C N   
1510 C CA  . THR   B 54  ? 0.1681 0.1680 0.1751 0.0322  -0.0114 0.0065  60  THR   C CA  
1511 C C   . THR   B 54  ? 0.1669 0.1629 0.1678 0.0295  -0.0092 0.0083  60  THR   C C   
1512 O O   . THR   B 54  ? 0.1827 0.1769 0.1786 0.0295  -0.0096 0.0090  60  THR   C O   
1513 C CB  . THR   B 54  ? 0.2137 0.2104 0.2183 0.0352  -0.0117 0.0074  60  THR   C CB  
1514 O OG1 . THR   B 54  ? 0.2635 0.2560 0.2601 0.0366  -0.0127 0.0088  60  THR   C OG1 
1515 C CG2 . THR   B 54  ? 0.2141 0.2152 0.2263 0.0381  -0.0142 0.0058  60  THR   C CG2 
1516 N N   . GLY   B 55  ? 0.1526 0.1477 0.1543 0.0272  -0.0069 0.0089  61  GLY   C N   
1517 C CA  . GLY   B 55  ? 0.1601 0.1523 0.1577 0.0244  -0.0054 0.0103  61  GLY   C CA  
1518 C C   . GLY   B 55  ? 0.1510 0.1419 0.1486 0.0227  -0.0038 0.0104  61  GLY   C C   
1519 O O   . GLY   B 55  ? 0.1618 0.1524 0.1604 0.0242  -0.0030 0.0098  61  GLY   C O   
1520 N N   . VAL   B 56  ? 0.1426 0.1325 0.1385 0.0199  -0.0033 0.0113  62  VAL   C N   
1521 C CA  . VAL   B 56  ? 0.1288 0.1173 0.1231 0.0183  -0.0025 0.0113  62  VAL   C CA  
1522 C C   . VAL   B 56  ? 0.1345 0.1266 0.1317 0.0160  -0.0026 0.0121  62  VAL   C C   
1523 O O   . VAL   B 56  ? 0.1568 0.1499 0.1553 0.0146  -0.0032 0.0129  62  VAL   C O   
1524 C CB  . VAL   B 56  ? 0.1502 0.1327 0.1393 0.0171  -0.0026 0.0113  62  VAL   C CB  
1525 C CG1 . VAL   B 56  ? 0.1723 0.1529 0.1586 0.0153  -0.0027 0.0107  62  VAL   C CG1 
1526 C CG2 . VAL   B 56  ? 0.1671 0.1453 0.1536 0.0198  -0.0021 0.0108  62  VAL   C CG2 
1527 N N   . TYR   B 57  ? 0.1353 0.1291 0.1332 0.0157  -0.0018 0.0123  63  TYR   C N   
1528 C CA  . TYR   B 57  ? 0.1235 0.1206 0.1241 0.0138  -0.0021 0.0137  63  TYR   C CA  
1529 C C   . TYR   B 57  ? 0.1389 0.1338 0.1345 0.0126  -0.0026 0.0140  63  TYR   C C   
1530 O O   . TYR   B 57  ? 0.1573 0.1493 0.1482 0.0139  -0.0017 0.0131  63  TYR   C O   
1531 C CB  . TYR   B 57  ? 0.1309 0.1329 0.1383 0.0147  -0.0008 0.0143  63  TYR   C CB  
1532 C CG  . TYR   B 57  ? 0.1388 0.1414 0.1461 0.0159  0.0013  0.0149  63  TYR   C CG  
1533 C CD1 . TYR   B 57  ? 0.1517 0.1532 0.1590 0.0182  0.0028  0.0139  63  TYR   C CD1 
1534 C CD2 . TYR   B 57  ? 0.1494 0.1537 0.1571 0.0152  0.0021  0.0170  63  TYR   C CD2 
1535 C CE1 . TYR   B 57  ? 0.1607 0.1628 0.1686 0.0196  0.0058  0.0148  63  TYR   C CE1 
1536 C CE2 . TYR   B 57  ? 0.1557 0.1603 0.1628 0.0168  0.0048  0.0182  63  TYR   C CE2 
1537 C CZ  . TYR   B 57  ? 0.1575 0.1610 0.1648 0.0189  0.0070  0.0170  63  TYR   C CZ  
1538 O OH  . TYR   B 57  ? 0.1782 0.1818 0.1855 0.0207  0.0108  0.0185  63  TYR   C OH  
1539 N N   . TYR   B 58  ? 0.1369 0.1338 0.1340 0.0106  -0.0039 0.0153  64  TYR   C N   
1540 C CA  . TYR   B 58  ? 0.1456 0.1412 0.1379 0.0096  -0.0054 0.0157  64  TYR   C CA  
1541 C C   . TYR   B 58  ? 0.1542 0.1529 0.1473 0.0108  -0.0040 0.0176  64  TYR   C C   
1542 O O   . TYR   B 58  ? 0.1507 0.1537 0.1504 0.0105  -0.0034 0.0195  64  TYR   C O   
1543 C CB  . TYR   B 58  ? 0.1506 0.1467 0.1445 0.0068  -0.0082 0.0163  64  TYR   C CB  
1544 C CG  . TYR   B 58  ? 0.1679 0.1626 0.1564 0.0060  -0.0108 0.0160  64  TYR   C CG  
1545 C CD1 . TYR   B 58  ? 0.1899 0.1793 0.1704 0.0064  -0.0116 0.0135  64  TYR   C CD1 
1546 C CD2 . TYR   B 58  ? 0.1684 0.1668 0.1591 0.0051  -0.0128 0.0181  64  TYR   C CD2 
1547 C CE1 . TYR   B 58  ? 0.1920 0.1798 0.1661 0.0059  -0.0144 0.0126  64  TYR   C CE1 
1548 C CE2 . TYR   B 58  ? 0.1786 0.1757 0.1631 0.0047  -0.0159 0.0178  64  TYR   C CE2 
1549 C CZ  . TYR   B 58  ? 0.1964 0.1881 0.1723 0.0050  -0.0169 0.0147  64  TYR   C CZ  
1550 O OH  . TYR   B 58  ? 0.2370 0.2270 0.2052 0.0049  -0.0205 0.0137  64  TYR   C OH  
1551 N N   . CYS   B 59  ? 0.1533 0.1494 0.1393 0.0121  -0.0032 0.0172  65  CYS   C N   
1552 C CA  . CYS   B 59  ? 0.1646 0.1626 0.1494 0.0137  -0.0012 0.0196  65  CYS   C CA  
1553 C C   . CYS   B 59  ? 0.1801 0.1765 0.1568 0.0131  -0.0041 0.0201  65  CYS   C C   
1554 O O   . CYS   B 59  ? 0.1905 0.1823 0.1580 0.0138  -0.0047 0.0179  65  CYS   C O   
1555 C CB  . CYS   B 59  ? 0.1746 0.1709 0.1573 0.0164  0.0028  0.0190  65  CYS   C CB  
1556 S SG  . CYS   B 59  ? 0.1931 0.1907 0.1733 0.0188  0.0067  0.0224  65  CYS   C SG  
1557 N N   . SER   B 60  ? 0.1726 0.1726 0.1529 0.0120  -0.0062 0.0226  66  SER   C N   
1558 C CA  . SER   B 60  ? 0.1869 0.1860 0.1603 0.0114  -0.0101 0.0230  66  SER   C CA  
1559 C C   . SER   B 60  ? 0.1931 0.1898 0.1561 0.0141  -0.0086 0.0238  66  SER   C C   
1560 O O   . SER   B 60  ? 0.2222 0.2155 0.1754 0.0141  -0.0119 0.0219  66  SER   C O   
1561 C CB  . SER   B 60  ? 0.2127 0.2166 0.1932 0.0100  -0.0125 0.0260  66  SER   C CB  
1562 O OG  . SER   B 60  ? 0.2692 0.2726 0.2433 0.0096  -0.0172 0.0261  66  SER   C OG  
1563 N N   . SER   B 61  ? 0.1863 0.1844 0.1511 0.0165  -0.0035 0.0266  67  SER   C N   
1564 C CA  . SER   B 61  ? 0.1939 0.1895 0.1486 0.0196  -0.0008 0.0281  67  SER   C CA  
1565 C C   . SER   B 61  ? 0.2309 0.2209 0.1759 0.0210  0.0008  0.0244  67  SER   C C   
1566 O O   . SER   B 61  ? 0.2604 0.2473 0.1944 0.0237  0.0028  0.0250  67  SER   C O   
1567 C CB  . SER   B 61  ? 0.2001 0.1986 0.1612 0.0216  0.0050  0.0324  67  SER   C CB  
1568 O OG  . SER   B 61  ? 0.2165 0.2157 0.1860 0.0218  0.0089  0.0311  67  SER   C OG  
1569 N N   . ARG   B 62  ? 0.2143 0.2025 0.1628 0.0197  0.0004  0.0207  68  ARG   C N   
1570 C CA  . ARG   B 62  ? 0.2174 0.1997 0.1575 0.0209  0.0015  0.0169  68  ARG   C CA  
1571 C C   . ARG   B 62  ? 0.2224 0.2011 0.1592 0.0183  -0.0040 0.0127  68  ARG   C C   
1572 O O   . ARG   B 62  ? 0.2434 0.2166 0.1740 0.0190  -0.0035 0.0090  68  ARG   C O   
1573 C CB  . ARG   B 62  ? 0.2195 0.2020 0.1666 0.0222  0.0063  0.0163  68  ARG   C CB  
1574 C CG  . ARG   B 62  ? 0.2724 0.2582 0.2245 0.0247  0.0121  0.0200  68  ARG   C CG  
1575 C CD  . ARG   B 62  ? 0.2746 0.2564 0.2156 0.0280  0.0161  0.0203  68  ARG   C CD  
1576 N NE  . ARG   B 62  ? 0.3156 0.3003 0.2620 0.0305  0.0226  0.0244  68  ARG   C NE  
1577 C CZ  . ARG   B 62  ? 0.3728 0.3599 0.3191 0.0313  0.0243  0.0289  68  ARG   C CZ  
1578 N NH1 . ARG   B 62  ? 0.3774 0.3648 0.3177 0.0301  0.0195  0.0300  68  ARG   C NH1 
1579 N NH2 . ARG   B 62  ? 0.3864 0.3755 0.3386 0.0336  0.0309  0.0326  68  ARG   C NH2 
1580 N N   . ARG   B 63  ? 0.2264 0.2083 0.1692 0.0152  -0.0086 0.0133  69  ARG   C N   
1581 C CA  . ARG   B 63  ? 0.2431 0.2224 0.1867 0.0121  -0.0134 0.0099  69  ARG   C CA  
1582 C C   . ARG   B 63  ? 0.2547 0.2303 0.2007 0.0122  -0.0110 0.0073  69  ARG   C C   
1583 O O   . ARG   B 63  ? 0.2855 0.2554 0.2263 0.0115  -0.0126 0.0036  69  ARG   C O   
1584 C CB  . ARG   B 63  ? 0.2547 0.2298 0.1871 0.0119  -0.0178 0.0069  69  ARG   C CB  
1585 C CG  . ARG   B 63  ? 0.3028 0.2813 0.2323 0.0118  -0.0216 0.0094  69  ARG   C CG  
1586 C CD  . ARG   B 63  ? 0.3656 0.3491 0.3059 0.0085  -0.0259 0.0108  69  ARG   C CD  
1587 N NE  . ARG   B 63  ? 0.3883 0.3740 0.3244 0.0084  -0.0312 0.0120  69  ARG   C NE  
1588 C CZ  . ARG   B 63  ? 0.3934 0.3840 0.3314 0.0099  -0.0306 0.0168  69  ARG   C CZ  
1589 N NH1 . ARG   B 63  ? 0.3685 0.3619 0.3127 0.0114  -0.0248 0.0205  69  ARG   C NH1 
1590 N NH2 . ARG   B 63  ? 0.4029 0.3953 0.3369 0.0101  -0.0361 0.0180  69  ARG   C NH2 
1591 N N   . LYS   B 64  ? 0.2270 0.2056 0.1806 0.0132  -0.0072 0.0093  70  LYS   C N   
1592 C CA  . LYS   B 64  ? 0.2270 0.2026 0.1826 0.0140  -0.0050 0.0074  70  LYS   C CA  
1593 C C   . LYS   B 64  ? 0.2095 0.1892 0.1753 0.0134  -0.0042 0.0092  70  LYS   C C   
1594 O O   . LYS   B 64  ? 0.2043 0.1892 0.1759 0.0135  -0.0034 0.0118  70  LYS   C O   
1595 C CB  . LYS   B 64  ? 0.2771 0.2511 0.2289 0.0176  -0.0003 0.0072  70  LYS   C CB  
1596 C CG  . LYS   B 64  ? 0.4087 0.3760 0.3490 0.0189  -0.0001 0.0040  70  LYS   C CG  
1597 C CD  . LYS   B 64  ? 0.5040 0.4690 0.4425 0.0225  0.0053  0.0035  70  LYS   C CD  
1598 C CE  . LYS   B 64  ? 0.5743 0.5323 0.5003 0.0242  0.0060  0.0001  70  LYS   C CE  
1599 N NZ  . LYS   B 64  ? 0.6273 0.5850 0.5441 0.0237  0.0033  0.0002  70  LYS   C NZ  
1600 N N   . HIS   B 65  ? 0.1986 0.1753 0.1661 0.0130  -0.0043 0.0077  71  HIS   C N   
1601 C CA  . HIS   B 65  ? 0.1976 0.1771 0.1725 0.0133  -0.0034 0.0089  71  HIS   C CA  
1602 C C   . HIS   B 65  ? 0.2172 0.1957 0.1924 0.0164  -0.0004 0.0084  71  HIS   C C   
1603 O O   . HIS   B 65  ? 0.2530 0.2263 0.2236 0.0177  0.0005  0.0065  71  HIS   C O   
1604 C CB  . HIS   B 65  ? 0.1994 0.1757 0.1755 0.0113  -0.0052 0.0083  71  HIS   C CB  
1605 C CG  . HIS   B 65  ? 0.1944 0.1725 0.1728 0.0081  -0.0079 0.0091  71  HIS   C CG  
1606 N ND1 . HIS   B 65  ? 0.2271 0.2094 0.2120 0.0070  -0.0080 0.0112  71  HIS   C ND1 
1607 C CD2 . HIS   B 65  ? 0.1941 0.1702 0.1694 0.0060  -0.0107 0.0079  71  HIS   C CD2 
1608 C CE1 . HIS   B 65  ? 0.2037 0.1866 0.1903 0.0043  -0.0105 0.0115  71  HIS   C CE1 
1609 N NE2 . HIS   B 65  ? 0.2226 0.2021 0.2039 0.0035  -0.0126 0.0095  71  HIS   C NE2 
1610 N N   . TYR   B 66  ? 0.1867 0.1702 0.1685 0.0178  0.0011  0.0098  72  TYR   C N   
1611 C CA  . TYR   B 66  ? 0.1751 0.1588 0.1593 0.0208  0.0036  0.0094  72  TYR   C CA  
1612 C C   . TYR   B 66  ? 0.1661 0.1517 0.1559 0.0216  0.0026  0.0095  72  TYR   C C   
1613 O O   . TYR   B 66  ? 0.1674 0.1569 0.1616 0.0205  0.0013  0.0103  72  TYR   C O   
1614 C CB  . TYR   B 66  ? 0.1822 0.1706 0.1709 0.0220  0.0062  0.0108  72  TYR   C CB  
1615 C CG  . TYR   B 66  ? 0.1910 0.1776 0.1733 0.0225  0.0083  0.0113  72  TYR   C CG  
1616 C CD1 . TYR   B 66  ? 0.2215 0.2044 0.1992 0.0250  0.0113  0.0101  72  TYR   C CD1 
1617 C CD2 . TYR   B 66  ? 0.1964 0.1851 0.1773 0.0211  0.0076  0.0131  72  TYR   C CD2 
1618 C CE1 . TYR   B 66  ? 0.2358 0.2165 0.2059 0.0259  0.0136  0.0105  72  TYR   C CE1 
1619 C CE2 . TYR   B 66  ? 0.2085 0.1955 0.1822 0.0221  0.0095  0.0139  72  TYR   C CE2 
1620 C CZ  . TYR   B 66  ? 0.2200 0.2029 0.1878 0.0246  0.0126  0.0125  72  TYR   C CZ  
1621 O OH  . TYR   B 66  ? 0.2614 0.2421 0.2202 0.0260  0.0145  0.0132  72  TYR   C OH  
1622 N N   . PRO   B 67  ? 0.1701 0.1527 0.1593 0.0238  0.0031  0.0085  73  PRO   C N   
1623 C CA  . PRO   B 67  ? 0.1557 0.1405 0.1496 0.0253  0.0018  0.0088  73  PRO   C CA  
1624 C C   . PRO   B 67  ? 0.1695 0.1603 0.1716 0.0269  0.0025  0.0088  73  PRO   C C   
1625 O O   . PRO   B 67  ? 0.1901 0.1815 0.1942 0.0284  0.0052  0.0087  73  PRO   C O   
1626 C CB  . PRO   B 67  ? 0.1949 0.1745 0.1859 0.0276  0.0022  0.0081  73  PRO   C CB  
1627 C CG  . PRO   B 67  ? 0.2320 0.2079 0.2188 0.0279  0.0046  0.0070  73  PRO   C CG  
1628 C CD  . PRO   B 67  ? 0.1936 0.1708 0.1778 0.0254  0.0049  0.0072  73  PRO   C CD  
1629 N N   . VAL   B 68  ? 0.1531 0.1481 0.1601 0.0267  0.0005  0.0089  74  VAL   C N   
1630 C CA  . VAL   B 68  ? 0.1582 0.1589 0.1744 0.0277  0.0007  0.0085  74  VAL   C CA  
1631 C C   . VAL   B 68  ? 0.1501 0.1534 0.1701 0.0291  -0.0025 0.0074  74  VAL   C C   
1632 O O   . VAL   B 68  ? 0.1543 0.1558 0.1694 0.0287  -0.0047 0.0074  74  VAL   C O   
1633 C CB  . VAL   B 68  ? 0.1733 0.1775 0.1931 0.0253  0.0017  0.0093  74  VAL   C CB  
1634 C CG1 . VAL   B 68  ? 0.1933 0.1962 0.2105 0.0248  0.0050  0.0107  74  VAL   C CG1 
1635 C CG2 . VAL   B 68  ? 0.1845 0.1883 0.2011 0.0231  -0.0004 0.0096  74  VAL   C CG2 
1636 N N   . SER   B 69  ? 0.1449 0.1529 0.1743 0.0307  -0.0030 0.0064  75  SER   C N   
1637 C CA  . SER   B 69  ? 0.1445 0.1564 0.1794 0.0318  -0.0068 0.0046  75  SER   C CA  
1638 C C   . SER   B 69  ? 0.1453 0.1612 0.1870 0.0295  -0.0064 0.0040  75  SER   C C   
1639 O O   . SER   B 69  ? 0.1503 0.1677 0.1967 0.0283  -0.0030 0.0051  75  SER   C O   
1640 C CB  . SER   B 69  ? 0.1729 0.1879 0.2164 0.0346  -0.0077 0.0035  75  SER   C CB  
1641 O OG  . SER   B 69  ? 0.2490 0.2601 0.2869 0.0370  -0.0078 0.0043  75  SER   C OG  
1642 N N   . PHE   B 70  ? 0.1320 0.1491 0.1732 0.0289  -0.0093 0.0024  76  PHE   C N   
1643 C CA  . PHE   B 70  ? 0.1275 0.1478 0.1753 0.0268  -0.0089 0.0016  76  PHE   C CA  
1644 C C   . PHE   B 70  ? 0.1353 0.1589 0.1885 0.0277  -0.0130 -0.0018 76  PHE   C C   
1645 O O   . PHE   B 70  ? 0.1386 0.1612 0.1866 0.0297  -0.0166 -0.0033 76  PHE   C O   
1646 C CB  . PHE   B 70  ? 0.1417 0.1594 0.1828 0.0243  -0.0072 0.0033  76  PHE   C CB  
1647 C CG  . PHE   B 70  ? 0.1342 0.1485 0.1655 0.0247  -0.0090 0.0032  76  PHE   C CG  
1648 C CD1 . PHE   B 70  ? 0.1354 0.1452 0.1582 0.0250  -0.0082 0.0050  76  PHE   C CD1 
1649 C CD2 . PHE   B 70  ? 0.1483 0.1633 0.1788 0.0248  -0.0111 0.0013  76  PHE   C CD2 
1650 C CE1 . PHE   B 70  ? 0.1459 0.1524 0.1607 0.0253  -0.0091 0.0055  76  PHE   C CE1 
1651 C CE2 . PHE   B 70  ? 0.1529 0.1644 0.1741 0.0253  -0.0117 0.0018  76  PHE   C CE2 
1652 C CZ  . PHE   B 70  ? 0.1543 0.1618 0.1681 0.0257  -0.0107 0.0042  76  PHE   C CZ  
1653 N N   . SER   B 71  ? 0.1215 0.1486 0.1851 0.0263  -0.0126 -0.0032 77  SER   C N   
1654 C CA  . SER   B 71  ? 0.1327 0.1632 0.2035 0.0269  -0.0169 -0.0074 77  SER   C CA  
1655 C C   . SER   B 71  ? 0.1498 0.1784 0.2133 0.0266  -0.0190 -0.0093 77  SER   C C   
1656 O O   . SER   B 71  ? 0.1748 0.2001 0.2296 0.0255  -0.0167 -0.0071 77  SER   C O   
1657 C CB  . SER   B 71  ? 0.1411 0.1758 0.2275 0.0255  -0.0153 -0.0082 77  SER   C CB  
1658 O OG  . SER   B 71  ? 0.1632 0.1971 0.2509 0.0230  -0.0116 -0.0063 77  SER   C OG  
1659 N N   . LYS   B 72  ? 0.1684 0.1990 0.2355 0.0276  -0.0236 -0.0138 78  LYS   C N   
1660 C CA  . LYS   B 72  ? 0.1748 0.2033 0.2341 0.0278  -0.0254 -0.0162 78  LYS   C CA  
1661 C C   . LYS   B 72  ? 0.1763 0.2053 0.2422 0.0250  -0.0222 -0.0165 78  LYS   C C   
1662 O O   . LYS   B 72  ? 0.1851 0.2170 0.2639 0.0234  -0.0208 -0.0166 78  LYS   C O   
1663 C CB  . LYS   B 72  ? 0.2454 0.2758 0.3059 0.0301  -0.0318 -0.0216 78  LYS   C CB  
1664 C CG  . LYS   B 72  ? 0.3093 0.3392 0.3631 0.0334  -0.0352 -0.0209 78  LYS   C CG  
1665 C CD  . LYS   B 72  ? 0.4519 0.4810 0.4971 0.0365  -0.0413 -0.0249 78  LYS   C CD  
1666 C CE  . LYS   B 72  ? 0.5401 0.5670 0.5744 0.0401  -0.0435 -0.0226 78  LYS   C CE  
1667 N NZ  . LYS   B 72  ? 0.5969 0.6225 0.6210 0.0436  -0.0493 -0.0261 78  LYS   C NZ  
1668 N N   . PRO   B 73  ? 0.1700 0.1961 0.2282 0.0245  -0.0208 -0.0164 79  PRO   C N   
1669 C CA  . PRO   B 73  ? 0.1634 0.1898 0.2285 0.0221  -0.0177 -0.0163 79  PRO   C CA  
1670 C C   . PRO   B 73  ? 0.1680 0.1972 0.2454 0.0216  -0.0201 -0.0212 79  PRO   C C   
1671 O O   . PRO   B 73  ? 0.1996 0.2288 0.2750 0.0233  -0.0248 -0.0263 79  PRO   C O   
1672 C CB  . PRO   B 73  ? 0.1930 0.2159 0.2474 0.0225  -0.0166 -0.0164 79  PRO   C CB  
1673 C CG  . PRO   B 73  ? 0.2252 0.2456 0.2670 0.0244  -0.0176 -0.0145 79  PRO   C CG  
1674 C CD  . PRO   B 73  ? 0.1910 0.2132 0.2345 0.0262  -0.0214 -0.0158 79  PRO   C CD  
1675 N N   . SER   B 74  ? 0.1426 0.1739 0.2328 0.0195  -0.0171 -0.0197 80  SER   C N   
1676 C CA  . SER   B 74  ? 0.1507 0.1846 0.2554 0.0187  -0.0191 -0.0241 80  SER   C CA  
1677 C C   . SER   B 74  ? 0.1456 0.1798 0.2613 0.0163  -0.0142 -0.0217 80  SER   C C   
1678 O O   . SER   B 74  ? 0.1439 0.1767 0.2556 0.0155  -0.0099 -0.0164 80  SER   C O   
1679 C CB  . SER   B 74  ? 0.1914 0.2290 0.3049 0.0193  -0.0212 -0.0246 80  SER   C CB  
1680 O OG  . SER   B 74  ? 0.2567 0.2943 0.3610 0.0218  -0.0254 -0.0257 80  SER   C OG  
1681 N N   . LEU   B 75  ? 0.1507 0.1868 0.2811 0.0152  -0.0152 -0.0255 81  LEU   C N   
1682 C CA  . LEU   B 75  ? 0.1659 0.2022 0.3092 0.0131  -0.0107 -0.0233 81  LEU   C CA  
1683 C C   . LEU   B 75  ? 0.1646 0.2039 0.3190 0.0124  -0.0079 -0.0194 81  LEU   C C   
1684 O O   . LEU   B 75  ? 0.1875 0.2298 0.3522 0.0125  -0.0106 -0.0226 81  LEU   C O   
1685 C CB  . LEU   B 75  ? 0.1836 0.2196 0.3376 0.0123  -0.0133 -0.0301 81  LEU   C CB  
1686 C CG  . LEU   B 75  ? 0.2148 0.2502 0.3826 0.0102  -0.0088 -0.0285 81  LEU   C CG  
1687 C CD1 . LEU   B 75  ? 0.2117 0.2439 0.3707 0.0103  -0.0047 -0.0245 81  LEU   C CD1 
1688 C CD2 . LEU   B 75  ? 0.2354 0.2705 0.4152 0.0094  -0.0123 -0.0365 81  LEU   C CD2 
1689 N N   . ILE   B 76  ? 0.1728 0.2113 0.3238 0.0122  -0.0026 -0.0125 82  ILE   C N   
1690 C CA  . ILE   B 76  ? 0.1864 0.2269 0.3437 0.0122  0.0011  -0.0079 82  ILE   C CA  
1691 C C   . ILE   B 76  ? 0.1829 0.2230 0.3499 0.0109  0.0071  -0.0031 82  ILE   C C   
1692 O O   . ILE   B 76  ? 0.1676 0.2053 0.3286 0.0105  0.0091  -0.0002 82  ILE   C O   
1693 C CB  . ILE   B 76  ? 0.2195 0.2586 0.3611 0.0136  0.0021  -0.0038 82  ILE   C CB  
1694 C CG1 . ILE   B 76  ? 0.2493 0.2882 0.3808 0.0152  -0.0032 -0.0074 82  ILE   C CG1 
1695 C CG2 . ILE   B 76  ? 0.2387 0.2788 0.3840 0.0139  0.0070  0.0015  82  ILE   C CG2 
1696 C CD1 . ILE   B 76  ? 0.2741 0.3164 0.4143 0.0162  -0.0056 -0.0100 82  ILE   C CD1 
1697 N N   . PHE   B 77  ? 0.1827 0.2250 0.3645 0.0104  0.0103  -0.0014 83  PHE   C N   
1698 C CA  . PHE   B 77  ? 0.1858 0.2273 0.3761 0.0096  0.0167  0.0043  83  PHE   C CA  
1699 C C   . PHE   B 77  ? 0.1942 0.2345 0.3719 0.0110  0.0207  0.0112  83  PHE   C C   
1700 O O   . PHE   B 77  ? 0.2183 0.2597 0.3918 0.0122  0.0210  0.0120  83  PHE   C O   
1701 C CB  . PHE   B 77  ? 0.1867 0.2308 0.3980 0.0086  0.0195  0.0040  83  PHE   C CB  
1702 C CG  . PHE   B 77  ? 0.1971 0.2397 0.4184 0.0078  0.0261  0.0097  83  PHE   C CG  
1703 C CD1 . PHE   B 77  ? 0.2104 0.2511 0.4381 0.0065  0.0259  0.0079  83  PHE   C CD1 
1704 C CD2 . PHE   B 77  ? 0.2159 0.2585 0.4386 0.0088  0.0330  0.0171  83  PHE   C CD2 
1705 C CE1 . PHE   B 77  ? 0.2281 0.2670 0.4645 0.0061  0.0321  0.0138  83  PHE   C CE1 
1706 C CE2 . PHE   B 77  ? 0.2188 0.2596 0.4491 0.0085  0.0393  0.0231  83  PHE   C CE2 
1707 C CZ  . PHE   B 77  ? 0.2234 0.2625 0.4612 0.0071  0.0387  0.0215  83  PHE   C CZ  
1708 N N   . VAL   B 78  ? 0.1699 0.2077 0.3414 0.0110  0.0236  0.0160  84  VAL   C N   
1709 C CA  . VAL   B 78  ? 0.1744 0.2108 0.3328 0.0123  0.0266  0.0221  84  VAL   C CA  
1710 C C   . VAL   B 78  ? 0.1694 0.2051 0.3349 0.0127  0.0331  0.0288  84  VAL   C C   
1711 O O   . VAL   B 78  ? 0.1654 0.2004 0.3395 0.0118  0.0345  0.0298  84  VAL   C O   
1712 C CB  . VAL   B 78  ? 0.1865 0.2208 0.3309 0.0123  0.0235  0.0220  84  VAL   C CB  
1713 C CG1 . VAL   B 78  ? 0.2094 0.2422 0.3401 0.0135  0.0253  0.0275  84  VAL   C CG1 
1714 C CG2 . VAL   B 78  ? 0.1940 0.2285 0.3317 0.0121  0.0176  0.0157  84  VAL   C CG2 
1715 N N   . GLU   B 79  ? 0.1640 0.1995 0.3256 0.0143  0.0375  0.0336  85  GLU   C N   
1716 C CA  . GLU   B 79  ? 0.1658 0.2000 0.3315 0.0152  0.0442  0.0409  85  GLU   C CA  
1717 C C   . GLU   B 79  ? 0.1703 0.2023 0.3254 0.0158  0.0440  0.0453  85  GLU   C C   
1718 O O   . GLU   B 79  ? 0.1643 0.1957 0.3075 0.0155  0.0391  0.0430  85  GLU   C O   
1719 C CB  . GLU   B 79  ? 0.2001 0.2342 0.3616 0.0173  0.0492  0.0449  85  GLU   C CB  
1720 C CG  . GLU   B 79  ? 0.2545 0.2915 0.4309 0.0169  0.0508  0.0420  85  GLU   C CG  
1721 C CD  . GLU   B 79  ? 0.3642 0.4027 0.5626 0.0153  0.0540  0.0423  85  GLU   C CD  
1722 O OE1 . GLU   B 79  ? 0.4124 0.4490 0.6147 0.0157  0.0592  0.0482  85  GLU   C OE1 
1723 O OE2 . GLU   B 79  ? 0.3893 0.4305 0.6012 0.0138  0.0509  0.0365  85  GLU   C OE2 
1724 N N   . ALA   B 80  ? 0.1757 0.2066 0.3369 0.0165  0.0493  0.0516  86  ALA   C N   
1725 C CA  . ALA   B 80  ? 0.1867 0.2158 0.3397 0.0174  0.0492  0.0564  86  ALA   C CA  
1726 C C   . ALA   B 80  ? 0.2045 0.2325 0.3372 0.0190  0.0470  0.0583  86  ALA   C C   
1727 O O   . ALA   B 80  ? 0.2254 0.2529 0.3512 0.0204  0.0490  0.0591  86  ALA   C O   
1728 C CB  . ALA   B 80  ? 0.1917 0.2194 0.3534 0.0187  0.0562  0.0641  86  ALA   C CB  
1729 N N   . SER   B 81  ? 0.1930 0.2207 0.3174 0.0188  0.0426  0.0581  87  SER   C N   
1730 C CA  . SER   B 81  ? 0.2114 0.2379 0.3180 0.0200  0.0399  0.0597  87  SER   C CA  
1731 C C   . SER   B 81  ? 0.2228 0.2486 0.3256 0.0213  0.0400  0.0659  87  SER   C C   
1732 O O   . SER   B 81  ? 0.2282 0.2542 0.3427 0.0214  0.0428  0.0691  87  SER   C O   
1733 C CB  . SER   B 81  ? 0.1994 0.2267 0.2996 0.0183  0.0336  0.0533  87  SER   C CB  
1734 O OG  . SER   B 81  ? 0.2055 0.2336 0.3105 0.0170  0.0308  0.0523  87  SER   C OG  
1735 N N   . GLU   B 82  ? 0.2455 0.2706 0.3329 0.0223  0.0366  0.0674  88  GLU   C N   
1736 C CA  . GLU   B 82  ? 0.2545 0.2795 0.3386 0.0237  0.0357  0.0731  88  GLU   C CA  
1737 C C   . GLU   B 82  ? 0.2503 0.2771 0.3434 0.0220  0.0324  0.0714  88  GLU   C C   
1738 O O   . GLU   B 82  ? 0.2748 0.3019 0.3710 0.0232  0.0329  0.0766  88  GLU   C O   
1739 C CB  . GLU   B 82  ? 0.3168 0.3406 0.3826 0.0254  0.0323  0.0749  88  GLU   C CB  
1740 C CG  . GLU   B 82  ? 0.4150 0.4396 0.4732 0.0234  0.0256  0.0694  88  GLU   C CG  
1741 C CD  . GLU   B 82  ? 0.5036 0.5270 0.5455 0.0251  0.0220  0.0715  88  GLU   C CD  
1742 O OE1 . GLU   B 82  ? 0.5301 0.5511 0.5625 0.0276  0.0250  0.0745  88  GLU   C OE1 
1743 O OE2 . GLU   B 82  ? 0.5127 0.5374 0.5515 0.0239  0.0162  0.0702  88  GLU   C OE2 
1744 N N   . TYR   B 83  ? 0.2124 0.2402 0.3108 0.0196  0.0300  0.0646  89  TYR   C N   
1745 C CA  . TYR   B 83  ? 0.2053 0.2345 0.3106 0.0182  0.0272  0.0625  89  TYR   C CA  
1746 C C   . TYR   B 83  ? 0.2036 0.2330 0.3238 0.0167  0.0292  0.0583  89  TYR   C C   
1747 O O   . TYR   B 83  ? 0.2048 0.2347 0.3314 0.0160  0.0281  0.0571  89  TYR   C O   
1748 C CB  . TYR   B 83  ? 0.2015 0.2315 0.2970 0.0169  0.0216  0.0585  89  TYR   C CB  
1749 C CG  . TYR   B 83  ? 0.1896 0.2187 0.2782 0.0160  0.0203  0.0532  89  TYR   C CG  
1750 C CD1 . TYR   B 83  ? 0.1983 0.2262 0.2750 0.0170  0.0200  0.0543  89  TYR   C CD1 
1751 C CD2 . TYR   B 83  ? 0.1806 0.2101 0.2747 0.0145  0.0198  0.0472  89  TYR   C CD2 
1752 C CE1 . TYR   B 83  ? 0.1904 0.2173 0.2617 0.0164  0.0192  0.0497  89  TYR   C CE1 
1753 C CE2 . TYR   B 83  ? 0.1914 0.2201 0.2794 0.0140  0.0184  0.0429  89  TYR   C CE2 
1754 C CZ  . TYR   B 83  ? 0.1877 0.2151 0.2651 0.0150  0.0184  0.0443  89  TYR   C CZ  
1755 O OH  . TYR   B 83  ? 0.2021 0.2287 0.2746 0.0148  0.0175  0.0403  89  TYR   C OH  
1756 N N   . TYR   B 84  ? 0.1837 0.2126 0.3100 0.0163  0.0320  0.0559  90  TYR   C N   
1757 C CA  . TYR   B 84  ? 0.1731 0.2019 0.3145 0.0149  0.0335  0.0518  90  TYR   C CA  
1758 C C   . TYR   B 84  ? 0.1666 0.1949 0.3177 0.0153  0.0387  0.0541  90  TYR   C C   
1759 O O   . TYR   B 84  ? 0.1718 0.2001 0.3166 0.0163  0.0404  0.0561  90  TYR   C O   
1760 C CB  . TYR   B 84  ? 0.1586 0.1881 0.2988 0.0133  0.0298  0.0435  90  TYR   C CB  
1761 C CG  . TYR   B 84  ? 0.1444 0.1741 0.2786 0.0126  0.0257  0.0402  90  TYR   C CG  
1762 C CD1 . TYR   B 84  ? 0.1450 0.1745 0.2863 0.0124  0.0260  0.0401  90  TYR   C CD1 
1763 C CD2 . TYR   B 84  ? 0.1386 0.1685 0.2606 0.0123  0.0221  0.0375  90  TYR   C CD2 
1764 C CE1 . TYR   B 84  ? 0.1409 0.1706 0.2773 0.0120  0.0230  0.0372  90  TYR   C CE1 
1765 C CE2 . TYR   B 84  ? 0.1340 0.1640 0.2512 0.0117  0.0191  0.0350  90  TYR   C CE2 
1766 C CZ  . TYR   B 84  ? 0.1433 0.1734 0.2677 0.0116  0.0197  0.0348  90  TYR   C CZ  
1767 O OH  . TYR   B 84  ? 0.1409 0.1712 0.2610 0.0112  0.0175  0.0327  90  TYR   C OH  
1768 N N   . PRO   B 85  ? 0.1647 0.1925 0.3321 0.0145  0.0414  0.0531  91  PRO   C N   
1769 C CA  . PRO   B 85  ? 0.1564 0.1841 0.3356 0.0143  0.0461  0.0541  91  PRO   C CA  
1770 C C   . PRO   B 85  ? 0.1600 0.1893 0.3402 0.0130  0.0434  0.0468  91  PRO   C C   
1771 O O   . PRO   B 85  ? 0.1561 0.1862 0.3280 0.0122  0.0381  0.0411  91  PRO   C O   
1772 C CB  . PRO   B 85  ? 0.1587 0.1852 0.3555 0.0134  0.0486  0.0538  91  PRO   C CB  
1773 C CG  . PRO   B 85  ? 0.1615 0.1881 0.3560 0.0123  0.0435  0.0476  91  PRO   C CG  
1774 C CD  . PRO   B 85  ? 0.1686 0.1959 0.3450 0.0134  0.0401  0.0498  91  PRO   C CD  
1775 N N   . ALA   B 86  ? 0.1498 0.1798 0.3415 0.0127  0.0472  0.0471  92  ALA   C N   
1776 C CA  . ALA   B 86  ? 0.1636 0.1956 0.3597 0.0115  0.0444  0.0402  92  ALA   C CA  
1777 C C   . ALA   B 86  ? 0.1740 0.2062 0.3788 0.0095  0.0400  0.0325  92  ALA   C C   
1778 O O   . ALA   B 86  ? 0.1938 0.2245 0.4105 0.0088  0.0420  0.0330  92  ALA   C O   
1779 C CB  . ALA   B 86  ? 0.1587 0.1918 0.3688 0.0115  0.0499  0.0426  92  ALA   C CB  
1780 N N   . ARG   B 87  ? 0.1607 0.1940 0.3576 0.0091  0.0341  0.0259  93  ARG   C N   
1781 C CA  . ARG   B 87  ? 0.1605 0.1933 0.3615 0.0079  0.0297  0.0185  93  ARG   C CA  
1782 C C   . ARG   B 87  ? 0.1688 0.2031 0.3615 0.0079  0.0238  0.0119  93  ARG   C C   
1783 O O   . ARG   B 87  ? 0.1675 0.2026 0.3493 0.0089  0.0231  0.0135  93  ARG   C O   
1784 C CB  . ARG   B 87  ? 0.1629 0.1936 0.3563 0.0082  0.0292  0.0199  93  ARG   C CB  
1785 C CG  . ARG   B 87  ? 0.1599 0.1907 0.3343 0.0093  0.0266  0.0215  93  ARG   C CG  
1786 C CD  . ARG   B 87  ? 0.1598 0.1892 0.3288 0.0095  0.0259  0.0225  93  ARG   C CD  
1787 N NE  . ARG   B 87  ? 0.1612 0.1909 0.3140 0.0101  0.0225  0.0221  93  ARG   C NE  
1788 C CZ  . ARG   B 87  ? 0.1790 0.2080 0.3258 0.0101  0.0204  0.0201  93  ARG   C CZ  
1789 N NH1 . ARG   B 87  ? 0.1899 0.2177 0.3445 0.0098  0.0213  0.0184  93  ARG   C NH1 
1790 N NH2 . ARG   B 87  ? 0.1880 0.2171 0.3216 0.0103  0.0178  0.0198  93  ARG   C NH2 
1791 N N   . TYR   B 88  ? 0.1864 0.2203 0.3822 0.0072  0.0195  0.0045  94  TYR   C N   
1792 C CA  . TYR   B 88  ? 0.2001 0.2348 0.3855 0.0077  0.0137  -0.0014 94  TYR   C CA  
1793 C C   . TYR   B 88  ? 0.1747 0.2074 0.3432 0.0086  0.0125  -0.0002 94  TYR   C C   
1794 O O   . TYR   B 88  ? 0.1893 0.2202 0.3585 0.0084  0.0140  0.0008  94  TYR   C O   
1795 C CB  . TYR   B 88  ? 0.2283 0.2629 0.4224 0.0069  0.0094  -0.0099 94  TYR   C CB  
1796 C CG  . TYR   B 88  ? 0.2535 0.2907 0.4644 0.0059  0.0089  -0.0125 94  TYR   C CG  
1797 C CD1 . TYR   B 88  ? 0.2684 0.3086 0.4780 0.0066  0.0054  -0.0149 94  TYR   C CD1 
1798 C CD2 . TYR   B 88  ? 0.2654 0.3023 0.4949 0.0043  0.0124  -0.0121 94  TYR   C CD2 
1799 C CE1 . TYR   B 88  ? 0.2774 0.3206 0.5043 0.0056  0.0050  -0.0170 94  TYR   C CE1 
1800 C CE2 . TYR   B 88  ? 0.2740 0.3135 0.5209 0.0031  0.0123  -0.0142 94  TYR   C CE2 
1801 C CZ  . TYR   B 88  ? 0.2870 0.3301 0.5329 0.0038  0.0085  -0.0167 94  TYR   C CZ  
1802 O OH  . TYR   B 88  ? 0.3118 0.3581 0.5769 0.0025  0.0083  -0.0189 94  TYR   C OH  
1803 N N   . GLN   B 89  ? 0.1485 0.1815 0.3034 0.0096  0.0100  -0.0001 95  GLN   C N   
1804 C CA  . GLN   B 89  ? 0.1425 0.1739 0.2826 0.0103  0.0086  0.0004  95  GLN   C CA  
1805 C C   . GLN   B 89  ? 0.1415 0.1727 0.2744 0.0111  0.0036  -0.0058 95  GLN   C C   
1806 O O   . GLN   B 89  ? 0.1493 0.1820 0.2824 0.0117  0.0013  -0.0077 95  GLN   C O   
1807 C CB  . GLN   B 89  ? 0.1429 0.1742 0.2731 0.0108  0.0104  0.0066  95  GLN   C CB  
1808 C CG  . GLN   B 89  ? 0.1637 0.1935 0.2809 0.0111  0.0092  0.0076  95  GLN   C CG  
1809 C CD  . GLN   B 89  ? 0.1643 0.1939 0.2744 0.0112  0.0110  0.0137  95  GLN   C CD  
1810 O OE1 . GLN   B 89  ? 0.1722 0.2022 0.2871 0.0111  0.0141  0.0183  95  GLN   C OE1 
1811 N NE2 . GLN   B 89  ? 0.1493 0.1778 0.2475 0.0114  0.0091  0.0138  95  GLN   C NE2 
1812 N N   . SER   B 90  ? 0.1388 0.1680 0.2649 0.0115  0.0022  -0.0086 96  SER   C N   
1813 C CA  . SER   B 90  ? 0.1453 0.1737 0.2628 0.0128  -0.0022 -0.0142 96  SER   C CA  
1814 C C   . SER   B 90  ? 0.1383 0.1655 0.2403 0.0139  -0.0029 -0.0116 96  SER   C C   
1815 O O   . SER   B 90  ? 0.1413 0.1680 0.2393 0.0133  -0.0001 -0.0064 96  SER   C O   
1816 C CB  . SER   B 90  ? 0.1677 0.1939 0.2860 0.0131  -0.0031 -0.0194 96  SER   C CB  
1817 O OG  . SER   B 90  ? 0.1807 0.2051 0.2937 0.0131  0.0001  -0.0160 96  SER   C OG  
1818 N N   . HIS   B 91  ? 0.1342 0.1608 0.2281 0.0154  -0.0067 -0.0153 97  HIS   C N   
1819 C CA  . HIS   B 91  ? 0.1360 0.1610 0.2157 0.0166  -0.0074 -0.0133 97  HIS   C CA  
1820 C C   . HIS   B 91  ? 0.1372 0.1629 0.2152 0.0160  -0.0055 -0.0079 97  HIS   C C   
1821 O O   . HIS   B 91  ? 0.1508 0.1747 0.2198 0.0159  -0.0043 -0.0046 97  HIS   C O   
1822 C CB  . HIS   B 91  ? 0.1548 0.1770 0.2267 0.0169  -0.0055 -0.0128 97  HIS   C CB  
1823 C CG  . HIS   B 91  ? 0.1770 0.1977 0.2481 0.0180  -0.0069 -0.0184 97  HIS   C CG  
1824 N ND1 . HIS   B 91  ? 0.2114 0.2299 0.2709 0.0203  -0.0094 -0.0215 97  HIS   C ND1 
1825 C CD2 . HIS   B 91  ? 0.1799 0.2006 0.2602 0.0174  -0.0060 -0.0215 97  HIS   C CD2 
1826 C CE1 . HIS   B 91  ? 0.2104 0.2275 0.2710 0.0211  -0.0100 -0.0266 97  HIS   C CE1 
1827 N NE2 . HIS   B 91  ? 0.2025 0.2208 0.2760 0.0193  -0.0080 -0.0271 97  HIS   C NE2 
1828 N N   . LEU   B 92  ? 0.1259 0.1539 0.2122 0.0157  -0.0054 -0.0073 98  LEU   C N   
1829 C CA  . LEU   B 92  ? 0.1330 0.1614 0.2181 0.0154  -0.0032 -0.0026 98  LEU   C CA  
1830 C C   . LEU   B 92  ? 0.1226 0.1515 0.2046 0.0169  -0.0057 -0.0039 98  LEU   C C   
1831 O O   . LEU   B 92  ? 0.1320 0.1627 0.2195 0.0178  -0.0088 -0.0080 98  LEU   C O   
1832 C CB  . LEU   B 92  ? 0.1461 0.1765 0.2436 0.0142  0.0000  -0.0002 98  LEU   C CB  
1833 C CG  . LEU   B 92  ? 0.1622 0.1925 0.2570 0.0142  0.0031  0.0051  98  LEU   C CG  
1834 C CD1 . LEU   B 92  ? 0.1701 0.1985 0.2560 0.0136  0.0044  0.0088  98  LEU   C CD1 
1835 C CD2 . LEU   B 92  ? 0.1628 0.1950 0.2699 0.0137  0.0068  0.0075  98  LEU   C CD2 
1836 N N   . MET   B 93  ? 0.1193 0.1466 0.1927 0.0174  -0.0048 -0.0007 99  MET   C N   
1837 C CA  . MET   B 93  ? 0.1151 0.1423 0.1851 0.0191  -0.0065 -0.0013 99  MET   C CA  
1838 C C   . MET   B 93  ? 0.1192 0.1466 0.1912 0.0188  -0.0030 0.0025  99  MET   C C   
1839 O O   . MET   B 93  ? 0.1414 0.1672 0.2090 0.0177  -0.0004 0.0058  99  MET   C O   
1840 C CB  . MET   B 93  ? 0.1465 0.1702 0.2033 0.0200  -0.0078 -0.0008 99  MET   C CB  
1841 C CG  . MET   B 93  ? 0.1730 0.1958 0.2258 0.0207  -0.0105 -0.0040 99  MET   C CG  
1842 S SD  . MET   B 93  ? 0.1825 0.2008 0.2206 0.0216  -0.0106 -0.0023 99  MET   C SD  
1843 C CE  . MET   B 93  ? 0.1987 0.2159 0.2359 0.0189  -0.0067 0.0019  99  MET   C CE  
1844 N N   . LEU   B 94  ? 0.1157 0.1451 0.1936 0.0201  -0.0029 0.0020  100 LEU   C N   
1845 C CA  . LEU   B 94  ? 0.1230 0.1521 0.2020 0.0203  0.0013  0.0054  100 LEU   C CA  
1846 C C   . LEU   B 94  ? 0.1288 0.1558 0.2001 0.0221  0.0007  0.0057  100 LEU   C C   
1847 O O   . LEU   B 94  ? 0.1436 0.1710 0.2143 0.0236  -0.0027 0.0031  100 LEU   C O   
1848 C CB  . LEU   B 94  ? 0.1358 0.1689 0.2299 0.0205  0.0034  0.0053  100 LEU   C CB  
1849 C CG  . LEU   B 94  ? 0.1520 0.1870 0.2568 0.0188  0.0048  0.0053  100 LEU   C CG  
1850 C CD1 . LEU   B 94  ? 0.1862 0.2247 0.3066 0.0190  0.0075  0.0056  100 LEU   C CD1 
1851 C CD2 . LEU   B 94  ? 0.1686 0.2015 0.2681 0.0175  0.0082  0.0095  100 LEU   C CD2 
1852 N N   . ALA   B 95  ? 0.1354 0.1602 0.2014 0.0223  0.0043  0.0088  101 ALA   C N   
1853 C CA  . ALA   B 95  ? 0.1308 0.1533 0.1911 0.0241  0.0050  0.0091  101 ALA   C CA  
1854 C C   . ALA   B 95  ? 0.1318 0.1542 0.1944 0.0248  0.0102  0.0118  101 ALA   C C   
1855 O O   . ALA   B 95  ? 0.1343 0.1575 0.1992 0.0237  0.0130  0.0141  101 ALA   C O   
1856 C CB  . ALA   B 95  ? 0.1458 0.1634 0.1925 0.0237  0.0036  0.0095  101 ALA   C CB  
1857 N N   . VAL   B 96  ? 0.1360 0.1571 0.1971 0.0269  0.0119  0.0118  102 VAL   C N   
1858 C CA  . VAL   B 96  ? 0.1505 0.1706 0.2110 0.0281  0.0175  0.0144  102 VAL   C CA  
1859 C C   . VAL   B 96  ? 0.1603 0.1750 0.2057 0.0276  0.0180  0.0156  102 VAL   C C   
1860 O O   . VAL   B 96  ? 0.1789 0.1898 0.2158 0.0280  0.0157  0.0140  102 VAL   C O   
1861 C CB  . VAL   B 96  ? 0.1722 0.1929 0.2380 0.0308  0.0193  0.0136  102 VAL   C CB  
1862 C CG1 . VAL   B 96  ? 0.1885 0.2074 0.2521 0.0324  0.0260  0.0163  102 VAL   C CG1 
1863 C CG2 . VAL   B 96  ? 0.1787 0.2055 0.2609 0.0310  0.0177  0.0121  102 VAL   C CG2 
1864 N N   . GLY   B 97  ? 0.1692 0.1834 0.2117 0.0267  0.0207  0.0183  103 GLY   C N   
1865 C CA  . GLY   B 97  ? 0.1887 0.1982 0.2173 0.0261  0.0202  0.0190  103 GLY   C CA  
1866 C C   . GLY   B 97  ? 0.1913 0.2013 0.2179 0.0253  0.0221  0.0223  103 GLY   C C   
1867 O O   . GLY   B 97  ? 0.2118 0.2254 0.2481 0.0250  0.0241  0.0243  103 GLY   C O   
1868 N N   . HIS   B 98  ? 0.1969 0.2030 0.2110 0.0251  0.0213  0.0228  104 HIS   C N   
1869 C CA  . HIS   B 98  ? 0.1998 0.2058 0.2098 0.0248  0.0225  0.0262  104 HIS   C CA  
1870 C C   . HIS   B 98  ? 0.1875 0.1956 0.1995 0.0223  0.0185  0.0269  104 HIS   C C   
1871 O O   . HIS   B 98  ? 0.1920 0.1991 0.2010 0.0206  0.0142  0.0246  104 HIS   C O   
1872 C CB  . HIS   B 98  ? 0.2430 0.2441 0.2384 0.0261  0.0231  0.0262  104 HIS   C CB  
1873 C CG  . HIS   B 98  ? 0.2942 0.2952 0.2843 0.0268  0.0247  0.0301  104 HIS   C CG  
1874 N ND1 . HIS   B 98  ? 0.3174 0.3199 0.3119 0.0288  0.0307  0.0340  104 HIS   C ND1 
1875 C CD2 . HIS   B 98  ? 0.3318 0.3317 0.3135 0.0257  0.0210  0.0310  104 HIS   C CD2 
1876 C CE1 . HIS   B 98  ? 0.3484 0.3503 0.3358 0.0292  0.0305  0.0374  104 HIS   C CE1 
1877 N NE2 . HIS   B 98  ? 0.3521 0.3525 0.3316 0.0275  0.0244  0.0356  104 HIS   C NE2 
1878 N N   . SER   B 99  ? 0.1827 0.1935 0.2002 0.0222  0.0204  0.0304  105 SER   C N   
1879 C CA  . SER   B 99  ? 0.1885 0.2013 0.2086 0.0201  0.0173  0.0315  105 SER   C CA  
1880 C C   . SER   B 99  ? 0.2109 0.2248 0.2320 0.0210  0.0200  0.0365  105 SER   C C   
1881 O O   . SER   B 99  ? 0.2389 0.2546 0.2690 0.0219  0.0244  0.0387  105 SER   C O   
1882 C CB  . SER   B 99  ? 0.2002 0.2162 0.2323 0.0188  0.0161  0.0294  105 SER   C CB  
1883 O OG  . SER   B 99  ? 0.2059 0.2237 0.2418 0.0172  0.0141  0.0306  105 SER   C OG  
1884 N N   . GLU   B 100 ? 0.2052 0.2175 0.2167 0.0209  0.0175  0.0383  106 GLU   C N   
1885 C CA  . GLU   B 100 ? 0.2039 0.2170 0.2141 0.0220  0.0188  0.0434  106 GLU   C CA  
1886 C C   . GLU   B 100 ? 0.1880 0.2042 0.2066 0.0198  0.0155  0.0440  106 GLU   C C   
1887 O O   . GLU   B 100 ? 0.1828 0.1998 0.2038 0.0177  0.0119  0.0405  106 GLU   C O   
1888 C CB  . GLU   B 100 ? 0.2489 0.2589 0.2434 0.0230  0.0161  0.0442  106 GLU   C CB  
1889 C CG  . GLU   B 100 ? 0.3251 0.3307 0.3075 0.0252  0.0182  0.0428  106 GLU   C CG  
1890 C CD  . GLU   B 100 ? 0.3870 0.3917 0.3673 0.0285  0.0250  0.0471  106 GLU   C CD  
1891 O OE1 . GLU   B 100 ? 0.3969 0.3979 0.3678 0.0306  0.0277  0.0459  106 GLU   C OE1 
1892 O OE2 . GLU   B 100 ? 0.4069 0.4141 0.3953 0.0290  0.0280  0.0517  106 GLU   C OE2 
1893 N N   . PRO   B 101 ? 0.1962 0.2141 0.2191 0.0206  0.0170  0.0488  107 PRO   C N   
1894 C CA  . PRO   B 101 ? 0.1858 0.2065 0.2169 0.0188  0.0142  0.0493  107 PRO   C CA  
1895 C C   . PRO   B 101 ? 0.1891 0.2097 0.2139 0.0172  0.0082  0.0471  107 PRO   C C   
1896 O O   . PRO   B 101 ? 0.1819 0.2042 0.2132 0.0152  0.0060  0.0449  107 PRO   C O   
1897 C CB  . PRO   B 101 ? 0.2148 0.2363 0.2483 0.0206  0.0166  0.0557  107 PRO   C CB  
1898 C CG  . PRO   B 101 ? 0.2456 0.2653 0.2761 0.0230  0.0222  0.0583  107 PRO   C CG  
1899 C CD  . PRO   B 101 ? 0.2217 0.2390 0.2434 0.0232  0.0221  0.0542  107 PRO   C CD  
1900 N N   . GLY   B 102 ? 0.1840 0.2024 0.1963 0.0179  0.0056  0.0475  108 GLY   C N   
1901 C CA  . GLY   B 102 ? 0.1807 0.1990 0.1883 0.0161  -0.0003 0.0453  108 GLY   C CA  
1902 C C   . GLY   B 102 ? 0.1746 0.1917 0.1827 0.0140  -0.0018 0.0400  108 GLY   C C   
1903 O O   . GLY   B 102 ? 0.1916 0.2088 0.1990 0.0121  -0.0060 0.0381  108 GLY   C O   
1904 N N   . ASP   B 103 ? 0.1597 0.1754 0.1692 0.0146  0.0017  0.0378  109 ASP   C N   
1905 C CA  . ASP   B 103 ? 0.1535 0.1677 0.1632 0.0132  0.0006  0.0333  109 ASP   C CA  
1906 C C   . ASP   B 103 ? 0.1499 0.1667 0.1696 0.0116  0.0003  0.0322  109 ASP   C C   
1907 O O   . ASP   B 103 ? 0.1588 0.1745 0.1783 0.0105  -0.0011 0.0291  109 ASP   C O   
1908 C CB  . ASP   B 103 ? 0.1690 0.1812 0.1768 0.0148  0.0040  0.0314  109 ASP   C CB  
1909 C CG  . ASP   B 103 ? 0.1890 0.1974 0.1849 0.0163  0.0042  0.0313  109 ASP   C CG  
1910 O OD1 . ASP   B 103 ? 0.2067 0.2131 0.1951 0.0153  0.0003  0.0302  109 ASP   C OD1 
1911 O OD2 . ASP   B 103 ? 0.2072 0.2146 0.2016 0.0185  0.0084  0.0322  109 ASP   C OD2 
1912 N N   . CYS   B 104 ? 0.1382 0.1581 0.1667 0.0118  0.0018  0.0347  110 CYS   C N   
1913 C CA  . CYS   B 104 ? 0.1355 0.1574 0.1729 0.0106  0.0017  0.0332  110 CYS   C CA  
1914 C C   . CYS   B 104 ? 0.1366 0.1583 0.1724 0.0088  -0.0015 0.0321  110 CYS   C C   
1915 O O   . CYS   B 104 ? 0.1548 0.1769 0.1875 0.0082  -0.0041 0.0339  110 CYS   C O   
1916 C CB  . CYS   B 104 ? 0.1310 0.1556 0.1777 0.0110  0.0037  0.0363  110 CYS   C CB  
1917 S SG  . CYS   B 104 ? 0.1600 0.1849 0.2136 0.0126  0.0083  0.0369  110 CYS   C SG  
1918 N N   . GLY   B 105 ? 0.1150 0.1363 0.1531 0.0081  -0.0013 0.0292  111 GLY   C N   
1919 C CA  . GLY   B 105 ? 0.1292 0.1501 0.1669 0.0065  -0.0033 0.0284  111 GLY   C CA  
1920 C C   . GLY   B 105 ? 0.1355 0.1529 0.1656 0.0059  -0.0046 0.0260  111 GLY   C C   
1921 O O   . GLY   B 105 ? 0.1570 0.1735 0.1873 0.0047  -0.0054 0.0251  111 GLY   C O   
1922 N N   . GLY   B 106 ? 0.1452 0.1603 0.1690 0.0070  -0.0044 0.0251  112 GLY   C N   
1923 C CA  . GLY   B 106 ? 0.1477 0.1589 0.1648 0.0068  -0.0053 0.0227  112 GLY   C CA  
1924 C C   . GLY   B 106 ? 0.1425 0.1528 0.1612 0.0072  -0.0041 0.0208  112 GLY   C C   
1925 O O   . GLY   B 106 ? 0.1425 0.1546 0.1654 0.0085  -0.0025 0.0202  112 GLY   C O   
1926 N N   . ILE   B 107 ? 0.1355 0.1429 0.1511 0.0063  -0.0050 0.0197  113 ILE   C N   
1927 C CA  . ILE   B 107 ? 0.1321 0.1382 0.1478 0.0072  -0.0038 0.0184  113 ILE   C CA  
1928 C C   . ILE   B 107 ? 0.1336 0.1374 0.1452 0.0092  -0.0034 0.0166  113 ILE   C C   
1929 O O   . ILE   B 107 ? 0.1409 0.1418 0.1478 0.0094  -0.0039 0.0161  113 ILE   C O   
1930 C CB  . ILE   B 107 ? 0.1718 0.1756 0.1867 0.0054  -0.0042 0.0189  113 ILE   C CB  
1931 C CG1 . ILE   B 107 ? 0.2122 0.2195 0.2340 0.0041  -0.0037 0.0206  113 ILE   C CG1 
1932 C CG2 . ILE   B 107 ? 0.1784 0.1789 0.1898 0.0068  -0.0030 0.0179  113 ILE   C CG2 
1933 C CD1 . ILE   B 107 ? 0.2538 0.2599 0.2777 0.0022  -0.0034 0.0217  113 ILE   C CD1 
1934 N N   . LEU   B 108 ? 0.1224 0.1273 0.1361 0.0108  -0.0027 0.0155  114 LEU   C N   
1935 C CA  . LEU   B 108 ? 0.1263 0.1294 0.1371 0.0130  -0.0029 0.0139  114 LEU   C CA  
1936 C C   . LEU   B 108 ? 0.1390 0.1392 0.1460 0.0134  -0.0029 0.0138  114 LEU   C C   
1937 O O   . LEU   B 108 ? 0.1354 0.1369 0.1442 0.0132  -0.0023 0.0140  114 LEU   C O   
1938 C CB  . LEU   B 108 ? 0.1247 0.1313 0.1407 0.0146  -0.0028 0.0124  114 LEU   C CB  
1939 C CG  . LEU   B 108 ? 0.1424 0.1481 0.1569 0.0172  -0.0038 0.0106  114 LEU   C CG  
1940 C CD1 . LEU   B 108 ? 0.1596 0.1634 0.1719 0.0182  -0.0034 0.0107  114 LEU   C CD1 
1941 C CD2 . LEU   B 108 ? 0.1526 0.1623 0.1740 0.0183  -0.0044 0.0086  114 LEU   C CD2 
1942 N N   . ARG   B 109 ? 0.1324 0.1285 0.1344 0.0142  -0.0031 0.0138  115 ARG   C N   
1943 C CA  . ARG   B 109 ? 0.1591 0.1519 0.1573 0.0148  -0.0025 0.0146  115 ARG   C CA  
1944 C C   . ARG   B 109 ? 0.1661 0.1561 0.1601 0.0178  -0.0031 0.0139  115 ARG   C C   
1945 O O   . ARG   B 109 ? 0.1613 0.1508 0.1552 0.0187  -0.0037 0.0131  115 ARG   C O   
1946 C CB  . ARG   B 109 ? 0.2056 0.1949 0.2026 0.0124  -0.0018 0.0161  115 ARG   C CB  
1947 C CG  . ARG   B 109 ? 0.2560 0.2419 0.2505 0.0120  -0.0026 0.0155  115 ARG   C CG  
1948 C CD  . ARG   B 109 ? 0.3474 0.3301 0.3422 0.0091  -0.0025 0.0164  115 ARG   C CD  
1949 N NE  . ARG   B 109 ? 0.4195 0.4056 0.4183 0.0064  -0.0037 0.0166  115 ARG   C NE  
1950 C CZ  . ARG   B 109 ? 0.5175 0.5054 0.5209 0.0043  -0.0033 0.0181  115 ARG   C CZ  
1951 N NH1 . ARG   B 109 ? 0.5352 0.5217 0.5394 0.0047  -0.0011 0.0196  115 ARG   C NH1 
1952 N NH2 . ARG   B 109 ? 0.5347 0.5259 0.5421 0.0023  -0.0050 0.0184  115 ARG   C NH2 
1953 N N   . CYS   B 110 ? 0.1607 0.1491 0.1512 0.0195  -0.0028 0.0145  116 CYS   C N   
1954 C CA  . CYS   B 110 ? 0.1725 0.1580 0.1583 0.0228  -0.0036 0.0146  116 CYS   C CA  
1955 C C   . CYS   B 110 ? 0.2029 0.1830 0.1837 0.0229  -0.0016 0.0173  116 CYS   C C   
1956 O O   . CYS   B 110 ? 0.2001 0.1791 0.1824 0.0201  0.0003  0.0187  116 CYS   C O   
1957 C CB  . CYS   B 110 ? 0.1575 0.1462 0.1430 0.0256  -0.0056 0.0129  116 CYS   C CB  
1958 S SG  . CYS   B 110 ? 0.1749 0.1636 0.1567 0.0261  -0.0044 0.0133  116 CYS   C SG  
1959 N N   . GLN   B 111 ? 0.2145 0.1912 0.1899 0.0262  -0.0020 0.0183  117 GLN   C N   
1960 C CA  . GLN   B 111 ? 0.2426 0.2136 0.2134 0.0266  0.0006  0.0215  117 GLN   C CA  
1961 C C   . GLN   B 111 ? 0.2389 0.2103 0.2079 0.0261  0.0030  0.0230  117 GLN   C C   
1962 O O   . GLN   B 111 ? 0.2570 0.2244 0.2248 0.0252  0.0062  0.0260  117 GLN   C O   
1963 C CB  . GLN   B 111 ? 0.2658 0.2330 0.2307 0.0309  -0.0002 0.0229  117 GLN   C CB  
1964 C CG  . GLN   B 111 ? 0.3268 0.2966 0.2869 0.0347  -0.0023 0.0222  117 GLN   C CG  
1965 C CD  . GLN   B 111 ? 0.4541 0.4211 0.4087 0.0394  -0.0042 0.0235  117 GLN   C CD  
1966 O OE1 . GLN   B 111 ? 0.4920 0.4617 0.4495 0.0412  -0.0075 0.0215  117 GLN   C OE1 
1967 N NE2 . GLN   B 111 ? 0.4607 0.4227 0.4079 0.0417  -0.0021 0.0271  117 GLN   C NE2 
1968 N N   . HIS   B 112 ? 0.2130 0.1892 0.1828 0.0267  0.0018  0.0208  118 HIS   C N   
1969 C CA  . HIS   B 112 ? 0.2143 0.1907 0.1820 0.0268  0.0045  0.0219  118 HIS   C CA  
1970 C C   . HIS   B 112 ? 0.2155 0.1947 0.1907 0.0228  0.0063  0.0219  118 HIS   C C   
1971 O O   . HIS   B 112 ? 0.2270 0.2061 0.2017 0.0227  0.0094  0.0232  118 HIS   C O   
1972 C CB  . HIS   B 112 ? 0.2201 0.1991 0.1836 0.0301  0.0022  0.0192  118 HIS   C CB  
1973 C CG  . HIS   B 112 ? 0.2074 0.1846 0.1641 0.0343  -0.0007 0.0191  118 HIS   C CG  
1974 N ND1 . HIS   B 112 ? 0.2160 0.1967 0.1757 0.0356  -0.0051 0.0160  118 HIS   C ND1 
1975 C CD2 . HIS   B 112 ? 0.2500 0.2224 0.1974 0.0379  0.0004  0.0218  118 HIS   C CD2 
1976 C CE1 . HIS   B 112 ? 0.2415 0.2197 0.1946 0.0395  -0.0071 0.0169  118 HIS   C CE1 
1977 N NE2 . HIS   B 112 ? 0.2534 0.2265 0.1982 0.0413  -0.0040 0.0205  118 HIS   C NE2 
1978 N N   . GLY   B 113 ? 0.1972 0.1791 0.1789 0.0200  0.0046  0.0206  119 GLY   C N   
1979 C CA  . GLY   B 113 ? 0.1936 0.1784 0.1824 0.0165  0.0056  0.0208  119 GLY   C CA  
1980 C C   . GLY   B 113 ? 0.1631 0.1529 0.1570 0.0156  0.0030  0.0183  119 GLY   C C   
1981 O O   . GLY   B 113 ? 0.1693 0.1596 0.1625 0.0166  0.0008  0.0167  119 GLY   C O   
1982 N N   . VAL   B 114 ? 0.1563 0.1496 0.1560 0.0136  0.0039  0.0184  120 VAL   C N   
1983 C CA  . VAL   B 114 ? 0.1562 0.1539 0.1615 0.0127  0.0021  0.0169  120 VAL   C CA  
1984 C C   . VAL   B 114 ? 0.1529 0.1529 0.1581 0.0150  0.0012  0.0143  120 VAL   C C   
1985 O O   . VAL   B 114 ? 0.1677 0.1679 0.1716 0.0163  0.0025  0.0136  120 VAL   C O   
1986 C CB  . VAL   B 114 ? 0.1701 0.1706 0.1822 0.0101  0.0032  0.0184  120 VAL   C CB  
1987 C CG1 . VAL   B 114 ? 0.1850 0.1897 0.2025 0.0095  0.0018  0.0175  120 VAL   C CG1 
1988 C CG2 . VAL   B 114 ? 0.1824 0.1811 0.1959 0.0074  0.0031  0.0204  120 VAL   C CG2 
1989 N N   . VAL   B 115 ? 0.1374 0.1390 0.1441 0.0156  -0.0009 0.0127  121 VAL   C N   
1990 C CA  . VAL   B 115 ? 0.1401 0.1443 0.1489 0.0175  -0.0024 0.0099  121 VAL   C CA  
1991 C C   . VAL   B 115 ? 0.1463 0.1543 0.1630 0.0161  -0.0019 0.0093  121 VAL   C C   
1992 O O   . VAL   B 115 ? 0.1531 0.1627 0.1725 0.0170  -0.0021 0.0070  121 VAL   C O   
1993 C CB  . VAL   B 115 ? 0.1456 0.1497 0.1538 0.0190  -0.0044 0.0088  121 VAL   C CB  
1994 C CG1 . VAL   B 115 ? 0.1577 0.1652 0.1708 0.0204  -0.0063 0.0058  121 VAL   C CG1 
1995 C CG2 . VAL   B 115 ? 0.1704 0.1704 0.1710 0.0209  -0.0049 0.0095  121 VAL   C CG2 
1996 N N   . GLY   B 116 ? 0.1365 0.1457 0.1569 0.0141  -0.0014 0.0112  122 GLY   C N   
1997 C CA  . GLY   B 116 ? 0.1441 0.1567 0.1723 0.0130  -0.0007 0.0116  122 GLY   C CA  
1998 C C   . GLY   B 116 ? 0.1275 0.1407 0.1570 0.0113  -0.0006 0.0142  122 GLY   C C   
1999 O O   . GLY   B 116 ? 0.1361 0.1469 0.1606 0.0106  -0.0011 0.0153  122 GLY   C O   
2000 N N   . ILE   B 117 ? 0.1180 0.1340 0.1539 0.0107  0.0000  0.0152  123 ILE   C N   
2001 C CA  . ILE   B 117 ? 0.1198 0.1365 0.1559 0.0096  -0.0001 0.0180  123 ILE   C CA  
2002 C C   . ILE   B 117 ? 0.1154 0.1337 0.1553 0.0104  0.0008  0.0184  123 ILE   C C   
2003 O O   . ILE   B 117 ? 0.1251 0.1452 0.1715 0.0111  0.0017  0.0171  123 ILE   C O   
2004 C CB  . ILE   B 117 ? 0.1374 0.1559 0.1777 0.0082  0.0002  0.0204  123 ILE   C CB  
2005 C CG1 . ILE   B 117 ? 0.1515 0.1723 0.1997 0.0086  0.0018  0.0199  123 ILE   C CG1 
2006 C CG2 . ILE   B 117 ? 0.1500 0.1669 0.1871 0.0070  -0.0004 0.0208  123 ILE   C CG2 
2007 C CD1 . ILE   B 117 ? 0.1551 0.1782 0.2092 0.0076  0.0024  0.0229  123 ILE   C CD1 
2008 N N   . VAL   B 118 ? 0.1173 0.1349 0.1536 0.0104  0.0008  0.0203  124 VAL   C N   
2009 C CA  . VAL   B 118 ? 0.1250 0.1439 0.1645 0.0114  0.0026  0.0216  124 VAL   C CA  
2010 C C   . VAL   B 118 ? 0.1237 0.1453 0.1717 0.0111  0.0041  0.0236  124 VAL   C C   
2011 O O   . VAL   B 118 ? 0.1204 0.1429 0.1693 0.0101  0.0034  0.0255  124 VAL   C O   
2012 C CB  . VAL   B 118 ? 0.1296 0.1467 0.1619 0.0117  0.0026  0.0236  124 VAL   C CB  
2013 C CG1 . VAL   B 118 ? 0.1370 0.1553 0.1723 0.0130  0.0056  0.0259  124 VAL   C CG1 
2014 C CG2 . VAL   B 118 ? 0.1356 0.1493 0.1601 0.0121  0.0017  0.0214  124 VAL   C CG2 
2015 N N   . SER   B 119 ? 0.1207 0.1439 0.1762 0.0119  0.0061  0.0231  125 SER   C N   
2016 C CA  . SER   B 119 ? 0.1182 0.1434 0.1832 0.0117  0.0079  0.0249  125 SER   C CA  
2017 C C   . SER   B 119 ? 0.1263 0.1523 0.1967 0.0127  0.0110  0.0272  125 SER   C C   
2018 O O   . SER   B 119 ? 0.1327 0.1597 0.2090 0.0127  0.0130  0.0304  125 SER   C O   
2019 C CB  . SER   B 119 ? 0.1318 0.1578 0.2032 0.0114  0.0073  0.0211  125 SER   C CB  
2020 O OG  . SER   B 119 ? 0.1379 0.1653 0.2195 0.0112  0.0093  0.0222  125 SER   C OG  
2021 N N   . THR   B 120 ? 0.1282 0.1538 0.1980 0.0136  0.0119  0.0258  126 THR   C N   
2022 C CA  . THR   B 120 ? 0.1264 0.1529 0.2029 0.0146  0.0158  0.0281  126 THR   C CA  
2023 C C   . THR   B 120 ? 0.1280 0.1530 0.1965 0.0160  0.0172  0.0292  126 THR   C C   
2024 O O   . THR   B 120 ? 0.1256 0.1488 0.1852 0.0161  0.0148  0.0270  126 THR   C O   
2025 C CB  . THR   B 120 ? 0.1267 0.1553 0.2161 0.0144  0.0164  0.0249  126 THR   C CB  
2026 O OG1 . THR   B 120 ? 0.1416 0.1702 0.2288 0.0150  0.0144  0.0211  126 THR   C OG1 
2027 C CG2 . THR   B 120 ? 0.1405 0.1699 0.2368 0.0132  0.0149  0.0227  126 THR   C CG2 
2028 N N   . GLY   B 121 ? 0.1495 0.1746 0.2213 0.0172  0.0216  0.0327  127 GLY   C N   
2029 C CA  . GLY   B 121 ? 0.1728 0.1962 0.2375 0.0190  0.0241  0.0340  127 GLY   C CA  
2030 C C   . GLY   B 121 ? 0.2169 0.2413 0.2900 0.0204  0.0300  0.0373  127 GLY   C C   
2031 O O   . GLY   B 121 ? 0.2309 0.2566 0.3126 0.0200  0.0324  0.0402  127 GLY   C O   
2032 N N   . GLY   B 122 ? 0.2470 0.2703 0.3166 0.0221  0.0330  0.0376  128 GLY   C N   
2033 C CA  . GLY   B 122 ? 0.2664 0.2904 0.3440 0.0238  0.0397  0.0411  128 GLY   C CA  
2034 C C   . GLY   B 122 ? 0.2679 0.2939 0.3551 0.0243  0.0412  0.0382  128 GLY   C C   
2035 O O   . GLY   B 122 ? 0.2672 0.2948 0.3584 0.0233  0.0366  0.0334  128 GLY   C O   
2036 N N   . ASN   B 123 ? 0.2575 0.2834 0.3487 0.0263  0.0478  0.0414  129 ASN   C N   
2037 C CA  . ASN   B 123 ? 0.2718 0.3001 0.3738 0.0272  0.0499  0.0392  129 ASN   C CA  
2038 C C   . ASN   B 123 ? 0.2487 0.2756 0.3414 0.0280  0.0460  0.0349  129 ASN   C C   
2039 O O   . ASN   B 123 ? 0.2764 0.3060 0.3790 0.0283  0.0449  0.0318  129 ASN   C O   
2040 C CB  . ASN   B 123 ? 0.3236 0.3565 0.4452 0.0251  0.0477  0.0364  129 ASN   C CB  
2041 C CG  . ASN   B 123 ? 0.4245 0.4594 0.5621 0.0249  0.0538  0.0403  129 ASN   C CG  
2042 O OD1 . ASN   B 123 ? 0.4377 0.4724 0.5786 0.0269  0.0610  0.0443  129 ASN   C OD1 
2043 N ND2 . ASN   B 123 ? 0.4702 0.5069 0.6189 0.0226  0.0515  0.0392  129 ASN   C ND2 
2044 N N   . GLY   B 124 ? 0.2218 0.2446 0.2968 0.0285  0.0438  0.0348  130 GLY   C N   
2045 C CA  . GLY   B 124 ? 0.2089 0.2294 0.2749 0.0291  0.0403  0.0309  130 GLY   C CA  
2046 C C   . GLY   B 124 ? 0.1879 0.2099 0.2565 0.0272  0.0332  0.0265  130 GLY   C C   
2047 O O   . GLY   B 124 ? 0.1932 0.2140 0.2577 0.0280  0.0306  0.0235  130 GLY   C O   
2048 N N   . LEU   B 125 ? 0.1714 0.1957 0.2459 0.0250  0.0305  0.0263  131 LEU   C N   
2049 C CA  . LEU   B 125 ? 0.1688 0.1942 0.2445 0.0234  0.0242  0.0223  131 LEU   C CA  
2050 C C   . LEU   B 125 ? 0.1758 0.1992 0.2424 0.0217  0.0215  0.0231  131 LEU   C C   
2051 O O   . LEU   B 125 ? 0.2035 0.2264 0.2683 0.0213  0.0238  0.0266  131 LEU   C O   
2052 C CB  . LEU   B 125 ? 0.1847 0.2145 0.2766 0.0224  0.0232  0.0205  131 LEU   C CB  
2053 C CG  . LEU   B 125 ? 0.2122 0.2451 0.3167 0.0238  0.0255  0.0196  131 LEU   C CG  
2054 C CD1 . LEU   B 125 ? 0.2508 0.2878 0.3733 0.0225  0.0262  0.0190  131 LEU   C CD1 
2055 C CD2 . LEU   B 125 ? 0.2196 0.2525 0.3212 0.0251  0.0214  0.0160  131 LEU   C CD2 
2056 N N   . VAL   B 126 ? 0.1374 0.1596 0.1981 0.0209  0.0167  0.0201  132 VAL   C N   
2057 C CA  . VAL   B 126 ? 0.1265 0.1475 0.1808 0.0192  0.0140  0.0205  132 VAL   C CA  
2058 C C   . VAL   B 126 ? 0.1236 0.1467 0.1844 0.0181  0.0105  0.0173  132 VAL   C C   
2059 O O   . VAL   B 126 ? 0.1252 0.1489 0.1879 0.0189  0.0083  0.0142  132 VAL   C O   
2060 C CB  . VAL   B 126 ? 0.1372 0.1542 0.1780 0.0191  0.0119  0.0200  132 VAL   C CB  
2061 C CG1 . VAL   B 126 ? 0.1662 0.1816 0.2044 0.0202  0.0102  0.0170  132 VAL   C CG1 
2062 C CG2 . VAL   B 126 ? 0.1429 0.1593 0.1798 0.0171  0.0089  0.0202  132 VAL   C CG2 
2063 N N   . GLY   B 127 ? 0.1179 0.1419 0.1818 0.0167  0.0102  0.0181  133 GLY   C N   
2064 C CA  . GLY   B 127 ? 0.1129 0.1383 0.1816 0.0159  0.0073  0.0148  133 GLY   C CA  
2065 C C   . GLY   B 127 ? 0.1156 0.1392 0.1766 0.0149  0.0053  0.0149  133 GLY   C C   
2066 O O   . GLY   B 127 ? 0.1214 0.1443 0.1792 0.0140  0.0063  0.0180  133 GLY   C O   
2067 N N   . PHE   B 128 ? 0.1044 0.1275 0.1631 0.0150  0.0026  0.0117  134 PHE   C N   
2068 C CA  . PHE   B 128 ? 0.1122 0.1335 0.1644 0.0142  0.0012  0.0116  134 PHE   C CA  
2069 C C   . PHE   B 128 ? 0.1168 0.1392 0.1738 0.0140  0.0004  0.0091  134 PHE   C C   
2070 O O   . PHE   B 128 ? 0.1217 0.1449 0.1820 0.0150  -0.0011 0.0057  134 PHE   C O   
2071 C CB  . PHE   B 128 ? 0.1207 0.1392 0.1638 0.0151  -0.0007 0.0104  134 PHE   C CB  
2072 C CG  . PHE   B 128 ? 0.1213 0.1381 0.1597 0.0157  -0.0001 0.0117  134 PHE   C CG  
2073 C CD1 . PHE   B 128 ? 0.1285 0.1432 0.1609 0.0147  0.0005  0.0141  134 PHE   C CD1 
2074 C CD2 . PHE   B 128 ? 0.1324 0.1497 0.1729 0.0174  -0.0001 0.0104  134 PHE   C CD2 
2075 C CE1 . PHE   B 128 ? 0.1397 0.1521 0.1668 0.0154  0.0011  0.0146  134 PHE   C CE1 
2076 C CE2 . PHE   B 128 ? 0.1400 0.1553 0.1761 0.0183  0.0010  0.0114  134 PHE   C CE2 
2077 C CZ  . PHE   B 128 ? 0.1384 0.1509 0.1672 0.0173  0.0017  0.0134  134 PHE   C CZ  
2078 N N   . ALA   B 129 ? 0.1188 0.1410 0.1759 0.0129  0.0013  0.0107  135 ALA   C N   
2079 C CA  . ALA   B 129 ? 0.1151 0.1375 0.1751 0.0130  0.0011  0.0082  135 ALA   C CA  
2080 C C   . ALA   B 129 ? 0.1327 0.1528 0.1837 0.0138  -0.0003 0.0064  135 ALA   C C   
2081 O O   . ALA   B 129 ? 0.1370 0.1555 0.1820 0.0132  0.0002  0.0087  135 ALA   C O   
2082 C CB  . ALA   B 129 ? 0.1249 0.1481 0.1890 0.0118  0.0031  0.0110  135 ALA   C CB  
2083 N N   . ASP   B 130 ? 0.1277 0.1474 0.1776 0.0154  -0.0021 0.0024  136 ASP   C N   
2084 C CA  . ASP   B 130 ? 0.1374 0.1545 0.1780 0.0168  -0.0032 0.0010  136 ASP   C CA  
2085 C C   . ASP   B 130 ? 0.1447 0.1606 0.1833 0.0165  -0.0010 0.0015  136 ASP   C C   
2086 O O   . ASP   B 130 ? 0.1506 0.1677 0.1957 0.0159  0.0003  0.0006  136 ASP   C O   
2087 C CB  . ASP   B 130 ? 0.1577 0.1751 0.1979 0.0189  -0.0062 -0.0037 136 ASP   C CB  
2088 C CG  . ASP   B 130 ? 0.2063 0.2208 0.2354 0.0211  -0.0075 -0.0048 136 ASP   C CG  
2089 O OD1 . ASP   B 130 ? 0.1883 0.2008 0.2108 0.0214  -0.0072 -0.0021 136 ASP   C OD1 
2090 O OD2 . ASP   B 130 ? 0.2514 0.2651 0.2779 0.0227  -0.0087 -0.0084 136 ASP   C OD2 
2091 N N   . VAL   B 131 ? 0.1427 0.1559 0.1729 0.0169  -0.0002 0.0032  137 VAL   C N   
2092 C CA  . VAL   B 131 ? 0.1452 0.1570 0.1733 0.0170  0.0025  0.0036  137 VAL   C CA  
2093 C C   . VAL   B 131 ? 0.1616 0.1701 0.1794 0.0196  0.0024  0.0020  137 VAL   C C   
2094 O O   . VAL   B 131 ? 0.1647 0.1715 0.1793 0.0202  0.0053  0.0026  137 VAL   C O   
2095 C CB  . VAL   B 131 ? 0.1521 0.1641 0.1819 0.0149  0.0047  0.0081  137 VAL   C CB  
2096 C CG1 . VAL   B 131 ? 0.1499 0.1650 0.1889 0.0129  0.0047  0.0099  137 VAL   C CG1 
2097 C CG2 . VAL   B 131 ? 0.1566 0.1663 0.1800 0.0146  0.0040  0.0102  137 VAL   C CG2 
2098 N N   . ARG   B 132 ? 0.1547 0.1623 0.1672 0.0214  -0.0007 0.0004  138 ARG   C N   
2099 C CA  . ARG   B 132 ? 0.1545 0.1586 0.1557 0.0243  -0.0010 -0.0003 138 ARG   C CA  
2100 C C   . ARG   B 132 ? 0.1735 0.1766 0.1708 0.0266  -0.0010 -0.0042 138 ARG   C C   
2101 O O   . ARG   B 132 ? 0.1957 0.1953 0.1825 0.0291  0.0002  -0.0038 138 ARG   C O   
2102 C CB  . ARG   B 132 ? 0.1565 0.1603 0.1541 0.0259  -0.0048 -0.0009 138 ARG   C CB  
2103 C CG  . ARG   B 132 ? 0.1532 0.1565 0.1521 0.0242  -0.0042 0.0028  138 ARG   C CG  
2104 C CD  . ARG   B 132 ? 0.1612 0.1641 0.1574 0.0261  -0.0075 0.0021  138 ARG   C CD  
2105 N NE  . ARG   B 132 ? 0.1549 0.1619 0.1593 0.0260  -0.0104 -0.0011 138 ARG   C NE  
2106 C CZ  . ARG   B 132 ? 0.1736 0.1817 0.1796 0.0274  -0.0133 -0.0021 138 ARG   C CZ  
2107 N NH1 . ARG   B 132 ? 0.1777 0.1832 0.1768 0.0295  -0.0143 -0.0006 138 ARG   C NH1 
2108 N NH2 . ARG   B 132 ? 0.1820 0.1940 0.1975 0.0269  -0.0151 -0.0046 138 ARG   C NH2 
2109 N N   . ASP   B 133 ? 0.1655 0.1711 0.1704 0.0260  -0.0020 -0.0079 139 ASP   C N   
2110 C CA  . ASP   B 133 ? 0.1772 0.1813 0.1783 0.0282  -0.0022 -0.0125 139 ASP   C CA  
2111 C C   . ASP   B 133 ? 0.1900 0.1928 0.1921 0.0276  0.0033  -0.0111 139 ASP   C C   
2112 O O   . ASP   B 133 ? 0.2101 0.2108 0.2074 0.0298  0.0043  -0.0147 139 ASP   C O   
2113 C CB  . ASP   B 133 ? 0.1914 0.1983 0.2017 0.0277  -0.0058 -0.0176 139 ASP   C CB  
2114 C CG  . ASP   B 133 ? 0.2192 0.2289 0.2432 0.0245  -0.0035 -0.0161 139 ASP   C CG  
2115 O OD1 . ASP   B 133 ? 0.1988 0.2099 0.2263 0.0224  -0.0019 -0.0112 139 ASP   C OD1 
2116 O OD2 . ASP   B 133 ? 0.2412 0.2515 0.2721 0.0242  -0.0033 -0.0198 139 ASP   C OD2 
2117 N N   . LEU   B 134 ? 0.1816 0.1857 0.1901 0.0249  0.0066  -0.0062 140 LEU   C N   
2118 C CA  . LEU   B 134 ? 0.1762 0.1801 0.1884 0.0242  0.0116  -0.0045 140 LEU   C CA  
2119 C C   . LEU   B 134 ? 0.1829 0.1834 0.1856 0.0257  0.0155  -0.0015 140 LEU   C C   
2120 O O   . LEU   B 134 ? 0.1835 0.1843 0.1888 0.0239  0.0179  0.0033  140 LEU   C O   
2121 C CB  . LEU   B 134 ? 0.1658 0.1732 0.1899 0.0208  0.0125  -0.0006 140 LEU   C CB  
2122 C CG  . LEU   B 134 ? 0.1739 0.1843 0.2075 0.0195  0.0096  -0.0025 140 LEU   C CG  
2123 C CD1 . LEU   B 134 ? 0.1781 0.1915 0.2209 0.0167  0.0104  0.0021  140 LEU   C CD1 
2124 C CD2 . LEU   B 134 ? 0.1878 0.1979 0.2257 0.0206  0.0101  -0.0072 140 LEU   C CD2 
2125 N N   . LEU   B 135 ? 0.1975 0.1944 0.1887 0.0293  0.0159  -0.0044 141 LEU   C N   
2126 C CA  . LEU   B 135 ? 0.2111 0.2042 0.1918 0.0313  0.0197  -0.0012 141 LEU   C CA  
2127 C C   . LEU   B 135 ? 0.2119 0.2047 0.1971 0.0304  0.0265  0.0024  141 LEU   C C   
2128 O O   . LEU   B 135 ? 0.2256 0.2164 0.2074 0.0305  0.0302  0.0069  141 LEU   C O   
2129 C CB  . LEU   B 135 ? 0.2178 0.2068 0.1836 0.0359  0.0187  -0.0049 141 LEU   C CB  
2130 C CG  . LEU   B 135 ? 0.2578 0.2478 0.2203 0.0372  0.0111  -0.0093 141 LEU   C CG  
2131 C CD1 . LEU   B 135 ? 0.2752 0.2610 0.2213 0.0422  0.0095  -0.0126 141 LEU   C CD1 
2132 C CD2 . LEU   B 135 ? 0.2614 0.2529 0.2262 0.0356  0.0079  -0.0060 141 LEU   C CD2 
2133 N N   . TRP   B 136 ? 0.2072 0.2020 0.2012 0.0296  0.0282  0.0004  142 TRP   C N   
2134 C CA  . TRP   B 136 ? 0.2152 0.2104 0.2155 0.0289  0.0347  0.0035  142 TRP   C CA  
2135 C C   . TRP   B 136 ? 0.2193 0.2176 0.2298 0.0252  0.0353  0.0092  142 TRP   C C   
2136 O O   . TRP   B 136 ? 0.2410 0.2397 0.2566 0.0246  0.0405  0.0127  142 TRP   C O   
2137 C CB  . TRP   B 136 ? 0.2124 0.2091 0.2209 0.0290  0.0359  -0.0001 142 TRP   C CB  
2138 C CG  . TRP   B 136 ? 0.2036 0.2041 0.2228 0.0264  0.0309  -0.0016 142 TRP   C CG  
2139 C CD1 . TRP   B 136 ? 0.2157 0.2163 0.2342 0.0270  0.0262  -0.0068 142 TRP   C CD1 
2140 C CD2 . TRP   B 136 ? 0.1973 0.2022 0.2300 0.0231  0.0306  0.0023  142 TRP   C CD2 
2141 N NE1 . TRP   B 136 ? 0.2222 0.2267 0.2530 0.0241  0.0236  -0.0058 142 TRP   C NE1 
2142 C CE2 . TRP   B 136 ? 0.2091 0.2162 0.2479 0.0219  0.0261  -0.0003 142 TRP   C CE2 
2143 C CE3 . TRP   B 136 ? 0.2025 0.2098 0.2430 0.0210  0.0334  0.0077  142 TRP   C CE3 
2144 C CZ2 . TRP   B 136 ? 0.1978 0.2088 0.2484 0.0192  0.0248  0.0029  142 TRP   C CZ2 
2145 C CZ3 . TRP   B 136 ? 0.2083 0.2198 0.2607 0.0183  0.0313  0.0102  142 TRP   C CZ3 
2146 C CH2 . TRP   B 136 ? 0.2012 0.2143 0.2576 0.0176  0.0272  0.0080  142 TRP   C CH2 
2147 N N   . LEU   B 137 ? 0.2059 0.2064 0.2194 0.0228  0.0301  0.0101  143 LEU   C N   
2148 C CA  . LEU   B 137 ? 0.2118 0.2146 0.2331 0.0195  0.0301  0.0149  143 LEU   C CA  
2149 C C   . LEU   B 137 ? 0.2440 0.2436 0.2598 0.0199  0.0337  0.0187  143 LEU   C C   
2150 O O   . LEU   B 137 ? 0.2588 0.2600 0.2826 0.0174  0.0353  0.0226  143 LEU   C O   
2151 C CB  . LEU   B 137 ? 0.2048 0.2095 0.2279 0.0175  0.0243  0.0148  143 LEU   C CB  
2152 C CG  . LEU   B 137 ? 0.1914 0.1998 0.2228 0.0164  0.0213  0.0128  143 LEU   C CG  
2153 C CD1 . LEU   B 137 ? 0.2024 0.2116 0.2327 0.0153  0.0163  0.0123  143 LEU   C CD1 
2154 C CD2 . LEU   B 137 ? 0.2030 0.2150 0.2466 0.0141  0.0229  0.0159  143 LEU   C CD2 
2155 N N   . ASP   B 138 ? 0.2503 0.2454 0.2530 0.0232  0.0349  0.0176  144 ASP   C N   
2156 C CA  . ASP   B 138 ? 0.2778 0.2690 0.2745 0.0241  0.0389  0.0216  144 ASP   C CA  
2157 C C   . ASP   B 138 ? 0.3138 0.3033 0.3107 0.0256  0.0467  0.0239  144 ASP   C C   
2158 O O   . ASP   B 138 ? 0.3286 0.3147 0.3214 0.0263  0.0510  0.0278  144 ASP   C O   
2159 C CB  . ASP   B 138 ? 0.2840 0.2707 0.2655 0.0275  0.0368  0.0203  144 ASP   C CB  
2160 C CG  . ASP   B 138 ? 0.2946 0.2824 0.2753 0.0265  0.0298  0.0185  144 ASP   C CG  
2161 O OD1 . ASP   B 138 ? 0.2953 0.2865 0.2859 0.0230  0.0272  0.0193  144 ASP   C OD1 
2162 O OD2 . ASP   B 138 ? 0.3307 0.3161 0.3009 0.0296  0.0270  0.0164  144 ASP   C OD2 
2163 N N   . GLU   B 139 ? 0.3319 0.3234 0.3339 0.0262  0.0491  0.0218  145 GLU   C N   
2164 C CA  . GLU   B 139 ? 0.3850 0.3747 0.3869 0.0282  0.0572  0.0236  145 GLU   C CA  
2165 C C   . GLU   B 139 ? 0.4300 0.4244 0.4478 0.0261  0.0599  0.0244  145 GLU   C C   
2166 O O   . GLU   B 139 ? 0.4278 0.4266 0.4555 0.0234  0.0550  0.0233  145 GLU   C O   
2167 C CB  . GLU   B 139 ? 0.4426 0.4278 0.4291 0.0332  0.0588  0.0193  145 GLU   C CB  
2168 C CG  . GLU   B 139 ? 0.5375 0.5247 0.5255 0.0335  0.0537  0.0130  145 GLU   C CG  
2169 C CD  . GLU   B 139 ? 0.6451 0.6283 0.6178 0.0378  0.0519  0.0074  145 GLU   C CD  
2170 O OE1 . GLU   B 139 ? 0.6537 0.6376 0.6287 0.0386  0.0505  0.0022  145 GLU   C OE1 
2171 O OE2 . GLU   B 139 ? 0.6804 0.6596 0.6390 0.0406  0.0516  0.0081  145 GLU   C OE2 
2172 N N   . GLU   B 140 ? 0.4667 0.4599 0.4867 0.0278  0.0680  0.0266  146 GLU   C N   
2173 C CA  . GLU   B 140 ? 0.5016 0.4988 0.5365 0.0268  0.0720  0.0277  146 GLU   C CA  
2174 C C   . GLU   B 140 ? 0.5316 0.5335 0.5827 0.0226  0.0720  0.0329  146 GLU   C C   
2175 O O   . GLU   B 140 ? 0.5489 0.5516 0.6084 0.0226  0.0788  0.0365  146 GLU   C O   
2176 C CB  . GLU   B 140 ? 0.5256 0.5253 0.5649 0.0269  0.0681  0.0229  146 GLU   C CB  
2177 C CG  . GLU   B 140 ? 0.5995 0.6041 0.6564 0.0254  0.0706  0.0245  146 GLU   C CG  
2178 C CD  . GLU   B 140 ? 0.7024 0.7049 0.7592 0.0289  0.0782  0.0228  146 GLU   C CD  
2179 O OE1 . GLU   B 140 ? 0.7208 0.7219 0.7746 0.0308  0.0768  0.0176  146 GLU   C OE1 
2180 O OE2 . GLU   B 140 ? 0.7348 0.7367 0.7950 0.0299  0.0858  0.0264  146 GLU   C OE2 
2181 N N1  . A1B2W C .   ? 0.3975 0.3625 0.4486 0.0471  0.0625  -0.0181 201 A1B2W A N1  
2182 C C4  . A1B2W C .   ? 0.4068 0.3569 0.4471 0.0417  0.0664  -0.0280 201 A1B2W A C4  
2183 C C5  . A1B2W C .   ? 0.3945 0.3682 0.4429 0.0466  0.0628  -0.0180 201 A1B2W A C5  
2184 C C6  . A1B2W C .   ? 0.4200 0.3892 0.4551 0.0410  0.0683  -0.0279 201 A1B2W A C6  
2185 C C7  . A1B2W C .   ? 0.4231 0.3855 0.4685 0.0450  0.0826  -0.0322 201 A1B2W A C7  
2186 C C8  . A1B2W C .   ? 0.4349 0.3932 0.4674 0.0388  0.0899  -0.0426 201 A1B2W A C8  
2187 C C10 . A1B2W C .   ? 0.4219 0.4037 0.4506 0.0386  0.0625  -0.0252 201 A1B2W A C10 
2188 O O1  . A1B2W C .   ? 0.3789 0.3651 0.4362 0.0503  0.0596  -0.0097 201 A1B2W A O1  
2189 C C3  . A1B2W C .   ? 0.4072 0.3555 0.4408 0.0378  0.0573  -0.0269 201 A1B2W A C3  
2190 C C2  . A1B2W C .   ? 0.3839 0.3361 0.4320 0.0437  0.0541  -0.0174 201 A1B2W A C2  
2191 C C11 . A1B2W C .   ? 0.3765 0.3467 0.4418 0.0523  0.0587  -0.0079 201 A1B2W A C11 
2192 C C1  . A1B2W C .   ? 0.3637 0.3315 0.4209 0.0481  0.0501  -0.0078 201 A1B2W A C1  
2193 C C   . A1B2W C .   ? 0.3444 0.3183 0.4141 0.0517  0.0459  0.0024  201 A1B2W A C   
2194 O O   . A1B2W C .   ? 0.3480 0.3197 0.4328 0.0572  0.0514  0.0074  201 A1B2W A O   
2195 N N   . A1B2W C .   ? 0.3093 0.2907 0.3732 0.0483  0.0367  0.0056  201 A1B2W A N   
2196 O O2  . A1B2W C .   ? 0.4385 0.3985 0.4576 0.0330  0.0658  -0.0355 201 A1B2W A O2  
2197 C C9  . A1B2W C .   ? 0.4222 0.4020 0.4379 0.0325  0.0671  -0.0334 201 A1B2W A C9  
2198 S S   . A1B2W C .   ? 0.4374 0.4117 0.4631 0.0365  0.0838  -0.0391 201 A1B2W A S   
# 
