data_2ZAY
# 
_entry.id   2ZAY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.387 
_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   2ZAY         pdb_00002zay 10.2210/pdb2zay/pdb 
RCSB  RCSB027742   ?            ?                   
WWPDB D_1000027742 ?            ?                   
# 
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 
1 'Structure model' 1 0 2007-10-23 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2018-11-14 
4 'Structure model' 1 3 2021-02-03 
5 'Structure model' 1 4 2024-02-21 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Source and taxonomy'       
2 2 'Structure model' 'Version format compliance' 
3 3 'Structure model' 'Data collection'           
4 3 'Structure model' 'Structure summary'         
5 4 'Structure model' 'Database references'       
6 4 'Structure model' 'Structure summary'         
7 5 'Structure model' 'Data collection'           
8 5 'Structure model' 'Database references'       
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' audit_author       
2 4 'Structure model' audit_author       
3 4 'Structure model' citation_author    
4 4 'Structure model' struct_ref_seq_dif 
5 5 'Structure model' chem_comp_atom     
6 5 'Structure model' chem_comp_bond     
7 5 'Structure model' database_2         
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_audit_author.identifier_ORCID'      
2 4 'Structure model' '_audit_author.identifier_ORCID'      
3 4 'Structure model' '_citation_author.identifier_ORCID'   
4 4 'Structure model' '_struct_ref_seq_dif.details'         
5 5 'Structure model' '_database_2.pdbx_DOI'                
6 5 'Structure model' '_database_2.pdbx_database_accession' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2ZAY 
_pdbx_database_status.recvd_initial_deposition_date   2007-10-12 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_database_related.db_name        TargetDB 
_pdbx_database_related.db_id          NYSGXRC-11006u 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fedorov, A.A.'                                                  1 ?                   
'Fedorov, E.V.'                                                  2 ?                   
'Meyer, A.'                                                      3 ?                   
'Sauder, J.M.'                                                   4 0000-0002-0254-4955 
'Burley, S.K.'                                                   5 0000-0002-2487-9713 
'Almo, S.C.'                                                     6 ?                   
'New York SGX Research Center for Structural Genomics (NYSGXRC)' 7 ?                   
# 
_citation.id                        primary 
_citation.title                     'Crystal structure of response regulator from Desulfuromonas acetoxidans.' 
_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.ordinal 
_citation_author.identifier_ORCID 
primary 'Fedorov, A.A.' 1 ?                   
primary 'Fedorov, E.V.' 2 ?                   
primary 'Meyer, A.'     3 ?                   
primary 'Sauder, J.M.'  4 ?                   
primary 'Burley, S.K.'  5 0000-0002-2487-9713 
primary 'Almo, S.C.'    6 ?                   
# 
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 'Response regulator receiver protein' 16135.799 2  ? ? 'Residues 150-285' ? 
2 water   nat water                                 18.015    57 ? ? ?                  ? 
# 
_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       
;MSLAEGKWWRIMLVDTQLPALAASISALSQEGFDIIQCGNAIEAVPVAVKTHPHLIITEANMPKISGMDLFNSLKKNPQT
ASIPVIALSGRATAKEEAQLLDMGFIDFIAKPVNAIRLSARIKRVLKLLYEDLSAPPAREGHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSLAEGKWWRIMLVDTQLPALAASISALSQEGFDIIQCGNAIEAVPVAVKTHPHLIITEANMPKISGMDLFNSLKKNPQT
ASIPVIALSGRATAKEEAQLLDMGFIDFIAKPVNAIRLSARIKRVLKLLYEDLSAPPAREGHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         NYSGXRC-11006u 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LEU n 
1 4   ALA n 
1 5   GLU n 
1 6   GLY n 
1 7   LYS n 
1 8   TRP n 
1 9   TRP n 
1 10  ARG n 
1 11  ILE n 
1 12  MET n 
1 13  LEU n 
1 14  VAL n 
1 15  ASP n 
1 16  THR n 
1 17  GLN n 
1 18  LEU n 
1 19  PRO n 
1 20  ALA n 
1 21  LEU n 
1 22  ALA n 
1 23  ALA n 
1 24  SER n 
1 25  ILE n 
1 26  SER n 
1 27  ALA n 
1 28  LEU n 
1 29  SER n 
1 30  GLN n 
1 31  GLU n 
1 32  GLY n 
1 33  PHE n 
1 34  ASP n 
1 35  ILE n 
1 36  ILE n 
1 37  GLN n 
1 38  CYS n 
1 39  GLY n 
1 40  ASN n 
1 41  ALA n 
1 42  ILE n 
1 43  GLU n 
1 44  ALA n 
1 45  VAL n 
1 46  PRO n 
1 47  VAL n 
1 48  ALA n 
1 49  VAL n 
1 50  LYS n 
1 51  THR n 
1 52  HIS n 
1 53  PRO n 
1 54  HIS n 
1 55  LEU n 
1 56  ILE n 
1 57  ILE n 
1 58  THR n 
1 59  GLU n 
1 60  ALA n 
1 61  ASN n 
1 62  MET n 
1 63  PRO n 
1 64  LYS n 
1 65  ILE n 
1 66  SER n 
1 67  GLY n 
1 68  MET n 
1 69  ASP n 
1 70  LEU n 
1 71  PHE n 
1 72  ASN n 
1 73  SER n 
1 74  LEU n 
1 75  LYS n 
1 76  LYS n 
1 77  ASN n 
1 78  PRO n 
1 79  GLN n 
1 80  THR n 
1 81  ALA n 
1 82  SER n 
1 83  ILE n 
1 84  PRO n 
1 85  VAL n 
1 86  ILE n 
1 87  ALA n 
1 88  LEU n 
1 89  SER n 
1 90  GLY n 
1 91  ARG n 
1 92  ALA n 
1 93  THR n 
1 94  ALA n 
1 95  LYS n 
1 96  GLU n 
1 97  GLU n 
1 98  ALA n 
1 99  GLN n 
1 100 LEU n 
1 101 LEU n 
1 102 ASP n 
1 103 MET n 
1 104 GLY n 
1 105 PHE n 
1 106 ILE n 
1 107 ASP n 
1 108 PHE n 
1 109 ILE n 
1 110 ALA n 
1 111 LYS n 
1 112 PRO n 
1 113 VAL n 
1 114 ASN n 
1 115 ALA n 
1 116 ILE n 
1 117 ARG n 
1 118 LEU n 
1 119 SER n 
1 120 ALA n 
1 121 ARG n 
1 122 ILE n 
1 123 LYS n 
1 124 ARG n 
1 125 VAL n 
1 126 LEU n 
1 127 LYS n 
1 128 LEU n 
1 129 LEU n 
1 130 TYR n 
1 131 GLU n 
1 132 ASP n 
1 133 LEU n 
1 134 SER n 
1 135 ALA n 
1 136 PRO n 
1 137 PRO n 
1 138 ALA n 
1 139 ARG n 
1 140 GLU n 
1 141 GLY n 
1 142 HIS n 
1 143 HIS n 
1 144 HIS n 
1 145 HIS n 
1 146 HIS n 
1 147 HIS 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     Desulfuromonas 
_entity_src_gen.pdbx_gene_src_gene                 Dace_1490 
_entity_src_gen.gene_src_species                   'Desulfuromonas acetoxidans' 
_entity_src_gen.gene_src_strain                    'DSM 684' 
_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      'Desulfuromonas acetoxidans' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     281689 
_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                     Escherichia 
_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 
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 
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 
# 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LEU 3   3   ?   ?   ?   A . n 
A 1 4   ALA 4   4   ?   ?   ?   A . n 
A 1 5   GLU 5   5   ?   ?   ?   A . n 
A 1 6   GLY 6   6   ?   ?   ?   A . n 
A 1 7   LYS 7   7   ?   ?   ?   A . n 
A 1 8   TRP 8   8   8   TRP TRP A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  MET 12  12  12  MET MET A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  ASP 15  15  15  ASP ASP A . n 
A 1 16  THR 16  16  16  THR THR A . n 
A 1 17  GLN 17  17  17  GLN GLN A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  PRO 19  19  19  PRO PRO A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  SER 24  24  24  SER SER A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  GLY 32  32  32  GLY GLY A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  GLN 37  37  37  GLN GLN A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  THR 51  51  51  THR THR A . n 
A 1 52  HIS 52  52  52  HIS HIS A . n 
A 1 53  PRO 53  53  53  PRO PRO A . n 
A 1 54  HIS 54  54  54  HIS HIS A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  ILE 56  56  56  ILE ILE A . n 
A 1 57  ILE 57  57  57  ILE ILE A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  GLU 59  59  59  GLU GLU A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  MET 62  62  62  MET MET A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  LYS 64  64  64  LYS LYS A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  SER 66  66  66  SER SER A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  MET 68  68  68  MET MET A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  PHE 71  71  71  PHE PHE A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  SER 82  82  82  SER SER A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  ILE 86  86  86  ILE ILE A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  LYS 95  95  95  LYS LYS A . n 
A 1 96  GLU 96  96  96  GLU GLU A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 MET 103 103 103 MET MET A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 PHE 105 105 105 PHE PHE A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 ASP 107 107 107 ASP ASP A . n 
A 1 108 PHE 108 108 108 PHE PHE A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 ASN 114 114 114 ASN ASN A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ILE 116 116 116 ILE ILE A . n 
A 1 117 ARG 117 117 117 ARG ARG A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 SER 119 119 119 SER SER A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 LYS 123 123 123 LYS LYS A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 TYR 130 130 130 TYR TYR A . n 
A 1 131 GLU 131 131 ?   ?   ?   A . n 
A 1 132 ASP 132 132 ?   ?   ?   A . n 
A 1 133 LEU 133 133 ?   ?   ?   A . n 
A 1 134 SER 134 134 ?   ?   ?   A . n 
A 1 135 ALA 135 135 ?   ?   ?   A . n 
A 1 136 PRO 136 136 ?   ?   ?   A . n 
A 1 137 PRO 137 137 ?   ?   ?   A . n 
A 1 138 ALA 138 138 ?   ?   ?   A . n 
A 1 139 ARG 139 139 ?   ?   ?   A . n 
A 1 140 GLU 140 140 ?   ?   ?   A . n 
A 1 141 GLY 141 141 ?   ?   ?   A . n 
A 1 142 HIS 142 142 ?   ?   ?   A . n 
A 1 143 HIS 143 143 ?   ?   ?   A . n 
A 1 144 HIS 144 144 ?   ?   ?   A . n 
A 1 145 HIS 145 145 ?   ?   ?   A . n 
A 1 146 HIS 146 146 ?   ?   ?   A . n 
A 1 147 HIS 147 147 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LEU 3   3   ?   ?   ?   B . n 
B 1 4   ALA 4   4   ?   ?   ?   B . n 
B 1 5   GLU 5   5   ?   ?   ?   B . n 
B 1 6   GLY 6   6   ?   ?   ?   B . n 
B 1 7   LYS 7   7   ?   ?   ?   B . n 
B 1 8   TRP 8   8   8   TRP TRP B . n 
B 1 9   TRP 9   9   9   TRP TRP B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  ILE 11  11  11  ILE ILE B . n 
B 1 12  MET 12  12  12  MET MET B . n 
B 1 13  LEU 13  13  13  LEU LEU B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  ASP 15  15  15  ASP ASP B . n 
B 1 16  THR 16  16  16  THR THR B . n 
B 1 17  GLN 17  17  17  GLN GLN B . n 
B 1 18  LEU 18  18  18  LEU LEU B . n 
B 1 19  PRO 19  19  19  PRO PRO B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  LEU 21  21  21  LEU LEU B . n 
B 1 22  ALA 22  22  22  ALA ALA B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  SER 24  24  24  SER SER B . n 
B 1 25  ILE 25  25  25  ILE ILE B . n 
B 1 26  SER 26  26  26  SER SER B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LEU 28  28  28  LEU LEU B . n 
B 1 29  SER 29  29  29  SER SER B . n 
B 1 30  GLN 30  30  30  GLN GLN B . n 
B 1 31  GLU 31  31  31  GLU GLU B . n 
B 1 32  GLY 32  32  32  GLY GLY B . n 
B 1 33  PHE 33  33  33  PHE PHE B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  GLN 37  37  37  GLN GLN B . n 
B 1 38  CYS 38  38  38  CYS CYS B . n 
B 1 39  GLY 39  39  39  GLY GLY B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  ILE 42  42  42  ILE ILE B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  VAL 45  45  45  VAL VAL B . n 
B 1 46  PRO 46  46  46  PRO PRO B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  ALA 48  48  48  ALA ALA B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  LYS 50  50  50  LYS LYS B . n 
B 1 51  THR 51  51  51  THR THR B . n 
B 1 52  HIS 52  52  52  HIS HIS B . n 
B 1 53  PRO 53  53  53  PRO PRO B . n 
B 1 54  HIS 54  54  54  HIS HIS B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  ILE 56  56  56  ILE ILE B . n 
B 1 57  ILE 57  57  57  ILE ILE B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  GLU 59  59  59  GLU GLU B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  ASN 61  61  61  ASN ASN B . n 
B 1 62  MET 62  62  62  MET MET B . n 
B 1 63  PRO 63  63  63  PRO PRO B . n 
B 1 64  LYS 64  64  64  LYS LYS B . n 
B 1 65  ILE 65  65  65  ILE ILE B . n 
B 1 66  SER 66  66  66  SER SER B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  MET 68  68  68  MET MET B . n 
B 1 69  ASP 69  69  69  ASP ASP B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  PHE 71  71  71  PHE PHE B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  LEU 74  74  74  LEU LEU B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  ASN 77  77  77  ASN ASN B . n 
B 1 78  PRO 78  78  78  PRO PRO B . n 
B 1 79  GLN 79  79  79  GLN GLN B . n 
B 1 80  THR 80  80  80  THR THR B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  SER 82  82  82  SER SER B . n 
B 1 83  ILE 83  83  83  ILE ILE B . n 
B 1 84  PRO 84  84  84  PRO PRO B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  ILE 86  86  86  ILE ILE B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  SER 89  89  89  SER SER B . n 
B 1 90  GLY 90  90  90  GLY GLY B . n 
B 1 91  ARG 91  91  91  ARG ARG B . n 
B 1 92  ALA 92  92  92  ALA ALA B . n 
B 1 93  THR 93  93  93  THR THR B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  LYS 95  95  95  LYS LYS B . n 
B 1 96  GLU 96  96  96  GLU GLU B . n 
B 1 97  GLU 97  97  97  GLU GLU B . n 
B 1 98  ALA 98  98  98  ALA ALA B . n 
B 1 99  GLN 99  99  99  GLN GLN B . n 
B 1 100 LEU 100 100 100 LEU LEU B . n 
B 1 101 LEU 101 101 101 LEU LEU B . n 
B 1 102 ASP 102 102 102 ASP ASP B . n 
B 1 103 MET 103 103 103 MET MET B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 PHE 105 105 105 PHE PHE B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 ASP 107 107 107 ASP ASP B . n 
B 1 108 PHE 108 108 108 PHE PHE B . n 
B 1 109 ILE 109 109 109 ILE ILE B . n 
B 1 110 ALA 110 110 110 ALA ALA B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 PRO 112 112 112 PRO PRO B . n 
B 1 113 VAL 113 113 113 VAL VAL B . n 
B 1 114 ASN 114 114 114 ASN ASN B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 ILE 116 116 116 ILE ILE B . n 
B 1 117 ARG 117 117 117 ARG ARG B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 SER 119 119 119 SER SER B . n 
B 1 120 ALA 120 120 120 ALA ALA B . n 
B 1 121 ARG 121 121 121 ARG ARG B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 LYS 123 123 123 LYS LYS B . n 
B 1 124 ARG 124 124 124 ARG ARG B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LYS 127 127 127 LYS LYS B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 TYR 130 130 130 TYR TYR B . n 
B 1 131 GLU 131 131 ?   ?   ?   B . n 
B 1 132 ASP 132 132 ?   ?   ?   B . n 
B 1 133 LEU 133 133 ?   ?   ?   B . n 
B 1 134 SER 134 134 ?   ?   ?   B . n 
B 1 135 ALA 135 135 ?   ?   ?   B . n 
B 1 136 PRO 136 136 ?   ?   ?   B . n 
B 1 137 PRO 137 137 ?   ?   ?   B . n 
B 1 138 ALA 138 138 ?   ?   ?   B . n 
B 1 139 ARG 139 139 ?   ?   ?   B . n 
B 1 140 GLU 140 140 ?   ?   ?   B . n 
B 1 141 GLY 141 141 ?   ?   ?   B . n 
B 1 142 HIS 142 142 ?   ?   ?   B . n 
B 1 143 HIS 143 143 ?   ?   ?   B . n 
B 1 144 HIS 144 144 ?   ?   ?   B . n 
B 1 145 HIS 145 145 ?   ?   ?   B . n 
B 1 146 HIS 146 146 ?   ?   ?   B . n 
B 1 147 HIS 147 147 ?   ?   ?   B . n 
# 
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 HOH 1  148 1   HOH HOH A . 
C 2 HOH 2  149 7   HOH HOH A . 
C 2 HOH 3  150 8   HOH HOH A . 
C 2 HOH 4  151 9   HOH HOH A . 
C 2 HOH 5  152 11  HOH HOH A . 
C 2 HOH 6  153 12  HOH HOH A . 
C 2 HOH 7  154 13  HOH HOH A . 
C 2 HOH 8  155 14  HOH HOH A . 
C 2 HOH 9  156 15  HOH HOH A . 
C 2 HOH 10 157 17  HOH HOH A . 
C 2 HOH 11 158 20  HOH HOH A . 
C 2 HOH 12 159 24  HOH HOH A . 
C 2 HOH 13 160 34  HOH HOH A . 
C 2 HOH 14 161 36  HOH HOH A . 
C 2 HOH 15 162 37  HOH HOH A . 
C 2 HOH 16 163 38  HOH HOH A . 
C 2 HOH 17 164 39  HOH HOH A . 
C 2 HOH 18 165 42  HOH HOH A . 
C 2 HOH 19 166 43  HOH HOH A . 
C 2 HOH 20 167 44  HOH HOH A . 
C 2 HOH 21 168 45  HOH HOH A . 
C 2 HOH 22 169 46  HOH HOH A . 
C 2 HOH 23 170 49  HOH HOH A . 
C 2 HOH 24 171 50  HOH HOH A . 
C 2 HOH 25 172 52  HOH HOH A . 
C 2 HOH 26 173 53  HOH HOH A . 
C 2 HOH 27 174 57  HOH HOH A . 
C 2 HOH 28 175 75  HOH HOH A . 
C 2 HOH 29 176 77  HOH HOH A . 
C 2 HOH 30 177 78  HOH HOH A . 
C 2 HOH 31 178 81  HOH HOH A . 
D 2 HOH 1  148 2   HOH HOH B . 
D 2 HOH 2  149 3   HOH HOH B . 
D 2 HOH 3  150 4   HOH HOH B . 
D 2 HOH 4  151 5   HOH HOH B . 
D 2 HOH 5  152 6   HOH HOH B . 
D 2 HOH 6  153 10  HOH HOH B . 
D 2 HOH 7  154 16  HOH HOH B . 
D 2 HOH 8  155 21  HOH HOH B . 
D 2 HOH 9  156 25  HOH HOH B . 
D 2 HOH 10 157 26  HOH HOH B . 
D 2 HOH 11 158 27  HOH HOH B . 
D 2 HOH 12 159 28  HOH HOH B . 
D 2 HOH 13 160 29  HOH HOH B . 
D 2 HOH 14 161 30  HOH HOH B . 
D 2 HOH 15 162 31  HOH HOH B . 
D 2 HOH 16 163 32  HOH HOH B . 
D 2 HOH 17 164 33  HOH HOH B . 
D 2 HOH 18 165 35  HOH HOH B . 
D 2 HOH 19 166 47  HOH HOH B . 
D 2 HOH 20 167 55  HOH HOH B . 
D 2 HOH 21 168 66  HOH HOH B . 
D 2 HOH 22 169 68  HOH HOH B . 
D 2 HOH 23 170 72  HOH HOH B . 
D 2 HOH 24 171 74  HOH HOH B . 
D 2 HOH 25 172 83  HOH HOH B . 
D 2 HOH 26 173 146 HOH HOH B . 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CNS       refinement        1.1     ? 1 
ADSC      'data collection' Quantum ? 2 
DENZO     'data reduction'  .       ? 3 
SCALEPACK 'data scaling'    .       ? 4 
SHELX     phasing           .       ? 5 
# 
_cell.entry_id           2ZAY 
_cell.length_a           47.215 
_cell.length_b           59.016 
_cell.length_c           88.967 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2ZAY 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
# 
_exptl.entry_id          2ZAY 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      1.92 
_exptl_crystal.density_percent_sol   35.95 
_exptl_crystal.description           'The structure factor file contains Friedel pairs' 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pdbx_details    '3.5 M Sodium formate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 4' 
_diffrn_detector.pdbx_collection_date   2007-09-15 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Si 111 CHANNEL' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97915 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'NSLS BEAMLINE X4A' 
_diffrn_source.pdbx_synchrotron_site       NSLS 
_diffrn_source.pdbx_synchrotron_beamline   X4A 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.97915 
# 
_reflns.entry_id                     2ZAY 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.observed_criterion_sigma_F   0.0 
_reflns.d_resolution_low             25.0 
_reflns.d_resolution_high            2.0 
_reflns.number_obs                   17384 
_reflns.number_all                   17384 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.083 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        17.7 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_refine.entry_id                                 2ZAY 
_refine.ls_number_reflns_obs                     17384 
_refine.ls_number_reflns_all                     17384 
_refine.pdbx_ls_sigma_I                          0.0 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               1867229.72 
_refine.pdbx_data_cutoff_low_absF                0.000000 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             24.59 
_refine.ls_d_res_high                            2.00 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_R_factor_obs                          0.225 
_refine.ls_R_factor_all                          0.225 
_refine.ls_R_factor_R_work                       0.225 
_refine.ls_R_factor_R_free                       0.261 
_refine.ls_R_factor_R_free_error                 0.009 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  891 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               31.2 
_refine.aniso_B[1][1]                            -2.78 
_refine.aniso_B[2][2]                            8.87 
_refine.aniso_B[3][3]                            -6.09 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.solvent_model_param_ksol                 0.394229 
_refine.solvent_model_param_bsol                 49.0604 
_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                                  'The Friedel pairs were used in phasing' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          SAD 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_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.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        2ZAY 
_refine_analyze.Luzzati_coordinate_error_obs    0.25 
_refine_analyze.Luzzati_sigma_a_obs             0.16 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.30 
_refine_analyze.Luzzati_sigma_a_free            0.17 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1888 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             57 
_refine_hist.number_atoms_total               1945 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        24.59 
# 
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 
c_bond_d           0.007 ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg        1.3   ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d 22.7  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d 0.74  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it        1.46  1.50 ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it       2.29  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it        2.35  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it       3.44  2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   10 
_refine_ls_shell.d_res_high                       2.00 
_refine_ls_shell.d_res_low                        2.07 
_refine_ls_shell.number_reflns_R_work             1620 
_refine_ls_shell.R_factor_R_work                  0.256 
_refine_ls_shell.percent_reflns_obs               99.9 
_refine_ls_shell.R_factor_R_free                  0.309 
_refine_ls_shell.R_factor_R_free_error            0.034 
_refine_ls_shell.percent_reflns_R_free            4.9 
_refine_ls_shell.number_reflns_R_free             83 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 protein_rep.param      protein.top           'X-RAY DIFFRACTION' 
2 water_rep.param        water.top             'X-RAY DIFFRACTION' 
3 ion.param              ion.top               'X-RAY DIFFRACTION' 
4 &_1_PARAMETER_INFILE_4 &_1_TOPOLOGY_INFILE_4 'X-RAY DIFFRACTION' 
5 &_1_PARAMETER_INFILE_5 &_1_TOPOLOGY_INFILE_5 'X-RAY DIFFRACTION' 
# 
_database_PDB_matrix.entry_id          2ZAY 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_struct.entry_id                  2ZAY 
_struct.title                     'Crystal structure of response regulator from Desulfuromonas acetoxidans' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2ZAY 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
_struct_keywords.text            
;Structural genomics, NYSGXRC, target 11006u, response regulator, PSI-2, Protein Structure Initiative, New York SGX Research Center for Structural Genomics, SIGNALING 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 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q1JZD9_DESAC 
_struct_ref.pdbx_db_accession          Q1JZD9 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AEGKWWRIMLVDTQLPALAASISALSQEGFDIIQCGNAIEAVPVAVKTHPHLIITEANMPKISGMDLFNSLKKNPQTASI
PVIALSGRATAKEEAQLLDMGFIDFIAKPVNAIRLSARIKRVLKLLYEDLSAPPAR
;
_struct_ref.pdbx_align_begin           150 
_struct_ref.pdbx_db_isoform            ? 
# 
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 2ZAY A 4 ? 139 ? Q1JZD9 150 ? 285 ? 4 139 
2 1 2ZAY B 4 ? 139 ? Q1JZD9 150 ? 285 ? 4 139 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 2ZAY MET A 1   ? UNP Q1JZD9 ? ? 'expression tag' 1   1  
1 2ZAY SER A 2   ? UNP Q1JZD9 ? ? 'expression tag' 2   2  
1 2ZAY LEU A 3   ? UNP Q1JZD9 ? ? 'expression tag' 3   3  
1 2ZAY GLU A 140 ? UNP Q1JZD9 ? ? 'expression tag' 140 4  
1 2ZAY GLY A 141 ? UNP Q1JZD9 ? ? 'expression tag' 141 5  
1 2ZAY HIS A 142 ? UNP Q1JZD9 ? ? 'expression tag' 142 6  
1 2ZAY HIS A 143 ? UNP Q1JZD9 ? ? 'expression tag' 143 7  
1 2ZAY HIS A 144 ? UNP Q1JZD9 ? ? 'expression tag' 144 8  
1 2ZAY HIS A 145 ? UNP Q1JZD9 ? ? 'expression tag' 145 9  
1 2ZAY HIS A 146 ? UNP Q1JZD9 ? ? 'expression tag' 146 10 
1 2ZAY HIS A 147 ? UNP Q1JZD9 ? ? 'expression tag' 147 11 
2 2ZAY MET B 1   ? UNP Q1JZD9 ? ? 'expression tag' 1   12 
2 2ZAY SER B 2   ? UNP Q1JZD9 ? ? 'expression tag' 2   13 
2 2ZAY LEU B 3   ? UNP Q1JZD9 ? ? 'expression tag' 3   14 
2 2ZAY GLU B 140 ? UNP Q1JZD9 ? ? 'expression tag' 140 15 
2 2ZAY GLY B 141 ? UNP Q1JZD9 ? ? 'expression tag' 141 16 
2 2ZAY HIS B 142 ? UNP Q1JZD9 ? ? 'expression tag' 142 17 
2 2ZAY HIS B 143 ? UNP Q1JZD9 ? ? 'expression tag' 143 18 
2 2ZAY HIS B 144 ? UNP Q1JZD9 ? ? 'expression tag' 144 19 
2 2ZAY HIS B 145 ? UNP Q1JZD9 ? ? 'expression tag' 145 20 
2 2ZAY HIS B 146 ? UNP Q1JZD9 ? ? 'expression tag' 146 21 
2 2ZAY HIS B 147 ? UNP Q1JZD9 ? ? 'expression tag' 147 22 
# 
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_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA 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 
2 1 B,D 
# 
_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 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  1  GLN A 17  ? ALA A 20  ? GLN A 17  ALA A 20  5 ? 4  
HELX_P HELX_P2  2  LEU A 21  ? GLY A 32  ? LEU A 21  GLY A 32  1 ? 12 
HELX_P HELX_P3  3  ASN A 40  ? HIS A 52  ? ASN A 40  HIS A 52  1 ? 13 
HELX_P HELX_P4  4  SER A 66  ? LYS A 76  ? SER A 66  LYS A 76  1 ? 11 
HELX_P HELX_P5  5  THR A 93  ? GLY A 104 ? THR A 93  GLY A 104 1 ? 12 
HELX_P HELX_P6  6  ASN A 114 ? TYR A 130 ? ASN A 114 TYR A 130 1 ? 17 
HELX_P HELX_P7  7  GLN B 17  ? ALA B 20  ? GLN B 17  ALA B 20  5 ? 4  
HELX_P HELX_P8  8  LEU B 21  ? GLY B 32  ? LEU B 21  GLY B 32  1 ? 12 
HELX_P HELX_P9  9  ASN B 40  ? HIS B 52  ? ASN B 40  HIS B 52  1 ? 13 
HELX_P HELX_P10 10 ASP B 69  ? LYS B 76  ? ASP B 69  LYS B 76  1 ? 8  
HELX_P HELX_P11 11 THR B 93  ? GLY B 104 ? THR B 93  GLY B 104 1 ? 12 
HELX_P HELX_P12 12 ASN B 114 ? TYR B 130 ? ASN B 114 TYR B 130 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LYS 111 A . ? LYS 111 A PRO 112 A ? PRO 112 A 1 -0.23 
2 LYS 111 B . ? LYS 111 B PRO 112 B ? PRO 112 B 1 0.02  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 5 ? 
# 
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 
A 1 2 ? parallel 
A 2 3 ? parallel 
A 3 4 ? parallel 
A 4 5 ? parallel 
B 1 2 ? parallel 
B 2 3 ? parallel 
B 3 4 ? parallel 
B 4 5 ? 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 
A 1 PHE A 33  ? CYS A 38  ? PHE A 33  CYS A 38  
A 2 TRP A 9   ? VAL A 14  ? TRP A 9   VAL A 14  
A 3 LEU A 55  ? GLU A 59  ? LEU A 55  GLU A 59  
A 4 VAL A 85  ? SER A 89  ? VAL A 85  SER A 89  
A 5 ASP A 107 ? ALA A 110 ? ASP A 107 ALA A 110 
B 1 ASP B 34  ? CYS B 38  ? ASP B 34  CYS B 38  
B 2 ARG B 10  ? VAL B 14  ? ARG B 10  VAL B 14  
B 3 LEU B 55  ? GLU B 59  ? LEU B 55  GLU B 59  
B 4 VAL B 85  ? SER B 89  ? VAL B 85  SER B 89  
B 5 ASP B 107 ? ALA B 110 ? ASP B 107 ALA B 110 
# 
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 
A 1 2 O ILE A 36 ? O ILE A 36 N LEU A 13  ? N LEU A 13  
A 2 3 N VAL A 14 ? N VAL A 14 O ILE A 57  ? O ILE A 57  
A 3 4 N ILE A 56 ? N ILE A 56 O ILE A 86  ? O ILE A 86  
A 4 5 N ALA A 87 ? N ALA A 87 O ILE A 109 ? O ILE A 109 
B 1 2 O ILE B 36 ? O ILE B 36 N LEU B 13  ? N LEU B 13  
B 2 3 N MET B 12 ? N MET B 12 O ILE B 57  ? O ILE B 57  
B 3 4 N ILE B 56 ? N ILE B 56 O ILE B 86  ? O ILE B 86  
B 4 5 N ALA B 87 ? N ALA B 87 O ILE B 109 ? O ILE B 109 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     161 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     170 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_455 
_pdbx_validate_symm_contact.dist              2.18 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    LYS 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     64 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             73.20 
_pdbx_validate_torsion.psi             -71.69 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'PSI, Protein Structure Initiative' 
_pdbx_SG_project.full_name_of_center   'New York SGX Research Center for Structural Genomics' 
_pdbx_SG_project.initial_of_center     NYSGXRC 
# 
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 MET 1   ? A MET 1   
2  1 Y 1 A SER 2   ? A SER 2   
3  1 Y 1 A LEU 3   ? A LEU 3   
4  1 Y 1 A ALA 4   ? A ALA 4   
5  1 Y 1 A GLU 5   ? A GLU 5   
6  1 Y 1 A GLY 6   ? A GLY 6   
7  1 Y 1 A LYS 7   ? A LYS 7   
8  1 Y 1 A GLU 131 ? A GLU 131 
9  1 Y 1 A ASP 132 ? A ASP 132 
10 1 Y 1 A LEU 133 ? A LEU 133 
11 1 Y 1 A SER 134 ? A SER 134 
12 1 Y 1 A ALA 135 ? A ALA 135 
13 1 Y 1 A PRO 136 ? A PRO 136 
14 1 Y 1 A PRO 137 ? A PRO 137 
15 1 Y 1 A ALA 138 ? A ALA 138 
16 1 Y 1 A ARG 139 ? A ARG 139 
17 1 Y 1 A GLU 140 ? A GLU 140 
18 1 Y 1 A GLY 141 ? A GLY 141 
19 1 Y 1 A HIS 142 ? A HIS 142 
20 1 Y 1 A HIS 143 ? A HIS 143 
21 1 Y 1 A HIS 144 ? A HIS 144 
22 1 Y 1 A HIS 145 ? A HIS 145 
23 1 Y 1 A HIS 146 ? A HIS 146 
24 1 Y 1 A HIS 147 ? A HIS 147 
25 1 Y 1 B MET 1   ? B MET 1   
26 1 Y 1 B SER 2   ? B SER 2   
27 1 Y 1 B LEU 3   ? B LEU 3   
28 1 Y 1 B ALA 4   ? B ALA 4   
29 1 Y 1 B GLU 5   ? B GLU 5   
30 1 Y 1 B GLY 6   ? B GLY 6   
31 1 Y 1 B LYS 7   ? B LYS 7   
32 1 Y 1 B GLU 131 ? B GLU 131 
33 1 Y 1 B ASP 132 ? B ASP 132 
34 1 Y 1 B LEU 133 ? B LEU 133 
35 1 Y 1 B SER 134 ? B SER 134 
36 1 Y 1 B ALA 135 ? B ALA 135 
37 1 Y 1 B PRO 136 ? B PRO 136 
38 1 Y 1 B PRO 137 ? B PRO 137 
39 1 Y 1 B ALA 138 ? B ALA 138 
40 1 Y 1 B ARG 139 ? B ARG 139 
41 1 Y 1 B GLU 140 ? B GLU 140 
42 1 Y 1 B GLY 141 ? B GLY 141 
43 1 Y 1 B HIS 142 ? B HIS 142 
44 1 Y 1 B HIS 143 ? B HIS 143 
45 1 Y 1 B HIS 144 ? B HIS 144 
46 1 Y 1 B HIS 145 ? B HIS 145 
47 1 Y 1 B HIS 146 ? B HIS 146 
48 1 Y 1 B HIS 147 ? B HIS 147 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_atom_sites.entry_id                    2ZAY 
_atom_sites.fract_transf_matrix[1][1]   0.021180 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016945 
_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]   0.011240 
_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 
# 
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   . TRP A 1 8   ? 37.625 28.204  15.069  1.00 46.12 ? 8   TRP A N   1 
ATOM   2    C CA  . TRP A 1 8   ? 36.238 28.364  15.603  1.00 46.08 ? 8   TRP A CA  1 
ATOM   3    C C   . TRP A 1 8   ? 35.393 27.170  15.174  1.00 42.72 ? 8   TRP A C   1 
ATOM   4    O O   . TRP A 1 8   ? 34.738 27.211  14.133  1.00 43.10 ? 8   TRP A O   1 
ATOM   5    C CB  . TRP A 1 8   ? 35.612 29.657  15.066  1.00 50.35 ? 8   TRP A CB  1 
ATOM   6    C CG  . TRP A 1 8   ? 34.300 30.016  15.716  1.00 55.25 ? 8   TRP A CG  1 
ATOM   7    C CD1 . TRP A 1 8   ? 33.144 29.283  15.703  1.00 55.84 ? 8   TRP A CD1 1 
ATOM   8    C CD2 . TRP A 1 8   ? 34.017 31.192  16.486  1.00 57.20 ? 8   TRP A CD2 1 
ATOM   9    N NE1 . TRP A 1 8   ? 32.163 29.928  16.418  1.00 56.13 ? 8   TRP A NE1 1 
ATOM   10   C CE2 . TRP A 1 8   ? 32.671 31.102  16.910  1.00 57.96 ? 8   TRP A CE2 1 
ATOM   11   C CE3 . TRP A 1 8   ? 34.771 32.315  16.861  1.00 58.62 ? 8   TRP A CE3 1 
ATOM   12   C CZ2 . TRP A 1 8   ? 32.061 32.094  17.691  1.00 57.97 ? 8   TRP A CZ2 1 
ATOM   13   C CZ3 . TRP A 1 8   ? 34.164 33.300  17.637  1.00 58.74 ? 8   TRP A CZ3 1 
ATOM   14   C CH2 . TRP A 1 8   ? 32.821 33.181  18.043  1.00 58.85 ? 8   TRP A CH2 1 
ATOM   15   N N   . TRP A 1 9   ? 35.418 26.106  15.972  1.00 38.64 ? 9   TRP A N   1 
ATOM   16   C CA  . TRP A 1 9   ? 34.650 24.907  15.651  1.00 32.40 ? 9   TRP A CA  1 
ATOM   17   C C   . TRP A 1 9   ? 33.436 24.727  16.561  1.00 29.43 ? 9   TRP A C   1 
ATOM   18   O O   . TRP A 1 9   ? 33.579 24.550  17.777  1.00 29.62 ? 9   TRP A O   1 
ATOM   19   C CB  . TRP A 1 9   ? 35.539 23.667  15.745  1.00 31.20 ? 9   TRP A CB  1 
ATOM   20   C CG  . TRP A 1 9   ? 36.674 23.632  14.747  1.00 31.96 ? 9   TRP A CG  1 
ATOM   21   C CD1 . TRP A 1 9   ? 38.002 23.808  15.008  1.00 32.48 ? 9   TRP A CD1 1 
ATOM   22   C CD2 . TRP A 1 9   ? 36.574 23.376  13.338  1.00 30.44 ? 9   TRP A CD2 1 
ATOM   23   N NE1 . TRP A 1 9   ? 38.737 23.672  13.852  1.00 31.81 ? 9   TRP A NE1 1 
ATOM   24   C CE2 . TRP A 1 9   ? 37.885 23.407  12.813  1.00 30.58 ? 9   TRP A CE2 1 
ATOM   25   C CE3 . TRP A 1 9   ? 35.503 23.123  12.471  1.00 29.61 ? 9   TRP A CE3 1 
ATOM   26   C CZ2 . TRP A 1 9   ? 38.157 23.192  11.459  1.00 31.31 ? 9   TRP A CZ2 1 
ATOM   27   C CZ3 . TRP A 1 9   ? 35.774 22.908  11.118  1.00 30.92 ? 9   TRP A CZ3 1 
ATOM   28   C CH2 . TRP A 1 9   ? 37.093 22.944  10.628  1.00 31.09 ? 9   TRP A CH2 1 
ATOM   29   N N   . ARG A 1 10  ? 32.245 24.772  15.967  1.00 25.61 ? 10  ARG A N   1 
ATOM   30   C CA  . ARG A 1 10  ? 31.005 24.592  16.715  1.00 24.16 ? 10  ARG A CA  1 
ATOM   31   C C   . ARG A 1 10  ? 30.711 23.103  16.725  1.00 23.43 ? 10  ARG A C   1 
ATOM   32   O O   . ARG A 1 10  ? 30.636 22.478  15.668  1.00 21.00 ? 10  ARG A O   1 
ATOM   33   C CB  . ARG A 1 10  ? 29.831 25.307  16.036  1.00 23.82 ? 10  ARG A CB  1 
ATOM   34   C CG  . ARG A 1 10  ? 30.030 26.798  15.802  1.00 28.91 ? 10  ARG A CG  1 
ATOM   35   C CD  . ARG A 1 10  ? 28.954 27.349  14.855  1.00 31.66 ? 10  ARG A CD  1 
ATOM   36   N NE  . ARG A 1 10  ? 29.505 28.417  14.028  1.00 38.72 ? 10  ARG A NE  1 
ATOM   37   C CZ  . ARG A 1 10  ? 29.651 28.353  12.711  1.00 38.39 ? 10  ARG A CZ  1 
ATOM   38   N NH1 . ARG A 1 10  ? 29.281 27.270  12.038  1.00 36.10 ? 10  ARG A NH1 1 
ATOM   39   N NH2 . ARG A 1 10  ? 30.187 29.380  12.063  1.00 44.59 ? 10  ARG A NH2 1 
ATOM   40   N N   . ILE A 1 11  ? 30.537 22.541  17.914  1.00 22.83 ? 11  ILE A N   1 
ATOM   41   C CA  . ILE A 1 11  ? 30.251 21.120  18.041  1.00 22.34 ? 11  ILE A CA  1 
ATOM   42   C C   . ILE A 1 11  ? 28.976 20.939  18.858  1.00 23.77 ? 11  ILE A C   1 
ATOM   43   O O   . ILE A 1 11  ? 28.925 21.367  20.006  1.00 24.45 ? 11  ILE A O   1 
ATOM   44   C CB  . ILE A 1 11  ? 31.406 20.387  18.773  1.00 23.61 ? 11  ILE A CB  1 
ATOM   45   C CG1 . ILE A 1 11  ? 32.738 20.653  18.066  1.00 22.39 ? 11  ILE A CG1 1 
ATOM   46   C CG2 . ILE A 1 11  ? 31.119 18.889  18.834  1.00 24.26 ? 11  ILE A CG2 1 
ATOM   47   C CD1 . ILE A 1 11  ? 32.869 20.001  16.701  1.00 25.21 ? 11  ILE A CD1 1 
ATOM   48   N N   . MET A 1 12  ? 27.945 20.331  18.279  1.00 21.46 ? 12  MET A N   1 
ATOM   49   C CA  . MET A 1 12  ? 26.721 20.106  19.045  1.00 23.43 ? 12  MET A CA  1 
ATOM   50   C C   . MET A 1 12  ? 26.768 18.712  19.655  1.00 23.60 ? 12  MET A C   1 
ATOM   51   O O   . MET A 1 12  ? 27.095 17.742  18.977  1.00 25.77 ? 12  MET A O   1 
ATOM   52   C CB  . MET A 1 12  ? 25.469 20.242  18.167  1.00 23.53 ? 12  MET A CB  1 
ATOM   53   C CG  . MET A 1 12  ? 24.149 19.907  18.906  1.00 25.13 ? 12  MET A CG  1 
ATOM   54   S SD  . MET A 1 12  ? 22.604 20.161  17.932  1.00 21.40 ? 12  MET A SD  1 
ATOM   55   C CE  . MET A 1 12  ? 22.641 21.794  17.729  1.00 26.23 ? 12  MET A CE  1 
ATOM   56   N N   . LEU A 1 13  ? 26.458 18.620  20.944  1.00 22.17 ? 13  LEU A N   1 
ATOM   57   C CA  . LEU A 1 13  ? 26.445 17.335  21.641  1.00 23.66 ? 13  LEU A CA  1 
ATOM   58   C C   . LEU A 1 13  ? 25.029 17.070  22.164  1.00 22.72 ? 13  LEU A C   1 
ATOM   59   O O   . LEU A 1 13  ? 24.474 17.896  22.882  1.00 24.33 ? 13  LEU A O   1 
ATOM   60   C CB  . LEU A 1 13  ? 27.435 17.375  22.806  1.00 24.74 ? 13  LEU A CB  1 
ATOM   61   C CG  . LEU A 1 13  ? 27.479 16.193  23.770  1.00 29.61 ? 13  LEU A CG  1 
ATOM   62   C CD1 . LEU A 1 13  ? 27.862 14.931  23.017  1.00 29.40 ? 13  LEU A CD1 1 
ATOM   63   C CD2 . LEU A 1 13  ? 28.492 16.486  24.879  1.00 29.78 ? 13  LEU A CD2 1 
ATOM   64   N N   . VAL A 1 14  ? 24.454 15.924  21.803  1.00 21.69 ? 14  VAL A N   1 
ATOM   65   C CA  . VAL A 1 14  ? 23.100 15.556  22.230  1.00 21.54 ? 14  VAL A CA  1 
ATOM   66   C C   . VAL A 1 14  ? 23.176 14.280  23.078  1.00 23.73 ? 14  VAL A C   1 
ATOM   67   O O   . VAL A 1 14  ? 23.605 13.232  22.593  1.00 22.65 ? 14  VAL A O   1 
ATOM   68   C CB  . VAL A 1 14  ? 22.181 15.265  21.010  1.00 21.36 ? 14  VAL A CB  1 
ATOM   69   C CG1 . VAL A 1 14  ? 20.728 15.202  21.463  1.00 20.57 ? 14  VAL A CG1 1 
ATOM   70   C CG2 . VAL A 1 14  ? 22.367 16.322  19.936  1.00 21.23 ? 14  VAL A CG2 1 
ATOM   71   N N   . ASP A 1 15  ? 22.763 14.361  24.339  1.00 24.53 ? 15  ASP A N   1 
ATOM   72   C CA  . ASP A 1 15  ? 22.815 13.194  25.225  1.00 26.93 ? 15  ASP A CA  1 
ATOM   73   C C   . ASP A 1 15  ? 21.763 13.361  26.318  1.00 27.83 ? 15  ASP A C   1 
ATOM   74   O O   . ASP A 1 15  ? 21.517 14.480  26.772  1.00 26.30 ? 15  ASP A O   1 
ATOM   75   C CB  . ASP A 1 15  ? 24.205 13.076  25.860  1.00 28.15 ? 15  ASP A CB  1 
ATOM   76   C CG  . ASP A 1 15  ? 24.458 11.700  26.467  1.00 33.27 ? 15  ASP A CG  1 
ATOM   77   O OD1 . ASP A 1 15  ? 24.925 10.803  25.738  1.00 34.10 ? 15  ASP A OD1 1 
ATOM   78   O OD2 . ASP A 1 15  ? 24.178 11.512  27.668  1.00 34.81 ? 15  ASP A OD2 1 
ATOM   79   N N   . THR A 1 16  ? 21.147 12.259  26.742  1.00 28.55 ? 16  THR A N   1 
ATOM   80   C CA  . THR A 1 16  ? 20.114 12.324  27.770  1.00 31.18 ? 16  THR A CA  1 
ATOM   81   C C   . THR A 1 16  ? 20.673 12.447  29.190  1.00 33.87 ? 16  THR A C   1 
ATOM   82   O O   . THR A 1 16  ? 19.922 12.656  30.144  1.00 35.59 ? 16  THR A O   1 
ATOM   83   C CB  . THR A 1 16  ? 19.157 11.106  27.690  1.00 31.57 ? 16  THR A CB  1 
ATOM   84   O OG1 . THR A 1 16  ? 19.911 9.890   27.753  1.00 28.59 ? 16  THR A OG1 1 
ATOM   85   C CG2 . THR A 1 16  ? 18.359 11.139  26.389  1.00 30.51 ? 16  THR A CG2 1 
ATOM   86   N N   . GLN A 1 17  ? 21.986 12.311  29.332  1.00 35.22 ? 17  GLN A N   1 
ATOM   87   C CA  . GLN A 1 17  ? 22.624 12.456  30.636  1.00 37.88 ? 17  GLN A CA  1 
ATOM   88   C C   . GLN A 1 17  ? 23.911 13.258  30.479  1.00 36.56 ? 17  GLN A C   1 
ATOM   89   O O   . GLN A 1 17  ? 25.018 12.760  30.709  1.00 36.76 ? 17  GLN A O   1 
ATOM   90   C CB  . GLN A 1 17  ? 22.898 11.084  31.273  1.00 41.39 ? 17  GLN A CB  1 
ATOM   91   C CG  . GLN A 1 17  ? 23.816 10.177  30.486  1.00 47.87 ? 17  GLN A CG  1 
ATOM   92   C CD  . GLN A 1 17  ? 23.680 8.720   30.899  1.00 51.89 ? 17  GLN A CD  1 
ATOM   93   O OE1 . GLN A 1 17  ? 22.587 8.149   30.853  1.00 53.94 ? 17  GLN A OE1 1 
ATOM   94   N NE2 . GLN A 1 17  ? 24.793 8.108   31.299  1.00 54.89 ? 17  GLN A NE2 1 
ATOM   95   N N   . LEU A 1 18  ? 23.741 14.514  30.074  1.00 35.59 ? 18  LEU A N   1 
ATOM   96   C CA  . LEU A 1 18  ? 24.851 15.438  29.869  1.00 35.35 ? 18  LEU A CA  1 
ATOM   97   C C   . LEU A 1 18  ? 25.771 15.575  31.083  1.00 37.19 ? 18  LEU A C   1 
ATOM   98   O O   . LEU A 1 18  ? 26.984 15.729  30.933  1.00 38.12 ? 18  LEU A O   1 
ATOM   99   C CB  . LEU A 1 18  ? 24.310 16.813  29.465  1.00 33.33 ? 18  LEU A CB  1 
ATOM   100  C CG  . LEU A 1 18  ? 23.735 16.905  28.046  1.00 31.17 ? 18  LEU A CG  1 
ATOM   101  C CD1 . LEU A 1 18  ? 22.996 18.220  27.860  1.00 29.37 ? 18  LEU A CD1 1 
ATOM   102  C CD2 . LEU A 1 18  ? 24.872 16.782  27.033  1.00 30.97 ? 18  LEU A CD2 1 
ATOM   103  N N   . PRO A 1 19  ? 25.208 15.539  32.303  1.00 38.10 ? 19  PRO A N   1 
ATOM   104  C CA  . PRO A 1 19  ? 26.053 15.661  33.495  1.00 38.77 ? 19  PRO A CA  1 
ATOM   105  C C   . PRO A 1 19  ? 27.166 14.611  33.520  1.00 39.28 ? 19  PRO A C   1 
ATOM   106  O O   . PRO A 1 19  ? 28.275 14.877  33.979  1.00 40.88 ? 19  PRO A O   1 
ATOM   107  C CB  . PRO A 1 19  ? 25.057 15.478  34.635  1.00 38.76 ? 19  PRO A CB  1 
ATOM   108  C CG  . PRO A 1 19  ? 23.822 16.112  34.084  1.00 38.69 ? 19  PRO A CG  1 
ATOM   109  C CD  . PRO A 1 19  ? 23.780 15.564  32.672  1.00 37.97 ? 19  PRO A CD  1 
ATOM   110  N N   . ALA A 1 20  ? 26.866 13.420  33.016  1.00 39.90 ? 20  ALA A N   1 
ATOM   111  C CA  . ALA A 1 20  ? 27.847 12.341  32.987  1.00 41.10 ? 20  ALA A CA  1 
ATOM   112  C C   . ALA A 1 20  ? 29.005 12.644  32.040  1.00 41.71 ? 20  ALA A C   1 
ATOM   113  O O   . ALA A 1 20  ? 30.082 12.056  32.165  1.00 42.66 ? 20  ALA A O   1 
ATOM   114  C CB  . ALA A 1 20  ? 27.177 11.036  32.581  1.00 41.41 ? 20  ALA A CB  1 
ATOM   115  N N   . LEU A 1 21  ? 28.785 13.559  31.097  1.00 40.37 ? 21  LEU A N   1 
ATOM   116  C CA  . LEU A 1 21  ? 29.821 13.924  30.134  1.00 39.85 ? 21  LEU A CA  1 
ATOM   117  C C   . LEU A 1 21  ? 30.515 15.235  30.487  1.00 38.91 ? 21  LEU A C   1 
ATOM   118  O O   . LEU A 1 21  ? 31.464 15.641  29.816  1.00 38.01 ? 21  LEU A O   1 
ATOM   119  C CB  . LEU A 1 21  ? 29.223 14.027  28.727  1.00 39.57 ? 21  LEU A CB  1 
ATOM   120  C CG  . LEU A 1 21  ? 28.738 12.705  28.124  1.00 41.52 ? 21  LEU A CG  1 
ATOM   121  C CD1 . LEU A 1 21  ? 28.007 12.959  26.815  1.00 41.75 ? 21  LEU A CD1 1 
ATOM   122  C CD2 . LEU A 1 21  ? 29.930 11.784  27.906  1.00 42.17 ? 21  LEU A CD2 1 
ATOM   123  N N   . ALA A 1 22  ? 30.043 15.882  31.549  1.00 38.63 ? 22  ALA A N   1 
ATOM   124  C CA  . ALA A 1 22  ? 30.601 17.155  32.001  1.00 38.32 ? 22  ALA A CA  1 
ATOM   125  C C   . ALA A 1 22  ? 32.128 17.178  31.956  1.00 38.00 ? 22  ALA A C   1 
ATOM   126  O O   . ALA A 1 22  ? 32.732 18.144  31.485  1.00 37.63 ? 22  ALA A O   1 
ATOM   127  C CB  . ALA A 1 22  ? 30.117 17.455  33.418  1.00 38.99 ? 22  ALA A CB  1 
ATOM   128  N N   . ALA A 1 23  ? 32.745 16.108  32.445  1.00 37.62 ? 23  ALA A N   1 
ATOM   129  C CA  . ALA A 1 23  ? 34.199 15.998  32.471  1.00 37.32 ? 23  ALA A CA  1 
ATOM   130  C C   . ALA A 1 23  ? 34.796 16.090  31.073  1.00 36.59 ? 23  ALA A C   1 
ATOM   131  O O   . ALA A 1 23  ? 35.702 16.883  30.828  1.00 34.89 ? 23  ALA A O   1 
ATOM   132  C CB  . ALA A 1 23  ? 34.606 14.680  33.123  1.00 40.09 ? 23  ALA A CB  1 
ATOM   133  N N   . SER A 1 24  ? 34.280 15.272  30.161  1.00 36.88 ? 24  SER A N   1 
ATOM   134  C CA  . SER A 1 24  ? 34.756 15.247  28.780  1.00 37.40 ? 24  SER A CA  1 
ATOM   135  C C   . SER A 1 24  ? 34.490 16.561  28.058  1.00 35.90 ? 24  SER A C   1 
ATOM   136  O O   . SER A 1 24  ? 35.340 17.059  27.322  1.00 36.73 ? 24  SER A O   1 
ATOM   137  C CB  . SER A 1 24  ? 34.083 14.103  28.018  1.00 38.77 ? 24  SER A CB  1 
ATOM   138  O OG  . SER A 1 24  ? 34.381 12.858  28.624  1.00 43.70 ? 24  SER A OG  1 
ATOM   139  N N   . ILE A 1 25  ? 33.304 17.114  28.267  1.00 34.92 ? 25  ILE A N   1 
ATOM   140  C CA  . ILE A 1 25  ? 32.923 18.371  27.638  1.00 34.78 ? 25  ILE A CA  1 
ATOM   141  C C   . ILE A 1 25  ? 33.864 19.509  28.039  1.00 34.20 ? 25  ILE A C   1 
ATOM   142  O O   . ILE A 1 25  ? 34.266 20.316  27.202  1.00 33.44 ? 25  ILE A O   1 
ATOM   143  C CB  . ILE A 1 25  ? 31.470 18.741  28.009  1.00 35.62 ? 25  ILE A CB  1 
ATOM   144  C CG1 . ILE A 1 25  ? 30.514 17.702  27.411  1.00 36.05 ? 25  ILE A CG1 1 
ATOM   145  C CG2 . ILE A 1 25  ? 31.135 20.146  27.515  1.00 35.54 ? 25  ILE A CG2 1 
ATOM   146  C CD1 . ILE A 1 25  ? 29.071 17.872  27.829  1.00 37.15 ? 25  ILE A CD1 1 
ATOM   147  N N   . SER A 1 26  ? 34.220 19.565  29.318  1.00 34.56 ? 26  SER A N   1 
ATOM   148  C CA  . SER A 1 26  ? 35.116 20.610  29.805  1.00 33.74 ? 26  SER A CA  1 
ATOM   149  C C   . SER A 1 26  ? 36.473 20.525  29.120  1.00 32.89 ? 26  SER A C   1 
ATOM   150  O O   . SER A 1 26  ? 37.063 21.546  28.774  1.00 33.04 ? 26  SER A O   1 
ATOM   151  C CB  . SER A 1 26  ? 35.297 20.493  31.322  1.00 35.43 ? 26  SER A CB  1 
ATOM   152  O OG  . SER A 1 26  ? 34.071 20.724  31.999  1.00 37.15 ? 26  SER A OG  1 
ATOM   153  N N   . ALA A 1 27  ? 36.960 19.305  28.918  1.00 32.35 ? 27  ALA A N   1 
ATOM   154  C CA  . ALA A 1 27  ? 38.256 19.090  28.281  1.00 32.11 ? 27  ALA A CA  1 
ATOM   155  C C   . ALA A 1 27  ? 38.273 19.550  26.826  1.00 31.96 ? 27  ALA A C   1 
ATOM   156  O O   . ALA A 1 27  ? 39.304 19.994  26.322  1.00 31.74 ? 27  ALA A O   1 
ATOM   157  C CB  . ALA A 1 27  ? 38.641 17.608  28.366  1.00 31.91 ? 27  ALA A CB  1 
ATOM   158  N N   . LEU A 1 28  ? 37.131 19.435  26.152  1.00 30.15 ? 28  LEU A N   1 
ATOM   159  C CA  . LEU A 1 28  ? 37.022 19.841  24.752  1.00 30.35 ? 28  LEU A CA  1 
ATOM   160  C C   . LEU A 1 28  ? 37.022 21.355  24.602  1.00 31.55 ? 28  LEU A C   1 
ATOM   161  O O   . LEU A 1 28  ? 37.563 21.893  23.636  1.00 28.42 ? 28  LEU A O   1 
ATOM   162  C CB  . LEU A 1 28  ? 35.744 19.270  24.131  1.00 30.50 ? 28  LEU A CB  1 
ATOM   163  C CG  . LEU A 1 28  ? 35.725 17.761  23.879  1.00 30.50 ? 28  LEU A CG  1 
ATOM   164  C CD1 . LEU A 1 28  ? 34.370 17.357  23.309  1.00 31.59 ? 28  LEU A CD1 1 
ATOM   165  C CD2 . LEU A 1 28  ? 36.841 17.385  22.906  1.00 30.22 ? 28  LEU A CD2 1 
ATOM   166  N N   . SER A 1 29  ? 36.402 22.042  25.558  1.00 33.90 ? 29  SER A N   1 
ATOM   167  C CA  . SER A 1 29  ? 36.344 23.497  25.520  1.00 37.27 ? 29  SER A CA  1 
ATOM   168  C C   . SER A 1 29  ? 37.778 23.975  25.508  1.00 38.11 ? 29  SER A C   1 
ATOM   169  O O   . SER A 1 29  ? 38.164 24.827  24.711  1.00 39.62 ? 29  SER A O   1 
ATOM   170  C CB  . SER A 1 29  ? 35.629 24.040  26.762  1.00 38.36 ? 29  SER A CB  1 
ATOM   171  O OG  . SER A 1 29  ? 34.370 23.412  26.942  1.00 42.39 ? 29  SER A OG  1 
ATOM   172  N N   . GLN A 1 30  ? 38.567 23.394  26.401  1.00 40.68 ? 30  GLN A N   1 
ATOM   173  C CA  . GLN A 1 30  ? 39.976 23.721  26.529  1.00 42.91 ? 30  GLN A CA  1 
ATOM   174  C C   . GLN A 1 30  ? 40.697 23.481  25.208  1.00 43.00 ? 30  GLN A C   1 
ATOM   175  O O   . GLN A 1 30  ? 41.658 24.170  24.877  1.00 42.31 ? 30  GLN A O   1 
ATOM   176  C CB  . GLN A 1 30  ? 40.589 22.851  27.629  1.00 45.17 ? 30  GLN A CB  1 
ATOM   177  C CG  . GLN A 1 30  ? 42.080 23.021  27.819  1.00 45.70 ? 30  GLN A CG  1 
ATOM   178  C CD  . GLN A 1 30  ? 42.584 22.246  29.020  1.00 45.49 ? 30  GLN A CD  1 
ATOM   179  O OE1 . GLN A 1 30  ? 42.068 22.398  30.128  1.00 44.84 ? 30  GLN A OE1 1 
ATOM   180  N NE2 . GLN A 1 30  ? 43.596 21.414  28.809  1.00 45.03 ? 30  GLN A NE2 1 
ATOM   181  N N   . GLU A 1 31  ? 40.212 22.493  24.463  1.00 43.10 ? 31  GLU A N   1 
ATOM   182  C CA  . GLU A 1 31  ? 40.777 22.118  23.174  1.00 43.10 ? 31  GLU A CA  1 
ATOM   183  C C   . GLU A 1 31  ? 40.452 23.172  22.117  1.00 42.28 ? 31  GLU A C   1 
ATOM   184  O O   . GLU A 1 31  ? 41.050 23.189  21.043  1.00 43.37 ? 31  GLU A O   1 
ATOM   185  C CB  . GLU A 1 31  ? 40.203 20.768  22.740  1.00 45.01 ? 31  GLU A CB  1 
ATOM   186  C CG  . GLU A 1 31  ? 41.076 19.979  21.787  1.00 49.96 ? 31  GLU A CG  1 
ATOM   187  C CD  . GLU A 1 31  ? 42.196 19.244  22.498  1.00 52.51 ? 31  GLU A CD  1 
ATOM   188  O OE1 . GLU A 1 31  ? 42.932 18.489  21.830  1.00 55.48 ? 31  GLU A OE1 1 
ATOM   189  O OE2 . GLU A 1 31  ? 42.341 19.417  23.727  1.00 54.28 ? 31  GLU A OE2 1 
ATOM   190  N N   . GLY A 1 32  ? 39.493 24.042  22.419  1.00 40.35 ? 32  GLY A N   1 
ATOM   191  C CA  . GLY A 1 32  ? 39.114 25.079  21.476  1.00 37.68 ? 32  GLY A CA  1 
ATOM   192  C C   . GLY A 1 32  ? 37.771 24.848  20.803  1.00 35.82 ? 32  GLY A C   1 
ATOM   193  O O   . GLY A 1 32  ? 37.397 25.578  19.887  1.00 37.12 ? 32  GLY A O   1 
ATOM   194  N N   . PHE A 1 33  ? 37.041 23.833  21.245  1.00 32.76 ? 33  PHE A N   1 
ATOM   195  C CA  . PHE A 1 33  ? 35.738 23.539  20.665  1.00 30.49 ? 33  PHE A CA  1 
ATOM   196  C C   . PHE A 1 33  ? 34.648 24.334  21.376  1.00 30.71 ? 33  PHE A C   1 
ATOM   197  O O   . PHE A 1 33  ? 34.674 24.486  22.595  1.00 28.81 ? 33  PHE A O   1 
ATOM   198  C CB  . PHE A 1 33  ? 35.426 22.039  20.765  1.00 29.41 ? 33  PHE A CB  1 
ATOM   199  C CG  . PHE A 1 33  ? 36.368 21.169  19.978  1.00 30.38 ? 33  PHE A CG  1 
ATOM   200  C CD1 . PHE A 1 33  ? 36.462 21.300  18.594  1.00 32.04 ? 33  PHE A CD1 1 
ATOM   201  C CD2 . PHE A 1 33  ? 37.167 20.229  20.620  1.00 30.13 ? 33  PHE A CD2 1 
ATOM   202  C CE1 . PHE A 1 33  ? 37.342 20.507  17.858  1.00 32.95 ? 33  PHE A CE1 1 
ATOM   203  C CE2 . PHE A 1 33  ? 38.052 19.429  19.897  1.00 34.01 ? 33  PHE A CE2 1 
ATOM   204  C CZ  . PHE A 1 33  ? 38.140 19.568  18.509  1.00 34.46 ? 33  PHE A CZ  1 
ATOM   205  N N   . ASP A 1 34  ? 33.705 24.853  20.597  1.00 30.56 ? 34  ASP A N   1 
ATOM   206  C CA  . ASP A 1 34  ? 32.579 25.609  21.133  1.00 31.24 ? 34  ASP A CA  1 
ATOM   207  C C   . ASP A 1 34  ? 31.458 24.576  21.250  1.00 30.32 ? 34  ASP A C   1 
ATOM   208  O O   . ASP A 1 34  ? 30.819 24.239  20.254  1.00 27.13 ? 34  ASP A O   1 
ATOM   209  C CB  . ASP A 1 34  ? 32.176 26.713  20.154  1.00 31.70 ? 34  ASP A CB  1 
ATOM   210  C CG  . ASP A 1 34  ? 31.125 27.646  20.723  1.00 35.48 ? 34  ASP A CG  1 
ATOM   211  O OD1 . ASP A 1 34  ? 30.554 27.337  21.794  1.00 34.52 ? 34  ASP A OD1 1 
ATOM   212  O OD2 . ASP A 1 34  ? 30.868 28.690  20.089  1.00 36.21 ? 34  ASP A OD2 1 
ATOM   213  N N   . ILE A 1 35  ? 31.230 24.073  22.460  1.00 29.67 ? 35  ILE A N   1 
ATOM   214  C CA  . ILE A 1 35  ? 30.221 23.041  22.675  1.00 30.24 ? 35  ILE A CA  1 
ATOM   215  C C   . ILE A 1 35  ? 28.789 23.521  22.904  1.00 30.40 ? 35  ILE A C   1 
ATOM   216  O O   . ILE A 1 35  ? 28.502 24.296  23.818  1.00 31.40 ? 35  ILE A O   1 
ATOM   217  C CB  . ILE A 1 35  ? 30.607 22.128  23.858  1.00 32.02 ? 35  ILE A CB  1 
ATOM   218  C CG1 . ILE A 1 35  ? 32.008 21.556  23.643  1.00 31.97 ? 35  ILE A CG1 1 
ATOM   219  C CG2 . ILE A 1 35  ? 29.591 21.009  24.003  1.00 31.85 ? 35  ILE A CG2 1 
ATOM   220  C CD1 . ILE A 1 35  ? 32.155 20.710  22.389  1.00 35.97 ? 35  ILE A CD1 1 
ATOM   221  N N   . ILE A 1 36  ? 27.894 23.035  22.054  1.00 26.41 ? 36  ILE A N   1 
ATOM   222  C CA  . ILE A 1 36  ? 26.480 23.355  22.129  1.00 25.01 ? 36  ILE A CA  1 
ATOM   223  C C   . ILE A 1 36  ? 25.854 22.087  22.700  1.00 25.66 ? 36  ILE A C   1 
ATOM   224  O O   . ILE A 1 36  ? 25.921 21.027  22.079  1.00 24.36 ? 36  ILE A O   1 
ATOM   225  C CB  . ILE A 1 36  ? 25.919 23.656  20.713  1.00 25.27 ? 36  ILE A CB  1 
ATOM   226  C CG1 . ILE A 1 36  ? 26.617 24.902  20.144  1.00 23.99 ? 36  ILE A CG1 1 
ATOM   227  C CG2 . ILE A 1 36  ? 24.406 23.848  20.771  1.00 24.66 ? 36  ILE A CG2 1 
ATOM   228  C CD1 . ILE A 1 36  ? 26.355 25.141  18.665  1.00 25.69 ? 36  ILE A CD1 1 
ATOM   229  N N   . GLN A 1 37  ? 25.257 22.191  23.885  1.00 25.24 ? 37  GLN A N   1 
ATOM   230  C CA  . GLN A 1 37  ? 24.670 21.024  24.548  1.00 27.09 ? 37  GLN A CA  1 
ATOM   231  C C   . GLN A 1 37  ? 23.155 20.906  24.487  1.00 26.16 ? 37  GLN A C   1 
ATOM   232  O O   . GLN A 1 37  ? 22.444 21.823  24.880  1.00 26.84 ? 37  GLN A O   1 
ATOM   233  C CB  . GLN A 1 37  ? 25.080 21.001  26.020  1.00 28.27 ? 37  GLN A CB  1 
ATOM   234  C CG  . GLN A 1 37  ? 26.569 21.026  26.267  1.00 31.22 ? 37  GLN A CG  1 
ATOM   235  C CD  . GLN A 1 37  ? 26.898 20.890  27.739  1.00 33.17 ? 37  GLN A CD  1 
ATOM   236  O OE1 . GLN A 1 37  ? 26.466 19.943  28.393  1.00 35.45 ? 37  GLN A OE1 1 
ATOM   237  N NE2 . GLN A 1 37  ? 27.668 21.835  28.268  1.00 35.82 ? 37  GLN A NE2 1 
ATOM   238  N N   . CYS A 1 38  ? 22.671 19.757  24.016  1.00 26.27 ? 38  CYS A N   1 
ATOM   239  C CA  . CYS A 1 38  ? 21.241 19.488  23.931  1.00 26.72 ? 38  CYS A CA  1 
ATOM   240  C C   . CYS A 1 38  ? 20.923 18.217  24.722  1.00 28.63 ? 38  CYS A C   1 
ATOM   241  O O   . CYS A 1 38  ? 21.638 17.213  24.626  1.00 25.98 ? 38  CYS A O   1 
ATOM   242  C CB  . CYS A 1 38  ? 20.816 19.323  22.473  1.00 28.65 ? 38  CYS A CB  1 
ATOM   243  S SG  . CYS A 1 38  ? 20.996 20.842  21.502  1.00 32.60 ? 38  CYS A SG  1 
ATOM   244  N N   . GLY A 1 39  ? 19.845 18.269  25.502  1.00 29.84 ? 39  GLY A N   1 
ATOM   245  C CA  . GLY A 1 39  ? 19.459 17.134  26.320  1.00 29.80 ? 39  GLY A CA  1 
ATOM   246  C C   . GLY A 1 39  ? 18.631 16.067  25.633  1.00 31.87 ? 39  GLY A C   1 
ATOM   247  O O   . GLY A 1 39  ? 18.461 14.976  26.178  1.00 31.97 ? 39  GLY A O   1 
ATOM   248  N N   . ASN A 1 40  ? 18.100 16.373  24.453  1.00 32.29 ? 40  ASN A N   1 
ATOM   249  C CA  . ASN A 1 40  ? 17.306 15.402  23.709  1.00 33.65 ? 40  ASN A CA  1 
ATOM   250  C C   . ASN A 1 40  ? 17.179 15.786  22.237  1.00 32.57 ? 40  ASN A C   1 
ATOM   251  O O   . ASN A 1 40  ? 17.543 16.890  21.840  1.00 31.21 ? 40  ASN A O   1 
ATOM   252  C CB  . ASN A 1 40  ? 15.917 15.243  24.335  1.00 35.29 ? 40  ASN A CB  1 
ATOM   253  C CG  . ASN A 1 40  ? 15.131 16.530  24.340  1.00 36.57 ? 40  ASN A CG  1 
ATOM   254  O OD1 . ASN A 1 40  ? 14.854 17.107  23.289  1.00 36.81 ? 40  ASN A OD1 1 
ATOM   255  N ND2 . ASN A 1 40  ? 14.764 16.987  25.526  1.00 39.11 ? 40  ASN A ND2 1 
ATOM   256  N N   . ALA A 1 41  ? 16.660 14.862  21.436  1.00 31.50 ? 41  ALA A N   1 
ATOM   257  C CA  . ALA A 1 41  ? 16.509 15.073  20.004  1.00 33.14 ? 41  ALA A CA  1 
ATOM   258  C C   . ALA A 1 41  ? 15.505 16.160  19.632  1.00 32.85 ? 41  ALA A C   1 
ATOM   259  O O   . ALA A 1 41  ? 15.641 16.804  18.593  1.00 32.33 ? 41  ALA A O   1 
ATOM   260  C CB  . ALA A 1 41  ? 16.129 13.756  19.333  1.00 33.04 ? 41  ALA A CB  1 
ATOM   261  N N   . ILE A 1 42  ? 14.501 16.354  20.478  1.00 32.78 ? 42  ILE A N   1 
ATOM   262  C CA  . ILE A 1 42  ? 13.473 17.364  20.246  1.00 34.64 ? 42  ILE A CA  1 
ATOM   263  C C   . ILE A 1 42  ? 14.040 18.774  20.070  1.00 33.53 ? 42  ILE A C   1 
ATOM   264  O O   . ILE A 1 42  ? 13.652 19.487  19.150  1.00 34.78 ? 42  ILE A O   1 
ATOM   265  C CB  . ILE A 1 42  ? 12.459 17.377  21.402  1.00 36.80 ? 42  ILE A CB  1 
ATOM   266  C CG1 . ILE A 1 42  ? 11.678 16.060  21.407  1.00 39.55 ? 42  ILE A CG1 1 
ATOM   267  C CG2 . ILE A 1 42  ? 11.532 18.580  21.274  1.00 36.70 ? 42  ILE A CG2 1 
ATOM   268  C CD1 . ILE A 1 42  ? 10.936 15.794  22.700  1.00 42.91 ? 42  ILE A CD1 1 
ATOM   269  N N   . GLU A 1 43  ? 14.945 19.187  20.948  1.00 33.35 ? 43  GLU A N   1 
ATOM   270  C CA  . GLU A 1 43  ? 15.522 20.522  20.815  1.00 35.53 ? 43  GLU A CA  1 
ATOM   271  C C   . GLU A 1 43  ? 16.716 20.532  19.860  1.00 33.71 ? 43  GLU A C   1 
ATOM   272  O O   . GLU A 1 43  ? 16.999 21.547  19.226  1.00 33.71 ? 43  GLU A O   1 
ATOM   273  C CB  . GLU A 1 43  ? 15.960 21.080  22.175  1.00 37.74 ? 43  GLU A CB  1 
ATOM   274  C CG  . GLU A 1 43  ? 16.975 20.237  22.930  1.00 41.39 ? 43  GLU A CG  1 
ATOM   275  C CD  . GLU A 1 43  ? 17.621 21.003  24.082  1.00 45.09 ? 43  GLU A CD  1 
ATOM   276  O OE1 . GLU A 1 43  ? 18.205 20.362  24.985  1.00 45.44 ? 43  GLU A OE1 1 
ATOM   277  O OE2 . GLU A 1 43  ? 17.553 22.250  24.078  1.00 46.83 ? 43  GLU A OE2 1 
ATOM   278  N N   . ALA A 1 44  ? 17.396 19.393  19.747  1.00 30.89 ? 44  ALA A N   1 
ATOM   279  C CA  . ALA A 1 44  ? 18.574 19.273  18.888  1.00 29.13 ? 44  ALA A CA  1 
ATOM   280  C C   . ALA A 1 44  ? 18.385 19.681  17.429  1.00 26.77 ? 44  ALA A C   1 
ATOM   281  O O   . ALA A 1 44  ? 19.222 20.392  16.875  1.00 24.96 ? 44  ALA A O   1 
ATOM   282  C CB  . ALA A 1 44  ? 19.123 17.842  18.956  1.00 28.88 ? 44  ALA A CB  1 
ATOM   283  N N   . VAL A 1 45  ? 17.304 19.230  16.798  1.00 26.89 ? 45  VAL A N   1 
ATOM   284  C CA  . VAL A 1 45  ? 17.074 19.557  15.390  1.00 27.44 ? 45  VAL A CA  1 
ATOM   285  C C   . VAL A 1 45  ? 16.954 21.057  15.105  1.00 28.33 ? 45  VAL A C   1 
ATOM   286  O O   . VAL A 1 45  ? 17.702 21.601  14.291  1.00 26.27 ? 45  VAL A O   1 
ATOM   287  C CB  . VAL A 1 45  ? 15.827 18.823  14.837  1.00 31.12 ? 45  VAL A CB  1 
ATOM   288  C CG1 . VAL A 1 45  ? 15.594 19.219  13.389  1.00 30.47 ? 45  VAL A CG1 1 
ATOM   289  C CG2 . VAL A 1 45  ? 16.025 17.309  14.943  1.00 28.66 ? 45  VAL A CG2 1 
ATOM   290  N N   . PRO A 1 46  ? 16.005 21.746  15.756  1.00 27.95 ? 46  PRO A N   1 
ATOM   291  C CA  . PRO A 1 46  ? 15.869 23.188  15.507  1.00 27.92 ? 46  PRO A CA  1 
ATOM   292  C C   . PRO A 1 46  ? 17.156 23.934  15.874  1.00 25.50 ? 46  PRO A C   1 
ATOM   293  O O   . PRO A 1 46  ? 17.550 24.890  15.203  1.00 26.51 ? 46  PRO A O   1 
ATOM   294  C CB  . PRO A 1 46  ? 14.698 23.586  16.409  1.00 29.75 ? 46  PRO A CB  1 
ATOM   295  C CG  . PRO A 1 46  ? 13.874 22.315  16.463  1.00 30.12 ? 46  PRO A CG  1 
ATOM   296  C CD  . PRO A 1 46  ? 14.941 21.265  16.654  1.00 29.34 ? 46  PRO A CD  1 
ATOM   297  N N   . VAL A 1 47  ? 17.801 23.505  16.953  1.00 24.04 ? 47  VAL A N   1 
ATOM   298  C CA  . VAL A 1 47  ? 19.046 24.141  17.375  1.00 23.73 ? 47  VAL A CA  1 
ATOM   299  C C   . VAL A 1 47  ? 20.118 23.947  16.301  1.00 23.13 ? 47  VAL A C   1 
ATOM   300  O O   . VAL A 1 47  ? 20.860 24.874  15.983  1.00 23.05 ? 47  VAL A O   1 
ATOM   301  C CB  . VAL A 1 47  ? 19.556 23.566  18.713  1.00 25.15 ? 47  VAL A CB  1 
ATOM   302  C CG1 . VAL A 1 47  ? 20.949 24.106  19.022  1.00 25.12 ? 47  VAL A CG1 1 
ATOM   303  C CG2 . VAL A 1 47  ? 18.604 23.955  19.840  1.00 26.23 ? 47  VAL A CG2 1 
ATOM   304  N N   . ALA A 1 48  ? 20.193 22.748  15.731  1.00 20.12 ? 48  ALA A N   1 
ATOM   305  C CA  . ALA A 1 48  ? 21.192 22.491  14.695  1.00 21.54 ? 48  ALA A CA  1 
ATOM   306  C C   . ALA A 1 48  ? 20.955 23.378  13.483  1.00 22.81 ? 48  ALA A C   1 
ATOM   307  O O   . ALA A 1 48  ? 21.888 23.953  12.926  1.00 22.96 ? 48  ALA A O   1 
ATOM   308  C CB  . ALA A 1 48  ? 21.158 21.026  14.281  1.00 21.23 ? 48  ALA A CB  1 
ATOM   309  N N   . VAL A 1 49  ? 19.695 23.491  13.077  1.00 23.83 ? 49  VAL A N   1 
ATOM   310  C CA  . VAL A 1 49  ? 19.341 24.298  11.919  1.00 26.06 ? 49  VAL A CA  1 
ATOM   311  C C   . VAL A 1 49  ? 19.726 25.765  12.086  1.00 26.93 ? 49  VAL A C   1 
ATOM   312  O O   . VAL A 1 49  ? 20.134 26.408  11.123  1.00 27.99 ? 49  VAL A O   1 
ATOM   313  C CB  . VAL A 1 49  ? 17.821 24.179  11.613  1.00 24.83 ? 49  VAL A CB  1 
ATOM   314  C CG1 . VAL A 1 49  ? 17.409 25.192  10.553  1.00 28.37 ? 49  VAL A CG1 1 
ATOM   315  C CG2 . VAL A 1 49  ? 17.513 22.759  11.126  1.00 26.67 ? 49  VAL A CG2 1 
ATOM   316  N N   . LYS A 1 50  ? 19.629 26.297  13.301  1.00 26.89 ? 50  LYS A N   1 
ATOM   317  C CA  . LYS A 1 50  ? 19.973 27.699  13.500  1.00 28.33 ? 50  LYS A CA  1 
ATOM   318  C C   . LYS A 1 50  ? 21.397 27.984  13.964  1.00 26.58 ? 50  LYS A C   1 
ATOM   319  O O   . LYS A 1 50  ? 21.875 29.104  13.807  1.00 27.60 ? 50  LYS A O   1 
ATOM   320  C CB  . LYS A 1 50  ? 18.975 28.369  14.454  1.00 30.62 ? 50  LYS A CB  1 
ATOM   321  C CG  . LYS A 1 50  ? 18.892 27.771  15.837  1.00 34.11 ? 50  LYS A CG  1 
ATOM   322  C CD  . LYS A 1 50  ? 17.704 28.370  16.589  1.00 34.78 ? 50  LYS A CD  1 
ATOM   323  C CE  . LYS A 1 50  ? 17.570 27.804  17.991  1.00 35.93 ? 50  LYS A CE  1 
ATOM   324  N NZ  . LYS A 1 50  ? 16.418 28.427  18.708  1.00 35.26 ? 50  LYS A NZ  1 
ATOM   325  N N   . THR A 1 51  ? 22.082 26.988  14.520  1.00 24.10 ? 51  THR A N   1 
ATOM   326  C CA  . THR A 1 51  ? 23.449 27.204  14.989  1.00 23.85 ? 51  THR A CA  1 
ATOM   327  C C   . THR A 1 51  ? 24.492 26.643  14.034  1.00 22.06 ? 51  THR A C   1 
ATOM   328  O O   . THR A 1 51  ? 25.680 26.925  14.171  1.00 22.22 ? 51  THR A O   1 
ATOM   329  C CB  . THR A 1 51  ? 23.687 26.591  16.386  1.00 25.55 ? 51  THR A CB  1 
ATOM   330  O OG1 . THR A 1 51  ? 23.697 25.163  16.288  1.00 26.17 ? 51  THR A OG1 1 
ATOM   331  C CG2 . THR A 1 51  ? 22.592 27.026  17.359  1.00 25.93 ? 51  THR A CG2 1 
ATOM   332  N N   . HIS A 1 52  ? 24.053 25.824  13.080  1.00 22.91 ? 52  HIS A N   1 
ATOM   333  C CA  . HIS A 1 52  ? 24.963 25.269  12.082  1.00 19.43 ? 52  HIS A CA  1 
ATOM   334  C C   . HIS A 1 52  ? 26.258 24.682  12.655  1.00 19.78 ? 52  HIS A C   1 
ATOM   335  O O   . HIS A 1 52  ? 27.360 25.118  12.294  1.00 20.04 ? 52  HIS A O   1 
ATOM   336  C CB  . HIS A 1 52  ? 25.323 26.367  11.075  1.00 20.65 ? 52  HIS A CB  1 
ATOM   337  C CG  . HIS A 1 52  ? 24.136 27.106  10.544  1.00 21.73 ? 52  HIS A CG  1 
ATOM   338  N ND1 . HIS A 1 52  ? 23.334 26.606  9.541   1.00 22.32 ? 52  HIS A ND1 1 
ATOM   339  C CD2 . HIS A 1 52  ? 23.583 28.284  10.916  1.00 22.29 ? 52  HIS A CD2 1 
ATOM   340  C CE1 . HIS A 1 52  ? 22.336 27.444  9.319   1.00 22.35 ? 52  HIS A CE1 1 
ATOM   341  N NE2 . HIS A 1 52  ? 22.464 28.470  10.141  1.00 22.44 ? 52  HIS A NE2 1 
ATOM   342  N N   . PRO A 1 53  ? 26.156 23.687  13.551  1.00 19.35 ? 53  PRO A N   1 
ATOM   343  C CA  . PRO A 1 53  ? 27.389 23.112  14.100  1.00 18.35 ? 53  PRO A CA  1 
ATOM   344  C C   . PRO A 1 53  ? 28.222 22.495  12.973  1.00 19.62 ? 53  PRO A C   1 
ATOM   345  O O   . PRO A 1 53  ? 27.665 22.064  11.962  1.00 18.35 ? 53  PRO A O   1 
ATOM   346  C CB  . PRO A 1 53  ? 26.872 22.053  15.070  1.00 19.83 ? 53  PRO A CB  1 
ATOM   347  C CG  . PRO A 1 53  ? 25.568 21.618  14.425  1.00 19.54 ? 53  PRO A CG  1 
ATOM   348  C CD  . PRO A 1 53  ? 24.971 22.951  14.027  1.00 17.78 ? 53  PRO A CD  1 
ATOM   349  N N   . HIS A 1 54  ? 29.542 22.457  13.141  1.00 18.23 ? 54  HIS A N   1 
ATOM   350  C CA  . HIS A 1 54  ? 30.408 21.862  12.122  1.00 20.07 ? 54  HIS A CA  1 
ATOM   351  C C   . HIS A 1 54  ? 30.329 20.343  12.207  1.00 19.79 ? 54  HIS A C   1 
ATOM   352  O O   . HIS A 1 54  ? 30.579 19.633  11.232  1.00 20.85 ? 54  HIS A O   1 
ATOM   353  C CB  . HIS A 1 54  ? 31.867 22.285  12.315  1.00 21.04 ? 54  HIS A CB  1 
ATOM   354  C CG  . HIS A 1 54  ? 32.122 23.735  12.051  1.00 22.77 ? 54  HIS A CG  1 
ATOM   355  N ND1 . HIS A 1 54  ? 32.081 24.690  13.044  1.00 21.52 ? 54  HIS A ND1 1 
ATOM   356  C CD2 . HIS A 1 54  ? 32.417 24.395  10.905  1.00 24.78 ? 54  HIS A CD2 1 
ATOM   357  C CE1 . HIS A 1 54  ? 32.342 25.876  12.522  1.00 24.91 ? 54  HIS A CE1 1 
ATOM   358  N NE2 . HIS A 1 54  ? 32.549 25.725  11.225  1.00 23.86 ? 54  HIS A NE2 1 
ATOM   359  N N   . LEU A 1 55  ? 29.994 19.849  13.392  1.00 19.71 ? 55  LEU A N   1 
ATOM   360  C CA  . LEU A 1 55  ? 29.890 18.413  13.608  1.00 19.64 ? 55  LEU A CA  1 
ATOM   361  C C   . LEU A 1 55  ? 28.920 18.154  14.752  1.00 19.14 ? 55  LEU A C   1 
ATOM   362  O O   . LEU A 1 55  ? 28.812 18.957  15.676  1.00 19.79 ? 55  LEU A O   1 
ATOM   363  C CB  . LEU A 1 55  ? 31.273 17.829  13.918  1.00 21.50 ? 55  LEU A CB  1 
ATOM   364  C CG  . LEU A 1 55  ? 31.326 16.310  14.090  1.00 22.27 ? 55  LEU A CG  1 
ATOM   365  C CD1 . LEU A 1 55  ? 32.688 15.785  13.659  1.00 28.54 ? 55  LEU A CD1 1 
ATOM   366  C CD2 . LEU A 1 55  ? 31.040 15.964  15.532  1.00 26.17 ? 55  LEU A CD2 1 
ATOM   367  N N   . ILE A 1 56  ? 28.220 17.027  14.686  1.00 17.78 ? 56  ILE A N   1 
ATOM   368  C CA  . ILE A 1 56  ? 27.238 16.685  15.705  1.00 18.28 ? 56  ILE A CA  1 
ATOM   369  C C   . ILE A 1 56  ? 27.580 15.356  16.344  1.00 19.17 ? 56  ILE A C   1 
ATOM   370  O O   . ILE A 1 56  ? 27.979 14.409  15.663  1.00 19.34 ? 56  ILE A O   1 
ATOM   371  C CB  . ILE A 1 56  ? 25.818 16.617  15.081  1.00 17.77 ? 56  ILE A CB  1 
ATOM   372  C CG1 . ILE A 1 56  ? 25.436 18.002  14.542  1.00 17.02 ? 56  ILE A CG1 1 
ATOM   373  C CG2 . ILE A 1 56  ? 24.802 16.122  16.112  1.00 16.05 ? 56  ILE A CG2 1 
ATOM   374  C CD1 . ILE A 1 56  ? 24.184 18.013  13.696  1.00 19.99 ? 56  ILE A CD1 1 
ATOM   375  N N   . ILE A 1 57  ? 27.452 15.296  17.664  1.00 18.64 ? 57  ILE A N   1 
ATOM   376  C CA  . ILE A 1 57  ? 27.731 14.069  18.401  1.00 19.61 ? 57  ILE A CA  1 
ATOM   377  C C   . ILE A 1 57  ? 26.431 13.737  19.127  1.00 20.35 ? 57  ILE A C   1 
ATOM   378  O O   . ILE A 1 57  ? 25.923 14.552  19.897  1.00 20.41 ? 57  ILE A O   1 
ATOM   379  C CB  . ILE A 1 57  ? 28.834 14.285  19.454  1.00 19.98 ? 57  ILE A CB  1 
ATOM   380  C CG1 . ILE A 1 57  ? 30.137 14.709  18.778  1.00 23.27 ? 57  ILE A CG1 1 
ATOM   381  C CG2 . ILE A 1 57  ? 29.033 13.013  20.263  1.00 21.96 ? 57  ILE A CG2 1 
ATOM   382  C CD1 . ILE A 1 57  ? 31.217 15.156  19.769  1.00 22.22 ? 57  ILE A CD1 1 
ATOM   383  N N   . THR A 1 58  ? 25.884 12.554  18.888  1.00 18.89 ? 58  THR A N   1 
ATOM   384  C CA  . THR A 1 58  ? 24.638 12.203  19.552  1.00 20.77 ? 58  THR A CA  1 
ATOM   385  C C   . THR A 1 58  ? 24.647 10.826  20.181  1.00 22.47 ? 58  THR A C   1 
ATOM   386  O O   . THR A 1 58  ? 25.293 9.904   19.685  1.00 22.83 ? 58  THR A O   1 
ATOM   387  C CB  . THR A 1 58  ? 23.440 12.256  18.577  1.00 21.83 ? 58  THR A CB  1 
ATOM   388  O OG1 . THR A 1 58  ? 22.243 11.929  19.289  1.00 21.14 ? 58  THR A OG1 1 
ATOM   389  C CG2 . THR A 1 58  ? 23.620 11.252  17.430  1.00 20.28 ? 58  THR A CG2 1 
ATOM   390  N N   . GLU A 1 59  ? 23.933 10.700  21.295  1.00 23.98 ? 59  GLU A N   1 
ATOM   391  C CA  . GLU A 1 59  ? 23.798 9.421   21.968  1.00 25.29 ? 59  GLU A CA  1 
ATOM   392  C C   . GLU A 1 59  ? 22.998 8.585   20.968  1.00 24.51 ? 59  GLU A C   1 
ATOM   393  O O   . GLU A 1 59  ? 22.082 9.100   20.330  1.00 23.49 ? 59  GLU A O   1 
ATOM   394  C CB  . GLU A 1 59  ? 22.998 9.600   23.260  1.00 27.02 ? 59  GLU A CB  1 
ATOM   395  C CG  . GLU A 1 59  ? 22.866 8.347   24.103  1.00 30.58 ? 59  GLU A CG  1 
ATOM   396  C CD  . GLU A 1 59  ? 22.145 8.615   25.416  1.00 34.01 ? 59  GLU A CD  1 
ATOM   397  O OE1 . GLU A 1 59  ? 22.144 7.725   26.295  1.00 35.31 ? 59  GLU A OE1 1 
ATOM   398  O OE2 . GLU A 1 59  ? 21.574 9.716   25.562  1.00 32.71 ? 59  GLU A OE2 1 
ATOM   399  N N   . ALA A 1 60  ? 23.339 7.309   20.826  1.00 26.18 ? 60  ALA A N   1 
ATOM   400  C CA  . ALA A 1 60  ? 22.637 6.448   19.882  1.00 27.35 ? 60  ALA A CA  1 
ATOM   401  C C   . ALA A 1 60  ? 21.259 6.032   20.374  1.00 29.72 ? 60  ALA A C   1 
ATOM   402  O O   . ALA A 1 60  ? 20.265 6.170   19.664  1.00 30.81 ? 60  ALA A O   1 
ATOM   403  C CB  . ALA A 1 60  ? 23.471 5.214   19.590  1.00 29.47 ? 60  ALA A CB  1 
ATOM   404  N N   . ASN A 1 61  ? 21.198 5.527   21.597  1.00 30.90 ? 61  ASN A N   1 
ATOM   405  C CA  . ASN A 1 61  ? 19.932 5.075   22.152  1.00 34.01 ? 61  ASN A CA  1 
ATOM   406  C C   . ASN A 1 61  ? 19.333 6.049   23.159  1.00 33.95 ? 61  ASN A C   1 
ATOM   407  O O   . ASN A 1 61  ? 19.740 6.081   24.317  1.00 35.55 ? 61  ASN A O   1 
ATOM   408  C CB  . ASN A 1 61  ? 20.137 3.703   22.795  1.00 34.87 ? 61  ASN A CB  1 
ATOM   409  C CG  . ASN A 1 61  ? 20.787 2.715   21.842  1.00 36.47 ? 61  ASN A CG  1 
ATOM   410  O OD1 . ASN A 1 61  ? 20.171 2.276   20.871  1.00 36.40 ? 61  ASN A OD1 1 
ATOM   411  N ND2 . ASN A 1 61  ? 22.046 2.377   22.104  1.00 38.31 ? 61  ASN A ND2 1 
ATOM   412  N N   . MET A 1 62  ? 18.377 6.852   22.697  1.00 34.67 ? 62  MET A N   1 
ATOM   413  C CA  . MET A 1 62  ? 17.681 7.820   23.543  1.00 34.49 ? 62  MET A CA  1 
ATOM   414  C C   . MET A 1 62  ? 16.190 7.467   23.517  1.00 36.99 ? 62  MET A C   1 
ATOM   415  O O   . MET A 1 62  ? 15.651 7.088   22.473  1.00 37.51 ? 62  MET A O   1 
ATOM   416  C CB  . MET A 1 62  ? 17.869 9.255   23.022  1.00 30.95 ? 62  MET A CB  1 
ATOM   417  C CG  . MET A 1 62  ? 19.304 9.762   23.027  1.00 26.67 ? 62  MET A CG  1 
ATOM   418  S SD  . MET A 1 62  ? 19.471 11.529  22.603  1.00 20.33 ? 62  MET A SD  1 
ATOM   419  C CE  . MET A 1 62  ? 19.157 11.483  20.804  1.00 25.06 ? 62  MET A CE  1 
ATOM   420  N N   . PRO A 1 63  ? 15.506 7.581   24.666  1.00 38.41 ? 63  PRO A N   1 
ATOM   421  C CA  . PRO A 1 63  ? 14.077 7.258   24.706  1.00 39.69 ? 63  PRO A CA  1 
ATOM   422  C C   . PRO A 1 63  ? 13.259 8.213   23.848  1.00 39.99 ? 63  PRO A C   1 
ATOM   423  O O   . PRO A 1 63  ? 13.631 9.370   23.679  1.00 41.21 ? 63  PRO A O   1 
ATOM   424  C CB  . PRO A 1 63  ? 13.742 7.365   26.194  1.00 39.26 ? 63  PRO A CB  1 
ATOM   425  C CG  . PRO A 1 63  ? 14.692 8.414   26.676  1.00 40.62 ? 63  PRO A CG  1 
ATOM   426  C CD  . PRO A 1 63  ? 15.984 8.019   25.990  1.00 39.11 ? 63  PRO A CD  1 
ATOM   427  N N   . LYS A 1 64  ? 12.149 7.715   23.308  1.00 41.67 ? 64  LYS A N   1 
ATOM   428  C CA  . LYS A 1 64  ? 11.263 8.510   22.462  1.00 43.10 ? 64  LYS A CA  1 
ATOM   429  C C   . LYS A 1 64  ? 11.899 8.743   21.092  1.00 42.33 ? 64  LYS A C   1 
ATOM   430  O O   . LYS A 1 64  ? 11.461 8.166   20.095  1.00 44.03 ? 64  LYS A O   1 
ATOM   431  C CB  . LYS A 1 64  ? 10.947 9.858   23.126  1.00 45.74 ? 64  LYS A CB  1 
ATOM   432  C CG  . LYS A 1 64  ? 10.352 9.753   24.527  1.00 48.72 ? 64  LYS A CG  1 
ATOM   433  C CD  . LYS A 1 64  ? 8.976  9.103   24.509  1.00 52.44 ? 64  LYS A CD  1 
ATOM   434  C CE  . LYS A 1 64  ? 8.407  8.981   25.918  1.00 53.88 ? 64  LYS A CE  1 
ATOM   435  N NZ  . LYS A 1 64  ? 7.050  8.364   25.925  1.00 55.30 ? 64  LYS A NZ  1 
ATOM   436  N N   . ILE A 1 65  ? 12.930 9.585   21.048  1.00 40.25 ? 65  ILE A N   1 
ATOM   437  C CA  . ILE A 1 65  ? 13.625 9.881   19.800  1.00 36.47 ? 65  ILE A CA  1 
ATOM   438  C C   . ILE A 1 65  ? 15.087 9.446   19.905  1.00 34.49 ? 65  ILE A C   1 
ATOM   439  O O   . ILE A 1 65  ? 15.844 9.951   20.733  1.00 35.53 ? 65  ILE A O   1 
ATOM   440  C CB  . ILE A 1 65  ? 13.562 11.376  19.467  1.00 36.07 ? 65  ILE A CB  1 
ATOM   441  C CG1 . ILE A 1 65  ? 12.123 11.877  19.602  1.00 37.43 ? 65  ILE A CG1 1 
ATOM   442  C CG2 . ILE A 1 65  ? 14.047 11.605  18.039  1.00 36.82 ? 65  ILE A CG2 1 
ATOM   443  C CD1 . ILE A 1 65  ? 11.934 13.336  19.228  1.00 37.73 ? 65  ILE A CD1 1 
ATOM   444  N N   . SER A 1 66  ? 15.476 8.505   19.055  1.00 31.78 ? 66  SER A N   1 
ATOM   445  C CA  . SER A 1 66  ? 16.830 7.963   19.072  1.00 29.39 ? 66  SER A CA  1 
ATOM   446  C C   . SER A 1 66  ? 17.835 8.764   18.251  1.00 28.00 ? 66  SER A C   1 
ATOM   447  O O   . SER A 1 66  ? 17.474 9.701   17.534  1.00 23.31 ? 66  SER A O   1 
ATOM   448  C CB  . SER A 1 66  ? 16.811 6.528   18.551  1.00 30.16 ? 66  SER A CB  1 
ATOM   449  O OG  . SER A 1 66  ? 16.668 6.525   17.142  1.00 28.50 ? 66  SER A OG  1 
ATOM   450  N N   . GLY A 1 67  ? 19.103 8.381   18.372  1.00 27.45 ? 67  GLY A N   1 
ATOM   451  C CA  . GLY A 1 67  ? 20.157 9.038   17.618  1.00 26.60 ? 67  GLY A CA  1 
ATOM   452  C C   . GLY A 1 67  ? 19.934 8.797   16.135  1.00 25.80 ? 67  GLY A C   1 
ATOM   453  O O   . GLY A 1 67  ? 20.244 9.653   15.308  1.00 24.31 ? 67  GLY A O   1 
ATOM   454  N N   . MET A 1 68  ? 19.403 7.625   15.790  1.00 26.72 ? 68  MET A N   1 
ATOM   455  C CA  . MET A 1 68  ? 19.123 7.312   14.386  1.00 26.51 ? 68  MET A CA  1 
ATOM   456  C C   . MET A 1 68  ? 17.975 8.183   13.875  1.00 25.46 ? 68  MET A C   1 
ATOM   457  O O   . MET A 1 68  ? 17.960 8.575   12.708  1.00 23.10 ? 68  MET A O   1 
ATOM   458  C CB  . MET A 1 68  ? 18.763 5.832   14.207  1.00 27.81 ? 68  MET A CB  1 
ATOM   459  C CG  . MET A 1 68  ? 19.946 4.880   14.312  1.00 31.63 ? 68  MET A CG  1 
ATOM   460  S SD  . MET A 1 68  ? 19.514 3.150   13.925  1.00 34.35 ? 68  MET A SD  1 
ATOM   461  C CE  . MET A 1 68  ? 18.560 2.736   15.384  1.00 35.98 ? 68  MET A CE  1 
ATOM   462  N N   . ASP A 1 69  ? 17.016 8.483   14.751  1.00 24.36 ? 69  ASP A N   1 
ATOM   463  C CA  . ASP A 1 69  ? 15.882 9.329   14.381  1.00 25.90 ? 69  ASP A CA  1 
ATOM   464  C C   . ASP A 1 69  ? 16.395 10.738  14.128  1.00 23.61 ? 69  ASP A C   1 
ATOM   465  O O   . ASP A 1 69  ? 15.980 11.403  13.179  1.00 22.61 ? 69  ASP A O   1 
ATOM   466  C CB  . ASP A 1 69  ? 14.835 9.375   15.500  1.00 29.45 ? 69  ASP A CB  1 
ATOM   467  C CG  . ASP A 1 69  ? 14.103 8.060   15.671  1.00 34.66 ? 69  ASP A CG  1 
ATOM   468  O OD1 . ASP A 1 69  ? 13.760 7.442   14.639  1.00 35.35 ? 69  ASP A OD1 1 
ATOM   469  O OD2 . ASP A 1 69  ? 13.860 7.655   16.832  1.00 35.15 ? 69  ASP A OD2 1 
ATOM   470  N N   . LEU A 1 70  ? 17.302 11.187  14.991  1.00 23.03 ? 70  LEU A N   1 
ATOM   471  C CA  . LEU A 1 70  ? 17.894 12.514  14.858  1.00 21.89 ? 70  LEU A CA  1 
ATOM   472  C C   . LEU A 1 70  ? 18.680 12.568  13.552  1.00 21.14 ? 70  LEU A C   1 
ATOM   473  O O   . LEU A 1 70  ? 18.571 13.530  12.794  1.00 20.26 ? 70  LEU A O   1 
ATOM   474  C CB  . LEU A 1 70  ? 18.833 12.808  16.036  1.00 23.01 ? 70  LEU A CB  1 
ATOM   475  C CG  . LEU A 1 70  ? 19.592 14.145  15.991  1.00 24.26 ? 70  LEU A CG  1 
ATOM   476  C CD1 . LEU A 1 70  ? 18.600 15.284  15.840  1.00 26.05 ? 70  LEU A CD1 1 
ATOM   477  C CD2 . LEU A 1 70  ? 20.420 14.325  17.264  1.00 28.07 ? 70  LEU A CD2 1 
ATOM   478  N N   . PHE A 1 71  ? 19.477 11.532  13.298  1.00 18.82 ? 71  PHE A N   1 
ATOM   479  C CA  . PHE A 1 71  ? 20.264 11.476  12.073  1.00 19.31 ? 71  PHE A CA  1 
ATOM   480  C C   . PHE A 1 71  ? 19.347 11.651  10.857  1.00 20.36 ? 71  PHE A C   1 
ATOM   481  O O   . PHE A 1 71  ? 19.630 12.450  9.961   1.00 19.06 ? 71  PHE A O   1 
ATOM   482  C CB  . PHE A 1 71  ? 20.979 10.132  11.967  1.00 19.14 ? 71  PHE A CB  1 
ATOM   483  C CG  . PHE A 1 71  ? 21.885 10.019  10.769  1.00 19.63 ? 71  PHE A CG  1 
ATOM   484  C CD1 . PHE A 1 71  ? 23.200 10.463  10.833  1.00 18.83 ? 71  PHE A CD1 1 
ATOM   485  C CD2 . PHE A 1 71  ? 21.419 9.473   9.577   1.00 19.14 ? 71  PHE A CD2 1 
ATOM   486  C CE1 . PHE A 1 71  ? 24.048 10.361  9.725   1.00 21.72 ? 71  PHE A CE1 1 
ATOM   487  C CE2 . PHE A 1 71  ? 22.246 9.366   8.465   1.00 19.57 ? 71  PHE A CE2 1 
ATOM   488  C CZ  . PHE A 1 71  ? 23.570 9.810   8.535   1.00 20.14 ? 71  PHE A CZ  1 
ATOM   489  N N   . ASN A 1 72  ? 18.248 10.900  10.829  1.00 19.51 ? 72  ASN A N   1 
ATOM   490  C CA  . ASN A 1 72  ? 17.313 10.982  9.706   1.00 21.95 ? 72  ASN A CA  1 
ATOM   491  C C   . ASN A 1 72  ? 16.656 12.356  9.596   1.00 23.04 ? 72  ASN A C   1 
ATOM   492  O O   . ASN A 1 72  ? 16.468 12.866  8.489   1.00 21.73 ? 72  ASN A O   1 
ATOM   493  C CB  . ASN A 1 72  ? 16.218 9.911   9.819   1.00 25.29 ? 72  ASN A CB  1 
ATOM   494  C CG  . ASN A 1 72  ? 16.756 8.497   9.645   1.00 27.80 ? 72  ASN A CG  1 
ATOM   495  O OD1 . ASN A 1 72  ? 17.727 8.274   8.919   1.00 28.25 ? 72  ASN A OD1 1 
ATOM   496  N ND2 . ASN A 1 72  ? 16.110 7.533   10.294  1.00 30.09 ? 72  ASN A ND2 1 
ATOM   497  N N   . SER A 1 73  ? 16.303 12.950  10.733  1.00 22.54 ? 73  SER A N   1 
ATOM   498  C CA  . SER A 1 73  ? 15.672 14.270  10.720  1.00 24.32 ? 73  SER A CA  1 
ATOM   499  C C   . SER A 1 73  ? 16.621 15.332  10.170  1.00 23.33 ? 73  SER A C   1 
ATOM   500  O O   . SER A 1 73  ? 16.207 16.237  9.449   1.00 24.34 ? 73  SER A O   1 
ATOM   501  C CB  . SER A 1 73  ? 15.217 14.654  12.129  1.00 24.49 ? 73  SER A CB  1 
ATOM   502  O OG  . SER A 1 73  ? 14.203 13.774  12.571  1.00 28.55 ? 73  SER A OG  1 
ATOM   503  N N   . LEU A 1 74  ? 17.900 15.222  10.516  1.00 22.72 ? 74  LEU A N   1 
ATOM   504  C CA  . LEU A 1 74  ? 18.900 16.170  10.038  1.00 22.03 ? 74  LEU A CA  1 
ATOM   505  C C   . LEU A 1 74  ? 19.060 16.064  8.522   1.00 23.67 ? 74  LEU A C   1 
ATOM   506  O O   . LEU A 1 74  ? 19.372 17.046  7.845   1.00 22.16 ? 74  LEU A O   1 
ATOM   507  C CB  . LEU A 1 74  ? 20.241 15.891  10.721  1.00 20.99 ? 74  LEU A CB  1 
ATOM   508  C CG  . LEU A 1 74  ? 20.236 16.199  12.224  1.00 22.67 ? 74  LEU A CG  1 
ATOM   509  C CD1 . LEU A 1 74  ? 21.465 15.605  12.897  1.00 21.93 ? 74  LEU A CD1 1 
ATOM   510  C CD2 . LEU A 1 74  ? 20.184 17.718  12.420  1.00 21.61 ? 74  LEU A CD2 1 
ATOM   511  N N   . LYS A 1 75  ? 18.843 14.866  7.991   1.00 23.56 ? 75  LYS A N   1 
ATOM   512  C CA  . LYS A 1 75  ? 18.976 14.639  6.555   1.00 27.32 ? 75  LYS A CA  1 
ATOM   513  C C   . LYS A 1 75  ? 17.842 15.284  5.770   1.00 28.25 ? 75  LYS A C   1 
ATOM   514  O O   . LYS A 1 75  ? 17.938 15.449  4.556   1.00 31.26 ? 75  LYS A O   1 
ATOM   515  C CB  . LYS A 1 75  ? 19.017 13.135  6.259   1.00 27.14 ? 75  LYS A CB  1 
ATOM   516  C CG  . LYS A 1 75  ? 20.357 12.476  6.533   1.00 29.09 ? 75  LYS A CG  1 
ATOM   517  C CD  . LYS A 1 75  ? 21.382 12.893  5.492   1.00 31.21 ? 75  LYS A CD  1 
ATOM   518  C CE  . LYS A 1 75  ? 22.762 12.272  5.746   1.00 33.56 ? 75  LYS A CE  1 
ATOM   519  N NZ  . LYS A 1 75  ? 23.483 12.884  6.903   1.00 30.37 ? 75  LYS A NZ  1 
ATOM   520  N N   . LYS A 1 76  ? 16.779 15.670  6.463   1.00 28.93 ? 76  LYS A N   1 
ATOM   521  C CA  . LYS A 1 76  ? 15.629 16.275  5.802   1.00 30.56 ? 76  LYS A CA  1 
ATOM   522  C C   . LYS A 1 76  ? 15.745 17.777  5.540   1.00 30.36 ? 76  LYS A C   1 
ATOM   523  O O   . LYS A 1 76  ? 14.959 18.343  4.779   1.00 30.90 ? 76  LYS A O   1 
ATOM   524  C CB  . LYS A 1 76  ? 14.363 15.989  6.611   1.00 32.13 ? 76  LYS A CB  1 
ATOM   525  C CG  . LYS A 1 76  ? 13.998 14.508  6.677   1.00 36.77 ? 76  LYS A CG  1 
ATOM   526  C CD  . LYS A 1 76  ? 12.690 14.288  7.428   1.00 40.53 ? 76  LYS A CD  1 
ATOM   527  C CE  . LYS A 1 76  ? 11.527 15.000  6.741   1.00 42.89 ? 76  LYS A CE  1 
ATOM   528  N NZ  . LYS A 1 76  ? 10.248 14.830  7.488   1.00 44.12 ? 76  LYS A NZ  1 
ATOM   529  N N   . ASN A 1 77  ? 16.724 18.422  6.160   1.00 27.27 ? 77  ASN A N   1 
ATOM   530  C CA  . ASN A 1 77  ? 16.909 19.859  5.976   1.00 24.78 ? 77  ASN A CA  1 
ATOM   531  C C   . ASN A 1 77  ? 18.234 20.112  5.253   1.00 24.60 ? 77  ASN A C   1 
ATOM   532  O O   . ASN A 1 77  ? 19.296 19.687  5.715   1.00 23.65 ? 77  ASN A O   1 
ATOM   533  C CB  . ASN A 1 77  ? 16.914 20.552  7.342   1.00 24.46 ? 77  ASN A CB  1 
ATOM   534  C CG  . ASN A 1 77  ? 16.809 22.055  7.235   1.00 23.68 ? 77  ASN A CG  1 
ATOM   535  O OD1 . ASN A 1 77  ? 17.570 22.696  6.507   1.00 22.37 ? 77  ASN A OD1 1 
ATOM   536  N ND2 . ASN A 1 77  ? 15.866 22.632  7.970   1.00 23.67 ? 77  ASN A ND2 1 
ATOM   537  N N   . PRO A 1 78  ? 18.187 20.803  4.100   1.00 23.46 ? 78  PRO A N   1 
ATOM   538  C CA  . PRO A 1 78  ? 19.397 21.100  3.325   1.00 21.60 ? 78  PRO A CA  1 
ATOM   539  C C   . PRO A 1 78  ? 20.484 21.800  4.139   1.00 21.41 ? 78  PRO A C   1 
ATOM   540  O O   . PRO A 1 78  ? 21.664 21.673  3.837   1.00 21.55 ? 78  PRO A O   1 
ATOM   541  C CB  . PRO A 1 78  ? 18.871 21.977  2.188   1.00 21.84 ? 78  PRO A CB  1 
ATOM   542  C CG  . PRO A 1 78  ? 17.492 21.416  1.957   1.00 22.49 ? 78  PRO A CG  1 
ATOM   543  C CD  . PRO A 1 78  ? 16.981 21.256  3.381   1.00 23.75 ? 78  PRO A CD  1 
ATOM   544  N N   . GLN A 1 79  ? 20.091 22.534  5.172   1.00 20.62 ? 79  GLN A N   1 
ATOM   545  C CA  . GLN A 1 79  ? 21.073 23.235  5.996   1.00 22.65 ? 79  GLN A CA  1 
ATOM   546  C C   . GLN A 1 79  ? 21.922 22.277  6.822   1.00 22.05 ? 79  GLN A C   1 
ATOM   547  O O   . GLN A 1 79  ? 23.103 22.529  7.050   1.00 24.41 ? 79  GLN A O   1 
ATOM   548  C CB  . GLN A 1 79  ? 20.380 24.217  6.944   1.00 23.28 ? 79  GLN A CB  1 
ATOM   549  C CG  . GLN A 1 79  ? 19.700 25.388  6.263   1.00 27.79 ? 79  GLN A CG  1 
ATOM   550  C CD  . GLN A 1 79  ? 20.665 26.226  5.450   1.00 33.81 ? 79  GLN A CD  1 
ATOM   551  O OE1 . GLN A 1 79  ? 21.704 26.670  5.955   1.00 39.20 ? 79  GLN A OE1 1 
ATOM   552  N NE2 . GLN A 1 79  ? 20.331 26.453  4.185   1.00 34.03 ? 79  GLN A NE2 1 
ATOM   553  N N   . THR A 1 80  ? 21.325 21.168  7.245   1.00 20.96 ? 80  THR A N   1 
ATOM   554  C CA  . THR A 1 80  ? 22.020 20.205  8.099   1.00 20.79 ? 80  THR A CA  1 
ATOM   555  C C   . THR A 1 80  ? 22.305 18.822  7.513   1.00 21.66 ? 80  THR A C   1 
ATOM   556  O O   . THR A 1 80  ? 22.990 18.011  8.144   1.00 20.66 ? 80  THR A O   1 
ATOM   557  C CB  . THR A 1 80  ? 21.207 19.995  9.382   1.00 21.20 ? 80  THR A CB  1 
ATOM   558  O OG1 . THR A 1 80  ? 19.898 19.506  9.038   1.00 21.86 ? 80  THR A OG1 1 
ATOM   559  C CG2 . THR A 1 80  ? 21.063 21.317  10.134  1.00 23.37 ? 80  THR A CG2 1 
ATOM   560  N N   . ALA A 1 81  ? 21.786 18.559  6.316   1.00 20.29 ? 81  ALA A N   1 
ATOM   561  C CA  . ALA A 1 81  ? 21.935 17.257  5.670   1.00 20.64 ? 81  ALA A CA  1 
ATOM   562  C C   . ALA A 1 81  ? 23.348 16.745  5.431   1.00 21.68 ? 81  ALA A C   1 
ATOM   563  O O   . ALA A 1 81  ? 23.545 15.533  5.295   1.00 20.05 ? 81  ALA A O   1 
ATOM   564  C CB  . ALA A 1 81  ? 21.160 17.248  4.363   1.00 21.19 ? 81  ALA A CB  1 
ATOM   565  N N   . SER A 1 82  ? 24.324 17.648  5.355   1.00 18.11 ? 82  SER A N   1 
ATOM   566  C CA  . SER A 1 82  ? 25.701 17.232  5.129   1.00 21.24 ? 82  SER A CA  1 
ATOM   567  C C   . SER A 1 82  ? 26.603 17.343  6.353   1.00 20.58 ? 82  SER A C   1 
ATOM   568  O O   . SER A 1 82  ? 27.781 17.009  6.275   1.00 21.38 ? 82  SER A O   1 
ATOM   569  C CB  . SER A 1 82  ? 26.323 18.020  3.969   1.00 21.91 ? 82  SER A CB  1 
ATOM   570  O OG  . SER A 1 82  ? 25.761 17.619  2.731   1.00 24.78 ? 82  SER A OG  1 
ATOM   571  N N   . ILE A 1 83  ? 26.064 17.806  7.480   1.00 20.17 ? 83  ILE A N   1 
ATOM   572  C CA  . ILE A 1 83  ? 26.881 17.924  8.695   1.00 19.77 ? 83  ILE A CA  1 
ATOM   573  C C   . ILE A 1 83  ? 27.234 16.522  9.178   1.00 19.87 ? 83  ILE A C   1 
ATOM   574  O O   . ILE A 1 83  ? 26.360 15.667  9.288   1.00 19.40 ? 83  ILE A O   1 
ATOM   575  C CB  . ILE A 1 83  ? 26.125 18.645  9.821   1.00 19.32 ? 83  ILE A CB  1 
ATOM   576  C CG1 . ILE A 1 83  ? 25.824 20.092  9.410   1.00 21.04 ? 83  ILE A CG1 1 
ATOM   577  C CG2 . ILE A 1 83  ? 26.953 18.597  11.104  1.00 19.55 ? 83  ILE A CG2 1 
ATOM   578  C CD1 . ILE A 1 83  ? 24.920 20.842  10.406  1.00 20.94 ? 83  ILE A CD1 1 
ATOM   579  N N   . PRO A 1 84  ? 28.519 16.263  9.469   1.00 19.80 ? 84  PRO A N   1 
ATOM   580  C CA  . PRO A 1 84  ? 28.872 14.915  9.934   1.00 19.43 ? 84  PRO A CA  1 
ATOM   581  C C   . PRO A 1 84  ? 28.317 14.618  11.321  1.00 19.32 ? 84  PRO A C   1 
ATOM   582  O O   . PRO A 1 84  ? 28.240 15.505  12.172  1.00 19.61 ? 84  PRO A O   1 
ATOM   583  C CB  . PRO A 1 84  ? 30.401 14.920  9.901   1.00 20.09 ? 84  PRO A CB  1 
ATOM   584  C CG  . PRO A 1 84  ? 30.746 16.369  10.164  1.00 19.09 ? 84  PRO A CG  1 
ATOM   585  C CD  . PRO A 1 84  ? 29.723 17.102  9.312   1.00 20.15 ? 84  PRO A CD  1 
ATOM   586  N N   . VAL A 1 85  ? 27.930 13.366  11.541  1.00 18.24 ? 85  VAL A N   1 
ATOM   587  C CA  . VAL A 1 85  ? 27.366 12.968  12.832  1.00 18.05 ? 85  VAL A CA  1 
ATOM   588  C C   . VAL A 1 85  ? 28.111 11.771  13.411  1.00 18.04 ? 85  VAL A C   1 
ATOM   589  O O   . VAL A 1 85  ? 28.286 10.748  12.741  1.00 18.43 ? 85  VAL A O   1 
ATOM   590  C CB  . VAL A 1 85  ? 25.857 12.606  12.697  1.00 16.74 ? 85  VAL A CB  1 
ATOM   591  C CG1 . VAL A 1 85  ? 25.246 12.375  14.088  1.00 18.79 ? 85  VAL A CG1 1 
ATOM   592  C CG2 . VAL A 1 85  ? 25.108 13.733  11.975  1.00 17.92 ? 85  VAL A CG2 1 
ATOM   593  N N   . ILE A 1 86  ? 28.561 11.912  14.655  1.00 17.36 ? 86  ILE A N   1 
ATOM   594  C CA  . ILE A 1 86  ? 29.269 10.841  15.355  1.00 17.14 ? 86  ILE A CA  1 
ATOM   595  C C   . ILE A 1 86  ? 28.305 10.245  16.372  1.00 18.76 ? 86  ILE A C   1 
ATOM   596  O O   . ILE A 1 86  ? 27.619 10.985  17.079  1.00 19.96 ? 86  ILE A O   1 
ATOM   597  C CB  . ILE A 1 86  ? 30.500 11.372  16.138  1.00 17.24 ? 86  ILE A CB  1 
ATOM   598  C CG1 . ILE A 1 86  ? 31.608 11.802  15.168  1.00 16.34 ? 86  ILE A CG1 1 
ATOM   599  C CG2 . ILE A 1 86  ? 31.023 10.281  17.097  1.00 16.69 ? 86  ILE A CG2 1 
ATOM   600  C CD1 . ILE A 1 86  ? 32.830 12.351  15.878  1.00 18.47 ? 86  ILE A CD1 1 
ATOM   601  N N   . ALA A 1 87  ? 28.235 8.919   16.439  1.00 18.95 ? 87  ALA A N   1 
ATOM   602  C CA  . ALA A 1 87  ? 27.362 8.271   17.406  1.00 20.23 ? 87  ALA A CA  1 
ATOM   603  C C   . ALA A 1 87  ? 28.141 7.857   18.645  1.00 20.10 ? 87  ALA A C   1 
ATOM   604  O O   . ALA A 1 87  ? 29.269 7.376   18.553  1.00 20.46 ? 87  ALA A O   1 
ATOM   605  C CB  . ALA A 1 87  ? 26.689 7.042   16.788  1.00 19.10 ? 87  ALA A CB  1 
ATOM   606  N N   . LEU A 1 88  ? 27.519 8.056   19.801  1.00 21.71 ? 88  LEU A N   1 
ATOM   607  C CA  . LEU A 1 88  ? 28.091 7.691   21.087  1.00 23.64 ? 88  LEU A CA  1 
ATOM   608  C C   . LEU A 1 88  ? 27.128 6.650   21.651  1.00 23.64 ? 88  LEU A C   1 
ATOM   609  O O   . LEU A 1 88  ? 25.929 6.889   21.721  1.00 24.04 ? 88  LEU A O   1 
ATOM   610  C CB  . LEU A 1 88  ? 28.140 8.916   22.001  1.00 26.06 ? 88  LEU A CB  1 
ATOM   611  C CG  . LEU A 1 88  ? 29.506 9.498   22.367  1.00 30.17 ? 88  LEU A CG  1 
ATOM   612  C CD1 . LEU A 1 88  ? 30.386 9.646   21.139  1.00 28.58 ? 88  LEU A CD1 1 
ATOM   613  C CD2 . LEU A 1 88  ? 29.292 10.837  23.067  1.00 32.10 ? 88  LEU A CD2 1 
ATOM   614  N N   . SER A 1 89  ? 27.630 5.487   22.044  1.00 25.40 ? 89  SER A N   1 
ATOM   615  C CA  . SER A 1 89  ? 26.717 4.484   22.564  1.00 25.58 ? 89  SER A CA  1 
ATOM   616  C C   . SER A 1 89  ? 27.227 3.740   23.776  1.00 26.67 ? 89  SER A C   1 
ATOM   617  O O   . SER A 1 89  ? 28.397 3.356   23.846  1.00 23.54 ? 89  SER A O   1 
ATOM   618  C CB  . SER A 1 89  ? 26.357 3.477   21.471  1.00 27.17 ? 89  SER A CB  1 
ATOM   619  O OG  . SER A 1 89  ? 25.526 2.454   21.995  1.00 26.74 ? 89  SER A OG  1 
ATOM   620  N N   . GLY A 1 90  ? 26.325 3.546   24.731  1.00 28.58 ? 90  GLY A N   1 
ATOM   621  C CA  . GLY A 1 90  ? 26.665 2.829   25.942  1.00 32.25 ? 90  GLY A CA  1 
ATOM   622  C C   . GLY A 1 90  ? 26.488 1.332   25.769  1.00 32.71 ? 90  GLY A C   1 
ATOM   623  O O   . GLY A 1 90  ? 26.728 0.568   26.702  1.00 34.51 ? 90  GLY A O   1 
ATOM   624  N N   . ARG A 1 91  ? 26.055 0.909   24.584  1.00 32.46 ? 91  ARG A N   1 
ATOM   625  C CA  . ARG A 1 91  ? 25.867 -0.513  24.299  1.00 33.84 ? 91  ARG A CA  1 
ATOM   626  C C   . ARG A 1 91  ? 27.038 -0.975  23.449  1.00 33.67 ? 91  ARG A C   1 
ATOM   627  O O   . ARG A 1 91  ? 27.793 -1.869  23.829  1.00 34.79 ? 91  ARG A O   1 
ATOM   628  C CB  . ARG A 1 91  ? 24.546 -0.738  23.559  1.00 34.24 ? 91  ARG A CB  1 
ATOM   629  C CG  . ARG A 1 91  ? 23.360 -0.230  24.341  1.00 37.26 ? 91  ARG A CG  1 
ATOM   630  C CD  . ARG A 1 91  ? 22.035 -0.614  23.712  1.00 40.21 ? 91  ARG A CD  1 
ATOM   631  N NE  . ARG A 1 91  ? 20.935 -0.261  24.606  1.00 42.57 ? 91  ARG A NE  1 
ATOM   632  C CZ  . ARG A 1 91  ? 19.662 -0.577  24.399  1.00 42.21 ? 91  ARG A CZ  1 
ATOM   633  N NH1 . ARG A 1 91  ? 19.312 -1.261  23.316  1.00 40.92 ? 91  ARG A NH1 1 
ATOM   634  N NH2 . ARG A 1 91  ? 18.741 -0.214  25.283  1.00 42.55 ? 91  ARG A NH2 1 
ATOM   635  N N   . ALA A 1 92  ? 27.187 -0.355  22.289  1.00 33.43 ? 92  ALA A N   1 
ATOM   636  C CA  . ALA A 1 92  ? 28.296 -0.661  21.404  1.00 31.97 ? 92  ALA A CA  1 
ATOM   637  C C   . ALA A 1 92  ? 28.512 -2.134  21.042  1.00 31.43 ? 92  ALA A C   1 
ATOM   638  O O   . ALA A 1 92  ? 29.635 -2.645  21.113  1.00 31.24 ? 92  ALA A O   1 
ATOM   639  C CB  . ALA A 1 92  ? 29.576 -0.081  21.991  1.00 31.67 ? 92  ALA A CB  1 
ATOM   640  N N   . THR A 1 93  ? 27.444 -2.823  20.664  1.00 28.24 ? 93  THR A N   1 
ATOM   641  C CA  . THR A 1 93  ? 27.589 -4.199  20.222  1.00 27.74 ? 93  THR A CA  1 
ATOM   642  C C   . THR A 1 93  ? 28.206 -4.048  18.828  1.00 29.11 ? 93  THR A C   1 
ATOM   643  O O   . THR A 1 93  ? 28.153 -2.959  18.245  1.00 25.83 ? 93  THR A O   1 
ATOM   644  C CB  . THR A 1 93  ? 26.227 -4.892  20.085  1.00 27.82 ? 93  THR A CB  1 
ATOM   645  O OG1 . THR A 1 93  ? 25.368 -4.091  19.261  1.00 29.73 ? 93  THR A OG1 1 
ATOM   646  C CG2 . THR A 1 93  ? 25.580 -5.079  21.459  1.00 29.47 ? 93  THR A CG2 1 
ATOM   647  N N   . ALA A 1 94  ? 28.790 -5.119  18.297  1.00 29.39 ? 94  ALA A N   1 
ATOM   648  C CA  . ALA A 1 94  ? 29.391 -5.061  16.968  1.00 28.66 ? 94  ALA A CA  1 
ATOM   649  C C   . ALA A 1 94  ? 28.296 -4.771  15.956  1.00 28.47 ? 94  ALA A C   1 
ATOM   650  O O   . ALA A 1 94  ? 28.497 -4.013  15.003  1.00 24.89 ? 94  ALA A O   1 
ATOM   651  C CB  . ALA A 1 94  ? 30.074 -6.385  16.633  1.00 30.16 ? 94  ALA A CB  1 
ATOM   652  N N   . LYS A 1 95  ? 27.126 -5.369  16.175  1.00 27.59 ? 95  LYS A N   1 
ATOM   653  C CA  . LYS A 1 95  ? 26.004 -5.174  15.274  1.00 28.50 ? 95  LYS A CA  1 
ATOM   654  C C   . LYS A 1 95  ? 25.504 -3.736  15.301  1.00 27.22 ? 95  LYS A C   1 
ATOM   655  O O   . LYS A 1 95  ? 25.136 -3.199  14.266  1.00 25.94 ? 95  LYS A O   1 
ATOM   656  C CB  . LYS A 1 95  ? 24.857 -6.126  15.623  1.00 32.03 ? 95  LYS A CB  1 
ATOM   657  C CG  . LYS A 1 95  ? 23.689 -6.045  14.646  1.00 36.06 ? 95  LYS A CG  1 
ATOM   658  C CD  . LYS A 1 95  ? 22.591 -7.037  14.995  1.00 41.31 ? 95  LYS A CD  1 
ATOM   659  C CE  . LYS A 1 95  ? 23.041 -8.479  14.795  1.00 42.01 ? 95  LYS A CE  1 
ATOM   660  N NZ  . LYS A 1 95  ? 23.144 -8.852  13.355  1.00 45.88 ? 95  LYS A NZ  1 
ATOM   661  N N   . GLU A 1 96  ? 25.486 -3.109  16.475  1.00 25.06 ? 96  GLU A N   1 
ATOM   662  C CA  . GLU A 1 96  ? 25.020 -1.726  16.550  1.00 26.15 ? 96  GLU A CA  1 
ATOM   663  C C   . GLU A 1 96  ? 26.017 -0.819  15.850  1.00 23.19 ? 96  GLU A C   1 
ATOM   664  O O   . GLU A 1 96  ? 25.631 0.067   15.081  1.00 24.83 ? 96  GLU A O   1 
ATOM   665  C CB  . GLU A 1 96  ? 24.871 -1.255  17.995  1.00 26.59 ? 96  GLU A CB  1 
ATOM   666  C CG  . GLU A 1 96  ? 24.251 0.139   18.100  1.00 31.30 ? 96  GLU A CG  1 
ATOM   667  C CD  . GLU A 1 96  ? 24.401 0.752   19.479  1.00 32.64 ? 96  GLU A CD  1 
ATOM   668  O OE1 . GLU A 1 96  ? 23.477 1.463   19.919  1.00 38.10 ? 96  GLU A OE1 1 
ATOM   669  O OE2 . GLU A 1 96  ? 25.449 0.536   20.120  1.00 36.63 ? 96  GLU A OE2 1 
ATOM   670  N N   . GLU A 1 97  ? 27.301 -1.038  16.125  1.00 22.15 ? 97  GLU A N   1 
ATOM   671  C CA  . GLU A 1 97  ? 28.349 -0.233  15.502  1.00 22.20 ? 97  GLU A CA  1 
ATOM   672  C C   . GLU A 1 97  ? 28.219 -0.317  13.987  1.00 22.69 ? 97  GLU A C   1 
ATOM   673  O O   . GLU A 1 97  ? 28.186 0.710   13.305  1.00 20.82 ? 97  GLU A O   1 
ATOM   674  C CB  . GLU A 1 97  ? 29.743 -0.709  15.937  1.00 21.43 ? 97  GLU A CB  1 
ATOM   675  C CG  . GLU A 1 97  ? 30.902 0.112   15.326  1.00 20.86 ? 97  GLU A CG  1 
ATOM   676  C CD  . GLU A 1 97  ? 32.245 -0.160  15.996  1.00 25.11 ? 97  GLU A CD  1 
ATOM   677  O OE1 . GLU A 1 97  ? 32.263 -0.785  17.082  1.00 24.80 ? 97  GLU A OE1 1 
ATOM   678  O OE2 . GLU A 1 97  ? 33.286 0.264   15.441  1.00 25.71 ? 97  GLU A OE2 1 
ATOM   679  N N   . ALA A 1 98  ? 28.131 -1.540  13.458  1.00 22.95 ? 98  ALA A N   1 
ATOM   680  C CA  . ALA A 1 98  ? 27.996 -1.722  12.013  1.00 22.35 ? 98  ALA A CA  1 
ATOM   681  C C   . ALA A 1 98  ? 26.733 -1.066  11.461  1.00 21.93 ? 98  ALA A C   1 
ATOM   682  O O   . ALA A 1 98  ? 26.779 -0.432  10.410  1.00 22.07 ? 98  ALA A O   1 
ATOM   683  C CB  . ALA A 1 98  ? 28.016 -3.211  11.653  1.00 24.66 ? 98  ALA A CB  1 
ATOM   684  N N   . GLN A 1 99  ? 25.604 -1.207  12.158  1.00 22.28 ? 99  GLN A N   1 
ATOM   685  C CA  . GLN A 1 99  ? 24.365 -0.591  11.677  1.00 24.35 ? 99  GLN A CA  1 
ATOM   686  C C   . GLN A 1 99  ? 24.467 0.934   11.567  1.00 23.66 ? 99  GLN A C   1 
ATOM   687  O O   . GLN A 1 99  ? 24.054 1.524   10.562  1.00 22.88 ? 99  GLN A O   1 
ATOM   688  C CB  . GLN A 1 99  ? 23.185 -0.946  12.592  1.00 29.06 ? 99  GLN A CB  1 
ATOM   689  C CG  . GLN A 1 99  ? 21.950 -0.063  12.367  1.00 35.08 ? 99  GLN A CG  1 
ATOM   690  C CD  . GLN A 1 99  ? 20.777 -0.429  13.271  1.00 39.38 ? 99  GLN A CD  1 
ATOM   691  O OE1 . GLN A 1 99  ? 20.955 -0.712  14.460  1.00 41.04 ? 99  GLN A OE1 1 
ATOM   692  N NE2 . GLN A 1 99  ? 19.570 -0.409  12.713  1.00 40.17 ? 99  GLN A NE2 1 
ATOM   693  N N   . LEU A 1 100 ? 25.013 1.577   12.595  1.00 21.20 ? 100 LEU A N   1 
ATOM   694  C CA  . LEU A 1 100 ? 25.136 3.033   12.574  1.00 22.53 ? 100 LEU A CA  1 
ATOM   695  C C   . LEU A 1 100 ? 26.110 3.495   11.492  1.00 19.53 ? 100 LEU A C   1 
ATOM   696  O O   . LEU A 1 100 ? 25.821 4.428   10.739  1.00 19.60 ? 100 LEU A O   1 
ATOM   697  C CB  . LEU A 1 100 ? 25.578 3.546   13.941  1.00 24.01 ? 100 LEU A CB  1 
ATOM   698  C CG  . LEU A 1 100 ? 24.551 3.335   15.060  1.00 30.08 ? 100 LEU A CG  1 
ATOM   699  C CD1 . LEU A 1 100 ? 25.063 3.988   16.343  1.00 30.95 ? 100 LEU A CD1 1 
ATOM   700  C CD2 . LEU A 1 100 ? 23.213 3.928   14.661  1.00 31.14 ? 100 LEU A CD2 1 
ATOM   701  N N   . LEU A 1 101 ? 27.258 2.841   11.403  1.00 20.31 ? 101 LEU A N   1 
ATOM   702  C CA  . LEU A 1 101 ? 28.222 3.204   10.367  1.00 19.94 ? 101 LEU A CA  1 
ATOM   703  C C   . LEU A 1 101 ? 27.618 2.972   8.972   1.00 20.81 ? 101 LEU A C   1 
ATOM   704  O O   . LEU A 1 101 ? 27.801 3.787   8.066   1.00 19.89 ? 101 LEU A O   1 
ATOM   705  C CB  . LEU A 1 101 ? 29.514 2.387   10.517  1.00 19.42 ? 101 LEU A CB  1 
ATOM   706  C CG  . LEU A 1 101 ? 30.399 2.696   11.730  1.00 22.54 ? 101 LEU A CG  1 
ATOM   707  C CD1 . LEU A 1 101 ? 31.651 1.836   11.682  1.00 19.90 ? 101 LEU A CD1 1 
ATOM   708  C CD2 . LEU A 1 101 ? 30.782 4.174   11.725  1.00 21.76 ? 101 LEU A CD2 1 
ATOM   709  N N   . ASP A 1 102 ? 26.897 1.865   8.802   1.00 21.28 ? 102 ASP A N   1 
ATOM   710  C CA  . ASP A 1 102 ? 26.295 1.555   7.498   1.00 23.58 ? 102 ASP A CA  1 
ATOM   711  C C   . ASP A 1 102 ? 25.276 2.607   7.071   1.00 23.82 ? 102 ASP A C   1 
ATOM   712  O O   . ASP A 1 102 ? 25.131 2.889   5.881   1.00 23.79 ? 102 ASP A O   1 
ATOM   713  C CB  . ASP A 1 102 ? 25.649 0.161   7.514   1.00 24.95 ? 102 ASP A CB  1 
ATOM   714  C CG  . ASP A 1 102 ? 26.682 -0.965  7.576   1.00 30.77 ? 102 ASP A CG  1 
ATOM   715  O OD1 . ASP A 1 102 ? 27.851 -0.743  7.194   1.00 32.49 ? 102 ASP A OD1 1 
ATOM   716  O OD2 . ASP A 1 102 ? 26.329 -2.086  7.993   1.00 33.64 ? 102 ASP A OD2 1 
ATOM   717  N N   . MET A 1 103 ? 24.593 3.184   8.060   1.00 23.96 ? 103 MET A N   1 
ATOM   718  C CA  . MET A 1 103 ? 23.583 4.238   7.890   1.00 24.59 ? 103 MET A CA  1 
ATOM   719  C C   . MET A 1 103 ? 24.166 5.559   7.414   1.00 23.93 ? 103 MET A C   1 
ATOM   720  O O   . MET A 1 103 ? 23.470 6.360   6.778   1.00 24.72 ? 103 MET A O   1 
ATOM   721  C CB  . MET A 1 103 ? 22.918 4.551   9.225   1.00 26.70 ? 103 MET A CB  1 
ATOM   722  C CG  . MET A 1 103 ? 21.607 3.910   9.486   1.00 29.39 ? 103 MET A CG  1 
ATOM   723  S SD  . MET A 1 103 ? 21.068 4.485   11.093  1.00 18.59 ? 103 MET A SD  1 
ATOM   724  C CE  . MET A 1 103 ? 20.252 6.009   10.670  1.00 22.08 ? 103 MET A CE  1 
ATOM   725  N N   . GLY A 1 104 ? 25.419 5.817   7.775   1.00 21.25 ? 104 GLY A N   1 
ATOM   726  C CA  . GLY A 1 104 ? 26.036 7.066   7.372   1.00 20.80 ? 104 GLY A CA  1 
ATOM   727  C C   . GLY A 1 104 ? 26.668 7.851   8.509   1.00 20.15 ? 104 GLY A C   1 
ATOM   728  O O   . GLY A 1 104 ? 27.229 8.929   8.282   1.00 18.30 ? 104 GLY A O   1 
ATOM   729  N N   . PHE A 1 105 ? 26.561 7.351   9.737   1.00 18.12 ? 105 PHE A N   1 
ATOM   730  C CA  . PHE A 1 105 ? 27.202 8.042   10.854  1.00 19.30 ? 105 PHE A CA  1 
ATOM   731  C C   . PHE A 1 105 ? 28.682 8.089   10.486  1.00 19.28 ? 105 PHE A C   1 
ATOM   732  O O   . PHE A 1 105 ? 29.249 7.083   10.050  1.00 17.66 ? 105 PHE A O   1 
ATOM   733  C CB  . PHE A 1 105 ? 26.992 7.272   12.163  1.00 18.84 ? 105 PHE A CB  1 
ATOM   734  C CG  . PHE A 1 105 ? 25.692 7.605   12.860  1.00 20.33 ? 105 PHE A CG  1 
ATOM   735  C CD1 . PHE A 1 105 ? 25.625 8.652   13.771  1.00 18.93 ? 105 PHE A CD1 1 
ATOM   736  C CD2 . PHE A 1 105 ? 24.525 6.892   12.572  1.00 20.62 ? 105 PHE A CD2 1 
ATOM   737  C CE1 . PHE A 1 105 ? 24.410 8.995   14.392  1.00 19.78 ? 105 PHE A CE1 1 
ATOM   738  C CE2 . PHE A 1 105 ? 23.304 7.227   13.187  1.00 20.24 ? 105 PHE A CE2 1 
ATOM   739  C CZ  . PHE A 1 105 ? 23.250 8.277   14.094  1.00 20.51 ? 105 PHE A CZ  1 
ATOM   740  N N   . ILE A 1 106 ? 29.311 9.248   10.650  1.00 16.48 ? 106 ILE A N   1 
ATOM   741  C CA  . ILE A 1 106 ? 30.716 9.376   10.264  1.00 19.03 ? 106 ILE A CA  1 
ATOM   742  C C   . ILE A 1 106 ? 31.682 8.617   11.173  1.00 18.69 ? 106 ILE A C   1 
ATOM   743  O O   . ILE A 1 106 ? 32.797 8.280   10.762  1.00 20.22 ? 106 ILE A O   1 
ATOM   744  C CB  . ILE A 1 106 ? 31.127 10.864  10.167  1.00 19.39 ? 106 ILE A CB  1 
ATOM   745  C CG1 . ILE A 1 106 ? 32.295 11.004  9.192   1.00 23.77 ? 106 ILE A CG1 1 
ATOM   746  C CG2 . ILE A 1 106 ? 31.465 11.407  11.542  1.00 19.79 ? 106 ILE A CG2 1 
ATOM   747  C CD1 . ILE A 1 106 ? 32.573 12.433  8.795   1.00 27.27 ? 106 ILE A CD1 1 
ATOM   748  N N   . ASP A 1 107 ? 31.273 8.366   12.411  1.00 18.03 ? 107 ASP A N   1 
ATOM   749  C CA  . ASP A 1 107 ? 32.100 7.599   13.344  1.00 19.19 ? 107 ASP A CA  1 
ATOM   750  C C   . ASP A 1 107 ? 31.210 7.047   14.456  1.00 18.62 ? 107 ASP A C   1 
ATOM   751  O O   . ASP A 1 107 ? 30.045 7.441   14.591  1.00 17.72 ? 107 ASP A O   1 
ATOM   752  C CB  . ASP A 1 107 ? 33.230 8.451   13.952  1.00 19.41 ? 107 ASP A CB  1 
ATOM   753  C CG  . ASP A 1 107 ? 34.460 7.611   14.328  1.00 22.85 ? 107 ASP A CG  1 
ATOM   754  O OD1 . ASP A 1 107 ? 34.315 6.386   14.544  1.00 25.49 ? 107 ASP A OD1 1 
ATOM   755  O OD2 . ASP A 1 107 ? 35.574 8.170   14.415  1.00 22.90 ? 107 ASP A OD2 1 
ATOM   756  N N   . PHE A 1 108 ? 31.762 6.125   15.236  1.00 18.50 ? 108 PHE A N   1 
ATOM   757  C CA  . PHE A 1 108 ? 31.037 5.495   16.335  1.00 20.72 ? 108 PHE A CA  1 
ATOM   758  C C   . PHE A 1 108 ? 31.995 5.350   17.512  1.00 22.30 ? 108 PHE A C   1 
ATOM   759  O O   . PHE A 1 108 ? 33.088 4.793   17.364  1.00 22.53 ? 108 PHE A O   1 
ATOM   760  C CB  . PHE A 1 108 ? 30.538 4.119   15.897  1.00 22.22 ? 108 PHE A CB  1 
ATOM   761  C CG  . PHE A 1 108 ? 29.804 3.367   16.973  1.00 23.85 ? 108 PHE A CG  1 
ATOM   762  C CD1 . PHE A 1 108 ? 28.425 3.485   17.105  1.00 25.30 ? 108 PHE A CD1 1 
ATOM   763  C CD2 . PHE A 1 108 ? 30.497 2.540   17.855  1.00 27.81 ? 108 PHE A CD2 1 
ATOM   764  C CE1 . PHE A 1 108 ? 27.738 2.786   18.102  1.00 27.94 ? 108 PHE A CE1 1 
ATOM   765  C CE2 . PHE A 1 108 ? 29.826 1.835   18.858  1.00 28.82 ? 108 PHE A CE2 1 
ATOM   766  C CZ  . PHE A 1 108 ? 28.441 1.959   18.980  1.00 28.93 ? 108 PHE A CZ  1 
ATOM   767  N N   . ILE A 1 109 ? 31.591 5.848   18.675  1.00 22.04 ? 109 ILE A N   1 
ATOM   768  C CA  . ILE A 1 109 ? 32.436 5.785   19.860  1.00 24.39 ? 109 ILE A CA  1 
ATOM   769  C C   . ILE A 1 109 ? 31.691 5.157   21.023  1.00 24.35 ? 109 ILE A C   1 
ATOM   770  O O   . ILE A 1 109 ? 30.607 5.607   21.396  1.00 24.53 ? 109 ILE A O   1 
ATOM   771  C CB  . ILE A 1 109 ? 32.894 7.194   20.284  1.00 25.62 ? 109 ILE A CB  1 
ATOM   772  C CG1 . ILE A 1 109 ? 33.563 7.900   19.101  1.00 26.34 ? 109 ILE A CG1 1 
ATOM   773  C CG2 . ILE A 1 109 ? 33.864 7.097   21.467  1.00 27.98 ? 109 ILE A CG2 1 
ATOM   774  C CD1 . ILE A 1 109 ? 33.937 9.345   19.395  1.00 26.28 ? 109 ILE A CD1 1 
ATOM   775  N N   . ALA A 1 110 ? 32.280 4.114   21.596  1.00 25.13 ? 110 ALA A N   1 
ATOM   776  C CA  . ALA A 1 110 ? 31.669 3.426   22.722  1.00 26.33 ? 110 ALA A CA  1 
ATOM   777  C C   . ALA A 1 110 ? 31.915 4.145   24.044  1.00 28.34 ? 110 ALA A C   1 
ATOM   778  O O   . ALA A 1 110 ? 33.032 4.587   24.323  1.00 29.12 ? 110 ALA A O   1 
ATOM   779  C CB  . ALA A 1 110 ? 32.202 1.999   22.807  1.00 28.03 ? 110 ALA A CB  1 
ATOM   780  N N   . LYS A 1 111 ? 30.861 4.280   24.842  1.00 29.30 ? 111 LYS A N   1 
ATOM   781  C CA  . LYS A 1 111 ? 30.968 4.889   26.162  1.00 32.95 ? 111 LYS A CA  1 
ATOM   782  C C   . LYS A 1 111 ? 31.596 3.811   27.055  1.00 35.36 ? 111 LYS A C   1 
ATOM   783  O O   . LYS A 1 111 ? 31.568 2.629   26.713  1.00 35.77 ? 111 LYS A O   1 
ATOM   784  C CB  . LYS A 1 111 ? 29.579 5.250   26.707  1.00 32.90 ? 111 LYS A CB  1 
ATOM   785  C CG  . LYS A 1 111 ? 28.903 6.453   26.060  1.00 34.70 ? 111 LYS A CG  1 
ATOM   786  C CD  . LYS A 1 111 ? 27.481 6.601   26.593  1.00 37.46 ? 111 LYS A CD  1 
ATOM   787  C CE  . LYS A 1 111 ? 27.035 8.059   26.691  1.00 39.56 ? 111 LYS A CE  1 
ATOM   788  N NZ  . LYS A 1 111 ? 27.059 8.769   25.392  1.00 43.47 ? 111 LYS A NZ  1 
ATOM   789  N N   . PRO A 1 112 ? 32.184 4.201   28.200  1.00 37.48 ? 112 PRO A N   1 
ATOM   790  C CA  . PRO A 1 112 ? 32.292 5.576   28.688  1.00 38.32 ? 112 PRO A CA  1 
ATOM   791  C C   . PRO A 1 112 ? 33.210 6.386   27.788  1.00 39.18 ? 112 PRO A C   1 
ATOM   792  O O   . PRO A 1 112 ? 34.129 5.848   27.170  1.00 39.55 ? 112 PRO A O   1 
ATOM   793  C CB  . PRO A 1 112 ? 32.852 5.397   30.099  1.00 39.21 ? 112 PRO A CB  1 
ATOM   794  C CG  . PRO A 1 112 ? 33.683 4.167   29.969  1.00 38.74 ? 112 PRO A CG  1 
ATOM   795  C CD  . PRO A 1 112 ? 32.785 3.263   29.166  1.00 37.36 ? 112 PRO A CD  1 
ATOM   796  N N   . VAL A 1 113 ? 32.946 7.684   27.720  1.00 40.66 ? 113 VAL A N   1 
ATOM   797  C CA  . VAL A 1 113 ? 33.718 8.586   26.888  1.00 41.07 ? 113 VAL A CA  1 
ATOM   798  C C   . VAL A 1 113 ? 35.039 9.005   27.515  1.00 40.98 ? 113 VAL A C   1 
ATOM   799  O O   . VAL A 1 113 ? 35.108 9.331   28.699  1.00 40.93 ? 113 VAL A O   1 
ATOM   800  C CB  . VAL A 1 113 ? 32.910 9.858   26.580  1.00 42.85 ? 113 VAL A CB  1 
ATOM   801  C CG1 . VAL A 1 113 ? 33.722 10.796  25.698  1.00 44.05 ? 113 VAL A CG1 1 
ATOM   802  C CG2 . VAL A 1 113 ? 31.601 9.484   25.909  1.00 43.54 ? 113 VAL A CG2 1 
ATOM   803  N N   . ASN A 1 114 ? 36.089 8.979   26.707  1.00 39.85 ? 114 ASN A N   1 
ATOM   804  C CA  . ASN A 1 114 ? 37.406 9.396   27.146  1.00 38.90 ? 114 ASN A CA  1 
ATOM   805  C C   . ASN A 1 114 ? 37.727 10.671  26.367  1.00 38.15 ? 114 ASN A C   1 
ATOM   806  O O   . ASN A 1 114 ? 37.786 10.661  25.137  1.00 37.28 ? 114 ASN A O   1 
ATOM   807  C CB  . ASN A 1 114 ? 38.441 8.317   26.843  1.00 40.43 ? 114 ASN A CB  1 
ATOM   808  C CG  . ASN A 1 114 ? 39.849 8.765   27.173  1.00 42.23 ? 114 ASN A CG  1 
ATOM   809  O OD1 . ASN A 1 114 ? 40.331 9.770   26.643  1.00 41.29 ? 114 ASN A OD1 1 
ATOM   810  N ND2 . ASN A 1 114 ? 40.518 8.026   28.053  1.00 43.13 ? 114 ASN A ND2 1 
ATOM   811  N N   . ALA A 1 115 ? 37.926 11.767  27.090  1.00 36.32 ? 115 ALA A N   1 
ATOM   812  C CA  . ALA A 1 115 ? 38.215 13.058  26.476  1.00 35.33 ? 115 ALA A CA  1 
ATOM   813  C C   . ALA A 1 115 ? 39.349 13.055  25.446  1.00 33.14 ? 115 ALA A C   1 
ATOM   814  O O   . ALA A 1 115 ? 39.254 13.726  24.425  1.00 32.62 ? 115 ALA A O   1 
ATOM   815  C CB  . ALA A 1 115 ? 38.499 14.092  27.564  1.00 35.84 ? 115 ALA A CB  1 
ATOM   816  N N   . ILE A 1 116 ? 40.421 12.311  25.705  1.00 32.26 ? 116 ILE A N   1 
ATOM   817  C CA  . ILE A 1 116 ? 41.546 12.265  24.767  1.00 31.94 ? 116 ILE A CA  1 
ATOM   818  C C   . ILE A 1 116 ? 41.130 11.586  23.463  1.00 30.72 ? 116 ILE A C   1 
ATOM   819  O O   . ILE A 1 116 ? 41.469 12.046  22.369  1.00 30.34 ? 116 ILE A O   1 
ATOM   820  C CB  . ILE A 1 116 ? 42.754 11.504  25.371  1.00 33.63 ? 116 ILE A CB  1 
ATOM   821  C CG1 . ILE A 1 116 ? 43.287 12.262  26.593  1.00 36.14 ? 116 ILE A CG1 1 
ATOM   822  C CG2 . ILE A 1 116 ? 43.857 11.354  24.332  1.00 32.18 ? 116 ILE A CG2 1 
ATOM   823  C CD1 . ILE A 1 116 ? 44.434 11.555  27.308  1.00 37.30 ? 116 ILE A CD1 1 
ATOM   824  N N   . ARG A 1 117 ? 40.387 10.495  23.595  1.00 30.26 ? 117 ARG A N   1 
ATOM   825  C CA  . ARG A 1 117 ? 39.901 9.731   22.452  1.00 30.96 ? 117 ARG A CA  1 
ATOM   826  C C   . ARG A 1 117 ? 38.870 10.541  21.669  1.00 29.60 ? 117 ARG A C   1 
ATOM   827  O O   . ARG A 1 117 ? 38.935 10.631  20.442  1.00 26.51 ? 117 ARG A O   1 
ATOM   828  C CB  . ARG A 1 117 ? 39.276 8.422   22.949  1.00 35.03 ? 117 ARG A CB  1 
ATOM   829  C CG  . ARG A 1 117 ? 38.869 7.440   21.866  1.00 40.12 ? 117 ARG A CG  1 
ATOM   830  C CD  . ARG A 1 117 ? 38.673 6.042   22.464  1.00 43.54 ? 117 ARG A CD  1 
ATOM   831  N NE  . ARG A 1 117 ? 39.848 5.631   23.231  1.00 47.54 ? 117 ARG A NE  1 
ATOM   832  C CZ  . ARG A 1 117 ? 40.007 4.432   23.783  1.00 48.56 ? 117 ARG A CZ  1 
ATOM   833  N NH1 . ARG A 1 117 ? 39.064 3.508   23.658  1.00 51.40 ? 117 ARG A NH1 1 
ATOM   834  N NH2 . ARG A 1 117 ? 41.110 4.155   24.462  1.00 50.35 ? 117 ARG A NH2 1 
ATOM   835  N N   . LEU A 1 118 ? 37.927 11.142  22.386  1.00 28.35 ? 118 LEU A N   1 
ATOM   836  C CA  . LEU A 1 118 ? 36.880 11.933  21.744  1.00 28.21 ? 118 LEU A CA  1 
ATOM   837  C C   . LEU A 1 118 ? 37.455 13.117  20.971  1.00 27.02 ? 118 LEU A C   1 
ATOM   838  O O   . LEU A 1 118 ? 37.057 13.384  19.840  1.00 25.02 ? 118 LEU A O   1 
ATOM   839  C CB  . LEU A 1 118 ? 35.887 12.437  22.790  1.00 26.89 ? 118 LEU A CB  1 
ATOM   840  C CG  . LEU A 1 118 ? 34.706 13.245  22.245  1.00 30.22 ? 118 LEU A CG  1 
ATOM   841  C CD1 . LEU A 1 118 ? 33.943 12.421  21.207  1.00 28.62 ? 118 LEU A CD1 1 
ATOM   842  C CD2 . LEU A 1 118 ? 33.789 13.629  23.396  1.00 30.26 ? 118 LEU A CD2 1 
ATOM   843  N N   . SER A 1 119 ? 38.397 13.821  21.589  1.00 26.92 ? 119 SER A N   1 
ATOM   844  C CA  . SER A 1 119 ? 39.028 14.970  20.955  1.00 26.96 ? 119 SER A CA  1 
ATOM   845  C C   . SER A 1 119 ? 39.682 14.588  19.631  1.00 26.23 ? 119 SER A C   1 
ATOM   846  O O   . SER A 1 119 ? 39.461 15.242  18.611  1.00 26.77 ? 119 SER A O   1 
ATOM   847  C CB  . SER A 1 119 ? 40.080 15.573  21.884  1.00 29.49 ? 119 SER A CB  1 
ATOM   848  O OG  . SER A 1 119 ? 40.764 16.637  21.242  1.00 35.00 ? 119 SER A OG  1 
ATOM   849  N N   . ALA A 1 120 ? 40.493 13.534  19.653  1.00 23.55 ? 120 ALA A N   1 
ATOM   850  C CA  . ALA A 1 120 ? 41.177 13.071  18.449  1.00 24.22 ? 120 ALA A CA  1 
ATOM   851  C C   . ALA A 1 120 ? 40.190 12.624  17.362  1.00 23.22 ? 120 ALA A C   1 
ATOM   852  O O   . ALA A 1 120 ? 40.418 12.861  16.178  1.00 23.62 ? 120 ALA A O   1 
ATOM   853  C CB  . ALA A 1 120 ? 42.117 11.922  18.800  1.00 26.40 ? 120 ALA A CB  1 
ATOM   854  N N   . ARG A 1 121 ? 39.103 11.974  17.773  1.00 22.97 ? 121 ARG A N   1 
ATOM   855  C CA  . ARG A 1 121 ? 38.082 11.481  16.838  1.00 23.37 ? 121 ARG A CA  1 
ATOM   856  C C   . ARG A 1 121 ? 37.378 12.642  16.136  1.00 22.39 ? 121 ARG A C   1 
ATOM   857  O O   . ARG A 1 121 ? 37.113 12.589  14.935  1.00 22.58 ? 121 ARG A O   1 
ATOM   858  C CB  . ARG A 1 121 ? 37.061 10.618  17.591  1.00 23.62 ? 121 ARG A CB  1 
ATOM   859  C CG  . ARG A 1 121 ? 37.591 9.245   18.005  1.00 25.87 ? 121 ARG A CG  1 
ATOM   860  C CD  . ARG A 1 121 ? 37.515 8.275   16.842  1.00 27.54 ? 121 ARG A CD  1 
ATOM   861  N NE  . ARG A 1 121 ? 38.183 7.001   17.099  1.00 25.30 ? 121 ARG A NE  1 
ATOM   862  C CZ  . ARG A 1 121 ? 38.264 6.024   16.202  1.00 25.05 ? 121 ARG A CZ  1 
ATOM   863  N NH1 . ARG A 1 121 ? 37.712 6.186   15.007  1.00 25.24 ? 121 ARG A NH1 1 
ATOM   864  N NH2 . ARG A 1 121 ? 38.907 4.898   16.486  1.00 22.60 ? 121 ARG A NH2 1 
ATOM   865  N N   . ILE A 1 122 ? 37.077 13.686  16.897  1.00 21.36 ? 122 ILE A N   1 
ATOM   866  C CA  . ILE A 1 122 ? 36.439 14.883  16.361  1.00 22.60 ? 122 ILE A CA  1 
ATOM   867  C C   . ILE A 1 122 ? 37.386 15.536  15.358  1.00 22.82 ? 122 ILE A C   1 
ATOM   868  O O   . ILE A 1 122 ? 37.005 15.821  14.221  1.00 21.13 ? 122 ILE A O   1 
ATOM   869  C CB  . ILE A 1 122 ? 36.126 15.898  17.492  1.00 22.18 ? 122 ILE A CB  1 
ATOM   870  C CG1 . ILE A 1 122 ? 35.031 15.330  18.400  1.00 22.77 ? 122 ILE A CG1 1 
ATOM   871  C CG2 . ILE A 1 122 ? 35.706 17.249  16.902  1.00 24.58 ? 122 ILE A CG2 1 
ATOM   872  C CD1 . ILE A 1 122 ? 34.678 16.219  19.584  1.00 23.55 ? 122 ILE A CD1 1 
ATOM   873  N N   . LYS A 1 123 ? 38.632 15.748  15.775  1.00 23.81 ? 123 LYS A N   1 
ATOM   874  C CA  . LYS A 1 123 ? 39.622 16.382  14.910  1.00 25.07 ? 123 LYS A CA  1 
ATOM   875  C C   . LYS A 1 123 ? 39.877 15.620  13.620  1.00 25.91 ? 123 LYS A C   1 
ATOM   876  O O   . LYS A 1 123 ? 40.013 16.223  12.561  1.00 23.41 ? 123 LYS A O   1 
ATOM   877  C CB  . LYS A 1 123 ? 40.948 16.562  15.656  1.00 28.04 ? 123 LYS A CB  1 
ATOM   878  C CG  . LYS A 1 123 ? 40.915 17.647  16.719  1.00 30.50 ? 123 LYS A CG  1 
ATOM   879  C CD  . LYS A 1 123 ? 42.203 17.650  17.536  1.00 35.39 ? 123 LYS A CD  1 
ATOM   880  C CE  . LYS A 1 123 ? 42.197 18.772  18.564  1.00 39.08 ? 123 LYS A CE  1 
ATOM   881  N NZ  . LYS A 1 123 ? 43.459 18.795  19.354  1.00 42.85 ? 123 LYS A NZ  1 
ATOM   882  N N   . ARG A 1 124 ? 39.934 14.294  13.699  1.00 25.69 ? 124 ARG A N   1 
ATOM   883  C CA  . ARG A 1 124 ? 40.190 13.518  12.496  1.00 27.52 ? 124 ARG A CA  1 
ATOM   884  C C   . ARG A 1 124 ? 39.105 13.757  11.451  1.00 26.34 ? 124 ARG A C   1 
ATOM   885  O O   . ARG A 1 124 ? 39.399 13.933  10.271  1.00 25.30 ? 124 ARG A O   1 
ATOM   886  C CB  . ARG A 1 124 ? 40.271 12.024  12.810  1.00 30.75 ? 124 ARG A CB  1 
ATOM   887  C CG  . ARG A 1 124 ? 40.890 11.234  11.668  1.00 36.14 ? 124 ARG A CG  1 
ATOM   888  C CD  . ARG A 1 124 ? 42.358 11.623  11.482  1.00 37.72 ? 124 ARG A CD  1 
ATOM   889  N NE  . ARG A 1 124 ? 42.904 11.188  10.199  1.00 41.86 ? 124 ARG A NE  1 
ATOM   890  C CZ  . ARG A 1 124 ? 42.628 11.767  9.034   1.00 45.10 ? 124 ARG A CZ  1 
ATOM   891  N NH1 . ARG A 1 124 ? 41.810 12.812  8.990   1.00 43.94 ? 124 ARG A NH1 1 
ATOM   892  N NH2 . ARG A 1 124 ? 43.174 11.308  7.914   1.00 42.97 ? 124 ARG A NH2 1 
ATOM   893  N N   . VAL A 1 125 ? 37.854 13.762  11.898  1.00 24.76 ? 125 VAL A N   1 
ATOM   894  C CA  . VAL A 1 125 ? 36.719 13.975  11.014  1.00 25.08 ? 125 VAL A CA  1 
ATOM   895  C C   . VAL A 1 125 ? 36.727 15.388  10.449  1.00 24.54 ? 125 VAL A C   1 
ATOM   896  O O   . VAL A 1 125 ? 36.455 15.593  9.266   1.00 27.08 ? 125 VAL A O   1 
ATOM   897  C CB  . VAL A 1 125 ? 35.387 13.739  11.760  1.00 24.77 ? 125 VAL A CB  1 
ATOM   898  C CG1 . VAL A 1 125 ? 34.216 14.223  10.913  1.00 25.48 ? 125 VAL A CG1 1 
ATOM   899  C CG2 . VAL A 1 125 ? 35.228 12.263  12.059  1.00 23.76 ? 125 VAL A CG2 1 
ATOM   900  N N   . LEU A 1 126 ? 37.033 16.361  11.299  1.00 24.16 ? 126 LEU A N   1 
ATOM   901  C CA  . LEU A 1 126 ? 37.070 17.747  10.858  1.00 25.23 ? 126 LEU A CA  1 
ATOM   902  C C   . LEU A 1 126 ? 38.185 17.938  9.829   1.00 27.65 ? 126 LEU A C   1 
ATOM   903  O O   . LEU A 1 126 ? 38.002 18.634  8.839   1.00 25.78 ? 126 LEU A O   1 
ATOM   904  C CB  . LEU A 1 126 ? 37.290 18.684  12.051  1.00 23.73 ? 126 LEU A CB  1 
ATOM   905  C CG  . LEU A 1 126 ? 36.184 18.739  13.116  1.00 24.62 ? 126 LEU A CG  1 
ATOM   906  C CD1 . LEU A 1 126 ? 36.572 19.748  14.210  1.00 23.71 ? 126 LEU A CD1 1 
ATOM   907  C CD2 . LEU A 1 126 ? 34.857 19.143  12.470  1.00 22.15 ? 126 LEU A CD2 1 
ATOM   908  N N   . LYS A 1 127 ? 39.337 17.310  10.054  1.00 28.79 ? 127 LYS A N   1 
ATOM   909  C CA  . LYS A 1 127 ? 40.445 17.448  9.116   1.00 30.24 ? 127 LYS A CA  1 
ATOM   910  C C   . LYS A 1 127 ? 40.082 16.856  7.763   1.00 29.41 ? 127 LYS A C   1 
ATOM   911  O O   . LYS A 1 127 ? 40.427 17.412  6.724   1.00 30.74 ? 127 LYS A O   1 
ATOM   912  C CB  . LYS A 1 127 ? 41.706 16.755  9.643   1.00 32.09 ? 127 LYS A CB  1 
ATOM   913  C CG  . LYS A 1 127 ? 42.219 17.286  10.966  1.00 37.89 ? 127 LYS A CG  1 
ATOM   914  C CD  . LYS A 1 127 ? 43.649 16.821  11.226  1.00 40.37 ? 127 LYS A CD  1 
ATOM   915  C CE  . LYS A 1 127 ? 43.854 16.405  12.680  1.00 44.39 ? 127 LYS A CE  1 
ATOM   916  N NZ  . LYS A 1 127 ? 43.292 15.049  12.974  1.00 38.82 ? 127 LYS A NZ  1 
ATOM   917  N N   . LEU A 1 128 ? 39.386 15.725  7.784   1.00 29.37 ? 128 LEU A N   1 
ATOM   918  C CA  . LEU A 1 128 ? 38.971 15.041  6.564   1.00 30.75 ? 128 LEU A CA  1 
ATOM   919  C C   . LEU A 1 128 ? 37.905 15.774  5.755   1.00 31.01 ? 128 LEU A C   1 
ATOM   920  O O   . LEU A 1 128 ? 37.984 15.835  4.526   1.00 27.79 ? 128 LEU A O   1 
ATOM   921  C CB  . LEU A 1 128 ? 38.430 13.648  6.895   1.00 33.47 ? 128 LEU A CB  1 
ATOM   922  C CG  . LEU A 1 128 ? 39.397 12.580  7.409   1.00 37.96 ? 128 LEU A CG  1 
ATOM   923  C CD1 . LEU A 1 128 ? 38.612 11.346  7.830   1.00 40.84 ? 128 LEU A CD1 1 
ATOM   924  C CD2 . LEU A 1 128 ? 40.411 12.230  6.321   1.00 41.03 ? 128 LEU A CD2 1 
ATOM   925  N N   . LEU A 1 129 ? 36.905 16.317  6.443   1.00 30.28 ? 129 LEU A N   1 
ATOM   926  C CA  . LEU A 1 129 ? 35.801 16.995  5.770   1.00 32.77 ? 129 LEU A CA  1 
ATOM   927  C C   . LEU A 1 129 ? 35.950 18.489  5.504   1.00 32.34 ? 129 LEU A C   1 
ATOM   928  O O   . LEU A 1 129 ? 35.347 19.008  4.568   1.00 34.61 ? 129 LEU A O   1 
ATOM   929  C CB  . LEU A 1 129 ? 34.492 16.746  6.534   1.00 33.25 ? 129 LEU A CB  1 
ATOM   930  C CG  . LEU A 1 129 ? 33.879 15.342  6.452   1.00 35.13 ? 129 LEU A CG  1 
ATOM   931  C CD1 . LEU A 1 129 ? 33.632 14.967  5.000   1.00 36.25 ? 129 LEU A CD1 1 
ATOM   932  C CD2 . LEU A 1 129 ? 34.810 14.328  7.091   1.00 40.13 ? 129 LEU A CD2 1 
ATOM   933  N N   . TYR A 1 130 ? 36.733 19.185  6.317   1.00 32.48 ? 130 TYR A N   1 
ATOM   934  C CA  . TYR A 1 130 ? 36.913 20.616  6.120   1.00 33.77 ? 130 TYR A CA  1 
ATOM   935  C C   . TYR A 1 130 ? 38.321 20.982  5.659   1.00 36.04 ? 130 TYR A C   1 
ATOM   936  O O   . TYR A 1 130 ? 38.423 21.746  4.676   1.00 39.22 ? 130 TYR A O   1 
ATOM   937  C CB  . TYR A 1 130 ? 36.573 21.383  7.401   1.00 29.67 ? 130 TYR A CB  1 
ATOM   938  C CG  . TYR A 1 130 ? 35.117 21.285  7.816   1.00 27.51 ? 130 TYR A CG  1 
ATOM   939  C CD1 . TYR A 1 130 ? 34.672 20.253  8.643   1.00 25.76 ? 130 TYR A CD1 1 
ATOM   940  C CD2 . TYR A 1 130 ? 34.190 22.240  7.400   1.00 24.79 ? 130 TYR A CD2 1 
ATOM   941  C CE1 . TYR A 1 130 ? 33.339 20.179  9.053   1.00 23.03 ? 130 TYR A CE1 1 
ATOM   942  C CE2 . TYR A 1 130 ? 32.858 22.178  7.804   1.00 25.54 ? 130 TYR A CE2 1 
ATOM   943  C CZ  . TYR A 1 130 ? 32.440 21.143  8.635   1.00 23.62 ? 130 TYR A CZ  1 
ATOM   944  O OH  . TYR A 1 130 ? 31.135 21.095  9.067   1.00 20.25 ? 130 TYR A OH  1 
ATOM   945  N N   . TRP B 1 8   ? 35.266 -4.981  -6.713  1.00 47.62 ? 8   TRP B N   1 
ATOM   946  C CA  . TRP B 1 8   ? 36.687 -5.431  -6.657  1.00 45.86 ? 8   TRP B CA  1 
ATOM   947  C C   . TRP B 1 8   ? 37.516 -4.453  -5.825  1.00 41.78 ? 8   TRP B C   1 
ATOM   948  O O   . TRP B 1 8   ? 38.392 -3.763  -6.350  1.00 42.15 ? 8   TRP B O   1 
ATOM   949  C CB  . TRP B 1 8   ? 37.275 -5.523  -8.071  1.00 51.06 ? 8   TRP B CB  1 
ATOM   950  C CG  . TRP B 1 8   ? 38.584 -6.284  -8.151  1.00 56.90 ? 8   TRP B CG  1 
ATOM   951  C CD1 . TRP B 1 8   ? 39.688 -6.121  -7.353  1.00 58.19 ? 8   TRP B CD1 1 
ATOM   952  C CD2 . TRP B 1 8   ? 38.918 -7.321  -9.085  1.00 59.52 ? 8   TRP B CD2 1 
ATOM   953  N NE1 . TRP B 1 8   ? 40.683 -6.992  -7.732  1.00 59.05 ? 8   TRP B NE1 1 
ATOM   954  C CE2 . TRP B 1 8   ? 40.238 -7.740  -8.792  1.00 60.31 ? 8   TRP B CE2 1 
ATOM   955  C CE3 . TRP B 1 8   ? 38.231 -7.937  -10.141 1.00 60.37 ? 8   TRP B CE3 1 
ATOM   956  C CZ2 . TRP B 1 8   ? 40.884 -8.751  -9.520  1.00 60.78 ? 8   TRP B CZ2 1 
ATOM   957  C CZ3 . TRP B 1 8   ? 38.875 -8.942  -10.865 1.00 61.01 ? 8   TRP B CZ3 1 
ATOM   958  C CH2 . TRP B 1 8   ? 40.189 -9.337  -10.548 1.00 60.52 ? 8   TRP B CH2 1 
ATOM   959  N N   . TRP B 1 9   ? 37.223 -4.381  -4.533  1.00 37.43 ? 9   TRP B N   1 
ATOM   960  C CA  . TRP B 1 9   ? 37.968 -3.499  -3.638  1.00 33.29 ? 9   TRP B CA  1 
ATOM   961  C C   . TRP B 1 9   ? 39.182 -4.257  -3.127  1.00 30.81 ? 9   TRP B C   1 
ATOM   962  O O   . TRP B 1 9   ? 39.056 -5.390  -2.651  1.00 30.44 ? 9   TRP B O   1 
ATOM   963  C CB  . TRP B 1 9   ? 37.113 -3.075  -2.441  1.00 32.03 ? 9   TRP B CB  1 
ATOM   964  C CG  . TRP B 1 9   ? 35.987 -2.155  -2.776  1.00 32.20 ? 9   TRP B CG  1 
ATOM   965  C CD1 . TRP B 1 9   ? 34.656 -2.461  -2.804  1.00 34.06 ? 9   TRP B CD1 1 
ATOM   966  C CD2 . TRP B 1 9   ? 36.086 -0.760  -3.082  1.00 31.14 ? 9   TRP B CD2 1 
ATOM   967  N NE1 . TRP B 1 9   ? 33.918 -1.339  -3.102  1.00 33.70 ? 9   TRP B NE1 1 
ATOM   968  C CE2 . TRP B 1 9   ? 34.771 -0.281  -3.278  1.00 33.69 ? 9   TRP B CE2 1 
ATOM   969  C CE3 . TRP B 1 9   ? 37.158 0.132   -3.209  1.00 29.38 ? 9   TRP B CE3 1 
ATOM   970  C CZ2 . TRP B 1 9   ? 34.498 1.055   -3.591  1.00 31.87 ? 9   TRP B CZ2 1 
ATOM   971  C CZ3 . TRP B 1 9   ? 36.888 1.459   -3.521  1.00 30.56 ? 9   TRP B CZ3 1 
ATOM   972  C CH2 . TRP B 1 9   ? 35.564 1.907   -3.709  1.00 31.99 ? 9   TRP B CH2 1 
ATOM   973  N N   . ARG B 1 10  ? 40.353 -3.633  -3.224  1.00 27.14 ? 10  ARG B N   1 
ATOM   974  C CA  . ARG B 1 10  ? 41.590 -4.253  -2.766  1.00 24.49 ? 10  ARG B CA  1 
ATOM   975  C C   . ARG B 1 10  ? 41.951 -3.704  -1.396  1.00 24.47 ? 10  ARG B C   1 
ATOM   976  O O   . ARG B 1 10  ? 42.124 -2.495  -1.236  1.00 21.53 ? 10  ARG B O   1 
ATOM   977  C CB  . ARG B 1 10  ? 42.742 -3.939  -3.719  1.00 25.30 ? 10  ARG B CB  1 
ATOM   978  C CG  . ARG B 1 10  ? 42.475 -4.247  -5.166  1.00 30.54 ? 10  ARG B CG  1 
ATOM   979  C CD  . ARG B 1 10  ? 43.646 -3.808  -6.034  1.00 31.72 ? 10  ARG B CD  1 
ATOM   980  N NE  . ARG B 1 10  ? 43.181 -3.546  -7.385  1.00 40.64 ? 10  ARG B NE  1 
ATOM   981  C CZ  . ARG B 1 10  ? 42.963 -2.334  -7.881  1.00 39.89 ? 10  ARG B CZ  1 
ATOM   982  N NH1 . ARG B 1 10  ? 43.183 -1.254  -7.144  1.00 38.51 ? 10  ARG B NH1 1 
ATOM   983  N NH2 . ARG B 1 10  ? 42.494 -2.209  -9.111  1.00 42.86 ? 10  ARG B NH2 1 
ATOM   984  N N   . ILE B 1 11  ? 42.080 -4.594  -0.418  1.00 22.55 ? 11  ILE B N   1 
ATOM   985  C CA  . ILE B 1 11  ? 42.430 -4.202  0.945   1.00 23.49 ? 11  ILE B CA  1 
ATOM   986  C C   . ILE B 1 11  ? 43.734 -4.909  1.318   1.00 24.52 ? 11  ILE B C   1 
ATOM   987  O O   . ILE B 1 11  ? 43.801 -6.137  1.278   1.00 26.12 ? 11  ILE B O   1 
ATOM   988  C CB  . ILE B 1 11  ? 41.332 -4.645  1.953   1.00 23.30 ? 11  ILE B CB  1 
ATOM   989  C CG1 . ILE B 1 11  ? 39.944 -4.223  1.453   1.00 27.27 ? 11  ILE B CG1 1 
ATOM   990  C CG2 . ILE B 1 11  ? 41.622 -4.060  3.338   1.00 24.70 ? 11  ILE B CG2 1 
ATOM   991  C CD1 . ILE B 1 11  ? 39.717 -2.717  1.386   1.00 27.43 ? 11  ILE B CD1 1 
ATOM   992  N N   . MET B 1 12  ? 44.770 -4.141  1.651   1.00 23.60 ? 12  MET B N   1 
ATOM   993  C CA  . MET B 1 12  ? 46.052 -4.721  2.050   1.00 23.91 ? 12  MET B CA  1 
ATOM   994  C C   . MET B 1 12  ? 46.146 -4.768  3.576   1.00 24.42 ? 12  MET B C   1 
ATOM   995  O O   . MET B 1 12  ? 45.887 -3.772  4.256   1.00 24.36 ? 12  MET B O   1 
ATOM   996  C CB  . MET B 1 12  ? 47.219 -3.901  1.494   1.00 22.04 ? 12  MET B CB  1 
ATOM   997  C CG  . MET B 1 12  ? 48.606 -4.442  1.898   1.00 25.78 ? 12  MET B CG  1 
ATOM   998  S SD  . MET B 1 12  ? 50.011 -3.577  1.104   1.00 22.09 ? 12  MET B SD  1 
ATOM   999  C CE  . MET B 1 12  ? 49.812 -4.125  -0.549  1.00 33.40 ? 12  MET B CE  1 
ATOM   1000 N N   . LEU B 1 13  ? 46.499 -5.931  4.112   1.00 24.89 ? 13  LEU B N   1 
ATOM   1001 C CA  . LEU B 1 13  ? 46.631 -6.094  5.558   1.00 25.30 ? 13  LEU B CA  1 
ATOM   1002 C C   . LEU B 1 13  ? 48.090 -6.354  5.893   1.00 25.48 ? 13  LEU B C   1 
ATOM   1003 O O   . LEU B 1 13  ? 48.695 -7.276  5.358   1.00 24.44 ? 13  LEU B O   1 
ATOM   1004 C CB  . LEU B 1 13  ? 45.772 -7.263  6.045   1.00 29.71 ? 13  LEU B CB  1 
ATOM   1005 C CG  . LEU B 1 13  ? 44.276 -7.016  6.247   1.00 34.23 ? 13  LEU B CG  1 
ATOM   1006 C CD1 . LEU B 1 13  ? 43.530 -8.348  6.227   1.00 35.71 ? 13  LEU B CD1 1 
ATOM   1007 C CD2 . LEU B 1 13  ? 44.049 -6.284  7.575   1.00 35.35 ? 13  LEU B CD2 1 
ATOM   1008 N N   . VAL B 1 14  ? 48.653 -5.535  6.775   1.00 24.45 ? 14  VAL B N   1 
ATOM   1009 C CA  . VAL B 1 14  ? 50.047 -5.690  7.166   1.00 26.00 ? 14  VAL B CA  1 
ATOM   1010 C C   . VAL B 1 14  ? 50.110 -6.000  8.658   1.00 26.86 ? 14  VAL B C   1 
ATOM   1011 O O   . VAL B 1 14  ? 49.635 -5.221  9.481   1.00 27.36 ? 14  VAL B O   1 
ATOM   1012 C CB  . VAL B 1 14  ? 50.855 -4.406  6.874   1.00 25.88 ? 14  VAL B CB  1 
ATOM   1013 C CG1 . VAL B 1 14  ? 52.342 -4.685  7.030   1.00 27.70 ? 14  VAL B CG1 1 
ATOM   1014 C CG2 . VAL B 1 14  ? 50.551 -3.909  5.457   1.00 28.87 ? 14  VAL B CG2 1 
ATOM   1015 N N   . ASP B 1 15  ? 50.691 -7.146  9.003   1.00 27.97 ? 15  ASP B N   1 
ATOM   1016 C CA  . ASP B 1 15  ? 50.787 -7.547  10.400  1.00 30.80 ? 15  ASP B CA  1 
ATOM   1017 C C   . ASP B 1 15  ? 51.724 -8.743  10.533  1.00 33.73 ? 15  ASP B C   1 
ATOM   1018 O O   . ASP B 1 15  ? 51.682 -9.662  9.711   1.00 34.38 ? 15  ASP B O   1 
ATOM   1019 C CB  . ASP B 1 15  ? 49.384 -7.892  10.918  1.00 31.88 ? 15  ASP B CB  1 
ATOM   1020 C CG  . ASP B 1 15  ? 49.343 -8.127  12.420  1.00 33.89 ? 15  ASP B CG  1 
ATOM   1021 O OD1 . ASP B 1 15  ? 48.289 -7.844  13.031  1.00 34.49 ? 15  ASP B OD1 1 
ATOM   1022 O OD2 . ASP B 1 15  ? 50.351 -8.601  12.987  1.00 33.83 ? 15  ASP B OD2 1 
ATOM   1023 N N   . THR B 1 16  ? 52.577 -8.727  11.554  1.00 36.56 ? 16  THR B N   1 
ATOM   1024 C CA  . THR B 1 16  ? 53.515 -9.830  11.766  1.00 40.63 ? 16  THR B CA  1 
ATOM   1025 C C   . THR B 1 16  ? 52.831 -11.009 12.450  1.00 42.74 ? 16  THR B C   1 
ATOM   1026 O O   . THR B 1 16  ? 53.461 -12.030 12.726  1.00 44.01 ? 16  THR B O   1 
ATOM   1027 C CB  . THR B 1 16  ? 54.728 -9.399  12.628  1.00 41.39 ? 16  THR B CB  1 
ATOM   1028 O OG1 . THR B 1 16  ? 54.289 -9.052  13.948  1.00 44.13 ? 16  THR B OG1 1 
ATOM   1029 C CG2 . THR B 1 16  ? 55.427 -8.208  12.003  1.00 41.70 ? 16  THR B CG2 1 
ATOM   1030 N N   . GLN B 1 17  ? 51.537 -10.865 12.713  1.00 43.58 ? 17  GLN B N   1 
ATOM   1031 C CA  . GLN B 1 17  ? 50.759 -11.912 13.366  1.00 44.39 ? 17  GLN B CA  1 
ATOM   1032 C C   . GLN B 1 17  ? 49.478 -12.153 12.571  1.00 43.21 ? 17  GLN B C   1 
ATOM   1033 O O   . GLN B 1 17  ? 48.378 -12.109 13.115  1.00 43.11 ? 17  GLN B O   1 
ATOM   1034 C CB  . GLN B 1 17  ? 50.421 -11.480 14.795  1.00 47.25 ? 17  GLN B CB  1 
ATOM   1035 C CG  . GLN B 1 17  ? 49.756 -12.545 15.649  1.00 52.82 ? 17  GLN B CG  1 
ATOM   1036 C CD  . GLN B 1 17  ? 49.340 -12.010 17.010  1.00 55.71 ? 17  GLN B CD  1 
ATOM   1037 O OE1 . GLN B 1 17  ? 50.144 -11.407 17.726  1.00 58.58 ? 17  GLN B OE1 1 
ATOM   1038 N NE2 . GLN B 1 17  ? 48.081 -12.230 17.376  1.00 57.03 ? 17  GLN B NE2 1 
ATOM   1039 N N   . LEU B 1 18  ? 49.633 -12.414 11.278  1.00 42.36 ? 18  LEU B N   1 
ATOM   1040 C CA  . LEU B 1 18  ? 48.496 -12.641 10.388  1.00 42.98 ? 18  LEU B CA  1 
ATOM   1041 C C   . LEU B 1 18  ? 47.601 -13.837 10.715  1.00 43.99 ? 18  LEU B C   1 
ATOM   1042 O O   . LEU B 1 18  ? 46.391 -13.790 10.484  1.00 43.14 ? 18  LEU B O   1 
ATOM   1043 C CB  . LEU B 1 18  ? 48.986 -12.756 8.943   1.00 42.04 ? 18  LEU B CB  1 
ATOM   1044 C CG  . LEU B 1 18  ? 49.447 -11.443 8.307   1.00 42.27 ? 18  LEU B CG  1 
ATOM   1045 C CD1 . LEU B 1 18  ? 50.131 -11.720 6.983   1.00 41.46 ? 18  LEU B CD1 1 
ATOM   1046 C CD2 . LEU B 1 18  ? 48.250 -10.524 8.121   1.00 40.11 ? 18  LEU B CD2 1 
ATOM   1047 N N   . PRO B 1 19  ? 48.178 -14.932 11.241  1.00 45.28 ? 19  PRO B N   1 
ATOM   1048 C CA  . PRO B 1 19  ? 47.340 -16.091 11.565  1.00 44.88 ? 19  PRO B CA  1 
ATOM   1049 C C   . PRO B 1 19  ? 46.201 -15.722 12.508  1.00 44.76 ? 19  PRO B C   1 
ATOM   1050 O O   . PRO B 1 19  ? 45.096 -16.244 12.394  1.00 44.24 ? 19  PRO B O   1 
ATOM   1051 C CB  . PRO B 1 19  ? 48.329 -17.060 12.204  1.00 46.01 ? 19  PRO B CB  1 
ATOM   1052 C CG  . PRO B 1 19  ? 49.600 -16.755 11.472  1.00 46.08 ? 19  PRO B CG  1 
ATOM   1053 C CD  . PRO B 1 19  ? 49.603 -15.242 11.455  1.00 44.83 ? 19  PRO B CD  1 
ATOM   1054 N N   . ALA B 1 20  ? 46.478 -14.805 13.428  1.00 45.41 ? 20  ALA B N   1 
ATOM   1055 C CA  . ALA B 1 20  ? 45.487 -14.366 14.405  1.00 46.21 ? 20  ALA B CA  1 
ATOM   1056 C C   . ALA B 1 20  ? 44.306 -13.636 13.772  1.00 46.37 ? 20  ALA B C   1 
ATOM   1057 O O   . ALA B 1 20  ? 43.263 -13.463 14.403  1.00 47.65 ? 20  ALA B O   1 
ATOM   1058 C CB  . ALA B 1 20  ? 46.153 -13.471 15.445  1.00 46.25 ? 20  ALA B CB  1 
ATOM   1059 N N   . LEU B 1 21  ? 44.468 -13.215 12.523  1.00 45.38 ? 21  LEU B N   1 
ATOM   1060 C CA  . LEU B 1 21  ? 43.415 -12.489 11.824  1.00 45.16 ? 21  LEU B CA  1 
ATOM   1061 C C   . LEU B 1 21  ? 42.769 -13.342 10.735  1.00 44.83 ? 21  LEU B C   1 
ATOM   1062 O O   . LEU B 1 21  ? 41.867 -12.888 10.028  1.00 44.10 ? 21  LEU B O   1 
ATOM   1063 C CB  . LEU B 1 21  ? 44.000 -11.212 11.214  1.00 45.24 ? 21  LEU B CB  1 
ATOM   1064 C CG  . LEU B 1 21  ? 44.706 -10.296 12.221  1.00 45.37 ? 21  LEU B CG  1 
ATOM   1065 C CD1 . LEU B 1 21  ? 45.481 -9.205  11.496  1.00 45.88 ? 21  LEU B CD1 1 
ATOM   1066 C CD2 . LEU B 1 21  ? 43.675 -9.698  13.164  1.00 44.52 ? 21  LEU B CD2 1 
ATOM   1067 N N   . ALA B 1 22  ? 43.238 -14.583 10.620  1.00 44.95 ? 22  ALA B N   1 
ATOM   1068 C CA  . ALA B 1 22  ? 42.748 -15.533 9.624   1.00 43.86 ? 22  ALA B CA  1 
ATOM   1069 C C   . ALA B 1 22  ? 41.227 -15.600 9.513   1.00 43.26 ? 22  ALA B C   1 
ATOM   1070 O O   . ALA B 1 22  ? 40.681 -15.664 8.410   1.00 41.91 ? 22  ALA B O   1 
ATOM   1071 C CB  . ALA B 1 22  ? 43.311 -16.922 9.923   1.00 44.66 ? 22  ALA B CB  1 
ATOM   1072 N N   . ALA B 1 23  ? 40.541 -15.590 10.652  1.00 43.24 ? 23  ALA B N   1 
ATOM   1073 C CA  . ALA B 1 23  ? 39.081 -15.655 10.651  1.00 43.78 ? 23  ALA B CA  1 
ATOM   1074 C C   . ALA B 1 23  ? 38.463 -14.387 10.059  1.00 44.61 ? 23  ALA B C   1 
ATOM   1075 O O   . ALA B 1 23  ? 37.459 -14.452 9.346   1.00 43.75 ? 23  ALA B O   1 
ATOM   1076 C CB  . ALA B 1 23  ? 38.567 -15.876 12.070  1.00 44.00 ? 23  ALA B CB  1 
ATOM   1077 N N   . SER B 1 24  ? 39.065 -13.237 10.357  1.00 44.50 ? 24  SER B N   1 
ATOM   1078 C CA  . SER B 1 24  ? 38.568 -11.965 9.844   1.00 43.79 ? 24  SER B CA  1 
ATOM   1079 C C   . SER B 1 24  ? 38.842 -11.868 8.348   1.00 42.51 ? 24  SER B C   1 
ATOM   1080 O O   . SER B 1 24  ? 38.001 -11.401 7.582   1.00 41.41 ? 24  SER B O   1 
ATOM   1081 C CB  . SER B 1 24  ? 39.237 -10.801 10.576  1.00 45.51 ? 24  SER B CB  1 
ATOM   1082 O OG  . SER B 1 24  ? 38.965 -10.858 11.967  1.00 47.63 ? 24  SER B OG  1 
ATOM   1083 N N   . ILE B 1 25  ? 40.021 -12.320 7.935   1.00 42.17 ? 25  ILE B N   1 
ATOM   1084 C CA  . ILE B 1 25  ? 40.387 -12.289 6.524   1.00 41.69 ? 25  ILE B CA  1 
ATOM   1085 C C   . ILE B 1 25  ? 39.380 -13.117 5.729   1.00 40.55 ? 25  ILE B C   1 
ATOM   1086 O O   . ILE B 1 25  ? 38.925 -12.701 4.664   1.00 40.46 ? 25  ILE B O   1 
ATOM   1087 C CB  . ILE B 1 25  ? 41.813 -12.847 6.303   1.00 42.19 ? 25  ILE B CB  1 
ATOM   1088 C CG1 . ILE B 1 25  ? 42.821 -12.024 7.109   1.00 43.07 ? 25  ILE B CG1 1 
ATOM   1089 C CG2 . ILE B 1 25  ? 42.174 -12.793 4.824   1.00 42.02 ? 25  ILE B CG2 1 
ATOM   1090 C CD1 . ILE B 1 25  ? 44.255 -12.522 7.005   1.00 44.09 ? 25  ILE B CD1 1 
ATOM   1091 N N   . SER B 1 26  ? 39.021 -14.284 6.257   1.00 40.16 ? 26  SER B N   1 
ATOM   1092 C CA  . SER B 1 26  ? 38.053 -15.146 5.589   1.00 40.29 ? 26  SER B CA  1 
ATOM   1093 C C   . SER B 1 26  ? 36.715 -14.427 5.479   1.00 38.46 ? 26  SER B C   1 
ATOM   1094 O O   . SER B 1 26  ? 36.058 -14.474 4.441   1.00 39.13 ? 26  SER B O   1 
ATOM   1095 C CB  . SER B 1 26  ? 37.861 -16.453 6.366   1.00 42.31 ? 26  SER B CB  1 
ATOM   1096 O OG  . SER B 1 26  ? 39.058 -17.205 6.415   1.00 46.58 ? 26  SER B OG  1 
ATOM   1097 N N   . ALA B 1 27  ? 36.314 -13.759 6.556   1.00 37.96 ? 27  ALA B N   1 
ATOM   1098 C CA  . ALA B 1 27  ? 35.046 -13.039 6.564   1.00 37.21 ? 27  ALA B CA  1 
ATOM   1099 C C   . ALA B 1 27  ? 35.025 -11.963 5.484   1.00 36.39 ? 27  ALA B C   1 
ATOM   1100 O O   . ALA B 1 27  ? 34.069 -11.860 4.710   1.00 35.97 ? 27  ALA B O   1 
ATOM   1101 C CB  . ALA B 1 27  ? 34.808 -12.418 7.928   1.00 37.26 ? 27  ALA B CB  1 
ATOM   1102 N N   . LEU B 1 28  ? 36.084 -11.162 5.431   1.00 36.30 ? 28  LEU B N   1 
ATOM   1103 C CA  . LEU B 1 28  ? 36.174 -10.097 4.440   1.00 35.68 ? 28  LEU B CA  1 
ATOM   1104 C C   . LEU B 1 28  ? 36.229 -10.666 3.028   1.00 35.80 ? 28  LEU B C   1 
ATOM   1105 O O   . LEU B 1 28  ? 35.624 -10.115 2.109   1.00 34.79 ? 28  LEU B O   1 
ATOM   1106 C CB  . LEU B 1 28  ? 37.406 -9.226  4.708   1.00 34.48 ? 28  LEU B CB  1 
ATOM   1107 C CG  . LEU B 1 28  ? 37.364 -8.446  6.026   1.00 33.89 ? 28  LEU B CG  1 
ATOM   1108 C CD1 . LEU B 1 28  ? 38.617 -7.592  6.170   1.00 32.98 ? 28  LEU B CD1 1 
ATOM   1109 C CD2 . LEU B 1 28  ? 36.117 -7.574  6.053   1.00 35.15 ? 28  LEU B CD2 1 
ATOM   1110 N N   . SER B 1 29  ? 36.956 -11.769 2.858   1.00 37.29 ? 29  SER B N   1 
ATOM   1111 C CA  . SER B 1 29  ? 37.067 -12.404 1.547   1.00 39.69 ? 29  SER B CA  1 
ATOM   1112 C C   . SER B 1 29  ? 35.692 -12.893 1.109   1.00 40.73 ? 29  SER B C   1 
ATOM   1113 O O   . SER B 1 29  ? 35.267 -12.667 -0.026  1.00 39.05 ? 29  SER B O   1 
ATOM   1114 C CB  . SER B 1 29  ? 38.033 -13.586 1.603   1.00 41.08 ? 29  SER B CB  1 
ATOM   1115 O OG  . SER B 1 29  ? 39.340 -13.162 1.942   1.00 45.28 ? 29  SER B OG  1 
ATOM   1116 N N   . GLN B 1 30  ? 35.001 -13.561 2.024   1.00 42.57 ? 30  GLN B N   1 
ATOM   1117 C CA  . GLN B 1 30  ? 33.670 -14.081 1.746   1.00 45.33 ? 30  GLN B CA  1 
ATOM   1118 C C   . GLN B 1 30  ? 32.754 -12.934 1.333   1.00 45.10 ? 30  GLN B C   1 
ATOM   1119 O O   . GLN B 1 30  ? 31.878 -13.095 0.486   1.00 45.13 ? 30  GLN B O   1 
ATOM   1120 C CB  . GLN B 1 30  ? 33.115 -14.780 2.989   1.00 47.64 ? 30  GLN B CB  1 
ATOM   1121 C CG  . GLN B 1 30  ? 31.797 -15.509 2.764   1.00 53.13 ? 30  GLN B CG  1 
ATOM   1122 C CD  . GLN B 1 30  ? 31.369 -16.332 3.971   1.00 55.03 ? 30  GLN B CD  1 
ATOM   1123 O OE1 . GLN B 1 30  ? 30.304 -16.955 3.968   1.00 56.74 ? 30  GLN B OE1 1 
ATOM   1124 N NE2 . GLN B 1 30  ? 32.200 -16.340 5.009   1.00 55.53 ? 30  GLN B NE2 1 
ATOM   1125 N N   . GLU B 1 31  ? 32.979 -11.766 1.925   1.00 44.42 ? 31  GLU B N   1 
ATOM   1126 C CA  . GLU B 1 31  ? 32.170 -10.594 1.629   1.00 43.46 ? 31  GLU B CA  1 
ATOM   1127 C C   . GLU B 1 31  ? 32.428 -10.020 0.235   1.00 42.20 ? 31  GLU B C   1 
ATOM   1128 O O   . GLU B 1 31  ? 31.610 -9.264  -0.290  1.00 42.11 ? 31  GLU B O   1 
ATOM   1129 C CB  . GLU B 1 31  ? 32.411 -9.521  2.691   1.00 45.71 ? 31  GLU B CB  1 
ATOM   1130 C CG  . GLU B 1 31  ? 31.415 -8.387  2.640   1.00 48.26 ? 31  GLU B CG  1 
ATOM   1131 C CD  . GLU B 1 31  ? 31.467 -7.518  3.875   1.00 49.81 ? 31  GLU B CD  1 
ATOM   1132 O OE1 . GLU B 1 31  ? 30.642 -6.586  3.979   1.00 51.64 ? 31  GLU B OE1 1 
ATOM   1133 O OE2 . GLU B 1 31  ? 32.329 -7.770  4.742   1.00 50.92 ? 31  GLU B OE2 1 
ATOM   1134 N N   . GLY B 1 32  ? 33.563 -10.375 -0.361  1.00 39.92 ? 32  GLY B N   1 
ATOM   1135 C CA  . GLY B 1 32  ? 33.868 -9.885  -1.694  1.00 37.97 ? 32  GLY B CA  1 
ATOM   1136 C C   . GLY B 1 32  ? 35.130 -9.050  -1.829  1.00 35.94 ? 32  GLY B C   1 
ATOM   1137 O O   . GLY B 1 32  ? 35.464 -8.622  -2.928  1.00 36.02 ? 32  GLY B O   1 
ATOM   1138 N N   . PHE B 1 33  ? 35.833 -8.813  -0.728  1.00 34.96 ? 33  PHE B N   1 
ATOM   1139 C CA  . PHE B 1 33  ? 37.060 -8.014  -0.770  1.00 34.72 ? 33  PHE B CA  1 
ATOM   1140 C C   . PHE B 1 33  ? 38.264 -8.799  -1.279  1.00 34.59 ? 33  PHE B C   1 
ATOM   1141 O O   . PHE B 1 33  ? 38.394 -9.989  -1.007  1.00 34.42 ? 33  PHE B O   1 
ATOM   1142 C CB  . PHE B 1 33  ? 37.390 -7.469  0.625   1.00 33.40 ? 33  PHE B CB  1 
ATOM   1143 C CG  . PHE B 1 33  ? 36.452 -6.396  1.098   1.00 32.83 ? 33  PHE B CG  1 
ATOM   1144 C CD1 . PHE B 1 33  ? 36.400 -5.164  0.451   1.00 33.49 ? 33  PHE B CD1 1 
ATOM   1145 C CD2 . PHE B 1 33  ? 35.622 -6.613  2.194   1.00 33.33 ? 33  PHE B CD2 1 
ATOM   1146 C CE1 . PHE B 1 33  ? 35.536 -4.163  0.888   1.00 31.67 ? 33  PHE B CE1 1 
ATOM   1147 C CE2 . PHE B 1 33  ? 34.749 -5.615  2.641   1.00 31.53 ? 33  PHE B CE2 1 
ATOM   1148 C CZ  . PHE B 1 33  ? 34.707 -4.390  1.986   1.00 31.60 ? 33  PHE B CZ  1 
ATOM   1149 N N   . ASP B 1 34  ? 39.139 -8.120  -2.018  1.00 34.68 ? 34  ASP B N   1 
ATOM   1150 C CA  . ASP B 1 34  ? 40.363 -8.722  -2.536  1.00 35.04 ? 34  ASP B CA  1 
ATOM   1151 C C   . ASP B 1 34  ? 41.390 -8.392  -1.456  1.00 35.25 ? 34  ASP B C   1 
ATOM   1152 O O   . ASP B 1 34  ? 41.885 -7.265  -1.389  1.00 33.77 ? 34  ASP B O   1 
ATOM   1153 C CB  . ASP B 1 34  ? 40.777 -8.055  -3.851  1.00 37.83 ? 34  ASP B CB  1 
ATOM   1154 C CG  . ASP B 1 34  ? 41.897 -8.799  -4.565  1.00 40.40 ? 34  ASP B CG  1 
ATOM   1155 O OD1 . ASP B 1 34  ? 42.757 -9.398  -3.889  1.00 39.53 ? 34  ASP B OD1 1 
ATOM   1156 O OD2 . ASP B 1 34  ? 41.921 -8.770  -5.813  1.00 44.67 ? 34  ASP B OD2 1 
ATOM   1157 N N   . ILE B 1 35  ? 41.703 -9.366  -0.611  1.00 34.33 ? 35  ILE B N   1 
ATOM   1158 C CA  . ILE B 1 35  ? 42.638 -9.145  0.481   1.00 33.47 ? 35  ILE B CA  1 
ATOM   1159 C C   . ILE B 1 35  ? 44.086 -9.461  0.134   1.00 33.25 ? 35  ILE B C   1 
ATOM   1160 O O   . ILE B 1 35  ? 44.409 -10.568 -0.293  1.00 32.37 ? 35  ILE B O   1 
ATOM   1161 C CB  . ILE B 1 35  ? 42.243 -9.977  1.710   1.00 35.49 ? 35  ILE B CB  1 
ATOM   1162 C CG1 . ILE B 1 35  ? 40.769 -9.735  2.050   1.00 35.27 ? 35  ILE B CG1 1 
ATOM   1163 C CG2 . ILE B 1 35  ? 43.132 -9.608  2.888   1.00 35.83 ? 35  ILE B CG2 1 
ATOM   1164 C CD1 . ILE B 1 35  ? 40.445 -8.288  2.411   1.00 37.28 ? 35  ILE B CD1 1 
ATOM   1165 N N   . ILE B 1 36  ? 44.948 -8.467  0.331   1.00 31.10 ? 36  ILE B N   1 
ATOM   1166 C CA  . ILE B 1 36  ? 46.379 -8.578  0.068   1.00 30.06 ? 36  ILE B CA  1 
ATOM   1167 C C   . ILE B 1 36  ? 47.085 -8.632  1.418   1.00 30.49 ? 36  ILE B C   1 
ATOM   1168 O O   . ILE B 1 36  ? 47.084 -7.648  2.157   1.00 29.64 ? 36  ILE B O   1 
ATOM   1169 C CB  . ILE B 1 36  ? 46.899 -7.336  -0.688  1.00 30.64 ? 36  ILE B CB  1 
ATOM   1170 C CG1 . ILE B 1 36  ? 46.154 -7.184  -2.015  1.00 30.35 ? 36  ILE B CG1 1 
ATOM   1171 C CG2 . ILE B 1 36  ? 48.410 -7.446  -0.891  1.00 29.48 ? 36  ILE B CG2 1 
ATOM   1172 C CD1 . ILE B 1 36  ? 46.402 -5.851  -2.706  1.00 31.44 ? 36  ILE B CD1 1 
ATOM   1173 N N   . GLN B 1 37  ? 47.693 -9.772  1.732   1.00 30.40 ? 37  GLN B N   1 
ATOM   1174 C CA  . GLN B 1 37  ? 48.381 -9.950  3.011   1.00 29.15 ? 37  GLN B CA  1 
ATOM   1175 C C   . GLN B 1 37  ? 49.884 -9.715  2.925   1.00 29.26 ? 37  GLN B C   1 
ATOM   1176 O O   . GLN B 1 37  ? 50.528 -10.088 1.944   1.00 29.75 ? 37  GLN B O   1 
ATOM   1177 C CB  . GLN B 1 37  ? 48.143 -11.364 3.547   1.00 31.11 ? 37  GLN B CB  1 
ATOM   1178 C CG  . GLN B 1 37  ? 46.689 -11.758 3.714   1.00 34.02 ? 37  GLN B CG  1 
ATOM   1179 C CD  . GLN B 1 37  ? 46.531 -13.133 4.341   1.00 35.74 ? 37  GLN B CD  1 
ATOM   1180 O OE1 . GLN B 1 37  ? 46.973 -13.369 5.464   1.00 37.65 ? 37  GLN B OE1 1 
ATOM   1181 N NE2 . GLN B 1 37  ? 45.899 -14.048 3.615   1.00 34.79 ? 37  GLN B NE2 1 
ATOM   1182 N N   . CYS B 1 38  ? 50.436 -9.090  3.960   1.00 28.73 ? 38  CYS B N   1 
ATOM   1183 C CA  . CYS B 1 38  ? 51.872 -8.829  4.029   1.00 29.94 ? 38  CYS B CA  1 
ATOM   1184 C C   . CYS B 1 38  ? 52.296 -9.073  5.466   1.00 32.43 ? 38  CYS B C   1 
ATOM   1185 O O   . CYS B 1 38  ? 51.873 -8.357  6.375   1.00 31.10 ? 38  CYS B O   1 
ATOM   1186 C CB  . CYS B 1 38  ? 52.199 -7.387  3.636   1.00 30.26 ? 38  CYS B CB  1 
ATOM   1187 S SG  . CYS B 1 38  ? 53.982 -7.055  3.586   1.00 35.87 ? 38  CYS B SG  1 
ATOM   1188 N N   . GLY B 1 39  ? 53.135 -10.084 5.664   1.00 34.76 ? 39  GLY B N   1 
ATOM   1189 C CA  . GLY B 1 39  ? 53.580 -10.426 7.000   1.00 37.75 ? 39  GLY B CA  1 
ATOM   1190 C C   . GLY B 1 39  ? 54.852 -9.762  7.479   1.00 40.06 ? 39  GLY B C   1 
ATOM   1191 O O   . GLY B 1 39  ? 55.302 -10.042 8.587   1.00 40.52 ? 39  GLY B O   1 
ATOM   1192 N N   . ASN B 1 40  ? 55.441 -8.890  6.666   1.00 42.23 ? 40  ASN B N   1 
ATOM   1193 C CA  . ASN B 1 40  ? 56.668 -8.213  7.076   1.00 45.08 ? 40  ASN B CA  1 
ATOM   1194 C C   . ASN B 1 40  ? 56.792 -6.795  6.513   1.00 44.98 ? 40  ASN B C   1 
ATOM   1195 O O   . ASN B 1 40  ? 56.629 -6.562  5.313   1.00 44.73 ? 40  ASN B O   1 
ATOM   1196 C CB  . ASN B 1 40  ? 57.887 -9.052  6.685   1.00 48.23 ? 40  ASN B CB  1 
ATOM   1197 C CG  . ASN B 1 40  ? 58.113 -9.091  5.197   1.00 51.46 ? 40  ASN B CG  1 
ATOM   1198 O OD1 . ASN B 1 40  ? 58.493 -8.088  4.593   1.00 53.29 ? 40  ASN B OD1 1 
ATOM   1199 N ND2 . ASN B 1 40  ? 57.877 -10.251 4.589   1.00 52.98 ? 40  ASN B ND2 1 
ATOM   1200 N N   . ALA B 1 41  ? 57.087 -5.857  7.407   1.00 44.38 ? 41  ALA B N   1 
ATOM   1201 C CA  . ALA B 1 41  ? 57.220 -4.443  7.075   1.00 43.72 ? 41  ALA B CA  1 
ATOM   1202 C C   . ALA B 1 41  ? 58.129 -4.113  5.890   1.00 42.68 ? 41  ALA B C   1 
ATOM   1203 O O   . ALA B 1 41  ? 57.829 -3.215  5.102   1.00 41.59 ? 41  ALA B O   1 
ATOM   1204 C CB  . ALA B 1 41  ? 57.690 -3.685  8.305   1.00 45.45 ? 41  ALA B CB  1 
ATOM   1205 N N   . ILE B 1 42  ? 59.240 -4.832  5.772   1.00 41.83 ? 42  ILE B N   1 
ATOM   1206 C CA  . ILE B 1 42  ? 60.201 -4.597  4.696   1.00 41.34 ? 42  ILE B CA  1 
ATOM   1207 C C   . ILE B 1 42  ? 59.600 -4.720  3.295   1.00 39.23 ? 42  ILE B C   1 
ATOM   1208 O O   . ILE B 1 42  ? 60.028 -4.035  2.366   1.00 38.54 ? 42  ILE B O   1 
ATOM   1209 C CB  . ILE B 1 42  ? 61.395 -5.577  4.802   1.00 43.59 ? 42  ILE B CB  1 
ATOM   1210 C CG1 . ILE B 1 42  ? 62.005 -5.507  6.208   1.00 45.63 ? 42  ILE B CG1 1 
ATOM   1211 C CG2 . ILE B 1 42  ? 62.444 -5.232  3.752   1.00 44.94 ? 42  ILE B CG2 1 
ATOM   1212 C CD1 . ILE B 1 42  ? 63.146 -6.492  6.456   1.00 46.01 ? 42  ILE B CD1 1 
ATOM   1213 N N   . GLU B 1 43  ? 58.603 -5.585  3.145   1.00 36.74 ? 43  GLU B N   1 
ATOM   1214 C CA  . GLU B 1 43  ? 57.972 -5.801  1.843   1.00 36.43 ? 43  GLU B CA  1 
ATOM   1215 C C   . GLU B 1 43  ? 56.692 -4.993  1.635   1.00 33.59 ? 43  GLU B C   1 
ATOM   1216 O O   . GLU B 1 43  ? 56.188 -4.902  0.518   1.00 31.84 ? 43  GLU B O   1 
ATOM   1217 C CB  . GLU B 1 43  ? 57.654 -7.291  1.659   1.00 37.85 ? 43  GLU B CB  1 
ATOM   1218 C CG  . GLU B 1 43  ? 58.876 -8.207  1.731   1.00 42.80 ? 43  GLU B CG  1 
ATOM   1219 C CD  . GLU B 1 43  ? 58.515 -9.676  1.618   1.00 46.51 ? 43  GLU B CD  1 
ATOM   1220 O OE1 . GLU B 1 43  ? 59.411 -10.527 1.818   1.00 49.31 ? 43  GLU B OE1 1 
ATOM   1221 O OE2 . GLU B 1 43  ? 57.338 -9.984  1.326   1.00 47.93 ? 43  GLU B OE2 1 
ATOM   1222 N N   . ALA B 1 44  ? 56.178 -4.410  2.712   1.00 32.00 ? 44  ALA B N   1 
ATOM   1223 C CA  . ALA B 1 44  ? 54.939 -3.636  2.668   1.00 30.58 ? 44  ALA B CA  1 
ATOM   1224 C C   . ALA B 1 44  ? 54.830 -2.588  1.560   1.00 27.50 ? 44  ALA B C   1 
ATOM   1225 O O   . ALA B 1 44  ? 53.890 -2.617  0.771   1.00 26.81 ? 44  ALA B O   1 
ATOM   1226 C CB  . ALA B 1 44  ? 54.696 -2.977  4.027   1.00 30.26 ? 44  ALA B CB  1 
ATOM   1227 N N   . VAL B 1 45  ? 55.776 -1.656  1.499   1.00 27.17 ? 45  VAL B N   1 
ATOM   1228 C CA  . VAL B 1 45  ? 55.710 -0.615  0.479   1.00 26.96 ? 45  VAL B CA  1 
ATOM   1229 C C   . VAL B 1 45  ? 55.833 -1.188  -0.927  1.00 26.66 ? 45  VAL B C   1 
ATOM   1230 O O   . VAL B 1 45  ? 55.047 -0.845  -1.812  1.00 25.29 ? 45  VAL B O   1 
ATOM   1231 C CB  . VAL B 1 45  ? 56.787 0.477   0.710   1.00 29.26 ? 45  VAL B CB  1 
ATOM   1232 C CG1 . VAL B 1 45  ? 56.659 1.566   -0.349  1.00 32.06 ? 45  VAL B CG1 1 
ATOM   1233 C CG2 . VAL B 1 45  ? 56.613 1.083   2.100   1.00 32.85 ? 45  VAL B CG2 1 
ATOM   1234 N N   . PRO B 1 46  ? 56.823 -2.071  -1.162  1.00 27.05 ? 46  PRO B N   1 
ATOM   1235 C CA  . PRO B 1 46  ? 56.952 -2.640  -2.508  1.00 25.83 ? 46  PRO B CA  1 
ATOM   1236 C C   . PRO B 1 46  ? 55.655 -3.310  -2.946  1.00 24.35 ? 46  PRO B C   1 
ATOM   1237 O O   . PRO B 1 46  ? 55.238 -3.193  -4.098  1.00 24.43 ? 46  PRO B O   1 
ATOM   1238 C CB  . PRO B 1 46  ? 58.089 -3.642  -2.350  1.00 25.73 ? 46  PRO B CB  1 
ATOM   1239 C CG  . PRO B 1 46  ? 58.964 -2.985  -1.321  1.00 28.99 ? 46  PRO B CG  1 
ATOM   1240 C CD  . PRO B 1 46  ? 57.958 -2.476  -0.306  1.00 28.22 ? 46  PRO B CD  1 
ATOM   1241 N N   . VAL B 1 47  ? 55.013 -4.013  -2.019  1.00 24.63 ? 47  VAL B N   1 
ATOM   1242 C CA  . VAL B 1 47  ? 53.765 -4.697  -2.326  1.00 24.58 ? 47  VAL B CA  1 
ATOM   1243 C C   . VAL B 1 47  ? 52.633 -3.698  -2.613  1.00 24.44 ? 47  VAL B C   1 
ATOM   1244 O O   . VAL B 1 47  ? 51.847 -3.885  -3.545  1.00 24.02 ? 47  VAL B O   1 
ATOM   1245 C CB  . VAL B 1 47  ? 53.356 -5.645  -1.166  1.00 25.93 ? 47  VAL B CB  1 
ATOM   1246 C CG1 . VAL B 1 47  ? 51.984 -6.240  -1.428  1.00 26.87 ? 47  VAL B CG1 1 
ATOM   1247 C CG2 . VAL B 1 47  ? 54.383 -6.771  -1.029  1.00 29.08 ? 47  VAL B CG2 1 
ATOM   1248 N N   . ALA B 1 48  ? 52.555 -2.634  -1.824  1.00 23.67 ? 48  ALA B N   1 
ATOM   1249 C CA  . ALA B 1 48  ? 51.510 -1.634  -2.021  1.00 24.55 ? 48  ALA B CA  1 
ATOM   1250 C C   . ALA B 1 48  ? 51.685 -0.945  -3.367  1.00 25.35 ? 48  ALA B C   1 
ATOM   1251 O O   . ALA B 1 48  ? 50.719 -0.700  -4.086  1.00 24.92 ? 48  ALA B O   1 
ATOM   1252 C CB  . ALA B 1 48  ? 51.544 -0.603  -0.891  1.00 25.61 ? 48  ALA B CB  1 
ATOM   1253 N N   . VAL B 1 49  ? 52.930 -0.643  -3.709  1.00 27.57 ? 49  VAL B N   1 
ATOM   1254 C CA  . VAL B 1 49  ? 53.224 0.028   -4.964  1.00 29.02 ? 49  VAL B CA  1 
ATOM   1255 C C   . VAL B 1 49  ? 52.878 -0.839  -6.174  1.00 29.82 ? 49  VAL B C   1 
ATOM   1256 O O   . VAL B 1 49  ? 52.507 -0.317  -7.221  1.00 29.90 ? 49  VAL B O   1 
ATOM   1257 C CB  . VAL B 1 49  ? 54.714 0.461   -5.018  1.00 31.63 ? 49  VAL B CB  1 
ATOM   1258 C CG1 . VAL B 1 49  ? 55.051 1.032   -6.382  1.00 32.64 ? 49  VAL B CG1 1 
ATOM   1259 C CG2 . VAL B 1 49  ? 54.987 1.501   -3.927  1.00 30.21 ? 49  VAL B CG2 1 
ATOM   1260 N N   . LYS B 1 50  ? 52.968 -2.159  -6.036  1.00 30.52 ? 50  LYS B N   1 
ATOM   1261 C CA  . LYS B 1 50  ? 52.647 -3.027  -7.167  1.00 30.88 ? 50  LYS B CA  1 
ATOM   1262 C C   . LYS B 1 50  ? 51.196 -3.504  -7.225  1.00 29.19 ? 50  LYS B C   1 
ATOM   1263 O O   . LYS B 1 50  ? 50.712 -3.867  -8.296  1.00 28.55 ? 50  LYS B O   1 
ATOM   1264 C CB  . LYS B 1 50  ? 53.572 -4.249  -7.203  1.00 34.46 ? 50  LYS B CB  1 
ATOM   1265 C CG  . LYS B 1 50  ? 53.284 -5.302  -6.148  1.00 40.55 ? 50  LYS B CG  1 
ATOM   1266 C CD  . LYS B 1 50  ? 53.894 -6.645  -6.546  1.00 44.45 ? 50  LYS B CD  1 
ATOM   1267 C CE  . LYS B 1 50  ? 55.418 -6.589  -6.638  1.00 47.57 ? 50  LYS B CE  1 
ATOM   1268 N NZ  . LYS B 1 50  ? 56.091 -6.598  -5.305  1.00 49.00 ? 50  LYS B NZ  1 
ATOM   1269 N N   . THR B 1 51  ? 50.497 -3.502  -6.092  1.00 26.22 ? 51  THR B N   1 
ATOM   1270 C CA  . THR B 1 51  ? 49.107 -3.960  -6.081  1.00 26.30 ? 51  THR B CA  1 
ATOM   1271 C C   . THR B 1 51  ? 48.085 -2.835  -5.945  1.00 24.24 ? 51  THR B C   1 
ATOM   1272 O O   . THR B 1 51  ? 46.889 -3.056  -6.121  1.00 24.43 ? 51  THR B O   1 
ATOM   1273 C CB  . THR B 1 51  ? 48.855 -4.981  -4.956  1.00 25.97 ? 51  THR B CB  1 
ATOM   1274 O OG1 . THR B 1 51  ? 49.066 -4.358  -3.682  1.00 26.24 ? 51  THR B OG1 1 
ATOM   1275 C CG2 . THR B 1 51  ? 49.803 -6.175  -5.099  1.00 28.10 ? 51  THR B CG2 1 
ATOM   1276 N N   . HIS B 1 52  ? 48.553 -1.641  -5.597  1.00 23.44 ? 52  HIS B N   1 
ATOM   1277 C CA  . HIS B 1 52  ? 47.678 -0.476  -5.482  1.00 20.86 ? 52  HIS B CA  1 
ATOM   1278 C C   . HIS B 1 52  ? 46.398 -0.704  -4.679  1.00 20.48 ? 52  HIS B C   1 
ATOM   1279 O O   . HIS B 1 52  ? 45.288 -0.533  -5.188  1.00 20.58 ? 52  HIS B O   1 
ATOM   1280 C CB  . HIS B 1 52  ? 47.328 0.013   -6.895  1.00 23.40 ? 52  HIS B CB  1 
ATOM   1281 C CG  . HIS B 1 52  ? 48.533 0.280   -7.750  1.00 24.50 ? 52  HIS B CG  1 
ATOM   1282 N ND1 . HIS B 1 52  ? 49.337 1.389   -7.582  1.00 25.33 ? 52  HIS B ND1 1 
ATOM   1283 C CD2 . HIS B 1 52  ? 49.095 -0.443  -8.748  1.00 24.96 ? 52  HIS B CD2 1 
ATOM   1284 C CE1 . HIS B 1 52  ? 50.342 1.337   -8.438  1.00 25.23 ? 52  HIS B CE1 1 
ATOM   1285 N NE2 . HIS B 1 52  ? 50.219 0.235   -9.158  1.00 25.02 ? 52  HIS B NE2 1 
ATOM   1286 N N   . PRO B 1 53  ? 46.533 -1.096  -3.408  1.00 20.37 ? 53  PRO B N   1 
ATOM   1287 C CA  . PRO B 1 53  ? 45.336 -1.323  -2.593  1.00 19.07 ? 53  PRO B CA  1 
ATOM   1288 C C   . PRO B 1 53  ? 44.525 -0.036  -2.425  1.00 19.87 ? 53  PRO B C   1 
ATOM   1289 O O   . PRO B 1 53  ? 45.089 1.056   -2.398  1.00 20.69 ? 53  PRO B O   1 
ATOM   1290 C CB  . PRO B 1 53  ? 45.914 -1.818  -1.265  1.00 19.80 ? 53  PRO B CB  1 
ATOM   1291 C CG  . PRO B 1 53  ? 47.257 -1.109  -1.196  1.00 20.88 ? 53  PRO B CG  1 
ATOM   1292 C CD  . PRO B 1 53  ? 47.766 -1.272  -2.613  1.00 19.29 ? 53  PRO B CD  1 
ATOM   1293 N N   . HIS B 1 54  ? 43.205 -0.159  -2.335  1.00 20.26 ? 54  HIS B N   1 
ATOM   1294 C CA  . HIS B 1 54  ? 42.345 1.011   -2.136  1.00 20.02 ? 54  HIS B CA  1 
ATOM   1295 C C   . HIS B 1 54  ? 42.430 1.477   -0.688  1.00 19.11 ? 54  HIS B C   1 
ATOM   1296 O O   . HIS B 1 54  ? 42.135 2.632   -0.373  1.00 17.70 ? 54  HIS B O   1 
ATOM   1297 C CB  . HIS B 1 54  ? 40.876 0.680   -2.433  1.00 20.19 ? 54  HIS B CB  1 
ATOM   1298 C CG  . HIS B 1 54  ? 40.605 0.361   -3.867  1.00 20.87 ? 54  HIS B CG  1 
ATOM   1299 N ND1 . HIS B 1 54  ? 40.539 -0.931  -4.340  1.00 23.32 ? 54  HIS B ND1 1 
ATOM   1300 C CD2 . HIS B 1 54  ? 40.407 1.166   -4.938  1.00 23.08 ? 54  HIS B CD2 1 
ATOM   1301 C CE1 . HIS B 1 54  ? 40.312 -0.908  -5.641  1.00 23.82 ? 54  HIS B CE1 1 
ATOM   1302 N NE2 . HIS B 1 54  ? 40.228 0.352   -6.029  1.00 22.77 ? 54  HIS B NE2 1 
ATOM   1303 N N   . LEU B 1 55  ? 42.798 0.557   0.195   1.00 19.01 ? 55  LEU B N   1 
ATOM   1304 C CA  . LEU B 1 55  ? 42.912 0.872   1.616   1.00 18.82 ? 55  LEU B CA  1 
ATOM   1305 C C   . LEU B 1 55  ? 43.891 -0.093  2.262   1.00 19.89 ? 55  LEU B C   1 
ATOM   1306 O O   . LEU B 1 55  ? 43.949 -1.276  1.897   1.00 19.70 ? 55  LEU B O   1 
ATOM   1307 C CB  . LEU B 1 55  ? 41.530 0.782   2.285   1.00 22.50 ? 55  LEU B CB  1 
ATOM   1308 C CG  . LEU B 1 55  ? 41.439 1.007   3.802   1.00 25.74 ? 55  LEU B CG  1 
ATOM   1309 C CD1 . LEU B 1 55  ? 40.044 1.488   4.178   1.00 30.43 ? 55  LEU B CD1 1 
ATOM   1310 C CD2 . LEU B 1 55  ? 41.769 -0.285  4.523   1.00 28.88 ? 55  LEU B CD2 1 
ATOM   1311 N N   . ILE B 1 56  ? 44.659 0.421   3.220   1.00 18.72 ? 56  ILE B N   1 
ATOM   1312 C CA  . ILE B 1 56  ? 45.659 -0.372  3.925   1.00 17.79 ? 56  ILE B CA  1 
ATOM   1313 C C   . ILE B 1 56  ? 45.343 -0.429  5.419   1.00 19.56 ? 56  ILE B C   1 
ATOM   1314 O O   . ILE B 1 56  ? 44.982 0.578   6.029   1.00 19.72 ? 56  ILE B O   1 
ATOM   1315 C CB  . ILE B 1 56  ? 47.068 0.249   3.730   1.00 20.21 ? 56  ILE B CB  1 
ATOM   1316 C CG1 . ILE B 1 56  ? 47.427 0.236   2.238   1.00 19.06 ? 56  ILE B CG1 1 
ATOM   1317 C CG2 . ILE B 1 56  ? 48.106 -0.492  4.569   1.00 19.45 ? 56  ILE B CG2 1 
ATOM   1318 C CD1 . ILE B 1 56  ? 48.620 1.101   1.874   1.00 20.94 ? 56  ILE B CD1 1 
ATOM   1319 N N   . ILE B 1 57  ? 45.465 -1.616  5.999   1.00 18.45 ? 57  ILE B N   1 
ATOM   1320 C CA  . ILE B 1 57  ? 45.230 -1.800  7.427   1.00 19.53 ? 57  ILE B CA  1 
ATOM   1321 C C   . ILE B 1 57  ? 46.558 -2.335  7.929   1.00 20.54 ? 57  ILE B C   1 
ATOM   1322 O O   . ILE B 1 57  ? 47.044 -3.342  7.421   1.00 22.07 ? 57  ILE B O   1 
ATOM   1323 C CB  . ILE B 1 57  ? 44.118 -2.831  7.681   1.00 20.97 ? 57  ILE B CB  1 
ATOM   1324 C CG1 . ILE B 1 57  ? 42.830 -2.379  6.986   1.00 23.02 ? 57  ILE B CG1 1 
ATOM   1325 C CG2 . ILE B 1 57  ? 43.883 -2.991  9.187   1.00 22.12 ? 57  ILE B CG2 1 
ATOM   1326 C CD1 . ILE B 1 57  ? 41.662 -3.342  7.137   1.00 23.36 ? 57  ILE B CD1 1 
ATOM   1327 N N   . THR B 1 58  ? 47.158 -1.661  8.909   1.00 21.40 ? 58  THR B N   1 
ATOM   1328 C CA  . THR B 1 58  ? 48.458 -2.088  9.408   1.00 21.55 ? 58  THR B CA  1 
ATOM   1329 C C   . THR B 1 58  ? 48.581 -2.059  10.928  1.00 24.03 ? 58  THR B C   1 
ATOM   1330 O O   . THR B 1 58  ? 47.974 -1.220  11.594  1.00 22.31 ? 58  THR B O   1 
ATOM   1331 C CB  . THR B 1 58  ? 49.590 -1.206  8.803   1.00 21.50 ? 58  THR B CB  1 
ATOM   1332 O OG1 . THR B 1 58  ? 50.870 -1.742  9.167   1.00 23.97 ? 58  THR B OG1 1 
ATOM   1333 C CG2 . THR B 1 58  ? 49.496 0.230   9.324   1.00 19.91 ? 58  THR B CG2 1 
ATOM   1334 N N   . GLU B 1 59  ? 49.363 -2.991  11.467  1.00 26.60 ? 59  GLU B N   1 
ATOM   1335 C CA  . GLU B 1 59  ? 49.606 -3.046  12.908  1.00 28.65 ? 59  GLU B CA  1 
ATOM   1336 C C   . GLU B 1 59  ? 50.460 -1.824  13.222  1.00 27.77 ? 59  GLU B C   1 
ATOM   1337 O O   . GLU B 1 59  ? 51.517 -1.626  12.630  1.00 28.84 ? 59  GLU B O   1 
ATOM   1338 C CB  . GLU B 1 59  ? 50.346 -4.338  13.264  1.00 30.13 ? 59  GLU B CB  1 
ATOM   1339 C CG  . GLU B 1 59  ? 51.118 -4.298  14.575  1.00 34.66 ? 59  GLU B CG  1 
ATOM   1340 C CD  . GLU B 1 59  ? 50.270 -3.899  15.759  1.00 34.31 ? 59  GLU B CD  1 
ATOM   1341 O OE1 . GLU B 1 59  ? 49.246 -4.566  16.030  1.00 36.96 ? 59  GLU B OE1 1 
ATOM   1342 O OE2 . GLU B 1 59  ? 50.635 -2.911  16.424  1.00 35.87 ? 59  GLU B OE2 1 
ATOM   1343 N N   . ALA B 1 60  ? 50.000 -0.995  14.148  1.00 30.16 ? 60  ALA B N   1 
ATOM   1344 C CA  . ALA B 1 60  ? 50.720 0.224   14.470  1.00 31.41 ? 60  ALA B CA  1 
ATOM   1345 C C   . ALA B 1 60  ? 52.082 0.031   15.119  1.00 33.09 ? 60  ALA B C   1 
ATOM   1346 O O   . ALA B 1 60  ? 52.955 0.890   14.988  1.00 32.22 ? 60  ALA B O   1 
ATOM   1347 C CB  . ALA B 1 60  ? 49.855 1.114   15.343  1.00 33.19 ? 60  ALA B CB  1 
ATOM   1348 N N   . ASN B 1 61  ? 52.278 -1.096  15.794  1.00 33.58 ? 61  ASN B N   1 
ATOM   1349 C CA  . ASN B 1 61  ? 53.536 -1.338  16.490  1.00 35.98 ? 61  ASN B CA  1 
ATOM   1350 C C   . ASN B 1 61  ? 54.512 -2.342  15.882  1.00 36.96 ? 61  ASN B C   1 
ATOM   1351 O O   . ASN B 1 61  ? 55.273 -2.996  16.600  1.00 37.23 ? 61  ASN B O   1 
ATOM   1352 C CB  . ASN B 1 61  ? 53.230 -1.706  17.941  1.00 35.70 ? 61  ASN B CB  1 
ATOM   1353 C CG  . ASN B 1 61  ? 52.494 -0.596  18.666  1.00 38.46 ? 61  ASN B CG  1 
ATOM   1354 O OD1 . ASN B 1 61  ? 51.412 -0.803  19.223  1.00 39.46 ? 61  ASN B OD1 1 
ATOM   1355 N ND2 . ASN B 1 61  ? 53.075 0.598   18.652  1.00 38.87 ? 61  ASN B ND2 1 
ATOM   1356 N N   . MET B 1 62  ? 54.503 -2.466  14.562  1.00 38.09 ? 62  MET B N   1 
ATOM   1357 C CA  . MET B 1 62  ? 55.436 -3.375  13.917  1.00 39.53 ? 62  MET B CA  1 
ATOM   1358 C C   . MET B 1 62  ? 56.794 -2.695  13.925  1.00 40.45 ? 62  MET B C   1 
ATOM   1359 O O   . MET B 1 62  ? 56.871 -1.470  14.007  1.00 39.99 ? 62  MET B O   1 
ATOM   1360 C CB  . MET B 1 62  ? 55.025 -3.642  12.476  1.00 39.00 ? 62  MET B CB  1 
ATOM   1361 C CG  . MET B 1 62  ? 53.761 -4.441  12.330  1.00 39.62 ? 62  MET B CG  1 
ATOM   1362 S SD  . MET B 1 62  ? 53.690 -5.084  10.676  1.00 34.08 ? 62  MET B SD  1 
ATOM   1363 C CE  . MET B 1 62  ? 53.911 -3.575  9.743   1.00 37.67 ? 62  MET B CE  1 
ATOM   1364 N N   . PRO B 1 63  ? 57.885 -3.474  13.856  1.00 41.75 ? 63  PRO B N   1 
ATOM   1365 C CA  . PRO B 1 63  ? 59.197 -2.827  13.858  1.00 43.36 ? 63  PRO B CA  1 
ATOM   1366 C C   . PRO B 1 63  ? 59.330 -1.850  12.691  1.00 43.74 ? 63  PRO B C   1 
ATOM   1367 O O   . PRO B 1 63  ? 58.826 -2.098  11.597  1.00 42.74 ? 63  PRO B O   1 
ATOM   1368 C CB  . PRO B 1 63  ? 60.168 -4.007  13.766  1.00 44.41 ? 63  PRO B CB  1 
ATOM   1369 C CG  . PRO B 1 63  ? 59.358 -5.079  13.100  1.00 44.00 ? 63  PRO B CG  1 
ATOM   1370 C CD  . PRO B 1 63  ? 58.019 -4.937  13.757  1.00 42.98 ? 63  PRO B CD  1 
ATOM   1371 N N   . LYS B 1 64  ? 60.001 -0.732  12.941  1.00 45.71 ? 64  LYS B N   1 
ATOM   1372 C CA  . LYS B 1 64  ? 60.201 0.296   11.927  1.00 47.08 ? 64  LYS B CA  1 
ATOM   1373 C C   . LYS B 1 64  ? 61.313 -0.100  10.965  1.00 47.17 ? 64  LYS B C   1 
ATOM   1374 O O   . LYS B 1 64  ? 62.226 -0.843  11.327  1.00 46.41 ? 64  LYS B O   1 
ATOM   1375 C CB  . LYS B 1 64  ? 60.595 1.621   12.584  1.00 48.29 ? 64  LYS B CB  1 
ATOM   1376 C CG  . LYS B 1 64  ? 59.735 2.051   13.756  1.00 51.30 ? 64  LYS B CG  1 
ATOM   1377 C CD  . LYS B 1 64  ? 58.361 2.508   13.321  1.00 52.87 ? 64  LYS B CD  1 
ATOM   1378 C CE  . LYS B 1 64  ? 57.645 3.180   14.478  1.00 54.59 ? 64  LYS B CE  1 
ATOM   1379 N NZ  . LYS B 1 64  ? 58.425 4.344   14.997  1.00 54.11 ? 64  LYS B NZ  1 
ATOM   1380 N N   . ILE B 1 65  ? 61.232 0.400   9.737   1.00 47.29 ? 65  ILE B N   1 
ATOM   1381 C CA  . ILE B 1 65  ? 62.265 0.136   8.748   1.00 47.68 ? 65  ILE B CA  1 
ATOM   1382 C C   . ILE B 1 65  ? 63.149 1.375   8.770   1.00 47.21 ? 65  ILE B C   1 
ATOM   1383 O O   . ILE B 1 65  ? 62.736 2.452   8.332   1.00 45.98 ? 65  ILE B O   1 
ATOM   1384 C CB  . ILE B 1 65  ? 61.699 -0.028  7.322   1.00 49.15 ? 65  ILE B CB  1 
ATOM   1385 C CG1 . ILE B 1 65  ? 60.642 -1.133  7.292   1.00 50.52 ? 65  ILE B CG1 1 
ATOM   1386 C CG2 . ILE B 1 65  ? 62.831 -0.352  6.354   1.00 48.94 ? 65  ILE B CG2 1 
ATOM   1387 C CD1 . ILE B 1 65  ? 59.299 -0.709  7.861   1.00 52.94 ? 65  ILE B CD1 1 
ATOM   1388 N N   . SER B 1 66  ? 64.354 1.219   9.306   1.00 46.68 ? 66  SER B N   1 
ATOM   1389 C CA  . SER B 1 66  ? 65.314 2.309   9.407   1.00 46.07 ? 66  SER B CA  1 
ATOM   1390 C C   . SER B 1 66  ? 64.732 3.552   10.077  1.00 45.02 ? 66  SER B C   1 
ATOM   1391 O O   . SER B 1 66  ? 64.867 4.665   9.572   1.00 45.05 ? 66  SER B O   1 
ATOM   1392 C CB  . SER B 1 66  ? 65.867 2.664   8.023   1.00 47.48 ? 66  SER B CB  1 
ATOM   1393 O OG  . SER B 1 66  ? 64.844 3.099   7.148   1.00 51.01 ? 66  SER B OG  1 
ATOM   1394 N N   . GLY B 1 67  ? 64.073 3.343   11.213  1.00 44.40 ? 67  GLY B N   1 
ATOM   1395 C CA  . GLY B 1 67  ? 63.507 4.445   11.971  1.00 43.72 ? 67  GLY B CA  1 
ATOM   1396 C C   . GLY B 1 67  ? 62.239 5.104   11.462  1.00 43.08 ? 67  GLY B C   1 
ATOM   1397 O O   . GLY B 1 67  ? 61.903 6.202   11.905  1.00 45.14 ? 67  GLY B O   1 
ATOM   1398 N N   . MET B 1 68  ? 61.525 4.453   10.551  1.00 40.11 ? 68  MET B N   1 
ATOM   1399 C CA  . MET B 1 68  ? 60.300 5.038   10.019  1.00 37.78 ? 68  MET B CA  1 
ATOM   1400 C C   . MET B 1 68  ? 59.107 4.088   10.076  1.00 35.85 ? 68  MET B C   1 
ATOM   1401 O O   . MET B 1 68  ? 59.237 2.905   9.772   1.00 34.51 ? 68  MET B O   1 
ATOM   1402 C CB  . MET B 1 68  ? 60.522 5.482   8.573   1.00 37.41 ? 68  MET B CB  1 
ATOM   1403 C CG  . MET B 1 68  ? 59.321 6.171   7.947   1.00 39.24 ? 68  MET B CG  1 
ATOM   1404 S SD  . MET B 1 68  ? 59.786 7.107   6.482   1.00 36.74 ? 68  MET B SD  1 
ATOM   1405 C CE  . MET B 1 68  ? 60.967 8.231   7.259   1.00 36.04 ? 68  MET B CE  1 
ATOM   1406 N N   . ASP B 1 69  ? 57.954 4.621   10.475  1.00 34.09 ? 69  ASP B N   1 
ATOM   1407 C CA  . ASP B 1 69  ? 56.713 3.851   10.551  1.00 33.48 ? 69  ASP B CA  1 
ATOM   1408 C C   . ASP B 1 69  ? 56.295 3.532   9.119   1.00 30.64 ? 69  ASP B C   1 
ATOM   1409 O O   . ASP B 1 69  ? 56.711 4.211   8.184   1.00 30.46 ? 69  ASP B O   1 
ATOM   1410 C CB  . ASP B 1 69  ? 55.586 4.685   11.178  1.00 38.84 ? 69  ASP B CB  1 
ATOM   1411 C CG  . ASP B 1 69  ? 55.973 5.313   12.500  1.00 44.56 ? 69  ASP B CG  1 
ATOM   1412 O OD1 . ASP B 1 69  ? 56.973 6.068   12.540  1.00 49.25 ? 69  ASP B OD1 1 
ATOM   1413 O OD2 . ASP B 1 69  ? 55.265 5.063   13.500  1.00 47.50 ? 69  ASP B OD2 1 
ATOM   1414 N N   . LEU B 1 70  ? 55.463 2.512   8.944   1.00 28.10 ? 70  LEU B N   1 
ATOM   1415 C CA  . LEU B 1 70  ? 54.989 2.179   7.607   1.00 26.09 ? 70  LEU B CA  1 
ATOM   1416 C C   . LEU B 1 70  ? 54.172 3.360   7.077   1.00 23.99 ? 70  LEU B C   1 
ATOM   1417 O O   . LEU B 1 70  ? 54.294 3.746   5.912   1.00 22.12 ? 70  LEU B O   1 
ATOM   1418 C CB  . LEU B 1 70  ? 54.108 0.924   7.645   1.00 26.04 ? 70  LEU B CB  1 
ATOM   1419 C CG  . LEU B 1 70  ? 53.368 0.595   6.341   1.00 28.76 ? 70  LEU B CG  1 
ATOM   1420 C CD1 . LEU B 1 70  ? 54.356 0.510   5.185   1.00 27.38 ? 70  LEU B CD1 1 
ATOM   1421 C CD2 . LEU B 1 70  ? 52.600 -0.719  6.500   1.00 28.98 ? 70  LEU B CD2 1 
ATOM   1422 N N   . PHE B 1 71  ? 53.349 3.940   7.945   1.00 23.13 ? 71  PHE B N   1 
ATOM   1423 C CA  . PHE B 1 71  ? 52.500 5.062   7.553   1.00 23.92 ? 71  PHE B CA  1 
ATOM   1424 C C   . PHE B 1 71  ? 53.294 6.161   6.868   1.00 24.88 ? 71  PHE B C   1 
ATOM   1425 O O   . PHE B 1 71  ? 52.911 6.651   5.807   1.00 22.58 ? 71  PHE B O   1 
ATOM   1426 C CB  . PHE B 1 71  ? 51.786 5.661   8.767   1.00 24.08 ? 71  PHE B CB  1 
ATOM   1427 C CG  . PHE B 1 71  ? 50.834 6.774   8.413   1.00 23.66 ? 71  PHE B CG  1 
ATOM   1428 C CD1 . PHE B 1 71  ? 49.542 6.489   7.970   1.00 25.55 ? 71  PHE B CD1 1 
ATOM   1429 C CD2 . PHE B 1 71  ? 51.244 8.104   8.473   1.00 22.86 ? 71  PHE B CD2 1 
ATOM   1430 C CE1 . PHE B 1 71  ? 48.668 7.517   7.588   1.00 24.89 ? 71  PHE B CE1 1 
ATOM   1431 C CE2 . PHE B 1 71  ? 50.381 9.142   8.094   1.00 23.37 ? 71  PHE B CE2 1 
ATOM   1432 C CZ  . PHE B 1 71  ? 49.092 8.848   7.650   1.00 24.05 ? 71  PHE B CZ  1 
ATOM   1433 N N   . ASN B 1 72  ? 54.402 6.555   7.487   1.00 24.23 ? 72  ASN B N   1 
ATOM   1434 C CA  . ASN B 1 72  ? 55.241 7.605   6.931   1.00 26.04 ? 72  ASN B CA  1 
ATOM   1435 C C   . ASN B 1 72  ? 55.942 7.151   5.652   1.00 25.55 ? 72  ASN B C   1 
ATOM   1436 O O   . ASN B 1 72  ? 56.090 7.933   4.708   1.00 26.28 ? 72  ASN B O   1 
ATOM   1437 C CB  . ASN B 1 72  ? 56.259 8.059   7.983   1.00 26.92 ? 72  ASN B CB  1 
ATOM   1438 C CG  . ASN B 1 72  ? 55.630 8.923   9.064   1.00 31.42 ? 72  ASN B CG  1 
ATOM   1439 O OD1 . ASN B 1 72  ? 56.044 8.891   10.225  1.00 36.75 ? 72  ASN B OD1 1 
ATOM   1440 N ND2 . ASN B 1 72  ? 54.631 9.709   8.684   1.00 33.28 ? 72  ASN B ND2 1 
ATOM   1441 N N   . SER B 1 73  ? 56.367 5.891   5.614   1.00 25.32 ? 73  SER B N   1 
ATOM   1442 C CA  . SER B 1 73  ? 57.036 5.371   4.429   1.00 26.58 ? 73  SER B CA  1 
ATOM   1443 C C   . SER B 1 73  ? 56.114 5.461   3.223   1.00 26.50 ? 73  SER B C   1 
ATOM   1444 O O   . SER B 1 73  ? 56.553 5.794   2.120   1.00 25.32 ? 73  SER B O   1 
ATOM   1445 C CB  . SER B 1 73  ? 57.448 3.913   4.635   1.00 29.27 ? 73  SER B CB  1 
ATOM   1446 O OG  . SER B 1 73  ? 58.468 3.811   5.609   1.00 31.58 ? 73  SER B OG  1 
ATOM   1447 N N   . LEU B 1 74  ? 54.837 5.156   3.435   1.00 24.53 ? 74  LEU B N   1 
ATOM   1448 C CA  . LEU B 1 74  ? 53.857 5.193   2.351   1.00 25.74 ? 74  LEU B CA  1 
ATOM   1449 C C   . LEU B 1 74  ? 53.680 6.609   1.810   1.00 26.37 ? 74  LEU B C   1 
ATOM   1450 O O   . LEU B 1 74  ? 53.341 6.801   0.643   1.00 25.72 ? 74  LEU B O   1 
ATOM   1451 C CB  . LEU B 1 74  ? 52.511 4.643   2.839   1.00 22.90 ? 74  LEU B CB  1 
ATOM   1452 C CG  . LEU B 1 74  ? 52.452 3.127   3.071   1.00 23.00 ? 74  LEU B CG  1 
ATOM   1453 C CD1 . LEU B 1 74  ? 51.241 2.783   3.940   1.00 23.00 ? 74  LEU B CD1 1 
ATOM   1454 C CD2 . LEU B 1 74  ? 52.379 2.404   1.726   1.00 21.82 ? 74  LEU B CD2 1 
ATOM   1455 N N   . LYS B 1 75  ? 53.920 7.599   2.664   1.00 28.31 ? 75  LYS B N   1 
ATOM   1456 C CA  . LYS B 1 75  ? 53.783 9.000   2.273   1.00 30.75 ? 75  LYS B CA  1 
ATOM   1457 C C   . LYS B 1 75  ? 54.917 9.479   1.371   1.00 31.54 ? 75  LYS B C   1 
ATOM   1458 O O   . LYS B 1 75  ? 54.801 10.518  0.721   1.00 32.60 ? 75  LYS B O   1 
ATOM   1459 C CB  . LYS B 1 75  ? 53.709 9.879   3.526   1.00 31.53 ? 75  LYS B CB  1 
ATOM   1460 C CG  . LYS B 1 75  ? 52.380 9.798   4.264   1.00 33.40 ? 75  LYS B CG  1 
ATOM   1461 C CD  . LYS B 1 75  ? 51.315 10.619  3.545   1.00 35.96 ? 75  LYS B CD  1 
ATOM   1462 C CE  . LYS B 1 75  ? 49.970 10.601  4.278   1.00 37.86 ? 75  LYS B CE  1 
ATOM   1463 N NZ  . LYS B 1 75  ? 49.182 9.351   4.049   1.00 32.34 ? 75  LYS B NZ  1 
ATOM   1464 N N   . LYS B 1 76  ? 56.007 8.722   1.322   1.00 31.25 ? 76  LYS B N   1 
ATOM   1465 C CA  . LYS B 1 76  ? 57.152 9.098   0.500   1.00 32.86 ? 76  LYS B CA  1 
ATOM   1466 C C   . LYS B 1 76  ? 57.034 8.686   -0.971  1.00 31.73 ? 76  LYS B C   1 
ATOM   1467 O O   . LYS B 1 76  ? 57.872 9.057   -1.792  1.00 31.89 ? 76  LYS B O   1 
ATOM   1468 C CB  . LYS B 1 76  ? 58.431 8.509   1.100   1.00 35.00 ? 76  LYS B CB  1 
ATOM   1469 C CG  . LYS B 1 76  ? 58.832 9.142   2.432   1.00 36.72 ? 76  LYS B CG  1 
ATOM   1470 C CD  . LYS B 1 76  ? 59.962 8.370   3.106   1.00 42.12 ? 76  LYS B CD  1 
ATOM   1471 C CE  . LYS B 1 76  ? 61.195 8.265   2.220   1.00 44.52 ? 76  LYS B CE  1 
ATOM   1472 N NZ  . LYS B 1 76  ? 62.265 7.438   2.854   1.00 45.79 ? 76  LYS B NZ  1 
ATOM   1473 N N   . ASN B 1 77  ? 56.001 7.919   -1.307  1.00 28.69 ? 77  ASN B N   1 
ATOM   1474 C CA  . ASN B 1 77  ? 55.812 7.485   -2.685  1.00 24.84 ? 77  ASN B CA  1 
ATOM   1475 C C   . ASN B 1 77  ? 54.475 8.016   -3.201  1.00 22.78 ? 77  ASN B C   1 
ATOM   1476 O O   . ASN B 1 77  ? 53.422 7.738   -2.626  1.00 22.33 ? 77  ASN B O   1 
ATOM   1477 C CB  . ASN B 1 77  ? 55.852 5.953   -2.762  1.00 26.18 ? 77  ASN B CB  1 
ATOM   1478 C CG  . ASN B 1 77  ? 55.935 5.441   -4.190  1.00 24.96 ? 77  ASN B CG  1 
ATOM   1479 O OD1 . ASN B 1 77  ? 55.084 5.756   -5.023  1.00 23.96 ? 77  ASN B OD1 1 
ATOM   1480 N ND2 . ASN B 1 77  ? 56.959 4.643   -4.478  1.00 25.46 ? 77  ASN B ND2 1 
ATOM   1481 N N   . PRO B 1 78  ? 54.507 8.819   -4.284  1.00 22.26 ? 78  PRO B N   1 
ATOM   1482 C CA  . PRO B 1 78  ? 53.305 9.404   -4.889  1.00 21.60 ? 78  PRO B CA  1 
ATOM   1483 C C   . PRO B 1 78  ? 52.193 8.399   -5.186  1.00 20.74 ? 78  PRO B C   1 
ATOM   1484 O O   . PRO B 1 78  ? 51.014 8.747   -5.176  1.00 23.28 ? 78  PRO B O   1 
ATOM   1485 C CB  . PRO B 1 78  ? 53.843 10.055  -6.164  1.00 21.57 ? 78  PRO B CB  1 
ATOM   1486 C CG  . PRO B 1 78  ? 55.202 10.523  -5.746  1.00 21.00 ? 78  PRO B CG  1 
ATOM   1487 C CD  . PRO B 1 78  ? 55.726 9.328   -4.947  1.00 22.15 ? 78  PRO B CD  1 
ATOM   1488 N N   . GLN B 1 79  ? 52.568 7.157   -5.464  1.00 20.31 ? 79  GLN B N   1 
ATOM   1489 C CA  . GLN B 1 79  ? 51.575 6.133   -5.770  1.00 22.57 ? 79  GLN B CA  1 
ATOM   1490 C C   . GLN B 1 79  ? 50.717 5.747   -4.569  1.00 21.45 ? 79  GLN B C   1 
ATOM   1491 O O   . GLN B 1 79  ? 49.527 5.473   -4.714  1.00 22.00 ? 79  GLN B O   1 
ATOM   1492 C CB  . GLN B 1 79  ? 52.257 4.870   -6.310  1.00 23.33 ? 79  GLN B CB  1 
ATOM   1493 C CG  . GLN B 1 79  ? 52.892 5.038   -7.679  1.00 26.94 ? 79  GLN B CG  1 
ATOM   1494 C CD  . GLN B 1 79  ? 51.882 5.461   -8.726  1.00 30.47 ? 79  GLN B CD  1 
ATOM   1495 O OE1 . GLN B 1 79  ? 50.815 4.852   -8.862  1.00 32.48 ? 79  GLN B OE1 1 
ATOM   1496 N NE2 . GLN B 1 79  ? 52.210 6.508   -9.477  1.00 30.24 ? 79  GLN B NE2 1 
ATOM   1497 N N   . THR B 1 80  ? 51.322 5.749   -3.387  1.00 19.28 ? 80  THR B N   1 
ATOM   1498 C CA  . THR B 1 80  ? 50.633 5.336   -2.164  1.00 20.07 ? 80  THR B CA  1 
ATOM   1499 C C   . THR B 1 80  ? 50.348 6.426   -1.128  1.00 20.57 ? 80  THR B C   1 
ATOM   1500 O O   . THR B 1 80  ? 49.633 6.178   -0.151  1.00 19.61 ? 80  THR B O   1 
ATOM   1501 C CB  . THR B 1 80  ? 51.453 4.256   -1.453  1.00 20.82 ? 80  THR B CB  1 
ATOM   1502 O OG1 . THR B 1 80  ? 52.752 4.786   -1.151  1.00 22.14 ? 80  THR B OG1 1 
ATOM   1503 C CG2 . THR B 1 80  ? 51.618 3.033   -2.345  1.00 22.35 ? 80  THR B CG2 1 
ATOM   1504 N N   . ALA B 1 81  ? 50.897 7.620   -1.337  1.00 19.15 ? 81  ALA B N   1 
ATOM   1505 C CA  . ALA B 1 81  ? 50.733 8.722   -0.389  1.00 21.01 ? 81  ALA B CA  1 
ATOM   1506 C C   . ALA B 1 81  ? 49.307 9.130   -0.008  1.00 22.05 ? 81  ALA B C   1 
ATOM   1507 O O   . ALA B 1 81  ? 49.102 9.698   1.062   1.00 24.37 ? 81  ALA B O   1 
ATOM   1508 C CB  . ALA B 1 81  ? 51.509 9.949   -0.884  1.00 20.32 ? 81  ALA B CB  1 
ATOM   1509 N N   . SER B 1 82  ? 48.321 8.848   -0.857  1.00 19.98 ? 82  SER B N   1 
ATOM   1510 C CA  . SER B 1 82  ? 46.945 9.225   -0.534  1.00 21.21 ? 82  SER B CA  1 
ATOM   1511 C C   . SER B 1 82  ? 46.053 8.041   -0.191  1.00 19.99 ? 82  SER B C   1 
ATOM   1512 O O   . SER B 1 82  ? 44.864 8.205   0.044   1.00 19.95 ? 82  SER B O   1 
ATOM   1513 C CB  . SER B 1 82  ? 46.309 10.010  -1.687  1.00 23.01 ? 82  SER B CB  1 
ATOM   1514 O OG  . SER B 1 82  ? 46.902 11.287  -1.803  1.00 26.53 ? 82  SER B OG  1 
ATOM   1515 N N   . ILE B 1 83  ? 46.622 6.845   -0.169  1.00 20.06 ? 83  ILE B N   1 
ATOM   1516 C CA  . ILE B 1 83  ? 45.833 5.677   0.171   1.00 19.68 ? 83  ILE B CA  1 
ATOM   1517 C C   . ILE B 1 83  ? 45.484 5.764   1.661   1.00 19.91 ? 83  ILE B C   1 
ATOM   1518 O O   . ILE B 1 83  ? 46.365 5.970   2.508   1.00 16.90 ? 83  ILE B O   1 
ATOM   1519 C CB  . ILE B 1 83  ? 46.623 4.379   -0.108  1.00 20.43 ? 83  ILE B CB  1 
ATOM   1520 C CG1 . ILE B 1 83  ? 46.958 4.284   -1.603  1.00 20.44 ? 83  ILE B CG1 1 
ATOM   1521 C CG2 . ILE B 1 83  ? 45.806 3.163   0.321   1.00 20.68 ? 83  ILE B CG2 1 
ATOM   1522 C CD1 . ILE B 1 83  ? 47.715 3.006   -1.985  1.00 20.81 ? 83  ILE B CD1 1 
ATOM   1523 N N   . PRO B 1 84  ? 44.191 5.650   2.001   1.00 19.30 ? 84  PRO B N   1 
ATOM   1524 C CA  . PRO B 1 84  ? 43.829 5.724   3.421   1.00 19.42 ? 84  PRO B CA  1 
ATOM   1525 C C   . PRO B 1 84  ? 44.414 4.548   4.197   1.00 19.40 ? 84  PRO B C   1 
ATOM   1526 O O   . PRO B 1 84  ? 44.508 3.428   3.677   1.00 17.63 ? 84  PRO B O   1 
ATOM   1527 C CB  . PRO B 1 84  ? 42.295 5.710   3.397   1.00 21.13 ? 84  PRO B CB  1 
ATOM   1528 C CG  . PRO B 1 84  ? 41.969 4.949   2.147   1.00 18.71 ? 84  PRO B CG  1 
ATOM   1529 C CD  . PRO B 1 84  ? 42.995 5.491   1.155   1.00 19.84 ? 84  PRO B CD  1 
ATOM   1530 N N   . VAL B 1 85  ? 44.793 4.798   5.445   1.00 17.95 ? 85  VAL B N   1 
ATOM   1531 C CA  . VAL B 1 85  ? 45.378 3.754   6.272   1.00 19.13 ? 85  VAL B CA  1 
ATOM   1532 C C   . VAL B 1 85  ? 44.684 3.634   7.623   1.00 18.90 ? 85  VAL B C   1 
ATOM   1533 O O   . VAL B 1 85  ? 44.491 4.635   8.319   1.00 18.93 ? 85  VAL B O   1 
ATOM   1534 C CB  . VAL B 1 85  ? 46.877 4.025   6.549   1.00 21.34 ? 85  VAL B CB  1 
ATOM   1535 C CG1 . VAL B 1 85  ? 47.488 2.826   7.272   1.00 19.47 ? 85  VAL B CG1 1 
ATOM   1536 C CG2 . VAL B 1 85  ? 47.615 4.329   5.243   1.00 20.13 ? 85  VAL B CG2 1 
ATOM   1537 N N   . ILE B 1 86  ? 44.292 2.411   7.971   1.00 17.31 ? 86  ILE B N   1 
ATOM   1538 C CA  . ILE B 1 86  ? 43.659 2.137   9.255   1.00 18.92 ? 86  ILE B CA  1 
ATOM   1539 C C   . ILE B 1 86  ? 44.713 1.475   10.138  1.00 20.15 ? 86  ILE B C   1 
ATOM   1540 O O   . ILE B 1 86  ? 45.443 0.591   9.683   1.00 20.56 ? 86  ILE B O   1 
ATOM   1541 C CB  . ILE B 1 86  ? 42.458 1.171   9.115   1.00 19.63 ? 86  ILE B CB  1 
ATOM   1542 C CG1 . ILE B 1 86  ? 41.299 1.877   8.412   1.00 20.13 ? 86  ILE B CG1 1 
ATOM   1543 C CG2 . ILE B 1 86  ? 42.012 0.674   10.498  1.00 19.01 ? 86  ILE B CG2 1 
ATOM   1544 C CD1 . ILE B 1 86  ? 40.053 1.001   8.273   1.00 18.72 ? 86  ILE B CD1 1 
ATOM   1545 N N   . ALA B 1 87  ? 44.796 1.904   11.392  1.00 20.57 ? 87  ALA B N   1 
ATOM   1546 C CA  . ALA B 1 87  ? 45.770 1.336   12.309  1.00 21.11 ? 87  ALA B CA  1 
ATOM   1547 C C   . ALA B 1 87  ? 45.124 0.302   13.215  1.00 23.06 ? 87  ALA B C   1 
ATOM   1548 O O   . ALA B 1 87  ? 43.982 0.467   13.656  1.00 22.88 ? 87  ALA B O   1 
ATOM   1549 C CB  . ALA B 1 87  ? 46.395 2.433   13.152  1.00 21.94 ? 87  ALA B CB  1 
ATOM   1550 N N   . LEU B 1 88  ? 45.870 -0.768  13.470  1.00 25.98 ? 88  LEU B N   1 
ATOM   1551 C CA  . LEU B 1 88  ? 45.454 -1.862  14.344  1.00 28.90 ? 88  LEU B CA  1 
ATOM   1552 C C   . LEU B 1 88  ? 46.445 -1.867  15.503  1.00 29.53 ? 88  LEU B C   1 
ATOM   1553 O O   . LEU B 1 88  ? 47.641 -1.661  15.293  1.00 29.66 ? 88  LEU B O   1 
ATOM   1554 C CB  . LEU B 1 88  ? 45.560 -3.201  13.611  1.00 30.87 ? 88  LEU B CB  1 
ATOM   1555 C CG  . LEU B 1 88  ? 44.296 -3.950  13.200  1.00 32.84 ? 88  LEU B CG  1 
ATOM   1556 C CD1 . LEU B 1 88  ? 43.291 -2.999  12.582  1.00 31.72 ? 88  LEU B CD1 1 
ATOM   1557 C CD2 . LEU B 1 88  ? 44.680 -5.066  12.238  1.00 32.79 ? 88  LEU B CD2 1 
ATOM   1558 N N   . SER B 1 89  ? 45.966 -2.102  16.719  1.00 30.12 ? 89  SER B N   1 
ATOM   1559 C CA  . SER B 1 89  ? 46.871 -2.123  17.864  1.00 32.21 ? 89  SER B CA  1 
ATOM   1560 C C   . SER B 1 89  ? 46.399 -3.005  19.013  1.00 33.71 ? 89  SER B C   1 
ATOM   1561 O O   . SER B 1 89  ? 45.213 -3.032  19.345  1.00 31.71 ? 89  SER B O   1 
ATOM   1562 C CB  . SER B 1 89  ? 47.096 -0.705  18.384  1.00 31.45 ? 89  SER B CB  1 
ATOM   1563 O OG  . SER B 1 89  ? 47.971 -0.719  19.498  1.00 32.00 ? 89  SER B OG  1 
ATOM   1564 N N   . GLY B 1 90  ? 47.349 -3.715  19.616  1.00 37.13 ? 90  GLY B N   1 
ATOM   1565 C CA  . GLY B 1 90  ? 47.043 -4.586  20.738  1.00 41.54 ? 90  GLY B CA  1 
ATOM   1566 C C   . GLY B 1 90  ? 47.187 -3.861  22.067  1.00 44.35 ? 90  GLY B C   1 
ATOM   1567 O O   . GLY B 1 90  ? 46.782 -4.374  23.111  1.00 45.08 ? 90  GLY B O   1 
ATOM   1568 N N   . ARG B 1 91  ? 47.775 -2.670  22.034  1.00 46.37 ? 91  ARG B N   1 
ATOM   1569 C CA  . ARG B 1 91  ? 47.948 -1.868  23.240  1.00 49.82 ? 91  ARG B CA  1 
ATOM   1570 C C   . ARG B 1 91  ? 46.661 -1.072  23.410  1.00 50.56 ? 91  ARG B C   1 
ATOM   1571 O O   . ARG B 1 91  ? 46.007 -1.131  24.450  1.00 52.12 ? 91  ARG B O   1 
ATOM   1572 C CB  . ARG B 1 91  ? 49.149 -0.932  23.081  1.00 51.70 ? 91  ARG B CB  1 
ATOM   1573 C CG  . ARG B 1 91  ? 50.450 -1.678  22.793  1.00 54.27 ? 91  ARG B CG  1 
ATOM   1574 C CD  . ARG B 1 91  ? 51.622 -0.732  22.575  1.00 56.64 ? 91  ARG B CD  1 
ATOM   1575 N NE  . ARG B 1 91  ? 52.857 -1.454  22.269  1.00 58.04 ? 91  ARG B NE  1 
ATOM   1576 C CZ  . ARG B 1 91  ? 54.008 -0.867  21.948  1.00 59.23 ? 91  ARG B CZ  1 
ATOM   1577 N NH1 . ARG B 1 91  ? 54.087 0.456   21.888  1.00 59.65 ? 91  ARG B NH1 1 
ATOM   1578 N NH2 . ARG B 1 91  ? 55.083 -1.602  21.687  1.00 59.39 ? 91  ARG B NH2 1 
ATOM   1579 N N   . ALA B 1 92  ? 46.305 -0.335  22.367  1.00 51.06 ? 92  ALA B N   1 
ATOM   1580 C CA  . ALA B 1 92  ? 45.083 0.455   22.334  1.00 51.65 ? 92  ALA B CA  1 
ATOM   1581 C C   . ALA B 1 92  ? 44.758 1.278   23.576  1.00 51.78 ? 92  ALA B C   1 
ATOM   1582 O O   . ALA B 1 92  ? 43.753 1.030   24.248  1.00 52.54 ? 92  ALA B O   1 
ATOM   1583 C CB  . ALA B 1 92  ? 43.907 -0.452  22.007  1.00 51.65 ? 92  ALA B CB  1 
ATOM   1584 N N   . THR B 1 93  ? 45.602 2.256   23.882  1.00 50.45 ? 93  THR B N   1 
ATOM   1585 C CA  . THR B 1 93  ? 45.351 3.132   25.019  1.00 48.68 ? 93  THR B CA  1 
ATOM   1586 C C   . THR B 1 93  ? 44.777 4.405   24.409  1.00 48.10 ? 93  THR B C   1 
ATOM   1587 O O   . THR B 1 93  ? 45.110 4.750   23.274  1.00 47.81 ? 93  THR B O   1 
ATOM   1588 C CB  . THR B 1 93  ? 46.639 3.495   25.761  1.00 48.25 ? 93  THR B CB  1 
ATOM   1589 O OG1 . THR B 1 93  ? 47.462 4.304   24.915  1.00 48.35 ? 93  THR B OG1 1 
ATOM   1590 C CG2 . THR B 1 93  ? 47.396 2.240   26.157  1.00 48.26 ? 93  THR B CG2 1 
ATOM   1591 N N   . ALA B 1 94  ? 43.918 5.095   25.149  1.00 45.57 ? 94  ALA B N   1 
ATOM   1592 C CA  . ALA B 1 94  ? 43.317 6.323   24.649  1.00 43.76 ? 94  ALA B CA  1 
ATOM   1593 C C   . ALA B 1 94  ? 44.385 7.228   24.044  1.00 42.82 ? 94  ALA B C   1 
ATOM   1594 O O   . ALA B 1 94  ? 44.187 7.816   22.982  1.00 42.51 ? 94  ALA B O   1 
ATOM   1595 C CB  . ALA B 1 94  ? 42.592 7.049   25.777  1.00 43.51 ? 94  ALA B CB  1 
ATOM   1596 N N   . LYS B 1 95  ? 45.528 7.321   24.716  1.00 41.57 ? 95  LYS B N   1 
ATOM   1597 C CA  . LYS B 1 95  ? 46.615 8.171   24.248  1.00 41.49 ? 95  LYS B CA  1 
ATOM   1598 C C   . LYS B 1 95  ? 47.189 7.694   22.918  1.00 40.86 ? 95  LYS B C   1 
ATOM   1599 O O   . LYS B 1 95  ? 47.447 8.500   22.023  1.00 39.95 ? 95  LYS B O   1 
ATOM   1600 C CB  . LYS B 1 95  ? 47.731 8.225   25.295  1.00 43.78 ? 95  LYS B CB  1 
ATOM   1601 C CG  . LYS B 1 95  ? 48.646 9.430   25.156  1.00 46.49 ? 95  LYS B CG  1 
ATOM   1602 C CD  . LYS B 1 95  ? 49.744 9.415   26.212  1.00 50.52 ? 95  LYS B CD  1 
ATOM   1603 C CE  . LYS B 1 95  ? 50.263 10.822  26.495  1.00 50.98 ? 95  LYS B CE  1 
ATOM   1604 N NZ  . LYS B 1 95  ? 50.729 11.522  25.266  1.00 54.52 ? 95  LYS B NZ  1 
ATOM   1605 N N   . GLU B 1 96  ? 47.392 6.384   22.791  1.00 40.77 ? 96  GLU B N   1 
ATOM   1606 C CA  . GLU B 1 96  ? 47.946 5.829   21.562  1.00 40.08 ? 96  GLU B CA  1 
ATOM   1607 C C   . GLU B 1 96  ? 47.001 6.083   20.398  1.00 37.71 ? 96  GLU B C   1 
ATOM   1608 O O   . GLU B 1 96  ? 47.428 6.489   19.319  1.00 37.52 ? 96  GLU B O   1 
ATOM   1609 C CB  . GLU B 1 96  ? 48.172 4.322   21.690  1.00 42.44 ? 96  GLU B CB  1 
ATOM   1610 C CG  . GLU B 1 96  ? 49.007 3.749   20.551  1.00 45.10 ? 96  GLU B CG  1 
ATOM   1611 C CD  . GLU B 1 96  ? 48.881 2.244   20.415  1.00 46.75 ? 96  GLU B CD  1 
ATOM   1612 O OE1 . GLU B 1 96  ? 49.735 1.640   19.731  1.00 46.72 ? 96  GLU B OE1 1 
ATOM   1613 O OE2 . GLU B 1 96  ? 47.924 1.667   20.980  1.00 48.15 ? 96  GLU B OE2 1 
ATOM   1614 N N   . GLU B 1 97  ? 45.716 5.834   20.626  1.00 35.72 ? 97  GLU B N   1 
ATOM   1615 C CA  . GLU B 1 97  ? 44.707 6.034   19.598  1.00 33.76 ? 97  GLU B CA  1 
ATOM   1616 C C   . GLU B 1 97  ? 44.779 7.461   19.077  1.00 32.10 ? 97  GLU B C   1 
ATOM   1617 O O   . GLU B 1 97  ? 44.831 7.688   17.867  1.00 30.15 ? 97  GLU B O   1 
ATOM   1618 C CB  . GLU B 1 97  ? 43.310 5.763   20.162  1.00 35.33 ? 97  GLU B CB  1 
ATOM   1619 C CG  . GLU B 1 97  ? 42.206 5.753   19.111  1.00 33.29 ? 97  GLU B CG  1 
ATOM   1620 C CD  . GLU B 1 97  ? 40.849 5.419   19.693  1.00 34.47 ? 97  GLU B CD  1 
ATOM   1621 O OE1 . GLU B 1 97  ? 40.806 4.731   20.736  1.00 35.78 ? 97  GLU B OE1 1 
ATOM   1622 O OE2 . GLU B 1 97  ? 39.823 5.828   19.105  1.00 30.86 ? 97  GLU B OE2 1 
ATOM   1623 N N   . ALA B 1 98  ? 44.791 8.420   19.997  1.00 28.92 ? 98  ALA B N   1 
ATOM   1624 C CA  . ALA B 1 98  ? 44.846 9.830   19.627  1.00 29.39 ? 98  ALA B CA  1 
ATOM   1625 C C   . ALA B 1 98  ? 46.100 10.155  18.825  1.00 28.56 ? 98  ALA B C   1 
ATOM   1626 O O   . ALA B 1 98  ? 46.043 10.910  17.852  1.00 28.92 ? 98  ALA B O   1 
ATOM   1627 C CB  . ALA B 1 98  ? 44.777 10.711  20.885  1.00 28.21 ? 98  ALA B CB  1 
ATOM   1628 N N   . GLN B 1 99  ? 47.233 9.587   19.228  1.00 28.21 ? 99  GLN B N   1 
ATOM   1629 C CA  . GLN B 1 99  ? 48.485 9.839   18.522  1.00 29.33 ? 99  GLN B CA  1 
ATOM   1630 C C   . GLN B 1 99  ? 48.402 9.359   17.076  1.00 25.58 ? 99  GLN B C   1 
ATOM   1631 O O   . GLN B 1 99  ? 48.802 10.070  16.149  1.00 24.44 ? 99  GLN B O   1 
ATOM   1632 C CB  . GLN B 1 99  ? 49.653 9.124   19.206  1.00 33.22 ? 99  GLN B CB  1 
ATOM   1633 C CG  . GLN B 1 99  ? 50.988 9.389   18.529  1.00 41.94 ? 99  GLN B CG  1 
ATOM   1634 C CD  . GLN B 1 99  ? 51.946 8.209   18.620  1.00 47.11 ? 99  GLN B CD  1 
ATOM   1635 O OE1 . GLN B 1 99  ? 51.686 7.138   18.064  1.00 49.80 ? 99  GLN B OE1 1 
ATOM   1636 N NE2 . GLN B 1 99  ? 53.058 8.402   19.321  1.00 48.79 ? 99  GLN B NE2 1 
ATOM   1637 N N   . LEU B 1 100 ? 47.893 8.145   16.891  1.00 25.43 ? 100 LEU B N   1 
ATOM   1638 C CA  . LEU B 1 100 ? 47.770 7.576   15.552  1.00 25.42 ? 100 LEU B CA  1 
ATOM   1639 C C   . LEU B 1 100 ? 46.794 8.372   14.693  1.00 23.50 ? 100 LEU B C   1 
ATOM   1640 O O   . LEU B 1 100 ? 47.075 8.653   13.530  1.00 23.96 ? 100 LEU B O   1 
ATOM   1641 C CB  . LEU B 1 100 ? 47.333 6.112   15.637  1.00 25.58 ? 100 LEU B CB  1 
ATOM   1642 C CG  . LEU B 1 100 ? 48.370 5.209   16.316  1.00 28.11 ? 100 LEU B CG  1 
ATOM   1643 C CD1 . LEU B 1 100 ? 47.757 3.856   16.642  1.00 28.20 ? 100 LEU B CD1 1 
ATOM   1644 C CD2 . LEU B 1 100 ? 49.580 5.055   15.410  1.00 27.97 ? 100 LEU B CD2 1 
ATOM   1645 N N   . LEU B 1 101 ? 45.648 8.736   15.255  1.00 23.16 ? 101 LEU B N   1 
ATOM   1646 C CA  . LEU B 1 101 ? 44.692 9.528   14.493  1.00 23.23 ? 101 LEU B CA  1 
ATOM   1647 C C   . LEU B 1 101 ? 45.319 10.893  14.164  1.00 23.39 ? 101 LEU B C   1 
ATOM   1648 O O   . LEU B 1 101 ? 45.232 11.367  13.026  1.00 22.19 ? 101 LEU B O   1 
ATOM   1649 C CB  . LEU B 1 101 ? 43.389 9.706   15.280  1.00 22.70 ? 101 LEU B CB  1 
ATOM   1650 C CG  . LEU B 1 101 ? 42.543 8.440   15.466  1.00 24.22 ? 101 LEU B CG  1 
ATOM   1651 C CD1 . LEU B 1 101 ? 41.272 8.773   16.254  1.00 23.16 ? 101 LEU B CD1 1 
ATOM   1652 C CD2 . LEU B 1 101 ? 42.177 7.855   14.091  1.00 23.94 ? 101 LEU B CD2 1 
ATOM   1653 N N   . ASP B 1 102 ? 45.973 11.514  15.147  1.00 24.94 ? 102 ASP B N   1 
ATOM   1654 C CA  . ASP B 1 102 ? 46.599 12.819  14.910  1.00 27.24 ? 102 ASP B CA  1 
ATOM   1655 C C   . ASP B 1 102 ? 47.623 12.716  13.782  1.00 27.14 ? 102 ASP B C   1 
ATOM   1656 O O   . ASP B 1 102 ? 47.759 13.639  12.976  1.00 27.41 ? 102 ASP B O   1 
ATOM   1657 C CB  . ASP B 1 102 ? 47.287 13.347  16.175  1.00 29.68 ? 102 ASP B CB  1 
ATOM   1658 C CG  . ASP B 1 102 ? 46.300 13.792  17.241  1.00 34.00 ? 102 ASP B CG  1 
ATOM   1659 O OD1 . ASP B 1 102 ? 45.115 14.020  16.910  1.00 34.19 ? 102 ASP B OD1 1 
ATOM   1660 O OD2 . ASP B 1 102 ? 46.714 13.925  18.413  1.00 35.33 ? 102 ASP B OD2 1 
ATOM   1661 N N   . MET B 1 103 ? 48.331 11.585  13.739  1.00 27.70 ? 103 MET B N   1 
ATOM   1662 C CA  . MET B 1 103 ? 49.339 11.309  12.717  1.00 28.74 ? 103 MET B CA  1 
ATOM   1663 C C   . MET B 1 103 ? 48.783 11.321  11.297  1.00 28.17 ? 103 MET B C   1 
ATOM   1664 O O   . MET B 1 103 ? 49.495 11.648  10.344  1.00 28.70 ? 103 MET B O   1 
ATOM   1665 C CB  . MET B 1 103 ? 49.963 9.931   12.935  1.00 31.30 ? 103 MET B CB  1 
ATOM   1666 C CG  . MET B 1 103 ? 51.151 9.867   13.858  1.00 35.06 ? 103 MET B CG  1 
ATOM   1667 S SD  . MET B 1 103 ? 51.871 8.207   13.751  1.00 34.32 ? 103 MET B SD  1 
ATOM   1668 C CE  . MET B 1 103 ? 52.476 8.208   12.112  1.00 30.47 ? 103 MET B CE  1 
ATOM   1669 N N   . GLY B 1 104 ? 47.523 10.925  11.148  1.00 25.45 ? 104 GLY B N   1 
ATOM   1670 C CA  . GLY B 1 104 ? 46.940 10.884  9.821   1.00 23.42 ? 104 GLY B CA  1 
ATOM   1671 C C   . GLY B 1 104 ? 46.221 9.575   9.519   1.00 23.48 ? 104 GLY B C   1 
ATOM   1672 O O   . GLY B 1 104 ? 45.579 9.454   8.481   1.00 22.25 ? 104 GLY B O   1 
ATOM   1673 N N   . PHE B 1 105 ? 46.340 8.579   10.394  1.00 20.92 ? 105 PHE B N   1 
ATOM   1674 C CA  . PHE B 1 105 ? 45.618 7.320   10.163  1.00 20.60 ? 105 PHE B CA  1 
ATOM   1675 C C   . PHE B 1 105 ? 44.148 7.716   10.074  1.00 20.77 ? 105 PHE B C   1 
ATOM   1676 O O   . PHE B 1 105 ? 43.679 8.565   10.844  1.00 21.00 ? 105 PHE B O   1 
ATOM   1677 C CB  . PHE B 1 105 ? 45.834 6.351   11.330  1.00 21.25 ? 105 PHE B CB  1 
ATOM   1678 C CG  . PHE B 1 105 ? 47.118 5.572   11.240  1.00 20.66 ? 105 PHE B CG  1 
ATOM   1679 C CD1 . PHE B 1 105 ? 47.164 4.357   10.561  1.00 20.96 ? 105 PHE B CD1 1 
ATOM   1680 C CD2 . PHE B 1 105 ? 48.282 6.056   11.819  1.00 21.70 ? 105 PHE B CD2 1 
ATOM   1681 C CE1 . PHE B 1 105 ? 48.360 3.634   10.465  1.00 21.24 ? 105 PHE B CE1 1 
ATOM   1682 C CE2 . PHE B 1 105 ? 49.478 5.343   11.728  1.00 21.08 ? 105 PHE B CE2 1 
ATOM   1683 C CZ  . PHE B 1 105 ? 49.514 4.130   11.050  1.00 21.53 ? 105 PHE B CZ  1 
ATOM   1684 N N   . ILE B 1 106 ? 43.418 7.113   9.144   1.00 19.98 ? 106 ILE B N   1 
ATOM   1685 C CA  . ILE B 1 106 ? 42.011 7.466   8.966   1.00 20.80 ? 106 ILE B CA  1 
ATOM   1686 C C   . ILE B 1 106 ? 41.083 6.813   9.990   1.00 21.00 ? 106 ILE B C   1 
ATOM   1687 O O   . ILE B 1 106 ? 39.946 7.250   10.186  1.00 20.33 ? 106 ILE B O   1 
ATOM   1688 C CB  . ILE B 1 106 ? 41.548 7.133   7.540   1.00 20.97 ? 106 ILE B CB  1 
ATOM   1689 C CG1 . ILE B 1 106 ? 40.196 7.792   7.279   1.00 23.89 ? 106 ILE B CG1 1 
ATOM   1690 C CG2 . ILE B 1 106 ? 41.477 5.629   7.342   1.00 19.23 ? 106 ILE B CG2 1 
ATOM   1691 C CD1 . ILE B 1 106 ? 39.796 7.747   5.833   1.00 29.89 ? 106 ILE B CD1 1 
ATOM   1692 N N   . ASP B 1 107 ? 41.562 5.756   10.630  1.00 20.28 ? 107 ASP B N   1 
ATOM   1693 C CA  . ASP B 1 107 ? 40.792 5.095   11.675  1.00 21.39 ? 107 ASP B CA  1 
ATOM   1694 C C   . ASP B 1 107 ? 41.734 4.253   12.520  1.00 21.33 ? 107 ASP B C   1 
ATOM   1695 O O   . ASP B 1 107 ? 42.885 4.024   12.149  1.00 20.18 ? 107 ASP B O   1 
ATOM   1696 C CB  . ASP B 1 107 ? 39.687 4.208   11.094  1.00 20.77 ? 107 ASP B CB  1 
ATOM   1697 C CG  . ASP B 1 107 ? 38.458 4.145   12.000  1.00 23.90 ? 107 ASP B CG  1 
ATOM   1698 O OD1 . ASP B 1 107 ? 38.615 4.269   13.236  1.00 22.06 ? 107 ASP B OD1 1 
ATOM   1699 O OD2 . ASP B 1 107 ? 37.334 3.963   11.477  1.00 25.48 ? 107 ASP B OD2 1 
ATOM   1700 N N   . PHE B 1 108 ? 41.230 3.807   13.661  1.00 22.11 ? 108 PHE B N   1 
ATOM   1701 C CA  . PHE B 1 108 ? 41.993 2.995   14.594  1.00 23.65 ? 108 PHE B CA  1 
ATOM   1702 C C   . PHE B 1 108 ? 41.067 1.915   15.148  1.00 23.26 ? 108 PHE B C   1 
ATOM   1703 O O   . PHE B 1 108 ? 39.928 2.197   15.517  1.00 22.75 ? 108 PHE B O   1 
ATOM   1704 C CB  . PHE B 1 108 ? 42.504 3.861   15.747  1.00 25.10 ? 108 PHE B CB  1 
ATOM   1705 C CG  . PHE B 1 108 ? 43.055 3.069   16.898  1.00 28.11 ? 108 PHE B CG  1 
ATOM   1706 C CD1 . PHE B 1 108 ? 44.385 2.668   16.910  1.00 29.83 ? 108 PHE B CD1 1 
ATOM   1707 C CD2 . PHE B 1 108 ? 42.228 2.681   17.950  1.00 30.09 ? 108 PHE B CD2 1 
ATOM   1708 C CE1 . PHE B 1 108 ? 44.887 1.889   17.952  1.00 31.79 ? 108 PHE B CE1 1 
ATOM   1709 C CE2 . PHE B 1 108 ? 42.720 1.901   18.994  1.00 30.85 ? 108 PHE B CE2 1 
ATOM   1710 C CZ  . PHE B 1 108 ? 44.051 1.504   18.995  1.00 31.35 ? 108 PHE B CZ  1 
ATOM   1711 N N   . ILE B 1 109 ? 41.565 0.685   15.197  1.00 24.65 ? 109 ILE B N   1 
ATOM   1712 C CA  . ILE B 1 109 ? 40.801 -0.436  15.721  1.00 26.50 ? 109 ILE B CA  1 
ATOM   1713 C C   . ILE B 1 109 ? 41.674 -1.209  16.701  1.00 27.62 ? 109 ILE B C   1 
ATOM   1714 O O   . ILE B 1 109 ? 42.797 -1.590  16.377  1.00 27.43 ? 109 ILE B O   1 
ATOM   1715 C CB  . ILE B 1 109 ? 40.362 -1.389  14.598  1.00 27.84 ? 109 ILE B CB  1 
ATOM   1716 C CG1 . ILE B 1 109 ? 39.442 -0.649  13.626  1.00 26.19 ? 109 ILE B CG1 1 
ATOM   1717 C CG2 . ILE B 1 109 ? 39.658 -2.612  15.204  1.00 28.73 ? 109 ILE B CG2 1 
ATOM   1718 C CD1 . ILE B 1 109 ? 39.147 -1.429  12.359  1.00 28.10 ? 109 ILE B CD1 1 
ATOM   1719 N N   . ALA B 1 110 ? 41.158 -1.435  17.904  1.00 29.07 ? 110 ALA B N   1 
ATOM   1720 C CA  . ALA B 1 110 ? 41.909 -2.161  18.916  1.00 30.11 ? 110 ALA B CA  1 
ATOM   1721 C C   . ALA B 1 110 ? 41.704 -3.665  18.781  1.00 31.42 ? 110 ALA B C   1 
ATOM   1722 O O   . ALA B 1 110 ? 40.592 -4.129  18.527  1.00 32.22 ? 110 ALA B O   1 
ATOM   1723 C CB  . ALA B 1 110 ? 41.483 -1.702  20.306  1.00 31.81 ? 110 ALA B CB  1 
ATOM   1724 N N   . LYS B 1 111 ? 42.785 -4.422  18.936  1.00 31.44 ? 111 LYS B N   1 
ATOM   1725 C CA  . LYS B 1 111 ? 42.703 -5.875  18.869  1.00 33.25 ? 111 LYS B CA  1 
ATOM   1726 C C   . LYS B 1 111 ? 42.239 -6.336  20.247  1.00 34.35 ? 111 LYS B C   1 
ATOM   1727 O O   . LYS B 1 111 ? 42.482 -5.656  21.241  1.00 33.98 ? 111 LYS B O   1 
ATOM   1728 C CB  . LYS B 1 111 ? 44.074 -6.482  18.581  1.00 34.30 ? 111 LYS B CB  1 
ATOM   1729 C CG  . LYS B 1 111 ? 44.665 -6.124  17.234  1.00 36.15 ? 111 LYS B CG  1 
ATOM   1730 C CD  . LYS B 1 111 ? 46.079 -6.659  17.126  1.00 36.33 ? 111 LYS B CD  1 
ATOM   1731 C CE  . LYS B 1 111 ? 46.636 -6.433  15.742  1.00 38.00 ? 111 LYS B CE  1 
ATOM   1732 N NZ  . LYS B 1 111 ? 45.757 -7.102  14.748  1.00 43.68 ? 111 LYS B NZ  1 
ATOM   1733 N N   . PRO B 1 112 ? 41.574 -7.499  20.329  1.00 34.96 ? 112 PRO B N   1 
ATOM   1734 C CA  . PRO B 1 112 ? 41.225 -8.412  19.234  1.00 34.78 ? 112 PRO B CA  1 
ATOM   1735 C C   . PRO B 1 112 ? 40.212 -7.813  18.262  1.00 33.68 ? 112 PRO B C   1 
ATOM   1736 O O   . PRO B 1 112 ? 39.277 -7.123  18.666  1.00 33.81 ? 112 PRO B O   1 
ATOM   1737 C CB  . PRO B 1 112 ? 40.676 -9.632  19.972  1.00 35.93 ? 112 PRO B CB  1 
ATOM   1738 C CG  . PRO B 1 112 ? 40.021 -9.018  21.163  1.00 35.78 ? 112 PRO B CG  1 
ATOM   1739 C CD  . PRO B 1 112 ? 41.053 -8.003  21.612  1.00 35.42 ? 112 PRO B CD  1 
ATOM   1740 N N   . VAL B 1 113 ? 40.402 -8.099  16.981  1.00 33.82 ? 113 VAL B N   1 
ATOM   1741 C CA  . VAL B 1 113 ? 39.536 -7.583  15.928  1.00 34.45 ? 113 VAL B CA  1 
ATOM   1742 C C   . VAL B 1 113 ? 38.234 -8.361  15.726  1.00 34.08 ? 113 VAL B C   1 
ATOM   1743 O O   . VAL B 1 113 ? 38.235 -9.590  15.627  1.00 33.89 ? 113 VAL B O   1 
ATOM   1744 C CB  . VAL B 1 113 ? 40.290 -7.555  14.579  1.00 35.93 ? 113 VAL B CB  1 
ATOM   1745 C CG1 . VAL B 1 113 ? 39.379 -7.043  13.482  1.00 37.10 ? 113 VAL B CG1 1 
ATOM   1746 C CG2 . VAL B 1 113 ? 41.524 -6.678  14.696  1.00 36.92 ? 113 VAL B CG2 1 
ATOM   1747 N N   . ASN B 1 114 ? 37.126 -7.633  15.663  1.00 32.85 ? 114 ASN B N   1 
ATOM   1748 C CA  . ASN B 1 114 ? 35.820 -8.240  15.432  1.00 33.22 ? 114 ASN B CA  1 
ATOM   1749 C C   . ASN B 1 114 ? 35.504 -8.060  13.947  1.00 33.05 ? 114 ASN B C   1 
ATOM   1750 O O   . ASN B 1 114 ? 35.487 -6.938  13.447  1.00 30.81 ? 114 ASN B O   1 
ATOM   1751 C CB  . ASN B 1 114 ? 34.755 -7.555  16.290  1.00 33.08 ? 114 ASN B CB  1 
ATOM   1752 C CG  . ASN B 1 114 ? 33.354 -8.056  15.995  1.00 34.10 ? 114 ASN B CG  1 
ATOM   1753 O OD1 . ASN B 1 114 ? 32.830 -7.856  14.900  1.00 32.13 ? 114 ASN B OD1 1 
ATOM   1754 N ND2 . ASN B 1 114 ? 32.738 -8.713  16.977  1.00 31.56 ? 114 ASN B ND2 1 
ATOM   1755 N N   . ALA B 1 115 ? 35.260 -9.168  13.253  1.00 32.31 ? 115 ALA B N   1 
ATOM   1756 C CA  . ALA B 1 115 ? 34.973 -9.152  11.816  1.00 31.35 ? 115 ALA B CA  1 
ATOM   1757 C C   . ALA B 1 115 ? 33.834 -8.231  11.376  1.00 30.58 ? 115 ALA B C   1 
ATOM   1758 O O   . ALA B 1 115 ? 33.945 -7.543  10.354  1.00 28.27 ? 115 ALA B O   1 
ATOM   1759 C CB  . ALA B 1 115 ? 34.699 -10.568 11.337  1.00 33.00 ? 115 ALA B CB  1 
ATOM   1760 N N   . ILE B 1 116 ? 32.741 -8.220  12.132  1.00 28.04 ? 116 ILE B N   1 
ATOM   1761 C CA  . ILE B 1 116 ? 31.601 -7.378  11.791  1.00 29.45 ? 116 ILE B CA  1 
ATOM   1762 C C   . ILE B 1 116 ? 31.978 -5.906  11.897  1.00 28.43 ? 116 ILE B C   1 
ATOM   1763 O O   . ILE B 1 116 ? 31.615 -5.087  11.050  1.00 29.08 ? 116 ILE B O   1 
ATOM   1764 C CB  . ILE B 1 116 ? 30.406 -7.642  12.729  1.00 31.22 ? 116 ILE B CB  1 
ATOM   1765 C CG1 . ILE B 1 116 ? 29.989 -9.115  12.636  1.00 34.31 ? 116 ILE B CG1 1 
ATOM   1766 C CG2 . ILE B 1 116 ? 29.239 -6.743  12.349  1.00 29.65 ? 116 ILE B CG2 1 
ATOM   1767 C CD1 . ILE B 1 116 ? 28.919 -9.507  13.629  1.00 35.39 ? 116 ILE B CD1 1 
ATOM   1768 N N   . ARG B 1 117 ? 32.701 -5.584  12.961  1.00 27.43 ? 117 ARG B N   1 
ATOM   1769 C CA  . ARG B 1 117 ? 33.144 -4.227  13.219  1.00 28.19 ? 117 ARG B CA  1 
ATOM   1770 C C   . ARG B 1 117 ? 34.118 -3.808  12.117  1.00 26.33 ? 117 ARG B C   1 
ATOM   1771 O O   . ARG B 1 117 ? 33.978 -2.743  11.526  1.00 24.05 ? 117 ARG B O   1 
ATOM   1772 C CB  . ARG B 1 117 ? 33.821 -4.191  14.587  1.00 31.25 ? 117 ARG B CB  1 
ATOM   1773 C CG  . ARG B 1 117 ? 33.989 -2.830  15.197  1.00 37.38 ? 117 ARG B CG  1 
ATOM   1774 C CD  . ARG B 1 117 ? 34.242 -2.984  16.694  1.00 41.03 ? 117 ARG B CD  1 
ATOM   1775 N NE  . ARG B 1 117 ? 33.131 -3.673  17.348  1.00 44.55 ? 117 ARG B NE  1 
ATOM   1776 C CZ  . ARG B 1 117 ? 33.042 -3.879  18.657  1.00 44.42 ? 117 ARG B CZ  1 
ATOM   1777 N NH1 . ARG B 1 117 ? 34.002 -3.454  19.464  1.00 47.63 ? 117 ARG B NH1 1 
ATOM   1778 N NH2 . ARG B 1 117 ? 31.983 -4.496  19.163  1.00 47.20 ? 117 ARG B NH2 1 
ATOM   1779 N N   . LEU B 1 118 ? 35.087 -4.676  11.835  1.00 25.34 ? 118 LEU B N   1 
ATOM   1780 C CA  . LEU B 1 118 ? 36.104 -4.420  10.813  1.00 24.87 ? 118 LEU B CA  1 
ATOM   1781 C C   . LEU B 1 118 ? 35.510 -4.154  9.430   1.00 24.88 ? 118 LEU B C   1 
ATOM   1782 O O   . LEU B 1 118 ? 35.889 -3.200  8.752   1.00 22.57 ? 118 LEU B O   1 
ATOM   1783 C CB  . LEU B 1 118 ? 37.066 -5.607  10.731  1.00 26.28 ? 118 LEU B CB  1 
ATOM   1784 C CG  . LEU B 1 118 ? 38.248 -5.473  9.769   1.00 27.46 ? 118 LEU B CG  1 
ATOM   1785 C CD1 . LEU B 1 118 ? 39.072 -4.233  10.114  1.00 23.45 ? 118 LEU B CD1 1 
ATOM   1786 C CD2 . LEU B 1 118 ? 39.101 -6.736  9.855   1.00 28.00 ? 118 LEU B CD2 1 
ATOM   1787 N N   . SER B 1 119 ? 34.591 -5.012  9.003   1.00 23.06 ? 119 SER B N   1 
ATOM   1788 C CA  . SER B 1 119 ? 33.956 -4.834  7.706   1.00 23.08 ? 119 SER B CA  1 
ATOM   1789 C C   . SER B 1 119 ? 33.267 -3.474  7.613   1.00 21.48 ? 119 SER B C   1 
ATOM   1790 O O   . SER B 1 119 ? 33.399 -2.775  6.616   1.00 23.32 ? 119 SER B O   1 
ATOM   1791 C CB  . SER B 1 119 ? 32.930 -5.937  7.459   1.00 21.92 ? 119 SER B CB  1 
ATOM   1792 O OG  . SER B 1 119 ? 32.209 -5.675  6.269   1.00 26.46 ? 119 SER B OG  1 
ATOM   1793 N N   . ALA B 1 120 ? 32.543 -3.094  8.662   1.00 22.72 ? 120 ALA B N   1 
ATOM   1794 C CA  . ALA B 1 120 ? 31.824 -1.820  8.671   1.00 21.21 ? 120 ALA B CA  1 
ATOM   1795 C C   . ALA B 1 120 ? 32.773 -0.622  8.649   1.00 20.40 ? 120 ALA B C   1 
ATOM   1796 O O   . ALA B 1 120 ? 32.489 0.399   8.014   1.00 20.01 ? 120 ALA B O   1 
ATOM   1797 C CB  . ALA B 1 120 ? 30.914 -1.749  9.896   1.00 21.36 ? 120 ALA B CB  1 
ATOM   1798 N N   . ARG B 1 121 ? 33.888 -0.751  9.360   1.00 19.05 ? 121 ARG B N   1 
ATOM   1799 C CA  . ARG B 1 121 ? 34.896 0.302   9.425   1.00 21.20 ? 121 ARG B CA  1 
ATOM   1800 C C   . ARG B 1 121 ? 35.540 0.478   8.048   1.00 19.50 ? 121 ARG B C   1 
ATOM   1801 O O   . ARG B 1 121 ? 35.810 1.601   7.608   1.00 20.27 ? 121 ARG B O   1 
ATOM   1802 C CB  . ARG B 1 121 ? 35.967 -0.064  10.461  1.00 20.92 ? 121 ARG B CB  1 
ATOM   1803 C CG  . ARG B 1 121 ? 35.498 0.041   11.907  1.00 24.77 ? 121 ARG B CG  1 
ATOM   1804 C CD  . ARG B 1 121 ? 35.556 1.490   12.366  1.00 26.06 ? 121 ARG B CD  1 
ATOM   1805 N NE  . ARG B 1 121 ? 34.912 1.723   13.654  1.00 24.94 ? 121 ARG B NE  1 
ATOM   1806 C CZ  . ARG B 1 121 ? 34.776 2.928   14.196  1.00 23.85 ? 121 ARG B CZ  1 
ATOM   1807 N NH1 . ARG B 1 121 ? 35.252 3.989   13.559  1.00 22.77 ? 121 ARG B NH1 1 
ATOM   1808 N NH2 . ARG B 1 121 ? 34.137 3.081   15.347  1.00 22.22 ? 121 ARG B NH2 1 
ATOM   1809 N N   . ILE B 1 122 ? 35.790 -0.636  7.371   1.00 19.31 ? 122 ILE B N   1 
ATOM   1810 C CA  . ILE B 1 122 ? 36.390 -0.569  6.047   1.00 19.86 ? 122 ILE B CA  1 
ATOM   1811 C C   . ILE B 1 122 ? 35.443 0.149   5.093   1.00 21.63 ? 122 ILE B C   1 
ATOM   1812 O O   . ILE B 1 122 ? 35.840 1.057   4.374   1.00 19.82 ? 122 ILE B O   1 
ATOM   1813 C CB  . ILE B 1 122 ? 36.704 -1.975  5.491   1.00 19.90 ? 122 ILE B CB  1 
ATOM   1814 C CG1 . ILE B 1 122 ? 37.872 -2.592  6.268   1.00 21.65 ? 122 ILE B CG1 1 
ATOM   1815 C CG2 . ILE B 1 122 ? 37.028 -1.882  3.999   1.00 20.24 ? 122 ILE B CG2 1 
ATOM   1816 C CD1 . ILE B 1 122 ? 38.184 -4.044  5.893   1.00 21.37 ? 122 ILE B CD1 1 
ATOM   1817 N N   . LYS B 1 123 ? 34.176 -0.240  5.107   1.00 21.57 ? 123 LYS B N   1 
ATOM   1818 C CA  . LYS B 1 123 ? 33.210 0.382   4.215   1.00 22.72 ? 123 LYS B CA  1 
ATOM   1819 C C   . LYS B 1 123 ? 32.960 1.846   4.549   1.00 22.26 ? 123 LYS B C   1 
ATOM   1820 O O   . LYS B 1 123 ? 32.708 2.653   3.658   1.00 22.56 ? 123 LYS B O   1 
ATOM   1821 C CB  . LYS B 1 123 ? 31.907 -0.428  4.225   1.00 23.03 ? 123 LYS B CB  1 
ATOM   1822 C CG  . LYS B 1 123 ? 32.085 -1.786  3.549   1.00 27.31 ? 123 LYS B CG  1 
ATOM   1823 C CD  . LYS B 1 123 ? 30.802 -2.615  3.533   1.00 30.58 ? 123 LYS B CD  1 
ATOM   1824 C CE  . LYS B 1 123 ? 30.565 -3.302  4.857   1.00 33.41 ? 123 LYS B CE  1 
ATOM   1825 N NZ  . LYS B 1 123 ? 29.402 -4.239  4.762   1.00 35.98 ? 123 LYS B NZ  1 
ATOM   1826 N N   . ARG B 1 124 ? 33.056 2.195   5.827   1.00 22.87 ? 124 ARG B N   1 
ATOM   1827 C CA  . ARG B 1 124 ? 32.847 3.579   6.248   1.00 25.31 ? 124 ARG B CA  1 
ATOM   1828 C C   . ARG B 1 124 ? 33.880 4.460   5.556   1.00 25.24 ? 124 ARG B C   1 
ATOM   1829 O O   . ARG B 1 124 ? 33.551 5.502   4.981   1.00 25.13 ? 124 ARG B O   1 
ATOM   1830 C CB  . ARG B 1 124 ? 33.025 3.719   7.760   1.00 29.74 ? 124 ARG B CB  1 
ATOM   1831 C CG  . ARG B 1 124 ? 32.922 5.156   8.260   1.00 34.95 ? 124 ARG B CG  1 
ATOM   1832 C CD  . ARG B 1 124 ? 33.250 5.260   9.744   1.00 40.24 ? 124 ARG B CD  1 
ATOM   1833 N NE  . ARG B 1 124 ? 34.677 5.429   10.014  1.00 39.53 ? 124 ARG B NE  1 
ATOM   1834 C CZ  . ARG B 1 124 ? 35.343 6.567   9.843   1.00 41.04 ? 124 ARG B CZ  1 
ATOM   1835 N NH1 . ARG B 1 124 ? 34.708 7.640   9.400   1.00 42.35 ? 124 ARG B NH1 1 
ATOM   1836 N NH2 . ARG B 1 124 ? 36.647 6.635   10.110  1.00 37.14 ? 124 ARG B NH2 1 
ATOM   1837 N N   . VAL B 1 125 ? 35.133 4.026   5.615   1.00 23.52 ? 125 VAL B N   1 
ATOM   1838 C CA  . VAL B 1 125 ? 36.225 4.776   5.014   1.00 23.95 ? 125 VAL B CA  1 
ATOM   1839 C C   . VAL B 1 125 ? 36.132 4.831   3.494   1.00 23.47 ? 125 VAL B C   1 
ATOM   1840 O O   . VAL B 1 125 ? 36.331 5.890   2.898   1.00 24.31 ? 125 VAL B O   1 
ATOM   1841 C CB  . VAL B 1 125 ? 37.586 4.184   5.431   1.00 23.19 ? 125 VAL B CB  1 
ATOM   1842 C CG1 . VAL B 1 125 ? 38.710 4.844   4.648   1.00 24.40 ? 125 VAL B CG1 1 
ATOM   1843 C CG2 . VAL B 1 125 ? 37.797 4.392   6.928   1.00 23.77 ? 125 VAL B CG2 1 
ATOM   1844 N N   . LEU B 1 126 ? 35.828 3.698   2.867   1.00 22.86 ? 126 LEU B N   1 
ATOM   1845 C CA  . LEU B 1 126 ? 35.723 3.656   1.414   1.00 24.01 ? 126 LEU B CA  1 
ATOM   1846 C C   . LEU B 1 126 ? 34.623 4.597   0.927   1.00 26.58 ? 126 LEU B C   1 
ATOM   1847 O O   . LEU B 1 126 ? 34.781 5.278   -0.087  1.00 24.71 ? 126 LEU B O   1 
ATOM   1848 C CB  . LEU B 1 126 ? 35.450 2.225   0.933   1.00 22.60 ? 126 LEU B CB  1 
ATOM   1849 C CG  . LEU B 1 126 ? 36.572 1.202   1.180   1.00 23.46 ? 126 LEU B CG  1 
ATOM   1850 C CD1 . LEU B 1 126 ? 36.120 -0.186  0.725   1.00 22.45 ? 126 LEU B CD1 1 
ATOM   1851 C CD2 . LEU B 1 126 ? 37.836 1.624   0.440   1.00 21.90 ? 126 LEU B CD2 1 
ATOM   1852 N N   . LYS B 1 127 ? 33.511 4.645   1.653   1.00 26.65 ? 127 LYS B N   1 
ATOM   1853 C CA  . LYS B 1 127 ? 32.409 5.520   1.269   1.00 28.79 ? 127 LYS B CA  1 
ATOM   1854 C C   . LYS B 1 127 ? 32.802 6.988   1.372   1.00 28.37 ? 127 LYS B C   1 
ATOM   1855 O O   . LYS B 1 127 ? 32.391 7.800   0.552   1.00 29.19 ? 127 LYS B O   1 
ATOM   1856 C CB  . LYS B 1 127 ? 31.182 5.254   2.144   1.00 30.10 ? 127 LYS B CB  1 
ATOM   1857 C CG  . LYS B 1 127 ? 30.494 3.935   1.844   1.00 31.63 ? 127 LYS B CG  1 
ATOM   1858 C CD  . LYS B 1 127 ? 29.288 3.703   2.756   1.00 33.49 ? 127 LYS B CD  1 
ATOM   1859 C CE  . LYS B 1 127 ? 29.706 3.591   4.221   1.00 33.68 ? 127 LYS B CE  1 
ATOM   1860 N NZ  . LYS B 1 127 ? 28.567 3.186   5.083   1.00 33.01 ? 127 LYS B NZ  1 
ATOM   1861 N N   . LEU B 1 128 ? 33.599 7.322   2.379   1.00 29.05 ? 128 LEU B N   1 
ATOM   1862 C CA  . LEU B 1 128 ? 34.041 8.698   2.584   1.00 31.20 ? 128 LEU B CA  1 
ATOM   1863 C C   . LEU B 1 128 ? 35.082 9.154   1.562   1.00 32.12 ? 128 LEU B C   1 
ATOM   1864 O O   . LEU B 1 128 ? 35.068 10.305  1.124   1.00 31.79 ? 128 LEU B O   1 
ATOM   1865 C CB  . LEU B 1 128 ? 34.637 8.867   3.987   1.00 30.34 ? 128 LEU B CB  1 
ATOM   1866 C CG  . LEU B 1 128 ? 33.733 8.705   5.213   1.00 32.28 ? 128 LEU B CG  1 
ATOM   1867 C CD1 . LEU B 1 128 ? 34.563 8.856   6.481   1.00 35.10 ? 128 LEU B CD1 1 
ATOM   1868 C CD2 . LEU B 1 128 ? 32.628 9.747   5.180   1.00 34.36 ? 128 LEU B CD2 1 
ATOM   1869 N N   . LEU B 1 129 ? 35.981 8.251   1.181   1.00 31.78 ? 129 LEU B N   1 
ATOM   1870 C CA  . LEU B 1 129 ? 37.054 8.598   0.250   1.00 33.13 ? 129 LEU B CA  1 
ATOM   1871 C C   . LEU B 1 129 ? 36.854 8.290   -1.233  1.00 33.46 ? 129 LEU B C   1 
ATOM   1872 O O   . LEU B 1 129 ? 37.465 8.941   -2.079  1.00 34.44 ? 129 LEU B O   1 
ATOM   1873 C CB  . LEU B 1 129 ? 38.369 7.968   0.727   1.00 33.46 ? 129 LEU B CB  1 
ATOM   1874 C CG  . LEU B 1 129 ? 39.045 8.573   1.965   1.00 36.86 ? 129 LEU B CG  1 
ATOM   1875 C CD1 . LEU B 1 129 ? 39.469 10.009  1.673   1.00 38.24 ? 129 LEU B CD1 1 
ATOM   1876 C CD2 . LEU B 1 129 ? 38.100 8.539   3.149   1.00 37.70 ? 129 LEU B CD2 1 
ATOM   1877 N N   . TYR B 1 130 ? 36.019 7.311   -1.564  1.00 32.80 ? 130 TYR B N   1 
ATOM   1878 C CA  . TYR B 1 130 ? 35.802 6.982   -2.971  1.00 34.38 ? 130 TYR B CA  1 
ATOM   1879 C C   . TYR B 1 130 ? 34.398 7.326   -3.479  1.00 37.60 ? 130 TYR B C   1 
ATOM   1880 O O   . TYR B 1 130 ? 34.310 8.132   -4.432  1.00 41.37 ? 130 TYR B O   1 
ATOM   1881 C CB  . TYR B 1 130 ? 36.098 5.500   -3.223  1.00 28.90 ? 130 TYR B CB  1 
ATOM   1882 C CG  . TYR B 1 130 ? 37.556 5.126   -3.052  1.00 25.94 ? 130 TYR B CG  1 
ATOM   1883 C CD1 . TYR B 1 130 ? 38.061 4.741   -1.809  1.00 22.51 ? 130 TYR B CD1 1 
ATOM   1884 C CD2 . TYR B 1 130 ? 38.435 5.164   -4.137  1.00 23.66 ? 130 TYR B CD2 1 
ATOM   1885 C CE1 . TYR B 1 130 ? 39.409 4.397   -1.651  1.00 19.21 ? 130 TYR B CE1 1 
ATOM   1886 C CE2 . TYR B 1 130 ? 39.777 4.828   -3.992  1.00 20.67 ? 130 TYR B CE2 1 
ATOM   1887 C CZ  . TYR B 1 130 ? 40.261 4.442   -2.750  1.00 20.01 ? 130 TYR B CZ  1 
ATOM   1888 O OH  . TYR B 1 130 ? 41.590 4.088   -2.613  1.00 20.65 ? 130 TYR B OH  1 
HETATM 1889 O O   . HOH C 2 .   ? 27.611 11.423  9.141   1.00 22.65 ? 148 HOH A O   1 
HETATM 1890 O O   . HOH C 2 .   ? 22.454 -4.532  19.266  1.00 27.23 ? 149 HOH A O   1 
HETATM 1891 O O   . HOH C 2 .   ? 26.044 13.367  7.635   1.00 23.38 ? 150 HOH A O   1 
HETATM 1892 O O   . HOH C 2 .   ? 29.825 1.015   7.163   1.00 25.04 ? 151 HOH A O   1 
HETATM 1893 O O   . HOH C 2 .   ? 26.782 -7.683  17.631  1.00 30.59 ? 152 HOH A O   1 
HETATM 1894 O O   . HOH C 2 .   ? 43.098 13.485  15.161  1.00 26.44 ? 153 HOH A O   1 
HETATM 1895 O O   . HOH C 2 .   ? 24.393 24.351  8.636   1.00 26.54 ? 154 HOH A O   1 
HETATM 1896 O O   . HOH C 2 .   ? 23.575 15.918  9.636   1.00 23.83 ? 155 HOH A O   1 
HETATM 1897 O O   . HOH C 2 .   ? 23.396 4.768   23.924  1.00 40.42 ? 156 HOH A O   1 
HETATM 1898 O O   . HOH C 2 .   ? 20.944 15.338  29.301  1.00 29.29 ? 157 HOH A O   1 
HETATM 1899 O O   . HOH C 2 .   ? 20.083 4.638   16.999  1.00 36.68 ? 158 HOH A O   1 
HETATM 1900 O O   . HOH C 2 .   ? 21.067 30.910  10.725  1.00 28.60 ? 159 HOH A O   1 
HETATM 1901 O O   . HOH C 2 .   ? 21.977 0.352   8.930   1.00 33.40 ? 160 HOH A O   1 
HETATM 1902 O O   . HOH C 2 .   ? 15.223 25.637  7.702   1.00 37.27 ? 161 HOH A O   1 
HETATM 1903 O O   . HOH C 2 .   ? 37.478 9.834   13.727  1.00 30.59 ? 162 HOH A O   1 
HETATM 1904 O O   . HOH C 2 .   ? 18.916 28.083  9.262   1.00 34.13 ? 163 HOH A O   1 
HETATM 1905 O O   . HOH C 2 .   ? 24.768 -4.673  11.625  1.00 37.37 ? 164 HOH A O   1 
HETATM 1906 O O   . HOH C 2 .   ? 22.281 13.469  9.154   1.00 34.68 ? 165 HOH A O   1 
HETATM 1907 O O   . HOH C 2 .   ? 23.102 8.954   28.171  1.00 40.60 ? 166 HOH A O   1 
HETATM 1908 O O   . HOH C 2 .   ? 16.376 26.514  20.785  1.00 37.12 ? 167 HOH A O   1 
HETATM 1909 O O   . HOH C 2 .   ? 34.581 2.515   20.104  1.00 35.89 ? 168 HOH A O   1 
HETATM 1910 O O   . HOH C 2 .   ? 15.430 12.317  22.182  1.00 33.08 ? 169 HOH A O   1 
HETATM 1911 O O   . HOH C 2 .   ? 45.185 14.126  11.457  1.00 42.81 ? 170 HOH A O   1 
HETATM 1912 O O   . HOH C 2 .   ? 43.643 13.888  21.986  1.00 34.40 ? 171 HOH A O   1 
HETATM 1913 O O   . HOH C 2 .   ? 35.726 -0.675  15.858  1.00 38.61 ? 172 HOH A O   1 
HETATM 1914 O O   . HOH C 2 .   ? 17.764 17.493  2.553   1.00 33.24 ? 173 HOH A O   1 
HETATM 1915 O O   . HOH C 2 .   ? 20.224 17.962  30.239  1.00 33.92 ? 174 HOH A O   1 
HETATM 1916 O O   . HOH C 2 .   ? 28.147 13.527  5.747   1.00 41.79 ? 175 HOH A O   1 
HETATM 1917 O O   . HOH C 2 .   ? 24.726 -3.378  9.133   1.00 37.93 ? 176 HOH A O   1 
HETATM 1918 O O   . HOH C 2 .   ? 21.030 6.465   5.996   1.00 38.57 ? 177 HOH A O   1 
HETATM 1919 O O   . HOH C 2 .   ? 20.292 14.558  32.844  1.00 41.88 ? 178 HOH A O   1 
HETATM 1920 O O   . HOH D 2 .   ? 48.374 9.075   -5.842  1.00 18.13 ? 148 HOH B O   1 
HETATM 1921 O O   . HOH D 2 .   ? 47.913 7.391   -3.232  1.00 20.18 ? 149 HOH B O   1 
HETATM 1922 O O   . HOH D 2 .   ? 48.356 3.143   -5.757  1.00 25.39 ? 150 HOH B O   1 
HETATM 1923 O O   . HOH D 2 .   ? 45.014 7.697   6.254   1.00 21.11 ? 151 HOH B O   1 
HETATM 1924 O O   . HOH D 2 .   ? 52.493 2.765   10.577  1.00 25.72 ? 152 HOH B O   1 
HETATM 1925 O O   . HOH D 2 .   ? 51.558 -1.078  -11.184 1.00 28.84 ? 153 HOH B O   1 
HETATM 1926 O O   . HOH D 2 .   ? 38.675 0.092   18.922  1.00 26.10 ? 154 HOH B O   1 
HETATM 1927 O O   . HOH D 2 .   ? 49.152 5.580   2.506   1.00 23.19 ? 155 HOH B O   1 
HETATM 1928 O O   . HOH D 2 .   ? 57.184 3.444   -7.413  1.00 37.60 ? 156 HOH B O   1 
HETATM 1929 O O   . HOH D 2 .   ? 50.219 7.291   4.488   1.00 32.97 ? 157 HOH B O   1 
HETATM 1930 O O   . HOH D 2 .   ? 29.537 -5.428  9.240   1.00 28.01 ? 158 HOH B O   1 
HETATM 1931 O O   . HOH D 2 .   ? 46.647 8.357   4.051   1.00 33.28 ? 159 HOH B O   1 
HETATM 1932 O O   . HOH D 2 .   ? 57.238 -0.920  9.807   1.00 32.97 ? 160 HOH B O   1 
HETATM 1933 O O   . HOH D 2 .   ? 52.479 -0.073  10.602  1.00 33.61 ? 161 HOH B O   1 
HETATM 1934 O O   . HOH D 2 .   ? 55.405 0.343   10.956  1.00 28.81 ? 162 HOH B O   1 
HETATM 1935 O O   . HOH D 2 .   ? 57.122 10.563  5.204   1.00 34.57 ? 163 HOH B O   1 
HETATM 1936 O O   . HOH D 2 .   ? 29.998 -9.891  16.637  1.00 36.81 ? 164 HOH B O   1 
HETATM 1937 O O   . HOH D 2 .   ? 57.246 -3.252  -5.959  1.00 31.44 ? 165 HOH B O   1 
HETATM 1938 O O   . HOH D 2 .   ? 58.171 -1.286  3.460   1.00 34.87 ? 166 HOH B O   1 
HETATM 1939 O O   . HOH D 2 .   ? 53.663 1.450   -9.048  1.00 35.25 ? 167 HOH B O   1 
HETATM 1940 O O   . HOH D 2 .   ? 39.045 11.573  -1.617  1.00 40.74 ? 168 HOH B O   1 
HETATM 1941 O O   . HOH D 2 .   ? 37.511 1.353   16.787  1.00 37.92 ? 169 HOH B O   1 
HETATM 1942 O O   . HOH D 2 .   ? 39.825 2.034   -8.336  1.00 36.32 ? 170 HOH B O   1 
HETATM 1943 O O   . HOH D 2 .   ? 44.083 -13.349 1.301   1.00 40.09 ? 171 HOH B O   1 
HETATM 1944 O O   . HOH D 2 .   ? 52.588 3.693   13.289  1.00 36.25 ? 172 HOH B O   1 
HETATM 1945 O O   . HOH D 2 .   ? 44.264 14.754  19.315  1.00 42.27 ? 173 HOH B O   1 
# 
