data_9IM9
# 
_entry.id   9IM9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9IM9         pdb_00009im9 10.2210/pdb9im9/pdb 
WWPDB D_1300049085 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-14 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IM9 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              raoyijian@jiangnan.edu.cn 
_pdbx_contact_author.name_first         Yijian 
_pdbx_contact_author.name_last          Rao 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2481-0588 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fu, K.'    1 0009-0002-3339-2138 
'Rao, Y.J.' 2 0000-0003-2481-0588 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Am.Chem.Soc. 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            147 
_citation.language                  ? 
_citation.page_first                13190 
_citation.page_last                 13199 
_citation.title                     'Light-Driven Deracemization by a Designed Photoenzyme.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.4c16521 
_citation.pdbx_database_id_PubMed   40219972 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Li, M.'    1 ?                   
primary 'Zhang, Y.' 2 0000-0002-4941-8622 
primary 'Fu, K.'    3 ?                   
primary 'Deng, Z.'  4 0000-0003-2479-6050 
primary 'Yuan, Z.'  5 0000-0002-2435-0318 
primary 'Luo, Z.'   6 0000-0002-3087-5663 
primary 'Rao, Y.'   7 0000-0003-2481-0588 
# 
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 CTB10                                                                               16447.676 2   ? 
W13F,T107A,S120T,H111L,L124G ? ? 
2 non-polymer syn 'SULFATE ION'                                                                       96.063    4   ? ? ? ? 
3 non-polymer syn GLYCEROL                                                                            92.094    4   ? ? ? ? 
4 non-polymer syn "(3~{S})-1',1'-bis(chloranyl)-5-methyl-spiro[1~{H}-indole-3,2'-cyclopropane]-2-one" 242.101   2   ? ? ? ? 
5 water       nat water                                                                               18.015    198 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MGSIGEPNRLLC(PBF)SIYVTKKPDQSEEDHHNHVSKVNAPMMIPFLKKYGIVRYTVKHNDAYSKPKQAALMAGQPEEN
VLAYDTVFEMIVKDIESIQTMQKDEEFLRTAIPDLFNFADMTRTKGSGTWIEEFTFALEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSIGEPNRLLCFSIYVTKKPDQSEEDHHNHVSKVNAPMMIPFLKKYGIVRYTVKHNDAYSKPKQAALMAGQPEENVLAY
DTVFEMIVKDIESIQTMQKDEEFLRTAIPDLFNFADMTRTKGSGTWIEEFTFALEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                                                       SO4   
3 GLYCEROL                                                                            GOL   
4 "(3~{S})-1',1'-bis(chloranyl)-5-methyl-spiro[1~{H}-indole-3,2'-cyclopropane]-2-one" A1D9Q 
5 water                                                                               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   GLY n 
1 3   SER n 
1 4   ILE n 
1 5   GLY n 
1 6   GLU n 
1 7   PRO n 
1 8   ASN n 
1 9   ARG n 
1 10  LEU n 
1 11  LEU n 
1 12  CYS n 
1 13  PBF n 
1 14  SER n 
1 15  ILE n 
1 16  TYR n 
1 17  VAL n 
1 18  THR n 
1 19  LYS n 
1 20  LYS n 
1 21  PRO n 
1 22  ASP n 
1 23  GLN n 
1 24  SER n 
1 25  GLU n 
1 26  GLU n 
1 27  ASP n 
1 28  HIS n 
1 29  HIS n 
1 30  ASN n 
1 31  HIS n 
1 32  VAL n 
1 33  SER n 
1 34  LYS n 
1 35  VAL n 
1 36  ASN n 
1 37  ALA n 
1 38  PRO n 
1 39  MET n 
1 40  MET n 
1 41  ILE n 
1 42  PRO n 
1 43  PHE n 
1 44  LEU n 
1 45  LYS n 
1 46  LYS n 
1 47  TYR n 
1 48  GLY n 
1 49  ILE n 
1 50  VAL n 
1 51  ARG n 
1 52  TYR n 
1 53  THR n 
1 54  VAL n 
1 55  LYS n 
1 56  HIS n 
1 57  ASN n 
1 58  ASP n 
1 59  ALA n 
1 60  TYR n 
1 61  SER n 
1 62  LYS n 
1 63  PRO n 
1 64  LYS n 
1 65  GLN n 
1 66  ALA n 
1 67  ALA n 
1 68  LEU n 
1 69  MET n 
1 70  ALA n 
1 71  GLY n 
1 72  GLN n 
1 73  PRO n 
1 74  GLU n 
1 75  GLU n 
1 76  ASN n 
1 77  VAL n 
1 78  LEU n 
1 79  ALA n 
1 80  TYR n 
1 81  ASP n 
1 82  THR n 
1 83  VAL n 
1 84  PHE n 
1 85  GLU n 
1 86  MET n 
1 87  ILE n 
1 88  VAL n 
1 89  LYS n 
1 90  ASP n 
1 91  ILE n 
1 92  GLU n 
1 93  SER n 
1 94  ILE n 
1 95  GLN n 
1 96  THR n 
1 97  MET n 
1 98  GLN n 
1 99  LYS n 
1 100 ASP n 
1 101 GLU n 
1 102 GLU n 
1 103 PHE n 
1 104 LEU n 
1 105 ARG n 
1 106 THR n 
1 107 ALA n 
1 108 ILE n 
1 109 PRO n 
1 110 ASP n 
1 111 LEU n 
1 112 PHE n 
1 113 ASN n 
1 114 PHE n 
1 115 ALA n 
1 116 ASP n 
1 117 MET n 
1 118 THR n 
1 119 ARG n 
1 120 THR n 
1 121 LYS n 
1 122 GLY n 
1 123 SER n 
1 124 GLY n 
1 125 THR n 
1 126 TRP n 
1 127 ILE n 
1 128 GLU n 
1 129 GLU n 
1 130 PHE n 
1 131 THR n 
1 132 PHE n 
1 133 ALA n 
1 134 LEU n 
1 135 GLU n 
1 136 HIS n 
1 137 HIS n 
1 138 HIS n 
1 139 HIS n 
1 140 HIS n 
1 141 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                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   141 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Cercospora sp. JNU001' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2979285 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1D9Q non-polymer         . "(3~{S})-1',1'-bis(chloranyl)-5-methyl-spiro[1~{H}-indole-3,2'-cyclopropane]-2-one" ? 'C11 H9 Cl2 N O' 
242.101 
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  
GOL   non-polymer         . GLYCEROL                                                                            
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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 
PBF   'L-peptide linking' n 'PARA-(BENZOYL)-PHENYLALANINE'                                                      ? 'C16 H15 N O3'   
269.295 
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 
SO4   non-polymer         . 'SULFATE ION'                                                                       ? 'O4 S -2'        
96.063  
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   GLY 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   ?   ?   ?   A . n 
A 1 4   ILE 4   4   ?   ?   ?   A . n 
A 1 5   GLY 5   5   ?   ?   ?   A . n 
A 1 6   GLU 6   6   ?   ?   ?   A . n 
A 1 7   PRO 7   7   ?   ?   ?   A . n 
A 1 8   ASN 8   8   ?   ?   ?   A . n 
A 1 9   ARG 9   9   9   ARG ARG A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  CYS 12  12  12  CYS CYS A . n 
A 1 13  PBF 13  13  13  PBF PBF A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  ILE 15  15  15  ILE ILE A . n 
A 1 16  TYR 16  16  16  TYR TYR A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  GLN 23  23  23  GLN GLN A . n 
A 1 24  SER 24  24  24  SER SER A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  HIS 28  28  28  HIS HIS A . n 
A 1 29  HIS 29  29  29  HIS HIS A . n 
A 1 30  ASN 30  30  30  ASN ASN A . n 
A 1 31  HIS 31  31  31  HIS HIS A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  ASN 36  36  36  ASN ASN A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  MET 39  39  39  MET MET A . n 
A 1 40  MET 40  40  40  MET MET A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  TYR 47  47  47  TYR TYR A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  ILE 49  49  49  ILE ILE A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  ARG 51  51  51  ARG ARG A . n 
A 1 52  TYR 52  52  52  TYR TYR A . n 
A 1 53  THR 53  53  53  THR THR A . n 
A 1 54  VAL 54  54  54  VAL VAL A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  HIS 56  56  56  HIS HIS A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  ASP 58  58  58  ASP ASP A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  TYR 60  60  60  TYR TYR A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  LYS 62  62  62  LYS LYS 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  GLN 65  65  65  GLN GLN A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  MET 69  69  69  MET MET A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  GLN 72  72  72  GLN GLN A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  ASN 76  76  76  ASN ASN A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  TYR 80  80  80  TYR TYR A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  THR 82  82  82  THR THR A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  PHE 84  84  84  PHE PHE A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  MET 86  86  86  MET MET A . n 
A 1 87  ILE 87  87  87  ILE ILE A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  GLN 95  95  95  GLN GLN A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  MET 97  97  97  MET MET A . n 
A 1 98  GLN 98  98  98  GLN GLN A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 ASP 100 100 100 ASP ASP A . n 
A 1 101 GLU 101 101 101 GLU GLU A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 PRO 109 109 109 PRO PRO A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 ASN 113 113 113 ASN ASN A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ASP 116 116 116 ASP ASP A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 TRP 126 126 126 TRP TRP A . n 
A 1 127 ILE 127 127 127 ILE ILE A . n 
A 1 128 GLU 128 128 128 GLU GLU A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 ALA 133 133 ?   ?   ?   A . n 
A 1 134 LEU 134 134 ?   ?   ?   A . n 
A 1 135 GLU 135 135 ?   ?   ?   A . n 
A 1 136 HIS 136 136 ?   ?   ?   A . n 
A 1 137 HIS 137 137 ?   ?   ?   A . n 
A 1 138 HIS 138 138 ?   ?   ?   A . n 
A 1 139 HIS 139 139 ?   ?   ?   A . n 
A 1 140 HIS 140 140 ?   ?   ?   A . n 
A 1 141 HIS 141 141 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   GLY 2   2   ?   ?   ?   B . n 
B 1 3   SER 3   3   ?   ?   ?   B . n 
B 1 4   ILE 4   4   ?   ?   ?   B . n 
B 1 5   GLY 5   5   ?   ?   ?   B . n 
B 1 6   GLU 6   6   ?   ?   ?   B . n 
B 1 7   PRO 7   7   ?   ?   ?   B . n 
B 1 8   ASN 8   8   ?   ?   ?   B . n 
B 1 9   ARG 9   9   9   ARG ARG B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LEU 11  11  11  LEU LEU B . n 
B 1 12  CYS 12  12  12  CYS CYS B . n 
B 1 13  PBF 13  13  13  PBF PBF B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  ILE 15  15  15  ILE ILE B . n 
B 1 16  TYR 16  16  16  TYR TYR B . n 
B 1 17  VAL 17  17  17  VAL VAL B . n 
B 1 18  THR 18  18  18  THR THR B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  LYS 20  20  20  LYS LYS B . n 
B 1 21  PRO 21  21  21  PRO PRO B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  GLN 23  23  23  GLN GLN B . n 
B 1 24  SER 24  24  24  SER SER B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ASP 27  27  27  ASP ASP B . n 
B 1 28  HIS 28  28  28  HIS HIS B . n 
B 1 29  HIS 29  29  29  HIS HIS B . n 
B 1 30  ASN 30  30  30  ASN ASN B . n 
B 1 31  HIS 31  31  31  HIS HIS B . n 
B 1 32  VAL 32  32  32  VAL VAL B . n 
B 1 33  SER 33  33  33  SER SER B . n 
B 1 34  LYS 34  34  34  LYS LYS B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  ASN 36  36  36  ASN ASN B . n 
B 1 37  ALA 37  37  37  ALA ALA B . n 
B 1 38  PRO 38  38  38  PRO PRO B . n 
B 1 39  MET 39  39  39  MET MET B . n 
B 1 40  MET 40  40  40  MET MET B . n 
B 1 41  ILE 41  41  41  ILE ILE B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  PHE 43  43  43  PHE PHE B . n 
B 1 44  LEU 44  44  44  LEU LEU B . n 
B 1 45  LYS 45  45  45  LYS LYS B . n 
B 1 46  LYS 46  46  46  LYS LYS B . n 
B 1 47  TYR 47  47  47  TYR TYR B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  ILE 49  49  49  ILE ILE B . n 
B 1 50  VAL 50  50  50  VAL VAL B . n 
B 1 51  ARG 51  51  51  ARG ARG B . n 
B 1 52  TYR 52  52  52  TYR TYR B . n 
B 1 53  THR 53  53  53  THR THR B . n 
B 1 54  VAL 54  54  54  VAL VAL B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  HIS 56  56  56  HIS HIS B . n 
B 1 57  ASN 57  57  57  ASN ASN B . n 
B 1 58  ASP 58  58  58  ASP ASP B . n 
B 1 59  ALA 59  59  59  ALA ALA B . n 
B 1 60  TYR 60  60  60  TYR TYR B . n 
B 1 61  SER 61  61  61  SER SER B . n 
B 1 62  LYS 62  62  62  LYS LYS 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  GLN 65  65  65  GLN GLN B . n 
B 1 66  ALA 66  66  66  ALA ALA B . n 
B 1 67  ALA 67  67  67  ALA ALA B . n 
B 1 68  LEU 68  68  68  LEU LEU B . n 
B 1 69  MET 69  69  69  MET MET B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  GLN 72  72  72  GLN GLN B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  GLU 74  74  74  GLU GLU B . n 
B 1 75  GLU 75  75  75  GLU GLU B . n 
B 1 76  ASN 76  76  76  ASN ASN B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  TYR 80  80  80  TYR TYR B . n 
B 1 81  ASP 81  81  81  ASP ASP B . n 
B 1 82  THR 82  82  82  THR THR B . n 
B 1 83  VAL 83  83  83  VAL VAL B . n 
B 1 84  PHE 84  84  84  PHE PHE B . n 
B 1 85  GLU 85  85  85  GLU GLU B . n 
B 1 86  MET 86  86  86  MET MET B . n 
B 1 87  ILE 87  87  87  ILE ILE B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  LYS 89  89  89  LYS LYS B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  GLU 92  92  92  GLU GLU B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  ILE 94  94  94  ILE ILE B . n 
B 1 95  GLN 95  95  95  GLN GLN B . n 
B 1 96  THR 96  96  96  THR THR B . n 
B 1 97  MET 97  97  97  MET MET B . n 
B 1 98  GLN 98  98  98  GLN GLN B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 ASP 100 100 100 ASP ASP B . n 
B 1 101 GLU 101 101 101 GLU GLU B . n 
B 1 102 GLU 102 102 102 GLU GLU B . n 
B 1 103 PHE 103 103 103 PHE PHE B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 ARG 105 105 105 ARG ARG B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 ALA 107 107 107 ALA ALA B . n 
B 1 108 ILE 108 108 108 ILE ILE B . n 
B 1 109 PRO 109 109 109 PRO PRO B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 ASN 113 113 113 ASN ASN B . n 
B 1 114 PHE 114 114 114 PHE PHE B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 ASP 116 116 116 ASP ASP B . n 
B 1 117 MET 117 117 117 MET MET B . n 
B 1 118 THR 118 118 118 THR THR B . n 
B 1 119 ARG 119 119 119 ARG ARG B . n 
B 1 120 THR 120 120 120 THR THR B . n 
B 1 121 LYS 121 121 121 LYS LYS B . n 
B 1 122 GLY 122 122 122 GLY GLY B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 THR 125 125 125 THR THR B . n 
B 1 126 TRP 126 126 126 TRP TRP B . n 
B 1 127 ILE 127 127 127 ILE ILE B . n 
B 1 128 GLU 128 128 128 GLU GLU B . n 
B 1 129 GLU 129 129 129 GLU GLU B . n 
B 1 130 PHE 130 130 130 PHE PHE B . n 
B 1 131 THR 131 131 131 THR THR B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 ALA 133 133 ?   ?   ?   B . n 
B 1 134 LEU 134 134 ?   ?   ?   B . n 
B 1 135 GLU 135 135 ?   ?   ?   B . n 
B 1 136 HIS 136 136 ?   ?   ?   B . n 
B 1 137 HIS 137 137 ?   ?   ?   B . n 
B 1 138 HIS 138 138 ?   ?   ?   B . n 
B 1 139 HIS 139 139 ?   ?   ?   B . n 
B 1 140 HIS 140 140 ?   ?   ?   B . n 
B 1 141 HIS 141 141 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1D9Q 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1D9Q 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 SO4   1  201 202 SO4   SO4 A . 
D 2 SO4   1  202 204 SO4   SO4 A . 
E 3 GOL   1  203 205 GOL   GOL A . 
F 4 A1D9Q 1  204 206 A1D9Q LG3 A . 
G 3 GOL   1  205 203 GOL   GOL A . 
H 3 GOL   1  201 203 GOL   GOL B . 
I 2 SO4   1  202 202 SO4   SO4 B . 
J 2 SO4   1  203 204 SO4   SO4 B . 
K 3 GOL   1  204 205 GOL   GOL B . 
L 4 A1D9Q 1  205 206 A1D9Q LG3 B . 
M 5 HOH   1  301 141 HOH   HOH A . 
M 5 HOH   2  302 79  HOH   HOH A . 
M 5 HOH   3  303 51  HOH   HOH A . 
M 5 HOH   4  304 56  HOH   HOH A . 
M 5 HOH   5  305 6   HOH   HOH A . 
M 5 HOH   6  306 25  HOH   HOH A . 
M 5 HOH   7  307 198 HOH   HOH A . 
M 5 HOH   8  308 121 HOH   HOH A . 
M 5 HOH   9  309 21  HOH   HOH A . 
M 5 HOH   10 310 112 HOH   HOH A . 
M 5 HOH   11 311 69  HOH   HOH A . 
M 5 HOH   12 312 168 HOH   HOH A . 
M 5 HOH   13 313 88  HOH   HOH A . 
M 5 HOH   14 314 8   HOH   HOH A . 
M 5 HOH   15 315 40  HOH   HOH A . 
M 5 HOH   16 316 134 HOH   HOH A . 
M 5 HOH   17 317 14  HOH   HOH A . 
M 5 HOH   18 318 44  HOH   HOH A . 
M 5 HOH   19 319 2   HOH   HOH A . 
M 5 HOH   20 320 81  HOH   HOH A . 
M 5 HOH   21 321 211 HOH   HOH A . 
M 5 HOH   22 322 29  HOH   HOH A . 
M 5 HOH   23 323 28  HOH   HOH A . 
M 5 HOH   24 324 118 HOH   HOH A . 
M 5 HOH   25 325 80  HOH   HOH A . 
M 5 HOH   26 326 200 HOH   HOH A . 
M 5 HOH   27 327 116 HOH   HOH A . 
M 5 HOH   28 328 93  HOH   HOH A . 
M 5 HOH   29 329 11  HOH   HOH A . 
M 5 HOH   30 330 206 HOH   HOH A . 
M 5 HOH   31 331 176 HOH   HOH A . 
M 5 HOH   32 332 188 HOH   HOH A . 
M 5 HOH   33 333 103 HOH   HOH A . 
M 5 HOH   34 334 5   HOH   HOH A . 
M 5 HOH   35 335 89  HOH   HOH A . 
M 5 HOH   36 336 163 HOH   HOH A . 
M 5 HOH   37 337 161 HOH   HOH A . 
M 5 HOH   38 338 18  HOH   HOH A . 
M 5 HOH   39 339 67  HOH   HOH A . 
M 5 HOH   40 340 24  HOH   HOH A . 
M 5 HOH   41 341 45  HOH   HOH A . 
M 5 HOH   42 342 32  HOH   HOH A . 
M 5 HOH   43 343 37  HOH   HOH A . 
M 5 HOH   44 344 39  HOH   HOH A . 
M 5 HOH   45 345 7   HOH   HOH A . 
M 5 HOH   46 346 20  HOH   HOH A . 
M 5 HOH   47 347 48  HOH   HOH A . 
M 5 HOH   48 348 66  HOH   HOH A . 
M 5 HOH   49 349 202 HOH   HOH A . 
M 5 HOH   50 350 86  HOH   HOH A . 
M 5 HOH   51 351 72  HOH   HOH A . 
M 5 HOH   52 352 36  HOH   HOH A . 
M 5 HOH   53 353 10  HOH   HOH A . 
M 5 HOH   54 354 102 HOH   HOH A . 
M 5 HOH   55 355 148 HOH   HOH A . 
M 5 HOH   56 356 64  HOH   HOH A . 
M 5 HOH   57 357 157 HOH   HOH A . 
M 5 HOH   58 358 167 HOH   HOH A . 
M 5 HOH   59 359 47  HOH   HOH A . 
M 5 HOH   60 360 22  HOH   HOH A . 
M 5 HOH   61 361 147 HOH   HOH A . 
M 5 HOH   62 362 96  HOH   HOH A . 
M 5 HOH   63 363 153 HOH   HOH A . 
M 5 HOH   64 364 58  HOH   HOH A . 
M 5 HOH   65 365 138 HOH   HOH A . 
M 5 HOH   66 366 171 HOH   HOH A . 
M 5 HOH   67 367 97  HOH   HOH A . 
M 5 HOH   68 368 189 HOH   HOH A . 
M 5 HOH   69 369 207 HOH   HOH A . 
M 5 HOH   70 370 83  HOH   HOH A . 
M 5 HOH   71 371 124 HOH   HOH A . 
M 5 HOH   72 372 130 HOH   HOH A . 
M 5 HOH   73 373 156 HOH   HOH A . 
M 5 HOH   74 374 177 HOH   HOH A . 
M 5 HOH   75 375 178 HOH   HOH A . 
M 5 HOH   76 376 55  HOH   HOH A . 
M 5 HOH   77 377 60  HOH   HOH A . 
M 5 HOH   78 378 191 HOH   HOH A . 
M 5 HOH   79 379 180 HOH   HOH A . 
M 5 HOH   80 380 144 HOH   HOH A . 
M 5 HOH   81 381 110 HOH   HOH A . 
M 5 HOH   82 382 162 HOH   HOH A . 
M 5 HOH   83 383 105 HOH   HOH A . 
M 5 HOH   84 384 70  HOH   HOH A . 
M 5 HOH   85 385 74  HOH   HOH A . 
M 5 HOH   86 386 111 HOH   HOH A . 
M 5 HOH   87 387 172 HOH   HOH A . 
M 5 HOH   88 388 193 HOH   HOH A . 
M 5 HOH   89 389 187 HOH   HOH A . 
M 5 HOH   90 390 84  HOH   HOH A . 
M 5 HOH   91 391 170 HOH   HOH A . 
M 5 HOH   92 392 27  HOH   HOH A . 
M 5 HOH   93 393 137 HOH   HOH A . 
M 5 HOH   94 394 150 HOH   HOH A . 
M 5 HOH   95 395 164 HOH   HOH A . 
M 5 HOH   96 396 106 HOH   HOH A . 
M 5 HOH   97 397 129 HOH   HOH A . 
M 5 HOH   98 398 114 HOH   HOH A . 
M 5 HOH   99 399 113 HOH   HOH A . 
N 5 HOH   1  301 145 HOH   HOH B . 
N 5 HOH   2  302 43  HOH   HOH B . 
N 5 HOH   3  303 76  HOH   HOH B . 
N 5 HOH   4  304 99  HOH   HOH B . 
N 5 HOH   5  305 174 HOH   HOH B . 
N 5 HOH   6  306 65  HOH   HOH B . 
N 5 HOH   7  307 46  HOH   HOH B . 
N 5 HOH   8  308 73  HOH   HOH B . 
N 5 HOH   9  309 17  HOH   HOH B . 
N 5 HOH   10 310 13  HOH   HOH B . 
N 5 HOH   11 311 77  HOH   HOH B . 
N 5 HOH   12 312 15  HOH   HOH B . 
N 5 HOH   13 313 31  HOH   HOH B . 
N 5 HOH   14 314 41  HOH   HOH B . 
N 5 HOH   15 315 42  HOH   HOH B . 
N 5 HOH   16 316 57  HOH   HOH B . 
N 5 HOH   17 317 166 HOH   HOH B . 
N 5 HOH   18 318 127 HOH   HOH B . 
N 5 HOH   19 319 149 HOH   HOH B . 
N 5 HOH   20 320 91  HOH   HOH B . 
N 5 HOH   21 321 1   HOH   HOH B . 
N 5 HOH   22 322 90  HOH   HOH B . 
N 5 HOH   23 323 87  HOH   HOH B . 
N 5 HOH   24 324 63  HOH   HOH B . 
N 5 HOH   25 325 9   HOH   HOH B . 
N 5 HOH   26 326 197 HOH   HOH B . 
N 5 HOH   27 327 183 HOH   HOH B . 
N 5 HOH   28 328 195 HOH   HOH B . 
N 5 HOH   29 329 133 HOH   HOH B . 
N 5 HOH   30 330 35  HOH   HOH B . 
N 5 HOH   31 331 123 HOH   HOH B . 
N 5 HOH   32 332 30  HOH   HOH B . 
N 5 HOH   33 333 4   HOH   HOH B . 
N 5 HOH   34 334 104 HOH   HOH B . 
N 5 HOH   35 335 33  HOH   HOH B . 
N 5 HOH   36 336 182 HOH   HOH B . 
N 5 HOH   37 337 16  HOH   HOH B . 
N 5 HOH   38 338 61  HOH   HOH B . 
N 5 HOH   39 339 23  HOH   HOH B . 
N 5 HOH   40 340 62  HOH   HOH B . 
N 5 HOH   41 341 142 HOH   HOH B . 
N 5 HOH   42 342 59  HOH   HOH B . 
N 5 HOH   43 343 159 HOH   HOH B . 
N 5 HOH   44 344 3   HOH   HOH B . 
N 5 HOH   45 345 158 HOH   HOH B . 
N 5 HOH   46 346 82  HOH   HOH B . 
N 5 HOH   47 347 38  HOH   HOH B . 
N 5 HOH   48 348 75  HOH   HOH B . 
N 5 HOH   49 349 132 HOH   HOH B . 
N 5 HOH   50 350 209 HOH   HOH B . 
N 5 HOH   51 351 117 HOH   HOH B . 
N 5 HOH   52 352 50  HOH   HOH B . 
N 5 HOH   53 353 71  HOH   HOH B . 
N 5 HOH   54 354 12  HOH   HOH B . 
N 5 HOH   55 355 53  HOH   HOH B . 
N 5 HOH   56 356 175 HOH   HOH B . 
N 5 HOH   57 357 19  HOH   HOH B . 
N 5 HOH   58 358 107 HOH   HOH B . 
N 5 HOH   59 359 54  HOH   HOH B . 
N 5 HOH   60 360 165 HOH   HOH B . 
N 5 HOH   61 361 34  HOH   HOH B . 
N 5 HOH   62 362 151 HOH   HOH B . 
N 5 HOH   63 363 95  HOH   HOH B . 
N 5 HOH   64 364 92  HOH   HOH B . 
N 5 HOH   65 365 52  HOH   HOH B . 
N 5 HOH   66 366 115 HOH   HOH B . 
N 5 HOH   67 367 154 HOH   HOH B . 
N 5 HOH   68 368 210 HOH   HOH B . 
N 5 HOH   69 369 85  HOH   HOH B . 
N 5 HOH   70 370 169 HOH   HOH B . 
N 5 HOH   71 371 140 HOH   HOH B . 
N 5 HOH   72 372 122 HOH   HOH B . 
N 5 HOH   73 373 203 HOH   HOH B . 
N 5 HOH   74 374 208 HOH   HOH B . 
N 5 HOH   75 375 199 HOH   HOH B . 
N 5 HOH   76 376 49  HOH   HOH B . 
N 5 HOH   77 377 173 HOH   HOH B . 
N 5 HOH   78 378 109 HOH   HOH B . 
N 5 HOH   79 379 179 HOH   HOH B . 
N 5 HOH   80 380 152 HOH   HOH B . 
N 5 HOH   81 381 101 HOH   HOH B . 
N 5 HOH   82 382 128 HOH   HOH B . 
N 5 HOH   83 383 119 HOH   HOH B . 
N 5 HOH   84 384 68  HOH   HOH B . 
N 5 HOH   85 385 139 HOH   HOH B . 
N 5 HOH   86 386 78  HOH   HOH B . 
N 5 HOH   87 387 100 HOH   HOH B . 
N 5 HOH   88 388 201 HOH   HOH B . 
N 5 HOH   89 389 196 HOH   HOH B . 
N 5 HOH   90 390 125 HOH   HOH B . 
N 5 HOH   91 391 190 HOH   HOH B . 
N 5 HOH   92 392 94  HOH   HOH B . 
N 5 HOH   93 393 26  HOH   HOH B . 
N 5 HOH   94 394 143 HOH   HOH B . 
N 5 HOH   95 395 98  HOH   HOH B . 
N 5 HOH   96 396 160 HOH   HOH B . 
N 5 HOH   97 397 108 HOH   HOH B . 
N 5 HOH   98 398 136 HOH   HOH B . 
N 5 HOH   99 399 126 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 74  ? CG  ? A GLU 74  CG  
2  1 Y 1 A GLU 74  ? CD  ? A GLU 74  CD  
3  1 Y 1 A GLU 74  ? OE1 ? A GLU 74  OE1 
4  1 Y 1 A GLU 74  ? OE2 ? A GLU 74  OE2 
5  1 Y 1 A ARG 119 ? CG  ? A ARG 119 CG  
6  1 Y 1 A ARG 119 ? CD  ? A ARG 119 CD  
7  1 Y 1 A ARG 119 ? NE  ? A ARG 119 NE  
8  1 Y 1 A ARG 119 ? CZ  ? A ARG 119 CZ  
9  1 Y 1 A ARG 119 ? NH1 ? A ARG 119 NH1 
10 1 Y 1 A ARG 119 ? NH2 ? A ARG 119 NH2 
11 1 Y 1 B GLU 74  ? CG  ? B GLU 74  CG  
12 1 Y 1 B GLU 74  ? CD  ? B GLU 74  CD  
13 1 Y 1 B GLU 74  ? OE1 ? B GLU 74  OE1 
14 1 Y 1 B GLU 74  ? OE2 ? B GLU 74  OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IM9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     121.384 
_cell.length_a_esd                 ? 
_cell.length_b                     121.402 
_cell.length_b_esd                 ? 
_cell.length_c                     160.533 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        32 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9IM9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                22 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'F 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9IM9 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             4.93 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          75.04 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M (NH4)2OAc, 1.9 M (NH4)2SO4, 4% isopropanol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-04-05 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97954 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97954 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9IM9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.81 
_reflns.d_resolution_low                               48.46 
_reflns.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.number_all                                     ? 
_reflns.number_obs                                     53676 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.73 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          23.32 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.07398 
_reflns.pdbx_Rpim_I_all                                0.02035 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1.000 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.07107 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.81 
_reflns_shell.d_res_low                                     1.875 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.71 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5172 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               12.8 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.6367 
_reflns_shell.pdbx_Rpim_I_all                               0.1767 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.931 
_reflns_shell.pdbx_CC_star                                  0.982 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.79 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.6112 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.34 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.44 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.78 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               24.761 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9IM9 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.81 
_refine.ls_d_res_low                             48.46 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     50967 
_refine.ls_number_reflns_R_free                  2709 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.69 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18100 
_refine.ls_R_factor_R_free                       0.20092 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17993 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      9IKU 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.078 
_refine.pdbx_overall_ESU_R_Free                  0.079 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             1.681 
_refine.overall_SU_ML                            0.052 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.81 
_refine_hist.d_res_low                        48.46 
_refine_hist.number_atoms_solvent             198 
_refine_hist.number_atoms_total               2296 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2098 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.012  0.012  2141 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1971 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.084  1.839  2903 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.739  1.774  4555 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.513  5.000  246  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.493 5.000  11   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.403 10.000 369  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.148  0.200  315  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  2395 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  473  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.411  2.283  990  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.410  2.282  990  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.352  4.087  1234 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.352  4.091  1235 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.326  2.908  1151 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.324  2.910  1152 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.491  5.137  1664 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.902  23.73  2427 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.825  23.21  2374 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.810 
_refine_ls_shell.d_res_low                        1.857 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             193 
_refine_ls_shell.number_reflns_R_work             3624 
_refine_ls_shell.percent_reflns_obs               96.88 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.284 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.301 
# 
_struct.entry_id                     9IM9 
_struct.title                        'CTB10-M4-(S)-1d complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9IM9 
_struct_keywords.text            'artificial photoenzyme, BIOSYNTHETIC PROTEIN' 
_struct_keywords.pdbx_keywords   'BIOSYNTHETIC 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 ? 
E N N 3 ? 
F N N 4 ? 
G N N 3 ? 
H N N 3 ? 
I N N 2 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A977K7H6_9PEZI 
_struct_ref.pdbx_db_accession          A0A977K7H6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MGSIGEPNRLLCWSIYVTKKPDQSEEDHHNHVSKVNAPMMIPFLKKYGIVRYTVKHNDAYSKPKQAALMAGQPEENVLAY
DTVFEMIVKDIESIQTMQKDEEFLRTTIPDHFNFADMTRSKGSLTWIEEFTF
;
_struct_ref.pdbx_align_begin           1 
# 
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 9IM9 A 1 ? 132 ? A0A977K7H6 1 ? 132 ? 1 132 
2 1 9IM9 B 1 ? 132 ? A0A977K7H6 1 ? 132 ? 1 132 
# 
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 9IM9 PBF A 13  ? UNP A0A977K7H6 TRP 13  'engineered mutation' 13  1  
1 9IM9 ALA A 107 ? UNP A0A977K7H6 THR 107 'engineered mutation' 107 2  
1 9IM9 LEU A 111 ? UNP A0A977K7H6 HIS 111 'engineered mutation' 111 3  
1 9IM9 THR A 120 ? UNP A0A977K7H6 SER 120 'engineered mutation' 120 4  
1 9IM9 GLY A 124 ? UNP A0A977K7H6 LEU 124 'engineered mutation' 124 5  
1 9IM9 ALA A 133 ? UNP A0A977K7H6 ?   ?   'expression tag'      133 6  
1 9IM9 LEU A 134 ? UNP A0A977K7H6 ?   ?   'expression tag'      134 7  
1 9IM9 GLU A 135 ? UNP A0A977K7H6 ?   ?   'expression tag'      135 8  
1 9IM9 HIS A 136 ? UNP A0A977K7H6 ?   ?   'expression tag'      136 9  
1 9IM9 HIS A 137 ? UNP A0A977K7H6 ?   ?   'expression tag'      137 10 
1 9IM9 HIS A 138 ? UNP A0A977K7H6 ?   ?   'expression tag'      138 11 
1 9IM9 HIS A 139 ? UNP A0A977K7H6 ?   ?   'expression tag'      139 12 
1 9IM9 HIS A 140 ? UNP A0A977K7H6 ?   ?   'expression tag'      140 13 
1 9IM9 HIS A 141 ? UNP A0A977K7H6 ?   ?   'expression tag'      141 14 
2 9IM9 PBF B 13  ? UNP A0A977K7H6 TRP 13  'engineered mutation' 13  15 
2 9IM9 ALA B 107 ? UNP A0A977K7H6 THR 107 'engineered mutation' 107 16 
2 9IM9 LEU B 111 ? UNP A0A977K7H6 HIS 111 'engineered mutation' 111 17 
2 9IM9 THR B 120 ? UNP A0A977K7H6 SER 120 'engineered mutation' 120 18 
2 9IM9 GLY B 124 ? UNP A0A977K7H6 LEU 124 'engineered mutation' 124 19 
2 9IM9 ALA B 133 ? UNP A0A977K7H6 ?   ?   'expression tag'      133 20 
2 9IM9 LEU B 134 ? UNP A0A977K7H6 ?   ?   'expression tag'      134 21 
2 9IM9 GLU B 135 ? UNP A0A977K7H6 ?   ?   'expression tag'      135 22 
2 9IM9 HIS B 136 ? UNP A0A977K7H6 ?   ?   'expression tag'      136 23 
2 9IM9 HIS B 137 ? UNP A0A977K7H6 ?   ?   'expression tag'      137 24 
2 9IM9 HIS B 138 ? UNP A0A977K7H6 ?   ?   'expression tag'      138 25 
2 9IM9 HIS B 139 ? UNP A0A977K7H6 ?   ?   'expression tag'      139 26 
2 9IM9 HIS B 140 ? UNP A0A977K7H6 ?   ?   'expression tag'      140 27 
2 9IM9 HIS B 141 ? UNP A0A977K7H6 ?   ?   'expression tag'      141 28 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6430  ? 
1 MORE         -75   ? 
1 'SSA (A^2)'  11350 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   homology 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 24  ? VAL A 35  ? SER A 24  VAL A 35  1 ? 12 
HELX_P HELX_P2  AA2 VAL A 35  ? TYR A 47  ? VAL A 35  TYR A 47  1 ? 13 
HELX_P HELX_P3  AA3 SER A 61  ? MET A 69  ? SER A 61  MET A 69  1 ? 9  
HELX_P HELX_P4  AA4 PRO A 73  ? VAL A 77  ? PRO A 73  VAL A 77  5 ? 5  
HELX_P HELX_P5  AA5 ASP A 90  ? ASP A 100 ? ASP A 90  ASP A 100 1 ? 11 
HELX_P HELX_P6  AA6 ASP A 100 ? ARG A 105 ? ASP A 100 ARG A 105 1 ? 6  
HELX_P HELX_P7  AA7 THR A 106 ? PHE A 112 ? THR A 106 PHE A 112 1 ? 7  
HELX_P HELX_P8  AA8 SER B 24  ? VAL B 35  ? SER B 24  VAL B 35  1 ? 12 
HELX_P HELX_P9  AA9 VAL B 35  ? TYR B 47  ? VAL B 35  TYR B 47  1 ? 13 
HELX_P HELX_P10 AB1 SER B 61  ? MET B 69  ? SER B 61  MET B 69  1 ? 9  
HELX_P HELX_P11 AB2 PRO B 73  ? VAL B 77  ? PRO B 73  VAL B 77  5 ? 5  
HELX_P HELX_P12 AB3 ASP B 90  ? ASP B 100 ? ASP B 90  ASP B 100 1 ? 11 
HELX_P HELX_P13 AB4 ASP B 100 ? ARG B 105 ? ASP B 100 ARG B 105 1 ? 6  
HELX_P HELX_P14 AB5 THR B 106 ? PHE B 112 ? THR B 106 PHE B 112 1 ? 7  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A CYS 12 C ? ? ? 1_555 A PBF 13 N ? ? A CYS 12 A PBF 13 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale2 covale both ? A PBF 13 C ? ? ? 1_555 A SER 14 N ? ? A PBF 13 A SER 14 1_555 ? ? ? ? ? ? ? 1.324 ? ? 
covale3 covale both ? B CYS 12 C ? ? ? 1_555 B PBF 13 N ? ? B CYS 12 B PBF 13 1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale4 covale both ? B PBF 13 C ? ? ? 1_555 B SER 14 N ? ? B PBF 13 B SER 14 1_555 ? ? ? ? ? ? ? 1.321 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 PBF A 13 ? . . . . PBF A 13 ? 1_555 . . . . . . . PHE 1 PBF Benzoylation 'Named protein modification' 
2 PBF B 13 ? . . . . PBF B 13 ? 1_555 . . . . . . . PHE 1 PBF Benzoylation 'Named protein modification' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   9 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA1 8 9 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? VAL A 17  ? LEU A 10  VAL A 17  
AA1 2 THR A 82  ? VAL A 88  ? THR A 82  VAL A 88  
AA1 3 ARG A 51  ? HIS A 56  ? ARG A 51  HIS A 56  
AA1 4 LYS B 121 ? THR B 131 ? LYS B 121 THR B 131 
AA1 5 LEU B 10  ? VAL B 17  ? LEU B 10  VAL B 17  
AA1 6 THR B 82  ? VAL B 88  ? THR B 82  VAL B 88  
AA1 7 ARG B 51  ? HIS B 56  ? ARG B 51  HIS B 56  
AA1 8 LYS A 121 ? THR A 131 ? LYS A 121 THR A 131 
AA1 9 LEU A 10  ? VAL A 17  ? LEU A 10  VAL A 17  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 17  ? N VAL A 17  O THR A 82  ? O THR A 82  
AA1 2 3 O VAL A 83  ? O VAL A 83  N LYS A 55  ? N LYS A 55  
AA1 3 4 N HIS A 56  ? N HIS A 56  O TRP B 126 ? O TRP B 126 
AA1 4 5 O LYS B 121 ? O LYS B 121 N TYR B 16  ? N TYR B 16  
AA1 5 6 N LEU B 11  ? N LEU B 11  O VAL B 88  ? O VAL B 88  
AA1 6 7 O VAL B 83  ? O VAL B 83  N LYS B 55  ? N LYS B 55  
AA1 7 8 O HIS B 56  ? O HIS B 56  N TRP A 126 ? N TRP A 126 
AA1 8 9 O LYS A 121 ? O LYS A 121 N TYR A 16  ? N TYR A 16  
# 
_pdbx_entry_details.entry_id                   9IM9 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 THR A 106 ? ? -127.36 -72.99 
2 1 PHE A 114 ? ? -143.95 -18.81 
3 1 ASP B 22  ? ? 71.79   -5.99  
4 1 THR B 106 ? ? -127.53 -73.16 
5 1 PHE B 114 ? ? -145.47 -18.56 
# 
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 GLY 2   ? A GLY 2   
3  1 Y 1 A SER 3   ? A SER 3   
4  1 Y 1 A ILE 4   ? A ILE 4   
5  1 Y 1 A GLY 5   ? A GLY 5   
6  1 Y 1 A GLU 6   ? A GLU 6   
7  1 Y 1 A PRO 7   ? A PRO 7   
8  1 Y 1 A ASN 8   ? A ASN 8   
9  1 Y 1 A ALA 133 ? A ALA 133 
10 1 Y 1 A LEU 134 ? A LEU 134 
11 1 Y 1 A GLU 135 ? A GLU 135 
12 1 Y 1 A HIS 136 ? A HIS 136 
13 1 Y 1 A HIS 137 ? A HIS 137 
14 1 Y 1 A HIS 138 ? A HIS 138 
15 1 Y 1 A HIS 139 ? A HIS 139 
16 1 Y 1 A HIS 140 ? A HIS 140 
17 1 Y 1 A HIS 141 ? A HIS 141 
18 1 Y 1 B MET 1   ? B MET 1   
19 1 Y 1 B GLY 2   ? B GLY 2   
20 1 Y 1 B SER 3   ? B SER 3   
21 1 Y 1 B ILE 4   ? B ILE 4   
22 1 Y 1 B GLY 5   ? B GLY 5   
23 1 Y 1 B GLU 6   ? B GLU 6   
24 1 Y 1 B PRO 7   ? B PRO 7   
25 1 Y 1 B ASN 8   ? B ASN 8   
26 1 Y 1 B ALA 133 ? B ALA 133 
27 1 Y 1 B LEU 134 ? B LEU 134 
28 1 Y 1 B GLU 135 ? B GLU 135 
29 1 Y 1 B HIS 136 ? B HIS 136 
30 1 Y 1 B HIS 137 ? B HIS 137 
31 1 Y 1 B HIS 138 ? B HIS 138 
32 1 Y 1 B HIS 139 ? B HIS 139 
33 1 Y 1 B HIS 140 ? B HIS 140 
34 1 Y 1 B HIS 141 ? B HIS 141 
# 
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 
A1D9Q C2   C  Y N 1   
A1D9Q C4   C  Y N 2   
A1D9Q C5   C  Y N 3   
A1D9Q C6   C  N N 4   
A1D9Q N1   N  N N 5   
A1D9Q C1   C  N N 6   
A1D9Q C3   C  Y N 7   
A1D9Q O1   O  N N 8   
A1D9Q C7   C  N S 9   
A1D9Q C8   C  N N 10  
A1D9Q C9   C  N N 11  
A1D9Q CL1  CL N N 12  
A1D9Q CL2  CL N N 13  
A1D9Q C10  C  Y N 14  
A1D9Q C11  C  Y N 15  
A1D9Q H1   H  N N 16  
A1D9Q H2   H  N N 17  
A1D9Q H3   H  N N 18  
A1D9Q H4   H  N N 19  
A1D9Q H5   H  N N 20  
A1D9Q H6   H  N N 21  
A1D9Q H7   H  N N 22  
A1D9Q H8   H  N N 23  
A1D9Q H9   H  N N 24  
ALA   N    N  N N 25  
ALA   CA   C  N S 26  
ALA   C    C  N N 27  
ALA   O    O  N N 28  
ALA   CB   C  N N 29  
ALA   OXT  O  N N 30  
ALA   H    H  N N 31  
ALA   H2   H  N N 32  
ALA   HA   H  N N 33  
ALA   HB1  H  N N 34  
ALA   HB2  H  N N 35  
ALA   HB3  H  N N 36  
ALA   HXT  H  N N 37  
ARG   N    N  N N 38  
ARG   CA   C  N S 39  
ARG   C    C  N N 40  
ARG   O    O  N N 41  
ARG   CB   C  N N 42  
ARG   CG   C  N N 43  
ARG   CD   C  N N 44  
ARG   NE   N  N N 45  
ARG   CZ   C  N N 46  
ARG   NH1  N  N N 47  
ARG   NH2  N  N N 48  
ARG   OXT  O  N N 49  
ARG   H    H  N N 50  
ARG   H2   H  N N 51  
ARG   HA   H  N N 52  
ARG   HB2  H  N N 53  
ARG   HB3  H  N N 54  
ARG   HG2  H  N N 55  
ARG   HG3  H  N N 56  
ARG   HD2  H  N N 57  
ARG   HD3  H  N N 58  
ARG   HE   H  N N 59  
ARG   HH11 H  N N 60  
ARG   HH12 H  N N 61  
ARG   HH21 H  N N 62  
ARG   HH22 H  N N 63  
ARG   HXT  H  N N 64  
ASN   N    N  N N 65  
ASN   CA   C  N S 66  
ASN   C    C  N N 67  
ASN   O    O  N N 68  
ASN   CB   C  N N 69  
ASN   CG   C  N N 70  
ASN   OD1  O  N N 71  
ASN   ND2  N  N N 72  
ASN   OXT  O  N N 73  
ASN   H    H  N N 74  
ASN   H2   H  N N 75  
ASN   HA   H  N N 76  
ASN   HB2  H  N N 77  
ASN   HB3  H  N N 78  
ASN   HD21 H  N N 79  
ASN   HD22 H  N N 80  
ASN   HXT  H  N N 81  
ASP   N    N  N N 82  
ASP   CA   C  N S 83  
ASP   C    C  N N 84  
ASP   O    O  N N 85  
ASP   CB   C  N N 86  
ASP   CG   C  N N 87  
ASP   OD1  O  N N 88  
ASP   OD2  O  N N 89  
ASP   OXT  O  N N 90  
ASP   H    H  N N 91  
ASP   H2   H  N N 92  
ASP   HA   H  N N 93  
ASP   HB2  H  N N 94  
ASP   HB3  H  N N 95  
ASP   HD2  H  N N 96  
ASP   HXT  H  N N 97  
CYS   N    N  N N 98  
CYS   CA   C  N R 99  
CYS   C    C  N N 100 
CYS   O    O  N N 101 
CYS   CB   C  N N 102 
CYS   SG   S  N N 103 
CYS   OXT  O  N N 104 
CYS   H    H  N N 105 
CYS   H2   H  N N 106 
CYS   HA   H  N N 107 
CYS   HB2  H  N N 108 
CYS   HB3  H  N N 109 
CYS   HG   H  N N 110 
CYS   HXT  H  N N 111 
GLN   N    N  N N 112 
GLN   CA   C  N S 113 
GLN   C    C  N N 114 
GLN   O    O  N N 115 
GLN   CB   C  N N 116 
GLN   CG   C  N N 117 
GLN   CD   C  N N 118 
GLN   OE1  O  N N 119 
GLN   NE2  N  N N 120 
GLN   OXT  O  N N 121 
GLN   H    H  N N 122 
GLN   H2   H  N N 123 
GLN   HA   H  N N 124 
GLN   HB2  H  N N 125 
GLN   HB3  H  N N 126 
GLN   HG2  H  N N 127 
GLN   HG3  H  N N 128 
GLN   HE21 H  N N 129 
GLN   HE22 H  N N 130 
GLN   HXT  H  N N 131 
GLU   N    N  N N 132 
GLU   CA   C  N S 133 
GLU   C    C  N N 134 
GLU   O    O  N N 135 
GLU   CB   C  N N 136 
GLU   CG   C  N N 137 
GLU   CD   C  N N 138 
GLU   OE1  O  N N 139 
GLU   OE2  O  N N 140 
GLU   OXT  O  N N 141 
GLU   H    H  N N 142 
GLU   H2   H  N N 143 
GLU   HA   H  N N 144 
GLU   HB2  H  N N 145 
GLU   HB3  H  N N 146 
GLU   HG2  H  N N 147 
GLU   HG3  H  N N 148 
GLU   HE2  H  N N 149 
GLU   HXT  H  N N 150 
GLY   N    N  N N 151 
GLY   CA   C  N N 152 
GLY   C    C  N N 153 
GLY   O    O  N N 154 
GLY   OXT  O  N N 155 
GLY   H    H  N N 156 
GLY   H2   H  N N 157 
GLY   HA2  H  N N 158 
GLY   HA3  H  N N 159 
GLY   HXT  H  N N 160 
GOL   C1   C  N N 161 
GOL   O1   O  N N 162 
GOL   C2   C  N N 163 
GOL   O2   O  N N 164 
GOL   C3   C  N N 165 
GOL   O3   O  N N 166 
GOL   H11  H  N N 167 
GOL   H12  H  N N 168 
GOL   HO1  H  N N 169 
GOL   H2   H  N N 170 
GOL   HO2  H  N N 171 
GOL   H31  H  N N 172 
GOL   H32  H  N N 173 
GOL   HO3  H  N N 174 
HIS   N    N  N N 175 
HIS   CA   C  N S 176 
HIS   C    C  N N 177 
HIS   O    O  N N 178 
HIS   CB   C  N N 179 
HIS   CG   C  Y N 180 
HIS   ND1  N  Y N 181 
HIS   CD2  C  Y N 182 
HIS   CE1  C  Y N 183 
HIS   NE2  N  Y N 184 
HIS   OXT  O  N N 185 
HIS   H    H  N N 186 
HIS   H2   H  N N 187 
HIS   HA   H  N N 188 
HIS   HB2  H  N N 189 
HIS   HB3  H  N N 190 
HIS   HD1  H  N N 191 
HIS   HD2  H  N N 192 
HIS   HE1  H  N N 193 
HIS   HE2  H  N N 194 
HIS   HXT  H  N N 195 
HOH   O    O  N N 196 
HOH   H1   H  N N 197 
HOH   H2   H  N N 198 
ILE   N    N  N N 199 
ILE   CA   C  N S 200 
ILE   C    C  N N 201 
ILE   O    O  N N 202 
ILE   CB   C  N S 203 
ILE   CG1  C  N N 204 
ILE   CG2  C  N N 205 
ILE   CD1  C  N N 206 
ILE   OXT  O  N N 207 
ILE   H    H  N N 208 
ILE   H2   H  N N 209 
ILE   HA   H  N N 210 
ILE   HB   H  N N 211 
ILE   HG12 H  N N 212 
ILE   HG13 H  N N 213 
ILE   HG21 H  N N 214 
ILE   HG22 H  N N 215 
ILE   HG23 H  N N 216 
ILE   HD11 H  N N 217 
ILE   HD12 H  N N 218 
ILE   HD13 H  N N 219 
ILE   HXT  H  N N 220 
LEU   N    N  N N 221 
LEU   CA   C  N S 222 
LEU   C    C  N N 223 
LEU   O    O  N N 224 
LEU   CB   C  N N 225 
LEU   CG   C  N N 226 
LEU   CD1  C  N N 227 
LEU   CD2  C  N N 228 
LEU   OXT  O  N N 229 
LEU   H    H  N N 230 
LEU   H2   H  N N 231 
LEU   HA   H  N N 232 
LEU   HB2  H  N N 233 
LEU   HB3  H  N N 234 
LEU   HG   H  N N 235 
LEU   HD11 H  N N 236 
LEU   HD12 H  N N 237 
LEU   HD13 H  N N 238 
LEU   HD21 H  N N 239 
LEU   HD22 H  N N 240 
LEU   HD23 H  N N 241 
LEU   HXT  H  N N 242 
LYS   N    N  N N 243 
LYS   CA   C  N S 244 
LYS   C    C  N N 245 
LYS   O    O  N N 246 
LYS   CB   C  N N 247 
LYS   CG   C  N N 248 
LYS   CD   C  N N 249 
LYS   CE   C  N N 250 
LYS   NZ   N  N N 251 
LYS   OXT  O  N N 252 
LYS   H    H  N N 253 
LYS   H2   H  N N 254 
LYS   HA   H  N N 255 
LYS   HB2  H  N N 256 
LYS   HB3  H  N N 257 
LYS   HG2  H  N N 258 
LYS   HG3  H  N N 259 
LYS   HD2  H  N N 260 
LYS   HD3  H  N N 261 
LYS   HE2  H  N N 262 
LYS   HE3  H  N N 263 
LYS   HZ1  H  N N 264 
LYS   HZ2  H  N N 265 
LYS   HZ3  H  N N 266 
LYS   HXT  H  N N 267 
MET   N    N  N N 268 
MET   CA   C  N S 269 
MET   C    C  N N 270 
MET   O    O  N N 271 
MET   CB   C  N N 272 
MET   CG   C  N N 273 
MET   SD   S  N N 274 
MET   CE   C  N N 275 
MET   OXT  O  N N 276 
MET   H    H  N N 277 
MET   H2   H  N N 278 
MET   HA   H  N N 279 
MET   HB2  H  N N 280 
MET   HB3  H  N N 281 
MET   HG2  H  N N 282 
MET   HG3  H  N N 283 
MET   HE1  H  N N 284 
MET   HE2  H  N N 285 
MET   HE3  H  N N 286 
MET   HXT  H  N N 287 
PBF   N    N  N N 288 
PBF   C    C  N N 289 
PBF   O    O  N N 290 
PBF   CA   C  N S 291 
PBF   CB   C  N N 292 
PBF   CG   C  Y N 293 
PBF   CD1  C  Y N 294 
PBF   CD2  C  Y N 295 
PBF   CE1  C  Y N 296 
PBF   CE2  C  Y N 297 
PBF   CZ   C  Y N 298 
PBF   CN1  C  N N 299 
PBF   ON2  O  N N 300 
PBF   CT   C  Y N 301 
PBF   CI1  C  Y N 302 
PBF   CI2  C  Y N 303 
PBF   CK1  C  Y N 304 
PBF   CK2  C  Y N 305 
PBF   CL   C  Y N 306 
PBF   OXT  O  N N 307 
PBF   H    H  N N 308 
PBF   H2   H  N N 309 
PBF   HA   H  N N 310 
PBF   HB2  H  N N 311 
PBF   HB3  H  N N 312 
PBF   HD1  H  N N 313 
PBF   HD2  H  N N 314 
PBF   HE1  H  N N 315 
PBF   HE2  H  N N 316 
PBF   HI1  H  N N 317 
PBF   HI2  H  N N 318 
PBF   HK1  H  N N 319 
PBF   HK2  H  N N 320 
PBF   HCL  H  N N 321 
PBF   HXT  H  N N 322 
PHE   N    N  N N 323 
PHE   CA   C  N S 324 
PHE   C    C  N N 325 
PHE   O    O  N N 326 
PHE   CB   C  N N 327 
PHE   CG   C  Y N 328 
PHE   CD1  C  Y N 329 
PHE   CD2  C  Y N 330 
PHE   CE1  C  Y N 331 
PHE   CE2  C  Y N 332 
PHE   CZ   C  Y N 333 
PHE   OXT  O  N N 334 
PHE   H    H  N N 335 
PHE   H2   H  N N 336 
PHE   HA   H  N N 337 
PHE   HB2  H  N N 338 
PHE   HB3  H  N N 339 
PHE   HD1  H  N N 340 
PHE   HD2  H  N N 341 
PHE   HE1  H  N N 342 
PHE   HE2  H  N N 343 
PHE   HZ   H  N N 344 
PHE   HXT  H  N N 345 
PRO   N    N  N N 346 
PRO   CA   C  N S 347 
PRO   C    C  N N 348 
PRO   O    O  N N 349 
PRO   CB   C  N N 350 
PRO   CG   C  N N 351 
PRO   CD   C  N N 352 
PRO   OXT  O  N N 353 
PRO   H    H  N N 354 
PRO   HA   H  N N 355 
PRO   HB2  H  N N 356 
PRO   HB3  H  N N 357 
PRO   HG2  H  N N 358 
PRO   HG3  H  N N 359 
PRO   HD2  H  N N 360 
PRO   HD3  H  N N 361 
PRO   HXT  H  N N 362 
SER   N    N  N N 363 
SER   CA   C  N S 364 
SER   C    C  N N 365 
SER   O    O  N N 366 
SER   CB   C  N N 367 
SER   OG   O  N N 368 
SER   OXT  O  N N 369 
SER   H    H  N N 370 
SER   H2   H  N N 371 
SER   HA   H  N N 372 
SER   HB2  H  N N 373 
SER   HB3  H  N N 374 
SER   HG   H  N N 375 
SER   HXT  H  N N 376 
SO4   S    S  N N 377 
SO4   O1   O  N N 378 
SO4   O2   O  N N 379 
SO4   O3   O  N N 380 
SO4   O4   O  N N 381 
THR   N    N  N N 382 
THR   CA   C  N S 383 
THR   C    C  N N 384 
THR   O    O  N N 385 
THR   CB   C  N R 386 
THR   OG1  O  N N 387 
THR   CG2  C  N N 388 
THR   OXT  O  N N 389 
THR   H    H  N N 390 
THR   H2   H  N N 391 
THR   HA   H  N N 392 
THR   HB   H  N N 393 
THR   HG1  H  N N 394 
THR   HG21 H  N N 395 
THR   HG22 H  N N 396 
THR   HG23 H  N N 397 
THR   HXT  H  N N 398 
TRP   N    N  N N 399 
TRP   CA   C  N S 400 
TRP   C    C  N N 401 
TRP   O    O  N N 402 
TRP   CB   C  N N 403 
TRP   CG   C  Y N 404 
TRP   CD1  C  Y N 405 
TRP   CD2  C  Y N 406 
TRP   NE1  N  Y N 407 
TRP   CE2  C  Y N 408 
TRP   CE3  C  Y N 409 
TRP   CZ2  C  Y N 410 
TRP   CZ3  C  Y N 411 
TRP   CH2  C  Y N 412 
TRP   OXT  O  N N 413 
TRP   H    H  N N 414 
TRP   H2   H  N N 415 
TRP   HA   H  N N 416 
TRP   HB2  H  N N 417 
TRP   HB3  H  N N 418 
TRP   HD1  H  N N 419 
TRP   HE1  H  N N 420 
TRP   HE3  H  N N 421 
TRP   HZ2  H  N N 422 
TRP   HZ3  H  N N 423 
TRP   HH2  H  N N 424 
TRP   HXT  H  N N 425 
TYR   N    N  N N 426 
TYR   CA   C  N S 427 
TYR   C    C  N N 428 
TYR   O    O  N N 429 
TYR   CB   C  N N 430 
TYR   CG   C  Y N 431 
TYR   CD1  C  Y N 432 
TYR   CD2  C  Y N 433 
TYR   CE1  C  Y N 434 
TYR   CE2  C  Y N 435 
TYR   CZ   C  Y N 436 
TYR   OH   O  N N 437 
TYR   OXT  O  N N 438 
TYR   H    H  N N 439 
TYR   H2   H  N N 440 
TYR   HA   H  N N 441 
TYR   HB2  H  N N 442 
TYR   HB3  H  N N 443 
TYR   HD1  H  N N 444 
TYR   HD2  H  N N 445 
TYR   HE1  H  N N 446 
TYR   HE2  H  N N 447 
TYR   HH   H  N N 448 
TYR   HXT  H  N N 449 
VAL   N    N  N N 450 
VAL   CA   C  N S 451 
VAL   C    C  N N 452 
VAL   O    O  N N 453 
VAL   CB   C  N N 454 
VAL   CG1  C  N N 455 
VAL   CG2  C  N N 456 
VAL   OXT  O  N N 457 
VAL   H    H  N N 458 
VAL   H2   H  N N 459 
VAL   HA   H  N N 460 
VAL   HB   H  N N 461 
VAL   HG11 H  N N 462 
VAL   HG12 H  N N 463 
VAL   HG13 H  N N 464 
VAL   HG21 H  N N 465 
VAL   HG22 H  N N 466 
VAL   HG23 H  N N 467 
VAL   HXT  H  N N 468 
# 
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 
A1D9Q CL2 C9   sing N N 1   
A1D9Q N1  C6   sing N N 2   
A1D9Q N1  C5   sing N N 3   
A1D9Q O1  C6   doub N N 4   
A1D9Q C6  C7   sing N N 5   
A1D9Q C5  C10  doub Y N 6   
A1D9Q C5  C4   sing Y N 7   
A1D9Q C10 C11  sing Y N 8   
A1D9Q C9  C7   sing N N 9   
A1D9Q C9  CL1  sing N N 10  
A1D9Q C9  C8   sing N N 11  
A1D9Q C7  C4   sing N N 12  
A1D9Q C7  C8   sing N N 13  
A1D9Q C4  C3   doub Y N 14  
A1D9Q C11 C2   doub Y N 15  
A1D9Q C3  C2   sing Y N 16  
A1D9Q C2  C1   sing N N 17  
A1D9Q N1  H1   sing N N 18  
A1D9Q C1  H2   sing N N 19  
A1D9Q C1  H3   sing N N 20  
A1D9Q C1  H4   sing N N 21  
A1D9Q C3  H5   sing N N 22  
A1D9Q C8  H6   sing N N 23  
A1D9Q C8  H7   sing N N 24  
A1D9Q C10 H8   sing N N 25  
A1D9Q C11 H9   sing N N 26  
ALA   N   CA   sing N N 27  
ALA   N   H    sing N N 28  
ALA   N   H2   sing N N 29  
ALA   CA  C    sing N N 30  
ALA   CA  CB   sing N N 31  
ALA   CA  HA   sing N N 32  
ALA   C   O    doub N N 33  
ALA   C   OXT  sing N N 34  
ALA   CB  HB1  sing N N 35  
ALA   CB  HB2  sing N N 36  
ALA   CB  HB3  sing N N 37  
ALA   OXT HXT  sing N N 38  
ARG   N   CA   sing N N 39  
ARG   N   H    sing N N 40  
ARG   N   H2   sing N N 41  
ARG   CA  C    sing N N 42  
ARG   CA  CB   sing N N 43  
ARG   CA  HA   sing N N 44  
ARG   C   O    doub N N 45  
ARG   C   OXT  sing N N 46  
ARG   CB  CG   sing N N 47  
ARG   CB  HB2  sing N N 48  
ARG   CB  HB3  sing N N 49  
ARG   CG  CD   sing N N 50  
ARG   CG  HG2  sing N N 51  
ARG   CG  HG3  sing N N 52  
ARG   CD  NE   sing N N 53  
ARG   CD  HD2  sing N N 54  
ARG   CD  HD3  sing N N 55  
ARG   NE  CZ   sing N N 56  
ARG   NE  HE   sing N N 57  
ARG   CZ  NH1  sing N N 58  
ARG   CZ  NH2  doub N N 59  
ARG   NH1 HH11 sing N N 60  
ARG   NH1 HH12 sing N N 61  
ARG   NH2 HH21 sing N N 62  
ARG   NH2 HH22 sing N N 63  
ARG   OXT HXT  sing N N 64  
ASN   N   CA   sing N N 65  
ASN   N   H    sing N N 66  
ASN   N   H2   sing N N 67  
ASN   CA  C    sing N N 68  
ASN   CA  CB   sing N N 69  
ASN   CA  HA   sing N N 70  
ASN   C   O    doub N N 71  
ASN   C   OXT  sing N N 72  
ASN   CB  CG   sing N N 73  
ASN   CB  HB2  sing N N 74  
ASN   CB  HB3  sing N N 75  
ASN   CG  OD1  doub N N 76  
ASN   CG  ND2  sing N N 77  
ASN   ND2 HD21 sing N N 78  
ASN   ND2 HD22 sing N N 79  
ASN   OXT HXT  sing N N 80  
ASP   N   CA   sing N N 81  
ASP   N   H    sing N N 82  
ASP   N   H2   sing N N 83  
ASP   CA  C    sing N N 84  
ASP   CA  CB   sing N N 85  
ASP   CA  HA   sing N N 86  
ASP   C   O    doub N N 87  
ASP   C   OXT  sing N N 88  
ASP   CB  CG   sing N N 89  
ASP   CB  HB2  sing N N 90  
ASP   CB  HB3  sing N N 91  
ASP   CG  OD1  doub N N 92  
ASP   CG  OD2  sing N N 93  
ASP   OD2 HD2  sing N N 94  
ASP   OXT HXT  sing N N 95  
CYS   N   CA   sing N N 96  
CYS   N   H    sing N N 97  
CYS   N   H2   sing N N 98  
CYS   CA  C    sing N N 99  
CYS   CA  CB   sing N N 100 
CYS   CA  HA   sing N N 101 
CYS   C   O    doub N N 102 
CYS   C   OXT  sing N N 103 
CYS   CB  SG   sing N N 104 
CYS   CB  HB2  sing N N 105 
CYS   CB  HB3  sing N N 106 
CYS   SG  HG   sing N N 107 
CYS   OXT HXT  sing N N 108 
GLN   N   CA   sing N N 109 
GLN   N   H    sing N N 110 
GLN   N   H2   sing N N 111 
GLN   CA  C    sing N N 112 
GLN   CA  CB   sing N N 113 
GLN   CA  HA   sing N N 114 
GLN   C   O    doub N N 115 
GLN   C   OXT  sing N N 116 
GLN   CB  CG   sing N N 117 
GLN   CB  HB2  sing N N 118 
GLN   CB  HB3  sing N N 119 
GLN   CG  CD   sing N N 120 
GLN   CG  HG2  sing N N 121 
GLN   CG  HG3  sing N N 122 
GLN   CD  OE1  doub N N 123 
GLN   CD  NE2  sing N N 124 
GLN   NE2 HE21 sing N N 125 
GLN   NE2 HE22 sing N N 126 
GLN   OXT HXT  sing N N 127 
GLU   N   CA   sing N N 128 
GLU   N   H    sing N N 129 
GLU   N   H2   sing N N 130 
GLU   CA  C    sing N N 131 
GLU   CA  CB   sing N N 132 
GLU   CA  HA   sing N N 133 
GLU   C   O    doub N N 134 
GLU   C   OXT  sing N N 135 
GLU   CB  CG   sing N N 136 
GLU   CB  HB2  sing N N 137 
GLU   CB  HB3  sing N N 138 
GLU   CG  CD   sing N N 139 
GLU   CG  HG2  sing N N 140 
GLU   CG  HG3  sing N N 141 
GLU   CD  OE1  doub N N 142 
GLU   CD  OE2  sing N N 143 
GLU   OE2 HE2  sing N N 144 
GLU   OXT HXT  sing N N 145 
GLY   N   CA   sing N N 146 
GLY   N   H    sing N N 147 
GLY   N   H2   sing N N 148 
GLY   CA  C    sing N N 149 
GLY   CA  HA2  sing N N 150 
GLY   CA  HA3  sing N N 151 
GLY   C   O    doub N N 152 
GLY   C   OXT  sing N N 153 
GLY   OXT HXT  sing N N 154 
GOL   C1  O1   sing N N 155 
GOL   C1  C2   sing N N 156 
GOL   C1  H11  sing N N 157 
GOL   C1  H12  sing N N 158 
GOL   O1  HO1  sing N N 159 
GOL   C2  O2   sing N N 160 
GOL   C2  C3   sing N N 161 
GOL   C2  H2   sing N N 162 
GOL   O2  HO2  sing N N 163 
GOL   C3  O3   sing N N 164 
GOL   C3  H31  sing N N 165 
GOL   C3  H32  sing N N 166 
GOL   O3  HO3  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
PBF   N   CA   sing N N 276 
PBF   N   H    sing N N 277 
PBF   N   H2   sing N N 278 
PBF   C   O    doub N N 279 
PBF   C   CA   sing N N 280 
PBF   C   OXT  sing N N 281 
PBF   CA  CB   sing N N 282 
PBF   CA  HA   sing N N 283 
PBF   CB  CG   sing N N 284 
PBF   CB  HB2  sing N N 285 
PBF   CB  HB3  sing N N 286 
PBF   CG  CD1  doub Y N 287 
PBF   CG  CD2  sing Y N 288 
PBF   CD1 CE1  sing Y N 289 
PBF   CD1 HD1  sing N N 290 
PBF   CD2 CE2  doub Y N 291 
PBF   CD2 HD2  sing N N 292 
PBF   CE1 CZ   doub Y N 293 
PBF   CE1 HE1  sing N N 294 
PBF   CE2 CZ   sing Y N 295 
PBF   CE2 HE2  sing N N 296 
PBF   CZ  CN1  sing N N 297 
PBF   CN1 ON2  doub N N 298 
PBF   CN1 CT   sing N N 299 
PBF   CT  CI1  doub Y N 300 
PBF   CT  CI2  sing Y N 301 
PBF   CI1 CK1  sing Y N 302 
PBF   CI1 HI1  sing N N 303 
PBF   CI2 CK2  doub Y N 304 
PBF   CI2 HI2  sing N N 305 
PBF   CK1 CL   doub Y N 306 
PBF   CK1 HK1  sing N N 307 
PBF   CK2 CL   sing Y N 308 
PBF   CK2 HK2  sing N N 309 
PBF   CL  HCL  sing N N 310 
PBF   OXT HXT  sing N N 311 
PHE   N   CA   sing N N 312 
PHE   N   H    sing N N 313 
PHE   N   H2   sing N N 314 
PHE   CA  C    sing N N 315 
PHE   CA  CB   sing N N 316 
PHE   CA  HA   sing N N 317 
PHE   C   O    doub N N 318 
PHE   C   OXT  sing N N 319 
PHE   CB  CG   sing N N 320 
PHE   CB  HB2  sing N N 321 
PHE   CB  HB3  sing N N 322 
PHE   CG  CD1  doub Y N 323 
PHE   CG  CD2  sing Y N 324 
PHE   CD1 CE1  sing Y N 325 
PHE   CD1 HD1  sing N N 326 
PHE   CD2 CE2  doub Y N 327 
PHE   CD2 HD2  sing N N 328 
PHE   CE1 CZ   doub Y N 329 
PHE   CE1 HE1  sing N N 330 
PHE   CE2 CZ   sing Y N 331 
PHE   CE2 HE2  sing N N 332 
PHE   CZ  HZ   sing N N 333 
PHE   OXT HXT  sing N N 334 
PRO   N   CA   sing N N 335 
PRO   N   CD   sing N N 336 
PRO   N   H    sing N N 337 
PRO   CA  C    sing N N 338 
PRO   CA  CB   sing N N 339 
PRO   CA  HA   sing N N 340 
PRO   C   O    doub N N 341 
PRO   C   OXT  sing N N 342 
PRO   CB  CG   sing N N 343 
PRO   CB  HB2  sing N N 344 
PRO   CB  HB3  sing N N 345 
PRO   CG  CD   sing N N 346 
PRO   CG  HG2  sing N N 347 
PRO   CG  HG3  sing N N 348 
PRO   CD  HD2  sing N N 349 
PRO   CD  HD3  sing N N 350 
PRO   OXT HXT  sing N N 351 
SER   N   CA   sing N N 352 
SER   N   H    sing N N 353 
SER   N   H2   sing N N 354 
SER   CA  C    sing N N 355 
SER   CA  CB   sing N N 356 
SER   CA  HA   sing N N 357 
SER   C   O    doub N N 358 
SER   C   OXT  sing N N 359 
SER   CB  OG   sing N N 360 
SER   CB  HB2  sing N N 361 
SER   CB  HB3  sing N N 362 
SER   OG  HG   sing N N 363 
SER   OXT HXT  sing N N 364 
SO4   S   O1   doub N N 365 
SO4   S   O2   doub N N 366 
SO4   S   O3   sing N N 367 
SO4   S   O4   sing N N 368 
THR   N   CA   sing N N 369 
THR   N   H    sing N N 370 
THR   N   H2   sing N N 371 
THR   CA  C    sing N N 372 
THR   CA  CB   sing N N 373 
THR   CA  HA   sing N N 374 
THR   C   O    doub N N 375 
THR   C   OXT  sing N N 376 
THR   CB  OG1  sing N N 377 
THR   CB  CG2  sing N N 378 
THR   CB  HB   sing N N 379 
THR   OG1 HG1  sing N N 380 
THR   CG2 HG21 sing N N 381 
THR   CG2 HG22 sing N N 382 
THR   CG2 HG23 sing N N 383 
THR   OXT HXT  sing N N 384 
TRP   N   CA   sing N N 385 
TRP   N   H    sing N N 386 
TRP   N   H2   sing N N 387 
TRP   CA  C    sing N N 388 
TRP   CA  CB   sing N N 389 
TRP   CA  HA   sing N N 390 
TRP   C   O    doub N N 391 
TRP   C   OXT  sing N N 392 
TRP   CB  CG   sing N N 393 
TRP   CB  HB2  sing N N 394 
TRP   CB  HB3  sing N N 395 
TRP   CG  CD1  doub Y N 396 
TRP   CG  CD2  sing Y N 397 
TRP   CD1 NE1  sing Y N 398 
TRP   CD1 HD1  sing N N 399 
TRP   CD2 CE2  doub Y N 400 
TRP   CD2 CE3  sing Y N 401 
TRP   NE1 CE2  sing Y N 402 
TRP   NE1 HE1  sing N N 403 
TRP   CE2 CZ2  sing Y N 404 
TRP   CE3 CZ3  doub Y N 405 
TRP   CE3 HE3  sing N N 406 
TRP   CZ2 CH2  doub Y N 407 
TRP   CZ2 HZ2  sing N N 408 
TRP   CZ3 CH2  sing Y N 409 
TRP   CZ3 HZ3  sing N N 410 
TRP   CH2 HH2  sing N N 411 
TRP   OXT HXT  sing N N 412 
TYR   N   CA   sing N N 413 
TYR   N   H    sing N N 414 
TYR   N   H2   sing N N 415 
TYR   CA  C    sing N N 416 
TYR   CA  CB   sing N N 417 
TYR   CA  HA   sing N N 418 
TYR   C   O    doub N N 419 
TYR   C   OXT  sing N N 420 
TYR   CB  CG   sing N N 421 
TYR   CB  HB2  sing N N 422 
TYR   CB  HB3  sing N N 423 
TYR   CG  CD1  doub Y N 424 
TYR   CG  CD2  sing Y N 425 
TYR   CD1 CE1  sing Y N 426 
TYR   CD1 HD1  sing N N 427 
TYR   CD2 CE2  doub Y N 428 
TYR   CD2 HD2  sing N N 429 
TYR   CE1 CZ   doub Y N 430 
TYR   CE1 HE1  sing N N 431 
TYR   CE2 CZ   sing Y N 432 
TYR   CE2 HE2  sing N N 433 
TYR   CZ  OH   sing N N 434 
TYR   OH  HH   sing N N 435 
TYR   OXT HXT  sing N N 436 
VAL   N   CA   sing N N 437 
VAL   N   H    sing N N 438 
VAL   N   H2   sing N N 439 
VAL   CA  C    sing N N 440 
VAL   CA  CB   sing N N 441 
VAL   CA  HA   sing N N 442 
VAL   C   O    doub N N 443 
VAL   C   OXT  sing N N 444 
VAL   CB  CG1  sing N N 445 
VAL   CB  CG2  sing N N 446 
VAL   CB  HB   sing N N 447 
VAL   CG1 HG11 sing N N 448 
VAL   CG1 HG12 sing N N 449 
VAL   CG1 HG13 sing N N 450 
VAL   CG2 HG21 sing N N 451 
VAL   CG2 HG22 sing N N 452 
VAL   CG2 HG23 sing N N 453 
VAL   OXT HXT  sing N N 454 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Other private' China 2021YFC2102700 1 
'Other private' China BK20202002     2 
'Other private' China KYCX20_1812    3 
'Other private' China KYCX20_1816    4 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   9IKU 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9IM9 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.008238 
_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]   0.008237 
_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]   0.006229 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
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   . ARG   A 1 9   ? 11.421  31.274 7.465  1.00 35.40 ? 9   ARG   A N   1 
ATOM   2    C  CA  . ARG   A 1 9   ? 11.562  29.972 8.186  1.00 30.43 ? 9   ARG   A CA  1 
ATOM   3    C  C   . ARG   A 1 9   ? 12.109  30.223 9.584  1.00 28.15 ? 9   ARG   A C   1 
ATOM   4    O  O   . ARG   A 1 9   ? 13.163  30.837 9.748  1.00 31.34 ? 9   ARG   A O   1 
ATOM   5    C  CB  . ARG   A 1 9   ? 12.558  29.016 7.543  1.00 31.84 ? 9   ARG   A CB  1 
ATOM   6    C  CG  . ARG   A 1 9   ? 12.093  28.433 6.219  1.00 32.21 ? 9   ARG   A CG  1 
ATOM   7    C  CD  . ARG   A 1 9   ? 13.194  27.635 5.589  1.00 33.94 ? 9   ARG   A CD  1 
ATOM   8    N  NE  . ARG   A 1 9   ? 12.608  26.958 4.429  1.00 36.39 ? 9   ARG   A NE  1 
ATOM   9    C  CZ  . ARG   A 1 9   ? 13.198  26.060 3.671  1.00 35.29 ? 9   ARG   A CZ  1 
ATOM   10   N  NH1 . ARG   A 1 9   ? 14.428  25.683 3.900  1.00 33.69 ? 9   ARG   A NH1 1 
ATOM   11   N  NH2 . ARG   A 1 9   ? 12.502  25.476 2.710  1.00 38.14 ? 9   ARG   A NH2 1 
ATOM   12   N  N   . LEU   A 1 10  ? 11.418  29.684 10.584 1.00 26.54 ? 10  LEU   A N   1 
ATOM   13   C  CA  . LEU   A 1 10  ? 11.933  29.705 11.938 1.00 25.10 ? 10  LEU   A CA  1 
ATOM   14   C  C   . LEU   A 1 10  ? 12.912  28.564 12.126 1.00 22.08 ? 10  LEU   A C   1 
ATOM   15   O  O   . LEU   A 1 10  ? 12.876  27.538 11.451 1.00 21.38 ? 10  LEU   A O   1 
ATOM   16   C  CB  . LEU   A 1 10  ? 10.782  29.668 12.941 1.00 25.98 ? 10  LEU   A CB  1 
ATOM   17   C  CG  . LEU   A 1 10  ? 9.857   30.876 12.945 1.00 29.03 ? 10  LEU   A CG  1 
ATOM   18   C  CD1 . LEU   A 1 10  ? 8.745   30.678 13.971 1.00 34.07 ? 10  LEU   A CD1 1 
ATOM   19   C  CD2 . LEU   A 1 10  ? 10.599  32.135 13.209 1.00 31.71 ? 10  LEU   A CD2 1 
ATOM   20   N  N   . LEU   A 1 11  ? 13.830  28.762 13.088 1.00 22.58 ? 11  LEU   A N   1 
ATOM   21   C  CA  . LEU   A 1 11  ? 14.850  27.801 13.439 1.00 21.38 ? 11  LEU   A CA  1 
ATOM   22   C  C   . LEU   A 1 11  ? 14.626  27.308 14.875 1.00 21.74 ? 11  LEU   A C   1 
ATOM   23   O  O   . LEU   A 1 11  ? 14.021  27.989 15.649 1.00 22.44 ? 11  LEU   A O   1 
ATOM   24   C  CB  . LEU   A 1 11  ? 16.238  28.423 13.348 1.00 23.64 ? 11  LEU   A CB  1 
ATOM   25   C  CG  . LEU   A 1 11  ? 16.542  29.035 11.980 1.00 30.15 ? 11  LEU   A CG  1 
ATOM   26   C  CD1 . LEU   A 1 11  ? 17.689  29.967 12.117 1.00 36.52 ? 11  LEU   A CD1 1 
ATOM   27   C  CD2 . LEU   A 1 11  ? 16.782  27.874 11.057 1.00 29.59 ? 11  LEU   A CD2 1 
ATOM   28   N  N   . CYS   A 1 12  ? 15.140  26.119 15.146 1.00 23.19 ? 12  CYS   A N   1 
ATOM   29   C  CA  . CYS   A 1 12  ? 15.011  25.501 16.451 1.00 23.28 ? 12  CYS   A CA  1 
ATOM   30   C  C   . CYS   A 1 12  ? 16.373  25.002 16.896 1.00 20.58 ? 12  CYS   A C   1 
ATOM   31   O  O   . CYS   A 1 12  ? 17.047  24.274 16.201 1.00 20.22 ? 12  CYS   A O   1 
ATOM   32   C  CB  . CYS   A 1 12  ? 13.962  24.405 16.442 1.00 21.21 ? 12  CYS   A CB  1 
ATOM   33   S  SG  . CYS   A 1 12  ? 13.778  23.615 18.072 1.00 27.30 ? 12  CYS   A SG  1 
HETATM 34   N  N   . PBF   A 1 13  ? 16.735  25.417 18.115 1.00 21.07 ? 13  PBF   A N   1 
HETATM 35   C  C   . PBF   A 1 13  ? 17.504  23.984 19.886 1.00 18.33 ? 13  PBF   A C   1 
HETATM 36   O  O   . PBF   A 1 13  ? 16.788  24.435 20.776 1.00 19.57 ? 13  PBF   A O   1 
HETATM 37   C  CA  . PBF   A 1 13  ? 17.968  24.936 18.780 1.00 19.07 ? 13  PBF   A CA  1 
HETATM 38   C  CB  . PBF   A 1 13  ? 18.773  26.109 19.339 1.00 19.98 ? 13  PBF   A CB  1 
HETATM 39   C  CG  . PBF   A 1 13  ? 20.071  25.794 20.036 1.00 18.35 ? 13  PBF   A CG  1 
HETATM 40   C  CD1 . PBF   A 1 13  ? 20.472  26.555 21.119 1.00 22.10 ? 13  PBF   A CD1 1 
HETATM 41   C  CD2 . PBF   A 1 13  ? 20.913  24.785 19.599 1.00 18.00 ? 13  PBF   A CD2 1 
HETATM 42   C  CE1 . PBF   A 1 13  ? 21.668  26.313 21.763 1.00 21.40 ? 13  PBF   A CE1 1 
HETATM 43   C  CE2 . PBF   A 1 13  ? 22.116  24.532 20.234 1.00 21.20 ? 13  PBF   A CE2 1 
HETATM 44   C  CZ  . PBF   A 1 13  ? 22.500  25.287 21.338 1.00 21.79 ? 13  PBF   A CZ  1 
HETATM 45   C  CN1 . PBF   A 1 13  ? 23.790  25.078 22.049 1.00 26.88 ? 13  PBF   A CN1 1 
HETATM 46   O  ON2 . PBF   A 1 13  ? 24.479  26.051 22.317 1.00 26.86 ? 13  PBF   A ON2 1 
HETATM 47   C  CT  . PBF   A 1 13  ? 24.258  23.727 22.460 1.00 25.26 ? 13  PBF   A CT  1 
HETATM 48   C  CI1 . PBF   A 1 13  ? 25.587  23.552 22.823 1.00 27.10 ? 13  PBF   A CI1 1 
HETATM 49   C  CI2 . PBF   A 1 13  ? 23.397  22.640 22.526 1.00 22.32 ? 13  PBF   A CI2 1 
HETATM 50   C  CK1 . PBF   A 1 13  ? 26.044  22.309 23.221 1.00 29.62 ? 13  PBF   A CK1 1 
HETATM 51   C  CK2 . PBF   A 1 13  ? 23.866  21.403 22.926 1.00 22.50 ? 13  PBF   A CK2 1 
HETATM 52   C  CL  . PBF   A 1 13  ? 25.185  21.239 23.272 1.00 26.15 ? 13  PBF   A CL  1 
ATOM   53   N  N   . SER   A 1 14  ? 17.883  22.719 19.791 1.00 20.42 ? 14  SER   A N   1 
ATOM   54   C  CA  . SER   A 1 14  ? 17.461  21.676 20.719 1.00 22.86 ? 14  SER   A CA  1 
ATOM   55   C  C   . SER   A 1 14  ? 18.671  21.280 21.538 1.00 20.74 ? 14  SER   A C   1 
ATOM   56   O  O   . SER   A 1 14  ? 19.730  21.039 20.989 1.00 20.06 ? 14  SER   A O   1 
ATOM   57   C  CB  . SER   A 1 14  ? 16.895  20.458 19.965 1.00 22.58 ? 14  SER   A CB  1 
ATOM   58   O  OG  . SER   A 1 14  ? 15.811  20.921 19.177 1.00 23.64 ? 14  SER   A OG  1 
ATOM   59   N  N   . ILE   A 1 15  ? 18.489  21.156 22.846 1.00 20.41 ? 15  ILE   A N   1 
ATOM   60   C  CA  . ILE   A 1 15  ? 19.541  20.786 23.776 1.00 19.24 ? 15  ILE   A CA  1 
ATOM   61   C  C   . ILE   A 1 15  ? 19.082  19.575 24.590 1.00 18.77 ? 15  ILE   A C   1 
ATOM   62   O  O   . ILE   A 1 15  ? 18.044  19.708 25.240 1.00 18.56 ? 15  ILE   A O   1 
ATOM   63   C  CB  . ILE   A 1 15  ? 19.815  21.960 24.730 1.00 21.36 ? 15  ILE   A CB  1 
ATOM   64   C  CG1 . ILE   A 1 15  ? 19.986  23.264 23.930 1.00 24.82 ? 15  ILE   A CG1 1 
ATOM   65   C  CG2 . ILE   A 1 15  ? 21.029  21.646 25.595 1.00 22.14 ? 15  ILE   A CG2 1 
ATOM   66   C  CD1 . ILE   A 1 15  ? 20.314  24.475 24.793 1.00 34.40 ? 15  ILE   A CD1 1 
ATOM   67   N  N   . TYR   A 1 16  ? 19.801  18.466 24.423 1.00 19.45 ? 16  TYR   A N   1 
ATOM   68   C  CA  . TYR   A 1 16  ? 19.478  17.157 25.013 1.00 19.78 ? 16  TYR   A CA  1 
ATOM   69   C  C   . TYR   A 1 16  ? 20.357  16.949 26.237 1.00 18.09 ? 16  TYR   A C   1 
ATOM   70   O  O   . TYR   A 1 16  ? 21.569  16.711 26.118 1.00 20.37 ? 16  TYR   A O   1 
ATOM   71   C  CB  . TYR   A 1 16  ? 19.651  16.094 23.928 1.00 21.42 ? 16  TYR   A CB  1 
ATOM   72   C  CG  . TYR   A 1 16  ? 18.737  16.321 22.728 1.00 23.07 ? 16  TYR   A CG  1 
ATOM   73   C  CD1 . TYR   A 1 16  ? 19.141  17.142 21.688 1.00 28.40 ? 16  TYR   A CD1 1 
ATOM   74   C  CD2 . TYR   A 1 16  ? 17.508  15.663 22.590 1.00 25.91 ? 16  TYR   A CD2 1 
ATOM   75   C  CE1 . TYR   A 1 16  ? 18.354  17.337 20.563 1.00 31.15 ? 16  TYR   A CE1 1 
ATOM   76   C  CE2 . TYR   A 1 16  ? 16.680  15.917 21.498 1.00 26.32 ? 16  TYR   A CE2 1 
ATOM   77   C  CZ  . TYR   A 1 16  ? 17.116  16.731 20.476 1.00 32.09 ? 16  TYR   A CZ  1 
ATOM   78   O  OH  . TYR   A 1 16  ? 16.329  16.963 19.360 1.00 42.96 ? 16  TYR   A OH  1 
ATOM   79   N  N   . VAL   A 1 17  ? 19.717  17.005 27.404 1.00 18.83 ? 17  VAL   A N   1 
ATOM   80   C  CA  . VAL   A 1 17  ? 20.395  17.004 28.674 1.00 19.16 ? 17  VAL   A CA  1 
ATOM   81   C  C   . VAL   A 1 17  ? 20.297  15.664 29.391 1.00 19.07 ? 17  VAL   A C   1 
ATOM   82   O  O   . VAL   A 1 17  ? 19.192  15.120 29.570 1.00 20.22 ? 17  VAL   A O   1 
ATOM   83   C  CB  . VAL   A 1 17  ? 19.829  18.129 29.550 1.00 19.91 ? 17  VAL   A CB  1 
ATOM   84   C  CG1 . VAL   A 1 17  ? 20.402  18.101 30.954 1.00 19.48 ? 17  VAL   A CG1 1 
ATOM   85   C  CG2 . VAL   A 1 17  ? 20.148  19.481 28.892 1.00 23.45 ? 17  VAL   A CG2 1 
ATOM   86   N  N   . THR   A 1 18  ? 21.434  15.249 29.913 1.00 19.54 ? 18  THR   A N   1 
ATOM   87   C  CA  . THR   A 1 18  ? 21.541  14.120 30.827 1.00 18.84 ? 18  THR   A CA  1 
ATOM   88   C  C   . THR   A 1 18  ? 21.709  14.730 32.215 1.00 22.96 ? 18  THR   A C   1 
ATOM   89   O  O   . THR   A 1 18  ? 22.543  15.627 32.384 1.00 19.79 ? 18  THR   A O   1 
ATOM   90   C  CB  . THR   A 1 18  ? 22.699  13.199 30.450 1.00 21.99 ? 18  THR   A CB  1 
ATOM   91   O  OG1 . THR   A 1 18  ? 22.500  12.682 29.119 1.00 20.69 ? 18  THR   A OG1 1 
ATOM   92   C  CG2 . THR   A 1 18  ? 22.898  12.115 31.504 1.00 21.42 ? 18  THR   A CG2 1 
ATOM   93   N  N   . LYS   A 1 19  ? 20.936  14.253 33.202 1.00 19.44 ? 19  LYS   A N   1 
ATOM   94   C  CA  . LYS   A 1 19  ? 21.042  14.848 34.528 1.00 20.38 ? 19  LYS   A CA  1 
ATOM   95   C  C   . LYS   A 1 19  ? 22.423  14.671 35.153 1.00 19.50 ? 19  LYS   A C   1 
ATOM   96   O  O   . LYS   A 1 19  ? 23.185  13.727 34.884 1.00 21.02 ? 19  LYS   A O   1 
ATOM   97   C  CB  . LYS   A 1 19  ? 19.946  14.333 35.465 1.00 23.39 ? 19  LYS   A CB  1 
ATOM   98   C  CG  . LYS   A 1 19  ? 20.115  12.887 35.898 1.00 25.03 ? 19  LYS   A CG  1 
ATOM   99   C  CD  . LYS   A 1 19  ? 18.894  12.590 36.792 1.00 30.02 ? 19  LYS   A CD  1 
ATOM   100  C  CE  . LYS   A 1 19  ? 18.710  11.168 37.154 1.00 33.78 ? 19  LYS   A CE  1 
ATOM   101  N  NZ  . LYS   A 1 19  ? 19.828  10.652 37.907 1.00 37.39 ? 19  LYS   A NZ  1 
ATOM   102  N  N   . LYS   A 1 20  ? 22.742  15.612 36.046 1.00 20.23 ? 20  LYS   A N   1 
ATOM   103  C  CA  . LYS   A 1 20  ? 23.946  15.595 36.855 1.00 21.35 ? 20  LYS   A CA  1 
ATOM   104  C  C   . LYS   A 1 20  ? 24.074  14.243 37.550 1.00 21.92 ? 20  LYS   A C   1 
ATOM   105  O  O   . LYS   A 1 20  ? 23.107  13.777 38.138 1.00 22.25 ? 20  LYS   A O   1 
ATOM   106  C  CB  . LYS   A 1 20  ? 23.745  16.707 37.904 1.00 25.31 ? 20  LYS   A CB  1 
ATOM   107  C  CG  . LYS   A 1 20  ? 24.843  16.915 38.887 1.00 29.94 ? 20  LYS   A CG  1 
ATOM   108  C  CD  . LYS   A 1 20  ? 24.594  18.194 39.705 1.00 28.74 ? 20  LYS   A CD  1 
ATOM   109  C  CE  . LYS   A 1 20  ? 25.751  18.461 40.597 1.00 33.18 ? 20  LYS   A CE  1 
ATOM   110  N  NZ  . LYS   A 1 20  ? 25.805  17.494 41.697 1.00 27.88 ? 20  LYS   A NZ  1 
ATOM   111  N  N   . PRO   A 1 21  ? 25.271  13.637 37.549 1.00 26.60 ? 21  PRO   A N   1 
ATOM   112  C  CA  . PRO   A 1 21  ? 25.460  12.279 38.045 1.00 32.01 ? 21  PRO   A CA  1 
ATOM   113  C  C   . PRO   A 1 21  ? 24.968  12.219 39.488 1.00 37.09 ? 21  PRO   A C   1 
ATOM   114  O  O   . PRO   A 1 21  ? 25.216  13.139 40.257 1.00 32.26 ? 21  PRO   A O   1 
ATOM   115  C  CB  . PRO   A 1 21  ? 26.990  12.091 37.959 1.00 34.61 ? 21  PRO   A CB  1 
ATOM   116  C  CG  . PRO   A 1 21  ? 27.466  13.027 36.871 1.00 34.45 ? 21  PRO   A CG  1 
ATOM   117  C  CD  . PRO   A 1 21  ? 26.498  14.207 36.958 1.00 32.10 ? 21  PRO   A CD  1 
ATOM   118  N  N   . ASP   A 1 22  ? 24.216  11.188 39.844 1.00 39.85 ? 22  ASP   A N   1 
ATOM   119  C  CA  . ASP   A 1 22  ? 23.826  11.039 41.241 1.00 50.98 ? 22  ASP   A CA  1 
ATOM   120  C  C   . ASP   A 1 22  ? 22.883  12.147 41.736 1.00 50.48 ? 22  ASP   A C   1 
ATOM   121  O  O   . ASP   A 1 22  ? 22.610  12.200 42.926 1.00 52.44 ? 22  ASP   A O   1 
ATOM   122  C  CB  . ASP   A 1 22  ? 25.040  10.970 42.167 1.00 57.49 ? 22  ASP   A CB  1 
ATOM   123  C  CG  . ASP   A 1 22  ? 26.073  9.879  41.870 1.00 58.99 ? 22  ASP   A CG  1 
ATOM   124  O  OD1 . ASP   A 1 22  ? 25.719  8.873  41.230 1.00 52.99 ? 22  ASP   A OD1 1 
ATOM   125  O  OD2 . ASP   A 1 22  ? 27.241  10.061 42.260 1.00 60.82 ? 22  ASP   A OD2 1 
ATOM   126  N  N   . GLN   A 1 23  ? 22.352  13.024 40.869 1.00 35.58 ? 23  GLN   A N   1 
ATOM   127  C  CA  . GLN   A 1 23  ? 21.225  13.863 41.254 1.00 27.47 ? 23  GLN   A CA  1 
ATOM   128  C  C   . GLN   A 1 23  ? 19.952  13.040 41.040 1.00 27.22 ? 23  GLN   A C   1 
ATOM   129  O  O   . GLN   A 1 23  ? 19.761  12.377 40.011 1.00 30.03 ? 23  GLN   A O   1 
ATOM   130  C  CB  . GLN   A 1 23  ? 21.195  15.114 40.359 1.00 28.13 ? 23  GLN   A CB  1 
ATOM   131  C  CG  . GLN   A 1 23  ? 20.057  16.065 40.655 1.00 27.45 ? 23  GLN   A CG  1 
ATOM   132  C  CD  . GLN   A 1 23  ? 20.145  17.328 39.811 1.00 23.94 ? 23  GLN   A CD  1 
ATOM   133  O  OE1 . GLN   A 1 23  ? 20.085  17.256 38.591 1.00 22.63 ? 23  GLN   A OE1 1 
ATOM   134  N  NE2 . GLN   A 1 23  ? 20.141  18.465 40.461 1.00 25.48 ? 23  GLN   A NE2 1 
ATOM   135  N  N   . SER   A 1 24  ? 19.037  13.143 42.000 1.00 26.01 ? 24  SER   A N   1 
ATOM   136  C  CA  . SER   A 1 24  ? 17.731  12.456 41.887 1.00 26.05 ? 24  SER   A CA  1 
ATOM   137  C  C   . SER   A 1 24  ? 16.927  13.022 40.711 1.00 26.74 ? 24  SER   A C   1 
ATOM   138  O  O   . SER   A 1 24  ? 17.070  14.208 40.420 1.00 23.80 ? 24  SER   A O   1 
ATOM   139  C  CB  . SER   A 1 24  ? 16.942  12.636 43.159 1.00 24.64 ? 24  SER   A CB  1 
ATOM   140  O  OG  . SER   A 1 24  ? 16.134  13.795 43.147 1.00 21.13 ? 24  SER   A OG  1 
ATOM   141  N  N   . GLU   A 1 25  ? 16.059  12.206 40.123 1.00 25.86 ? 25  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 25  ? 15.159  12.707 39.057 1.00 27.33 ? 25  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 25  ? 14.310  13.857 39.619 1.00 24.01 ? 25  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 25  ? 14.186  14.882 38.961 1.00 23.46 ? 25  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 25  ? 14.267  11.568 38.559 1.00 33.30 ? 25  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 25  ? 14.805  10.879 37.311 1.00 41.83 ? 25  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 25  ? 13.895  9.823  36.710 1.00 38.69 ? 25  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 25  ? 12.690  9.804  37.026 1.00 41.44 ? 25  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 25  ? 14.421  9.013  35.923 1.00 30.68 ? 25  GLU   A OE2 1 
ATOM   150  N  N   . GLU   A 1 26  ? 13.749  13.662 40.805 1.00 21.32 ? 26  GLU   A N   1 
ATOM   151  C  CA  . GLU   A 1 26  ? 12.903  14.702 41.425 1.00 23.94 ? 26  GLU   A CA  1 
ATOM   152  C  C   . GLU   A 1 26  ? 13.717  15.994 41.570 1.00 21.73 ? 26  GLU   A C   1 
ATOM   153  O  O   . GLU   A 1 26  ? 13.205  17.059 41.224 1.00 21.80 ? 26  GLU   A O   1 
ATOM   154  C  CB  . GLU   A 1 26  ? 12.456  14.199 42.794 1.00 28.65 ? 26  GLU   A CB  1 
ATOM   155  C  CG  . GLU   A 1 26  ? 11.515  15.136 43.538 1.00 41.55 ? 26  GLU   A CG  1 
ATOM   156  C  CD  . GLU   A 1 26  ? 10.998  14.462 44.796 1.00 47.90 ? 26  GLU   A CD  1 
ATOM   157  O  OE1 . GLU   A 1 26  ? 10.223  13.500 44.663 1.00 46.43 ? 26  GLU   A OE1 1 
ATOM   158  O  OE2 . GLU   A 1 26  ? 11.385  14.884 45.900 1.00 58.35 ? 26  GLU   A OE2 1 
ATOM   159  N  N   . ASP   A 1 27  ? 14.945  15.866 42.048 1.00 19.97 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 27  ? 15.719  17.086 42.305 1.00 19.84 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 27  ? 16.086  17.760 40.974 1.00 20.90 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 27  ? 16.055  18.990 40.857 1.00 21.25 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 27  ? 16.947  16.813 43.152 1.00 22.65 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 27  ? 16.716  16.580 44.642 1.00 25.05 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 27  ? 15.596  16.775 45.081 1.00 24.90 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 27  ? 17.653  16.086 45.282 1.00 26.92 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . HIS   A 1 28  ? 16.374  16.936 39.974 1.00 19.51 ? 28  HIS   A N   1 
ATOM   168  C  CA  . HIS   A 1 28  ? 16.700  17.437 38.649 1.00 20.52 ? 28  HIS   A CA  1 
ATOM   169  C  C   . HIS   A 1 28  ? 15.539  18.224 38.073 1.00 20.38 ? 28  HIS   A C   1 
ATOM   170  O  O   . HIS   A 1 28  ? 15.689  19.369 37.669 1.00 19.46 ? 28  HIS   A O   1 
ATOM   171  C  CB  . HIS   A 1 28  ? 17.158  16.311 37.729 1.00 19.82 ? 28  HIS   A CB  1 
ATOM   172  C  CG  . HIS   A 1 28  ? 17.320  16.727 36.302 1.00 18.67 ? 28  HIS   A CG  1 
ATOM   173  N  ND1 . HIS   A 1 28  ? 18.514  17.277 35.848 1.00 18.77 ? 28  HIS   A ND1 1 
ATOM   174  C  CD2 . HIS   A 1 28  ? 16.516  16.632 35.218 1.00 19.73 ? 28  HIS   A CD2 1 
ATOM   175  C  CE1 . HIS   A 1 28  ? 18.422  17.466 34.544 1.00 17.29 ? 28  HIS   A CE1 1 
ATOM   176  N  NE2 . HIS   A 1 28  ? 17.206  17.128 34.126 1.00 19.38 ? 28  HIS   A NE2 1 
ATOM   177  N  N   . HIS   A 1 29  ? 14.355  17.594 37.975 1.00 20.28 ? 29  HIS   A N   1 
ATOM   178  C  CA  . HIS   A 1 29  ? 13.225  18.239 37.342 1.00 20.80 ? 29  HIS   A CA  1 
ATOM   179  C  C   . HIS   A 1 29  ? 12.705  19.446 38.132 1.00 20.08 ? 29  HIS   A C   1 
ATOM   180  O  O   . HIS   A 1 29  ? 12.276  20.430 37.534 1.00 20.25 ? 29  HIS   A O   1 
ATOM   181  C  CB  . HIS   A 1 29  ? 12.156  17.180 37.011 1.00 21.07 ? 29  HIS   A CB  1 
ATOM   182  C  CG  . HIS   A 1 29  ? 12.638  16.192 35.988 1.00 20.82 ? 29  HIS   A CG  1 
ATOM   183  N  ND1 . HIS   A 1 29  ? 12.648  16.522 34.636 1.00 22.16 ? 29  HIS   A ND1 1 
ATOM   184  C  CD2 . HIS   A 1 29  ? 13.218  15.002 36.089 1.00 21.67 ? 29  HIS   A CD2 1 
ATOM   185  C  CE1 . HIS   A 1 29  ? 13.197  15.527 33.959 1.00 21.56 ? 29  HIS   A CE1 1 
ATOM   186  N  NE2 . HIS   A 1 29  ? 13.546  14.575 34.824 1.00 21.73 ? 29  HIS   A NE2 1 
ATOM   187  N  N   . ASN   A 1 30  ? 12.724  19.396 39.482 1.00 18.33 ? 30  ASN   A N   1 
ATOM   188  C  CA  . ASN   A 1 30  ? 12.350  20.549 40.282 1.00 20.36 ? 30  ASN   A CA  1 
ATOM   189  C  C   . ASN   A 1 30  ? 13.298  21.719 39.997 1.00 21.10 ? 30  ASN   A C   1 
ATOM   190  O  O   . ASN   A 1 30  ? 12.846  22.844 39.838 1.00 18.91 ? 30  ASN   A O   1 
ATOM   191  C  CB  . ASN   A 1 30  ? 12.297  20.220 41.773 1.00 23.69 ? 30  ASN   A CB  1 
ATOM   192  C  CG  . ASN   A 1 30  ? 11.010  19.471 42.105 1.00 27.16 ? 30  ASN   A CG  1 
ATOM   193  O  OD1 . ASN   A 1 30  ? 9.953   19.733 41.527 1.00 26.17 ? 30  ASN   A OD1 1 
ATOM   194  N  ND2 . ASN   A 1 30  ? 11.078  18.533 43.019 1.00 26.42 ? 30  ASN   A ND2 1 
ATOM   195  N  N   . HIS   A 1 31  ? 14.588  21.441 39.922 1.00 20.46 ? 31  HIS   A N   1 
ATOM   196  C  CA  . HIS   A 1 31  ? 15.567  22.499 39.655 1.00 20.44 ? 31  HIS   A CA  1 
ATOM   197  C  C   . HIS   A 1 31  ? 15.290  23.115 38.278 1.00 17.55 ? 31  HIS   A C   1 
ATOM   198  O  O   . HIS   A 1 31  ? 15.198  24.341 38.115 1.00 18.18 ? 31  HIS   A O   1 
ATOM   199  C  CB  . HIS   A 1 31  ? 17.020  21.976 39.699 1.00 20.03 ? 31  HIS   A CB  1 
ATOM   200  C  CG  . HIS   A 1 31  ? 17.965  23.111 39.503 1.00 21.31 ? 31  HIS   A CG  1 
ATOM   201  N  ND1 . HIS   A 1 31  ? 18.472  23.906 40.513 1.00 19.91 ? 31  HIS   A ND1 1 
ATOM   202  C  CD2 . HIS   A 1 31  ? 18.358  23.696 38.359 1.00 21.90 ? 31  HIS   A CD2 1 
ATOM   203  C  CE1 . HIS   A 1 31  ? 19.219  24.873 39.967 1.00 21.21 ? 31  HIS   A CE1 1 
ATOM   204  N  NE2 . HIS   A 1 31  ? 19.130  24.786 38.700 1.00 21.33 ? 31  HIS   A NE2 1 
ATOM   205  N  N   . VAL   A 1 32  ? 15.100  22.248 37.272 1.00 17.29 ? 32  VAL   A N   1 
ATOM   206  C  CA  . VAL   A 1 32  ? 14.851  22.713 35.917 1.00 18.85 ? 32  VAL   A CA  1 
ATOM   207  C  C   . VAL   A 1 32  ? 13.603  23.575 35.856 1.00 17.93 ? 32  VAL   A C   1 
ATOM   208  O  O   . VAL   A 1 32  ? 13.643  24.671 35.322 1.00 17.03 ? 32  VAL   A O   1 
ATOM   209  C  CB  . VAL   A 1 32  ? 14.791  21.523 34.955 1.00 18.94 ? 32  VAL   A CB  1 
ATOM   210  C  CG1 . VAL   A 1 32  ? 14.145  21.951 33.648 1.00 21.69 ? 32  VAL   A CG1 1 
ATOM   211  C  CG2 . VAL   A 1 32  ? 16.175  20.911 34.751 1.00 19.41 ? 32  VAL   A CG2 1 
ATOM   212  N  N   . SER   A 1 33  ? 12.489  23.097 36.412 1.00 18.73 ? 33  SER   A N   1 
ATOM   213  C  CA  . SER   A 1 33  ? 11.210  23.789 36.342 1.00 19.04 ? 33  SER   A CA  1 
ATOM   214  C  C   . SER   A 1 33  ? 11.136  25.029 37.209 1.00 18.28 ? 33  SER   A C   1 
ATOM   215  O  O   . SER   A 1 33  ? 10.529  26.005 36.803 1.00 18.93 ? 33  SER   A O   1 
ATOM   216  C  CB  . SER   A 1 33  ? 10.013  22.903 36.661 1.00 22.65 ? 33  SER   A CB  1 
ATOM   217  O  OG  . SER   A 1 33  ? 9.933   21.898 35.666 1.00 25.32 ? 33  SER   A OG  1 
ATOM   218  N  N   . LYS   A 1 34  ? 11.689  24.958 38.418 1.00 19.47 ? 34  LYS   A N   1 
ATOM   219  C  CA  . LYS   A 1 34  ? 11.408  25.962 39.428 1.00 19.81 ? 34  LYS   A CA  1 
ATOM   220  C  C   . LYS   A 1 34  ? 12.514  27.031 39.495 1.00 19.83 ? 34  LYS   A C   1 
ATOM   221  O  O   . LYS   A 1 34  ? 12.238  28.154 39.927 1.00 18.24 ? 34  LYS   A O   1 
ATOM   222  C  CB  . LYS   A 1 34  ? 11.155  25.372 40.809 1.00 23.15 ? 34  LYS   A CB  1 
ATOM   223  C  CG  . LYS   A 1 34  ? 9.947   24.444 40.725 1.00 26.56 ? 34  LYS   A CG  1 
ATOM   224  C  CD  . LYS   A 1 34  ? 9.610   23.792 42.046 1.00 35.92 ? 34  LYS   A CD  1 
ATOM   225  C  CE  . LYS   A 1 34  ? 8.255   23.142 41.941 1.00 39.24 ? 34  LYS   A CE  1 
ATOM   226  N  NZ  . LYS   A 1 34  ? 8.191   22.277 43.110 1.00 49.96 ? 34  LYS   A NZ  1 
ATOM   227  N  N   . VAL   A 1 35  ? 13.737  26.687 39.072 1.00 17.19 ? 35  VAL   A N   1 
ATOM   228  C  CA  . VAL   A 1 35  ? 14.879  27.602 39.198 1.00 18.02 ? 35  VAL   A CA  1 
ATOM   229  C  C   . VAL   A 1 35  ? 15.427  27.984 37.832 1.00 18.84 ? 35  VAL   A C   1 
ATOM   230  O  O   . VAL   A 1 35  ? 15.626  29.156 37.568 1.00 19.76 ? 35  VAL   A O   1 
ATOM   231  C  CB  . VAL   A 1 35  ? 15.975  27.012 40.097 1.00 20.21 ? 35  VAL   A CB  1 
ATOM   232  C  CG1 . VAL   A 1 35  ? 17.179  27.955 40.185 1.00 22.74 ? 35  VAL   A CG1 1 
ATOM   233  C  CG2 . VAL   A 1 35  ? 15.427  26.689 41.495 1.00 22.60 ? 35  VAL   A CG2 1 
ATOM   234  N  N   . ASN   A 1 36  ? 15.786  27.006 36.987 1.00 18.33 ? 36  ASN   A N   1 
ATOM   235  C  CA  . ASN   A 1 36  ? 16.388  27.337 35.707 1.00 16.67 ? 36  ASN   A CA  1 
ATOM   236  C  C   . ASN   A 1 36  ? 15.427  28.145 34.840 1.00 17.24 ? 36  ASN   A C   1 
ATOM   237  O  O   . ASN   A 1 36  ? 15.820  29.098 34.179 1.00 18.56 ? 36  ASN   A O   1 
ATOM   238  C  CB  . ASN   A 1 36  ? 16.923  26.094 35.024 1.00 18.12 ? 36  ASN   A CB  1 
ATOM   239  C  CG  . ASN   A 1 36  ? 17.716  26.418 33.772 1.00 20.70 ? 36  ASN   A CG  1 
ATOM   240  O  OD1 . ASN   A 1 36  ? 17.208  26.321 32.659 1.00 20.74 ? 36  ASN   A OD1 1 
ATOM   241  N  ND2 . ASN   A 1 36  ? 18.926  26.919 33.967 1.00 21.05 ? 36  ASN   A ND2 1 
ATOM   242  N  N   . ALA   A 1 37  ? 14.164  27.722 34.774 1.00 19.20 ? 37  ALA   A N   1 
ATOM   243  C  CA  . ALA   A 1 37  ? 13.190  28.359 33.896 1.00 18.68 ? 37  ALA   A CA  1 
ATOM   244  C  C   . ALA   A 1 37  ? 13.028  29.836 34.209 1.00 18.50 ? 37  ALA   A C   1 
ATOM   245  O  O   . ALA   A 1 37  ? 13.168  30.651 33.293 1.00 19.12 ? 37  ALA   A O   1 
ATOM   246  C  CB  . ALA   A 1 37  ? 11.865  27.612 33.899 1.00 20.76 ? 37  ALA   A CB  1 
ATOM   247  N  N   . PRO   A 1 38  ? 12.735  30.277 35.461 1.00 20.48 ? 38  PRO   A N   1 
ATOM   248  C  CA  . PRO   A 1 38  ? 12.652  31.703 35.736 1.00 21.98 ? 38  PRO   A CA  1 
ATOM   249  C  C   . PRO   A 1 38  ? 13.950  32.460 35.487 1.00 19.72 ? 38  PRO   A C   1 
ATOM   250  O  O   . PRO   A 1 38  ? 13.912  33.640 35.172 1.00 19.98 ? 38  PRO   A O   1 
ATOM   251  C  CB  . PRO   A 1 38  ? 12.203  31.766 37.209 1.00 23.94 ? 38  PRO   A CB  1 
ATOM   252  C  CG  . PRO   A 1 38  ? 12.647  30.465 37.789 1.00 25.92 ? 38  PRO   A CG  1 
ATOM   253  C  CD  . PRO   A 1 38  ? 12.381  29.497 36.664 1.00 24.02 ? 38  PRO   A CD  1 
ATOM   254  N  N   . MET   A 1 39  ? 15.078  31.775 35.625 1.00 18.04 ? 39  MET   A N   1 
ATOM   255  C  CA  . MET   A 1 39  ? 16.389  32.409 35.355 1.00 18.31 ? 39  MET   A CA  1 
ATOM   256  C  C   . MET   A 1 39  ? 16.540  32.664 33.847 1.00 19.16 ? 39  MET   A C   1 
ATOM   257  O  O   . MET   A 1 39  ? 17.103  33.692 33.481 1.00 19.00 ? 39  MET   A O   1 
ATOM   258  C  CB  . MET   A 1 39  ? 17.509  31.484 35.840 1.00 20.56 ? 39  MET   A CB  1 
ATOM   259  C  CG  . MET   A 1 39  ? 18.905  32.037 35.723 1.00 23.56 ? 39  MET   A CG  1 
ATOM   260  S  SD  . MET   A 1 39  ? 20.097  30.820 36.315 1.00 27.10 ? 39  MET   A SD  1 
ATOM   261  C  CE  . MET   A 1 39  ? 19.433  30.370 37.922 1.00 26.99 ? 39  MET   A CE  1 
ATOM   262  N  N   . MET   A 1 40  ? 16.016  31.762 33.027 1.00 16.28 ? 40  MET   A N   1 
ATOM   263  C  CA  . MET   A 1 40  ? 16.173  31.861 31.556 1.00 18.41 ? 40  MET   A CA  1 
ATOM   264  C  C   . MET   A 1 40  ? 15.128  32.786 30.908 1.00 19.63 ? 40  MET   A C   1 
ATOM   265  O  O   . MET   A 1 40  ? 15.485  33.458 29.938 1.00 19.08 ? 40  MET   A O   1 
ATOM   266  C  CB  . MET   A 1 40  ? 16.034  30.470 30.925 1.00 18.57 ? 40  MET   A CB  1 
ATOM   267  C  CG  . MET   A 1 40  ? 17.203  29.556 31.186 1.00 21.38 ? 40  MET   A CG  1 
ATOM   268  S  SD  . MET   A 1 40  ? 18.648  30.109 30.262 1.00 21.72 ? 40  MET   A SD  1 
ATOM   269  C  CE  . MET   A 1 40  ? 18.039  29.989 28.575 1.00 24.22 ? 40  MET   A CE  1 
ATOM   270  N  N   . ILE   A 1 41  ? 13.909  32.845 31.448 1.00 19.79 ? 41  ILE   A N   1 
ATOM   271  C  CA  . ILE   A 1 41  ? 12.840  33.568 30.747 1.00 21.44 ? 41  ILE   A CA  1 
ATOM   272  C  C   . ILE   A 1 41  ? 13.210  35.010 30.393 1.00 21.01 ? 41  ILE   A C   1 
ATOM   273  O  O   . ILE   A 1 41  ? 12.965  35.450 29.274 1.00 22.46 ? 41  ILE   A O   1 
ATOM   274  C  CB  . ILE   A 1 41  ? 11.515  33.456 31.521 1.00 23.20 ? 41  ILE   A CB  1 
ATOM   275  C  CG1 . ILE   A 1 41  ? 10.936  32.103 31.223 1.00 27.38 ? 41  ILE   A CG1 1 
ATOM   276  C  CG2 . ILE   A 1 41  ? 10.554  34.598 31.138 1.00 26.74 ? 41  ILE   A CG2 1 
ATOM   277  C  CD1 . ILE   A 1 41  ? 9.814   31.713 32.156 1.00 35.07 ? 41  ILE   A CD1 1 
ATOM   278  N  N   . PRO   A 1 42  ? 13.810  35.801 31.290 1.00 20.03 ? 42  PRO   A N   1 
ATOM   279  C  CA  . PRO   A 1 42  ? 14.194  37.172 30.962 1.00 19.60 ? 42  PRO   A CA  1 
ATOM   280  C  C   . PRO   A 1 42  ? 15.130  37.295 29.788 1.00 18.96 ? 42  PRO   A C   1 
ATOM   281  O  O   . PRO   A 1 42  ? 14.960  38.167 28.936 1.00 20.69 ? 42  PRO   A O   1 
ATOM   282  C  CB  . PRO   A 1 42  ? 14.804  37.727 32.253 1.00 21.68 ? 42  PRO   A CB  1 
ATOM   283  C  CG  . PRO   A 1 42  ? 14.162  36.864 33.336 1.00 25.58 ? 42  PRO   A CG  1 
ATOM   284  C  CD  . PRO   A 1 42  ? 14.011  35.491 32.715 1.00 22.62 ? 42  PRO   A CD  1 
ATOM   285  N  N   . PHE   A 1 43  ? 16.069  36.348 29.684 1.00 19.04 ? 43  PHE   A N   1 
ATOM   286  C  CA  . PHE   A 1 43  ? 17.013  36.349 28.585 1.00 18.22 ? 43  PHE   A CA  1 
ATOM   287  C  C   . PHE   A 1 43  ? 16.323  36.008 27.281 1.00 20.13 ? 43  PHE   A C   1 
ATOM   288  O  O   . PHE   A 1 43  ? 16.558  36.641 26.256 1.00 23.19 ? 43  PHE   A O   1 
ATOM   289  C  CB  . PHE   A 1 43  ? 18.155  35.352 28.785 1.00 19.54 ? 43  PHE   A CB  1 
ATOM   290  C  CG  . PHE   A 1 43  ? 19.068  35.696 29.944 1.00 20.41 ? 43  PHE   A CG  1 
ATOM   291  C  CD1 . PHE   A 1 43  ? 19.981  36.742 29.866 1.00 22.15 ? 43  PHE   A CD1 1 
ATOM   292  C  CD2 . PHE   A 1 43  ? 18.980  35.011 31.136 1.00 18.45 ? 43  PHE   A CD2 1 
ATOM   293  C  CE1 . PHE   A 1 43  ? 20.777  37.038 30.952 1.00 23.02 ? 43  PHE   A CE1 1 
ATOM   294  C  CE2 . PHE   A 1 43  ? 19.828  35.276 32.197 1.00 23.19 ? 43  PHE   A CE2 1 
ATOM   295  C  CZ  . PHE   A 1 43  ? 20.716  36.309 32.102 1.00 22.42 ? 43  PHE   A CZ  1 
ATOM   296  N  N   . LEU   A 1 44  ? 15.450  34.981 27.334 1.00 19.57 ? 44  LEU   A N   1 
ATOM   297  C  CA  . LEU   A 1 44  ? 14.716  34.566 26.161 1.00 21.83 ? 44  LEU   A CA  1 
ATOM   298  C  C   . LEU   A 1 44  ? 13.841  35.724 25.630 1.00 20.48 ? 44  LEU   A C   1 
ATOM   299  O  O   . LEU   A 1 44  ? 13.801  35.968 24.432 1.00 23.34 ? 44  LEU   A O   1 
ATOM   300  C  CB  . LEU   A 1 44  ? 13.899  33.328 26.539 1.00 21.81 ? 44  LEU   A CB  1 
ATOM   301  C  CG  . LEU   A 1 44  ? 14.698  32.096 26.998 1.00 22.87 ? 44  LEU   A CG  1 
ATOM   302  C  CD1 . LEU   A 1 44  ? 13.788  30.991 27.559 1.00 27.02 ? 44  LEU   A CD1 1 
ATOM   303  C  CD2 . LEU   A 1 44  ? 15.521  31.539 25.916 1.00 24.82 ? 44  LEU   A CD2 1 
ATOM   304  N  N   . LYS   A 1 45  ? 13.179  36.447 26.510 1.00 20.12 ? 45  LYS   A N   1 
ATOM   305  C  CA  . LYS   A 1 45  ? 12.389  37.622 26.126 1.00 22.79 ? 45  LYS   A CA  1 
ATOM   306  C  C   . LYS   A 1 45  ? 13.277  38.701 25.494 1.00 24.59 ? 45  LYS   A C   1 
ATOM   307  O  O   . LYS   A 1 45  ? 13.010  39.217 24.399 1.00 25.84 ? 45  LYS   A O   1 
ATOM   308  C  CB  . LYS   A 1 45  ? 11.727  38.177 27.384 1.00 26.62 ? 45  LYS   A CB  1 
ATOM   309  C  CG  . LYS   A 1 45  ? 10.818  39.406 27.276 1.00 35.51 ? 45  LYS   A CG  1 
ATOM   310  C  CD  . LYS   A 1 45  ? 9.919   39.561 28.517 1.00 44.39 ? 45  LYS   A CD  1 
ATOM   311  C  CE  . LYS   A 1 45  ? 9.439   38.186 29.021 1.00 54.18 ? 45  LYS   A CE  1 
ATOM   312  N  NZ  . LYS   A 1 45  ? 8.606   38.131 30.230 1.00 54.15 ? 45  LYS   A NZ  1 
ATOM   313  N  N   . LYS   A 1 46  ? 14.369  39.017 26.167 1.00 22.71 ? 46  LYS   A N   1 
ATOM   314  C  CA  . LYS   A 1 46  ? 15.252  40.093 25.751 1.00 23.80 ? 46  LYS   A CA  1 
ATOM   315  C  C   . LYS   A 1 46  ? 15.769  39.828 24.348 1.00 23.57 ? 46  LYS   A C   1 
ATOM   316  O  O   . LYS   A 1 46  ? 15.884  40.766 23.561 1.00 25.98 ? 46  LYS   A O   1 
ATOM   317  C  CB  . LYS   A 1 46  ? 16.333  40.325 26.797 1.00 24.34 ? 46  LYS   A CB  1 
ATOM   318  C  CG  . LYS   A 1 46  ? 17.444  41.279 26.361 1.00 26.43 ? 46  LYS   A CG  1 
ATOM   319  C  CD  . LYS   A 1 46  ? 18.359  41.647 27.512 1.00 28.00 ? 46  LYS   A CD  1 
ATOM   320  C  CE  . LYS   A 1 46  ? 19.476  42.569 27.039 1.00 33.16 ? 46  LYS   A CE  1 
ATOM   321  N  NZ  . LYS   A 1 46  ? 20.212  42.922 28.264 1.00 39.91 ? 46  LYS   A NZ  1 
ATOM   322  N  N   . TYR   A 1 47  ? 16.179  38.583 24.070 1.00 22.75 ? 47  TYR   A N   1 
ATOM   323  C  CA  . TYR   A 1 47  ? 16.852  38.244 22.838 1.00 23.83 ? 47  TYR   A CA  1 
ATOM   324  C  C   . TYR   A 1 47  ? 15.878  37.756 21.761 1.00 23.10 ? 47  TYR   A C   1 
ATOM   325  O  O   . TYR   A 1 47  ? 16.352  37.370 20.682 1.00 25.51 ? 47  TYR   A O   1 
ATOM   326  C  CB  . TYR   A 1 47  ? 18.017  37.292 23.110 1.00 22.78 ? 47  TYR   A CB  1 
ATOM   327  C  CG  . TYR   A 1 47  ? 19.117  38.062 23.811 1.00 21.90 ? 47  TYR   A CG  1 
ATOM   328  C  CD1 . TYR   A 1 47  ? 19.889  38.961 23.097 1.00 23.46 ? 47  TYR   A CD1 1 
ATOM   329  C  CD2 . TYR   A 1 47  ? 19.341  37.971 25.190 1.00 22.69 ? 47  TYR   A CD2 1 
ATOM   330  C  CE1 . TYR   A 1 47  ? 20.864  39.734 23.705 1.00 23.02 ? 47  TYR   A CE1 1 
ATOM   331  C  CE2 . TYR   A 1 47  ? 20.294  38.766 25.821 1.00 22.80 ? 47  TYR   A CE2 1 
ATOM   332  C  CZ  . TYR   A 1 47  ? 21.097  39.593 25.057 1.00 25.35 ? 47  TYR   A CZ  1 
ATOM   333  O  OH  . TYR   A 1 47  ? 22.053  40.362 25.609 1.00 23.53 ? 47  TYR   A OH  1 
ATOM   334  N  N   . GLY   A 1 48  ? 14.567  37.839 22.007 1.00 25.71 ? 48  GLY   A N   1 
ATOM   335  C  CA  . GLY   A 1 48  ? 13.599  37.653 20.914 1.00 28.33 ? 48  GLY   A CA  1 
ATOM   336  C  C   . GLY   A 1 48  ? 13.301  36.196 20.576 1.00 27.20 ? 48  GLY   A C   1 
ATOM   337  O  O   . GLY   A 1 48  ? 12.808  35.889 19.500 1.00 24.71 ? 48  GLY   A O   1 
ATOM   338  N  N   . ILE   A 1 49  ? 13.536  35.272 21.511 1.00 23.43 ? 49  ILE   A N   1 
ATOM   339  C  CA  . ILE   A 1 49  ? 13.124  33.903 21.315 1.00 23.57 ? 49  ILE   A CA  1 
ATOM   340  C  C   . ILE   A 1 49  ? 11.588  33.910 21.219 1.00 26.03 ? 49  ILE   A C   1 
ATOM   341  O  O   . ILE   A 1 49  ? 10.872  34.598 21.969 1.00 26.37 ? 49  ILE   A O   1 
ATOM   342  C  CB  . ILE   A 1 49  ? 13.667  33.006 22.458 1.00 26.11 ? 49  ILE   A CB  1 
ATOM   343  C  CG1 . ILE   A 1 49  ? 15.144  32.639 22.236 1.00 24.49 ? 49  ILE   A CG1 1 
ATOM   344  C  CG2 . ILE   A 1 49  ? 12.856  31.721 22.570 1.00 25.69 ? 49  ILE   A CG2 1 
ATOM   345  C  CD1 . ILE   A 1 49  ? 16.159  33.785 22.115 1.00 26.56 ? 49  ILE   A CD1 1 
ATOM   346  N  N   . VAL   A 1 50  ? 11.086  33.133 20.274 1.00 25.39 ? 50  VAL   A N   1 
ATOM   347  C  CA  . VAL   A 1 50  ? 9.669   33.088 19.929 1.00 27.42 ? 50  VAL   A CA  1 
ATOM   348  C  C   . VAL   A 1 50  ? 8.954   32.062 20.812 1.00 25.05 ? 50  VAL   A C   1 
ATOM   349  O  O   . VAL   A 1 50  ? 7.861   32.332 21.287 1.00 27.33 ? 50  VAL   A O   1 
ATOM   350  C  CB  . VAL   A 1 50  ? 9.518   32.729 18.434 1.00 31.44 ? 50  VAL   A CB  1 
ATOM   351  C  CG1 . VAL   A 1 50  ? 8.063   32.530 18.069 1.00 40.64 ? 50  VAL   A CG1 1 
ATOM   352  C  CG2 . VAL   A 1 50  ? 10.147  33.805 17.556 1.00 36.62 ? 50  VAL   A CG2 1 
ATOM   353  N  N   . ARG   A 1 51  ? 9.590   30.912 21.070 1.00 23.73 ? 51  ARG   A N   1 
ATOM   354  C  CA  . ARG   A 1 51  ? 8.983   29.863 21.864 1.00 23.75 ? 51  ARG   A CA  1 
ATOM   355  C  C   . ARG   A 1 51  ? 10.094  29.090 22.561 1.00 21.46 ? 51  ARG   A C   1 
ATOM   356  O  O   . ARG   A 1 51  ? 11.163  28.856 21.992 1.00 22.15 ? 51  ARG   A O   1 
ATOM   357  C  CB  . ARG   A 1 51  ? 8.178   28.932 20.938 1.00 26.39 ? 51  ARG   A CB  1 
ATOM   358  C  CG  . ARG   A 1 51  ? 7.369   27.891 21.698 1.00 31.42 ? 51  ARG   A CG  1 
ATOM   359  C  CD  . ARG   A 1 51  ? 6.543   27.028 20.695 1.00 36.79 ? 51  ARG   A CD  1 
ATOM   360  N  NE  . ARG   A 1 51  ? 5.353   26.509 21.376 1.00 45.94 ? 51  ARG   A NE  1 
ATOM   361  C  CZ  . ARG   A 1 51  ? 4.193   27.159 21.625 1.00 48.50 ? 51  ARG   A CZ  1 
ATOM   362  N  NH1 . ARG   A 1 51  ? 3.932   28.369 21.123 1.00 46.87 ? 51  ARG   A NH1 1 
ATOM   363  N  NH2 . ARG   A 1 51  ? 3.254   26.544 22.333 1.00 46.00 ? 51  ARG   A NH2 1 
ATOM   364  N  N   . TYR   A 1 52  ? 9.822   28.712 23.800 1.00 22.37 ? 52  TYR   A N   1 
ATOM   365  C  CA  . TYR   A 1 52  ? 10.740  27.875 24.566 1.00 20.56 ? 52  TYR   A CA  1 
ATOM   366  C  C   . TYR   A 1 52  ? 9.952   26.733 25.189 1.00 21.72 ? 52  TYR   A C   1 
ATOM   367  O  O   . TYR   A 1 52  ? 8.933   26.993 25.841 1.00 23.00 ? 52  TYR   A O   1 
ATOM   368  C  CB  . TYR   A 1 52  ? 11.364  28.744 25.661 1.00 21.91 ? 52  TYR   A CB  1 
ATOM   369  C  CG  . TYR   A 1 52  ? 12.353  28.081 26.590 1.00 19.39 ? 52  TYR   A CG  1 
ATOM   370  C  CD1 . TYR   A 1 52  ? 13.543  27.620 26.082 1.00 21.65 ? 52  TYR   A CD1 1 
ATOM   371  C  CD2 . TYR   A 1 52  ? 12.174  28.064 27.971 1.00 20.50 ? 52  TYR   A CD2 1 
ATOM   372  C  CE1 . TYR   A 1 52  ? 14.543  27.145 26.901 1.00 23.58 ? 52  TYR   A CE1 1 
ATOM   373  C  CE2 . TYR   A 1 52  ? 13.169  27.570 28.801 1.00 19.08 ? 52  TYR   A CE2 1 
ATOM   374  C  CZ  . TYR   A 1 52  ? 14.336  27.084 28.258 1.00 23.48 ? 52  TYR   A CZ  1 
ATOM   375  O  OH  . TYR   A 1 52  ? 15.393  26.648 29.008 1.00 26.39 ? 52  TYR   A OH  1 
ATOM   376  N  N   . THR   A 1 53  ? 10.424  25.519 24.933 1.00 20.99 ? 53  THR   A N   1 
ATOM   377  C  CA  . THR   A 1 53  ? 9.754   24.310 25.391 1.00 21.37 ? 53  THR   A CA  1 
ATOM   378  C  C   . THR   A 1 53  ? 10.734  23.480 26.205 1.00 22.53 ? 53  THR   A C   1 
ATOM   379  O  O   . THR   A 1 53  ? 11.885  23.290 25.815 1.00 22.28 ? 53  THR   A O   1 
ATOM   380  C  CB  . THR   A 1 53  ? 9.225   23.516 24.198 1.00 22.27 ? 53  THR   A CB  1 
ATOM   381  O  OG1 . THR   A 1 53  ? 8.311   24.425 23.553 1.00 24.00 ? 53  THR   A OG1 1 
ATOM   382  C  CG2 . THR   A 1 53  ? 8.477   22.302 24.706 1.00 28.75 ? 53  THR   A CG2 1 
ATOM   383  N  N   . VAL   A 1 54  ? 10.250  22.960 27.332 1.00 20.86 ? 54  VAL   A N   1 
ATOM   384  C  CA  . VAL   A 1 54  ? 11.085  22.092 28.204 1.00 18.71 ? 54  VAL   A CA  1 
ATOM   385  C  C   . VAL   A 1 54  ? 10.381  20.729 28.292 1.00 19.13 ? 54  VAL   A C   1 
ATOM   386  O  O   . VAL   A 1 54  ? 9.252   20.692 28.765 1.00 20.33 ? 54  VAL   A O   1 
ATOM   387  C  CB  . VAL   A 1 54  ? 11.339  22.688 29.601 1.00 24.29 ? 54  VAL   A CB  1 
ATOM   388  C  CG1 . VAL   A 1 54  ? 12.302  21.833 30.409 1.00 23.70 ? 54  VAL   A CG1 1 
ATOM   389  C  CG2 . VAL   A 1 54  ? 11.825  24.127 29.514 1.00 25.49 ? 54  VAL   A CG2 1 
ATOM   390  N  N   . LYS   A 1 55  ? 11.047  19.687 27.819 1.00 19.35 ? 55  LYS   A N   1 
ATOM   391  C  CA  . LYS   A 1 55  ? 10.441  18.338 27.792 1.00 21.27 ? 55  LYS   A CA  1 
ATOM   392  C  C   . LYS   A 1 55  ? 11.083  17.489 28.892 1.00 20.87 ? 55  LYS   A C   1 
ATOM   393  O  O   . LYS   A 1 55  ? 12.311  17.400 28.917 1.00 23.57 ? 55  LYS   A O   1 
ATOM   394  C  CB  . LYS   A 1 55  ? 10.592  17.723 26.397 1.00 24.43 ? 55  LYS   A CB  1 
ATOM   395  C  CG  . LYS   A 1 55  ? 10.063  18.614 25.286 1.00 27.83 ? 55  LYS   A CG  1 
ATOM   396  C  CD  . LYS   A 1 55  ? 9.966   17.949 23.921 1.00 34.65 ? 55  LYS   A CD  1 
ATOM   397  C  CE  . LYS   A 1 55  ? 11.204  17.212 23.550 1.00 38.87 ? 55  LYS   A CE  1 
ATOM   398  N  NZ  . LYS   A 1 55  ? 11.097  16.631 22.211 1.00 49.59 ? 55  LYS   A NZ  1 
ATOM   399  N  N   . HIS   A 1 56  ? 10.251  16.870 29.723 1.00 19.68 ? 56  HIS   A N   1 
ATOM   400  C  CA  . HIS   A 1 56  ? 10.741  16.070 30.866 1.00 18.20 ? 56  HIS   A CA  1 
ATOM   401  C  C   . HIS   A 1 56  ? 10.479  14.572 30.672 1.00 19.60 ? 56  HIS   A C   1 
ATOM   402  O  O   . HIS   A 1 56  ? 9.376   14.210 30.286 1.00 19.76 ? 56  HIS   A O   1 
ATOM   403  C  CB  . HIS   A 1 56  ? 10.065  16.553 32.150 1.00 20.51 ? 56  HIS   A CB  1 
ATOM   404  C  CG  . HIS   A 1 56  ? 10.122  18.015 32.422 1.00 21.53 ? 56  HIS   A CG  1 
ATOM   405  N  ND1 . HIS   A 1 56  ? 11.021  18.552 33.314 1.00 23.46 ? 56  HIS   A ND1 1 
ATOM   406  C  CD2 . HIS   A 1 56  ? 9.387   19.036 31.979 1.00 24.10 ? 56  HIS   A CD2 1 
ATOM   407  C  CE1 . HIS   A 1 56  ? 10.836  19.857 33.385 1.00 24.16 ? 56  HIS   A CE1 1 
ATOM   408  N  NE2 . HIS   A 1 56  ? 9.848   20.172 32.587 1.00 22.66 ? 56  HIS   A NE2 1 
ATOM   409  N  N   . ASN   A 1 57  ? 11.483  13.751 30.937 1.00 21.08 ? 57  ASN   A N   1 
ATOM   410  C  CA  . ASN   A 1 57  ? 11.386  12.299 30.875 1.00 20.49 ? 57  ASN   A CA  1 
ATOM   411  C  C   . ASN   A 1 57  ? 11.606  11.747 32.277 1.00 20.68 ? 57  ASN   A C   1 
ATOM   412  O  O   . ASN   A 1 57  ? 12.742  11.433 32.667 1.00 23.95 ? 57  ASN   A O   1 
ATOM   413  C  CB  . ASN   A 1 57  ? 12.323  11.769 29.797 1.00 21.84 ? 57  ASN   A CB  1 
ATOM   414  C  CG  . ASN   A 1 57  ? 12.579  10.284 29.897 1.00 29.22 ? 57  ASN   A CG  1 
ATOM   415  O  OD1 . ASN   A 1 57  ? 11.667  9.513  30.231 1.00 24.01 ? 57  ASN   A OD1 1 
ATOM   416  N  ND2 . ASN   A 1 57  ? 13.829  9.866  29.718 1.00 29.77 ? 57  ASN   A ND2 1 
ATOM   417  N  N   . ASP   A 1 58  ? 10.485  11.612 33.001 1.00 21.97 ? 58  ASP   A N   1 
ATOM   418  C  CA  . ASP   A 1 58  ? 10.556  11.225 34.402 1.00 23.02 ? 58  ASP   A CA  1 
ATOM   419  C  C   . ASP   A 1 58  ? 9.446   10.228 34.774 1.00 27.45 ? 58  ASP   A C   1 
ATOM   420  O  O   . ASP   A 1 58  ? 8.769   9.659  33.903 1.00 23.35 ? 58  ASP   A O   1 
ATOM   421  C  CB  . ASP   A 1 58  ? 10.508  12.474 35.252 1.00 19.33 ? 58  ASP   A CB  1 
ATOM   422  C  CG  . ASP   A 1 58  ? 9.199   13.224 35.271 1.00 22.66 ? 58  ASP   A CG  1 
ATOM   423  O  OD1 . ASP   A 1 58  ? 8.195   12.718 34.658 1.00 23.42 ? 58  ASP   A OD1 1 
ATOM   424  O  OD2 . ASP   A 1 58  ? 9.128   14.296 35.935 1.00 24.22 ? 58  ASP   A OD2 1 
ATOM   425  N  N   . ALA   A 1 59  ? 9.235   10.052 36.095 1.00 26.50 ? 59  ALA   A N   1 
ATOM   426  C  CA  . ALA   A 1 59  ? 8.308   9.017  36.555 1.00 28.32 ? 59  ALA   A CA  1 
ATOM   427  C  C   . ALA   A 1 59  ? 6.888   9.299  36.106 1.00 25.05 ? 59  ALA   A C   1 
ATOM   428  O  O   . ALA   A 1 59  ? 6.129   8.327  35.897 1.00 28.41 ? 59  ALA   A O   1 
ATOM   429  C  CB  . ALA   A 1 59  ? 8.372   8.864  38.092 1.00 29.05 ? 59  ALA   A CB  1 
ATOM   430  N  N   . TYR   A 1 60  ? 6.517   10.563 35.910 1.00 20.76 ? 60  TYR   A N   1 
ATOM   431  C  CA  . TYR   A 1 60  ? 5.217   10.956 35.427 1.00 23.00 ? 60  TYR   A CA  1 
ATOM   432  C  C   . TYR   A 1 60  ? 4.976   10.541 33.968 1.00 24.98 ? 60  TYR   A C   1 
ATOM   433  O  O   . TYR   A 1 60  ? 3.908   10.040 33.621 1.00 23.11 ? 60  TYR   A O   1 
ATOM   434  C  CB  . TYR   A 1 60  ? 4.937   12.430 35.617 1.00 24.07 ? 60  TYR   A CB  1 
ATOM   435  C  CG  . TYR   A 1 60  ? 3.620   12.890 35.057 1.00 24.90 ? 60  TYR   A CG  1 
ATOM   436  C  CD1 . TYR   A 1 60  ? 2.459   12.691 35.798 1.00 31.71 ? 60  TYR   A CD1 1 
ATOM   437  C  CD2 . TYR   A 1 60  ? 3.490   13.387 33.759 1.00 25.64 ? 60  TYR   A CD2 1 
ATOM   438  C  CE1 . TYR   A 1 60  ? 1.235   13.104 35.325 1.00 31.93 ? 60  TYR   A CE1 1 
ATOM   439  C  CE2 . TYR   A 1 60  ? 2.270   13.823 33.285 1.00 27.19 ? 60  TYR   A CE2 1 
ATOM   440  C  CZ  . TYR   A 1 60  ? 1.126   13.583 34.039 1.00 31.93 ? 60  TYR   A CZ  1 
ATOM   441  O  OH  . TYR   A 1 60  ? -0.097  13.988 33.602 1.00 32.81 ? 60  TYR   A OH  1 
ATOM   442  N  N   . SER   A 1 61  ? 5.921   10.856 33.097 1.00 22.26 ? 61  SER   A N   1 
ATOM   443  C  CA  . SER   A 1 61  ? 5.815   10.610 31.666 1.00 22.74 ? 61  SER   A CA  1 
ATOM   444  C  C   . SER   A 1 61  ? 6.136   9.164  31.274 1.00 21.25 ? 61  SER   A C   1 
ATOM   445  O  O   . SER   A 1 61  ? 5.665   8.694  30.228 1.00 21.61 ? 61  SER   A O   1 
ATOM   446  C  CB  . SER   A 1 61  ? 6.782   11.649 30.943 1.00 19.79 ? 61  SER   A CB  1 
ATOM   447  O  OG  . SER   A 1 61  ? 8.140   11.343 31.241 1.00 21.66 ? 61  SER   A OG  1 
ATOM   448  N  N   . LYS   A 1 62  ? 6.980   8.448  32.030 1.00 20.33 ? 62  LYS   A N   1 
ATOM   449  C  CA  . LYS   A 1 62  ? 7.554   7.182  31.617 1.00 23.73 ? 62  LYS   A CA  1 
ATOM   450  C  C   . LYS   A 1 62  ? 6.467   6.134  31.257 1.00 23.47 ? 62  LYS   A C   1 
ATOM   451  O  O   . LYS   A 1 62  ? 6.617   5.434  30.254 1.00 21.32 ? 62  LYS   A O   1 
ATOM   452  C  CB  . LYS   A 1 62  ? 8.578   6.635  32.613 1.00 28.34 ? 62  LYS   A CB  1 
ATOM   453  C  CG  . LYS   A 1 62  ? 9.992   7.239  32.377 1.00 36.23 ? 62  LYS   A CG  1 
ATOM   454  C  CD  . LYS   A 1 62  ? 10.997  6.864  33.466 1.00 38.97 ? 62  LYS   A CD  1 
ATOM   455  C  CE  . LYS   A 1 62  ? 12.168  7.770  33.518 1.00 42.90 ? 62  LYS   A CE  1 
ATOM   456  N  NZ  . LYS   A 1 62  ? 12.764  7.775  32.188 1.00 39.18 ? 62  LYS   A NZ  1 
ATOM   457  N  N   . PRO   A 1 63  ? 5.347   5.985  32.008 1.00 24.91 ? 63  PRO   A N   1 
ATOM   458  C  CA  . PRO   A 1 63  ? 4.288   5.029  31.601 1.00 25.14 ? 63  PRO   A CA  1 
ATOM   459  C  C   . PRO   A 1 63  ? 3.621   5.410  30.281 1.00 24.79 ? 63  PRO   A C   1 
ATOM   460  O  O   . PRO   A 1 63  ? 3.210   4.542  29.488 1.00 23.06 ? 63  PRO   A O   1 
ATOM   461  C  CB  . PRO   A 1 63  ? 3.287   5.049  32.804 1.00 25.38 ? 63  PRO   A CB  1 
ATOM   462  C  CG  . PRO   A 1 63  ? 4.137   5.514  33.963 1.00 28.32 ? 63  PRO   A CG  1 
ATOM   463  C  CD  . PRO   A 1 63  ? 5.078   6.573  33.340 1.00 25.35 ? 63  PRO   A CD  1 
ATOM   464  N  N   . LYS   A 1 64  ? 3.578   6.721  29.994 1.00 21.32 ? 64  LYS   A N   1 
ATOM   465  C  CA  . LYS   A 1 64  ? 2.984   7.259  28.780 1.00 23.48 ? 64  LYS   A CA  1 
ATOM   466  C  C   . LYS   A 1 64  ? 3.907   6.938  27.613 1.00 24.81 ? 64  LYS   A C   1 
ATOM   467  O  O   . LYS   A 1 64  ? 3.471   6.472  26.556 1.00 22.65 ? 64  LYS   A O   1 
ATOM   468  C  CB  . LYS   A 1 64  ? 2.645   8.745  28.963 1.00 24.92 ? 64  LYS   A CB  1 
ATOM   469  C  CG  . LYS   A 1 64  ? 1.623   8.892  30.123 1.00 32.29 ? 64  LYS   A CG  1 
ATOM   470  C  CD  . LYS   A 1 64  ? 1.449   10.288 30.683 1.00 40.42 ? 64  LYS   A CD  1 
ATOM   471  C  CE  . LYS   A 1 64  ? 0.331   10.446 31.665 1.00 38.33 ? 64  LYS   A CE  1 
ATOM   472  N  NZ  . LYS   A 1 64  ? 0.782   9.923  32.937 1.00 43.25 ? 64  LYS   A NZ  1 
ATOM   473  N  N   . GLN   A 1 65  ? 5.206   7.199  27.799 1.00 21.50 ? 65  GLN   A N   1 
ATOM   474  C  CA  . GLN   A 1 65  ? 6.195   6.790  26.815 1.00 22.24 ? 65  GLN   A CA  1 
ATOM   475  C  C   . GLN   A 1 65  ? 6.197   5.283  26.556 1.00 21.87 ? 65  GLN   A C   1 
ATOM   476  O  O   . GLN   A 1 65  ? 6.314   4.848  25.407 1.00 21.58 ? 65  GLN   A O   1 
ATOM   477  C  CB  . GLN   A 1 65  ? 7.581   7.209  27.328 1.00 21.53 ? 65  GLN   A CB  1 
ATOM   478  C  CG  . GLN   A 1 65  ? 8.730   6.753  26.446 1.00 21.90 ? 65  GLN   A CG  1 
ATOM   479  C  CD  . GLN   A 1 65  ? 10.025  7.440  26.868 1.00 25.72 ? 65  GLN   A CD  1 
ATOM   480  O  OE1 . GLN   A 1 65  ? 10.400  8.500  26.350 1.00 22.46 ? 65  GLN   A OE1 1 
ATOM   481  N  NE2 . GLN   A 1 65  ? 10.654  6.908  27.904 1.00 26.49 ? 65  GLN   A NE2 1 
ATOM   482  N  N   . ALA   A 1 66  ? 6.108   4.468  27.616 1.00 21.02 ? 66  ALA   A N   1 
ATOM   483  C  CA  . ALA   A 1 66  ? 6.112   3.010  27.461 1.00 23.08 ? 66  ALA   A CA  1 
ATOM   484  C  C   . ALA   A 1 66  ? 4.896   2.567  26.630 1.00 21.43 ? 66  ALA   A C   1 
ATOM   485  O  O   . ALA   A 1 66  ? 5.047   1.659  25.841 1.00 25.32 ? 66  ALA   A O   1 
ATOM   486  C  CB  . ALA   A 1 66  ? 6.105   2.319  28.803 1.00 22.75 ? 66  ALA   A CB  1 
ATOM   487  N  N   . ALA   A 1 67  ? 3.765   3.239  26.781 1.00 21.35 ? 67  ALA   A N   1 
ATOM   488  C  CA  . ALA   A 1 67  ? 2.574   2.929  26.011 1.00 23.53 ? 67  ALA   A CA  1 
ATOM   489  C  C   . ALA   A 1 67  ? 2.770   3.340  24.556 1.00 25.05 ? 67  ALA   A C   1 
ATOM   490  O  O   . ALA   A 1 67  ? 2.525   2.562  23.664 1.00 23.95 ? 67  ALA   A O   1 
ATOM   491  C  CB  . ALA   A 1 67  ? 1.359   3.608  26.571 1.00 25.71 ? 67  ALA   A CB  1 
ATOM   492  N  N   . LEU   A 1 68  ? 3.258   4.551  24.306 1.00 20.38 ? 68  LEU   A N   1 
ATOM   493  C  CA  . LEU   A 1 68  ? 3.486   5.028  22.931 1.00 22.24 ? 68  LEU   A CA  1 
ATOM   494  C  C   . LEU   A 1 68  ? 4.515   4.170  22.211 1.00 21.70 ? 68  LEU   A C   1 
ATOM   495  O  O   . LEU   A 1 68  ? 4.439   3.972  20.995 1.00 23.78 ? 68  LEU   A O   1 
ATOM   496  C  CB  . LEU   A 1 68  ? 3.928   6.498  22.973 1.00 24.12 ? 68  LEU   A CB  1 
ATOM   497  C  CG  . LEU   A 1 68  ? 2.888   7.558  23.354 1.00 26.54 ? 68  LEU   A CG  1 
ATOM   498  C  CD1 . LEU   A 1 68  ? 3.568   8.856  23.813 1.00 29.09 ? 68  LEU   A CD1 1 
ATOM   499  C  CD2 . LEU   A 1 68  ? 1.960   7.898  22.232 1.00 29.44 ? 68  LEU   A CD2 1 
ATOM   500  N  N   . MET   A 1 69  ? 5.519   3.660  22.935 1.00 21.06 ? 69  MET   A N   1 
ATOM   501  C  CA  . MET   A 1 69  ? 6.629   2.964  22.321 1.00 22.32 ? 69  MET   A CA  1 
ATOM   502  C  C   . MET   A 1 69  ? 6.458   1.450  22.466 1.00 22.60 ? 69  MET   A C   1 
ATOM   503  O  O   . MET   A 1 69  ? 7.398   0.701  22.309 1.00 21.63 ? 69  MET   A O   1 
ATOM   504  C  CB  . MET   A 1 69  ? 7.968   3.427  22.930 1.00 23.64 ? 69  MET   A CB  1 
ATOM   505  C  CG  . MET   A 1 69  ? 8.253   4.908  22.730 1.00 25.60 ? 69  MET   A CG  1 
ATOM   506  S  SD  . MET   A 1 69  ? 8.426   5.322  20.985 1.00 26.55 ? 69  MET   A SD  1 
ATOM   507  C  CE  . MET   A 1 69  ? 9.982   4.496  20.662 1.00 24.60 ? 69  MET   A CE  1 
ATOM   508  N  N   . ALA   A 1 70  ? 5.238   0.973  22.772 1.00 24.33 ? 70  ALA   A N   1 
ATOM   509  C  CA  . ALA   A 1 70  ? 4.999   -0.451 22.976 1.00 26.52 ? 70  ALA   A CA  1 
ATOM   510  C  C   . ALA   A 1 70  ? 5.367   -1.199 21.698 1.00 20.48 ? 70  ALA   A C   1 
ATOM   511  O  O   . ALA   A 1 70  ? 5.035   -0.735 20.619 1.00 25.46 ? 70  ALA   A O   1 
ATOM   512  C  CB  . ALA   A 1 70  ? 3.526   -0.639 23.240 1.00 29.02 ? 70  ALA   A CB  1 
ATOM   513  N  N   . GLY   A 1 71  ? 6.129   -2.252 21.843 1.00 22.74 ? 71  GLY   A N   1 
ATOM   514  C  CA  . GLY   A 1 71  ? 6.532   -3.033 20.691 1.00 25.81 ? 71  GLY   A CA  1 
ATOM   515  C  C   . GLY   A 1 71  ? 7.807   -2.515 20.049 1.00 29.13 ? 71  GLY   A C   1 
ATOM   516  O  O   . GLY   A 1 71  ? 8.314   -3.136 19.115 1.00 25.28 ? 71  GLY   A O   1 
ATOM   517  N  N   . GLN   A 1 72  ? 8.317   -1.365 20.521 1.00 29.11 ? 72  GLN   A N   1 
ATOM   518  C  CA  . GLN   A 1 72  ? 9.608   -0.896 20.035 1.00 30.10 ? 72  GLN   A CA  1 
ATOM   519  C  C   . GLN   A 1 72  ? 10.750  -1.467 20.868 1.00 29.52 ? 72  GLN   A C   1 
ATOM   520  O  O   . GLN   A 1 72  ? 10.690  -1.578 22.071 1.00 31.06 ? 72  GLN   A O   1 
ATOM   521  C  CB  . GLN   A 1 72  ? 9.614   0.631  20.066 1.00 28.00 ? 72  GLN   A CB  1 
ATOM   522  C  CG  . GLN   A 1 72  ? 8.499   1.315  19.274 1.00 26.02 ? 72  GLN   A CG  1 
ATOM   523  C  CD  . GLN   A 1 72  ? 8.476   0.969  17.796 1.00 31.07 ? 72  GLN   A CD  1 
ATOM   524  O  OE1 . GLN   A 1 72  ? 9.514   0.646  17.232 1.00 32.72 ? 72  GLN   A OE1 1 
ATOM   525  N  NE2 . GLN   A 1 72  ? 7.315   1.118  17.166 1.00 32.69 ? 72  GLN   A NE2 1 
ATOM   526  N  N   . PRO   A 1 73  ? 11.906  -1.748 20.243 1.00 37.89 ? 73  PRO   A N   1 
ATOM   527  C  CA  . PRO   A 1 73  ? 13.126  -2.067 20.986 1.00 37.39 ? 73  PRO   A CA  1 
ATOM   528  C  C   . PRO   A 1 73  ? 13.541  -0.934 21.931 1.00 34.75 ? 73  PRO   A C   1 
ATOM   529  O  O   . PRO   A 1 73  ? 13.396  0.248  21.586 1.00 31.59 ? 73  PRO   A O   1 
ATOM   530  C  CB  . PRO   A 1 73  ? 14.198  -2.297 19.885 1.00 39.77 ? 73  PRO   A CB  1 
ATOM   531  C  CG  . PRO   A 1 73  ? 13.533  -2.091 18.543 1.00 43.19 ? 73  PRO   A CG  1 
ATOM   532  C  CD  . PRO   A 1 73  ? 12.105  -1.626 18.792 1.00 40.91 ? 73  PRO   A CD  1 
ATOM   533  N  N   . GLU   A 1 74  ? 14.044  -1.288 23.113 1.00 33.71 ? 74  GLU   A N   1 
ATOM   534  C  CA  . GLU   A 1 74  ? 14.371  -0.329 24.158 1.00 35.64 ? 74  GLU   A CA  1 
ATOM   535  C  C   . GLU   A 1 74  ? 15.413  0.676  23.651 1.00 28.98 ? 74  GLU   A C   1 
ATOM   536  O  O   . GLU   A 1 74  ? 15.406  1.836  24.039 1.00 33.09 ? 74  GLU   A O   1 
ATOM   537  C  CB  . GLU   A 1 74  ? 14.882  -0.993 25.443 1.00 43.67 ? 74  GLU   A CB  1 
ATOM   538  N  N   . GLU   A 1 75  ? 16.308  0.228  22.776 1.00 30.75 ? 75  GLU   A N   1 
ATOM   539  C  CA  . GLU   A 1 75  ? 17.352  1.094  22.256 1.00 38.63 ? 75  GLU   A CA  1 
ATOM   540  C  C   . GLU   A 1 75  ? 16.760  2.201  21.376 1.00 41.07 ? 75  GLU   A C   1 
ATOM   541  O  O   . GLU   A 1 75  ? 17.435  3.216  21.152 1.00 33.52 ? 75  GLU   A O   1 
ATOM   542  C  CB  . GLU   A 1 75  ? 18.367  0.315  21.427 1.00 40.47 ? 75  GLU   A CB  1 
ATOM   543  C  CG  . GLU   A 1 75  ? 17.695  -0.239 20.183 1.00 50.57 ? 75  GLU   A CG  1 
ATOM   544  C  CD  . GLU   A 1 75  ? 18.295  -1.492 19.609 1.00 61.25 ? 75  GLU   A CD  1 
ATOM   545  O  OE1 . GLU   A 1 75  ? 19.268  -1.365 18.831 1.00 63.92 ? 75  GLU   A OE1 1 
ATOM   546  O  OE2 . GLU   A 1 75  ? 17.771  -2.571 19.958 1.00 68.29 ? 75  GLU   A OE2 1 
ATOM   547  N  N   . ASN   A 1 76  ? 15.504  2.043  20.900 1.00 32.20 ? 76  ASN   A N   1 
ATOM   548  C  CA  . ASN   A 1 76  ? 14.902  3.076  20.052 1.00 30.48 ? 76  ASN   A CA  1 
ATOM   549  C  C   . ASN   A 1 76  ? 14.147  4.140  20.829 1.00 26.48 ? 76  ASN   A C   1 
ATOM   550  O  O   . ASN   A 1 76  ? 13.511  5.038  20.233 1.00 24.62 ? 76  ASN   A O   1 
ATOM   551  C  CB  . ASN   A 1 76  ? 14.046  2.429  18.991 1.00 34.29 ? 76  ASN   A CB  1 
ATOM   552  C  CG  . ASN   A 1 76  ? 14.909  1.647  18.028 1.00 42.43 ? 76  ASN   A CG  1 
ATOM   553  O  OD1 . ASN   A 1 76  ? 16.139  1.812  18.001 1.00 41.50 ? 76  ASN   A OD1 1 
ATOM   554  N  ND2 . ASN   A 1 76  ? 14.274  0.813  17.230 1.00 44.21 ? 76  ASN   A ND2 1 
ATOM   555  N  N   . VAL   A 1 77  ? 14.200  4.055  22.166 1.00 22.98 ? 77  VAL   A N   1 
ATOM   556  C  CA  . VAL   A 1 77  ? 13.645  5.055  23.016 1.00 24.88 ? 77  VAL   A CA  1 
ATOM   557  C  C   . VAL   A 1 77  ? 14.762  6.029  23.440 1.00 31.34 ? 77  VAL   A C   1 
ATOM   558  O  O   . VAL   A 1 77  ? 15.769  5.588  23.993 1.00 32.79 ? 77  VAL   A O   1 
ATOM   559  C  CB  . VAL   A 1 77  ? 13.022  4.428  24.268 1.00 25.74 ? 77  VAL   A CB  1 
ATOM   560  C  CG1 . VAL   A 1 77  ? 12.303  5.489  25.072 1.00 28.70 ? 77  VAL   A CG1 1 
ATOM   561  C  CG2 . VAL   A 1 77  ? 12.026  3.315  23.918 1.00 25.62 ? 77  VAL   A CG2 1 
ATOM   562  N  N   . LEU   A 1 78  ? 14.555  7.332  23.247 1.00 32.43 ? 78  LEU   A N   1 
ATOM   563  C  CA  . LEU   A 1 78  ? 15.491  8.366  23.749 1.00 29.09 ? 78  LEU   A CA  1 
ATOM   564  C  C   . LEU   A 1 78  ? 15.563  8.469  25.274 1.00 33.58 ? 78  LEU   A C   1 
ATOM   565  O  O   . LEU   A 1 78  ? 14.566  8.400  26.019 1.00 40.26 ? 78  LEU   A O   1 
ATOM   566  C  CB  . LEU   A 1 78  ? 15.090  9.702  23.161 1.00 30.14 ? 78  LEU   A CB  1 
ATOM   567  C  CG  . LEU   A 1 78  ? 15.414  9.839  21.662 1.00 45.06 ? 78  LEU   A CG  1 
ATOM   568  C  CD1 . LEU   A 1 78  ? 15.760  11.299 21.379 1.00 50.91 ? 78  LEU   A CD1 1 
ATOM   569  C  CD2 . LEU   A 1 78  ? 16.511  8.922  21.134 1.00 41.86 ? 78  LEU   A CD2 1 
ATOM   570  N  N   . ALA   A 1 79  ? 16.781  8.617  25.781 1.00 37.05 ? 79  ALA   A N   1 
ATOM   571  C  CA  . ALA   A 1 79  ? 16.972  8.476  27.218 1.00 41.34 ? 79  ALA   A CA  1 
ATOM   572  C  C   . ALA   A 1 79  ? 17.102  9.833  27.920 1.00 40.64 ? 79  ALA   A C   1 
ATOM   573  O  O   . ALA   A 1 79  ? 17.190  9.873  29.184 1.00 37.73 ? 79  ALA   A O   1 
ATOM   574  C  CB  . ALA   A 1 79  ? 18.156  7.554  27.513 1.00 44.90 ? 79  ALA   A CB  1 
ATOM   575  N  N   . TYR   A 1 80  ? 17.005  10.952 27.177 1.00 26.71 ? 80  TYR   A N   1 
ATOM   576  C  CA  . TYR   A 1 80  ? 17.465  12.174 27.833 1.00 21.61 ? 80  TYR   A CA  1 
ATOM   577  C  C   . TYR   A 1 80  ? 16.528  12.564 28.987 1.00 20.37 ? 80  TYR   A C   1 
ATOM   578  O  O   . TYR   A 1 80  ? 15.317  12.493 28.895 1.00 22.52 ? 80  TYR   A O   1 
ATOM   579  C  CB  . TYR   A 1 80  ? 17.645  13.355 26.873 1.00 22.75 ? 80  TYR   A CB  1 
ATOM   580  C  CG  . TYR   A 1 80  ? 18.650  12.973 25.806 1.00 23.26 ? 80  TYR   A CG  1 
ATOM   581  C  CD1 . TYR   A 1 80  ? 20.016  13.014 26.058 1.00 26.25 ? 80  TYR   A CD1 1 
ATOM   582  C  CD2 . TYR   A 1 80  ? 18.219  12.527 24.563 1.00 27.11 ? 80  TYR   A CD2 1 
ATOM   583  C  CE1 . TYR   A 1 80  ? 20.940  12.599 25.109 1.00 28.00 ? 80  TYR   A CE1 1 
ATOM   584  C  CE2 . TYR   A 1 80  ? 19.138  12.145 23.598 1.00 28.54 ? 80  TYR   A CE2 1 
ATOM   585  C  CZ  . TYR   A 1 80  ? 20.487  12.195 23.872 1.00 30.60 ? 80  TYR   A CZ  1 
ATOM   586  O  OH  . TYR   A 1 80  ? 21.318  11.770 22.889 1.00 36.51 ? 80  TYR   A OH  1 
ATOM   587  N  N   . ASP   A 1 81  ? 17.081  13.083 30.095 1.00 19.75 ? 81  ASP   A N   1 
ATOM   588  C  CA  . ASP   A 1 81  ? 16.251  13.514 31.208 1.00 17.49 ? 81  ASP   A CA  1 
ATOM   589  C  C   . ASP   A 1 81  ? 15.425  14.737 30.868 1.00 20.11 ? 81  ASP   A C   1 
ATOM   590  O  O   . ASP   A 1 81  ? 14.243  14.790 31.171 1.00 19.89 ? 81  ASP   A O   1 
ATOM   591  C  CB  . ASP   A 1 81  ? 17.158  13.750 32.424 1.00 19.49 ? 81  ASP   A CB  1 
ATOM   592  C  CG  . ASP   A 1 81  ? 17.877  12.506 32.886 1.00 20.45 ? 81  ASP   A CG  1 
ATOM   593  O  OD1 . ASP   A 1 81  ? 17.174  11.627 33.491 1.00 24.35 ? 81  ASP   A OD1 1 
ATOM   594  O  OD2 . ASP   A 1 81  ? 19.067  12.354 32.614 1.00 21.23 ? 81  ASP   A OD2 1 
ATOM   595  N  N   . THR   A 1 82  ? 16.063  15.753 30.230 1.00 17.97 ? 82  THR   A N   1 
ATOM   596  C  CA  . THR   A 1 82  ? 15.394  16.978 29.869 1.00 19.70 ? 82  THR   A CA  1 
ATOM   597  C  C   . THR   A 1 82  ? 15.825  17.373 28.461 1.00 18.95 ? 82  THR   A C   1 
ATOM   598  O  O   . THR   A 1 82  ? 16.994  17.180 28.105 1.00 20.23 ? 82  THR   A O   1 
ATOM   599  C  CB  . THR   A 1 82  ? 15.788  18.071 30.883 1.00 22.52 ? 82  THR   A CB  1 
ATOM   600  O  OG1 . THR   A 1 82  ? 15.133  17.660 32.085 1.00 28.48 ? 82  THR   A OG1 1 
ATOM   601  C  CG2 . THR   A 1 82  ? 15.100  19.353 30.506 1.00 26.84 ? 82  THR   A CG2 1 
ATOM   602  N  N   . VAL   A 1 83  ? 14.883  17.931 27.707 1.00 21.33 ? 83  VAL   A N   1 
ATOM   603  C  CA  . VAL   A 1 83  ? 15.203  18.492 26.388 1.00 20.26 ? 83  VAL   A CA  1 
ATOM   604  C  C   . VAL   A 1 83  ? 14.654  19.894 26.347 1.00 21.61 ? 83  VAL   A C   1 
ATOM   605  O  O   . VAL   A 1 83  ? 13.501  20.155 26.695 1.00 23.54 ? 83  VAL   A O   1 
ATOM   606  C  CB  . VAL   A 1 83  ? 14.658  17.671 25.200 1.00 22.61 ? 83  VAL   A CB  1 
ATOM   607  C  CG1 . VAL   A 1 83  ? 15.058  18.316 23.860 1.00 23.27 ? 83  VAL   A CG1 1 
ATOM   608  C  CG2 . VAL   A 1 83  ? 15.101  16.232 25.287 1.00 22.30 ? 83  VAL   A CG2 1 
ATOM   609  N  N   . PHE   A 1 84  ? 15.507  20.857 25.939 1.00 19.64 ? 84  PHE   A N   1 
ATOM   610  C  CA  . PHE   A 1 84  ? 15.092  22.225 25.836 1.00 18.01 ? 84  PHE   A CA  1 
ATOM   611  C  C   . PHE   A 1 84  ? 15.068  22.577 24.339 1.00 20.04 ? 84  PHE   A C   1 
ATOM   612  O  O   . PHE   A 1 84  ? 15.978  22.169 23.607 1.00 24.16 ? 84  PHE   A O   1 
ATOM   613  C  CB  . PHE   A 1 84  ? 16.145  23.123 26.482 1.00 20.12 ? 84  PHE   A CB  1 
ATOM   614  C  CG  . PHE   A 1 84  ? 16.376  22.857 27.954 1.00 18.68 ? 84  PHE   A CG  1 
ATOM   615  C  CD1 . PHE   A 1 84  ? 17.254  21.869 28.384 1.00 27.06 ? 84  PHE   A CD1 1 
ATOM   616  C  CD2 . PHE   A 1 84  ? 15.598  23.483 28.887 1.00 20.78 ? 84  PHE   A CD2 1 
ATOM   617  C  CE1 . PHE   A 1 84  ? 17.435  21.621 29.751 1.00 29.27 ? 84  PHE   A CE1 1 
ATOM   618  C  CE2 . PHE   A 1 84  ? 15.783  23.255 30.226 1.00 21.92 ? 84  PHE   A CE2 1 
ATOM   619  C  CZ  . PHE   A 1 84  ? 16.713  22.360 30.665 1.00 26.03 ? 84  PHE   A CZ  1 
ATOM   620  N  N   . GLU   A 1 85  ? 14.043  23.299 23.934 1.00 20.52 ? 85  GLU   A N   1 
ATOM   621  C  CA  . GLU   A 1 85  ? 13.970  23.782 22.555 1.00 22.67 ? 85  GLU   A CA  1 
ATOM   622  C  C   . GLU   A 1 85  ? 13.690  25.264 22.520 1.00 23.17 ? 85  GLU   A C   1 
ATOM   623  O  O   . GLU   A 1 85  ? 12.728  25.757 23.099 1.00 24.28 ? 85  GLU   A O   1 
ATOM   624  C  CB  . GLU   A 1 85  ? 12.825  23.053 21.869 1.00 26.41 ? 85  GLU   A CB  1 
ATOM   625  C  CG  . GLU   A 1 85  ? 13.182  21.575 21.764 1.00 33.65 ? 85  GLU   A CG  1 
ATOM   626  C  CD  . GLU   A 1 85  ? 12.169  20.736 21.037 1.00 48.37 ? 85  GLU   A CD  1 
ATOM   627  O  OE1 . GLU   A 1 85  ? 11.045  20.730 21.573 1.00 50.03 ? 85  GLU   A OE1 1 
ATOM   628  O  OE2 . GLU   A 1 85  ? 12.475  20.201 19.957 1.00 54.03 ? 85  GLU   A OE2 1 
ATOM   629  N  N   . MET   A 1 86  ? 14.546  25.988 21.775 1.00 22.79 ? 86  MET   A N   1 
ATOM   630  C  CA  . MET   A 1 86  ? 14.370  27.407 21.584 1.00 23.23 ? 86  MET   A CA  1 
ATOM   631  C  C   . MET   A 1 86  ? 14.117  27.675 20.095 1.00 20.07 ? 86  MET   A C   1 
ATOM   632  O  O   . MET   A 1 86  ? 14.972  27.328 19.281 1.00 21.84 ? 86  MET   A O   1 
ATOM   633  C  CB  . MET   A 1 86  ? 15.661  28.179 21.934 1.00 23.77 ? 86  MET   A CB  1 
ATOM   634  C  CG  . MET   A 1 86  ? 16.136  28.046 23.358 1.00 33.91 ? 86  MET   A CG  1 
ATOM   635  S  SD  . MET   A 1 86  ? 17.747  28.890 23.431 1.00 33.90 ? 86  MET   A SD  1 
ATOM   636  C  CE  . MET   A 1 86  ? 18.141  28.228 25.039 1.00 32.74 ? 86  MET   A CE  1 
ATOM   637  N  N   . ILE   A 1 87  ? 12.989  28.302 19.827 1.00 21.21 ? 87  ILE   A N   1 
ATOM   638  C  CA  . ILE   A 1 87  ? 12.605  28.693 18.480 1.00 20.60 ? 87  ILE   A CA  1 
ATOM   639  C  C   . ILE   A 1 87  ? 12.917  30.155 18.289 1.00 21.26 ? 87  ILE   A C   1 
ATOM   640  O  O   . ILE   A 1 87  ? 12.502  30.993 19.080 1.00 21.46 ? 87  ILE   A O   1 
ATOM   641  C  CB  . ILE   A 1 87  ? 11.125  28.342 18.234 1.00 24.13 ? 87  ILE   A CB  1 
ATOM   642  C  CG1 . ILE   A 1 87  ? 10.951  26.836 18.386 1.00 29.58 ? 87  ILE   A CG1 1 
ATOM   643  C  CG2 . ILE   A 1 87  ? 10.618  28.865 16.882 1.00 24.94 ? 87  ILE   A CG2 1 
ATOM   644  C  CD1 . ILE   A 1 87  ? 9.508   26.393 18.333 1.00 36.19 ? 87  ILE   A CD1 1 
ATOM   645  N  N   . VAL   A 1 88  ? 13.617  30.437 17.178 1.00 23.72 ? 88  VAL   A N   1 
ATOM   646  C  CA  . VAL   A 1 88  ? 14.067  31.791 16.914 1.00 21.95 ? 88  VAL   A CA  1 
ATOM   647  C  C   . VAL   A 1 88  ? 13.955  32.117 15.421 1.00 23.76 ? 88  VAL   A C   1 
ATOM   648  O  O   . VAL   A 1 88  ? 14.012  31.227 14.602 1.00 22.95 ? 88  VAL   A O   1 
ATOM   649  C  CB  . VAL   A 1 88  ? 15.529  31.950 17.363 1.00 24.48 ? 88  VAL   A CB  1 
ATOM   650  C  CG1 . VAL   A 1 88  ? 15.697  31.696 18.851 1.00 27.19 ? 88  VAL   A CG1 1 
ATOM   651  C  CG2 . VAL   A 1 88  ? 16.484  31.067 16.599 1.00 23.20 ? 88  VAL   A CG2 1 
ATOM   652  N  N   . LYS   A 1 89  ? 13.976  33.413 15.097 1.00 25.74 ? 89  LYS   A N   1 
ATOM   653  C  CA  . LYS   A 1 89  ? 13.996  33.870 13.699 1.00 28.56 ? 89  LYS   A CA  1 
ATOM   654  C  C   . LYS   A 1 89  ? 15.396  33.770 13.111 1.00 27.76 ? 89  LYS   A C   1 
ATOM   655  O  O   . LYS   A 1 89  ? 15.559  33.570 11.920 1.00 25.22 ? 89  LYS   A O   1 
ATOM   656  C  CB  . LYS   A 1 89  ? 13.484  35.310 13.602 1.00 31.37 ? 89  LYS   A CB  1 
ATOM   657  C  CG  . LYS   A 1 89  ? 12.041  35.474 14.042 1.00 44.15 ? 89  LYS   A CG  1 
ATOM   658  C  CD  . LYS   A 1 89  ? 11.589  36.929 14.116 1.00 56.92 ? 89  LYS   A CD  1 
ATOM   659  C  CE  . LYS   A 1 89  ? 10.381  37.103 14.981 1.00 64.66 ? 89  LYS   A CE  1 
ATOM   660  N  NZ  . LYS   A 1 89  ? 10.038  38.523 15.115 1.00 71.43 ? 89  LYS   A NZ  1 
ATOM   661  N  N   . ASP   A 1 90  ? 16.455  33.861 13.939 1.00 24.10 ? 90  ASP   A N   1 
ATOM   662  C  CA  . ASP   A 1 90  ? 17.825  33.858 13.442 1.00 24.90 ? 90  ASP   A CA  1 
ATOM   663  C  C   . ASP   A 1 90  ? 18.733  33.380 14.572 1.00 24.25 ? 90  ASP   A C   1 
ATOM   664  O  O   . ASP   A 1 90  ? 18.509  33.695 15.752 1.00 27.53 ? 90  ASP   A O   1 
ATOM   665  C  CB  . ASP   A 1 90  ? 18.222  35.255 12.993 1.00 29.51 ? 90  ASP   A CB  1 
ATOM   666  C  CG  . ASP   A 1 90  ? 17.874  36.292 14.040 1.00 41.21 ? 90  ASP   A CG  1 
ATOM   667  O  OD1 . ASP   A 1 90  ? 18.544  36.287 15.120 1.00 50.04 ? 90  ASP   A OD1 1 
ATOM   668  O  OD2 . ASP   A 1 90  ? 16.872  37.003 13.830 1.00 46.77 ? 90  ASP   A OD2 1 
ATOM   669  N  N   . ILE   A 1 91  ? 19.774  32.679 14.245 1.00 22.11 ? 91  ILE   A N   1 
ATOM   670  C  CA  . ILE   A 1 91  ? 20.594  32.118 15.318 1.00 24.74 ? 91  ILE   A CA  1 
ATOM   671  C  C   . ILE   A 1 91  ? 21.420  33.199 16.025 1.00 25.92 ? 91  ILE   A C   1 
ATOM   672  O  O   . ILE   A 1 91  ? 21.896  32.968 17.138 1.00 23.57 ? 91  ILE   A O   1 
ATOM   673  C  CB  . ILE   A 1 91  ? 21.471  30.990 14.784 1.00 34.27 ? 91  ILE   A CB  1 
ATOM   674  C  CG1 . ILE   A 1 91  ? 22.453  31.507 13.779 1.00 38.63 ? 91  ILE   A CG1 1 
ATOM   675  C  CG2 . ILE   A 1 91  ? 20.620  29.847 14.242 1.00 35.71 ? 91  ILE   A CG2 1 
ATOM   676  C  CD1 . ILE   A 1 91  ? 23.807  30.862 13.893 1.00 39.64 ? 91  ILE   A CD1 1 
ATOM   677  N  N   . GLU   A 1 92  ? 21.567  34.395 15.424 1.00 24.64 ? 92  GLU   A N   1 
ATOM   678  C  CA  . GLU   A 1 92  ? 22.264  35.489 16.114 1.00 27.99 ? 92  GLU   A CA  1 
ATOM   679  C  C   . GLU   A 1 92  ? 21.577  35.853 17.436 1.00 25.83 ? 92  GLU   A C   1 
ATOM   680  O  O   . GLU   A 1 92  ? 22.240  36.201 18.402 1.00 25.34 ? 92  GLU   A O   1 
ATOM   681  C  CB  . GLU   A 1 92  ? 22.404  36.656 15.132 1.00 37.87 ? 92  GLU   A CB  1 
ATOM   682  C  CG  . GLU   A 1 92  ? 22.382  38.045 15.765 1.00 47.87 ? 92  GLU   A CG  1 
ATOM   683  C  CD  . GLU   A 1 92  ? 22.701  39.182 14.785 1.00 59.19 ? 92  GLU   A CD  1 
ATOM   684  O  OE1 . GLU   A 1 92  ? 22.306  40.320 15.087 1.00 71.28 ? 92  GLU   A OE1 1 
ATOM   685  O  OE2 . GLU   A 1 92  ? 23.336  38.963 13.734 1.00 56.58 ? 92  GLU   A OE2 1 
ATOM   686  N  N   . SER   A 1 93  ? 20.267  35.668 17.519 1.00 25.21 ? 93  SER   A N   1 
ATOM   687  C  CA  . SER   A 1 93  ? 19.505  35.835 18.754 1.00 24.21 ? 93  SER   A CA  1 
ATOM   688  C  C   . SER   A 1 93  ? 20.059  34.946 19.866 1.00 22.15 ? 93  SER   A C   1 
ATOM   689  O  O   . SER   A 1 93  ? 20.298  35.418 20.980 1.00 23.51 ? 93  SER   A O   1 
ATOM   690  C  CB  . SER   A 1 93  ? 18.053  35.525 18.538 1.00 30.76 ? 93  SER   A CB  1 
ATOM   691  O  OG  . SER   A 1 93  ? 17.489  36.546 17.740 1.00 32.70 ? 93  SER   A OG  1 
ATOM   692  N  N   . ILE   A 1 94  ? 20.325  33.689 19.541 1.00 21.78 ? 94  ILE   A N   1 
ATOM   693  C  CA  . ILE   A 1 94  ? 20.876  32.751 20.505 1.00 21.13 ? 94  ILE   A CA  1 
ATOM   694  C  C   . ILE   A 1 94  ? 22.333  33.054 20.841 1.00 22.38 ? 94  ILE   A C   1 
ATOM   695  O  O   . ILE   A 1 94  ? 22.759  33.034 22.010 1.00 19.50 ? 94  ILE   A O   1 
ATOM   696  C  CB  . ILE   A 1 94  ? 20.699  31.315 19.996 1.00 21.05 ? 94  ILE   A CB  1 
ATOM   697  C  CG1 . ILE   A 1 94  ? 19.211  31.025 19.912 1.00 23.63 ? 94  ILE   A CG1 1 
ATOM   698  C  CG2 . ILE   A 1 94  ? 21.391  30.335 20.932 1.00 21.69 ? 94  ILE   A CG2 1 
ATOM   699  C  CD1 . ILE   A 1 94  ? 18.893  29.735 19.203 1.00 25.80 ? 94  ILE   A CD1 1 
ATOM   700  N  N   . GLN   A 1 95  ? 23.148  33.280 19.813 1.00 22.49 ? 95  GLN   A N   1 
ATOM   701  C  CA  . GLN   A 1 95  ? 24.562  33.525 20.079 1.00 21.04 ? 95  GLN   A CA  1 
ATOM   702  C  C   . GLN   A 1 95  ? 24.746  34.798 20.933 1.00 18.96 ? 95  GLN   A C   1 
ATOM   703  O  O   . GLN   A 1 95  ? 25.634  34.815 21.800 1.00 21.49 ? 95  GLN   A O   1 
ATOM   704  C  CB  . GLN   A 1 95  ? 25.334  33.555 18.764 1.00 23.92 ? 95  GLN   A CB  1 
ATOM   705  C  CG  . GLN   A 1 95  ? 25.329  32.208 18.032 1.00 25.89 ? 95  GLN   A CG  1 
ATOM   706  C  CD  . GLN   A 1 95  ? 26.281  32.140 16.859 1.00 25.53 ? 95  GLN   A CD  1 
ATOM   707  O  OE1 . GLN   A 1 95  ? 27.193  31.312 16.755 1.00 37.33 ? 95  GLN   A OE1 1 
ATOM   708  N  NE2 . GLN   A 1 95  ? 25.964  32.965 15.916 1.00 24.62 ? 95  GLN   A NE2 1 
ATOM   709  N  N   . THR   A 1 96  ? 23.953  35.842 20.661 1.00 19.96 ? 96  THR   A N   1 
ATOM   710  C  CA  . THR   A 1 96  ? 24.071  37.071 21.426 1.00 22.04 ? 96  THR   A CA  1 
ATOM   711  C  C   . THR   A 1 96  ? 23.651  36.835 22.883 1.00 22.41 ? 96  THR   A C   1 
ATOM   712  O  O   . THR   A 1 96  ? 24.340  37.279 23.823 1.00 18.92 ? 96  THR   A O   1 
ATOM   713  C  CB  . THR   A 1 96  ? 23.290  38.202 20.775 1.00 25.10 ? 96  THR   A CB  1 
ATOM   714  O  OG1 . THR   A 1 96  ? 23.867  38.296 19.460 1.00 26.88 ? 96  THR   A OG1 1 
ATOM   715  C  CG2 . THR   A 1 96  ? 23.557  39.498 21.507 1.00 26.82 ? 96  THR   A CG2 1 
ATOM   716  N  N   . MET   A 1 97  ? 22.598  36.046 23.072 1.00 20.58 ? 97  MET   A N   1 
ATOM   717  C  CA  . MET   A 1 97  ? 22.145  35.705 24.419 1.00 19.18 ? 97  MET   A CA  1 
ATOM   718  C  C   . MET   A 1 97  ? 23.270  35.001 25.192 1.00 19.21 ? 97  MET   A C   1 
ATOM   719  O  O   . MET   A 1 97  ? 23.563  35.270 26.347 1.00 19.43 ? 97  MET   A O   1 
ATOM   720  C  CB  . MET   A 1 97  ? 20.900  34.800 24.351 1.00 18.05 ? 97  MET   A CB  1 
ATOM   721  C  CG  . MET   A 1 97  ? 20.420  34.411 25.724 1.00 18.68 ? 97  MET   A CG  1 
ATOM   722  S  SD  . MET   A 1 97  ? 18.914  33.409 25.636 1.00 22.62 ? 97  MET   A SD  1 
ATOM   723  C  CE  . MET   A 1 97  ? 19.702  31.911 25.095 1.00 21.50 ? 97  MET   A CE  1 
ATOM   724  N  N   . GLN   A 1 98  ? 23.846  33.978 24.573 1.00 18.36 ? 98  GLN   A N   1 
ATOM   725  C  CA  . GLN   A 1 98  ? 24.857  33.137 25.171 1.00 20.47 ? 98  GLN   A CA  1 
ATOM   726  C  C   . GLN   A 1 98  ? 26.101  33.929 25.565 1.00 21.61 ? 98  GLN   A C   1 
ATOM   727  O  O   . GLN   A 1 98  ? 26.790  33.507 26.471 1.00 20.83 ? 98  GLN   A O   1 
ATOM   728  C  CB  . GLN   A 1 98  ? 25.226  32.007 24.211 1.00 23.65 ? 98  GLN   A CB  1 
ATOM   729  C  CG  . GLN   A 1 98  ? 24.136  30.956 24.162 1.00 24.66 ? 98  GLN   A CG  1 
ATOM   730  C  CD  . GLN   A 1 98  ? 24.479  29.862 23.173 1.00 28.68 ? 98  GLN   A CD  1 
ATOM   731  O  OE1 . GLN   A 1 98  ? 25.098  30.114 22.147 1.00 29.75 ? 98  GLN   A OE1 1 
ATOM   732  N  NE2 . GLN   A 1 98  ? 23.910  28.708 23.389 1.00 29.63 ? 98  GLN   A NE2 1 
ATOM   733  N  N   . LYS   A 1 99  ? 26.409  35.034 24.886 1.00 22.63 ? 99  LYS   A N   1 
ATOM   734  C  CA  . LYS   A 1 99  ? 27.618  35.779 25.227 1.00 23.93 ? 99  LYS   A CA  1 
ATOM   735  C  C   . LYS   A 1 99  ? 27.312  36.971 26.120 1.00 23.88 ? 99  LYS   A C   1 
ATOM   736  O  O   . LYS   A 1 99  ? 28.234  37.716 26.463 1.00 23.08 ? 99  LYS   A O   1 
ATOM   737  C  CB  . LYS   A 1 99  ? 28.362  36.237 23.959 1.00 28.20 ? 99  LYS   A CB  1 
ATOM   738  C  CG  . LYS   A 1 99  ? 28.921  35.124 23.105 1.00 28.90 ? 99  LYS   A CG  1 
ATOM   739  C  CD  . LYS   A 1 99  ? 29.910  34.279 23.888 1.00 35.93 ? 99  LYS   A CD  1 
ATOM   740  C  CE  . LYS   A 1 99  ? 30.681  33.301 23.040 1.00 51.27 ? 99  LYS   A CE  1 
ATOM   741  N  NZ  . LYS   A 1 99  ? 29.738  32.561 22.195 1.00 52.86 ? 99  LYS   A NZ  1 
ATOM   742  N  N   . ASP   A 1 100 ? 26.032  37.175 26.465 1.00 20.56 ? 100 ASP   A N   1 
ATOM   743  C  CA  . ASP   A 1 100 ? 25.621  38.264 27.328 1.00 21.87 ? 100 ASP   A CA  1 
ATOM   744  C  C   . ASP   A 1 100 ? 26.337  38.081 28.670 1.00 23.23 ? 100 ASP   A C   1 
ATOM   745  O  O   . ASP   A 1 100 ? 26.321  36.991 29.245 1.00 20.29 ? 100 ASP   A O   1 
ATOM   746  C  CB  . ASP   A 1 100 ? 24.107  38.310 27.429 1.00 20.08 ? 100 ASP   A CB  1 
ATOM   747  C  CG  . ASP   A 1 100 ? 23.490  39.290 28.404 1.00 24.63 ? 100 ASP   A CG  1 
ATOM   748  O  OD1 . ASP   A 1 100 ? 23.864  39.266 29.568 1.00 31.39 ? 100 ASP   A OD1 1 
ATOM   749  O  OD2 . ASP   A 1 100 ? 22.533  39.988 28.023 1.00 24.89 ? 100 ASP   A OD2 1 
ATOM   750  N  N   . GLU   A 1 101 ? 26.963  39.139 29.215 1.00 22.24 ? 101 GLU   A N   1 
ATOM   751  C  CA  . GLU   A 1 101 ? 27.812  38.863 30.375 1.00 22.82 ? 101 GLU   A CA  1 
ATOM   752  C  C   . GLU   A 1 101 ? 26.941  38.404 31.549 1.00 21.85 ? 101 GLU   A C   1 
ATOM   753  O  O   . GLU   A 1 101 ? 27.360  37.555 32.330 1.00 20.01 ? 101 GLU   A O   1 
ATOM   754  C  CB  . GLU   A 1 101 ? 28.646  40.060 30.813 1.00 24.43 ? 101 GLU   A CB  1 
ATOM   755  C  CG  . GLU   A 1 101 ? 27.803  41.264 31.197 1.00 21.54 ? 101 GLU   A CG  1 
ATOM   756  C  CD  . GLU   A 1 101 ? 27.452  41.333 32.688 1.00 26.28 ? 101 GLU   A CD  1 
ATOM   757  O  OE1 . GLU   A 1 101 ? 28.095  40.664 33.493 1.00 23.11 ? 101 GLU   A OE1 1 
ATOM   758  O  OE2 . GLU   A 1 101 ? 26.441  41.971 33.068 1.00 24.14 ? 101 GLU   A OE2 1 
ATOM   759  N  N   . GLU   A 1 102 ? 25.699  38.893 31.652 1.00 18.91 ? 102 GLU   A N   1 
ATOM   760  C  CA  . GLU   A 1 102 ? 24.815  38.401 32.706 1.00 18.74 ? 102 GLU   A CA  1 
ATOM   761  C  C   . GLU   A 1 102 ? 24.534  36.892 32.569 1.00 18.20 ? 102 GLU   A C   1 
ATOM   762  O  O   . GLU   A 1 102 ? 24.423  36.173 33.579 1.00 20.07 ? 102 GLU   A O   1 
ATOM   763  C  CB  . GLU   A 1 102 ? 23.532  39.224 32.755 1.00 21.44 ? 102 GLU   A CB  1 
ATOM   764  C  CG  . GLU   A 1 102 ? 22.662  38.995 33.976 1.00 22.82 ? 102 GLU   A CG  1 
ATOM   765  C  CD  . GLU   A 1 102 ? 21.305  39.707 33.750 1.00 25.63 ? 102 GLU   A CD  1 
ATOM   766  O  OE1 . GLU   A 1 102 ? 21.096  40.521 32.824 1.00 30.64 ? 102 GLU   A OE1 1 
ATOM   767  O  OE2 . GLU   A 1 102 ? 20.460  39.375 34.534 1.00 24.82 ? 102 GLU   A OE2 1 
ATOM   768  N  N   . PHE   A 1 103 ? 24.282  36.434 31.336 1.00 17.87 ? 103 PHE   A N   1 
ATOM   769  C  CA  . PHE   A 1 103 ? 24.065  35.026 31.039 1.00 17.08 ? 103 PHE   A CA  1 
ATOM   770  C  C   . PHE   A 1 103 ? 25.245  34.167 31.531 1.00 16.82 ? 103 PHE   A C   1 
ATOM   771  O  O   . PHE   A 1 103 ? 25.048  33.094 32.117 1.00 15.93 ? 103 PHE   A O   1 
ATOM   772  C  CB  . PHE   A 1 103 ? 23.844  34.893 29.537 1.00 18.45 ? 103 PHE   A CB  1 
ATOM   773  C  CG  . PHE   A 1 103 ? 23.292  33.535 29.105 1.00 18.36 ? 103 PHE   A CG  1 
ATOM   774  C  CD1 . PHE   A 1 103 ? 21.913  33.320 29.106 1.00 20.30 ? 103 PHE   A CD1 1 
ATOM   775  C  CD2 . PHE   A 1 103 ? 24.124  32.504 28.724 1.00 20.39 ? 103 PHE   A CD2 1 
ATOM   776  C  CE1 . PHE   A 1 103 ? 21.421  32.092 28.671 1.00 19.84 ? 103 PHE   A CE1 1 
ATOM   777  C  CE2 . PHE   A 1 103 ? 23.615  31.270 28.349 1.00 21.11 ? 103 PHE   A CE2 1 
ATOM   778  C  CZ  . PHE   A 1 103 ? 22.275  31.093 28.284 1.00 20.15 ? 103 PHE   A CZ  1 
ATOM   779  N  N   . LEU   A 1 104 ? 26.474  34.652 31.307 1.00 16.31 ? 104 LEU   A N   1 
ATOM   780  C  CA  . LEU   A 1 104 ? 27.697  33.944 31.660 1.00 16.33 ? 104 LEU   A CA  1 
ATOM   781  C  C   . LEU   A 1 104 ? 27.850  33.731 33.153 1.00 15.70 ? 104 LEU   A C   1 
ATOM   782  O  O   . LEU   A 1 104 ? 28.593  32.827 33.578 1.00 16.12 ? 104 LEU   A O   1 
ATOM   783  C  CB  . LEU   A 1 104 ? 28.936  34.656 31.077 1.00 18.70 ? 104 LEU   A CB  1 
ATOM   784  C  CG  . LEU   A 1 104 ? 29.055  34.654 29.551 1.00 21.61 ? 104 LEU   A CG  1 
ATOM   785  C  CD1 . LEU   A 1 104 ? 30.293  35.425 29.132 1.00 27.22 ? 104 LEU   A CD1 1 
ATOM   786  C  CD2 . LEU   A 1 104 ? 29.148  33.299 28.983 1.00 21.62 ? 104 LEU   A CD2 1 
ATOM   787  N  N   . ARG   A 1 105 ? 27.241  34.604 33.982 1.00 14.75 ? 105 ARG   A N   1 
ATOM   788  C  CA  . ARG   A 1 105 ? 27.319  34.463 35.435 1.00 16.57 ? 105 ARG   A CA  1 
ATOM   789  C  C   . ARG   A 1 105 ? 26.013  34.000 36.091 1.00 16.08 ? 105 ARG   A C   1 
ATOM   790  O  O   . ARG   A 1 105 ? 25.959  33.914 37.322 1.00 16.09 ? 105 ARG   A O   1 
ATOM   791  C  CB  . ARG   A 1 105 ? 27.864  35.748 36.062 1.00 17.71 ? 105 ARG   A CB  1 
ATOM   792  C  CG  . ARG   A 1 105 ? 27.067  37.010 35.803 1.00 18.29 ? 105 ARG   A CG  1 
ATOM   793  C  CD  . ARG   A 1 105 ? 27.486  38.296 36.554 1.00 18.60 ? 105 ARG   A CD  1 
ATOM   794  N  NE  . ARG   A 1 105 ? 26.861  39.452 35.899 1.00 19.17 ? 105 ARG   A NE  1 
ATOM   795  C  CZ  . ARG   A 1 105 ? 25.700  40.023 36.249 1.00 19.96 ? 105 ARG   A CZ  1 
ATOM   796  N  NH1 . ARG   A 1 105 ? 24.987  39.499 37.214 1.00 21.04 ? 105 ARG   A NH1 1 
ATOM   797  N  NH2 . ARG   A 1 105 ? 25.238  41.041 35.534 1.00 20.59 ? 105 ARG   A NH2 1 
ATOM   798  N  N   . THR   A 1 106 ? 25.007  33.585 35.288 1.00 16.50 ? 106 THR   A N   1 
ATOM   799  C  CA  . THR   A 1 106 ? 23.749  33.117 35.835 1.00 16.02 ? 106 THR   A CA  1 
ATOM   800  C  C   . THR   A 1 106 ? 23.435  31.733 35.238 1.00 17.39 ? 106 THR   A C   1 
ATOM   801  O  O   . THR   A 1 106 ? 23.570  30.711 35.910 1.00 16.87 ? 106 THR   A O   1 
ATOM   802  C  CB  . THR   A 1 106 ? 22.618  34.141 35.611 1.00 19.22 ? 106 THR   A CB  1 
ATOM   803  O  OG1 . THR   A 1 106 ? 22.493  34.412 34.213 1.00 20.98 ? 106 THR   A OG1 1 
ATOM   804  C  CG2 . THR   A 1 106 ? 22.954  35.486 36.232 1.00 19.34 ? 106 THR   A CG2 1 
ATOM   805  N  N   . ALA   A 1 107 ? 23.051  31.699 33.969 1.00 18.23 ? 107 ALA   A N   1 
ATOM   806  C  CA  . ALA   A 1 107 ? 22.614  30.479 33.288 1.00 18.00 ? 107 ALA   A CA  1 
ATOM   807  C  C   . ALA   A 1 107 ? 23.756  29.479 33.145 1.00 17.47 ? 107 ALA   A C   1 
ATOM   808  O  O   . ALA   A 1 107 ? 23.571  28.307 33.414 1.00 17.11 ? 107 ALA   A O   1 
ATOM   809  C  CB  . ALA   A 1 107 ? 22.009  30.805 31.939 1.00 19.06 ? 107 ALA   A CB  1 
ATOM   810  N  N   . ILE   A 1 108 ? 24.974  29.946 32.797 1.00 15.01 ? 108 ILE   A N   1 
ATOM   811  C  CA  . ILE   A 1 108 ? 26.092  29.027 32.551 1.00 16.44 ? 108 ILE   A CA  1 
ATOM   812  C  C   . ILE   A 1 108 ? 26.458  28.296 33.840 1.00 17.83 ? 108 ILE   A C   1 
ATOM   813  O  O   . ILE   A 1 108 ? 26.479  27.054 33.898 1.00 17.61 ? 108 ILE   A O   1 
ATOM   814  C  CB  . ILE   A 1 108 ? 27.277  29.751 31.876 1.00 17.32 ? 108 ILE   A CB  1 
ATOM   815  C  CG1 . ILE   A 1 108 ? 26.929  30.149 30.430 1.00 18.98 ? 108 ILE   A CG1 1 
ATOM   816  C  CG2 . ILE   A 1 108 ? 28.530  28.874 31.944 1.00 20.37 ? 108 ILE   A CG2 1 
ATOM   817  C  CD1 . ILE   A 1 108 ? 26.516  29.008 29.511 1.00 24.89 ? 108 ILE   A CD1 1 
ATOM   818  N  N   . PRO   A 1 109 ? 26.712  28.989 34.968 1.00 16.60 ? 109 PRO   A N   1 
ATOM   819  C  CA  . PRO   A 1 109 ? 27.018  28.270 36.201 1.00 16.14 ? 109 PRO   A CA  1 
ATOM   820  C  C   . PRO   A 1 109 ? 25.877  27.365 36.653 1.00 16.21 ? 109 PRO   A C   1 
ATOM   821  O  O   . PRO   A 1 109 ? 26.119  26.330 37.283 1.00 15.93 ? 109 PRO   A O   1 
ATOM   822  C  CB  . PRO   A 1 109 ? 27.357  29.361 37.262 1.00 18.53 ? 109 PRO   A CB  1 
ATOM   823  C  CG  . PRO   A 1 109 ? 26.980  30.653 36.592 1.00 17.98 ? 109 PRO   A CG  1 
ATOM   824  C  CD  . PRO   A 1 109 ? 26.902  30.454 35.097 1.00 18.78 ? 109 PRO   A CD  1 
ATOM   825  N  N   . ASP   A 1 110 ? 24.633  27.788 36.416 1.00 15.69 ? 110 ASP   A N   1 
ATOM   826  C  CA  . ASP   A 1 110 ? 23.497  27.011 36.873 1.00 18.08 ? 110 ASP   A CA  1 
ATOM   827  C  C   . ASP   A 1 110 ? 23.469  25.634 36.190 1.00 16.29 ? 110 ASP   A C   1 
ATOM   828  O  O   . ASP   A 1 110 ? 22.972  24.661 36.805 1.00 17.85 ? 110 ASP   A O   1 
ATOM   829  C  CB  . ASP   A 1 110 ? 22.153  27.636 36.578 1.00 19.05 ? 110 ASP   A CB  1 
ATOM   830  C  CG  . ASP   A 1 110 ? 21.011  26.997 37.350 1.00 22.22 ? 110 ASP   A CG  1 
ATOM   831  O  OD1 . ASP   A 1 110 ? 21.087  26.944 38.559 1.00 20.91 ? 110 ASP   A OD1 1 
ATOM   832  O  OD2 . ASP   A 1 110 ? 20.089  26.499 36.743 1.00 21.29 ? 110 ASP   A OD2 1 
ATOM   833  N  N   . LEU   A 1 111 ? 23.992  25.520 34.951 1.00 15.72 ? 111 LEU   A N   1 
ATOM   834  C  CA  . LEU   A 1 111 ? 24.019  24.218 34.247 1.00 17.64 ? 111 LEU   A CA  1 
ATOM   835  C  C   . LEU   A 1 111 ? 24.645  23.119 35.108 1.00 19.75 ? 111 LEU   A C   1 
ATOM   836  O  O   . LEU   A 1 111 ? 24.220  21.957 35.068 1.00 18.33 ? 111 LEU   A O   1 
ATOM   837  C  CB  . LEU   A 1 111 ? 24.788  24.321 32.915 1.00 18.92 ? 111 LEU   A CB  1 
ATOM   838  C  CG  . LEU   A 1 111 ? 24.227  25.308 31.889 1.00 21.09 ? 111 LEU   A CG  1 
ATOM   839  C  CD1 . LEU   A 1 111 ? 25.189  25.428 30.707 1.00 21.24 ? 111 LEU   A CD1 1 
ATOM   840  C  CD2 . LEU   A 1 111 ? 22.866  24.892 31.463 1.00 27.09 ? 111 LEU   A CD2 1 
ATOM   841  N  N   . PHE   A 1 112 ? 25.722  23.478 35.842 1.00 16.79 ? 112 PHE   A N   1 
ATOM   842  C  CA  . PHE   A 1 112 ? 26.479  22.513 36.618 1.00 17.07 ? 112 PHE   A CA  1 
ATOM   843  C  C   . PHE   A 1 112 ? 25.649  21.972 37.801 1.00 18.13 ? 112 PHE   A C   1 
ATOM   844  O  O   . PHE   A 1 112 ? 26.018  20.968 38.395 1.00 19.25 ? 112 PHE   A O   1 
ATOM   845  C  CB  . PHE   A 1 112 ? 27.832  23.072 37.066 1.00 18.19 ? 112 PHE   A CB  1 
ATOM   846  C  CG  . PHE   A 1 112 ? 28.732  23.304 35.873 1.00 17.41 ? 112 PHE   A CG  1 
ATOM   847  C  CD1 . PHE   A 1 112 ? 28.697  24.516 35.169 1.00 19.20 ? 112 PHE   A CD1 1 
ATOM   848  C  CD2 . PHE   A 1 112 ? 29.526  22.274 35.383 1.00 17.83 ? 112 PHE   A CD2 1 
ATOM   849  C  CE1 . PHE   A 1 112 ? 29.485  24.693 34.057 1.00 20.07 ? 112 PHE   A CE1 1 
ATOM   850  C  CE2 . PHE   A 1 112 ? 30.320  22.468 34.269 1.00 18.41 ? 112 PHE   A CE2 1 
ATOM   851  C  CZ  . PHE   A 1 112 ? 30.320  23.675 33.610 1.00 18.66 ? 112 PHE   A CZ  1 
ATOM   852  N  N   . ASN   A 1 113 ? 24.556  22.655 38.145 1.00 16.05 ? 113 ASN   A N   1 
ATOM   853  C  CA  . ASN   A 1 113 ? 23.710  22.226 39.241 1.00 16.99 ? 113 ASN   A CA  1 
ATOM   854  C  C   . ASN   A 1 113 ? 22.590  21.302 38.750 1.00 17.48 ? 113 ASN   A C   1 
ATOM   855  O  O   . ASN   A 1 113 ? 21.806  20.809 39.585 1.00 18.81 ? 113 ASN   A O   1 
ATOM   856  C  CB  . ASN   A 1 113 ? 23.143  23.417 39.991 1.00 17.97 ? 113 ASN   A CB  1 
ATOM   857  C  CG  . ASN   A 1 113 ? 24.241  24.091 40.758 1.00 20.78 ? 113 ASN   A CG  1 
ATOM   858  O  OD1 . ASN   A 1 113 ? 25.180  23.433 41.195 1.00 20.42 ? 113 ASN   A OD1 1 
ATOM   859  N  ND2 . ASN   A 1 113 ? 24.206  25.415 40.806 1.00 22.08 ? 113 ASN   A ND2 1 
ATOM   860  N  N   . PHE   A 1 114 ? 22.503  21.025 37.450 1.00 18.09 ? 114 PHE   A N   1 
ATOM   861  C  CA  . PHE   A 1 114 ? 21.495  20.043 37.022 1.00 17.96 ? 114 PHE   A CA  1 
ATOM   862  C  C   . PHE   A 1 114 ? 21.891  19.125 35.858 1.00 19.94 ? 114 PHE   A C   1 
ATOM   863  O  O   . PHE   A 1 114 ? 21.193  18.133 35.619 1.00 18.87 ? 114 PHE   A O   1 
ATOM   864  C  CB  . PHE   A 1 114 ? 20.144  20.709 36.741 1.00 18.19 ? 114 PHE   A CB  1 
ATOM   865  C  CG  . PHE   A 1 114 ? 20.094  21.607 35.514 1.00 18.49 ? 114 PHE   A CG  1 
ATOM   866  C  CD1 . PHE   A 1 114 ? 20.412  22.954 35.618 1.00 17.92 ? 114 PHE   A CD1 1 
ATOM   867  C  CD2 . PHE   A 1 114 ? 19.678  21.127 34.269 1.00 19.12 ? 114 PHE   A CD2 1 
ATOM   868  C  CE1 . PHE   A 1 114 ? 20.362  23.777 34.509 1.00 19.05 ? 114 PHE   A CE1 1 
ATOM   869  C  CE2 . PHE   A 1 114 ? 19.620  21.973 33.161 1.00 19.73 ? 114 PHE   A CE2 1 
ATOM   870  C  CZ  . PHE   A 1 114 ? 19.956  23.310 33.299 1.00 20.41 ? 114 PHE   A CZ  1 
ATOM   871  N  N   . ALA   A 1 115 ? 22.905  19.454 35.042 1.00 16.30 ? 115 ALA   A N   1 
ATOM   872  C  CA  . ALA   A 1 115 ? 23.273  18.710 33.860 1.00 18.43 ? 115 ALA   A CA  1 
ATOM   873  C  C   . ALA   A 1 115 ? 24.633  18.045 34.051 1.00 19.31 ? 115 ALA   A C   1 
ATOM   874  O  O   . ALA   A 1 115 ? 25.544  18.540 34.735 1.00 19.43 ? 115 ALA   A O   1 
ATOM   875  C  CB  . ALA   A 1 115 ? 23.263  19.651 32.681 1.00 18.82 ? 115 ALA   A CB  1 
ATOM   876  N  N   . ASP   A 1 116 ? 24.759  16.856 33.466 1.00 17.93 ? 116 ASP   A N   1 
ATOM   877  C  CA  . ASP   A 1 116 ? 26.038  16.245 33.312 1.00 20.31 ? 116 ASP   A CA  1 
ATOM   878  C  C   . ASP   A 1 116 ? 26.711  16.865 32.110 1.00 18.30 ? 116 ASP   A C   1 
ATOM   879  O  O   . ASP   A 1 116 ? 26.328  16.617 30.957 1.00 21.16 ? 116 ASP   A O   1 
ATOM   880  C  CB  . ASP   A 1 116 ? 25.958  14.747 33.054 1.00 25.04 ? 116 ASP   A CB  1 
ATOM   881  C  CG  . ASP   A 1 116 ? 27.316  14.072 32.923 1.00 27.67 ? 116 ASP   A CG  1 
ATOM   882  O  OD1 . ASP   A 1 116 ? 28.330  14.758 32.619 1.00 26.67 ? 116 ASP   A OD1 1 
ATOM   883  O  OD2 . ASP   A 1 116 ? 27.321  12.830 33.042 1.00 29.74 ? 116 ASP   A OD2 1 
ATOM   884  N  N   . MET   A 1 117 ? 27.636  17.771 32.389 1.00 18.46 ? 117 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 117 ? 28.125  18.646 31.343 1.00 19.26 ? 117 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 117 ? 29.146  17.951 30.434 1.00 23.18 ? 117 MET   A C   1 
ATOM   887  O  O   . MET   A 1 117 ? 29.693  18.572 29.507 1.00 25.37 ? 117 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 117 ? 28.636  19.976 31.940 1.00 19.14 ? 117 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 117 ? 27.429  20.900 32.332 1.00 20.00 ? 117 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 117 ? 26.435  21.479 30.976 1.00 25.19 ? 117 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 117 ? 27.575  22.605 30.144 1.00 33.63 ? 117 MET   A CE  1 
ATOM   892  N  N   . THR   A 1 118 ? 29.417  16.684 30.704 1.00 21.13 ? 118 THR   A N   1 
ATOM   893  C  CA  . THR   A 1 118 ? 30.284  15.932 29.808 1.00 26.32 ? 118 THR   A CA  1 
ATOM   894  C  C   . THR   A 1 118 ? 29.489  15.313 28.666 1.00 27.74 ? 118 THR   A C   1 
ATOM   895  O  O   . THR   A 1 118 ? 30.135  14.822 27.756 1.00 27.20 ? 118 THR   A O   1 
ATOM   896  C  CB  . THR   A 1 118 ? 31.030  14.824 30.552 1.00 27.63 ? 118 THR   A CB  1 
ATOM   897  O  OG1 . THR   A 1 118 ? 30.100  13.839 30.983 1.00 25.78 ? 118 THR   A OG1 1 
ATOM   898  C  CG2 . THR   A 1 118 ? 31.774  15.333 31.778 1.00 31.29 ? 118 THR   A CG2 1 
ATOM   899  N  N   . ARG   A 1 119 ? 28.150  15.354 28.686 1.00 27.28 ? 119 ARG   A N   1 
ATOM   900  C  CA  . ARG   A 1 119 ? 27.316  14.498 27.830 1.00 31.08 ? 119 ARG   A CA  1 
ATOM   901  C  C   . ARG   A 1 119 ? 26.248  15.264 27.030 1.00 27.96 ? 119 ARG   A C   1 
ATOM   902  O  O   . ARG   A 1 119 ? 25.444  14.641 26.341 1.00 29.68 ? 119 ARG   A O   1 
ATOM   903  C  CB  . ARG   A 1 119 ? 26.658  13.405 28.711 1.00 30.87 ? 119 ARG   A CB  1 
ATOM   904  N  N   . THR   A 1 120 ? 26.192  16.595 27.008 1.00 24.74 ? 120 THR   A N   1 
ATOM   905  C  CA  . THR   A 1 120 ? 25.065  17.261 26.343 1.00 23.98 ? 120 THR   A CA  1 
ATOM   906  C  C   . THR   A 1 120 ? 25.118  17.094 24.817 1.00 25.77 ? 120 THR   A C   1 
ATOM   907  O  O   . THR   A 1 120 ? 26.167  17.260 24.227 1.00 25.67 ? 120 THR   A O   1 
ATOM   908  C  CB  . THR   A 1 120 ? 25.034  18.750 26.705 1.00 24.54 ? 120 THR   A CB  1 
ATOM   909  O  OG1 . THR   A 1 120 ? 25.204  18.911 28.120 1.00 22.94 ? 120 THR   A OG1 1 
ATOM   910  C  CG2 . THR   A 1 120 ? 23.736  19.395 26.260 1.00 24.50 ? 120 THR   A CG2 1 
ATOM   911  N  N   . LYS   A 1 121 ? 23.974  16.798 24.158 1.00 22.56 ? 121 LYS   A N   1 
ATOM   912  C  CA  . LYS   A 1 121 ? 23.877  16.782 22.710 1.00 22.23 ? 121 LYS   A CA  1 
ATOM   913  C  C   . LYS   A 1 121 ? 23.009  17.926 22.213 1.00 20.06 ? 121 LYS   A C   1 
ATOM   914  O  O   . LYS   A 1 121 ? 22.207  18.489 22.934 1.00 20.69 ? 121 LYS   A O   1 
ATOM   915  C  CB  . LYS   A 1 121 ? 23.393  15.415 22.204 1.00 23.84 ? 121 LYS   A CB  1 
ATOM   916  C  CG  . LYS   A 1 121 ? 24.353  14.321 22.593 1.00 28.93 ? 121 LYS   A CG  1 
ATOM   917  C  CD  . LYS   A 1 121 ? 24.246  13.078 21.716 1.00 39.85 ? 121 LYS   A CD  1 
ATOM   918  C  CE  . LYS   A 1 121 ? 25.326  12.065 22.070 1.00 44.62 ? 121 LYS   A CE  1 
ATOM   919  N  NZ  . LYS   A 1 121 ? 25.457  11.219 20.876 1.00 48.67 ? 121 LYS   A NZ  1 
ATOM   920  N  N   . GLY   A 1 122 ? 23.139  18.294 20.936 1.00 19.10 ? 122 GLY   A N   1 
ATOM   921  C  CA  . GLY   A 1 122 ? 22.276  19.318 20.414 1.00 17.16 ? 122 GLY   A CA  1 
ATOM   922  C  C   . GLY   A 1 122 ? 22.000  19.173 18.912 1.00 17.40 ? 122 GLY   A C   1 
ATOM   923  O  O   . GLY   A 1 122 ? 22.695  18.399 18.232 1.00 22.37 ? 122 GLY   A O   1 
ATOM   924  N  N   . SER   A 1 123 ? 21.100  20.010 18.441 1.00 21.01 ? 123 SER   A N   1 
ATOM   925  C  CA  . SER   A 1 123 ? 20.829  20.143 17.021 1.00 23.10 ? 123 SER   A CA  1 
ATOM   926  C  C   . SER   A 1 123 ? 20.306  21.526 16.720 1.00 20.98 ? 123 SER   A C   1 
ATOM   927  O  O   . SER   A 1 123 ? 19.758  22.210 17.588 1.00 23.09 ? 123 SER   A O   1 
ATOM   928  C  CB  . SER   A 1 123 ? 19.780  19.114 16.580 1.00 22.43 ? 123 SER   A CB  1 
ATOM   929  O  OG  . SER   A 1 123 ? 18.532  19.491 17.099 1.00 24.74 ? 123 SER   A OG  1 
ATOM   930  N  N   . GLY   A 1 124 ? 20.389  21.876 15.416 1.00 19.65 ? 124 GLY   A N   1 
ATOM   931  C  CA  . GLY   A 1 124 ? 19.772  23.047 14.867 1.00 19.96 ? 124 GLY   A CA  1 
ATOM   932  C  C   . GLY   A 1 124 ? 19.023  22.706 13.583 1.00 19.37 ? 124 GLY   A C   1 
ATOM   933  O  O   . GLY   A 1 124 ? 19.607  22.063 12.713 1.00 22.49 ? 124 GLY   A O   1 
ATOM   934  N  N   . THR   A 1 125 ? 17.744  23.081 13.546 1.00 20.68 ? 125 THR   A N   1 
ATOM   935  C  CA  . THR   A 1 125 ? 16.854  22.639 12.470 1.00 19.49 ? 125 THR   A CA  1 
ATOM   936  C  C   . THR   A 1 125 ? 16.033  23.834 12.049 1.00 20.54 ? 125 THR   A C   1 
ATOM   937  O  O   . THR   A 1 125 ? 15.918  24.818 12.788 1.00 22.94 ? 125 THR   A O   1 
ATOM   938  C  CB  . THR   A 1 125 ? 15.945  21.503 12.997 1.00 20.96 ? 125 THR   A CB  1 
ATOM   939  O  OG1 . THR   A 1 125 ? 15.273  21.935 14.189 1.00 19.37 ? 125 THR   A OG1 1 
ATOM   940  C  CG2 . THR   A 1 125 ? 16.710  20.235 13.252 1.00 24.14 ? 125 THR   A CG2 1 
ATOM   941  N  N   . TRP   A 1 126 ? 15.415  23.762 10.836 1.00 19.94 ? 126 TRP   A N   1 
ATOM   942  C  CA  . TRP   A 1 126 ? 14.356  24.679 10.515 1.00 19.25 ? 126 TRP   A CA  1 
ATOM   943  C  C   . TRP   A 1 126 ? 13.018  23.942 10.664 1.00 20.69 ? 126 TRP   A C   1 
ATOM   944  O  O   . TRP   A 1 126 ? 12.975  22.729 10.478 1.00 21.12 ? 126 TRP   A O   1 
ATOM   945  C  CB  . TRP   A 1 126 ? 14.518  25.312 9.116  1.00 21.81 ? 126 TRP   A CB  1 
ATOM   946  C  CG  . TRP   A 1 126 ? 14.334  24.400 7.936  1.00 23.30 ? 126 TRP   A CG  1 
ATOM   947  C  CD1 . TRP   A 1 126 ? 15.261  23.640 7.301  1.00 21.15 ? 126 TRP   A CD1 1 
ATOM   948  C  CD2 . TRP   A 1 126 ? 13.072  24.161 7.254  1.00 22.35 ? 126 TRP   A CD2 1 
ATOM   949  N  NE1 . TRP   A 1 126 ? 14.675  22.985 6.245  1.00 23.52 ? 126 TRP   A NE1 1 
ATOM   950  C  CE2 . TRP   A 1 126 ? 13.345  23.276 6.193  1.00 24.91 ? 126 TRP   A CE2 1 
ATOM   951  C  CE3 . TRP   A 1 126 ? 11.780  24.641 7.423  1.00 21.93 ? 126 TRP   A CE3 1 
ATOM   952  C  CZ2 . TRP   A 1 126 ? 12.354  22.814 5.320  1.00 23.56 ? 126 TRP   A CZ2 1 
ATOM   953  C  CZ3 . TRP   A 1 126 ? 10.813  24.233 6.529  1.00 26.46 ? 126 TRP   A CZ3 1 
ATOM   954  C  CH2 . TRP   A 1 126 ? 11.098  23.323 5.507  1.00 23.67 ? 126 TRP   A CH2 1 
ATOM   955  N  N   . ILE   A 1 127 ? 11.985  24.687 11.022 1.00 22.57 ? 127 ILE   A N   1 
ATOM   956  C  CA  . ILE   A 1 127 ? 10.736  24.096 11.472 1.00 23.97 ? 127 ILE   A CA  1 
ATOM   957  C  C   . ILE   A 1 127 ? 9.547   24.575 10.672 1.00 27.74 ? 127 ILE   A C   1 
ATOM   958  O  O   . ILE   A 1 127 ? 9.505   25.673 10.109 1.00 28.65 ? 127 ILE   A O   1 
ATOM   959  C  CB  . ILE   A 1 127 ? 10.500  24.316 12.970 1.00 25.04 ? 127 ILE   A CB  1 
ATOM   960  C  CG1 . ILE   A 1 127 ? 10.122  25.757 13.304 1.00 31.43 ? 127 ILE   A CG1 1 
ATOM   961  C  CG2 . ILE   A 1 127 ? 11.709  23.823 13.713 1.00 25.40 ? 127 ILE   A CG2 1 
ATOM   962  C  CD1 . ILE   A 1 127 ? 9.630   25.968 14.720 1.00 33.47 ? 127 ILE   A CD1 1 
ATOM   963  N  N   . GLU   A 1 128 ? 8.516   23.723 10.729 1.00 24.46 ? 128 GLU   A N   1 
ATOM   964  C  CA  . GLU   A 1 128 ? 7.162   24.095 10.368 1.00 25.41 ? 128 GLU   A CA  1 
ATOM   965  C  C   . GLU   A 1 128 ? 6.296   23.777 11.585 1.00 23.60 ? 128 GLU   A C   1 
ATOM   966  O  O   . GLU   A 1 128 ? 6.532   22.760 12.210 1.00 22.86 ? 128 GLU   A O   1 
ATOM   967  C  CB  . GLU   A 1 128 ? 6.698   23.327 9.137  1.00 29.00 ? 128 GLU   A CB  1 
ATOM   968  C  CG  . GLU   A 1 128 ? 7.650   23.514 7.959  1.00 30.90 ? 128 GLU   A CG  1 
ATOM   969  C  CD  . GLU   A 1 128 ? 7.358   22.511 6.857  1.00 30.27 ? 128 GLU   A CD  1 
ATOM   970  O  OE1 . GLU   A 1 128 ? 7.773   21.347 6.886  1.00 28.76 ? 128 GLU   A OE1 1 
ATOM   971  O  OE2 . GLU   A 1 128 ? 6.638   22.971 5.972  1.00 34.49 ? 128 GLU   A OE2 1 
ATOM   972  N  N   . GLU   A 1 129 ? 5.355   24.676 11.859 1.00 23.76 ? 129 GLU   A N   1 
ATOM   973  C  CA  . GLU   A 1 129 ? 4.468   24.554 13.032 1.00 26.31 ? 129 GLU   A CA  1 
ATOM   974  C  C   . GLU   A 1 129 ? 2.998   24.634 12.625 1.00 29.40 ? 129 GLU   A C   1 
ATOM   975  O  O   . GLU   A 1 129 ? 2.670   25.411 11.722 1.00 27.75 ? 129 GLU   A O   1 
ATOM   976  C  CB  . GLU   A 1 129 ? 4.736   25.679 14.026 1.00 31.98 ? 129 GLU   A CB  1 
ATOM   977  C  CG  . GLU   A 1 129 ? 6.132   25.653 14.634 1.00 34.29 ? 129 GLU   A CG  1 
ATOM   978  C  CD  . GLU   A 1 129 ? 6.361   26.872 15.506 1.00 42.53 ? 129 GLU   A CD  1 
ATOM   979  O  OE1 . GLU   A 1 129 ? 6.578   27.960 14.942 1.00 43.08 ? 129 GLU   A OE1 1 
ATOM   980  O  OE2 . GLU   A 1 129 ? 6.326   26.732 16.739 1.00 39.04 ? 129 GLU   A OE2 1 
ATOM   981  N  N   . PHE   A 1 130 ? 2.162   23.854 13.290 1.00 25.48 ? 130 PHE   A N   1 
ATOM   982  C  CA  . PHE   A 1 130 ? 0.744   23.807 13.069 1.00 26.64 ? 130 PHE   A CA  1 
ATOM   983  C  C   . PHE   A 1 130 ? 0.006   23.777 14.411 1.00 29.59 ? 130 PHE   A C   1 
ATOM   984  O  O   . PHE   A 1 130 ? 0.370   22.978 15.261 1.00 28.97 ? 130 PHE   A O   1 
ATOM   985  C  CB  . PHE   A 1 130 ? 0.467   22.525 12.302 1.00 26.28 ? 130 PHE   A CB  1 
ATOM   986  C  CG  . PHE   A 1 130 ? 1.224   22.398 10.984 1.00 24.16 ? 130 PHE   A CG  1 
ATOM   987  C  CD1 . PHE   A 1 130 ? 0.687   22.927 9.818  1.00 25.14 ? 130 PHE   A CD1 1 
ATOM   988  C  CD2 . PHE   A 1 130 ? 2.436   21.725 10.920 1.00 24.23 ? 130 PHE   A CD2 1 
ATOM   989  C  CE1 . PHE   A 1 130 ? 1.342   22.785 8.614  1.00 27.82 ? 130 PHE   A CE1 1 
ATOM   990  C  CE2 . PHE   A 1 130 ? 3.090   21.590 9.699  1.00 25.97 ? 130 PHE   A CE2 1 
ATOM   991  C  CZ  . PHE   A 1 130 ? 2.538   22.141 8.558  1.00 26.85 ? 130 PHE   A CZ  1 
ATOM   992  N  N   . THR   A 1 131 ? -1.007  24.657 14.574 1.00 33.57 ? 131 THR   A N   1 
ATOM   993  C  CA  . THR   A 1 131 ? -1.911  24.666 15.734 1.00 34.75 ? 131 THR   A CA  1 
ATOM   994  C  C   . THR   A 1 131 ? -3.349  24.500 15.233 1.00 39.47 ? 131 THR   A C   1 
ATOM   995  O  O   . THR   A 1 131 ? -3.596  24.616 14.028 1.00 42.57 ? 131 THR   A O   1 
ATOM   996  C  CB  . THR   A 1 131 ? -1.710  25.962 16.509 1.00 40.93 ? 131 THR   A CB  1 
ATOM   997  O  OG1 . THR   A 1 131 ? -2.224  26.871 15.541 1.00 42.51 ? 131 THR   A OG1 1 
ATOM   998  C  CG2 . THR   A 1 131 ? -0.264  26.291 16.822 1.00 38.00 ? 131 THR   A CG2 1 
ATOM   999  N  N   . PHE   A 1 132 ? -4.294  24.082 16.093 1.00 41.93 ? 132 PHE   A N   1 
ATOM   1000 C  CA  . PHE   A 1 132 ? -5.567  23.559 15.581 1.00 45.78 ? 132 PHE   A CA  1 
ATOM   1001 C  C   . PHE   A 1 132 ? -6.821  24.281 16.172 1.00 48.89 ? 132 PHE   A C   1 
ATOM   1002 O  O   . PHE   A 1 132 ? -6.737  24.621 17.358 1.00 52.85 ? 132 PHE   A O   1 
ATOM   1003 C  CB  . PHE   A 1 132 ? -5.555  22.055 15.868 1.00 46.31 ? 132 PHE   A CB  1 
ATOM   1004 C  CG  . PHE   A 1 132 ? -4.512  21.335 15.028 1.00 34.99 ? 132 PHE   A CG  1 
ATOM   1005 C  CD1 . PHE   A 1 132 ? -4.774  21.000 13.709 1.00 42.71 ? 132 PHE   A CD1 1 
ATOM   1006 C  CD2 . PHE   A 1 132 ? -3.261  21.069 15.541 1.00 32.33 ? 132 PHE   A CD2 1 
ATOM   1007 C  CE1 . PHE   A 1 132 ? -3.810  20.374 12.933 1.00 40.91 ? 132 PHE   A CE1 1 
ATOM   1008 C  CE2 . PHE   A 1 132 ? -2.288  20.449 14.762 1.00 33.39 ? 132 PHE   A CE2 1 
ATOM   1009 C  CZ  . PHE   A 1 132 ? -2.565  20.108 13.455 1.00 34.49 ? 132 PHE   A CZ  1 
ATOM   1010 N  N   . ARG   B 1 9   ? -0.918  18.945 32.678 1.00 33.61 ? 9   ARG   B N   1 
ATOM   1011 C  CA  . ARG   B 1 9   ? 0.382   18.778 31.958 1.00 29.57 ? 9   ARG   B CA  1 
ATOM   1012 C  C   . ARG   B 1 9   ? 0.122   18.258 30.551 1.00 27.87 ? 9   ARG   B C   1 
ATOM   1013 O  O   . ARG   B 1 9   ? -0.512  17.216 30.383 1.00 30.90 ? 9   ARG   B O   1 
ATOM   1014 C  CB  . ARG   B 1 9   ? 1.303   17.736 32.584 1.00 30.59 ? 9   ARG   B CB  1 
ATOM   1015 C  CG  . ARG   B 1 9   ? 1.931   18.214 33.881 1.00 32.29 ? 9   ARG   B CG  1 
ATOM   1016 C  CD  . ARG   B 1 9   ? 2.716   17.134 34.537 1.00 33.86 ? 9   ARG   B CD  1 
ATOM   1017 N  NE  . ARG   B 1 9   ? 3.397   17.710 35.701 1.00 36.66 ? 9   ARG   B NE  1 
ATOM   1018 C  CZ  . ARG   B 1 9   ? 4.299   17.116 36.451 1.00 33.99 ? 9   ARG   B CZ  1 
ATOM   1019 N  NH1 . ARG   B 1 9   ? 4.695   15.893 36.209 1.00 33.96 ? 9   ARG   B NH1 1 
ATOM   1020 N  NH2 . ARG   B 1 9   ? 4.864   17.801 37.424 1.00 36.57 ? 9   ARG   B NH2 1 
ATOM   1021 N  N   . LEU   B 1 10  ? 0.667   18.946 29.550 1.00 26.02 ? 10  LEU   B N   1 
ATOM   1022 C  CA  . LEU   B 1 10  ? 0.656   18.423 28.198 1.00 26.30 ? 10  LEU   B CA  1 
ATOM   1023 C  C   . LEU   B 1 10  ? 1.789   17.437 28.004 1.00 21.95 ? 10  LEU   B C   1 
ATOM   1024 O  O   . LEU   B 1 10  ? 2.815   17.447 28.685 1.00 21.17 ? 10  LEU   B O   1 
ATOM   1025 C  CB  . LEU   B 1 10  ? 0.709   19.585 27.212 1.00 26.37 ? 10  LEU   B CB  1 
ATOM   1026 C  CG  . LEU   B 1 10  ? -0.493  20.511 27.208 1.00 29.85 ? 10  LEU   B CG  1 
ATOM   1027 C  CD1 . LEU   B 1 10  ? -0.295  21.622 26.172 1.00 35.01 ? 10  LEU   B CD1 1 
ATOM   1028 C  CD2 . LEU   B 1 10  ? -1.751  19.768 26.941 1.00 30.60 ? 10  LEU   B CD2 1 
ATOM   1029 N  N   . LEU   B 1 11  ? 1.551   16.566 27.027 1.00 22.26 ? 11  LEU   B N   1 
ATOM   1030 C  CA  . LEU   B 1 11  ? 2.542   15.526 26.698 1.00 21.91 ? 11  LEU   B CA  1 
ATOM   1031 C  C   . LEU   B 1 11  ? 3.050   15.732 25.269 1.00 22.42 ? 11  LEU   B C   1 
ATOM   1032 O  O   . LEU   B 1 11  ? 2.338   16.319 24.469 1.00 22.88 ? 11  LEU   B O   1 
ATOM   1033 C  CB  . LEU   B 1 11  ? 1.908   14.148 26.836 1.00 23.60 ? 11  LEU   B CB  1 
ATOM   1034 C  CG  . LEU   B 1 11  ? 1.287   13.841 28.199 1.00 30.21 ? 11  LEU   B CG  1 
ATOM   1035 C  CD1 . LEU   B 1 11  ? 0.331   12.676 28.083 1.00 37.21 ? 11  LEU   B CD1 1 
ATOM   1036 C  CD2 . LEU   B 1 11  ? 2.386   13.554 29.200 1.00 29.62 ? 11  LEU   B CD2 1 
ATOM   1037 N  N   . CYS   B 1 12  ? 4.232   15.188 25.006 1.00 23.00 ? 12  CYS   B N   1 
ATOM   1038 C  CA  . CYS   B 1 12  ? 4.838   15.315 23.665 1.00 23.35 ? 12  CYS   B CA  1 
ATOM   1039 C  C   . CYS   B 1 12  ? 5.333   13.956 23.166 1.00 20.43 ? 12  CYS   B C   1 
ATOM   1040 O  O   . CYS   B 1 12  ? 6.088   13.301 23.883 1.00 20.14 ? 12  CYS   B O   1 
ATOM   1041 C  CB  . CYS   B 1 12  ? 5.996   16.304 23.655 1.00 21.05 ? 12  CYS   B CB  1 
ATOM   1042 S  SG  . CYS   B 1 12  ? 6.703   16.577 22.012 1.00 26.90 ? 12  CYS   B SG  1 
HETATM 1043 N  N   . PBF   B 1 13  ? 4.874   13.573 21.982 1.00 21.09 ? 13  PBF   B N   1 
HETATM 1044 C  C   . PBF   B 1 13  ? 6.339   12.815 20.251 1.00 18.66 ? 13  PBF   B C   1 
HETATM 1045 O  O   . PBF   B 1 13  ? 5.923   13.535 19.349 1.00 19.44 ? 13  PBF   B O   1 
HETATM 1046 C  CA  . PBF   B 1 13  ? 5.363   12.342 21.326 1.00 19.11 ? 13  PBF   B CA  1 
HETATM 1047 C  CB  . PBF   B 1 13  ? 4.199   11.549 20.737 1.00 20.20 ? 13  PBF   B CB  1 
HETATM 1048 C  CG  . PBF   B 1 13  ? 4.524   10.248 20.054 1.00 17.60 ? 13  PBF   B CG  1 
HETATM 1049 C  CD1 . PBF   B 1 13  ? 5.533   9.413  20.508 1.00 17.56 ? 13  PBF   B CD1 1 
HETATM 1050 C  CD2 . PBF   B 1 13  ? 3.773   9.837  18.969 1.00 21.41 ? 13  PBF   B CD2 1 
HETATM 1051 C  CE1 . PBF   B 1 13  ? 5.794   8.206  19.885 1.00 21.54 ? 13  PBF   B CE1 1 
HETATM 1052 C  CE2 . PBF   B 1 13  ? 4.024   8.637  18.338 1.00 20.92 ? 13  PBF   B CE2 1 
HETATM 1053 C  CZ  . PBF   B 1 13  ? 5.049   7.812  18.779 1.00 21.40 ? 13  PBF   B CZ  1 
HETATM 1054 C  CN1 . PBF   B 1 13  ? 5.264   6.519  18.077 1.00 27.07 ? 13  PBF   B CN1 1 
HETATM 1055 O  ON2 . PBF   B 1 13  ? 4.294   5.826  17.812 1.00 26.87 ? 13  PBF   B ON2 1 
HETATM 1056 C  CT  . PBF   B 1 13  ? 6.618   6.056  17.669 1.00 24.42 ? 13  PBF   B CT  1 
HETATM 1057 C  CI1 . PBF   B 1 13  ? 7.700   6.924  17.599 1.00 22.80 ? 13  PBF   B CI1 1 
HETATM 1058 C  CI2 . PBF   B 1 13  ? 6.801   4.727  17.311 1.00 26.58 ? 13  PBF   B CI2 1 
HETATM 1059 C  CK1 . PBF   B 1 13  ? 8.940   6.461  17.201 1.00 22.66 ? 13  PBF   B CK1 1 
HETATM 1060 C  CK2 . PBF   B 1 13  ? 8.046   4.277  16.913 1.00 28.73 ? 13  PBF   B CK2 1 
HETATM 1061 C  CL  . PBF   B 1 13  ? 9.112   5.142  16.859 1.00 26.63 ? 13  PBF   B CL  1 
ATOM   1062 N  N   . SER   B 1 14  ? 7.594   12.435 20.407 1.00 20.76 ? 14  SER   B N   1 
ATOM   1063 C  CA  . SER   B 1 14  ? 8.643   12.893 19.476 1.00 22.04 ? 14  SER   B CA  1 
ATOM   1064 C  C   . SER   B 1 14  ? 9.089   11.702 18.627 1.00 20.39 ? 14  SER   B C   1 
ATOM   1065 O  O   . SER   B 1 14  ? 9.268   10.618 19.167 1.00 19.58 ? 14  SER   B O   1 
ATOM   1066 C  CB  . SER   B 1 14  ? 9.793   13.557 20.224 1.00 23.62 ? 14  SER   B CB  1 
ATOM   1067 O  OG  . SER   B 1 14  ? 9.341   14.698 20.936 1.00 24.82 ? 14  SER   B OG  1 
ATOM   1068 N  N   . ILE   B 1 15  ? 9.235   11.948 17.337 1.00 19.36 ? 15  ILE   B N   1 
ATOM   1069 C  CA  . ILE   B 1 15  ? 9.627   10.868 16.406 1.00 18.96 ? 15  ILE   B CA  1 
ATOM   1070 C  C   . ILE   B 1 15  ? 10.859  11.273 15.590 1.00 18.41 ? 15  ILE   B C   1 
ATOM   1071 O  O   . ILE   B 1 15  ? 10.758  12.243 14.843 1.00 18.45 ? 15  ILE   B O   1 
ATOM   1072 C  CB  . ILE   B 1 15  ? 8.438   10.516 15.488 1.00 20.50 ? 15  ILE   B CB  1 
ATOM   1073 C  CG1 . ILE   B 1 15  ? 7.137   10.415 16.291 1.00 24.44 ? 15  ILE   B CG1 1 
ATOM   1074 C  CG2 . ILE   B 1 15  ? 8.705   9.258  14.666 1.00 21.67 ? 15  ILE   B CG2 1 
ATOM   1075 C  CD1 . ILE   B 1 15  ? 5.919   10.093 15.449 1.00 35.04 ? 15  ILE   B CD1 1 
ATOM   1076 N  N   . TYR   B 1 16  ? 11.933  10.514 15.758 1.00 19.47 ? 16  TYR   B N   1 
ATOM   1077 C  CA  . TYR   B 1 16  ? 13.234  10.836 15.122 1.00 20.17 ? 16  TYR   B CA  1 
ATOM   1078 C  C   . TYR   B 1 16  ? 13.390  9.978  13.885 1.00 17.56 ? 16  TYR   B C   1 
ATOM   1079 O  O   . TYR   B 1 16  ? 13.620  8.777  13.992 1.00 19.86 ? 16  TYR   B O   1 
ATOM   1080 C  CB  . TYR   B 1 16  ? 14.278  10.683 16.230 1.00 22.66 ? 16  TYR   B CB  1 
ATOM   1081 C  CG  . TYR   B 1 16  ? 14.048  11.594 17.427 1.00 23.74 ? 16  TYR   B CG  1 
ATOM   1082 C  CD1 . TYR   B 1 16  ? 13.203  11.220 18.463 1.00 29.07 ? 16  TYR   B CD1 1 
ATOM   1083 C  CD2 . TYR   B 1 16  ? 14.677  12.827 17.520 1.00 26.55 ? 16  TYR   B CD2 1 
ATOM   1084 C  CE1 . TYR   B 1 16  ? 12.981  12.049 19.548 1.00 33.28 ? 16  TYR   B CE1 1 
ATOM   1085 C  CE2 . TYR   B 1 16  ? 14.468  13.664 18.602 1.00 26.36 ? 16  TYR   B CE2 1 
ATOM   1086 C  CZ  . TYR   B 1 16  ? 13.616  13.275 19.618 1.00 34.79 ? 16  TYR   B CZ  1 
ATOM   1087 O  OH  . TYR   B 1 16  ? 13.409  14.092 20.691 1.00 44.61 ? 16  TYR   B OH  1 
ATOM   1088 N  N   . VAL   B 1 17  ? 13.346  10.628 12.737 1.00 18.70 ? 17  VAL   B N   1 
ATOM   1089 C  CA  . VAL   B 1 17  ? 13.350  9.946  11.460 1.00 19.03 ? 17  VAL   B CA  1 
ATOM   1090 C  C   . VAL   B 1 17  ? 14.690  10.036 10.740 1.00 19.05 ? 17  VAL   B C   1 
ATOM   1091 O  O   . VAL   B 1 17  ? 15.241  11.141 10.555 1.00 19.58 ? 17  VAL   B O   1 
ATOM   1092 C  CB  . VAL   B 1 17  ? 12.227  10.509 10.594 1.00 19.09 ? 17  VAL   B CB  1 
ATOM   1093 C  CG1 . VAL   B 1 17  ? 12.269  9.939  9.183  1.00 19.28 ? 17  VAL   B CG1 1 
ATOM   1094 C  CG2 . VAL   B 1 17  ? 10.866  10.187 11.249 1.00 22.84 ? 17  VAL   B CG2 1 
ATOM   1095 N  N   . THR   B 1 18  ? 15.107  8.893  10.238 1.00 19.89 ? 18  THR   B N   1 
ATOM   1096 C  CA  . THR   B 1 18  ? 16.236  8.793  9.317  1.00 19.29 ? 18  THR   B CA  1 
ATOM   1097 C  C   . THR   B 1 18  ? 15.638  8.631  7.922  1.00 23.00 ? 18  THR   B C   1 
ATOM   1098 O  O   . THR   B 1 18  ? 14.741  7.787  7.737  1.00 19.90 ? 18  THR   B O   1 
ATOM   1099 C  CB  . THR   B 1 18  ? 17.149  7.631  9.699  1.00 21.90 ? 18  THR   B CB  1 
ATOM   1100 O  OG1 . THR   B 1 18  ? 17.670  7.841  11.018 1.00 20.73 ? 18  THR   B OG1 1 
ATOM   1101 C  CG2 . THR   B 1 18  ? 18.245  7.438  8.655  1.00 22.27 ? 18  THR   B CG2 1 
ATOM   1102 N  N   . LYS   B 1 19  ? 16.105  9.418  6.937  1.00 18.95 ? 19  LYS   B N   1 
ATOM   1103 C  CA  . LYS   B 1 19  ? 15.504  9.322  5.616  1.00 20.49 ? 19  LYS   B CA  1 
ATOM   1104 C  C   . LYS   B 1 19  ? 15.667  7.939  4.997  1.00 19.74 ? 19  LYS   B C   1 
ATOM   1105 O  O   . LYS   B 1 19  ? 16.615  7.177  5.244  1.00 21.07 ? 19  LYS   B O   1 
ATOM   1106 C  CB  . LYS   B 1 19  ? 16.025  10.381 4.641  1.00 23.50 ? 19  LYS   B CB  1 
ATOM   1107 C  CG  . LYS   B 1 19  ? 17.473  10.237 4.234  1.00 25.96 ? 19  LYS   B CG  1 
ATOM   1108 C  CD  . LYS   B 1 19  ? 17.793  11.460 3.354  1.00 30.24 ? 19  LYS   B CD  1 
ATOM   1109 C  CE  . LYS   B 1 19  ? 19.222  11.605 2.978  1.00 33.70 ? 19  LYS   B CE  1 
ATOM   1110 N  NZ  . LYS   B 1 19  ? 19.660  10.486 2.186  1.00 36.61 ? 19  LYS   B NZ  1 
ATOM   1111 N  N   . LYS   B 1 20  ? 14.758  7.643  4.068  1.00 20.13 ? 20  LYS   B N   1 
ATOM   1112 C  CA  . LYS   B 1 20  ? 14.764  6.419  3.284  1.00 21.87 ? 20  LYS   B CA  1 
ATOM   1113 C  C   . LYS   B 1 20  ? 16.107  6.272  2.576  1.00 21.66 ? 20  LYS   B C   1 
ATOM   1114 O  O   . LYS   B 1 20  ? 16.569  7.238  1.983  1.00 22.39 ? 20  LYS   B O   1 
ATOM   1115 C  CB  . LYS   B 1 20  ? 13.638  6.577  2.242  1.00 25.20 ? 20  LYS   B CB  1 
ATOM   1116 C  CG  . LYS   B 1 20  ? 13.454  5.495  1.240  1.00 30.05 ? 20  LYS   B CG  1 
ATOM   1117 C  CD  . LYS   B 1 20  ? 12.169  5.728  0.426  1.00 28.62 ? 20  LYS   B CD  1 
ATOM   1118 C  CE  . LYS   B 1 20  ? 11.907  4.547  -0.452 1.00 33.71 ? 20  LYS   B CE  1 
ATOM   1119 N  NZ  . LYS   B 1 20  ? 12.857  4.523  -1.568 1.00 28.11 ? 20  LYS   B NZ  1 
ATOM   1120 N  N   . PRO   B 1 21  ? 16.723  5.074  2.595  1.00 27.04 ? 21  PRO   B N   1 
ATOM   1121 C  CA  . PRO   B 1 21  ? 18.074  4.887  2.087  1.00 30.70 ? 21  PRO   B CA  1 
ATOM   1122 C  C   . PRO   B 1 21  ? 18.121  5.394  0.648  1.00 36.80 ? 21  PRO   B C   1 
ATOM   1123 O  O   . PRO   B 1 21  ? 17.207  5.134  -0.135 1.00 33.08 ? 21  PRO   B O   1 
ATOM   1124 C  CB  . PRO   B 1 21  ? 18.275  3.353  2.175  1.00 33.39 ? 21  PRO   B CB  1 
ATOM   1125 C  CG  . PRO   B 1 21  ? 17.368  2.891  3.287  1.00 34.15 ? 21  PRO   B CG  1 
ATOM   1126 C  CD  . PRO   B 1 21  ? 16.183  3.849  3.213  1.00 31.11 ? 21  PRO   B CD  1 
ATOM   1127 N  N   . ASP   B 1 22  ? 19.155  6.147  0.308  1.00 39.91 ? 22  ASP   B N   1 
ATOM   1128 C  CA  . ASP   B 1 22  ? 19.338  6.537  -1.085 1.00 50.26 ? 22  ASP   B CA  1 
ATOM   1129 C  C   . ASP   B 1 22  ? 18.319  7.579  -1.566 1.00 49.51 ? 22  ASP   B C   1 
ATOM   1130 O  O   . ASP   B 1 22  ? 18.484  8.091  -2.667 1.00 45.42 ? 22  ASP   B O   1 
ATOM   1131 C  CB  . ASP   B 1 22  ? 19.354  5.330  -2.020 1.00 59.51 ? 22  ASP   B CB  1 
ATOM   1132 C  CG  . ASP   B 1 22  ? 20.431  4.276  -1.739 1.00 62.77 ? 22  ASP   B CG  1 
ATOM   1133 O  OD1 . ASP   B 1 22  ? 21.428  4.601  -1.065 1.00 53.83 ? 22  ASP   B OD1 1 
ATOM   1134 O  OD2 . ASP   B 1 22  ? 20.252  3.121  -2.174 1.00 64.09 ? 22  ASP   B OD2 1 
ATOM   1135 N  N   . GLN   B 1 23  ? 17.300  7.960  -0.774 1.00 34.48 ? 23  GLN   B N   1 
ATOM   1136 C  CA  . GLN   B 1 23  ? 16.476  9.105  -1.138 1.00 26.76 ? 23  GLN   B CA  1 
ATOM   1137 C  C   . GLN   B 1 23  ? 17.298  10.378 -0.914 1.00 26.67 ? 23  GLN   B C   1 
ATOM   1138 O  O   . GLN   B 1 23  ? 17.943  10.565 0.132  1.00 28.84 ? 23  GLN   B O   1 
ATOM   1139 C  CB  . GLN   B 1 23  ? 15.231  9.134  -0.233 1.00 26.95 ? 23  GLN   B CB  1 
ATOM   1140 C  CG  . GLN   B 1 23  ? 14.287  10.278 -0.531 1.00 27.29 ? 23  GLN   B CG  1 
ATOM   1141 C  CD  . GLN   B 1 23  ? 13.023  10.207 0.306  1.00 25.77 ? 23  GLN   B CD  1 
ATOM   1142 O  OE1 . GLN   B 1 23  ? 13.086  10.256 1.525  1.00 22.73 ? 23  GLN   B OE1 1 
ATOM   1143 N  NE2 . GLN   B 1 23  ? 11.889  10.225 -0.359 1.00 26.13 ? 23  GLN   B NE2 1 
ATOM   1144 N  N   . SER   B 1 24  ? 17.244  11.306 -1.868 1.00 26.34 ? 24  SER   B N   1 
ATOM   1145 C  CA  . SER   B 1 24  ? 18.003  12.533 -1.720 1.00 26.72 ? 24  SER   B CA  1 
ATOM   1146 C  C   . SER   B 1 24  ? 17.417  13.381 -0.588 1.00 26.54 ? 24  SER   B C   1 
ATOM   1147 O  O   . SER   B 1 24  ? 16.223  13.314 -0.291 1.00 23.90 ? 24  SER   B O   1 
ATOM   1148 C  CB  . SER   B 1 24  ? 18.000  13.286 -3.008 1.00 24.87 ? 24  SER   B CB  1 
ATOM   1149 O  OG  . SER   B 1 24  ? 16.782  13.949 -3.254 1.00 21.42 ? 24  SER   B OG  1 
ATOM   1150 N  N   . GLU   B 1 25  ? 18.214  14.264 -0.010 1.00 25.14 ? 25  GLU   B N   1 
ATOM   1151 C  CA  . GLU   B 1 25  ? 17.679  15.178 1.031  1.00 27.48 ? 25  GLU   B CA  1 
ATOM   1152 C  C   . GLU   B 1 25  ? 16.532  16.032 0.459  1.00 24.65 ? 25  GLU   B C   1 
ATOM   1153 O  O   . GLU   B 1 25  ? 15.511  16.165 1.129  1.00 23.08 ? 25  GLU   B O   1 
ATOM   1154 C  CB  . GLU   B 1 25  ? 18.875  15.974 1.554  1.00 32.70 ? 25  GLU   B CB  1 
ATOM   1155 C  CG  . GLU   B 1 25  ? 18.541  17.121 2.494  1.00 43.27 ? 25  GLU   B CG  1 
ATOM   1156 C  CD  . GLU   B 1 25  ? 19.807  17.937 2.672  1.00 41.01 ? 25  GLU   B CD  1 
ATOM   1157 O  OE1 . GLU   B 1 25  ? 19.863  19.038 2.093  1.00 29.64 ? 25  GLU   B OE1 1 
ATOM   1158 O  OE2 . GLU   B 1 25  ? 20.726  17.464 3.366  1.00 40.27 ? 25  GLU   B OE2 1 
ATOM   1159 N  N   . GLU   B 1 26  ? 16.698  16.562 -0.750 1.00 22.18 ? 26  GLU   B N   1 
ATOM   1160 C  CA  . GLU   B 1 26  ? 15.695  17.407 -1.317 1.00 24.76 ? 26  GLU   B CA  1 
ATOM   1161 C  C   . GLU   B 1 26  ? 14.378  16.619 -1.467 1.00 21.39 ? 26  GLU   B C   1 
ATOM   1162 O  O   . GLU   B 1 26  ? 13.310  17.158 -1.153 1.00 21.98 ? 26  GLU   B O   1 
ATOM   1163 C  CB  . GLU   B 1 26  ? 16.209  17.856 -2.691 1.00 28.62 ? 26  GLU   B CB  1 
ATOM   1164 C  CG  . GLU   B 1 26  ? 15.412  18.964 -3.343 1.00 45.24 ? 26  GLU   B CG  1 
ATOM   1165 C  CD  . GLU   B 1 26  ? 16.127  19.462 -4.610 1.00 46.20 ? 26  GLU   B CD  1 
ATOM   1166 O  OE1 . GLU   B 1 26  ? 17.128  20.155 -4.483 1.00 52.17 ? 26  GLU   B OE1 1 
ATOM   1167 O  OE2 . GLU   B 1 26  ? 15.717  19.074 -5.703 1.00 57.35 ? 26  GLU   B OE2 1 
ATOM   1168 N  N   . ASP   B 1 27  ? 14.481  15.391 -1.929 1.00 20.79 ? 27  ASP   B N   1 
ATOM   1169 C  CA  . ASP   B 1 27  ? 13.272  14.609 -2.189 1.00 20.04 ? 27  ASP   B CA  1 
ATOM   1170 C  C   . ASP   B 1 27  ? 12.598  14.267 -0.849 1.00 20.46 ? 27  ASP   B C   1 
ATOM   1171 O  O   . ASP   B 1 27  ? 11.371  14.317 -0.724 1.00 21.23 ? 27  ASP   B O   1 
ATOM   1172 C  CB  . ASP   B 1 27  ? 13.555  13.384 -3.029 1.00 22.82 ? 27  ASP   B CB  1 
ATOM   1173 C  CG  . ASP   B 1 27  ? 13.787  13.624 -4.519 1.00 25.46 ? 27  ASP   B CG  1 
ATOM   1174 O  OD1 . ASP   B 1 27  ? 13.576  14.733 -4.946 1.00 24.83 ? 27  ASP   B OD1 1 
ATOM   1175 O  OD2 . ASP   B 1 27  ? 14.274  12.701 -5.183 1.00 27.30 ? 27  ASP   B OD2 1 
ATOM   1176 N  N   . HIS   B 1 28  ? 13.427  13.975 0.154  1.00 19.73 ? 28  HIS   B N   1 
ATOM   1177 C  CA  . HIS   B 1 28  ? 12.926  13.653 1.486  1.00 19.80 ? 28  HIS   B CA  1 
ATOM   1178 C  C   . HIS   B 1 28  ? 12.137  14.804 2.071  1.00 20.48 ? 28  HIS   B C   1 
ATOM   1179 O  O   . HIS   B 1 28  ? 10.986  14.648 2.475  1.00 20.43 ? 28  HIS   B O   1 
ATOM   1180 C  CB  . HIS   B 1 28  ? 14.043  13.163 2.403  1.00 19.82 ? 28  HIS   B CB  1 
ATOM   1181 C  CG  . HIS   B 1 28  ? 13.640  13.017 3.834  1.00 18.83 ? 28  HIS   B CG  1 
ATOM   1182 N  ND1 . HIS   B 1 28  ? 13.055  11.833 4.279  1.00 18.16 ? 28  HIS   B ND1 1 
ATOM   1183 C  CD2 . HIS   B 1 28  ? 13.741  13.822 4.929  1.00 19.46 ? 28  HIS   B CD2 1 
ATOM   1184 C  CE1 . HIS   B 1 28  ? 12.871  11.928 5.587  1.00 16.94 ? 28  HIS   B CE1 1 
ATOM   1185 N  NE2 . HIS   B 1 28  ? 13.230  13.133 6.006  1.00 19.41 ? 28  HIS   B NE2 1 
ATOM   1186 N  N   . HIS   B 1 29  ? 12.750  16.002 2.145  1.00 19.78 ? 29  HIS   B N   1 
ATOM   1187 C  CA  . HIS   B 1 29  ? 12.100  17.129 2.781  1.00 20.76 ? 29  HIS   B CA  1 
ATOM   1188 C  C   . HIS   B 1 29  ? 10.881  17.636 2.001  1.00 20.35 ? 29  HIS   B C   1 
ATOM   1189 O  O   . HIS   B 1 29  ? 9.911   18.062 2.620  1.00 20.56 ? 29  HIS   B O   1 
ATOM   1190 C  CB  . HIS   B 1 29  ? 13.158  18.204 3.121  1.00 20.48 ? 29  HIS   B CB  1 
ATOM   1191 C  CG  . HIS   B 1 29  ? 14.136  17.725 4.152  1.00 19.92 ? 29  HIS   B CG  1 
ATOM   1192 N  ND1 . HIS   B 1 29  ? 13.803  17.689 5.497  1.00 21.71 ? 29  HIS   B ND1 1 
ATOM   1193 C  CD2 . HIS   B 1 29  ? 15.313  17.150 4.048  1.00 20.62 ? 29  HIS   B CD2 1 
ATOM   1194 C  CE1 . HIS   B 1 29  ? 14.806  17.167 6.178  1.00 21.06 ? 29  HIS   B CE1 1 
ATOM   1195 N  NE2 . HIS   B 1 29  ? 15.754  16.815 5.316  1.00 20.91 ? 29  HIS   B NE2 1 
ATOM   1196 N  N   . ASN   B 1 30  ? 10.923  17.616 0.644  1.00 18.66 ? 30  ASN   B N   1 
ATOM   1197 C  CA  . ASN   B 1 30  ? 9.783   18.003 -0.160 1.00 20.54 ? 30  ASN   B CA  1 
ATOM   1198 C  C   . ASN   B 1 30  ? 8.612   17.055 0.130  1.00 19.86 ? 30  ASN   B C   1 
ATOM   1199 O  O   . ASN   B 1 30  ? 7.492   17.513 0.296  1.00 18.68 ? 30  ASN   B O   1 
ATOM   1200 C  CB  . ASN   B 1 30  ? 10.131  18.053 -1.645 1.00 23.80 ? 30  ASN   B CB  1 
ATOM   1201 C  CG  . ASN   B 1 30  ? 10.860  19.346 -1.983 1.00 27.79 ? 30  ASN   B CG  1 
ATOM   1202 O  OD1 . ASN   B 1 30  ? 10.590  20.394 -1.394 1.00 26.37 ? 30  ASN   B OD1 1 
ATOM   1203 N  ND2 . ASN   B 1 30  ? 11.788  19.292 -2.912 1.00 27.21 ? 30  ASN   B ND2 1 
ATOM   1204 N  N   . HIS   B 1 31  ? 8.893   15.768 0.219  1.00 19.32 ? 31  HIS   B N   1 
ATOM   1205 C  CA  . HIS   B 1 31  ? 7.850   14.774 0.483  1.00 19.84 ? 31  HIS   B CA  1 
ATOM   1206 C  C   . HIS   B 1 31  ? 7.241   15.059 1.858  1.00 17.90 ? 31  HIS   B C   1 
ATOM   1207 O  O   . HIS   B 1 31  ? 6.020   15.134 2.021  1.00 18.11 ? 31  HIS   B O   1 
ATOM   1208 C  CB  . HIS   B 1 31  ? 8.376   13.320 0.452  1.00 19.50 ? 31  HIS   B CB  1 
ATOM   1209 C  CG  . HIS   B 1 31  ? 7.239   12.377 0.648  1.00 20.87 ? 31  HIS   B CG  1 
ATOM   1210 N  ND1 . HIS   B 1 31  ? 6.456   11.869 -0.375 1.00 19.25 ? 31  HIS   B ND1 1 
ATOM   1211 C  CD2 . HIS   B 1 31  ? 6.628   12.011 1.786  1.00 21.45 ? 31  HIS   B CD2 1 
ATOM   1212 C  CE1 . HIS   B 1 31  ? 5.470   11.145 0.177  1.00 21.22 ? 31  HIS   B CE1 1 
ATOM   1213 N  NE2 . HIS   B 1 31  ? 5.540   11.236 1.446  1.00 20.48 ? 31  HIS   B NE2 1 
ATOM   1214 N  N   . VAL   B 1 32  ? 8.108   15.254 2.869  1.00 16.45 ? 32  VAL   B N   1 
ATOM   1215 C  CA  . VAL   B 1 32  ? 7.627   15.503 4.219  1.00 18.63 ? 32  VAL   B CA  1 
ATOM   1216 C  C   . VAL   B 1 32  ? 6.764   16.756 4.261  1.00 17.75 ? 32  VAL   B C   1 
ATOM   1217 O  O   . VAL   B 1 32  ? 5.671   16.737 4.826  1.00 16.48 ? 32  VAL   B O   1 
ATOM   1218 C  CB  . VAL   B 1 32  ? 8.822   15.577 5.167  1.00 18.96 ? 32  VAL   B CB  1 
ATOM   1219 C  CG1 . VAL   B 1 32  ? 8.399   16.208 6.477  1.00 20.59 ? 32  VAL   B CG1 1 
ATOM   1220 C  CG2 . VAL   B 1 32  ? 9.432   14.181 5.373  1.00 19.07 ? 32  VAL   B CG2 1 
ATOM   1221 N  N   . SER   B 1 33  ? 7.266   17.864 3.714  1.00 18.52 ? 33  SER   B N   1 
ATOM   1222 C  CA  . SER   B 1 33  ? 6.565   19.144 3.794  1.00 19.64 ? 33  SER   B CA  1 
ATOM   1223 C  C   . SER   B 1 33  ? 5.311   19.211 2.941  1.00 18.53 ? 33  SER   B C   1 
ATOM   1224 O  O   . SER   B 1 33  ? 4.328   19.817 3.352  1.00 19.54 ? 33  SER   B O   1 
ATOM   1225 C  CB  . SER   B 1 33  ? 7.433   20.363 3.494  1.00 22.86 ? 33  SER   B CB  1 
ATOM   1226 O  OG  . SER   B 1 33  ? 8.454   20.426 4.472  1.00 25.38 ? 33  SER   B OG  1 
ATOM   1227 N  N   . LYS   B 1 34  ? 5.378   18.674 1.726  1.00 18.38 ? 34  LYS   B N   1 
ATOM   1228 C  CA  . LYS   B 1 34  ? 4.367   18.954 0.730  1.00 19.16 ? 34  LYS   B CA  1 
ATOM   1229 C  C   . LYS   B 1 34  ? 3.298   17.845 0.662  1.00 19.27 ? 34  LYS   B C   1 
ATOM   1230 O  O   . LYS   B 1 34  ? 2.191   18.120 0.205  1.00 18.26 ? 34  LYS   B O   1 
ATOM   1231 C  CB  . LYS   B 1 34  ? 4.968   19.177 -0.653 1.00 22.24 ? 34  LYS   B CB  1 
ATOM   1232 C  CG  . LYS   B 1 34  ? 5.870   20.414 -0.596 1.00 26.53 ? 34  LYS   B CG  1 
ATOM   1233 C  CD  . LYS   B 1 34  ? 6.564   20.693 -1.913 1.00 35.31 ? 34  LYS   B CD  1 
ATOM   1234 C  CE  . LYS   B 1 34  ? 7.235   22.033 -1.802 1.00 42.08 ? 34  LYS   B CE  1 
ATOM   1235 N  NZ  . LYS   B 1 34  ? 8.095   22.111 -2.974 1.00 52.99 ? 34  LYS   B NZ  1 
ATOM   1236 N  N   . VAL   B 1 35  ? 3.641   16.624 1.076  1.00 16.88 ? 35  VAL   B N   1 
ATOM   1237 C  CA  . VAL   B 1 35  ? 2.756   15.462 0.938  1.00 18.14 ? 35  VAL   B CA  1 
ATOM   1238 C  C   . VAL   B 1 35  ? 2.382   14.912 2.305  1.00 18.73 ? 35  VAL   B C   1 
ATOM   1239 O  O   . VAL   B 1 35  ? 1.206   14.711 2.575  1.00 19.44 ? 35  VAL   B O   1 
ATOM   1240 C  CB  . VAL   B 1 35  ? 3.352   14.372 0.034  1.00 20.73 ? 35  VAL   B CB  1 
ATOM   1241 C  CG1 . VAL   B 1 35  ? 2.425   13.157 -0.057 1.00 22.17 ? 35  VAL   B CG1 1 
ATOM   1242 C  CG2 . VAL   B 1 35  ? 3.651   14.939 -1.354 1.00 22.92 ? 35  VAL   B CG2 1 
ATOM   1243 N  N   . ASN   B 1 36  ? 3.364   14.561 3.146  1.00 17.74 ? 36  ASN   B N   1 
ATOM   1244 C  CA  . ASN   B 1 36  ? 3.037   13.961 4.426  1.00 16.29 ? 36  ASN   B CA  1 
ATOM   1245 C  C   . ASN   B 1 36  ? 2.221   14.925 5.285  1.00 17.22 ? 36  ASN   B C   1 
ATOM   1246 O  O   . ASN   B 1 36  ? 1.280   14.523 5.960  1.00 18.59 ? 36  ASN   B O   1 
ATOM   1247 C  CB  . ASN   B 1 36  ? 4.263   13.409 5.121  1.00 17.70 ? 36  ASN   B CB  1 
ATOM   1248 C  CG  . ASN   B 1 36  ? 3.924   12.626 6.373  1.00 20.45 ? 36  ASN   B CG  1 
ATOM   1249 O  OD1 . ASN   B 1 36  ? 4.018   13.136 7.491  1.00 20.80 ? 36  ASN   B OD1 1 
ATOM   1250 N  ND2 . ASN   B 1 36  ? 3.411   11.423 6.176  1.00 21.23 ? 36  ASN   B ND2 1 
ATOM   1251 N  N   . ALA   B 1 37  ? 2.641   16.189 5.359  1.00 18.88 ? 37  ALA   B N   1 
ATOM   1252 C  CA  . ALA   B 1 37  ? 1.988   17.155 6.234  1.00 19.15 ? 37  ALA   B CA  1 
ATOM   1253 C  C   . ALA   B 1 37  ? 0.509   17.317 5.924  1.00 18.51 ? 37  ALA   B C   1 
ATOM   1254 O  O   . ALA   B 1 37  ? -0.319  17.206 6.846  1.00 18.63 ? 37  ALA   B O   1 
ATOM   1255 C  CB  . ALA   B 1 37  ? 2.719   18.484 6.232  1.00 21.96 ? 37  ALA   B CB  1 
ATOM   1256 N  N   . PRO   B 1 38  ? 0.072   17.605 4.669  1.00 21.74 ? 38  PRO   B N   1 
ATOM   1257 C  CA  . PRO   B 1 38  ? -1.353  17.693 4.388  1.00 22.40 ? 38  PRO   B CA  1 
ATOM   1258 C  C   . PRO   B 1 38  ? -2.107  16.393 4.636  1.00 20.20 ? 38  PRO   B C   1 
ATOM   1259 O  O   . PRO   B 1 38  ? -3.290  16.426 4.949  1.00 20.12 ? 38  PRO   B O   1 
ATOM   1260 C  CB  . PRO   B 1 38  ? -1.418  18.141 2.912  1.00 24.31 ? 38  PRO   B CB  1 
ATOM   1261 C  CG  . PRO   B 1 38  ? -0.112  17.708 2.335  1.00 26.84 ? 38  PRO   B CG  1 
ATOM   1262 C  CD  . PRO   B 1 38  ? 0.853   17.962 3.466  1.00 25.05 ? 38  PRO   B CD  1 
ATOM   1263 N  N   . MET   B 1 39  ? -1.413  15.269 4.508  1.00 18.22 ? 39  MET   B N   1 
ATOM   1264 C  CA  . MET   B 1 39  ? -2.046  13.960 4.781  1.00 18.15 ? 39  MET   B CA  1 
ATOM   1265 C  C   . MET   B 1 39  ? -2.304  13.814 6.288  1.00 18.36 ? 39  MET   B C   1 
ATOM   1266 O  O   . MET   B 1 39  ? -3.335  13.253 6.650  1.00 19.28 ? 39  MET   B O   1 
ATOM   1267 C  CB  . MET   B 1 39  ? -1.119  12.841 4.297  1.00 19.80 ? 39  MET   B CB  1 
ATOM   1268 C  CG  . MET   B 1 39  ? -1.679  11.447 4.409  1.00 24.21 ? 39  MET   B CG  1 
ATOM   1269 S  SD  . MET   B 1 39  ? -0.471  10.245 3.818  1.00 26.51 ? 39  MET   B SD  1 
ATOM   1270 C  CE  . MET   B 1 39  ? 0.031   10.929 2.235  1.00 26.33 ? 39  MET   B CE  1 
ATOM   1271 N  N   . MET   B 1 40  ? -1.403  14.335 7.110  1.00 16.28 ? 40  MET   B N   1 
ATOM   1272 C  CA  . MET   B 1 40  ? -1.503  14.177 8.581  1.00 17.67 ? 40  MET   B CA  1 
ATOM   1273 C  C   . MET   B 1 40  ? -2.438  15.215 9.228  1.00 19.33 ? 40  MET   B C   1 
ATOM   1274 O  O   . MET   B 1 40  ? -3.131  14.846 10.181 1.00 19.20 ? 40  MET   B O   1 
ATOM   1275 C  CB  . MET   B 1 40  ? -0.111  14.322 9.210  1.00 18.53 ? 40  MET   B CB  1 
ATOM   1276 C  CG  . MET   B 1 40  ? 0.804   13.152 8.955  1.00 21.59 ? 40  MET   B CG  1 
ATOM   1277 S  SD  . MET   B 1 40  ? 0.248   11.705 9.875  1.00 21.98 ? 40  MET   B SD  1 
ATOM   1278 C  CE  . MET   B 1 40  ? 0.322   12.319 11.562 1.00 24.16 ? 40  MET   B CE  1 
ATOM   1279 N  N   . ILE   B 1 41  ? -2.478  16.440 8.706  1.00 19.41 ? 41  ILE   B N   1 
ATOM   1280 C  CA  . ILE   B 1 41  ? -3.216  17.517 9.385  1.00 20.31 ? 41  ILE   B CA  1 
ATOM   1281 C  C   . ILE   B 1 41  ? -4.661  17.149 9.738  1.00 20.72 ? 41  ILE   B C   1 
ATOM   1282 O  O   . ILE   B 1 41  ? -5.107  17.400 10.856 1.00 21.89 ? 41  ILE   B O   1 
ATOM   1283 C  CB  . ILE   B 1 41  ? -3.100  18.833 8.605  1.00 23.53 ? 41  ILE   B CB  1 
ATOM   1284 C  CG1 . ILE   B 1 41  ? -1.754  19.434 8.924  1.00 27.12 ? 41  ILE   B CG1 1 
ATOM   1285 C  CG2 . ILE   B 1 41  ? -4.253  19.791 8.965  1.00 27.35 ? 41  ILE   B CG2 1 
ATOM   1286 C  CD1 . ILE   B 1 41  ? -1.375  20.566 8.001  1.00 36.32 ? 41  ILE   B CD1 1 
ATOM   1287 N  N   . PRO   B 1 42  ? -5.451  16.542 8.832  1.00 20.64 ? 42  PRO   B N   1 
ATOM   1288 C  CA  . PRO   B 1 42  ? -6.824  16.155 9.154  1.00 20.43 ? 42  PRO   B CA  1 
ATOM   1289 C  C   . PRO   B 1 42  ? -6.945  15.218 10.330 1.00 19.23 ? 42  PRO   B C   1 
ATOM   1290 O  O   . PRO   B 1 42  ? -7.833  15.373 11.176 1.00 20.81 ? 42  PRO   B O   1 
ATOM   1291 C  CB  . PRO   B 1 42  ? -7.363  15.537 7.857  1.00 22.12 ? 42  PRO   B CB  1 
ATOM   1292 C  CG  . PRO   B 1 42  ? -6.521  16.223 6.797  1.00 25.63 ? 42  PRO   B CG  1 
ATOM   1293 C  CD  . PRO   B 1 42  ? -5.134  16.343 7.411  1.00 22.21 ? 42  PRO   B CD  1 
ATOM   1294 N  N   . PHE   B 1 43  ? -6.000  14.273 10.430 1.00 18.50 ? 43  PHE   B N   1 
ATOM   1295 C  CA  . PHE   B 1 43  ? -5.999  13.345 11.540 1.00 18.09 ? 43  PHE   B CA  1 
ATOM   1296 C  C   . PHE   B 1 43  ? -5.657  14.032 12.854 1.00 20.56 ? 43  PHE   B C   1 
ATOM   1297 O  O   . PHE   B 1 43  ? -6.280  13.784 13.893 1.00 23.28 ? 43  PHE   B O   1 
ATOM   1298 C  CB  . PHE   B 1 43  ? -5.019  12.182 11.351 1.00 18.94 ? 43  PHE   B CB  1 
ATOM   1299 C  CG  . PHE   B 1 43  ? -5.359  11.278 10.186 1.00 20.63 ? 43  PHE   B CG  1 
ATOM   1300 C  CD1 . PHE   B 1 43  ? -6.396  10.349 10.270 1.00 21.60 ? 43  PHE   B CD1 1 
ATOM   1301 C  CD2 . PHE   B 1 43  ? -4.656  11.359 9.004  1.00 18.64 ? 43  PHE   B CD2 1 
ATOM   1302 C  CE1 . PHE   B 1 43  ? -6.695  9.566  9.176  1.00 22.38 ? 43  PHE   B CE1 1 
ATOM   1303 C  CE2 . PHE   B 1 43  ? -4.933  10.526 7.924  1.00 23.02 ? 43  PHE   B CE2 1 
ATOM   1304 C  CZ  . PHE   B 1 43  ? -5.967  9.638  8.022  1.00 21.31 ? 43  PHE   B CZ  1 
ATOM   1305 N  N   . LEU   B 1 44  ? -4.645  14.912 12.797 1.00 19.65 ? 44  LEU   B N   1 
ATOM   1306 C  CA  . LEU   B 1 44  ? -4.217  15.639 13.966 1.00 21.90 ? 44  LEU   B CA  1 
ATOM   1307 C  C   . LEU   B 1 44  ? -5.371  16.507 14.494 1.00 20.02 ? 44  LEU   B C   1 
ATOM   1308 O  O   . LEU   B 1 44  ? -5.591  16.571 15.692 1.00 23.51 ? 44  LEU   B O   1 
ATOM   1309 C  CB  . LEU   B 1 44  ? -2.989  16.469 13.587 1.00 22.26 ? 44  LEU   B CB  1 
ATOM   1310 C  CG  . LEU   B 1 44  ? -1.746  15.667 13.152 1.00 23.87 ? 44  LEU   B CG  1 
ATOM   1311 C  CD1 . LEU   B 1 44  ? -0.639  16.561 12.570 1.00 28.65 ? 44  LEU   B CD1 1 
ATOM   1312 C  CD2 . LEU   B 1 44  ? -1.189  14.809 14.232 1.00 25.44 ? 44  LEU   B CD2 1 
ATOM   1313 N  N   . LYS   B 1 45  ? -6.100  17.162 13.608 1.00 20.40 ? 45  LYS   B N   1 
ATOM   1314 C  CA  . LYS   B 1 45  ? -7.261  17.960 14.004 1.00 22.83 ? 45  LYS   B CA  1 
ATOM   1315 C  C   . LYS   B 1 45  ? -8.351  17.077 14.631 1.00 24.90 ? 45  LYS   B C   1 
ATOM   1316 O  O   . LYS   B 1 45  ? -8.861  17.328 15.733 1.00 24.61 ? 45  LYS   B O   1 
ATOM   1317 C  CB  . LYS   B 1 45  ? -7.799  18.631 12.740 1.00 26.35 ? 45  LYS   B CB  1 
ATOM   1318 C  CG  . LYS   B 1 45  ? -8.999  19.571 12.867 1.00 35.58 ? 45  LYS   B CG  1 
ATOM   1319 C  CD  . LYS   B 1 45  ? -9.170  20.445 11.608 1.00 44.72 ? 45  LYS   B CD  1 
ATOM   1320 C  CE  . LYS   B 1 45  ? -7.805  20.877 11.039 1.00 52.95 ? 45  LYS   B CE  1 
ATOM   1321 N  NZ  . LYS   B 1 45  ? -7.769  21.789 9.888  1.00 53.14 ? 45  LYS   B NZ  1 
ATOM   1322 N  N   . LYS   B 1 46  ? -8.653  15.980 13.966 1.00 22.25 ? 46  LYS   B N   1 
ATOM   1323 C  CA  . LYS   B 1 46  ? -9.727  15.095 14.380 1.00 24.33 ? 46  LYS   B CA  1 
ATOM   1324 C  C   . LYS   B 1 46  ? -9.464  14.578 15.784 1.00 24.67 ? 46  LYS   B C   1 
ATOM   1325 O  O   . LYS   B 1 46  ? -10.404 14.453 16.560 1.00 26.15 ? 46  LYS   B O   1 
ATOM   1326 C  CB  . LYS   B 1 46  ? -9.945  13.996 13.347 1.00 24.24 ? 46  LYS   B CB  1 
ATOM   1327 C  CG  . LYS   B 1 46  ? -10.901 12.883 13.772 1.00 26.95 ? 46  LYS   B CG  1 
ATOM   1328 C  CD  . LYS   B 1 46  ? -11.316 11.970 12.637 1.00 28.96 ? 46  LYS   B CD  1 
ATOM   1329 C  CE  . LYS   B 1 46  ? -12.232 10.871 13.153 1.00 34.18 ? 46  LYS   B CE  1 
ATOM   1330 N  NZ  . LYS   B 1 46  ? -12.566 10.071 11.968 1.00 42.94 ? 46  LYS   B NZ  1 
ATOM   1331 N  N   . TYR   B 1 47  ? -8.221  14.168 16.070 1.00 22.58 ? 47  TYR   B N   1 
ATOM   1332 C  CA  . TYR   B 1 47  ? -7.887  13.492 17.300 1.00 23.70 ? 47  TYR   B CA  1 
ATOM   1333 C  C   . TYR   B 1 47  ? -7.398  14.456 18.384 1.00 23.22 ? 47  TYR   B C   1 
ATOM   1334 O  O   . TYR   B 1 47  ? -7.003  13.985 19.465 1.00 25.89 ? 47  TYR   B O   1 
ATOM   1335 C  CB  . TYR   B 1 47  ? -6.935  12.327 17.018 1.00 23.19 ? 47  TYR   B CB  1 
ATOM   1336 C  CG  . TYR   B 1 47  ? -7.712  11.228 16.325 1.00 21.43 ? 47  TYR   B CG  1 
ATOM   1337 C  CD1 . TYR   B 1 47  ? -8.611  10.454 17.034 1.00 23.67 ? 47  TYR   B CD1 1 
ATOM   1338 C  CD2 . TYR   B 1 47  ? -7.621  11.010 14.949 1.00 21.80 ? 47  TYR   B CD2 1 
ATOM   1339 C  CE1 . TYR   B 1 47  ? -9.388  9.493  16.417 1.00 23.92 ? 47  TYR   B CE1 1 
ATOM   1340 C  CE2 . TYR   B 1 47  ? -8.407  10.057 14.313 1.00 23.06 ? 47  TYR   B CE2 1 
ATOM   1341 C  CZ  . TYR   B 1 47  ? -9.239  9.259  15.069 1.00 24.96 ? 47  TYR   B CZ  1 
ATOM   1342 O  OH  . TYR   B 1 47  ? -10.011 8.317  14.518 1.00 22.57 ? 47  TYR   B OH  1 
ATOM   1343 N  N   . GLY   B 1 48  ? -7.492  15.766 18.141 1.00 25.63 ? 48  GLY   B N   1 
ATOM   1344 C  CA  . GLY   B 1 48  ? -7.308  16.741 19.224 1.00 28.47 ? 48  GLY   B CA  1 
ATOM   1345 C  C   . GLY   B 1 48  ? -5.851  17.039 19.572 1.00 27.14 ? 48  GLY   B C   1 
ATOM   1346 O  O   . GLY   B 1 48  ? -5.533  17.528 20.645 1.00 24.96 ? 48  GLY   B O   1 
ATOM   1347 N  N   . ILE   B 1 49  ? -4.926  16.817 18.636 1.00 24.24 ? 49  ILE   B N   1 
ATOM   1348 C  CA  . ILE   B 1 49  ? -3.557  17.218 18.831 1.00 23.34 ? 49  ILE   B CA  1 
ATOM   1349 C  C   . ILE   B 1 49  ? -3.552  18.758 18.913 1.00 26.00 ? 49  ILE   B C   1 
ATOM   1350 O  O   . ILE   B 1 49  ? -4.234  19.467 18.153 1.00 25.60 ? 49  ILE   B O   1 
ATOM   1351 C  CB  . ILE   B 1 49  ? -2.654  16.664 17.697 1.00 25.07 ? 49  ILE   B CB  1 
ATOM   1352 C  CG1 . ILE   B 1 49  ? -2.297  15.198 17.934 1.00 24.29 ? 49  ILE   B CG1 1 
ATOM   1353 C  CG2 . ILE   B 1 49  ? -1.362  17.484 17.572 1.00 25.51 ? 49  ILE   B CG2 1 
ATOM   1354 C  CD1 . ILE   B 1 49  ? -3.445  14.191 17.990 1.00 25.63 ? 49  ILE   B CD1 1 
ATOM   1355 N  N   . VAL   B 1 50  ? -2.783  19.270 19.864 1.00 26.00 ? 50  VAL   B N   1 
ATOM   1356 C  CA  . VAL   B 1 50  ? -2.741  20.686 20.200 1.00 27.30 ? 50  VAL   B CA  1 
ATOM   1357 C  C   . VAL   B 1 50  ? -1.716  21.393 19.315 1.00 25.92 ? 50  VAL   B C   1 
ATOM   1358 O  O   . VAL   B 1 50  ? -1.984  22.493 18.849 1.00 27.27 ? 50  VAL   B O   1 
ATOM   1359 C  CB  . VAL   B 1 50  ? -2.380  20.855 21.696 1.00 31.82 ? 50  VAL   B CB  1 
ATOM   1360 C  CG1 . VAL   B 1 50  ? -2.239  22.320 22.074 1.00 39.54 ? 50  VAL   B CG1 1 
ATOM   1361 C  CG2 . VAL   B 1 50  ? -3.415  20.162 22.572 1.00 36.31 ? 50  VAL   B CG2 1 
ATOM   1362 N  N   . ARG   B 1 51  ? -0.573  20.748 19.065 1.00 23.69 ? 51  ARG   B N   1 
ATOM   1363 C  CA  . ARG   B 1 51  ? 0.481   21.365 18.276 1.00 23.25 ? 51  ARG   B CA  1 
ATOM   1364 C  C   . ARG   B 1 51  ? 1.263   20.259 17.582 1.00 22.11 ? 51  ARG   B C   1 
ATOM   1365 O  O   . ARG   B 1 51  ? 1.499   19.196 18.164 1.00 22.87 ? 51  ARG   B O   1 
ATOM   1366 C  CB  . ARG   B 1 51  ? 1.411   22.173 19.202 1.00 26.97 ? 51  ARG   B CB  1 
ATOM   1367 C  CG  . ARG   B 1 51  ? 2.447   22.976 18.434 1.00 31.56 ? 51  ARG   B CG  1 
ATOM   1368 C  CD  . ARG   B 1 51  ? 3.300   23.815 19.437 1.00 36.03 ? 51  ARG   B CD  1 
ATOM   1369 N  NE  . ARG   B 1 51  ? 3.831   25.013 18.774 1.00 45.18 ? 51  ARG   B NE  1 
ATOM   1370 C  CZ  . ARG   B 1 51  ? 3.192   26.185 18.508 1.00 47.18 ? 51  ARG   B CZ  1 
ATOM   1371 N  NH1 . ARG   B 1 51  ? 1.992   26.473 19.017 1.00 43.24 ? 51  ARG   B NH1 1 
ATOM   1372 N  NH2 . ARG   B 1 51  ? 3.810   27.119 17.792 1.00 44.95 ? 51  ARG   B NH2 1 
ATOM   1373 N  N   . TYR   B 1 52  ? 1.644   20.533 16.345 1.00 22.17 ? 52  TYR   B N   1 
ATOM   1374 C  CA  . TYR   B 1 52  ? 2.460   19.611 15.571 1.00 19.39 ? 52  TYR   B CA  1 
ATOM   1375 C  C   . TYR   B 1 52  ? 3.606   20.398 14.940 1.00 22.02 ? 52  TYR   B C   1 
ATOM   1376 O  O   . TYR   B 1 52  ? 3.350   21.395 14.277 1.00 23.50 ? 52  TYR   B O   1 
ATOM   1377 C  CB  . TYR   B 1 52  ? 1.597   18.978 14.482 1.00 21.85 ? 52  TYR   B CB  1 
ATOM   1378 C  CG  . TYR   B 1 52  ? 2.270   17.991 13.557 1.00 19.16 ? 52  TYR   B CG  1 
ATOM   1379 C  CD1 . TYR   B 1 52  ? 2.714   16.787 14.057 1.00 22.05 ? 52  TYR   B CD1 1 
ATOM   1380 C  CD2 . TYR   B 1 52  ? 2.268   18.171 12.177 1.00 20.79 ? 52  TYR   B CD2 1 
ATOM   1381 C  CE1 . TYR   B 1 52  ? 3.207   15.801 13.237 1.00 23.69 ? 52  TYR   B CE1 1 
ATOM   1382 C  CE2 . TYR   B 1 52  ? 2.757   17.183 11.343 1.00 19.51 ? 52  TYR   B CE2 1 
ATOM   1383 C  CZ  . TYR   B 1 52  ? 3.235   16.006 11.881 1.00 23.19 ? 52  TYR   B CZ  1 
ATOM   1384 O  OH  . TYR   B 1 52  ? 3.697   14.951 11.148 1.00 26.81 ? 52  TYR   B OH  1 
ATOM   1385 N  N   . THR   B 1 53  ? 4.814   19.930 15.195 1.00 20.85 ? 53  THR   B N   1 
ATOM   1386 C  CA  . THR   B 1 53  ? 6.024   20.600 14.727 1.00 21.61 ? 53  THR   B CA  1 
ATOM   1387 C  C   . THR   B 1 53  ? 6.854   19.619 13.914 1.00 21.35 ? 53  THR   B C   1 
ATOM   1388 O  O   . THR   B 1 53  ? 7.081   18.482 14.326 1.00 22.17 ? 53  THR   B O   1 
ATOM   1389 C  CB  . THR   B 1 53  ? 6.812   21.132 15.924 1.00 22.24 ? 53  THR   B CB  1 
ATOM   1390 O  OG1 . THR   B 1 53  ? 5.925   22.063 16.570 1.00 23.37 ? 53  THR   B OG1 1 
ATOM   1391 C  CG2 . THR   B 1 53  ? 8.022   21.898 15.434 1.00 30.53 ? 53  THR   B CG2 1 
ATOM   1392 N  N   . VAL   B 1 54  ? 7.381   20.108 12.791 1.00 20.28 ? 54  VAL   B N   1 
ATOM   1393 C  CA  . VAL   B 1 54  ? 8.254   19.275 11.919 1.00 18.47 ? 54  VAL   B CA  1 
ATOM   1394 C  C   . VAL   B 1 54  ? 9.620   19.974 11.836 1.00 19.27 ? 54  VAL   B C   1 
ATOM   1395 O  O   . VAL   B 1 54  ? 9.661   21.102 11.360 1.00 20.32 ? 54  VAL   B O   1 
ATOM   1396 C  CB  . VAL   B 1 54  ? 7.669   19.025 10.518 1.00 23.63 ? 54  VAL   B CB  1 
ATOM   1397 C  CG1 . VAL   B 1 54  ? 8.538   18.076 9.709  1.00 23.42 ? 54  VAL   B CG1 1 
ATOM   1398 C  CG2 . VAL   B 1 54  ? 6.235   18.520 10.598 1.00 25.17 ? 54  VAL   B CG2 1 
ATOM   1399 N  N   . LYS   B 1 55  ? 10.660  19.305 12.315 1.00 19.24 ? 55  LYS   B N   1 
ATOM   1400 C  CA  . LYS   B 1 55  ? 12.012  19.908 12.345 1.00 21.06 ? 55  LYS   B CA  1 
ATOM   1401 C  C   . LYS   B 1 55  ? 12.863  19.268 11.245 1.00 20.48 ? 55  LYS   B C   1 
ATOM   1402 O  O   . LYS   B 1 55  ? 12.958  18.040 11.225 1.00 23.65 ? 55  LYS   B O   1 
ATOM   1403 C  CB  . LYS   B 1 55  ? 12.632  19.755 13.736 1.00 23.70 ? 55  LYS   B CB  1 
ATOM   1404 C  CG  . LYS   B 1 55  ? 11.745  20.282 14.850 1.00 28.28 ? 55  LYS   B CG  1 
ATOM   1405 C  CD  . LYS   B 1 55  ? 12.407  20.351 16.218 1.00 34.62 ? 55  LYS   B CD  1 
ATOM   1406 C  CE  . LYS   B 1 55  ? 13.220  19.141 16.520 1.00 36.68 ? 55  LYS   B CE  1 
ATOM   1407 N  NZ  . LYS   B 1 55  ? 13.808  19.217 17.858 1.00 45.20 ? 55  LYS   B NZ  1 
ATOM   1408 N  N   . HIS   B 1 56  ? 13.472  20.102 10.408 1.00 20.18 ? 56  HIS   B N   1 
ATOM   1409 C  CA  . HIS   B 1 56  ? 14.277  19.615 9.268  1.00 18.49 ? 56  HIS   B CA  1 
ATOM   1410 C  C   . HIS   B 1 56  ? 15.776  19.871 9.460  1.00 19.89 ? 56  HIS   B C   1 
ATOM   1411 O  O   . HIS   B 1 56  ? 16.141  20.973 9.845  1.00 19.38 ? 56  HIS   B O   1 
ATOM   1412 C  CB  . HIS   B 1 56  ? 13.794  20.285 7.981  1.00 20.45 ? 56  HIS   B CB  1 
ATOM   1413 C  CG  . HIS   B 1 56  ? 12.333  20.222 7.709  1.00 21.81 ? 56  HIS   B CG  1 
ATOM   1414 N  ND1 . HIS   B 1 56  ? 11.802  19.334 6.802  1.00 24.00 ? 56  HIS   B ND1 1 
ATOM   1415 C  CD2 . HIS   B 1 56  ? 11.306  20.941 8.164  1.00 23.33 ? 56  HIS   B CD2 1 
ATOM   1416 C  CE1 . HIS   B 1 56  ? 10.496  19.507 6.735  1.00 23.37 ? 56  HIS   B CE1 1 
ATOM   1417 N  NE2 . HIS   B 1 56  ? 10.173  20.479 7.550  1.00 23.18 ? 56  HIS   B NE2 1 
ATOM   1418 N  N   . ASN   B 1 57  ? 16.593  18.863 9.198  1.00 20.60 ? 57  ASN   B N   1 
ATOM   1419 C  CA  . ASN   B 1 57  ? 18.047  18.944 9.255  1.00 20.21 ? 57  ASN   B CA  1 
ATOM   1420 C  C   . ASN   B 1 57  ? 18.596  18.739 7.846  1.00 21.13 ? 57  ASN   B C   1 
ATOM   1421 O  O   . ASN   B 1 57  ? 18.926  17.619 7.456  1.00 23.57 ? 57  ASN   B O   1 
ATOM   1422 C  CB  . ASN   B 1 57  ? 18.577  17.972 10.311 1.00 23.33 ? 57  ASN   B CB  1 
ATOM   1423 C  CG  . ASN   B 1 57  ? 20.068  17.757 10.254 1.00 30.03 ? 57  ASN   B CG  1 
ATOM   1424 O  OD1 . ASN   B 1 57  ? 20.837  18.677 9.933  1.00 23.37 ? 57  ASN   B OD1 1 
ATOM   1425 N  ND2 . ASN   B 1 57  ? 20.498  16.520 10.445 1.00 29.44 ? 57  ASN   B ND2 1 
ATOM   1426 N  N   . ASP   B 1 58  ? 18.723  19.856 7.125  1.00 21.99 ? 58  ASP   B N   1 
ATOM   1427 C  CA  . ASP   B 1 58  ? 19.116  19.796 5.722  1.00 24.05 ? 58  ASP   B CA  1 
ATOM   1428 C  C   . ASP   B 1 58  ? 20.116  20.902 5.357  1.00 27.47 ? 58  ASP   B C   1 
ATOM   1429 O  O   . ASP   B 1 58  ? 20.674  21.590 6.224  1.00 23.56 ? 58  ASP   B O   1 
ATOM   1430 C  CB  . ASP   B 1 58  ? 17.869  19.859 4.864  1.00 20.07 ? 58  ASP   B CB  1 
ATOM   1431 C  CG  . ASP   B 1 58  ? 17.113  21.157 4.855  1.00 22.23 ? 58  ASP   B CG  1 
ATOM   1432 O  OD1 . ASP   B 1 58  ? 17.627  22.155 5.465  1.00 22.96 ? 58  ASP   B OD1 1 
ATOM   1433 O  OD2 . ASP   B 1 58  ? 16.034  21.240 4.197  1.00 23.29 ? 58  ASP   B OD2 1 
ATOM   1434 N  N   . ALA   B 1 59  ? 20.295  21.119 4.037  1.00 26.06 ? 59  ALA   B N   1 
ATOM   1435 C  CA  . ALA   B 1 59  ? 21.316  22.062 3.583  1.00 27.91 ? 59  ALA   B CA  1 
ATOM   1436 C  C   . ALA   B 1 59  ? 21.036  23.474 4.058  1.00 25.65 ? 59  ALA   B C   1 
ATOM   1437 O  O   . ALA   B 1 59  ? 22.006  24.238 4.259  1.00 28.82 ? 59  ALA   B O   1 
ATOM   1438 C  CB  . ALA   B 1 59  ? 21.434  22.001 2.047  1.00 27.74 ? 59  ALA   B CB  1 
ATOM   1439 N  N   . TYR   B 1 60  ? 19.770  23.859 4.235  1.00 21.33 ? 60  TYR   B N   1 
ATOM   1440 C  CA  . TYR   B 1 60  ? 19.396  25.165 4.707  1.00 22.79 ? 60  TYR   B CA  1 
ATOM   1441 C  C   . TYR   B 1 60  ? 19.813  25.395 6.164  1.00 23.90 ? 60  TYR   B C   1 
ATOM   1442 O  O   . TYR   B 1 60  ? 20.276  26.475 6.530  1.00 22.24 ? 60  TYR   B O   1 
ATOM   1443 C  CB  . TYR   B 1 60  ? 17.919  25.438 4.520  1.00 23.59 ? 60  TYR   B CB  1 
ATOM   1444 C  CG  . TYR   B 1 60  ? 17.450  26.751 5.077  1.00 24.21 ? 60  TYR   B CG  1 
ATOM   1445 C  CD1 . TYR   B 1 60  ? 17.664  27.915 4.345  1.00 31.30 ? 60  TYR   B CD1 1 
ATOM   1446 C  CD2 . TYR   B 1 60  ? 16.935  26.876 6.362  1.00 25.45 ? 60  TYR   B CD2 1 
ATOM   1447 C  CE1 . TYR   B 1 60  ? 17.254  29.139 4.821  1.00 33.71 ? 60  TYR   B CE1 1 
ATOM   1448 C  CE2 . TYR   B 1 60  ? 16.514  28.094 6.845  1.00 28.45 ? 60  TYR   B CE2 1 
ATOM   1449 C  CZ  . TYR   B 1 60  ? 16.756  29.243 6.102  1.00 32.65 ? 60  TYR   B CZ  1 
ATOM   1450 O  OH  . TYR   B 1 60  ? 16.365  30.464 6.561  1.00 33.95 ? 60  TYR   B OH  1 
ATOM   1451 N  N   . SER   B 1 61  ? 19.494  24.443 7.028  1.00 22.03 ? 61  SER   B N   1 
ATOM   1452 C  CA  . SER   B 1 61  ? 19.734  24.560 8.464  1.00 22.51 ? 61  SER   B CA  1 
ATOM   1453 C  C   . SER   B 1 61  ? 21.174  24.213 8.861  1.00 21.09 ? 61  SER   B C   1 
ATOM   1454 O  O   . SER   B 1 61  ? 21.649  24.669 9.911  1.00 21.38 ? 61  SER   B O   1 
ATOM   1455 C  CB  . SER   B 1 61  ? 18.709  23.614 9.219  1.00 20.80 ? 61  SER   B CB  1 
ATOM   1456 O  OG  . SER   B 1 61  ? 18.976  22.255 8.891  1.00 21.10 ? 61  SER   B OG  1 
ATOM   1457 N  N   . LYS   B 1 62  ? 21.879  23.357 8.121  1.00 20.03 ? 62  LYS   B N   1 
ATOM   1458 C  CA  . LYS   B 1 62  ? 23.152  22.806 8.542  1.00 24.23 ? 62  LYS   B CA  1 
ATOM   1459 C  C   . LYS   B 1 62  ? 24.205  23.889 8.884  1.00 22.32 ? 62  LYS   B C   1 
ATOM   1460 O  O   . LYS   B 1 62  ? 24.914  23.742 9.883  1.00 21.05 ? 62  LYS   B O   1 
ATOM   1461 C  CB  . LYS   B 1 62  ? 23.714  21.787 7.555  1.00 28.97 ? 62  LYS   B CB  1 
ATOM   1462 C  CG  . LYS   B 1 62  ? 23.140  20.373 7.816  1.00 37.12 ? 62  LYS   B CG  1 
ATOM   1463 C  CD  . LYS   B 1 62  ? 23.447  19.402 6.682  1.00 38.63 ? 62  LYS   B CD  1 
ATOM   1464 C  CE  . LYS   B 1 62  ? 22.531  18.245 6.633  1.00 44.20 ? 62  LYS   B CE  1 
ATOM   1465 N  NZ  . LYS   B 1 62  ? 22.552  17.592 7.935  1.00 40.86 ? 62  LYS   B NZ  1 
ATOM   1466 N  N   . PRO   B 1 63  ? 24.372  24.995 8.118  1.00 24.48 ? 63  PRO   B N   1 
ATOM   1467 C  CA  . PRO   B 1 63  ? 25.321  26.055 8.524  1.00 24.47 ? 63  PRO   B CA  1 
ATOM   1468 C  C   . PRO   B 1 63  ? 24.931  26.727 9.840  1.00 24.32 ? 63  PRO   B C   1 
ATOM   1469 O  O   . PRO   B 1 63  ? 25.797  27.144 10.626 1.00 23.15 ? 63  PRO   B O   1 
ATOM   1470 C  CB  . PRO   B 1 63  ? 25.326  27.068 7.339  1.00 25.40 ? 63  PRO   B CB  1 
ATOM   1471 C  CG  . PRO   B 1 63  ? 24.801  26.269 6.176  1.00 27.81 ? 63  PRO   B CG  1 
ATOM   1472 C  CD  . PRO   B 1 63  ? 23.810  25.246 6.769  1.00 24.66 ? 63  PRO   B CD  1 
ATOM   1473 N  N   . LYS   B 1 64  ? 23.618  26.748 10.137 1.00 21.90 ? 64  LYS   B N   1 
ATOM   1474 C  CA  . LYS   B 1 64  ? 23.085  27.343 11.353 1.00 23.79 ? 64  LYS   B CA  1 
ATOM   1475 C  C   . LYS   B 1 64  ? 23.401  26.427 12.527 1.00 25.31 ? 64  LYS   B C   1 
ATOM   1476 O  O   . LYS   B 1 64  ? 23.857  26.881 13.588 1.00 22.75 ? 64  LYS   B O   1 
ATOM   1477 C  CB  . LYS   B 1 64  ? 21.603  27.679 11.158 1.00 26.64 ? 64  LYS   B CB  1 
ATOM   1478 C  CG  . LYS   B 1 64  ? 21.461  28.717 10.032 1.00 32.48 ? 64  LYS   B CG  1 
ATOM   1479 C  CD  . LYS   B 1 64  ? 20.051  28.943 9.542  1.00 40.86 ? 64  LYS   B CD  1 
ATOM   1480 C  CE  . LYS   B 1 64  ? 19.937  30.008 8.489  1.00 37.90 ? 64  LYS   B CE  1 
ATOM   1481 N  NZ  . LYS   B 1 64  ? 20.450  29.516 7.221  1.00 44.39 ? 64  LYS   B NZ  1 
ATOM   1482 N  N   . GLN   B 1 65  ? 23.140  25.128 12.343 1.00 21.83 ? 65  GLN   B N   1 
ATOM   1483 C  CA  . GLN   B 1 65  ? 23.547  24.137 13.322 1.00 22.16 ? 65  GLN   B CA  1 
ATOM   1484 C  C   . GLN   B 1 65  ? 25.056  24.154 13.586 1.00 20.99 ? 65  GLN   B C   1 
ATOM   1485 O  O   . GLN   B 1 65  ? 25.491  24.045 14.738 1.00 22.42 ? 65  GLN   B O   1 
ATOM   1486 C  CB  . GLN   B 1 65  ? 23.131  22.760 12.793 1.00 22.48 ? 65  GLN   B CB  1 
ATOM   1487 C  CG  . GLN   B 1 65  ? 23.587  21.623 13.689 1.00 22.34 ? 65  GLN   B CG  1 
ATOM   1488 C  CD  . GLN   B 1 65  ? 22.915  20.318 13.275 1.00 27.59 ? 65  GLN   B CD  1 
ATOM   1489 O  OE1 . GLN   B 1 65  ? 21.859  19.947 13.799 1.00 23.13 ? 65  GLN   B OE1 1 
ATOM   1490 N  NE2 . GLN   B 1 65  ? 23.457  19.672 12.249 1.00 28.71 ? 65  GLN   B NE2 1 
ATOM   1491 N  N   . ALA   B 1 66  ? 25.873  24.245 12.522 1.00 20.78 ? 66  ALA   B N   1 
ATOM   1492 C  CA  . ALA   B 1 66  ? 27.335  24.243 12.664 1.00 23.22 ? 66  ALA   B CA  1 
ATOM   1493 C  C   . ALA   B 1 66  ? 27.776  25.453 13.498 1.00 20.96 ? 66  ALA   B C   1 
ATOM   1494 O  O   . ALA   B 1 66  ? 28.670  25.309 14.313 1.00 23.72 ? 66  ALA   B O   1 
ATOM   1495 C  CB  . ALA   B 1 66  ? 28.028  24.251 11.312 1.00 22.14 ? 66  ALA   B CB  1 
ATOM   1496 N  N   . ALA   B 1 67  ? 27.104  26.585 13.339 1.00 21.14 ? 67  ALA   B N   1 
ATOM   1497 C  CA  . ALA   B 1 67  ? 27.413  27.773 14.119 1.00 23.34 ? 67  ALA   B CA  1 
ATOM   1498 C  C   . ALA   B 1 67  ? 26.995  27.584 15.572 1.00 25.10 ? 67  ALA   B C   1 
ATOM   1499 O  O   . ALA   B 1 67  ? 27.777  27.821 16.463 1.00 23.33 ? 67  ALA   B O   1 
ATOM   1500 C  CB  . ALA   B 1 67  ? 26.744  28.986 13.558 1.00 25.02 ? 67  ALA   B CB  1 
ATOM   1501 N  N   . LEU   B 1 68  ? 25.781  27.096 15.828 1.00 20.27 ? 68  LEU   B N   1 
ATOM   1502 C  CA  . LEU   B 1 68  ? 25.318  26.873 17.203 1.00 22.85 ? 68  LEU   B CA  1 
ATOM   1503 C  C   . LEU   B 1 68  ? 26.188  25.849 17.916 1.00 22.24 ? 68  LEU   B C   1 
ATOM   1504 O  O   . LEU   B 1 68  ? 26.384  25.927 19.124 1.00 24.36 ? 68  LEU   B O   1 
ATOM   1505 C  CB  . LEU   B 1 68  ? 23.857  26.408 17.166 1.00 24.47 ? 68  LEU   B CB  1 
ATOM   1506 C  CG  . LEU   B 1 68  ? 22.790  27.439 16.780 1.00 26.30 ? 68  LEU   B CG  1 
ATOM   1507 C  CD1 . LEU   B 1 68  ? 21.489  26.765 16.316 1.00 28.21 ? 68  LEU   B CD1 1 
ATOM   1508 C  CD2 . LEU   B 1 68  ? 22.455  28.378 17.900 1.00 29.81 ? 68  LEU   B CD2 1 
ATOM   1509 N  N   . MET   B 1 69  ? 26.669  24.823 17.200 1.00 21.57 ? 69  MET   B N   1 
ATOM   1510 C  CA  . MET   B 1 69  ? 27.377  23.724 17.801 1.00 22.04 ? 69  MET   B CA  1 
ATOM   1511 C  C   . MET   B 1 69  ? 28.893  23.900 17.652 1.00 22.89 ? 69  MET   B C   1 
ATOM   1512 O  O   . MET   B 1 69  ? 29.646  22.958 17.821 1.00 20.96 ? 69  MET   B O   1 
ATOM   1513 C  CB  . MET   B 1 69  ? 26.919  22.388 17.192 1.00 24.30 ? 69  MET   B CB  1 
ATOM   1514 C  CG  . MET   B 1 69  ? 25.448  22.073 17.410 1.00 25.74 ? 69  MET   B CG  1 
ATOM   1515 S  SD  . MET   B 1 69  ? 25.038  21.893 19.153 1.00 27.00 ? 69  MET   B SD  1 
ATOM   1516 C  CE  . MET   B 1 69  ? 25.825  20.318 19.481 1.00 25.47 ? 69  MET   B CE  1 
ATOM   1517 N  N   . ALA   B 1 70  ? 29.372  25.123 17.349 1.00 24.22 ? 70  ALA   B N   1 
ATOM   1518 C  CA  . ALA   B 1 70  ? 30.798  25.374 17.158 1.00 26.01 ? 70  ALA   B CA  1 
ATOM   1519 C  C   . ALA   B 1 70  ? 31.551  24.972 18.428 1.00 20.63 ? 70  ALA   B C   1 
ATOM   1520 O  O   . ALA   B 1 70  ? 31.105  25.310 19.511 1.00 25.15 ? 70  ALA   B O   1 
ATOM   1521 C  CB  . ALA   B 1 70  ? 30.983  26.852 16.944 1.00 27.89 ? 70  ALA   B CB  1 
ATOM   1522 N  N   . GLY   B 1 71  ? 32.609  24.205 18.272 1.00 22.61 ? 71  GLY   B N   1 
ATOM   1523 C  CA  . GLY   B 1 71  ? 33.387  23.796 19.426 1.00 25.51 ? 71  GLY   B CA  1 
ATOM   1524 C  C   . GLY   B 1 71  ? 32.866  22.525 20.082 1.00 29.47 ? 71  GLY   B C   1 
ATOM   1525 O  O   . GLY   B 1 71  ? 33.486  22.016 21.016 1.00 26.01 ? 71  GLY   B O   1 
ATOM   1526 N  N   . GLN   B 1 72  ? 31.714  22.013 19.610 1.00 29.97 ? 72  GLN   B N   1 
ATOM   1527 C  CA  . GLN   B 1 72  ? 31.237  20.730 20.114 1.00 30.03 ? 72  GLN   B CA  1 
ATOM   1528 C  C   . GLN   B 1 72  ? 31.802  19.585 19.286 1.00 30.01 ? 72  GLN   B C   1 
ATOM   1529 O  O   . GLN   B 1 72  ? 31.913  19.655 18.084 1.00 30.09 ? 72  GLN   B O   1 
ATOM   1530 C  CB  . GLN   B 1 72  ? 29.714  20.721 20.068 1.00 28.83 ? 72  GLN   B CB  1 
ATOM   1531 C  CG  . GLN   B 1 72  ? 29.022  21.839 20.850 1.00 25.95 ? 72  GLN   B CG  1 
ATOM   1532 C  CD  . GLN   B 1 72  ? 29.359  21.863 22.329 1.00 29.62 ? 72  GLN   B CD  1 
ATOM   1533 O  OE1 . GLN   B 1 72  ? 29.702  20.831 22.887 1.00 32.31 ? 72  GLN   B OE1 1 
ATOM   1534 N  NE2 . GLN   B 1 72  ? 29.223  23.024 22.959 1.00 32.31 ? 72  GLN   B NE2 1 
ATOM   1535 N  N   . PRO   B 1 73  ? 32.078  18.433 19.925 1.00 38.74 ? 73  PRO   B N   1 
ATOM   1536 C  CA  . PRO   B 1 73  ? 32.403  17.197 19.214 1.00 37.11 ? 73  PRO   B CA  1 
ATOM   1537 C  C   . PRO   B 1 73  ? 31.290  16.807 18.241 1.00 34.69 ? 73  PRO   B C   1 
ATOM   1538 O  O   . PRO   B 1 73  ? 30.106  16.975 18.556 1.00 31.36 ? 73  PRO   B O   1 
ATOM   1539 C  CB  . PRO   B 1 73  ? 32.537  16.132 20.349 1.00 38.39 ? 73  PRO   B CB  1 
ATOM   1540 C  CG  . PRO   B 1 73  ? 32.580  16.891 21.667 1.00 41.68 ? 73  PRO   B CG  1 
ATOM   1541 C  CD  . PRO   B 1 73  ? 31.968  18.261 21.386 1.00 39.85 ? 73  PRO   B CD  1 
ATOM   1542 N  N   . GLU   B 1 74  ? 31.659  16.298 17.069 1.00 33.09 ? 74  GLU   B N   1 
ATOM   1543 C  CA  . GLU   B 1 74  ? 30.700  15.994 16.017 1.00 35.99 ? 74  GLU   B CA  1 
ATOM   1544 C  C   . GLU   B 1 74  ? 29.708  14.940 16.518 1.00 29.82 ? 74  GLU   B C   1 
ATOM   1545 O  O   . GLU   B 1 74  ? 28.541  14.952 16.127 1.00 34.49 ? 74  GLU   B O   1 
ATOM   1546 C  CB  . GLU   B 1 74  ? 31.293  15.487 14.695 1.00 43.86 ? 74  GLU   B CB  1 
ATOM   1547 N  N   . GLU   B 1 75  ? 30.153  14.051 17.406 1.00 30.39 ? 75  GLU   B N   1 
ATOM   1548 C  CA  . GLU   B 1 75  ? 29.259  13.006 17.876 1.00 37.93 ? 75  GLU   B CA  1 
ATOM   1549 C  C   . GLU   B 1 75  ? 28.163  13.588 18.774 1.00 40.24 ? 75  GLU   B C   1 
ATOM   1550 O  O   . GLU   B 1 75  ? 27.159  12.906 19.018 1.00 34.00 ? 75  GLU   B O   1 
ATOM   1551 C  CB  . GLU   B 1 75  ? 29.929  11.842 18.599 1.00 41.51 ? 75  GLU   B CB  1 
ATOM   1552 C  CG  . GLU   B 1 75  ? 30.509  12.192 19.959 1.00 50.05 ? 75  GLU   B CG  1 
ATOM   1553 C  CD  . GLU   B 1 75  ? 31.987  12.501 19.961 1.00 60.87 ? 75  GLU   B CD  1 
ATOM   1554 O  OE1 . GLU   B 1 75  ? 32.515  12.351 21.085 1.00 65.33 ? 75  GLU   B OE1 1 
ATOM   1555 O  OE2 . GLU   B 1 75  ? 32.599  12.872 18.913 1.00 66.68 ? 75  GLU   B OE2 1 
ATOM   1556 N  N   . ASN   B 1 76  ? 28.311  14.857 19.213 1.00 31.52 ? 76  ASN   B N   1 
ATOM   1557 C  CA  . ASN   B 1 76  ? 27.300  15.474 20.075 1.00 30.32 ? 76  ASN   B CA  1 
ATOM   1558 C  C   . ASN   B 1 76  ? 26.225  16.213 19.302 1.00 26.61 ? 76  ASN   B C   1 
ATOM   1559 O  O   . ASN   B 1 76  ? 25.313  16.826 19.893 1.00 24.41 ? 76  ASN   B O   1 
ATOM   1560 C  CB  . ASN   B 1 76  ? 27.962  16.365 21.097 1.00 34.47 ? 76  ASN   B CB  1 
ATOM   1561 C  CG  . ASN   B 1 76  ? 28.745  15.528 22.076 1.00 42.60 ? 76  ASN   B CG  1 
ATOM   1562 O  OD1 . ASN   B 1 76  ? 28.584  14.302 22.128 1.00 41.52 ? 76  ASN   B OD1 1 
ATOM   1563 N  ND2 . ASN   B 1 76  ? 29.584  16.186 22.848 1.00 43.80 ? 76  ASN   B ND2 1 
ATOM   1564 N  N   . VAL   B 1 77  ? 26.302  16.091 17.981 1.00 23.12 ? 77  VAL   B N   1 
ATOM   1565 C  CA  . VAL   B 1 77  ? 25.270  16.699 17.111 1.00 24.51 ? 77  VAL   B CA  1 
ATOM   1566 C  C   . VAL   B 1 77  ? 24.278  15.605 16.676 1.00 31.78 ? 77  VAL   B C   1 
ATOM   1567 O  O   . VAL   B 1 77  ? 24.732  14.590 16.145 1.00 31.91 ? 77  VAL   B O   1 
ATOM   1568 C  CB  . VAL   B 1 77  ? 25.894  17.383 15.883 1.00 26.20 ? 77  VAL   B CB  1 
ATOM   1569 C  CG1 . VAL   B 1 77  ? 24.843  18.102 15.052 1.00 29.64 ? 77  VAL   B CG1 1 
ATOM   1570 C  CG2 . VAL   B 1 77  ? 27.019  18.332 16.273 1.00 26.05 ? 77  VAL   B CG2 1 
ATOM   1571 N  N   . LEU   B 1 78  ? 22.982  15.837 16.873 1.00 33.36 ? 78  LEU   B N   1 
ATOM   1572 C  CA  . LEU   B 1 78  ? 21.933  14.873 16.437 1.00 29.95 ? 78  LEU   B CA  1 
ATOM   1573 C  C   . LEU   B 1 78  ? 21.889  14.821 14.909 1.00 33.56 ? 78  LEU   B C   1 
ATOM   1574 O  O   . LEU   B 1 78  ? 21.980  15.873 14.258 1.00 41.24 ? 78  LEU   B O   1 
ATOM   1575 C  CB  . LEU   B 1 78  ? 20.589  15.284 17.013 1.00 29.22 ? 78  LEU   B CB  1 
ATOM   1576 C  CG  . LEU   B 1 78  ? 20.346  14.888 18.473 1.00 44.18 ? 78  LEU   B CG  1 
ATOM   1577 C  CD1 . LEU   B 1 78  ? 18.974  14.263 18.626 1.00 50.96 ? 78  LEU   B CD1 1 
ATOM   1578 C  CD2 . LEU   B 1 78  ? 21.415  13.950 19.000 1.00 41.94 ? 78  LEU   B CD2 1 
ATOM   1579 N  N   . ALA   B 1 79  ? 21.745  13.635 14.352 1.00 36.24 ? 79  ALA   B N   1 
ATOM   1580 C  CA  . ALA   B 1 79  ? 21.844  13.543 12.882 1.00 40.40 ? 79  ALA   B CA  1 
ATOM   1581 C  C   . ALA   B 1 79  ? 20.502  13.240 12.230 1.00 38.39 ? 79  ALA   B C   1 
ATOM   1582 O  O   . ALA   B 1 79  ? 20.486  13.007 11.002 1.00 35.10 ? 79  ALA   B O   1 
ATOM   1583 C  CB  . ALA   B 1 79  ? 22.855  12.487 12.513 1.00 43.55 ? 79  ALA   B CB  1 
ATOM   1584 N  N   . TYR   B 1 80  ? 19.407  13.334 12.971 1.00 26.60 ? 80  TYR   B N   1 
ATOM   1585 C  CA  . TYR   B 1 80  ? 18.185  12.880 12.299 1.00 22.51 ? 80  TYR   B CA  1 
ATOM   1586 C  C   . TYR   B 1 80  ? 17.794  13.823 11.153 1.00 19.80 ? 80  TYR   B C   1 
ATOM   1587 O  O   . TYR   B 1 80  ? 17.811  15.046 11.251 1.00 22.71 ? 80  TYR   B O   1 
ATOM   1588 C  CB  . TYR   B 1 80  ? 16.998  12.704 13.254 1.00 22.86 ? 80  TYR   B CB  1 
ATOM   1589 C  CG  . TYR   B 1 80  ? 17.386  11.693 14.312 1.00 23.54 ? 80  TYR   B CG  1 
ATOM   1590 C  CD1 . TYR   B 1 80  ? 17.340  10.325 14.060 1.00 25.08 ? 80  TYR   B CD1 1 
ATOM   1591 C  CD2 . TYR   B 1 80  ? 17.806  12.122 15.561 1.00 27.80 ? 80  TYR   B CD2 1 
ATOM   1592 C  CE1 . TYR   B 1 80  ? 17.739  9.395  15.011 1.00 28.01 ? 80  TYR   B CE1 1 
ATOM   1593 C  CE2 . TYR   B 1 80  ? 18.165  11.202 16.530 1.00 29.35 ? 80  TYR   B CE2 1 
ATOM   1594 C  CZ  . TYR   B 1 80  ? 18.129  9.851  16.253 1.00 30.51 ? 80  TYR   B CZ  1 
ATOM   1595 O  OH  . TYR   B 1 80  ? 18.564  9.028  17.243 1.00 36.81 ? 80  TYR   B OH  1 
ATOM   1596 N  N   . ASP   B 1 81  ? 17.304  13.249 10.063 1.00 19.65 ? 81  ASP   B N   1 
ATOM   1597 C  CA  . ASP   B 1 81  ? 16.865  14.078 8.910  1.00 18.24 ? 81  ASP   B CA  1 
ATOM   1598 C  C   . ASP   B 1 81  ? 15.625  14.898 9.280  1.00 19.57 ? 81  ASP   B C   1 
ATOM   1599 O  O   . ASP   B 1 81  ? 15.588  16.084 8.965  1.00 19.65 ? 81  ASP   B O   1 
ATOM   1600 C  CB  . ASP   B 1 81  ? 16.637  13.199 7.695  1.00 19.30 ? 81  ASP   B CB  1 
ATOM   1601 C  CG  . ASP   B 1 81  ? 17.880  12.463 7.224  1.00 19.96 ? 81  ASP   B CG  1 
ATOM   1602 O  OD1 . ASP   B 1 81  ? 18.726  13.111 6.587  1.00 23.99 ? 81  ASP   B OD1 1 
ATOM   1603 O  OD2 . ASP   B 1 81  ? 17.994  11.265 7.520  1.00 20.85 ? 81  ASP   B OD2 1 
ATOM   1604 N  N   . THR   B 1 82  ? 14.644  14.246 9.904  1.00 17.95 ? 82  THR   B N   1 
ATOM   1605 C  CA  . THR   B 1 82  ? 13.391  14.926 10.271 1.00 19.12 ? 82  THR   B CA  1 
ATOM   1606 C  C   . THR   B 1 82  ? 12.964  14.503 11.666 1.00 18.20 ? 82  THR   B C   1 
ATOM   1607 O  O   . THR   B 1 82  ? 13.185  13.345 12.022 1.00 21.01 ? 82  THR   B O   1 
ATOM   1608 C  CB  . THR   B 1 82  ? 12.311  14.650 9.217  1.00 23.00 ? 82  THR   B CB  1 
ATOM   1609 O  OG1 . THR   B 1 82  ? 12.793  15.154 7.978  1.00 27.78 ? 82  THR   B OG1 1 
ATOM   1610 C  CG2 . THR   B 1 82  ? 11.011  15.365 9.522  1.00 27.87 ? 82  THR   B CG2 1 
ATOM   1611 N  N   . VAL   B 1 83  ? 12.412  15.445 12.420 1.00 21.57 ? 83  VAL   B N   1 
ATOM   1612 C  CA  . VAL   B 1 83  ? 11.888  15.134 13.778 1.00 20.50 ? 83  VAL   B CA  1 
ATOM   1613 C  C   . VAL   B 1 83  ? 10.454  15.670 13.843 1.00 21.20 ? 83  VAL   B C   1 
ATOM   1614 O  O   . VAL   B 1 83  ? 10.239  16.831 13.488 1.00 23.63 ? 83  VAL   B O   1 
ATOM   1615 C  CB  . VAL   B 1 83  ? 12.760  15.677 14.926 1.00 23.49 ? 83  VAL   B CB  1 
ATOM   1616 C  CG1 . VAL   B 1 83  ? 12.152  15.346 16.284 1.00 24.20 ? 83  VAL   B CG1 1 
ATOM   1617 C  CG2 . VAL   B 1 83  ? 14.195  15.180 14.836 1.00 22.73 ? 83  VAL   B CG2 1 
ATOM   1618 N  N   . PHE   B 1 84  ? 9.521   14.807 14.232 1.00 19.70 ? 84  PHE   B N   1 
ATOM   1619 C  CA  . PHE   B 1 84  ? 8.106   15.208 14.340 1.00 17.60 ? 84  PHE   B CA  1 
ATOM   1620 C  C   . PHE   B 1 84  ? 7.746   15.255 15.803 1.00 20.19 ? 84  PHE   B C   1 
ATOM   1621 O  O   . PHE   B 1 84  ? 8.139   14.362 16.543 1.00 23.30 ? 84  PHE   B O   1 
ATOM   1622 C  CB  . PHE   B 1 84  ? 7.205   14.185 13.652 1.00 19.97 ? 84  PHE   B CB  1 
ATOM   1623 C  CG  . PHE   B 1 84  ? 7.478   13.997 12.169 1.00 18.45 ? 84  PHE   B CG  1 
ATOM   1624 C  CD1 . PHE   B 1 84  ? 6.827   14.776 11.225 1.00 21.18 ? 84  PHE   B CD1 1 
ATOM   1625 C  CD2 . PHE   B 1 84  ? 8.382   13.043 11.723 1.00 27.83 ? 84  PHE   B CD2 1 
ATOM   1626 C  CE1 . PHE   B 1 84  ? 7.067   14.603 9.876  1.00 21.64 ? 84  PHE   B CE1 1 
ATOM   1627 C  CE2 . PHE   B 1 84  ? 8.622   12.878 10.370 1.00 30.33 ? 84  PHE   B CE2 1 
ATOM   1628 C  CZ  . PHE   B 1 84  ? 7.962   13.656 9.451  1.00 25.46 ? 84  PHE   B CZ  1 
ATOM   1629 N  N   . GLU   B 1 85  ? 7.029   16.294 16.189 1.00 20.48 ? 85  GLU   B N   1 
ATOM   1630 C  CA  . GLU   B 1 85  ? 6.572   16.394 17.573 1.00 23.71 ? 85  GLU   B CA  1 
ATOM   1631 C  C   . GLU   B 1 85  ? 5.092   16.674 17.615 1.00 23.39 ? 85  GLU   B C   1 
ATOM   1632 O  O   . GLU   B 1 85  ? 4.617   17.654 17.045 1.00 23.92 ? 85  GLU   B O   1 
ATOM   1633 C  CB  . GLU   B 1 85  ? 7.272   17.570 18.262 1.00 26.67 ? 85  GLU   B CB  1 
ATOM   1634 C  CG  . GLU   B 1 85  ? 8.778   17.328 18.329 1.00 33.63 ? 85  GLU   B CG  1 
ATOM   1635 C  CD  . GLU   B 1 85  ? 9.640   18.021 19.385 1.00 47.53 ? 85  GLU   B CD  1 
ATOM   1636 O  OE1 . GLU   B 1 85  ? 10.817  17.660 19.244 1.00 57.43 ? 85  GLU   B OE1 1 
ATOM   1637 O  OE2 . GLU   B 1 85  ? 9.253   18.813 20.304 1.00 50.86 ? 85  GLU   B OE2 1 
ATOM   1638 N  N   . MET   B 1 86  ? 4.358   15.815 18.360 1.00 22.70 ? 86  MET   B N   1 
ATOM   1639 C  CA  . MET   B 1 86  ? 2.936   15.975 18.544 1.00 22.83 ? 86  MET   B CA  1 
ATOM   1640 C  C   . MET   B 1 86  ? 2.650   16.219 20.027 1.00 20.15 ? 86  MET   B C   1 
ATOM   1641 O  O   . MET   B 1 86  ? 3.013   15.375 20.848 1.00 22.07 ? 86  MET   B O   1 
ATOM   1642 C  CB  . MET   B 1 86  ? 2.154   14.692 18.194 1.00 23.89 ? 86  MET   B CB  1 
ATOM   1643 C  CG  . MET   B 1 86  ? 2.334   14.189 16.780 1.00 34.47 ? 86  MET   B CG  1 
ATOM   1644 S  SD  . MET   B 1 86  ? 1.474   12.588 16.692 1.00 33.18 ? 86  MET   B SD  1 
ATOM   1645 C  CE  . MET   B 1 86  ? 2.132   12.235 15.074 1.00 32.39 ? 86  MET   B CE  1 
ATOM   1646 N  N   . ILE   B 1 87  ? 2.014   17.348 20.292 1.00 20.74 ? 87  ILE   B N   1 
ATOM   1647 C  CA  . ILE   B 1 87  ? 1.659   17.733 21.648 1.00 20.84 ? 87  ILE   B CA  1 
ATOM   1648 C  C   . ILE   B 1 87  ? 0.200   17.433 21.861 1.00 21.12 ? 87  ILE   B C   1 
ATOM   1649 O  O   . ILE   B 1 87  ? -0.642  17.870 21.071 1.00 21.64 ? 87  ILE   B O   1 
ATOM   1650 C  CB  . ILE   B 1 87  ? 2.019   19.211 21.886 1.00 24.47 ? 87  ILE   B CB  1 
ATOM   1651 C  CG1 . ILE   B 1 87  ? 3.520   19.381 21.701 1.00 29.66 ? 87  ILE   B CG1 1 
ATOM   1652 C  CG2 . ILE   B 1 87  ? 1.540   19.702 23.257 1.00 26.74 ? 87  ILE   B CG2 1 
ATOM   1653 C  CD1 . ILE   B 1 87  ? 3.974   20.821 21.766 1.00 36.87 ? 87  ILE   B CD1 1 
ATOM   1654 N  N   . VAL   B 1 88  ? -0.068  16.702 22.957 1.00 23.13 ? 88  VAL   B N   1 
ATOM   1655 C  CA  . VAL   B 1 88  ? -1.424  16.267 23.240 1.00 22.14 ? 88  VAL   B CA  1 
ATOM   1656 C  C   . VAL   B 1 88  ? -1.755  16.393 24.731 1.00 24.22 ? 88  VAL   B C   1 
ATOM   1657 O  O   . VAL   B 1 88  ? -0.863  16.344 25.553 1.00 23.13 ? 88  VAL   B O   1 
ATOM   1658 C  CB  . VAL   B 1 88  ? -1.587  14.803 22.795 1.00 23.74 ? 88  VAL   B CB  1 
ATOM   1659 C  CG1 . VAL   B 1 88  ? -1.335  14.636 21.302 1.00 26.96 ? 88  VAL   B CG1 1 
ATOM   1660 C  CG2 . VAL   B 1 88  ? -0.704  13.836 23.547 1.00 23.43 ? 88  VAL   B CG2 1 
ATOM   1661 N  N   . LYS   B 1 89  ? -3.059  16.397 25.048 1.00 26.25 ? 89  LYS   B N   1 
ATOM   1662 C  CA  . LYS   B 1 89  ? -3.526  16.360 26.438 1.00 28.30 ? 89  LYS   B CA  1 
ATOM   1663 C  C   . LYS   B 1 89  ? -3.418  14.960 27.023 1.00 28.55 ? 89  LYS   B C   1 
ATOM   1664 O  O   . LYS   B 1 89  ? -3.198  14.800 28.211 1.00 26.51 ? 89  LYS   B O   1 
ATOM   1665 C  CB  . LYS   B 1 89  ? -4.962  16.881 26.550 1.00 30.94 ? 89  LYS   B CB  1 
ATOM   1666 C  CG  . LYS   B 1 89  ? -5.136  18.309 26.064 1.00 44.13 ? 89  LYS   B CG  1 
ATOM   1667 C  CD  . LYS   B 1 89  ? -6.585  18.791 26.072 1.00 57.02 ? 89  LYS   B CD  1 
ATOM   1668 C  CE  . LYS   B 1 89  ? -6.817  19.884 25.076 1.00 64.10 ? 89  LYS   B CE  1 
ATOM   1669 N  NZ  . LYS   B 1 89  ? -8.200  20.367 25.157 1.00 69.73 ? 89  LYS   B NZ  1 
ATOM   1670 N  N   . ASP   B 1 90  ? -3.521  13.903 26.194 1.00 24.63 ? 90  ASP   B N   1 
ATOM   1671 C  CA  . ASP   B 1 90  ? -3.496  12.533 26.688 1.00 25.61 ? 90  ASP   B CA  1 
ATOM   1672 C  C   . ASP   B 1 90  ? -3.020  11.626 25.561 1.00 23.98 ? 90  ASP   B C   1 
ATOM   1673 O  O   . ASP   B 1 90  ? -3.338  11.856 24.387 1.00 27.80 ? 90  ASP   B O   1 
ATOM   1674 C  CB  . ASP   B 1 90  ? -4.877  12.104 27.155 1.00 29.00 ? 90  ASP   B CB  1 
ATOM   1675 C  CG  . ASP   B 1 90  ? -5.932  12.438 26.126 1.00 41.41 ? 90  ASP   B CG  1 
ATOM   1676 O  OD1 . ASP   B 1 90  ? -5.964  11.735 25.068 1.00 51.29 ? 90  ASP   B OD1 1 
ATOM   1677 O  OD2 . ASP   B 1 90  ? -6.618  13.457 26.324 1.00 43.92 ? 90  ASP   B OD2 1 
ATOM   1678 N  N   . ILE   B 1 91  ? -2.314  10.569 25.887 1.00 21.86 ? 91  ILE   B N   1 
ATOM   1679 C  CA  . ILE   B 1 91  ? -1.742  9.722  24.802 1.00 25.70 ? 91  ILE   B CA  1 
ATOM   1680 C  C   . ILE   B 1 91  ? -2.863  8.925  24.100 1.00 26.29 ? 91  ILE   B C   1 
ATOM   1681 O  O   . ILE   B 1 91  ? -2.635  8.481  22.972 1.00 23.61 ? 91  ILE   B O   1 
ATOM   1682 C  CB  . ILE   B 1 91  ? -0.623  8.836  25.372 1.00 35.00 ? 91  ILE   B CB  1 
ATOM   1683 C  CG1 . ILE   B 1 91  ? -1.143  7.883  26.428 1.00 39.38 ? 91  ILE   B CG1 1 
ATOM   1684 C  CG2 . ILE   B 1 91  ? 0.524   9.695  25.899 1.00 37.00 ? 91  ILE   B CG2 1 
ATOM   1685 C  CD1 . ILE   B 1 91  ? -0.588  6.482  26.299 1.00 41.74 ? 91  ILE   B CD1 1 
ATOM   1686 N  N   . GLU   B 1 92  ? -4.035  8.796  24.730 1.00 24.84 ? 92  GLU   B N   1 
ATOM   1687 C  CA  . GLU   B 1 92  ? -5.128  8.098  24.046 1.00 27.71 ? 92  GLU   B CA  1 
ATOM   1688 C  C   . GLU   B 1 92  ? -5.478  8.783  22.720 1.00 24.76 ? 92  GLU   B C   1 
ATOM   1689 O  O   . GLU   B 1 92  ? -5.821  8.116  21.751 1.00 25.29 ? 92  GLU   B O   1 
ATOM   1690 C  CB  . GLU   B 1 92  ? -6.337  7.986  24.975 1.00 38.47 ? 92  GLU   B CB  1 
ATOM   1691 C  CG  . GLU   B 1 92  ? -7.642  7.689  24.242 1.00 49.05 ? 92  GLU   B CG  1 
ATOM   1692 C  CD  . GLU   B 1 92  ? -8.717  7.072  25.127 1.00 61.32 ? 92  GLU   B CD  1 
ATOM   1693 O  OE1 . GLU   B 1 92  ? -9.201  5.956  24.794 1.00 65.18 ? 92  GLU   B OE1 1 
ATOM   1694 O  OE2 . GLU   B 1 92  ? -9.052  7.709  26.148 1.00 57.17 ? 92  GLU   B OE2 1 
ATOM   1695 N  N   . SER   B 1 93  ? -5.259  10.090 22.625 1.00 24.56 ? 93  SER   B N   1 
ATOM   1696 C  CA  . SER   B 1 93  ? -5.469  10.839 21.391 1.00 25.50 ? 93  SER   B CA  1 
ATOM   1697 C  C   . SER   B 1 93  ? -4.589  10.288 20.272 1.00 22.64 ? 93  SER   B C   1 
ATOM   1698 O  O   . SER   B 1 93  ? -5.063  10.073 19.151 1.00 23.76 ? 93  SER   B O   1 
ATOM   1699 C  CB  . SER   B 1 93  ? -5.185  12.302 21.588 1.00 31.00 ? 93  SER   B CB  1 
ATOM   1700 O  OG  . SER   B 1 93  ? -6.207  12.850 22.397 1.00 33.11 ? 93  SER   B OG  1 
ATOM   1701 N  N   . ILE   B 1 94  ? -3.329  10.032 20.595 1.00 21.94 ? 94  ILE   B N   1 
ATOM   1702 C  CA  . ILE   B 1 94  ? -2.400  9.474  19.627 1.00 20.70 ? 94  ILE   B CA  1 
ATOM   1703 C  C   . ILE   B 1 94  ? -2.704  8.018  19.292 1.00 21.24 ? 94  ILE   B C   1 
ATOM   1704 O  O   . ILE   B 1 94  ? -2.684  7.595  18.129 1.00 19.96 ? 94  ILE   B O   1 
ATOM   1705 C  CB  . ILE   B 1 94  ? -0.965  9.657  20.122 1.00 20.34 ? 94  ILE   B CB  1 
ATOM   1706 C  CG1 . ILE   B 1 94  ? -0.678  11.145 20.193 1.00 23.76 ? 94  ILE   B CG1 1 
ATOM   1707 C  CG2 . ILE   B 1 94  ? 0.010   8.940  19.188 1.00 21.65 ? 94  ILE   B CG2 1 
ATOM   1708 C  CD1 . ILE   B 1 94  ? 0.596   11.471 20.937 1.00 24.71 ? 94  ILE   B CD1 1 
ATOM   1709 N  N   . GLN   B 1 95  ? -2.923  7.203  20.315 1.00 21.28 ? 95  GLN   B N   1 
ATOM   1710 C  CA  . GLN   B 1 95  ? -3.168  5.790  20.055 1.00 21.09 ? 95  GLN   B CA  1 
ATOM   1711 C  C   . GLN   B 1 95  ? -4.440  5.601  19.212 1.00 19.28 ? 95  GLN   B C   1 
ATOM   1712 O  O   . GLN   B 1 95  ? -4.458  4.715  18.339 1.00 21.33 ? 95  GLN   B O   1 
ATOM   1713 C  CB  . GLN   B 1 95  ? -3.214  5.027  21.367 1.00 23.11 ? 95  GLN   B CB  1 
ATOM   1714 C  CG  . GLN   B 1 95  ? -1.883  5.049  22.115 1.00 25.89 ? 95  GLN   B CG  1 
ATOM   1715 C  CD  . GLN   B 1 95  ? -1.852  4.129  23.309 1.00 25.75 ? 95  GLN   B CD  1 
ATOM   1716 O  OE1 . GLN   B 1 95  ? -2.599  4.369  24.228 1.00 27.38 ? 95  GLN   B OE1 1 
ATOM   1717 N  NE2 . GLN   B 1 95  ? -0.942  3.175  23.373 1.00 32.25 ? 95  GLN   B NE2 1 
ATOM   1718 N  N   . THR   B 1 96  ? -5.484  6.396  19.477 1.00 19.72 ? 96  THR   B N   1 
ATOM   1719 C  CA  . THR   B 1 96  ? -6.709  6.277  18.712 1.00 22.29 ? 96  THR   B CA  1 
ATOM   1720 C  C   . THR   B 1 96  ? -6.464  6.695  17.255 1.00 22.65 ? 96  THR   B C   1 
ATOM   1721 O  O   . THR   B 1 96  ? -6.914  6.015  16.305 1.00 19.04 ? 96  THR   B O   1 
ATOM   1722 C  CB  . THR   B 1 96  ? -7.856  7.044  19.369 1.00 23.98 ? 96  THR   B CB  1 
ATOM   1723 O  OG1 . THR   B 1 96  ? -7.962  6.444  20.680 1.00 25.03 ? 96  THR   B OG1 1 
ATOM   1724 C  CG2 . THR   B 1 96  ? -9.140  6.778  18.616 1.00 27.20 ? 96  THR   B CG2 1 
ATOM   1725 N  N   . MET   B 1 97  ? -5.711  7.779  17.063 1.00 20.70 ? 97  MET   B N   1 
ATOM   1726 C  CA  . MET   B 1 97  ? -5.360  8.212  15.714 1.00 18.81 ? 97  MET   B CA  1 
ATOM   1727 C  C   . MET   B 1 97  ? -4.648  7.087  14.952 1.00 18.96 ? 97  MET   B C   1 
ATOM   1728 O  O   . MET   B 1 97  ? -4.936  6.786  13.803 1.00 19.30 ? 97  MET   B O   1 
ATOM   1729 C  CB  . MET   B 1 97  ? -4.459  9.456  15.773 1.00 18.20 ? 97  MET   B CB  1 
ATOM   1730 C  CG  . MET   B 1 97  ? -4.041  9.915  14.410 1.00 18.55 ? 97  MET   B CG  1 
ATOM   1731 S  SD  . MET   B 1 97  ? -3.061  11.430 14.496 1.00 22.13 ? 97  MET   B SD  1 
ATOM   1732 C  CE  . MET   B 1 97  ? -1.574  10.658 15.097 1.00 21.91 ? 97  MET   B CE  1 
ATOM   1733 N  N   . GLN   B 1 98  ? -3.628  6.498  15.575 1.00 18.21 ? 98  GLN   B N   1 
ATOM   1734 C  CA  . GLN   B 1 98  ? -2.789  5.490  14.960 1.00 20.75 ? 98  GLN   B CA  1 
ATOM   1735 C  C   . GLN   B 1 98  ? -3.572  4.236  14.576 1.00 22.22 ? 98  GLN   B C   1 
ATOM   1736 O  O   . GLN   B 1 98  ? -3.155  3.554  13.673 1.00 20.07 ? 98  GLN   B O   1 
ATOM   1737 C  CB  . GLN   B 1 98  ? -1.645  5.133  15.896 1.00 24.44 ? 98  GLN   B CB  1 
ATOM   1738 C  CG  . GLN   B 1 98  ? -0.602  6.238  15.961 1.00 25.02 ? 98  GLN   B CG  1 
ATOM   1739 C  CD  . GLN   B 1 98  ? 0.500   5.893  16.936 1.00 28.37 ? 98  GLN   B CD  1 
ATOM   1740 O  OE1 . GLN   B 1 98  ? 0.257   5.243  17.946 1.00 29.77 ? 98  GLN   B OE1 1 
ATOM   1741 N  NE2 . GLN   B 1 98  ? 1.650   6.481  16.727 1.00 29.88 ? 98  GLN   B NE2 1 
ATOM   1742 N  N   . LYS   B 1 99  ? -4.675  3.925  15.255 1.00 22.75 ? 99  LYS   B N   1 
ATOM   1743 C  CA  . LYS   B 1 99  ? -5.429  2.722  14.916 1.00 24.80 ? 99  LYS   B CA  1 
ATOM   1744 C  C   . LYS   B 1 99  ? -6.627  3.034  14.034 1.00 22.67 ? 99  LYS   B C   1 
ATOM   1745 O  O   . LYS   B 1 99  ? -7.357  2.111  13.671 1.00 22.13 ? 99  LYS   B O   1 
ATOM   1746 C  CB  . LYS   B 1 99  ? -5.869  1.999  16.199 1.00 30.06 ? 99  LYS   B CB  1 
ATOM   1747 C  CG  . LYS   B 1 99  ? -4.721  1.437  17.044 1.00 29.92 ? 99  LYS   B CG  1 
ATOM   1748 C  CD  . LYS   B 1 99  ? -3.901  0.457  16.218 1.00 36.80 ? 99  LYS   B CD  1 
ATOM   1749 C  CE  . LYS   B 1 99  ? -3.032  -0.520 16.978 1.00 51.60 ? 99  LYS   B CE  1 
ATOM   1750 N  NZ  . LYS   B 1 99  ? -2.126  0.259  17.818 1.00 53.95 ? 99  LYS   B NZ  1 
ATOM   1751 N  N   . ASP   B 1 100 ? -6.828  4.312  13.685 1.00 20.07 ? 100 ASP   B N   1 
ATOM   1752 C  CA  . ASP   B 1 100 ? -7.904  4.727  12.809 1.00 22.30 ? 100 ASP   B CA  1 
ATOM   1753 C  C   . ASP   B 1 100 ? -7.718  4.015  11.470 1.00 23.44 ? 100 ASP   B C   1 
ATOM   1754 O  O   . ASP   B 1 100 ? -6.634  4.036  10.891 1.00 19.80 ? 100 ASP   B O   1 
ATOM   1755 C  CB  . ASP   B 1 100 ? -7.949  6.241  12.701 1.00 19.86 ? 100 ASP   B CB  1 
ATOM   1756 C  CG  . ASP   B 1 100 ? -8.923  6.866  11.727 1.00 24.42 ? 100 ASP   B CG  1 
ATOM   1757 O  OD1 . ASP   B 1 100 ? -8.940  6.455  10.590 1.00 30.94 ? 100 ASP   B OD1 1 
ATOM   1758 O  OD2 . ASP   B 1 100 ? -9.620  7.835  12.095 1.00 25.55 ? 100 ASP   B OD2 1 
ATOM   1759 N  N   . GLU   B 1 101 ? -8.774  3.380  10.932 1.00 22.02 ? 101 GLU   B N   1 
ATOM   1760 C  CA  . GLU   B 1 101 ? -8.494  2.539  9.764  1.00 22.90 ? 101 GLU   B CA  1 
ATOM   1761 C  C   . GLU   B 1 101 ? -8.044  3.412  8.589  1.00 21.71 ? 101 GLU   B C   1 
ATOM   1762 O  O   . GLU   B 1 101 ? -7.200  2.998  7.816  1.00 19.49 ? 101 GLU   B O   1 
ATOM   1763 C  CB  . GLU   B 1 101 ? -9.687  1.709  9.300  1.00 23.81 ? 101 GLU   B CB  1 
ATOM   1764 C  CG  . GLU   B 1 101 ? -10.897 2.561  8.955  1.00 20.38 ? 101 GLU   B CG  1 
ATOM   1765 C  CD  . GLU   B 1 101 ? -10.963 2.910  7.465  1.00 25.27 ? 101 GLU   B CD  1 
ATOM   1766 O  OE1 . GLU   B 1 101 ? -10.313 2.265  6.652  1.00 23.15 ? 101 GLU   B OE1 1 
ATOM   1767 O  OE2 . GLU   B 1 101 ? -11.607 3.905  7.090  1.00 24.36 ? 101 GLU   B OE2 1 
ATOM   1768 N  N   . GLU   B 1 102 ? -8.538  4.649  8.479  1.00 19.23 ? 102 GLU   B N   1 
ATOM   1769 C  CA  . GLU   B 1 102 ? -8.055  5.533  7.427  1.00 18.66 ? 102 GLU   B CA  1 
ATOM   1770 C  C   . GLU   B 1 102 ? -6.546  5.801  7.560  1.00 17.45 ? 102 GLU   B C   1 
ATOM   1771 O  O   . GLU   B 1 102 ? -5.840  5.933  6.551  1.00 20.32 ? 102 GLU   B O   1 
ATOM   1772 C  CB  . GLU   B 1 102 ? -8.886  6.813  7.394  1.00 21.31 ? 102 GLU   B CB  1 
ATOM   1773 C  CG  . GLU   B 1 102 ? -8.661  7.692  6.177  1.00 22.33 ? 102 GLU   B CG  1 
ATOM   1774 C  CD  . GLU   B 1 102 ? -9.359  9.060  6.361  1.00 25.75 ? 102 GLU   B CD  1 
ATOM   1775 O  OE1 . GLU   B 1 102 ? -10.199 9.258  7.273  1.00 31.60 ? 102 GLU   B OE1 1 
ATOM   1776 O  OE2 . GLU   B 1 102 ? -8.992  9.911  5.573  1.00 25.67 ? 102 GLU   B OE2 1 
ATOM   1777 N  N   . PHE   B 1 103 ? -6.087  6.060  8.793  1.00 17.71 ? 103 PHE   B N   1 
ATOM   1778 C  CA  . PHE   B 1 103 ? -4.686  6.282  9.098  1.00 16.98 ? 103 PHE   B CA  1 
ATOM   1779 C  C   . PHE   B 1 103 ? -3.825  5.103  8.609  1.00 16.89 ? 103 PHE   B C   1 
ATOM   1780 O  O   . PHE   B 1 103 ? -2.766  5.306  8.012  1.00 16.05 ? 103 PHE   B O   1 
ATOM   1781 C  CB  . PHE   B 1 103 ? -4.542  6.497  10.600 1.00 19.21 ? 103 PHE   B CB  1 
ATOM   1782 C  CG  . PHE   B 1 103 ? -3.179  7.056  11.020 1.00 18.67 ? 103 PHE   B CG  1 
ATOM   1783 C  CD1 . PHE   B 1 103 ? -2.963  8.434  11.023 1.00 19.94 ? 103 PHE   B CD1 1 
ATOM   1784 C  CD2 . PHE   B 1 103 ? -2.156  6.232  11.422 1.00 19.94 ? 103 PHE   B CD2 1 
ATOM   1785 C  CE1 . PHE   B 1 103 ? -1.734  8.933  11.450 1.00 19.43 ? 103 PHE   B CE1 1 
ATOM   1786 C  CE2 . PHE   B 1 103 ? -0.926  6.746  11.798 1.00 21.76 ? 103 PHE   B CE2 1 
ATOM   1787 C  CZ  . PHE   B 1 103 ? -0.744  8.086  11.862 1.00 19.39 ? 103 PHE   B CZ  1 
ATOM   1788 N  N   . LEU   B 1 104 ? -4.302  3.870  8.832  1.00 16.57 ? 104 LEU   B N   1 
ATOM   1789 C  CA  . LEU   B 1 104 ? -3.594  2.647  8.484  1.00 16.35 ? 104 LEU   B CA  1 
ATOM   1790 C  C   . LEU   B 1 104 ? -3.378  2.496  6.989  1.00 15.55 ? 104 LEU   B C   1 
ATOM   1791 O  O   . LEU   B 1 104 ? -2.474  1.759  6.562  1.00 15.89 ? 104 LEU   B O   1 
ATOM   1792 C  CB  . LEU   B 1 104 ? -4.304  1.411  9.078  1.00 18.50 ? 104 LEU   B CB  1 
ATOM   1793 C  CG  . LEU   B 1 104 ? -4.282  1.279  10.601 1.00 21.68 ? 104 LEU   B CG  1 
ATOM   1794 C  CD1 . LEU   B 1 104 ? -5.045  0.019  10.994 1.00 26.89 ? 104 LEU   B CD1 1 
ATOM   1795 C  CD2 . LEU   B 1 104 ? -2.922  1.190  11.145 1.00 22.14 ? 104 LEU   B CD2 1 
ATOM   1796 N  N   . ARG   B 1 105 ? -4.247  3.105  6.148  1.00 15.47 ? 105 ARG   B N   1 
ATOM   1797 C  CA  . ARG   B 1 105 ? -4.101  3.019  4.697  1.00 17.10 ? 105 ARG   B CA  1 
ATOM   1798 C  C   . ARG   B 1 105 ? -3.643  4.327  4.033  1.00 16.69 ? 105 ARG   B C   1 
ATOM   1799 O  O   . ARG   B 1 105 ? -3.561  4.382  2.803  1.00 16.51 ? 105 ARG   B O   1 
ATOM   1800 C  CB  . ARG   B 1 105 ? -5.385  2.473  4.073  1.00 17.59 ? 105 ARG   B CB  1 
ATOM   1801 C  CG  . ARG   B 1 105 ? -6.652  3.268  4.334  1.00 17.65 ? 105 ARG   B CG  1 
ATOM   1802 C  CD  . ARG   B 1 105 ? -7.936  2.863  3.575  1.00 18.75 ? 105 ARG   B CD  1 
ATOM   1803 N  NE  . ARG   B 1 105 ? -9.091  3.489  4.235  1.00 19.58 ? 105 ARG   B NE  1 
ATOM   1804 C  CZ  . ARG   B 1 105 ? -9.663  4.650  3.891  1.00 19.49 ? 105 ARG   B CZ  1 
ATOM   1805 N  NH1 . ARG   B 1 105 ? -9.130  5.349  2.927  1.00 20.99 ? 105 ARG   B NH1 1 
ATOM   1806 N  NH2 . ARG   B 1 105 ? -10.687 5.117  4.606  1.00 20.54 ? 105 ARG   B NH2 1 
ATOM   1807 N  N   . THR   B 1 106 ? -3.222  5.328  4.836  1.00 16.21 ? 106 THR   B N   1 
ATOM   1808 C  CA  . THR   B 1 106 ? -2.759  6.590  4.299  1.00 17.08 ? 106 THR   B CA  1 
ATOM   1809 C  C   . THR   B 1 106 ? -1.374  6.907  4.888  1.00 16.98 ? 106 THR   B C   1 
ATOM   1810 O  O   . THR   B 1 106 ? -0.347  6.758  4.224  1.00 16.90 ? 106 THR   B O   1 
ATOM   1811 C  CB  . THR   B 1 106 ? -3.793  7.711  4.550  1.00 19.45 ? 106 THR   B CB  1 
ATOM   1812 O  OG1 . THR   B 1 106 ? -4.072  7.853  5.941  1.00 21.16 ? 106 THR   B OG1 1 
ATOM   1813 C  CG2 . THR   B 1 106 ? -5.138  7.397  3.916  1.00 19.21 ? 106 THR   B CG2 1 
ATOM   1814 N  N   . ALA   B 1 107 ? -1.348  7.285  6.161  1.00 17.64 ? 107 ALA   B N   1 
ATOM   1815 C  CA  . ALA   B 1 107 ? -0.145  7.722  6.864  1.00 17.90 ? 107 ALA   B CA  1 
ATOM   1816 C  C   . ALA   B 1 107 ? 0.865   6.585  6.996  1.00 18.05 ? 107 ALA   B C   1 
ATOM   1817 O  O   . ALA   B 1 107 ? 2.037   6.773  6.717  1.00 18.04 ? 107 ALA   B O   1 
ATOM   1818 C  CB  . ALA   B 1 107 ? -0.481  8.324  8.203  1.00 18.55 ? 107 ALA   B CB  1 
ATOM   1819 N  N   . ILE   B 1 108 ? 0.403   5.367  7.343  1.00 14.98 ? 108 ILE   B N   1 
ATOM   1820 C  CA  . ILE   B 1 108 ? 1.316   4.251  7.574  1.00 16.52 ? 108 ILE   B CA  1 
ATOM   1821 C  C   . ILE   B 1 108 ? 2.049   3.901  6.285  1.00 18.39 ? 108 ILE   B C   1 
ATOM   1822 O  O   . ILE   B 1 108 ? 3.288   3.870  6.244  1.00 17.63 ? 108 ILE   B O   1 
ATOM   1823 C  CB  . ILE   B 1 108 ? 0.602   3.062  8.248  1.00 17.11 ? 108 ILE   B CB  1 
ATOM   1824 C  CG1 . ILE   B 1 108 ? 0.191   3.424  9.701  1.00 19.44 ? 108 ILE   B CG1 1 
ATOM   1825 C  CG2 . ILE   B 1 108 ? 1.508   1.833  8.200  1.00 20.14 ? 108 ILE   B CG2 1 
ATOM   1826 C  CD1 . ILE   B 1 108 ? 1.325   3.813  10.631 1.00 25.08 ? 108 ILE   B CD1 1 
ATOM   1827 N  N   . PRO   B 1 109 ? 1.353   3.648  5.159  1.00 16.44 ? 109 PRO   B N   1 
ATOM   1828 C  CA  . PRO   B 1 109 ? 2.071   3.333  3.932  1.00 15.59 ? 109 PRO   B CA  1 
ATOM   1829 C  C   . PRO   B 1 109 ? 2.981   4.465  3.478  1.00 16.02 ? 109 PRO   B C   1 
ATOM   1830 O  O   . PRO   B 1 109 ? 4.021   4.223  2.840  1.00 16.09 ? 109 PRO   B O   1 
ATOM   1831 C  CB  . PRO   B 1 109 ? 0.994   2.978  2.875  1.00 17.99 ? 109 PRO   B CB  1 
ATOM   1832 C  CG  . PRO   B 1 109 ? -0.306  3.363  3.541  1.00 18.29 ? 109 PRO   B CG  1 
ATOM   1833 C  CD  . PRO   B 1 109 ? -0.105  3.410  5.042  1.00 19.37 ? 109 PRO   B CD  1 
ATOM   1834 N  N   . ASP   B 1 110 ? 2.575   5.709  3.743  1.00 15.35 ? 110 ASP   B N   1 
ATOM   1835 C  CA  . ASP   B 1 110 ? 3.339   6.848  3.265  1.00 18.15 ? 110 ASP   B CA  1 
ATOM   1836 C  C   . ASP   B 1 110 ? 4.718   6.878  3.941  1.00 17.09 ? 110 ASP   B C   1 
ATOM   1837 O  O   . ASP   B 1 110 ? 5.694   7.380  3.331  1.00 18.50 ? 110 ASP   B O   1 
ATOM   1838 C  CB  . ASP   B 1 110 ? 2.702   8.190  3.564  1.00 19.38 ? 110 ASP   B CB  1 
ATOM   1839 C  CG  . ASP   B 1 110 ? 3.348   9.339  2.795  1.00 22.38 ? 110 ASP   B CG  1 
ATOM   1840 O  OD1 . ASP   B 1 110 ? 3.413   9.270  1.580  1.00 20.82 ? 110 ASP   B OD1 1 
ATOM   1841 O  OD2 . ASP   B 1 110 ? 3.877   10.235 3.401  1.00 21.58 ? 110 ASP   B OD2 1 
ATOM   1842 N  N   . LEU   B 1 111 ? 4.831   6.352  5.176  1.00 16.59 ? 111 LEU   B N   1 
ATOM   1843 C  CA  . LEU   B 1 111 ? 6.131   6.317  5.884  1.00 17.53 ? 111 LEU   B CA  1 
ATOM   1844 C  C   . LEU   B 1 111 ? 7.237   5.686  5.029  1.00 19.65 ? 111 LEU   B C   1 
ATOM   1845 O  O   . LEU   B 1 111 ? 8.392   6.130  5.070  1.00 18.32 ? 111 LEU   B O   1 
ATOM   1846 C  CB  . LEU   B 1 111 ? 6.032   5.581  7.228  1.00 18.54 ? 111 LEU   B CB  1 
ATOM   1847 C  CG  . LEU   B 1 111 ? 5.044   6.150  8.239  1.00 20.81 ? 111 LEU   B CG  1 
ATOM   1848 C  CD1 . LEU   B 1 111 ? 4.928   5.166  9.409  1.00 21.79 ? 111 LEU   B CD1 1 
ATOM   1849 C  CD2 . LEU   B 1 111 ? 5.484   7.496  8.693  1.00 27.50 ? 111 LEU   B CD2 1 
ATOM   1850 N  N   . PHE   B 1 112 ? 6.890   4.615  4.290  1.00 17.28 ? 112 PHE   B N   1 
ATOM   1851 C  CA  . PHE   B 1 112 ? 7.862   3.861  3.519  1.00 17.11 ? 112 PHE   B CA  1 
ATOM   1852 C  C   . PHE   B 1 112 ? 8.389   4.685  2.330  1.00 17.99 ? 112 PHE   B C   1 
ATOM   1853 O  O   . PHE   B 1 112 ? 9.388   4.314  1.733  1.00 19.18 ? 112 PHE   B O   1 
ATOM   1854 C  CB  . PHE   B 1 112 ? 7.292   2.514  3.063  1.00 18.45 ? 112 PHE   B CB  1 
ATOM   1855 C  CG  . PHE   B 1 112 ? 7.057   1.623  4.261  1.00 18.01 ? 112 PHE   B CG  1 
ATOM   1856 C  CD1 . PHE   B 1 112 ? 5.834   1.656  4.949  1.00 19.69 ? 112 PHE   B CD1 1 
ATOM   1857 C  CD2 . PHE   B 1 112 ? 8.081   0.827  4.747  1.00 17.81 ? 112 PHE   B CD2 1 
ATOM   1858 C  CE1 . PHE   B 1 112 ? 5.651   0.864  6.055  1.00 19.77 ? 112 PHE   B CE1 1 
ATOM   1859 C  CE2 . PHE   B 1 112 ? 7.882   0.028  5.856  1.00 18.05 ? 112 PHE   B CE2 1 
ATOM   1860 C  CZ  . PHE   B 1 112 ? 6.677   0.046  6.509  1.00 18.36 ? 112 PHE   B CZ  1 
ATOM   1861 N  N   . ASN   B 1 113 ? 7.699   5.776  1.980  1.00 15.97 ? 113 ASN   B N   1 
ATOM   1862 C  CA  . ASN   B 1 113 ? 8.132   6.629  0.886  1.00 16.91 ? 113 ASN   B CA  1 
ATOM   1863 C  C   . ASN   B 1 113 ? 9.052   7.758  1.382  1.00 17.00 ? 113 ASN   B C   1 
ATOM   1864 O  O   . ASN   B 1 113 ? 9.539   8.550  0.562  1.00 20.16 ? 113 ASN   B O   1 
ATOM   1865 C  CB  . ASN   B 1 113 ? 6.941   7.192  0.130  1.00 17.63 ? 113 ASN   B CB  1 
ATOM   1866 C  CG  . ASN   B 1 113 ? 6.262   6.088  -0.630 1.00 20.51 ? 113 ASN   B CG  1 
ATOM   1867 O  OD1 . ASN   B 1 113 ? 6.917   5.162  -1.093 1.00 21.25 ? 113 ASN   B OD1 1 
ATOM   1868 N  ND2 . ASN   B 1 113 ? 4.937   6.119  -0.677 1.00 22.46 ? 113 ASN   B ND2 1 
ATOM   1869 N  N   . PHE   B 1 114 ? 9.348   7.837  2.685  1.00 17.86 ? 114 PHE   B N   1 
ATOM   1870 C  CA  . PHE   B 1 114 ? 10.310  8.859  3.116  1.00 17.20 ? 114 PHE   B CA  1 
ATOM   1871 C  C   . PHE   B 1 114 ? 11.215  8.465  4.283  1.00 19.13 ? 114 PHE   B C   1 
ATOM   1872 O  O   . PHE   B 1 114 ? 12.208  9.154  4.529  1.00 18.52 ? 114 PHE   B O   1 
ATOM   1873 C  CB  . PHE   B 1 114 ? 9.641   10.205 3.400  1.00 17.77 ? 114 PHE   B CB  1 
ATOM   1874 C  CG  . PHE   B 1 114 ? 8.738   10.259 4.622  1.00 17.93 ? 114 PHE   B CG  1 
ATOM   1875 C  CD1 . PHE   B 1 114 ? 7.392   9.932  4.514  1.00 17.49 ? 114 PHE   B CD1 1 
ATOM   1876 C  CD2 . PHE   B 1 114 ? 9.209   10.680 5.860  1.00 18.99 ? 114 PHE   B CD2 1 
ATOM   1877 C  CE1 . PHE   B 1 114 ? 6.571   9.963  5.630  1.00 19.01 ? 114 PHE   B CE1 1 
ATOM   1878 C  CE2 . PHE   B 1 114 ? 8.360   10.734 6.961  1.00 19.63 ? 114 PHE   B CE2 1 
ATOM   1879 C  CZ  . PHE   B 1 114 ? 7.030   10.372 6.827  1.00 20.33 ? 114 PHE   B CZ  1 
ATOM   1880 N  N   . ALA   B 1 115 ? 10.882  7.443  5.080  1.00 16.56 ? 115 ALA   B N   1 
ATOM   1881 C  CA  . ALA   B 1 115 ? 11.635  7.078  6.254  1.00 18.45 ? 115 ALA   B CA  1 
ATOM   1882 C  C   . ALA   B 1 115 ? 12.315  5.728  6.062  1.00 19.65 ? 115 ALA   B C   1 
ATOM   1883 O  O   . ALA   B 1 115 ? 11.795  4.804  5.417  1.00 19.48 ? 115 ALA   B O   1 
ATOM   1884 C  CB  . ALA   B 1 115 ? 10.707  7.088  7.438  1.00 19.03 ? 115 ALA   B CB  1 
ATOM   1885 N  N   . ASP   B 1 116 ? 13.492  5.595  6.666  1.00 17.79 ? 116 ASP   B N   1 
ATOM   1886 C  CA  . ASP   B 1 116 ? 14.099  4.303  6.817  1.00 20.50 ? 116 ASP   B CA  1 
ATOM   1887 C  C   . ASP   B 1 116 ? 13.483  3.631  8.027  1.00 18.32 ? 116 ASP   B C   1 
ATOM   1888 O  O   . ASP   B 1 116 ? 13.739  4.002  9.188  1.00 21.34 ? 116 ASP   B O   1 
ATOM   1889 C  CB  . ASP   B 1 116 ? 15.600  4.379  7.070  1.00 25.18 ? 116 ASP   B CB  1 
ATOM   1890 C  CG  . ASP   B 1 116 ? 16.275  3.025  7.197  1.00 27.40 ? 116 ASP   B CG  1 
ATOM   1891 O  OD1 . ASP   B 1 116 ? 15.592  2.011  7.519  1.00 25.61 ? 116 ASP   B OD1 1 
ATOM   1892 O  OD2 . ASP   B 1 116 ? 17.514  3.023  7.062  1.00 30.04 ? 116 ASP   B OD2 1 
ATOM   1893 N  N   . MET   B 1 117 ? 12.567  2.713  7.753  1.00 18.12 ? 117 MET   B N   1 
ATOM   1894 C  CA  . MET   B 1 117 ? 11.700  2.226  8.810  1.00 19.04 ? 117 MET   B CA  1 
ATOM   1895 C  C   . MET   B 1 117 ? 12.389  1.181  9.706  1.00 23.31 ? 117 MET   B C   1 
ATOM   1896 O  O   . MET   B 1 117 ? 11.756  0.607  10.618 1.00 24.33 ? 117 MET   B O   1 
ATOM   1897 C  CB  . MET   B 1 117 ? 10.372  1.714  8.213  1.00 19.70 ? 117 MET   B CB  1 
ATOM   1898 C  CG  . MET   B 1 117 ? 9.448   2.908  7.798  1.00 19.80 ? 117 MET   B CG  1 
ATOM   1899 S  SD  . MET   B 1 117 ? 8.871   3.909  9.151  1.00 25.31 ? 117 MET   B SD  1 
ATOM   1900 C  CE  . MET   B 1 117 ? 7.782   2.771  10.033 1.00 34.47 ? 117 MET   B CE  1 
ATOM   1901 N  N   . THR   B 1 118 ? 13.661  0.911  9.435  1.00 21.56 ? 118 THR   B N   1 
ATOM   1902 C  CA  . THR   B 1 118 ? 14.422  0.052  10.332 1.00 27.28 ? 118 THR   B CA  1 
ATOM   1903 C  C   . THR   B 1 118 ? 15.030  0.854  11.477 1.00 28.24 ? 118 THR   B C   1 
ATOM   1904 O  O   . THR   B 1 118 ? 15.550  0.223  12.388 1.00 28.83 ? 118 THR   B O   1 
ATOM   1905 C  CB  . THR   B 1 118 ? 15.547  -0.677 9.592  1.00 27.60 ? 118 THR   B CB  1 
ATOM   1906 O  OG1 . THR   B 1 118 ? 16.534  0.263  9.170  1.00 26.25 ? 118 THR   B OG1 1 
ATOM   1907 C  CG2 . THR   B 1 118 ? 15.047  -1.459 8.384  1.00 31.34 ? 118 THR   B CG2 1 
ATOM   1908 N  N   . ARG   B 1 119 ? 14.980  2.191  11.454 1.00 27.79 ? 119 ARG   B N   1 
ATOM   1909 C  CA  . ARG   B 1 119 ? 15.818  3.016  12.326 1.00 32.14 ? 119 ARG   B CA  1 
ATOM   1910 C  C   . ARG   B 1 119 ? 15.077  4.109  13.106 1.00 28.78 ? 119 ARG   B C   1 
ATOM   1911 O  O   . ARG   B 1 119 ? 15.722  4.910  13.772 1.00 27.71 ? 119 ARG   B O   1 
ATOM   1912 C  CB  . ARG   B 1 119 ? 16.843  3.777  11.463 1.00 34.44 ? 119 ARG   B CB  1 
ATOM   1913 C  CG  . ARG   B 1 119 ? 17.994  2.921  10.949 1.00 42.99 ? 119 ARG   B CG  1 
ATOM   1914 C  CD  . ARG   B 1 119 ? 19.191  3.779  10.542 1.00 50.54 ? 119 ARG   B CD  1 
ATOM   1915 N  NE  . ARG   B 1 119 ? 20.405  2.978  10.342 1.00 59.80 ? 119 ARG   B NE  1 
ATOM   1916 C  CZ  . ARG   B 1 119 ? 20.555  1.962  9.475  1.00 66.74 ? 119 ARG   B CZ  1 
ATOM   1917 N  NH1 . ARG   B 1 119 ? 19.574  1.598  8.668  1.00 78.05 ? 119 ARG   B NH1 1 
ATOM   1918 N  NH2 . ARG   B 1 119 ? 21.699  1.305  9.389  1.00 62.16 ? 119 ARG   B NH2 1 
ATOM   1919 N  N   . THR   B 1 120 ? 13.751  4.182  13.128 1.00 25.20 ? 120 THR   B N   1 
ATOM   1920 C  CA  . THR   B 1 120 ? 13.101  5.316  13.799 1.00 23.73 ? 120 THR   B CA  1 
ATOM   1921 C  C   . THR   B 1 120 ? 13.258  5.235  15.323 1.00 25.42 ? 120 THR   B C   1 
ATOM   1922 O  O   . THR   B 1 120 ? 13.094  4.161  15.889 1.00 26.91 ? 120 THR   B O   1 
ATOM   1923 C  CB  . THR   B 1 120 ? 11.612  5.341  13.448 1.00 23.93 ? 120 THR   B CB  1 
ATOM   1924 O  OG1 . THR   B 1 120 ? 11.447  5.150  12.034 1.00 23.41 ? 120 THR   B OG1 1 
ATOM   1925 C  CG2 . THR   B 1 120 ? 10.979  6.644  13.900 1.00 23.53 ? 120 THR   B CG2 1 
ATOM   1926 N  N   . LYS   B 1 121 ? 13.563  6.377  15.988 1.00 22.57 ? 121 LYS   B N   1 
ATOM   1927 C  CA  . LYS   B 1 121 ? 13.573  6.467  17.438 1.00 22.46 ? 121 LYS   B CA  1 
ATOM   1928 C  C   . LYS   B 1 121 ? 12.423  7.331  17.926 1.00 19.96 ? 121 LYS   B C   1 
ATOM   1929 O  O   . LYS   B 1 121 ? 11.859  8.126  17.195 1.00 20.26 ? 121 LYS   B O   1 
ATOM   1930 C  CB  . LYS   B 1 121 ? 14.939  6.955  17.940 1.00 23.31 ? 121 LYS   B CB  1 
ATOM   1931 C  CG  . LYS   B 1 121 ? 16.047  6.023  17.508 1.00 28.29 ? 121 LYS   B CG  1 
ATOM   1932 C  CD  . LYS   B 1 121 ? 17.278  6.077  18.412 1.00 38.93 ? 121 LYS   B CD  1 
ATOM   1933 C  CE  . LYS   B 1 121 ? 18.312  5.015  18.079 1.00 44.07 ? 121 LYS   B CE  1 
ATOM   1934 N  NZ  . LYS   B 1 121 ? 19.133  4.920  19.299 1.00 48.22 ? 121 LYS   B NZ  1 
ATOM   1935 N  N   . GLY   B 1 122 ? 12.058  7.216  19.208 1.00 18.94 ? 122 GLY   B N   1 
ATOM   1936 C  CA  . GLY   B 1 122 ? 11.026  8.086  19.720 1.00 17.99 ? 122 GLY   B CA  1 
ATOM   1937 C  C   . GLY   B 1 122 ? 11.166  8.364  21.216 1.00 16.62 ? 122 GLY   B C   1 
ATOM   1938 O  O   . GLY   B 1 122 ? 11.950  7.669  21.885 1.00 22.51 ? 122 GLY   B O   1 
ATOM   1939 N  N   . SER   B 1 123 ? 10.322  9.258  21.691 1.00 21.06 ? 123 SER   B N   1 
ATOM   1940 C  CA  . SER   B 1 123 ? 10.190  9.540  23.113 1.00 23.24 ? 123 SER   B CA  1 
ATOM   1941 C  C   . SER   B 1 123 ? 8.797   10.053 23.415 1.00 21.58 ? 123 SER   B C   1 
ATOM   1942 O  O   . SER   B 1 123 ? 8.102   10.615 22.549 1.00 21.91 ? 123 SER   B O   1 
ATOM   1943 C  CB  . SER   B 1 123 ? 11.220  10.593 23.549 1.00 21.67 ? 123 SER   B CB  1 
ATOM   1944 O  OG  . SER   B 1 123 ? 10.859  11.839 23.012 1.00 25.84 ? 123 SER   B OG  1 
ATOM   1945 N  N   . GLY   B 1 124 ? 8.449   9.959  24.716 1.00 20.23 ? 124 GLY   B N   1 
ATOM   1946 C  CA  . GLY   B 1 124 ? 7.287   10.593 25.268 1.00 20.39 ? 124 GLY   B CA  1 
ATOM   1947 C  C   . GLY   B 1 124 ? 7.636   11.335 26.558 1.00 19.30 ? 124 GLY   B C   1 
ATOM   1948 O  O   . GLY   B 1 124 ? 8.297   10.755 27.415 1.00 24.11 ? 124 GLY   B O   1 
ATOM   1949 N  N   . THR   B 1 125 ? 7.256   12.609 26.588 1.00 20.88 ? 125 THR   B N   1 
ATOM   1950 C  CA  . THR   B 1 125 ? 7.717   13.496 27.662 1.00 20.01 ? 125 THR   B CA  1 
ATOM   1951 C  C   . THR   B 1 125 ? 6.518   14.314 28.080 1.00 20.57 ? 125 THR   B C   1 
ATOM   1952 O  O   . THR   B 1 125 ? 5.550   14.415 27.329 1.00 23.71 ? 125 THR   B O   1 
ATOM   1953 C  CB  . THR   B 1 125 ? 8.854   14.399 27.130 1.00 21.33 ? 125 THR   B CB  1 
ATOM   1954 O  OG1 . THR   B 1 125 ? 8.416   15.066 25.932 1.00 20.10 ? 125 THR   B OG1 1 
ATOM   1955 C  CG2 . THR   B 1 125 ? 10.129  13.632 26.923 1.00 23.65 ? 125 THR   B CG2 1 
ATOM   1956 N  N   . TRP   B 1 126 ? 6.638   14.931 29.259 1.00 19.38 ? 126 TRP   B N   1 
ATOM   1957 C  CA  . TRP   B 1 126 ? 5.648   15.943 29.678 1.00 18.41 ? 126 TRP   B CA  1 
ATOM   1958 C  C   . TRP   B 1 126 ? 6.350   17.290 29.467 1.00 19.67 ? 126 TRP   B C   1 
ATOM   1959 O  O   . TRP   B 1 126 ? 7.567   17.372 29.661 1.00 21.48 ? 126 TRP   B O   1 
ATOM   1960 C  CB  . TRP   B 1 126 ? 5.101   15.731 31.097 1.00 21.12 ? 126 TRP   B CB  1 
ATOM   1961 C  CG  . TRP   B 1 126 ? 6.026   15.986 32.250 1.00 22.78 ? 126 TRP   B CG  1 
ATOM   1962 C  CD1 . TRP   B 1 126 ? 6.785   15.070 32.912 1.00 21.83 ? 126 TRP   B CD1 1 
ATOM   1963 C  CD2 . TRP   B 1 126 ? 6.221   17.242 32.931 1.00 23.11 ? 126 TRP   B CD2 1 
ATOM   1964 N  NE1 . TRP   B 1 126 ? 7.462   15.671 33.936 1.00 24.56 ? 126 TRP   B NE1 1 
ATOM   1965 C  CE2 . TRP   B 1 126 ? 7.135   16.999 33.976 1.00 24.93 ? 126 TRP   B CE2 1 
ATOM   1966 C  CE3 . TRP   B 1 126 ? 5.725   18.535 32.752 1.00 22.68 ? 126 TRP   B CE3 1 
ATOM   1967 C  CZ2 . TRP   B 1 126 ? 7.562   18.006 34.836 1.00 24.43 ? 126 TRP   B CZ2 1 
ATOM   1968 C  CZ3 . TRP   B 1 126 ? 6.144   19.526 33.607 1.00 27.23 ? 126 TRP   B CZ3 1 
ATOM   1969 C  CH2 . TRP   B 1 126 ? 7.046   19.264 34.635 1.00 23.20 ? 126 TRP   B CH2 1 
ATOM   1970 N  N   . ILE   B 1 127 ? 5.597   18.305 29.089 1.00 22.32 ? 127 ILE   B N   1 
ATOM   1971 C  CA  . ILE   B 1 127 ? 6.279   19.553 28.665 1.00 23.89 ? 127 ILE   B CA  1 
ATOM   1972 C  C   . ILE   B 1 127 ? 5.829   20.818 29.390 1.00 27.84 ? 127 ILE   B C   1 
ATOM   1973 O  O   . ILE   B 1 127 ? 4.757   20.817 30.010 1.00 28.95 ? 127 ILE   B O   1 
ATOM   1974 C  CB  . ILE   B 1 127 ? 6.080   19.748 27.150 1.00 24.78 ? 127 ILE   B CB  1 
ATOM   1975 C  CG1 . ILE   B 1 127 ? 4.634   20.108 26.833 1.00 31.37 ? 127 ILE   B CG1 1 
ATOM   1976 C  CG2 . ILE   B 1 127 ? 6.542   18.524 26.366 1.00 25.72 ? 127 ILE   B CG2 1 
ATOM   1977 C  CD1 . ILE   B 1 127 ? 4.408   20.558 25.406 1.00 34.11 ? 127 ILE   B CD1 1 
ATOM   1978 N  N   . GLU   B 1 128 ? 6.679   21.832 29.309 1.00 24.40 ? 128 GLU   B N   1 
ATOM   1979 C  CA  . GLU   B 1 128 ? 6.329   23.178 29.794 1.00 25.29 ? 128 GLU   B CA  1 
ATOM   1980 C  C   . GLU   B 1 128 ? 6.593   24.079 28.579 1.00 22.96 ? 128 GLU   B C   1 
ATOM   1981 O  O   . GLU   B 1 128 ? 7.605   23.868 27.914 1.00 23.09 ? 128 GLU   B O   1 
ATOM   1982 C  CB  . GLU   B 1 128 ? 7.140   23.590 31.016 1.00 29.03 ? 128 GLU   B CB  1 
ATOM   1983 C  CG  . GLU   B 1 128 ? 6.890   22.698 32.224 1.00 30.41 ? 128 GLU   B CG  1 
ATOM   1984 C  CD  . GLU   B 1 128 ? 7.859   23.014 33.340 1.00 29.87 ? 128 GLU   B CD  1 
ATOM   1985 O  OE1 . GLU   B 1 128 ? 9.025   22.603 33.242 1.00 28.41 ? 128 GLU   B OE1 1 
ATOM   1986 O  OE2 . GLU   B 1 128 ? 7.441   23.694 34.289 1.00 34.10 ? 128 GLU   B OE2 1 
ATOM   1987 N  N   . GLU   B 1 129 ? 5.674   24.987 28.294 1.00 23.90 ? 129 GLU   B N   1 
ATOM   1988 C  CA  . GLU   B 1 129 ? 5.787   25.873 27.118 1.00 26.31 ? 129 GLU   B CA  1 
ATOM   1989 C  C   . GLU   B 1 129 ? 5.707   27.345 27.521 1.00 29.24 ? 129 GLU   B C   1 
ATOM   1990 O  O   . GLU   B 1 129 ? 4.923   27.676 28.415 1.00 28.03 ? 129 GLU   B O   1 
ATOM   1991 C  CB  . GLU   B 1 129 ? 4.663   25.607 26.121 1.00 33.12 ? 129 GLU   B CB  1 
ATOM   1992 C  CG  . GLU   B 1 129 ? 4.729   24.239 25.456 1.00 35.83 ? 129 GLU   B CG  1 
ATOM   1993 C  CD  . GLU   B 1 129 ? 3.508   24.008 24.585 1.00 42.81 ? 129 GLU   B CD  1 
ATOM   1994 O  OE1 . GLU   B 1 129 ? 2.417   23.833 25.156 1.00 41.56 ? 129 GLU   B OE1 1 
ATOM   1995 O  OE2 . GLU   B 1 129 ? 3.649   23.999 23.351 1.00 40.67 ? 129 GLU   B OE2 1 
ATOM   1996 N  N   . PHE   B 1 130 ? 6.489   28.176 26.855 1.00 24.20 ? 130 PHE   B N   1 
ATOM   1997 C  CA  . PHE   B 1 130 ? 6.558   29.592 27.069 1.00 26.79 ? 130 PHE   B CA  1 
ATOM   1998 C  C   . PHE   B 1 130 ? 6.596   30.331 25.727 1.00 30.47 ? 130 PHE   B C   1 
ATOM   1999 O  O   . PHE   B 1 130 ? 7.388   29.976 24.866 1.00 29.71 ? 130 PHE   B O   1 
ATOM   2000 C  CB  . PHE   B 1 130 ? 7.842   29.874 27.832 1.00 26.02 ? 130 PHE   B CB  1 
ATOM   2001 C  CG  . PHE   B 1 130 ? 7.958   29.113 29.147 1.00 23.98 ? 130 PHE   B CG  1 
ATOM   2002 C  CD1 . PHE   B 1 130 ? 7.404   29.636 30.305 1.00 25.56 ? 130 PHE   B CD1 1 
ATOM   2003 C  CD2 . PHE   B 1 130 ? 8.634   27.895 29.212 1.00 24.01 ? 130 PHE   B CD2 1 
ATOM   2004 C  CE1 . PHE   B 1 130 ? 7.533   28.977 31.506 1.00 27.35 ? 130 PHE   B CE1 1 
ATOM   2005 C  CE2 . PHE   B 1 130 ? 8.752   27.242 30.435 1.00 25.18 ? 130 PHE   B CE2 1 
ATOM   2006 C  CZ  . PHE   B 1 130 ? 8.175   27.781 31.563 1.00 26.37 ? 130 PHE   B CZ  1 
ATOM   2007 N  N   . THR   B 1 131 ? 5.715   31.336 25.579 1.00 34.10 ? 131 THR   B N   1 
ATOM   2008 C  CA  . THR   B 1 131 ? 5.658   32.182 24.388 1.00 34.38 ? 131 THR   B CA  1 
ATOM   2009 C  C   . THR   B 1 131 ? 5.853   33.623 24.830 1.00 40.59 ? 131 THR   B C   1 
ATOM   2010 O  O   . THR   B 1 131 ? 5.710   33.956 26.013 1.00 42.55 ? 131 THR   B O   1 
ATOM   2011 C  CB  . THR   B 1 131 ? 4.351   31.991 23.624 1.00 40.64 ? 131 THR   B CB  1 
ATOM   2012 O  OG1 . THR   B 1 131 ? 3.430   32.493 24.582 1.00 43.11 ? 131 THR   B OG1 1 
ATOM   2013 C  CG2 . THR   B 1 131 ? 4.020   30.551 23.294 1.00 38.67 ? 131 THR   B CG2 1 
ATOM   2014 N  N   . PHE   B 1 132 ? 6.357   34.427 23.893 1.00 44.82 ? 132 PHE   B N   1 
ATOM   2015 C  CA  . PHE   B 1 132 ? 6.750   35.800 24.145 1.00 49.62 ? 132 PHE   B CA  1 
ATOM   2016 C  C   . PHE   B 1 132 ? 6.227   36.649 22.965 1.00 52.20 ? 132 PHE   B C   1 
ATOM   2017 O  O   . PHE   B 1 132 ? 5.606   37.636 23.339 1.00 53.93 ? 132 PHE   B O   1 
ATOM   2018 C  CB  . PHE   B 1 132 ? 8.275   35.927 24.255 1.00 47.65 ? 132 PHE   B CB  1 
ATOM   2019 C  CG  . PHE   B 1 132 ? 8.978   34.871 25.096 1.00 35.43 ? 132 PHE   B CG  1 
ATOM   2020 C  CD1 . PHE   B 1 132 ? 9.283   33.639 24.556 1.00 31.17 ? 132 PHE   B CD1 1 
ATOM   2021 C  CD2 . PHE   B 1 132 ? 9.303   35.108 26.421 1.00 40.96 ? 132 PHE   B CD2 1 
ATOM   2022 C  CE1 . PHE   B 1 132 ? 9.913   32.661 25.317 1.00 33.31 ? 132 PHE   B CE1 1 
ATOM   2023 C  CE2 . PHE   B 1 132 ? 9.929   34.132 27.182 1.00 39.16 ? 132 PHE   B CE2 1 
ATOM   2024 C  CZ  . PHE   B 1 132 ? 10.228  32.907 26.633 1.00 33.94 ? 132 PHE   B CZ  1 
HETATM 2025 S  S   . SO4   C 2 .   ? 22.043  17.361 43.819 1.00 48.57 ? 201 SO4   A S   1 
HETATM 2026 O  O1  . SO4   C 2 .   ? 23.217  18.122 43.359 1.00 39.45 ? 201 SO4   A O1  1 
HETATM 2027 O  O2  . SO4   C 2 .   ? 21.977  17.306 45.262 1.00 54.01 ? 201 SO4   A O2  1 
HETATM 2028 O  O3  . SO4   C 2 .   ? 20.780  18.012 43.325 1.00 37.87 ? 201 SO4   A O3  1 
HETATM 2029 O  O4  . SO4   C 2 .   ? 22.139  16.012 43.300 1.00 49.96 ? 201 SO4   A O4  1 
HETATM 2030 S  S   . SO4   D 2 .   ? 16.315  8.682  41.216 1.00 84.05 ? 202 SO4   A S   1 
HETATM 2031 O  O1  . SO4   D 2 .   ? 14.982  9.209  41.360 1.00 74.17 ? 202 SO4   A O1  1 
HETATM 2032 O  O2  . SO4   D 2 .   ? 17.000  8.779  42.494 1.00 79.46 ? 202 SO4   A O2  1 
HETATM 2033 O  O3  . SO4   D 2 .   ? 16.246  7.306  40.786 1.00 93.50 ? 202 SO4   A O3  1 
HETATM 2034 O  O4  . SO4   D 2 .   ? 17.032  9.421  40.217 1.00 74.91 ? 202 SO4   A O4  1 
HETATM 2035 C  C1  . GOL   E 3 .   ? 5.797   31.013 16.276 1.00 20.00 ? 203 GOL   A C1  1 
HETATM 2036 O  O1  . GOL   E 3 .   ? 4.990   30.751 15.134 1.00 20.00 ? 203 GOL   A O1  1 
HETATM 2037 C  C2  . GOL   E 3 .   ? 5.539   30.009 17.377 1.00 20.00 ? 203 GOL   A C2  1 
HETATM 2038 O  O2  . GOL   E 3 .   ? 6.771   29.408 17.764 1.00 20.00 ? 203 GOL   A O2  1 
HETATM 2039 C  C3  . GOL   E 3 .   ? 4.841   30.599 18.584 1.00 20.00 ? 203 GOL   A C3  1 
HETATM 2040 O  O3  . GOL   E 3 .   ? 5.603   30.432 19.774 1.00 20.00 ? 203 GOL   A O3  1 
HETATM 2041 H  H11 . GOL   E 3 .   ? 5.606   31.921 16.610 1.00 20.00 ? 203 GOL   A H11 1 
HETATM 2042 H  H12 . GOL   E 3 .   ? 6.748   30.970 16.019 1.00 20.00 ? 203 GOL   A H12 1 
HETATM 2043 H  HO1 . GOL   E 3 .   ? 5.096   29.942 14.916 1.00 20.00 ? 203 GOL   A HO1 1 
HETATM 2044 H  H2  . GOL   E 3 .   ? 4.958   29.308 17.008 1.00 20.00 ? 203 GOL   A H2  1 
HETATM 2045 H  HO2 . GOL   E 3 .   ? 7.115   29.879 18.375 1.00 20.00 ? 203 GOL   A HO2 1 
HETATM 2046 H  H31 . GOL   E 3 .   ? 4.683   31.561 18.431 1.00 20.00 ? 203 GOL   A H31 1 
HETATM 2047 H  H32 . GOL   E 3 .   ? 3.965   30.157 18.698 1.00 20.00 ? 203 GOL   A H32 1 
HETATM 2048 H  HO3 . GOL   E 3 .   ? 6.132   31.087 19.857 1.00 20.00 ? 203 GOL   A HO3 1 
HETATM 2049 C  C2  . A1D9Q F 4 .   ? 23.476  22.966 28.214 1.00 44.37 ? 204 A1D9Q A C2  1 
HETATM 2050 C  C4  . A1D9Q F 4 .   ? 23.655  25.206 27.342 1.00 52.21 ? 204 A1D9Q A C4  1 
HETATM 2051 C  C5  . A1D9Q F 4 .   ? 24.775  24.841 26.681 1.00 53.79 ? 204 A1D9Q A C5  1 
HETATM 2052 C  C6  . A1D9Q F 4 .   ? 24.684  27.075 26.284 1.00 57.25 ? 204 A1D9Q A C6  1 
HETATM 2053 N  N1  . A1D9Q F 4 .   ? 25.283  25.909 25.967 1.00 55.81 ? 204 A1D9Q A N1  1 
HETATM 2054 C  C1  . A1D9Q F 4 .   ? 22.755  21.952 29.065 1.00 44.82 ? 204 A1D9Q A C1  1 
HETATM 2055 C  C3  . A1D9Q F 4 .   ? 23.000  24.270 28.112 1.00 46.06 ? 204 A1D9Q A C3  1 
HETATM 2056 O  O1  . A1D9Q F 4 .   ? 25.110  28.220 26.059 1.00 48.10 ? 204 A1D9Q A O1  1 
HETATM 2057 C  C7  . A1D9Q F 4 .   ? 23.417  26.670 27.069 1.00 52.25 ? 204 A1D9Q A C7  1 
HETATM 2058 C  C8  . A1D9Q F 4 .   ? 22.879  27.726 27.998 1.00 53.13 ? 204 A1D9Q A C8  1 
HETATM 2059 C  C9  . A1D9Q F 4 .   ? 22.054  27.276 26.857 1.00 55.59 ? 204 A1D9Q A C9  1 
HETATM 2060 CL CL1 . A1D9Q F 4 .   ? 20.534  26.472 27.221 1.00 72.90 ? 204 A1D9Q A CL1 1 
HETATM 2061 CL CL2 . A1D9Q F 4 .   ? 21.853  28.348 25.476 1.00 58.14 ? 204 A1D9Q A CL2 1 
HETATM 2062 C  C10 . A1D9Q F 4 .   ? 25.277  23.557 26.752 1.00 49.79 ? 204 A1D9Q A C10 1 
HETATM 2063 C  C11 . A1D9Q F 4 .   ? 24.625  22.613 27.526 1.00 50.35 ? 204 A1D9Q A C11 1 
HETATM 2064 C  C1  . GOL   G 3 .   ? 12.306  -0.647 13.974 1.00 54.40 ? 205 GOL   A C1  1 
HETATM 2065 O  O1  . GOL   G 3 .   ? 12.916  -1.540 14.904 1.00 63.72 ? 205 GOL   A O1  1 
HETATM 2066 C  C2  . GOL   G 3 .   ? 10.829  -0.952 13.751 1.00 41.50 ? 205 GOL   A C2  1 
HETATM 2067 O  O2  . GOL   G 3 .   ? 10.169  -1.526 14.897 1.00 50.84 ? 205 GOL   A O2  1 
HETATM 2068 C  C3  . GOL   G 3 .   ? 10.623  -1.783 12.526 1.00 37.13 ? 205 GOL   A C3  1 
HETATM 2069 O  O3  . GOL   G 3 .   ? 11.067  -3.137 12.571 1.00 32.82 ? 205 GOL   A O3  1 
HETATM 2070 C  C1  . GOL   H 3 .   ? 32.198  19.675 27.649 1.00 38.27 ? 201 GOL   B C1  1 
HETATM 2071 O  O1  . GOL   H 3 .   ? 33.557  19.260 27.546 1.00 34.15 ? 201 GOL   B O1  1 
HETATM 2072 C  C2  . GOL   H 3 .   ? 31.336  19.539 26.436 1.00 36.82 ? 201 GOL   B C2  1 
HETATM 2073 O  O2  . GOL   H 3 .   ? 31.940  20.125 25.263 1.00 51.25 ? 201 GOL   B O2  1 
HETATM 2074 C  C3  . GOL   H 3 .   ? 30.888  18.094 26.239 1.00 51.56 ? 201 GOL   B C3  1 
HETATM 2075 O  O3  . GOL   H 3 .   ? 31.547  17.455 25.148 1.00 60.11 ? 201 GOL   B O3  1 
HETATM 2076 S  S   . SO4   I 2 .   ? 12.995  8.286  -3.687 1.00 49.17 ? 202 SO4   B S   1 
HETATM 2077 O  O1  . SO4   I 2 .   ? 14.346  8.240  -3.182 1.00 51.06 ? 202 SO4   B O1  1 
HETATM 2078 O  O2  . SO4   I 2 .   ? 12.330  9.561  -3.225 1.00 39.01 ? 202 SO4   B O2  1 
HETATM 2079 O  O3  . SO4   I 2 .   ? 13.029  8.284  -5.131 1.00 55.29 ? 202 SO4   B O3  1 
HETATM 2080 O  O4  . SO4   I 2 .   ? 12.270  7.104  -3.189 1.00 39.94 ? 202 SO4   B O4  1 
HETATM 2081 S  S   . SO4   J 2 .   ? 21.640  13.954 -1.025 1.00 82.81 ? 203 SO4   B S   1 
HETATM 2082 O  O1  . SO4   J 2 .   ? 21.092  15.276 -1.213 1.00 76.48 ? 203 SO4   B O1  1 
HETATM 2083 O  O2  . SO4   J 2 .   ? 21.586  13.234 -2.287 1.00 78.29 ? 203 SO4   B O2  1 
HETATM 2084 O  O3  . SO4   J 2 .   ? 23.006  14.057 -0.579 1.00 98.07 ? 203 SO4   B O3  1 
HETATM 2085 O  O4  . SO4   J 2 .   ? 20.896  13.248 -0.018 1.00 79.57 ? 203 SO4   B O4  1 
HETATM 2086 C  C1  . GOL   K 3 .   ? -0.704  24.579 23.889 1.00 20.00 ? 204 GOL   B C1  1 
HETATM 2087 O  O1  . GOL   K 3 .   ? -0.428  25.339 25.061 1.00 20.00 ? 204 GOL   B O1  1 
HETATM 2088 C  C2  . GOL   K 3 .   ? 0.313   24.846 22.802 1.00 20.00 ? 204 GOL   B C2  1 
HETATM 2089 O  O2  . GOL   K 3 .   ? 0.918   23.615 22.415 1.00 20.00 ? 204 GOL   B O2  1 
HETATM 2090 C  C3  . GOL   K 3 .   ? -0.261  25.545 21.588 1.00 20.00 ? 204 GOL   B C3  1 
HETATM 2091 O  O3  . GOL   K 3 .   ? -0.025  24.807 20.394 1.00 20.00 ? 204 GOL   B O3  1 
HETATM 2092 H  H11 . GOL   K 3 .   ? -1.605  24.807 23.558 1.00 20.00 ? 204 GOL   B H11 1 
HETATM 2093 H  H12 . GOL   K 3 .   ? -0.690  23.619 24.114 1.00 20.00 ? 204 GOL   B H12 1 
HETATM 2094 H  HO1 . GOL   K 3 .   ? 0.363   25.168 25.304 1.00 20.00 ? 204 GOL   B HO1 1 
HETATM 2095 H  H2  . GOL   K 3 .   ? 1.010   25.427 23.181 1.00 20.00 ? 204 GOL   B H2  1 
HETATM 2096 H  HO2 . GOL   K 3 .   ? 0.474   23.299 21.768 1.00 20.00 ? 204 GOL   B HO2 1 
HETATM 2097 H  H31 . GOL   K 3 .   ? 0.151   26.438 21.504 1.00 20.00 ? 204 GOL   B H31 1 
HETATM 2098 H  H32 . GOL   K 3 .   ? -1.233  25.663 21.710 1.00 20.00 ? 204 GOL   B H32 1 
HETATM 2099 H  HO3 . GOL   K 3 .   ? -0.512  25.119 19.779 1.00 20.00 ? 204 GOL   B HO3 1 
HETATM 2100 C  C2  . A1D9Q L 4 .   ? 7.411   6.801  11.961 1.00 45.40 ? 205 A1D9Q B C2  1 
HETATM 2101 C  C4  . A1D9Q L 4 .   ? 5.162   6.678  12.820 1.00 51.60 ? 205 A1D9Q B C4  1 
HETATM 2102 C  C5  . A1D9Q L 4 .   ? 5.502   5.563  13.503 1.00 52.13 ? 205 A1D9Q B C5  1 
HETATM 2103 C  C6  . A1D9Q L 4 .   ? 3.263   5.688  13.857 1.00 57.92 ? 205 A1D9Q B C6  1 
HETATM 2104 N  N1  . A1D9Q L 4 .   ? 4.418   5.091  14.218 1.00 55.23 ? 205 A1D9Q B N1  1 
HETATM 2105 C  C1  . A1D9Q L 4 .   ? 8.442   7.491  11.104 1.00 44.45 ? 205 A1D9Q B C1  1 
HETATM 2106 C  C3  . A1D9Q L 4 .   ? 6.114   7.301  12.045 1.00 47.42 ? 205 A1D9Q B C3  1 
HETATM 2107 O  O1  . A1D9Q L 4 .   ? 2.108   5.269  14.045 1.00 45.77 ? 205 A1D9Q B O1  1 
HETATM 2108 C  C7  . A1D9Q L 4 .   ? 3.701   6.946  13.077 1.00 52.55 ? 205 A1D9Q B C7  1 
HETATM 2109 C  C8  . A1D9Q L 4 .   ? 2.670   7.513  12.136 1.00 52.07 ? 205 A1D9Q B C8  1 
HETATM 2110 C  C9  . A1D9Q L 4 .   ? 3.122   8.320  13.288 1.00 54.27 ? 205 A1D9Q B C9  1 
HETATM 2111 CL CL1 . A1D9Q L 4 .   ? 3.976   9.818  12.950 1.00 73.28 ? 205 A1D9Q B CL1 1 
HETATM 2112 CL CL2 . A1D9Q L 4 .   ? 2.031   8.539  14.652 1.00 57.05 ? 205 A1D9Q B CL2 1 
HETATM 2113 C  C10 . A1D9Q L 4 .   ? 6.778   5.037  13.450 1.00 51.72 ? 205 A1D9Q B C10 1 
HETATM 2114 C  C11 . A1D9Q L 4 .   ? 7.739   5.659  12.671 1.00 50.77 ? 205 A1D9Q B C11 1 
HETATM 2115 O  O   . HOH   M 5 .   ? 22.483  17.702 47.475 1.00 44.16 ? 301 HOH   A O   1 
HETATM 2116 O  O   . HOH   M 5 .   ? 19.140  19.485 44.258 1.00 33.83 ? 302 HOH   A O   1 
HETATM 2117 O  O   . HOH   M 5 .   ? 29.272  41.694 35.384 1.00 30.52 ? 303 HOH   A O   1 
HETATM 2118 O  O   . HOH   M 5 .   ? 13.635  11.133 42.186 1.00 28.95 ? 304 HOH   A O   1 
HETATM 2119 O  O   . HOH   M 5 .   ? 9.017   9.513  29.754 1.00 21.91 ? 305 HOH   A O   1 
HETATM 2120 O  O   . HOH   M 5 .   ? 13.324  17.796 44.726 1.00 27.70 ? 306 HOH   A O   1 
HETATM 2121 O  O   . HOH   M 5 .   ? 17.742  9.378  34.533 1.00 52.51 ? 307 HOH   A O   1 
HETATM 2122 O  O   . HOH   M 5 .   ? -0.686  14.455 31.163 1.00 42.39 ? 308 HOH   A O   1 
HETATM 2123 O  O   . HOH   M 5 .   ? 14.850  26.650 31.525 1.00 30.20 ? 309 HOH   A O   1 
HETATM 2124 O  O   . HOH   M 5 .   ? 6.646   5.885  36.564 1.00 38.23 ? 310 HOH   A O   1 
HETATM 2125 O  O   . HOH   M 5 .   ? 23.187  11.142 34.925 1.00 29.95 ? 311 HOH   A O   1 
HETATM 2126 O  O   . HOH   M 5 .   ? 11.565  1.808  16.134 1.00 46.87 ? 312 HOH   A O   1 
HETATM 2127 O  O   . HOH   M 5 .   ? 11.074  37.030 22.881 1.00 37.59 ? 313 HOH   A O   1 
HETATM 2128 O  O   . HOH   M 5 .   ? 22.852  14.355 27.151 1.00 23.62 ? 314 HOH   A O   1 
HETATM 2129 O  O   . HOH   M 5 .   ? 12.274  10.235 26.953 1.00 29.47 ? 315 HOH   A O   1 
HETATM 2130 O  O   . HOH   M 5 .   ? 15.096  43.270 23.652 1.00 42.82 ? 316 HOH   A O   1 
HETATM 2131 O  O   . HOH   M 5 .   ? 28.146  26.325 38.963 1.00 23.57 ? 317 HOH   A O   1 
HETATM 2132 O  O   . HOH   M 5 .   ? 20.698  40.528 29.832 1.00 29.60 ? 318 HOH   A O   1 
HETATM 2133 O  O   . HOH   M 5 .   ? 14.609  12.205 34.376 1.00 23.12 ? 319 HOH   A O   1 
HETATM 2134 O  O   . HOH   M 5 .   ? 2.575   2.087  30.233 1.00 31.44 ? 320 HOH   A O   1 
HETATM 2135 O  O   . HOH   M 5 .   ? 16.846  8.927  31.633 1.00 54.36 ? 321 HOH   A O   1 
HETATM 2136 O  O   . HOH   M 5 .   ? 7.046   14.782 37.504 1.00 29.41 ? 322 HOH   A O   1 
HETATM 2137 O  O   . HOH   M 5 .   ? 11.816  35.182 35.691 1.00 28.15 ? 323 HOH   A O   1 
HETATM 2138 O  O   . HOH   M 5 .   ? 10.736  38.099 31.813 1.00 42.50 ? 324 HOH   A O   1 
HETATM 2139 O  O   . HOH   M 5 .   ? 27.816  19.368 27.765 1.00 34.25 ? 325 HOH   A O   1 
HETATM 2140 O  O   . HOH   M 5 .   ? 16.667  3.706  25.683 1.00 50.59 ? 326 HOH   A O   1 
HETATM 2141 O  O   . HOH   M 5 .   ? 27.121  15.029 40.393 1.00 42.69 ? 327 HOH   A O   1 
HETATM 2142 O  O   . HOH   M 5 .   ? 26.289  39.129 23.785 1.00 30.40 ? 328 HOH   A O   1 
HETATM 2143 O  O   . HOH   M 5 .   ? 9.685   28.963 40.182 1.00 21.27 ? 329 HOH   A O   1 
HETATM 2144 O  O   . HOH   M 5 .   ? 25.774  44.378 34.068 1.00 49.50 ? 330 HOH   A O   1 
HETATM 2145 O  O   . HOH   M 5 .   ? 13.235  33.576 10.559 1.00 47.54 ? 331 HOH   A O   1 
HETATM 2146 O  O   . HOH   M 5 .   ? 19.124  8.385  24.461 1.00 42.23 ? 332 HOH   A O   1 
HETATM 2147 O  O   . HOH   M 5 .   ? 9.659   25.828 21.681 1.00 34.29 ? 333 HOH   A O   1 
HETATM 2148 O  O   . HOH   M 5 .   ? 30.359  31.789 35.365 1.00 19.25 ? 334 HOH   A O   1 
HETATM 2149 O  O   . HOH   M 5 .   ? 8.924   28.335 10.177 1.00 33.86 ? 335 HOH   A O   1 
HETATM 2150 O  O   . HOH   M 5 .   ? -4.445  23.941 18.814 1.00 44.35 ? 336 HOH   A O   1 
HETATM 2151 O  O   . HOH   M 5 .   ? 17.558  39.177 19.026 1.00 47.49 ? 337 HOH   A O   1 
HETATM 2152 O  O   . HOH   M 5 .   ? 16.640  21.412 16.617 1.00 27.44 ? 338 HOH   A O   1 
HETATM 2153 O  O   . HOH   M 5 .   ? 25.573  10.832 33.743 1.00 29.50 ? 339 HOH   A O   1 
HETATM 2154 O  O   . HOH   M 5 .   ? 16.582  20.534 43.067 1.00 26.31 ? 340 HOH   A O   1 
HETATM 2155 O  O   . HOH   M 5 .   ? 19.735  14.610 44.263 1.00 27.67 ? 341 HOH   A O   1 
HETATM 2156 O  O   . HOH   M 5 .   ? 13.838  40.578 29.632 1.00 28.47 ? 342 HOH   A O   1 
HETATM 2157 O  O   . HOH   M 5 .   ? 27.427  32.722 39.324 1.00 28.82 ? 343 HOH   A O   1 
HETATM 2158 O  O   . HOH   M 5 .   ? 10.548  14.431 38.295 1.00 25.50 ? 344 HOH   A O   1 
HETATM 2159 O  O   . HOH   M 5 .   ? 22.287  20.615 42.296 1.00 20.18 ? 345 HOH   A O   1 
HETATM 2160 O  O   . HOH   M 5 .   ? 8.822   26.268 34.646 1.00 24.34 ? 346 HOH   A O   1 
HETATM 2161 O  O   . HOH   M 5 .   ? 27.210  18.923 36.920 1.00 27.36 ? 347 HOH   A O   1 
HETATM 2162 O  O   . HOH   M 5 .   ? 5.493   19.903 7.584  1.00 29.70 ? 348 HOH   A O   1 
HETATM 2163 O  O   . HOH   M 5 .   ? 22.749  43.817 27.522 1.00 49.39 ? 349 HOH   A O   1 
HETATM 2164 O  O   . HOH   M 5 .   ? 19.096  24.475 43.184 1.00 33.47 ? 350 HOH   A O   1 
HETATM 2165 O  O   . HOH   M 5 .   ? 27.839  23.985 40.504 1.00 28.43 ? 351 HOH   A O   1 
HETATM 2166 O  O   . HOH   M 5 .   ? 28.822  18.153 34.906 1.00 27.35 ? 352 HOH   A O   1 
HETATM 2167 O  O   . HOH   M 5 .   ? 23.817  17.033 29.689 1.00 21.38 ? 353 HOH   A O   1 
HETATM 2168 O  O   . HOH   M 5 .   ? 29.352  15.389 35.183 1.00 34.09 ? 354 HOH   A O   1 
HETATM 2169 O  O   . HOH   M 5 .   ? 20.416  10.765 28.933 1.00 39.39 ? 355 HOH   A O   1 
HETATM 2170 O  O   . HOH   M 5 .   ? 13.168  24.981 32.531 1.00 27.40 ? 356 HOH   A O   1 
HETATM 2171 O  O   . HOH   M 5 .   ? 18.404  5.586  22.424 1.00 48.68 ? 357 HOH   A O   1 
HETATM 2172 O  O   . HOH   M 5 .   ? 6.877   -3.180 24.449 1.00 42.10 ? 358 HOH   A O   1 
HETATM 2173 O  O   . HOH   M 5 .   ? 5.023   1.784  19.237 1.00 28.83 ? 359 HOH   A O   1 
HETATM 2174 O  O   . HOH   M 5 .   ? 18.034  38.554 33.244 1.00 26.01 ? 360 HOH   A O   1 
HETATM 2175 O  O   . HOH   M 5 .   ? 15.175  13.277 45.813 1.00 39.00 ? 361 HOH   A O   1 
HETATM 2176 O  O   . HOH   M 5 .   ? 5.329   27.106 10.284 1.00 34.62 ? 362 HOH   A O   1 
HETATM 2177 O  O   . HOH   M 5 .   ? 18.814  42.249 33.293 1.00 42.56 ? 363 HOH   A O   1 
HETATM 2178 O  O   . HOH   M 5 .   ? 9.294   4.742  29.333 1.00 28.43 ? 364 HOH   A O   1 
HETATM 2179 O  O   . HOH   M 5 .   ? 31.064  37.246 25.878 1.00 36.55 ? 365 HOH   A O   1 
HETATM 2180 O  O   . HOH   M 5 .   ? 11.330  7.193  36.917 1.00 44.10 ? 366 HOH   A O   1 
HETATM 2181 O  O   . HOH   M 5 .   ? 13.392  14.507 27.881 1.00 34.97 ? 367 HOH   A O   1 
HETATM 2182 O  O   . HOH   M 5 .   ? 19.867  9.752  31.402 1.00 47.29 ? 368 HOH   A O   1 
HETATM 2183 O  O   . HOH   M 5 .   ? 11.012  38.057 18.406 1.00 49.66 ? 369 HOH   A O   1 
HETATM 2184 O  O   . HOH   M 5 .   ? 13.523  6.963  28.859 1.00 33.58 ? 370 HOH   A O   1 
HETATM 2185 O  O   . HOH   M 5 .   ? 17.673  32.811 9.810  1.00 35.50 ? 371 HOH   A O   1 
HETATM 2186 O  O   . HOH   M 5 .   ? 20.590  9.908  33.758 1.00 39.31 ? 372 HOH   A O   1 
HETATM 2187 O  O   . HOH   M 5 .   ? 4.458   25.113 6.531  1.00 50.92 ? 373 HOH   A O   1 
HETATM 2188 O  O   . HOH   M 5 .   ? 10.082  39.300 23.323 1.00 49.43 ? 374 HOH   A O   1 
HETATM 2189 O  O   . HOH   M 5 .   ? 6.691   28.639 11.886 1.00 44.58 ? 375 HOH   A O   1 
HETATM 2190 O  O   . HOH   M 5 .   ? 13.719  12.514 26.126 1.00 26.01 ? 376 HOH   A O   1 
HETATM 2191 O  O   . HOH   M 5 .   ? 16.338  23.307 42.946 1.00 28.56 ? 377 HOH   A O   1 
HETATM 2192 O  O   . HOH   M 5 .   ? 28.306  32.295 13.700 1.00 48.62 ? 378 HOH   A O   1 
HETATM 2193 O  O   . HOH   M 5 .   ? 6.727   2.843  32.628 1.00 50.53 ? 379 HOH   A O   1 
HETATM 2194 O  O   . HOH   M 5 .   ? 19.784  44.518 31.388 1.00 57.43 ? 380 HOH   A O   1 
HETATM 2195 O  O   . HOH   M 5 .   ? 8.082   28.237 38.146 1.00 35.28 ? 381 HOH   A O   1 
HETATM 2196 O  O   . HOH   M 5 .   ? 9.143   1.880  13.888 1.00 52.68 ? 382 HOH   A O   1 
HETATM 2197 O  O   . HOH   M 5 .   ? 9.842   3.389  27.364 1.00 36.68 ? 383 HOH   A O   1 
HETATM 2198 O  O   . HOH   M 5 .   ? 18.063  39.502 30.500 1.00 30.94 ? 384 HOH   A O   1 
HETATM 2199 O  O   . HOH   M 5 .   ? 16.278  20.326 46.066 1.00 33.22 ? 385 HOH   A O   1 
HETATM 2200 O  O   . HOH   M 5 .   ? 12.992  42.163 27.729 1.00 37.80 ? 386 HOH   A O   1 
HETATM 2201 O  O   . HOH   M 5 .   ? 20.008  12.331 45.661 1.00 51.38 ? 387 HOH   A O   1 
HETATM 2202 O  O   . HOH   M 5 .   ? 13.625  20.252 45.595 1.00 46.20 ? 388 HOH   A O   1 
HETATM 2203 O  O   . HOH   M 5 .   ? 28.513  16.595 38.862 1.00 43.30 ? 389 HOH   A O   1 
HETATM 2204 O  O   . HOH   M 5 .   ? 16.302  41.558 30.723 1.00 36.62 ? 390 HOH   A O   1 
HETATM 2205 O  O   . HOH   M 5 .   ? 6.179   31.353 11.236 1.00 50.03 ? 391 HOH   A O   1 
HETATM 2206 O  O   . HOH   M 5 .   ? 29.965  32.921 37.771 1.00 28.25 ? 392 HOH   A O   1 
HETATM 2207 O  O   . HOH   M 5 .   ? 10.620  23.704 46.159 1.00 38.74 ? 393 HOH   A O   1 
HETATM 2208 O  O   . HOH   M 5 .   ? 12.618  3.204  28.044 1.00 46.35 ? 394 HOH   A O   1 
HETATM 2209 O  O   . HOH   M 5 .   ? 20.992  9.281  26.415 1.00 49.22 ? 395 HOH   A O   1 
HETATM 2210 O  O   . HOH   M 5 .   ? 12.019  40.289 31.802 1.00 37.23 ? 396 HOH   A O   1 
HETATM 2211 O  O   . HOH   M 5 .   ? 4.520   1.297  32.164 1.00 49.13 ? 397 HOH   A O   1 
HETATM 2212 O  O   . HOH   M 5 .   ? 9.524   33.804 35.970 1.00 38.84 ? 398 HOH   A O   1 
HETATM 2213 O  O   . HOH   M 5 .   ? 8.406   27.998 42.237 1.00 32.51 ? 399 HOH   A O   1 
HETATM 2214 O  O   . HOH   N 5 .   ? 12.712  7.712  -7.287 1.00 44.57 ? 301 HOH   B O   1 
HETATM 2215 O  O   . HOH   N 5 .   ? -11.333 1.109  4.751  1.00 32.05 ? 302 HOH   B O   1 
HETATM 2216 O  O   . HOH   N 5 .   ? 10.810  11.243 -4.192 1.00 34.90 ? 303 HOH   B O   1 
HETATM 2217 O  O   . HOH   N 5 .   ? 15.922  30.970 8.934  1.00 42.57 ? 304 HOH   B O   1 
HETATM 2218 O  O   . HOH   N 5 .   ? 15.348  13.023 -7.449 1.00 47.55 ? 305 HOH   B O   1 
HETATM 2219 O  O   . HOH   N 5 .   ? 19.199  16.721 -2.102 1.00 30.03 ? 306 HOH   B O   1 
HETATM 2220 O  O   . HOH   N 5 .   ? 12.545  17.057 -4.571 1.00 28.34 ? 307 HOH   B O   1 
HETATM 2221 O  O   . HOH   N 5 .   ? 19.195  7.181  5.213  1.00 29.64 ? 308 HOH   B O   1 
HETATM 2222 O  O   . HOH   N 5 .   ? 3.679   15.448 8.597  1.00 29.21 ? 309 HOH   B O   1 
HETATM 2223 O  O   . HOH   N 5 .   ? 15.983  7.502  12.995 1.00 25.52 ? 310 HOH   B O   1 
HETATM 2224 O  O   . HOH   N 5 .   ? -6.670  19.239 17.208 1.00 38.00 ? 311 HOH   B O   1 
HETATM 2225 O  O   . HOH   N 5 .   ? 4.046   2.204  1.165  1.00 23.55 ? 312 HOH   B O   1 
HETATM 2226 O  O   . HOH   N 5 .   ? -4.823  18.492 4.414  1.00 28.11 ? 313 HOH   B O   1 
HETATM 2227 O  O   . HOH   N 5 .   ? 20.089  18.113 13.146 1.00 27.41 ? 314 HOH   B O   1 
HETATM 2228 O  O   . HOH   N 5 .   ? 15.595  23.292 2.608  1.00 29.76 ? 315 HOH   B O   1 
HETATM 2229 O  O   . HOH   N 5 .   ? -10.177 9.663  10.277 1.00 29.71 ? 316 HOH   B O   1 
HETATM 2230 O  O   . HOH   N 5 .   ? 15.989  -0.148 14.965 1.00 55.00 ? 317 HOH   B O   1 
HETATM 2231 O  O   . HOH   N 5 .   ? 24.491  23.675 3.555  1.00 37.98 ? 318 HOH   B O   1 
HETATM 2232 O  O   . HOH   N 5 .   ? -12.955 15.182 16.472 1.00 42.57 ? 319 HOH   B O   1 
HETATM 2233 O  O   . HOH   N 5 .   ? 28.280  27.738 9.862  1.00 32.88 ? 320 HOH   B O   1 
HETATM 2234 O  O   . HOH   N 5 .   ? 18.155  15.722 5.738  1.00 22.45 ? 321 HOH   B O   1 
HETATM 2235 O  O   . HOH   N 5 .   ? -4.849  16.259 22.897 1.00 40.34 ? 322 HOH   B O   1 
HETATM 2236 O  O   . HOH   N 5 .   ? 10.965  2.468  12.380 1.00 33.95 ? 323 HOH   B O   1 
HETATM 2237 O  O   . HOH   N 5 .   ? 13.287  17.071 20.109 1.00 39.66 ? 324 HOH   B O   1 
HETATM 2238 O  O   . HOH   N 5 .   ? 1.381   20.663 -0.082 1.00 21.68 ? 325 HOH   B O   1 
HETATM 2239 O  O   . HOH   N 5 .   ? -13.496 7.616  12.556 1.00 48.02 ? 326 HOH   B O   1 
HETATM 2240 O  O   . HOH   N 5 .   ? 26.525  13.825 14.271 1.00 50.15 ? 327 HOH   B O   1 
HETATM 2241 O  O   . HOH   N 5 .   ? -3.107  17.109 29.627 1.00 51.42 ? 328 HOH   B O   1 
HETATM 2242 O  O   . HOH   N 5 .   ? 17.017  15.122 -5.683 1.00 38.55 ? 329 HOH   B O   1 
HETATM 2243 O  O   . HOH   N 5 .   ? -10.216 16.483 10.479 1.00 28.20 ? 330 HOH   B O   1 
HETATM 2244 O  O   . HOH   N 5 .   ? 4.536   20.675 18.456 1.00 35.05 ? 331 HOH   B O   1 
HETATM 2245 O  O   . HOH   N 5 .   ? 9.841   13.780 -2.919 1.00 25.46 ? 332 HOH   B O   1 
HETATM 2246 O  O   . HOH   N 5 .   ? -1.436  0.005  4.745  1.00 18.71 ? 333 HOH   B O   1 
HETATM 2247 O  O   . HOH   N 5 .   ? 15.289  3.193  -0.288 1.00 40.49 ? 334 HOH   B O   1 
HETATM 2248 O  O   . HOH   N 5 .   ? -2.396  2.916  0.806  1.00 28.28 ? 335 HOH   B O   1 
HETATM 2249 O  O   . HOH   N 5 .   ? -8.405  10.844 24.203 1.00 55.49 ? 336 HOH   B O   1 
HETATM 2250 O  O   . HOH   N 5 .   ? 8.927   13.710 23.535 1.00 27.43 ? 337 HOH   B O   1 
HETATM 2251 O  O   . HOH   N 5 .   ? 10.457  24.849 32.576 1.00 29.86 ? 338 HOH   B O   1 
HETATM 2252 O  O   . HOH   N 5 .   ? 4.067   21.528 5.491  1.00 23.67 ? 339 HOH   B O   1 
HETATM 2253 O  O   . HOH   N 5 .   ? 19.531  4.774  6.385  1.00 29.46 ? 340 HOH   B O   1 
HETATM 2254 O  O   . HOH   N 5 .   ? 22.008  11.245 15.712 1.00 41.47 ? 341 HOH   B O   1 
HETATM 2255 O  O   . HOH   N 5 .   ? 15.766  10.636 -4.113 1.00 28.52 ? 342 HOH   B O   1 
HETATM 2256 O  O   . HOH   N 5 .   ? -8.775  12.649 21.122 1.00 47.37 ? 343 HOH   B O   1 
HETATM 2257 O  O   . HOH   N 5 .   ? 9.734   8.055  -2.158 1.00 19.67 ? 344 HOH   B O   1 
HETATM 2258 O  O   . HOH   N 5 .   ? 33.550  23.505 15.756 1.00 43.20 ? 345 HOH   B O   1 
HETATM 2259 O  O   . HOH   N 5 .   ? 5.849   11.305 -3.026 1.00 34.16 ? 346 HOH   B O   1 
HETATM 2260 O  O   . HOH   N 5 .   ? 15.930  19.784 1.833  1.00 24.88 ? 347 HOH   B O   1 
HETATM 2261 O  O   . HOH   N 5 .   ? 1.995   21.368 29.973 1.00 34.62 ? 348 HOH   B O   1 
HETATM 2262 O  O   . HOH   N 5 .   ? 19.574  9.875  11.288 1.00 38.92 ? 349 HOH   B O   1 
HETATM 2263 O  O   . HOH   N 5 .   ? -14.071 4.579  5.945  1.00 51.22 ? 350 HOH   B O   1 
HETATM 2264 O  O   . HOH   N 5 .   ? 2.873   9.276  7.891  1.00 37.65 ? 351 HOH   B O   1 
HETATM 2265 O  O   . HOH   N 5 .   ? 11.455  3.117  3.206  1.00 27.81 ? 352 HOH   B O   1 
HETATM 2266 O  O   . HOH   N 5 .   ? 6.381   2.495  -0.375 1.00 28.15 ? 353 HOH   B O   1 
HETATM 2267 O  O   . HOH   N 5 .   ? 13.316  6.529  10.427 1.00 20.65 ? 354 HOH   B O   1 
HETATM 2268 O  O   . HOH   N 5 .   ? 5.366   17.197 7.605  1.00 27.94 ? 355 HOH   B O   1 
HETATM 2269 O  O   . HOH   N 5 .   ? 13.161  13.274 23.854 1.00 42.07 ? 356 HOH   B O   1 
HETATM 2270 O  O   . HOH   N 5 .   ? -8.210  12.305 6.896  1.00 25.91 ? 357 HOH   B O   1 
HETATM 2271 O  O   . HOH   N 5 .   ? 14.975  1.010  4.925  1.00 34.01 ? 358 HOH   B O   1 
HETATM 2272 O  O   . HOH   N 5 .   ? 28.590  25.329 20.866 1.00 28.51 ? 359 HOH   B O   1 
HETATM 2273 O  O   . HOH   N 5 .   ? 23.116  19.022 3.172  1.00 43.15 ? 360 HOH   B O   1 
HETATM 2274 O  O   . HOH   N 5 .   ? 12.197  1.502  5.178  1.00 27.20 ? 361 HOH   B O   1 
HETATM 2275 O  O   . HOH   N 5 .   ? -11.903 11.542 6.830  1.00 41.86 ? 362 HOH   B O   1 
HETATM 2276 O  O   . HOH   N 5 .   ? 15.842  16.928 12.218 1.00 32.91 ? 363 HOH   B O   1 
HETATM 2277 O  O   . HOH   N 5 .   ? 3.217   24.994 29.856 1.00 33.64 ? 364 HOH   B O   1 
HETATM 2278 O  O   . HOH   N 5 .   ? 25.569  21.039 10.773 1.00 27.41 ? 365 HOH   B O   1 
HETATM 2279 O  O   . HOH   N 5 .   ? -6.927  -0.733 14.213 1.00 38.52 ? 366 HOH   B O   1 
HETATM 2280 O  O   . HOH   N 5 .   ? 24.705  11.944 17.702 1.00 48.21 ? 367 HOH   B O   1 
HETATM 2281 O  O   . HOH   N 5 .   ? 23.326  30.109 6.857  1.00 57.43 ? 368 HOH   B O   1 
HETATM 2282 O  O   . HOH   N 5 .   ? 23.311  16.851 11.341 1.00 33.63 ? 369 HOH   B O   1 
HETATM 2283 O  O   . HOH   N 5 .   ? 13.723  21.303 -4.050 1.00 49.10 ? 370 HOH   B O   1 
HETATM 2284 O  O   . HOH   N 5 .   ? 34.632  16.304 16.519 1.00 52.39 ? 371 HOH   B O   1 
HETATM 2285 O  O   . HOH   N 5 .   ? -2.472  12.636 30.362 1.00 36.06 ? 372 HOH   B O   1 
HETATM 2286 O  O   . HOH   N 5 .   ? 18.411  17.260 -4.954 1.00 63.99 ? 373 HOH   B O   1 
HETATM 2287 O  O   . HOH   N 5 .   ? -8.869  20.381 16.715 1.00 51.20 ? 374 HOH   B O   1 
HETATM 2288 O  O   . HOH   N 5 .   ? 1.685   23.695 28.283 1.00 45.90 ? 375 HOH   B O   1 
HETATM 2289 O  O   . HOH   N 5 .   ? 7.020   14.008 -2.815 1.00 28.93 ? 376 HOH   B O   1 
HETATM 2290 O  O   . HOH   N 5 .   ? 17.961  23.100 1.399  1.00 41.43 ? 377 HOH   B O   1 
HETATM 2291 O  O   . HOH   N 5 .   ? 7.129   16.985 -3.122 1.00 35.25 ? 378 HOH   B O   1 
HETATM 2292 O  O   . HOH   N 5 .   ? 27.551  23.658 7.462  1.00 49.40 ? 379 HOH   B O   1 
HETATM 2293 O  O   . HOH   N 5 .   ? 18.061  10.232 -5.434 1.00 48.15 ? 380 HOH   B O   1 
HETATM 2294 O  O   . HOH   N 5 .   ? 2.104   22.238 2.000  1.00 36.11 ? 381 HOH   B O   1 
HETATM 2295 O  O   . HOH   N 5 .   ? -10.455 1.058  1.993  1.00 41.49 ? 382 HOH   B O   1 
HETATM 2296 O  O   . HOH   N 5 .   ? 27.011  20.530 12.792 1.00 35.37 ? 383 HOH   B O   1 
HETATM 2297 O  O   . HOH   N 5 .   ? -9.165  12.267 9.620  1.00 30.47 ? 384 HOH   B O   1 
HETATM 2298 O  O   . HOH   N 5 .   ? 5.083   23.196 1.984  1.00 43.93 ? 385 HOH   B O   1 
HETATM 2299 O  O   . HOH   N 5 .   ? 10.040  14.077 -5.986 1.00 33.43 ? 386 HOH   B O   1 
HETATM 2300 O  O   . HOH   N 5 .   ? -11.791 17.360 12.372 1.00 38.14 ? 387 HOH   B O   1 
HETATM 2301 O  O   . HOH   N 5 .   ? -1.042  24.243 28.693 1.00 51.20 ? 388 HOH   B O   1 
HETATM 2302 O  O   . HOH   N 5 .   ? -9.551  10.038 20.645 1.00 49.95 ? 389 HOH   B O   1 
HETATM 2303 O  O   . HOH   N 5 .   ? 13.680  1.882  1.301  1.00 43.84 ? 390 HOH   B O   1 
HETATM 2304 O  O   . HOH   N 5 .   ? 10.077  16.728 -5.455 1.00 45.67 ? 391 HOH   B O   1 
HETATM 2305 O  O   . HOH   N 5 .   ? -11.220 14.073 9.399  1.00 35.81 ? 392 HOH   B O   1 
HETATM 2306 O  O   . HOH   N 5 .   ? -2.580  0.345  2.408  1.00 27.69 ? 393 HOH   B O   1 
HETATM 2307 O  O   . HOH   N 5 .   ? 27.172  17.740 12.115 1.00 46.06 ? 394 HOH   B O   1 
HETATM 2308 O  O   . HOH   N 5 .   ? -9.997  18.342 8.367  1.00 36.83 ? 395 HOH   B O   1 
HETATM 2309 O  O   . HOH   N 5 .   ? 21.108  9.325  13.575 1.00 47.75 ? 396 HOH   B O   1 
HETATM 2310 O  O   . HOH   N 5 .   ? 2.331   21.936 -2.084 1.00 33.78 ? 397 HOH   B O   1 
HETATM 2311 O  O   . HOH   N 5 .   ? 29.016  25.671 7.918  1.00 48.81 ? 398 HOH   B O   1 
HETATM 2312 O  O   . HOH   N 5 .   ? -3.434  20.838 4.170  1.00 39.12 ? 399 HOH   B O   1 
# 
