data_8ZCI
# 
_entry.id   8ZCI 
# 
_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   8ZCI         pdb_00008zci 10.2210/pdb8zci/pdb 
WWPDB D_1300047486 ?            ?                   
# 
_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       2025-04-30 
_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                        8ZCI 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ssugiyama@kochi-u.ac.jp 
_pdbx_contact_author.name_first         Shigeru 
_pdbx_contact_author.name_last          Sugiyama 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0563-6799 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Sugiyama, S.' 1 ? 
'Tanaka, J.'   2 ? 
'Matsuoka, S.' 3 ? 
'Murata, M.'   4 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'X-ray structure of the human heart fatty acid-binding protein complexed with R-Ibuprofen' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sugiyama, S.' 1 ? 
primary 'Tanaka, J.'   2 ? 
primary 'Matsuoka, S.' 3 ? 
primary 'Murata, M.'   4 ? 
# 
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 'Fatty acid-binding protein, heart'               14879.022 1   ? ? ? ? 
2 non-polymer syn '(2R)-2-[4-(2-methylpropyl)phenyl]propanoic acid' 206.281   1   ? ? ? ? 
3 non-polymer syn 'TETRAETHYLENE GLYCOL'                            194.226   1   ? ? ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                           106.120   1   ? ? ? ? 
5 non-polymer syn 'ACETIC ACID'                                     60.052    1   ? ? ? ? 
6 non-polymer syn 'TRIETHYLENE GLYCOL'                              150.173   1   ? ? ? ? 
7 non-polymer syn GLYCEROL                                          92.094    1   ? ? ? ? 
8 water       nat water                                             18.015    194 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Fatty acid-binding protein 3,Heart-type fatty acid-binding protein,H-FABP,Mammary-derived growth inhibitor,MDGI,Muscle fatty acid-binding protein,M-FABP
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDETTADDRK
VKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEKEA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDETTADDRK
VKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEKEA
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2R)-2-[4-(2-methylpropyl)phenyl]propanoic acid' IZP 
3 'TETRAETHYLENE GLYCOL'                            PG4 
4 'DI(HYDROXYETHYL)ETHER'                           PEG 
5 'ACETIC ACID'                                     ACY 
6 'TRIETHYLENE GLYCOL'                              PGE 
7 GLYCEROL                                          GOL 
8 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   VAL n 
1 3   ASP n 
1 4   ALA n 
1 5   PHE n 
1 6   LEU n 
1 7   GLY n 
1 8   THR n 
1 9   TRP n 
1 10  LYS n 
1 11  LEU n 
1 12  VAL n 
1 13  ASP n 
1 14  SER n 
1 15  LYS n 
1 16  ASN n 
1 17  PHE n 
1 18  ASP n 
1 19  ASP n 
1 20  TYR n 
1 21  MET n 
1 22  LYS n 
1 23  SER n 
1 24  LEU n 
1 25  GLY n 
1 26  VAL n 
1 27  GLY n 
1 28  PHE n 
1 29  ALA n 
1 30  THR n 
1 31  ARG n 
1 32  GLN n 
1 33  VAL n 
1 34  ALA n 
1 35  SER n 
1 36  MET n 
1 37  THR n 
1 38  LYS n 
1 39  PRO n 
1 40  THR n 
1 41  THR n 
1 42  ILE n 
1 43  ILE n 
1 44  GLU n 
1 45  LYS n 
1 46  ASN n 
1 47  GLY n 
1 48  ASP n 
1 49  ILE n 
1 50  LEU n 
1 51  THR n 
1 52  LEU n 
1 53  LYS n 
1 54  THR n 
1 55  HIS n 
1 56  SER n 
1 57  THR n 
1 58  PHE n 
1 59  LYS n 
1 60  ASN n 
1 61  THR n 
1 62  GLU n 
1 63  ILE n 
1 64  SER n 
1 65  PHE n 
1 66  LYS n 
1 67  LEU n 
1 68  GLY n 
1 69  VAL n 
1 70  GLU n 
1 71  PHE n 
1 72  ASP n 
1 73  GLU n 
1 74  THR n 
1 75  THR n 
1 76  ALA n 
1 77  ASP n 
1 78  ASP n 
1 79  ARG n 
1 80  LYS n 
1 81  VAL n 
1 82  LYS n 
1 83  SER n 
1 84  ILE n 
1 85  VAL n 
1 86  THR n 
1 87  LEU n 
1 88  ASP n 
1 89  GLY n 
1 90  GLY n 
1 91  LYS n 
1 92  LEU n 
1 93  VAL n 
1 94  HIS n 
1 95  LEU n 
1 96  GLN n 
1 97  LYS n 
1 98  TRP n 
1 99  ASP n 
1 100 GLY n 
1 101 GLN n 
1 102 GLU n 
1 103 THR n 
1 104 THR n 
1 105 LEU n 
1 106 VAL n 
1 107 ARG n 
1 108 GLU n 
1 109 LEU n 
1 110 ILE n 
1 111 ASP n 
1 112 GLY n 
1 113 LYS n 
1 114 LEU n 
1 115 ILE n 
1 116 LEU n 
1 117 THR n 
1 118 LEU n 
1 119 THR n 
1 120 HIS n 
1 121 GLY n 
1 122 THR n 
1 123 ALA n 
1 124 VAL n 
1 125 CYS n 
1 126 THR n 
1 127 ARG n 
1 128 THR n 
1 129 TYR n 
1 130 GLU n 
1 131 LYS n 
1 132 GLU n 
1 133 ALA 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                   133 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'FABP3, FABP11, MDGI' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ACY non-polymer         . 'ACETIC ACID'                                     ?                               'C2 H4 O2'       
60.052  
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 
IZP non-polymer         . '(2R)-2-[4-(2-methylpropyl)phenyl]propanoic acid' '(R)-Ibuprofen'                 'C13 H18 O2'     
206.281 
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                           ?                               'C4 H10 O3'      
106.120 
PG4 non-polymer         . 'TETRAETHYLENE GLYCOL'                            ?                               'C8 H18 O5'      
194.226 
PGE non-polymer         . 'TRIETHYLENE GLYCOL'                              ?                               'C6 H14 O4'      
150.173 
PHE 'L-peptide linking' y PHENYLALANINE                                     ?                               'C9 H11 N O2'    
165.189 
PRO 'L-peptide linking' y PROLINE                                           ?                               'C5 H9 N O2'     
115.130 
SER 'L-peptide linking' y SERINE                                            ?                               'C3 H7 N O3'     
105.093 
THR 'L-peptide linking' y THREONINE                                         ?                               'C4 H9 N O3'     
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                        ?                               'C11 H12 N2 O2'  
204.225 
TYR 'L-peptide linking' y TYROSINE                                          ?                               'C9 H11 N O3'    
181.189 
VAL 'L-peptide linking' y VALINE                                            ?                               'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   0   MET ALA A . n 
A 1 2   VAL 2   1   1   VAL VAL A . n 
A 1 3   ASP 3   2   2   ASP ASP A . n 
A 1 4   ALA 4   3   3   ALA ALA A . n 
A 1 5   PHE 5   4   4   PHE PHE A . n 
A 1 6   LEU 6   5   5   LEU LEU A . n 
A 1 7   GLY 7   6   6   GLY GLY A . n 
A 1 8   THR 8   7   7   THR THR A . n 
A 1 9   TRP 9   8   8   TRP TRP A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  LEU 11  10  10  LEU LEU A . n 
A 1 12  VAL 12  11  11  VAL VAL A . n 
A 1 13  ASP 13  12  12  ASP ASP A . n 
A 1 14  SER 14  13  13  SER SER A . n 
A 1 15  LYS 15  14  14  LYS LYS A . n 
A 1 16  ASN 16  15  15  ASN ASN A . n 
A 1 17  PHE 17  16  16  PHE PHE A . n 
A 1 18  ASP 18  17  17  ASP ASP A . n 
A 1 19  ASP 19  18  18  ASP ASP A . n 
A 1 20  TYR 20  19  19  TYR TYR A . n 
A 1 21  MET 21  20  20  MET MET A . n 
A 1 22  LYS 22  21  21  LYS LYS A . n 
A 1 23  SER 23  22  22  SER SER A . n 
A 1 24  LEU 24  23  23  LEU LEU A . n 
A 1 25  GLY 25  24  24  GLY GLY A . n 
A 1 26  VAL 26  25  25  VAL VAL A . n 
A 1 27  GLY 27  26  26  GLY GLY A . n 
A 1 28  PHE 28  27  27  PHE PHE A . n 
A 1 29  ALA 29  28  28  ALA ALA A . n 
A 1 30  THR 30  29  29  THR THR A . n 
A 1 31  ARG 31  30  30  ARG ARG A . n 
A 1 32  GLN 32  31  31  GLN GLN A . n 
A 1 33  VAL 33  32  32  VAL VAL A . n 
A 1 34  ALA 34  33  33  ALA ALA A . n 
A 1 35  SER 35  34  34  SER SER A . n 
A 1 36  MET 36  35  35  MET MET A . n 
A 1 37  THR 37  36  36  THR THR A . n 
A 1 38  LYS 38  37  37  LYS LYS A . n 
A 1 39  PRO 39  38  38  PRO PRO A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  THR 41  40  40  THR THR A . n 
A 1 42  ILE 42  41  41  ILE ILE A . n 
A 1 43  ILE 43  42  42  ILE ILE A . n 
A 1 44  GLU 44  43  43  GLU GLU A . n 
A 1 45  LYS 45  44  44  LYS LYS A . n 
A 1 46  ASN 46  45  45  ASN ASN A . n 
A 1 47  GLY 47  46  46  GLY GLY A . n 
A 1 48  ASP 48  47  47  ASP ASP A . n 
A 1 49  ILE 49  48  48  ILE ILE A . n 
A 1 50  LEU 50  49  49  LEU LEU A . n 
A 1 51  THR 51  50  50  THR THR A . n 
A 1 52  LEU 52  51  51  LEU LEU A . n 
A 1 53  LYS 53  52  52  LYS LYS A . n 
A 1 54  THR 54  53  53  THR THR A . n 
A 1 55  HIS 55  54  54  HIS HIS A . n 
A 1 56  SER 56  55  55  SER SER A . n 
A 1 57  THR 57  56  56  THR THR A . n 
A 1 58  PHE 58  57  57  PHE PHE A . n 
A 1 59  LYS 59  58  58  LYS LYS A . n 
A 1 60  ASN 60  59  59  ASN ASN A . n 
A 1 61  THR 61  60  60  THR THR A . n 
A 1 62  GLU 62  61  61  GLU GLU A . n 
A 1 63  ILE 63  62  62  ILE ILE A . n 
A 1 64  SER 64  63  63  SER SER A . n 
A 1 65  PHE 65  64  64  PHE PHE A . n 
A 1 66  LYS 66  65  65  LYS LYS A . n 
A 1 67  LEU 67  66  66  LEU LEU A . n 
A 1 68  GLY 68  67  67  GLY GLY A . n 
A 1 69  VAL 69  68  68  VAL VAL A . n 
A 1 70  GLU 70  69  69  GLU GLU A . n 
A 1 71  PHE 71  70  70  PHE PHE A . n 
A 1 72  ASP 72  71  71  ASP ASP A . n 
A 1 73  GLU 73  72  72  GLU GLU A . n 
A 1 74  THR 74  73  73  THR THR A . n 
A 1 75  THR 75  74  74  THR THR A . n 
A 1 76  ALA 76  75  75  ALA ALA A . n 
A 1 77  ASP 77  76  76  ASP ASP A . n 
A 1 78  ASP 78  77  77  ASP ASP A . n 
A 1 79  ARG 79  78  78  ARG ARG A . n 
A 1 80  LYS 80  79  79  LYS LYS A . n 
A 1 81  VAL 81  80  80  VAL VAL A . n 
A 1 82  LYS 82  81  81  LYS LYS A . n 
A 1 83  SER 83  82  82  SER SER A . n 
A 1 84  ILE 84  83  83  ILE ILE A . n 
A 1 85  VAL 85  84  84  VAL VAL A . n 
A 1 86  THR 86  85  85  THR THR A . n 
A 1 87  LEU 87  86  86  LEU LEU A . n 
A 1 88  ASP 88  87  87  ASP ASP A . n 
A 1 89  GLY 89  88  88  GLY GLY A . n 
A 1 90  GLY 90  89  89  GLY GLY A . n 
A 1 91  LYS 91  90  90  LYS LYS A . n 
A 1 92  LEU 92  91  91  LEU LEU A . n 
A 1 93  VAL 93  92  92  VAL VAL A . n 
A 1 94  HIS 94  93  93  HIS HIS A . n 
A 1 95  LEU 95  94  94  LEU LEU A . n 
A 1 96  GLN 96  95  95  GLN GLN A . n 
A 1 97  LYS 97  96  96  LYS LYS A . n 
A 1 98  TRP 98  97  97  TRP TRP A . n 
A 1 99  ASP 99  98  98  ASP ASP A . n 
A 1 100 GLY 100 99  99  GLY GLY A . n 
A 1 101 GLN 101 100 100 GLN GLN A . n 
A 1 102 GLU 102 101 101 GLU GLU A . n 
A 1 103 THR 103 102 102 THR THR A . n 
A 1 104 THR 104 103 103 THR THR A . n 
A 1 105 LEU 105 104 104 LEU LEU A . n 
A 1 106 VAL 106 105 105 VAL VAL A . n 
A 1 107 ARG 107 106 106 ARG ARG A . n 
A 1 108 GLU 108 107 107 GLU GLU A . n 
A 1 109 LEU 109 108 108 LEU LEU A . n 
A 1 110 ILE 110 109 109 ILE ILE A . n 
A 1 111 ASP 111 110 110 ASP ASP A . n 
A 1 112 GLY 112 111 111 GLY GLY A . n 
A 1 113 LYS 113 112 112 LYS LYS A . n 
A 1 114 LEU 114 113 113 LEU LEU A . n 
A 1 115 ILE 115 114 114 ILE ILE A . n 
A 1 116 LEU 116 115 115 LEU LEU A . n 
A 1 117 THR 117 116 116 THR THR A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 THR 119 118 118 THR THR A . n 
A 1 120 HIS 120 119 119 HIS HIS A . n 
A 1 121 GLY 121 120 120 GLY GLY A . n 
A 1 122 THR 122 121 121 THR THR A . n 
A 1 123 ALA 123 122 122 ALA ALA A . n 
A 1 124 VAL 124 123 123 VAL VAL A . n 
A 1 125 CYS 125 124 124 CYS CYS A . n 
A 1 126 THR 126 125 125 THR THR A . n 
A 1 127 ARG 127 126 126 ARG ARG A . n 
A 1 128 THR 128 127 127 THR THR A . n 
A 1 129 TYR 129 128 128 TYR TYR A . n 
A 1 130 GLU 130 129 129 GLU GLU A . n 
A 1 131 LYS 131 130 130 LYS LYS A . n 
A 1 132 GLU 132 131 131 GLU GLU A . n 
A 1 133 ALA 133 132 132 ALA ALA A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        IZP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   IZP 
_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 
B 2 IZP 1   200 200 IZP IZP A . 
C 3 PG4 1   201 201 PG4 PG4 A . 
D 4 PEG 1   202 202 PEG PEG A . 
E 5 ACY 1   203 203 ACY ACY A . 
F 6 PGE 1   204 204 PGE PGE A . 
G 7 GOL 1   205 205 GOL GOL A . 
H 8 HOH 1   301 378 HOH HOH A . 
H 8 HOH 2   302 300 HOH HOH A . 
H 8 HOH 3   303 327 HOH HOH A . 
H 8 HOH 4   304 128 HOH HOH A . 
H 8 HOH 5   305 366 HOH HOH A . 
H 8 HOH 6   306 259 HOH HOH A . 
H 8 HOH 7   307 280 HOH HOH A . 
H 8 HOH 8   308 376 HOH HOH A . 
H 8 HOH 9   309 60  HOH HOH A . 
H 8 HOH 10  310 293 HOH HOH A . 
H 8 HOH 11  311 153 HOH HOH A . 
H 8 HOH 12  312 397 HOH HOH A . 
H 8 HOH 13  313 122 HOH HOH A . 
H 8 HOH 14  314 412 HOH HOH A . 
H 8 HOH 15  315 77  HOH HOH A . 
H 8 HOH 16  316 36  HOH HOH A . 
H 8 HOH 17  317 403 HOH HOH A . 
H 8 HOH 18  318 90  HOH HOH A . 
H 8 HOH 19  319 275 HOH HOH A . 
H 8 HOH 20  320 407 HOH HOH A . 
H 8 HOH 21  321 24  HOH HOH A . 
H 8 HOH 22  322 270 HOH HOH A . 
H 8 HOH 23  323 49  HOH HOH A . 
H 8 HOH 24  324 44  HOH HOH A . 
H 8 HOH 25  325 323 HOH HOH A . 
H 8 HOH 26  326 95  HOH HOH A . 
H 8 HOH 27  327 251 HOH HOH A . 
H 8 HOH 28  328 97  HOH HOH A . 
H 8 HOH 29  329 287 HOH HOH A . 
H 8 HOH 30  330 113 HOH HOH A . 
H 8 HOH 31  331 91  HOH HOH A . 
H 8 HOH 32  332 380 HOH HOH A . 
H 8 HOH 33  333 28  HOH HOH A . 
H 8 HOH 34  334 389 HOH HOH A . 
H 8 HOH 35  335 16  HOH HOH A . 
H 8 HOH 36  336 298 HOH HOH A . 
H 8 HOH 37  337 37  HOH HOH A . 
H 8 HOH 38  338 78  HOH HOH A . 
H 8 HOH 39  339 11  HOH HOH A . 
H 8 HOH 40  340 250 HOH HOH A . 
H 8 HOH 41  341 13  HOH HOH A . 
H 8 HOH 42  342 166 HOH HOH A . 
H 8 HOH 43  343 54  HOH HOH A . 
H 8 HOH 44  344 6   HOH HOH A . 
H 8 HOH 45  345 56  HOH HOH A . 
H 8 HOH 46  346 14  HOH HOH A . 
H 8 HOH 47  347 315 HOH HOH A . 
H 8 HOH 48  348 375 HOH HOH A . 
H 8 HOH 49  349 52  HOH HOH A . 
H 8 HOH 50  350 368 HOH HOH A . 
H 8 HOH 51  351 245 HOH HOH A . 
H 8 HOH 52  352 40  HOH HOH A . 
H 8 HOH 53  353 30  HOH HOH A . 
H 8 HOH 54  354 381 HOH HOH A . 
H 8 HOH 55  355 394 HOH HOH A . 
H 8 HOH 56  356 288 HOH HOH A . 
H 8 HOH 57  357 402 HOH HOH A . 
H 8 HOH 58  358 33  HOH HOH A . 
H 8 HOH 59  359 284 HOH HOH A . 
H 8 HOH 60  360 51  HOH HOH A . 
H 8 HOH 61  361 25  HOH HOH A . 
H 8 HOH 62  362 365 HOH HOH A . 
H 8 HOH 63  363 266 HOH HOH A . 
H 8 HOH 64  364 137 HOH HOH A . 
H 8 HOH 65  365 3   HOH HOH A . 
H 8 HOH 66  366 17  HOH HOH A . 
H 8 HOH 67  367 190 HOH HOH A . 
H 8 HOH 68  368 4   HOH HOH A . 
H 8 HOH 69  369 55  HOH HOH A . 
H 8 HOH 70  370 46  HOH HOH A . 
H 8 HOH 71  371 107 HOH HOH A . 
H 8 HOH 72  372 18  HOH HOH A . 
H 8 HOH 73  373 341 HOH HOH A . 
H 8 HOH 74  374 272 HOH HOH A . 
H 8 HOH 75  375 81  HOH HOH A . 
H 8 HOH 76  376 9   HOH HOH A . 
H 8 HOH 77  377 39  HOH HOH A . 
H 8 HOH 78  378 1   HOH HOH A . 
H 8 HOH 79  379 5   HOH HOH A . 
H 8 HOH 80  380 64  HOH HOH A . 
H 8 HOH 81  381 367 HOH HOH A . 
H 8 HOH 82  382 10  HOH HOH A . 
H 8 HOH 83  383 82  HOH HOH A . 
H 8 HOH 84  384 372 HOH HOH A . 
H 8 HOH 85  385 99  HOH HOH A . 
H 8 HOH 86  386 255 HOH HOH A . 
H 8 HOH 87  387 67  HOH HOH A . 
H 8 HOH 88  388 83  HOH HOH A . 
H 8 HOH 89  389 74  HOH HOH A . 
H 8 HOH 90  390 34  HOH HOH A . 
H 8 HOH 91  391 42  HOH HOH A . 
H 8 HOH 92  392 35  HOH HOH A . 
H 8 HOH 93  393 2   HOH HOH A . 
H 8 HOH 94  394 29  HOH HOH A . 
H 8 HOH 95  395 19  HOH HOH A . 
H 8 HOH 96  396 73  HOH HOH A . 
H 8 HOH 97  397 370 HOH HOH A . 
H 8 HOH 98  398 391 HOH HOH A . 
H 8 HOH 99  399 104 HOH HOH A . 
H 8 HOH 100 400 76  HOH HOH A . 
H 8 HOH 101 401 32  HOH HOH A . 
H 8 HOH 102 402 23  HOH HOH A . 
H 8 HOH 103 403 27  HOH HOH A . 
H 8 HOH 104 404 58  HOH HOH A . 
H 8 HOH 105 405 286 HOH HOH A . 
H 8 HOH 106 406 306 HOH HOH A . 
H 8 HOH 107 407 12  HOH HOH A . 
H 8 HOH 108 408 7   HOH HOH A . 
H 8 HOH 109 409 43  HOH HOH A . 
H 8 HOH 110 410 312 HOH HOH A . 
H 8 HOH 111 411 15  HOH HOH A . 
H 8 HOH 112 412 373 HOH HOH A . 
H 8 HOH 113 413 47  HOH HOH A . 
H 8 HOH 114 414 399 HOH HOH A . 
H 8 HOH 115 415 66  HOH HOH A . 
H 8 HOH 116 416 21  HOH HOH A . 
H 8 HOH 117 417 282 HOH HOH A . 
H 8 HOH 118 418 45  HOH HOH A . 
H 8 HOH 119 419 20  HOH HOH A . 
H 8 HOH 120 420 273 HOH HOH A . 
H 8 HOH 121 421 302 HOH HOH A . 
H 8 HOH 122 422 304 HOH HOH A . 
H 8 HOH 123 423 383 HOH HOH A . 
H 8 HOH 124 424 385 HOH HOH A . 
H 8 HOH 125 425 151 HOH HOH A . 
H 8 HOH 126 426 183 HOH HOH A . 
H 8 HOH 127 427 386 HOH HOH A . 
H 8 HOH 128 428 88  HOH HOH A . 
H 8 HOH 129 429 379 HOH HOH A . 
H 8 HOH 130 430 121 HOH HOH A . 
H 8 HOH 131 431 75  HOH HOH A . 
H 8 HOH 132 432 297 HOH HOH A . 
H 8 HOH 133 433 382 HOH HOH A . 
H 8 HOH 134 434 69  HOH HOH A . 
H 8 HOH 135 435 408 HOH HOH A . 
H 8 HOH 136 436 283 HOH HOH A . 
H 8 HOH 137 437 41  HOH HOH A . 
H 8 HOH 138 438 200 HOH HOH A . 
H 8 HOH 139 439 165 HOH HOH A . 
H 8 HOH 140 440 152 HOH HOH A . 
H 8 HOH 141 441 409 HOH HOH A . 
H 8 HOH 142 442 404 HOH HOH A . 
H 8 HOH 143 443 396 HOH HOH A . 
H 8 HOH 144 444 93  HOH HOH A . 
H 8 HOH 145 445 271 HOH HOH A . 
H 8 HOH 146 446 388 HOH HOH A . 
H 8 HOH 147 447 401 HOH HOH A . 
H 8 HOH 148 448 277 HOH HOH A . 
H 8 HOH 149 449 239 HOH HOH A . 
H 8 HOH 150 450 48  HOH HOH A . 
H 8 HOH 151 451 278 HOH HOH A . 
H 8 HOH 152 452 70  HOH HOH A . 
H 8 HOH 153 453 279 HOH HOH A . 
H 8 HOH 154 454 405 HOH HOH A . 
H 8 HOH 155 455 87  HOH HOH A . 
H 8 HOH 156 456 276 HOH HOH A . 
H 8 HOH 157 457 332 HOH HOH A . 
H 8 HOH 158 458 374 HOH HOH A . 
H 8 HOH 159 459 267 HOH HOH A . 
H 8 HOH 160 460 305 HOH HOH A . 
H 8 HOH 161 461 289 HOH HOH A . 
H 8 HOH 162 462 377 HOH HOH A . 
H 8 HOH 163 463 333 HOH HOH A . 
H 8 HOH 164 464 96  HOH HOH A . 
H 8 HOH 165 465 329 HOH HOH A . 
H 8 HOH 166 466 258 HOH HOH A . 
H 8 HOH 167 467 371 HOH HOH A . 
H 8 HOH 168 468 410 HOH HOH A . 
H 8 HOH 169 469 336 HOH HOH A . 
H 8 HOH 170 470 182 HOH HOH A . 
H 8 HOH 171 471 247 HOH HOH A . 
H 8 HOH 172 472 61  HOH HOH A . 
H 8 HOH 173 473 243 HOH HOH A . 
H 8 HOH 174 474 296 HOH HOH A . 
H 8 HOH 175 475 101 HOH HOH A . 
H 8 HOH 176 476 140 HOH HOH A . 
H 8 HOH 177 477 384 HOH HOH A . 
H 8 HOH 178 478 390 HOH HOH A . 
H 8 HOH 179 479 400 HOH HOH A . 
H 8 HOH 180 480 393 HOH HOH A . 
H 8 HOH 181 481 254 HOH HOH A . 
H 8 HOH 182 482 85  HOH HOH A . 
H 8 HOH 183 483 324 HOH HOH A . 
H 8 HOH 184 484 350 HOH HOH A . 
H 8 HOH 185 485 68  HOH HOH A . 
H 8 HOH 186 486 290 HOH HOH A . 
H 8 HOH 187 487 406 HOH HOH A . 
H 8 HOH 188 488 387 HOH HOH A . 
H 8 HOH 189 489 411 HOH HOH A . 
H 8 HOH 190 490 392 HOH HOH A . 
H 8 HOH 191 491 65  HOH HOH A . 
H 8 HOH 192 492 335 HOH HOH A . 
H 8 HOH 193 493 308 HOH HOH A . 
H 8 HOH 194 494 253 HOH HOH A . 
# 
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 MET 0 ? CG ? A MET 1 CG 
2 1 Y 1 A MET 0 ? SD ? A MET 1 SD 
3 1 Y 1 A MET 0 ? CE ? A MET 1 CE 
# 
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   ? ? ? 5.8.0238 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        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                     8ZCI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     69.201 
_cell.length_a_esd                 ? 
_cell.length_b                     107.868 
_cell.length_b_esd                 ? 
_cell.length_c                     48.146 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8ZCI 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_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                   8ZCI 
_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             3.02 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          59.26 
_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              4.5 
_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    '0.1M Na-citrate (pH4.5), 40%PEG400' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MAR CCD 300 mm' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-05-12 
_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   0.90000 
_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                        'SPRING-8 BEAMLINE BL44XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.90000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL44XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZCI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.35 
_reflns.d_resolution_low                               58.24 
_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                                     39678 
_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                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.4 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.052 
_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                                    1.35 
_reflns_shell.d_res_low                                     1.37 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1968 
_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                               ? 
_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                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.389 
_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]                            1.44 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.04 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -1.40 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               23.079 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.977 
_refine.correlation_coeff_Fo_to_Fc_free          0.971 
_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                                 8ZCI 
_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                            1.35 
_refine.ls_d_res_low                             31.93 
_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                     37593 
_refine.ls_number_reflns_R_free                  1987 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.97 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.13409 
_refine.ls_R_factor_R_free                       0.16569 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.13238 
_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                      3WVM 
_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                       0.043 
_refine.pdbx_overall_ESU_R_Free                  0.044 
_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                             1.923 
_refine.overall_SU_ML                            0.033 
_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                       1.35 
_refine_hist.d_res_low                        31.93 
_refine_hist.number_atoms_solvent             194 
_refine_hist.number_atoms_total               1290 
_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        1041 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         55 
_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' ? 0.014  0.013  1213 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  1182 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.690  1.662  1641 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.431  1.606  2756 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.643  5.000  155  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 34.494 24.200 50   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.271 15.000 223  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.421 15.000 4    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.087  0.200  166  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  1346 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  234  ? 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' ? 2.772  1.929  591  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.576  1.922  589  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.212  2.896  755  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.262  2.902  756  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.957  2.425  622  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.955  2.431  623  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.638  3.446  887  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.880  26.322 1303 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.410  24.984 1249 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 2.749  3.000  2394 ? 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                       1.350 
_refine_ls_shell.d_res_low                        1.385 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             133 
_refine_ls_shell.number_reflns_R_work             2716 
_refine_ls_shell.percent_reflns_obs               97.84 
_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                  0.267 
_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                  0.298 
# 
_struct.entry_id                     8ZCI 
_struct.title                        'X-ray structure of the human heart fatty acid-binding protein complexed with R-Ibuprofen' 
_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        8ZCI 
_struct_keywords.text            'FABP, Complex, Binding protein, R-Ibuprofen, LIPID BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'LIPID BINDING 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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
H N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FABPH_HUMAN 
_struct_ref.pdbx_db_accession          P05413 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDETTADDRK
VKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEKEA
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8ZCI 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 133 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P05413 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  133 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       0 
_struct_ref_seq.pdbx_auth_seq_align_end       132 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 1060 ? 
1 MORE         14   ? 
1 'SSA (A^2)'  7290 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 MET A 1  ? LEU A 6  ? MET A 0  LEU A 5  5 ? 6 
HELX_P HELX_P2 AA2 ASN A 16 ? LEU A 24 ? ASN A 15 LEU A 23 1 ? 9 
HELX_P HELX_P3 AA3 GLY A 27 ? SER A 35 ? GLY A 26 SER A 34 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   10 
_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 
AA1 9 10 ? 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  THR A 61  ? PHE A 65  ? THR A 60  PHE A 64  
AA1 2  ILE A 49  ? HIS A 55  ? ILE A 48  HIS A 54  
AA1 3  THR A 40  ? ASN A 46  ? THR A 39  ASN A 45  
AA1 4  GLY A 7   ? LYS A 15  ? GLY A 6   LYS A 14  
AA1 5  ALA A 123 ? LYS A 131 ? ALA A 122 LYS A 130 
AA1 6  LYS A 113 ? HIS A 120 ? LYS A 112 HIS A 119 
AA1 7  GLN A 101 ? ILE A 110 ? GLN A 100 ILE A 109 
AA1 8  LYS A 91  ? TRP A 98  ? LYS A 90  TRP A 97  
AA1 9  LYS A 80  ? ASP A 88  ? LYS A 79  ASP A 87  
AA1 10 PHE A 71  ? THR A 74  ? PHE A 70  THR A 73  
# 
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  O PHE A 65  ? O PHE A 64  N LEU A 50  ? N LEU A 49  
AA1 2 3  O HIS A 55  ? O HIS A 54  N THR A 40  ? N THR A 39  
AA1 3 4  O THR A 41  ? O THR A 40  N TRP A 9   ? N TRP A 8   
AA1 4 5  N VAL A 12  ? N VAL A 11  O THR A 128 ? O THR A 127 
AA1 5 6  O ARG A 127 ? O ARG A 126 N LEU A 116 ? N LEU A 115 
AA1 6 7  O ILE A 115 ? O ILE A 114 N GLU A 108 ? N GLU A 107 
AA1 7 8  O ARG A 107 ? O ARG A 106 N LEU A 92  ? N LEU A 91  
AA1 8 9  O VAL A 93  ? O VAL A 92  N THR A 86  ? N THR A 85  
AA1 9 10 O VAL A 81  ? O VAL A 80  N GLU A 73  ? N GLU A 72  
# 
_pdbx_entry_details.entry_id                   8ZCI 
_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   N 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       494 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.17 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
ACY C    C N N 1   
ACY O    O N N 2   
ACY OXT  O N N 3   
ACY CH3  C N N 4   
ACY HXT  H N N 5   
ACY H1   H N N 6   
ACY H2   H N N 7   
ACY H3   H N N 8   
ALA N    N N N 9   
ALA CA   C N S 10  
ALA C    C N N 11  
ALA O    O N N 12  
ALA CB   C N N 13  
ALA OXT  O N N 14  
ALA H    H N N 15  
ALA H2   H N N 16  
ALA HA   H N N 17  
ALA HB1  H N N 18  
ALA HB2  H N N 19  
ALA HB3  H N N 20  
ALA HXT  H N N 21  
ARG N    N N N 22  
ARG CA   C N S 23  
ARG C    C N N 24  
ARG O    O N N 25  
ARG CB   C N N 26  
ARG CG   C N N 27  
ARG CD   C N N 28  
ARG NE   N N N 29  
ARG CZ   C N N 30  
ARG NH1  N N N 31  
ARG NH2  N N N 32  
ARG OXT  O N N 33  
ARG H    H N N 34  
ARG H2   H N N 35  
ARG HA   H N N 36  
ARG HB2  H N N 37  
ARG HB3  H N N 38  
ARG HG2  H N N 39  
ARG HG3  H N N 40  
ARG HD2  H N N 41  
ARG HD3  H N N 42  
ARG HE   H N N 43  
ARG HH11 H N N 44  
ARG HH12 H N N 45  
ARG HH21 H N N 46  
ARG HH22 H N N 47  
ARG HXT  H N N 48  
ASN N    N N N 49  
ASN CA   C N S 50  
ASN C    C N N 51  
ASN O    O N N 52  
ASN CB   C N N 53  
ASN CG   C N N 54  
ASN OD1  O N N 55  
ASN ND2  N N N 56  
ASN OXT  O N N 57  
ASN H    H N N 58  
ASN H2   H N N 59  
ASN HA   H N N 60  
ASN HB2  H N N 61  
ASN HB3  H N N 62  
ASN HD21 H N N 63  
ASN HD22 H N N 64  
ASN HXT  H N N 65  
ASP N    N N N 66  
ASP CA   C N S 67  
ASP C    C N N 68  
ASP O    O N N 69  
ASP CB   C N N 70  
ASP CG   C N N 71  
ASP OD1  O N N 72  
ASP OD2  O N N 73  
ASP OXT  O N N 74  
ASP H    H N N 75  
ASP H2   H N N 76  
ASP HA   H N N 77  
ASP HB2  H N N 78  
ASP HB3  H N N 79  
ASP HD2  H N N 80  
ASP HXT  H N N 81  
CYS N    N N N 82  
CYS CA   C N R 83  
CYS C    C N N 84  
CYS O    O N N 85  
CYS CB   C N N 86  
CYS SG   S N N 87  
CYS OXT  O N N 88  
CYS H    H N N 89  
CYS H2   H N N 90  
CYS HA   H N N 91  
CYS HB2  H N N 92  
CYS HB3  H N N 93  
CYS HG   H N N 94  
CYS HXT  H N N 95  
GLN N    N N N 96  
GLN CA   C N S 97  
GLN C    C N N 98  
GLN O    O N N 99  
GLN CB   C N N 100 
GLN CG   C N N 101 
GLN CD   C N N 102 
GLN OE1  O N N 103 
GLN NE2  N N N 104 
GLN OXT  O N N 105 
GLN H    H N N 106 
GLN H2   H N N 107 
GLN HA   H N N 108 
GLN HB2  H N N 109 
GLN HB3  H N N 110 
GLN HG2  H N N 111 
GLN HG3  H N N 112 
GLN HE21 H N N 113 
GLN HE22 H N N 114 
GLN HXT  H N N 115 
GLU N    N N N 116 
GLU CA   C N S 117 
GLU C    C N N 118 
GLU O    O N N 119 
GLU CB   C N N 120 
GLU CG   C N N 121 
GLU CD   C N N 122 
GLU OE1  O N N 123 
GLU OE2  O N N 124 
GLU OXT  O N N 125 
GLU H    H N N 126 
GLU H2   H N N 127 
GLU HA   H N N 128 
GLU HB2  H N N 129 
GLU HB3  H N N 130 
GLU HG2  H N N 131 
GLU HG3  H N N 132 
GLU HE2  H N N 133 
GLU HXT  H N N 134 
GLY N    N N N 135 
GLY CA   C N N 136 
GLY C    C N N 137 
GLY O    O N N 138 
GLY OXT  O N N 139 
GLY H    H N N 140 
GLY H2   H N N 141 
GLY HA2  H N N 142 
GLY HA3  H N N 143 
GLY HXT  H N N 144 
GOL C1   C N N 145 
GOL O1   O N N 146 
GOL C2   C N N 147 
GOL O2   O N N 148 
GOL C3   C N N 149 
GOL O3   O N N 150 
GOL H11  H N N 151 
GOL H12  H N N 152 
GOL HO1  H N N 153 
GOL H2   H N N 154 
GOL HO2  H N N 155 
GOL H31  H N N 156 
GOL H32  H N N 157 
GOL HO3  H N N 158 
HIS N    N N N 159 
HIS CA   C N S 160 
HIS C    C N N 161 
HIS O    O N N 162 
HIS CB   C N N 163 
HIS CG   C Y N 164 
HIS ND1  N Y N 165 
HIS CD2  C Y N 166 
HIS CE1  C Y N 167 
HIS NE2  N Y N 168 
HIS OXT  O N N 169 
HIS H    H N N 170 
HIS H2   H N N 171 
HIS HA   H N N 172 
HIS HB2  H N N 173 
HIS HB3  H N N 174 
HIS HD1  H N N 175 
HIS HD2  H N N 176 
HIS HE1  H N N 177 
HIS HE2  H N N 178 
HIS HXT  H N N 179 
HOH O    O N N 180 
HOH H1   H N N 181 
HOH H2   H N N 182 
ILE N    N N N 183 
ILE CA   C N S 184 
ILE C    C N N 185 
ILE O    O N N 186 
ILE CB   C N S 187 
ILE CG1  C N N 188 
ILE CG2  C N N 189 
ILE CD1  C N N 190 
ILE OXT  O N N 191 
ILE H    H N N 192 
ILE H2   H N N 193 
ILE HA   H N N 194 
ILE HB   H N N 195 
ILE HG12 H N N 196 
ILE HG13 H N N 197 
ILE HG21 H N N 198 
ILE HG22 H N N 199 
ILE HG23 H N N 200 
ILE HD11 H N N 201 
ILE HD12 H N N 202 
ILE HD13 H N N 203 
ILE HXT  H N N 204 
IZP C1   C N N 205 
IZP O1   O N N 206 
IZP C2   C N N 207 
IZP O2   O N N 208 
IZP C3   C N N 209 
IZP C4   C N N 210 
IZP C5   C N N 211 
IZP C6   C N R 212 
IZP C7   C N N 213 
IZP C8   C Y N 214 
IZP C9   C Y N 215 
IZP C10  C Y N 216 
IZP C11  C Y N 217 
IZP C12  C Y N 218 
IZP C13  C Y N 219 
IZP HO1  H N N 220 
IZP H2   H N N 221 
IZP H2A  H N N 222 
IZP H3   H N N 223 
IZP H4   H N N 224 
IZP H4A  H N N 225 
IZP H4B  H N N 226 
IZP H5   H N N 227 
IZP H5A  H N N 228 
IZP H5B  H N N 229 
IZP H6   H N N 230 
IZP H7   H N N 231 
IZP H7A  H N N 232 
IZP H7B  H N N 233 
IZP H9   H N N 234 
IZP H10  H N N 235 
IZP H12  H N N 236 
IZP H13  H N N 237 
LEU N    N N N 238 
LEU CA   C N S 239 
LEU C    C N N 240 
LEU O    O N N 241 
LEU CB   C N N 242 
LEU CG   C N N 243 
LEU CD1  C N N 244 
LEU CD2  C N N 245 
LEU OXT  O N N 246 
LEU H    H N N 247 
LEU H2   H N N 248 
LEU HA   H N N 249 
LEU HB2  H N N 250 
LEU HB3  H N N 251 
LEU HG   H N N 252 
LEU HD11 H N N 253 
LEU HD12 H N N 254 
LEU HD13 H N N 255 
LEU HD21 H N N 256 
LEU HD22 H N N 257 
LEU HD23 H N N 258 
LEU HXT  H N N 259 
LYS N    N N N 260 
LYS CA   C N S 261 
LYS C    C N N 262 
LYS O    O N N 263 
LYS CB   C N N 264 
LYS CG   C N N 265 
LYS CD   C N N 266 
LYS CE   C N N 267 
LYS NZ   N N N 268 
LYS OXT  O N N 269 
LYS H    H N N 270 
LYS H2   H N N 271 
LYS HA   H N N 272 
LYS HB2  H N N 273 
LYS HB3  H N N 274 
LYS HG2  H N N 275 
LYS HG3  H N N 276 
LYS HD2  H N N 277 
LYS HD3  H N N 278 
LYS HE2  H N N 279 
LYS HE3  H N N 280 
LYS HZ1  H N N 281 
LYS HZ2  H N N 282 
LYS HZ3  H N N 283 
LYS HXT  H N N 284 
MET N    N N N 285 
MET CA   C N S 286 
MET C    C N N 287 
MET O    O N N 288 
MET CB   C N N 289 
MET CG   C N N 290 
MET SD   S N N 291 
MET CE   C N N 292 
MET OXT  O N N 293 
MET H    H N N 294 
MET H2   H N N 295 
MET HA   H N N 296 
MET HB2  H N N 297 
MET HB3  H N N 298 
MET HG2  H N N 299 
MET HG3  H N N 300 
MET HE1  H N N 301 
MET HE2  H N N 302 
MET HE3  H N N 303 
MET HXT  H N N 304 
PEG C1   C N N 305 
PEG O1   O N N 306 
PEG C2   C N N 307 
PEG O2   O N N 308 
PEG C3   C N N 309 
PEG C4   C N N 310 
PEG O4   O N N 311 
PEG H11  H N N 312 
PEG H12  H N N 313 
PEG HO1  H N N 314 
PEG H21  H N N 315 
PEG H22  H N N 316 
PEG H31  H N N 317 
PEG H32  H N N 318 
PEG H41  H N N 319 
PEG H42  H N N 320 
PEG HO4  H N N 321 
PG4 O1   O N N 322 
PG4 C1   C N N 323 
PG4 C2   C N N 324 
PG4 O2   O N N 325 
PG4 C3   C N N 326 
PG4 C4   C N N 327 
PG4 O3   O N N 328 
PG4 C5   C N N 329 
PG4 C6   C N N 330 
PG4 O4   O N N 331 
PG4 C7   C N N 332 
PG4 C8   C N N 333 
PG4 O5   O N N 334 
PG4 HO1  H N N 335 
PG4 H11  H N N 336 
PG4 H12  H N N 337 
PG4 H21  H N N 338 
PG4 H22  H N N 339 
PG4 H31  H N N 340 
PG4 H32  H N N 341 
PG4 H41  H N N 342 
PG4 H42  H N N 343 
PG4 H51  H N N 344 
PG4 H52  H N N 345 
PG4 H61  H N N 346 
PG4 H62  H N N 347 
PG4 H71  H N N 348 
PG4 H72  H N N 349 
PG4 H81  H N N 350 
PG4 H82  H N N 351 
PG4 HO5  H N N 352 
PGE C1   C N N 353 
PGE O1   O N N 354 
PGE C2   C N N 355 
PGE O2   O N N 356 
PGE C3   C N N 357 
PGE C4   C N N 358 
PGE O4   O N N 359 
PGE C6   C N N 360 
PGE C5   C N N 361 
PGE O3   O N N 362 
PGE H1   H N N 363 
PGE H12  H N N 364 
PGE HO1  H N N 365 
PGE H2   H N N 366 
PGE H22  H N N 367 
PGE H3   H N N 368 
PGE H32  H N N 369 
PGE H4   H N N 370 
PGE H42  H N N 371 
PGE HO4  H N N 372 
PGE H6   H N N 373 
PGE H62  H N N 374 
PGE H5   H N N 375 
PGE H52  H N N 376 
PHE N    N N N 377 
PHE CA   C N S 378 
PHE C    C N N 379 
PHE O    O N N 380 
PHE CB   C N N 381 
PHE CG   C Y N 382 
PHE CD1  C Y N 383 
PHE CD2  C Y N 384 
PHE CE1  C Y N 385 
PHE CE2  C Y N 386 
PHE CZ   C Y N 387 
PHE OXT  O N N 388 
PHE H    H N N 389 
PHE H2   H N N 390 
PHE HA   H N N 391 
PHE HB2  H N N 392 
PHE HB3  H N N 393 
PHE HD1  H N N 394 
PHE HD2  H N N 395 
PHE HE1  H N N 396 
PHE HE2  H N N 397 
PHE HZ   H N N 398 
PHE HXT  H N N 399 
PRO N    N N N 400 
PRO CA   C N S 401 
PRO C    C N N 402 
PRO O    O N N 403 
PRO CB   C N N 404 
PRO CG   C N N 405 
PRO CD   C N N 406 
PRO OXT  O N N 407 
PRO H    H N N 408 
PRO HA   H N N 409 
PRO HB2  H N N 410 
PRO HB3  H N N 411 
PRO HG2  H N N 412 
PRO HG3  H N N 413 
PRO HD2  H N N 414 
PRO HD3  H N N 415 
PRO HXT  H N N 416 
SER N    N N N 417 
SER CA   C N S 418 
SER C    C N N 419 
SER O    O N N 420 
SER CB   C N N 421 
SER OG   O N N 422 
SER OXT  O N N 423 
SER H    H N N 424 
SER H2   H N N 425 
SER HA   H N N 426 
SER HB2  H N N 427 
SER HB3  H N N 428 
SER HG   H N N 429 
SER HXT  H N N 430 
THR N    N N N 431 
THR CA   C N S 432 
THR C    C N N 433 
THR O    O N N 434 
THR CB   C N R 435 
THR OG1  O N N 436 
THR CG2  C N N 437 
THR OXT  O N N 438 
THR H    H N N 439 
THR H2   H N N 440 
THR HA   H N N 441 
THR HB   H N N 442 
THR HG1  H N N 443 
THR HG21 H N N 444 
THR HG22 H N N 445 
THR HG23 H N N 446 
THR HXT  H N N 447 
TRP N    N N N 448 
TRP CA   C N S 449 
TRP C    C N N 450 
TRP O    O N N 451 
TRP CB   C N N 452 
TRP CG   C Y N 453 
TRP CD1  C Y N 454 
TRP CD2  C Y N 455 
TRP NE1  N Y N 456 
TRP CE2  C Y N 457 
TRP CE3  C Y N 458 
TRP CZ2  C Y N 459 
TRP CZ3  C Y N 460 
TRP CH2  C Y N 461 
TRP OXT  O N N 462 
TRP H    H N N 463 
TRP H2   H N N 464 
TRP HA   H N N 465 
TRP HB2  H N N 466 
TRP HB3  H N N 467 
TRP HD1  H N N 468 
TRP HE1  H N N 469 
TRP HE3  H N N 470 
TRP HZ2  H N N 471 
TRP HZ3  H N N 472 
TRP HH2  H N N 473 
TRP HXT  H N N 474 
TYR N    N N N 475 
TYR CA   C N S 476 
TYR C    C N N 477 
TYR O    O N N 478 
TYR CB   C N N 479 
TYR CG   C Y N 480 
TYR CD1  C Y N 481 
TYR CD2  C Y N 482 
TYR CE1  C Y N 483 
TYR CE2  C Y N 484 
TYR CZ   C Y N 485 
TYR OH   O N N 486 
TYR OXT  O N N 487 
TYR H    H N N 488 
TYR H2   H N N 489 
TYR HA   H N N 490 
TYR HB2  H N N 491 
TYR HB3  H N N 492 
TYR HD1  H N N 493 
TYR HD2  H N N 494 
TYR HE1  H N N 495 
TYR HE2  H N N 496 
TYR HH   H N N 497 
TYR HXT  H N N 498 
VAL N    N N N 499 
VAL CA   C N S 500 
VAL C    C N N 501 
VAL O    O N N 502 
VAL CB   C N N 503 
VAL CG1  C N N 504 
VAL CG2  C N N 505 
VAL OXT  O N N 506 
VAL H    H N N 507 
VAL H2   H N N 508 
VAL HA   H N N 509 
VAL HB   H N N 510 
VAL HG11 H N N 511 
VAL HG12 H N N 512 
VAL HG13 H N N 513 
VAL HG21 H N N 514 
VAL HG22 H N N 515 
VAL HG23 H N N 516 
VAL HXT  H N N 517 
# 
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 
ACY C   O    doub N N 1   
ACY C   OXT  sing N N 2   
ACY C   CH3  sing N N 3   
ACY OXT HXT  sing N N 4   
ACY CH3 H1   sing N N 5   
ACY CH3 H2   sing N N 6   
ACY CH3 H3   sing N N 7   
ALA N   CA   sing N N 8   
ALA N   H    sing N N 9   
ALA N   H2   sing N N 10  
ALA CA  C    sing N N 11  
ALA CA  CB   sing N N 12  
ALA CA  HA   sing N N 13  
ALA C   O    doub N N 14  
ALA C   OXT  sing N N 15  
ALA CB  HB1  sing N N 16  
ALA CB  HB2  sing N N 17  
ALA CB  HB3  sing N N 18  
ALA OXT HXT  sing N N 19  
ARG N   CA   sing N N 20  
ARG N   H    sing N N 21  
ARG N   H2   sing N N 22  
ARG CA  C    sing N N 23  
ARG CA  CB   sing N N 24  
ARG CA  HA   sing N N 25  
ARG C   O    doub N N 26  
ARG C   OXT  sing N N 27  
ARG CB  CG   sing N N 28  
ARG CB  HB2  sing N N 29  
ARG CB  HB3  sing N N 30  
ARG CG  CD   sing N N 31  
ARG CG  HG2  sing N N 32  
ARG CG  HG3  sing N N 33  
ARG CD  NE   sing N N 34  
ARG CD  HD2  sing N N 35  
ARG CD  HD3  sing N N 36  
ARG NE  CZ   sing N N 37  
ARG NE  HE   sing N N 38  
ARG CZ  NH1  sing N N 39  
ARG CZ  NH2  doub N N 40  
ARG NH1 HH11 sing N N 41  
ARG NH1 HH12 sing N N 42  
ARG NH2 HH21 sing N N 43  
ARG NH2 HH22 sing N N 44  
ARG OXT HXT  sing N N 45  
ASN N   CA   sing N N 46  
ASN N   H    sing N N 47  
ASN N   H2   sing N N 48  
ASN CA  C    sing N N 49  
ASN CA  CB   sing N N 50  
ASN CA  HA   sing N N 51  
ASN C   O    doub N N 52  
ASN C   OXT  sing N N 53  
ASN CB  CG   sing N N 54  
ASN CB  HB2  sing N N 55  
ASN CB  HB3  sing N N 56  
ASN CG  OD1  doub N N 57  
ASN CG  ND2  sing N N 58  
ASN ND2 HD21 sing N N 59  
ASN ND2 HD22 sing N N 60  
ASN OXT HXT  sing N N 61  
ASP N   CA   sing N N 62  
ASP N   H    sing N N 63  
ASP N   H2   sing N N 64  
ASP CA  C    sing N N 65  
ASP CA  CB   sing N N 66  
ASP CA  HA   sing N N 67  
ASP C   O    doub N N 68  
ASP C   OXT  sing N N 69  
ASP CB  CG   sing N N 70  
ASP CB  HB2  sing N N 71  
ASP CB  HB3  sing N N 72  
ASP CG  OD1  doub N N 73  
ASP CG  OD2  sing N N 74  
ASP OD2 HD2  sing N N 75  
ASP OXT HXT  sing N N 76  
CYS N   CA   sing N N 77  
CYS N   H    sing N N 78  
CYS N   H2   sing N N 79  
CYS CA  C    sing N N 80  
CYS CA  CB   sing N N 81  
CYS CA  HA   sing N N 82  
CYS C   O    doub N N 83  
CYS C   OXT  sing N N 84  
CYS CB  SG   sing N N 85  
CYS CB  HB2  sing N N 86  
CYS CB  HB3  sing N N 87  
CYS SG  HG   sing N N 88  
CYS OXT HXT  sing N N 89  
GLN N   CA   sing N N 90  
GLN N   H    sing N N 91  
GLN N   H2   sing N N 92  
GLN CA  C    sing N N 93  
GLN CA  CB   sing N N 94  
GLN CA  HA   sing N N 95  
GLN C   O    doub N N 96  
GLN C   OXT  sing N N 97  
GLN CB  CG   sing N N 98  
GLN CB  HB2  sing N N 99  
GLN CB  HB3  sing N N 100 
GLN CG  CD   sing N N 101 
GLN CG  HG2  sing N N 102 
GLN CG  HG3  sing N N 103 
GLN CD  OE1  doub N N 104 
GLN CD  NE2  sing N N 105 
GLN NE2 HE21 sing N N 106 
GLN NE2 HE22 sing N N 107 
GLN OXT HXT  sing N N 108 
GLU N   CA   sing N N 109 
GLU N   H    sing N N 110 
GLU N   H2   sing N N 111 
GLU CA  C    sing N N 112 
GLU CA  CB   sing N N 113 
GLU CA  HA   sing N N 114 
GLU C   O    doub N N 115 
GLU C   OXT  sing N N 116 
GLU CB  CG   sing N N 117 
GLU CB  HB2  sing N N 118 
GLU CB  HB3  sing N N 119 
GLU CG  CD   sing N N 120 
GLU CG  HG2  sing N N 121 
GLU CG  HG3  sing N N 122 
GLU CD  OE1  doub N N 123 
GLU CD  OE2  sing N N 124 
GLU OE2 HE2  sing N N 125 
GLU OXT HXT  sing N N 126 
GLY N   CA   sing N N 127 
GLY N   H    sing N N 128 
GLY N   H2   sing N N 129 
GLY CA  C    sing N N 130 
GLY CA  HA2  sing N N 131 
GLY CA  HA3  sing N N 132 
GLY C   O    doub N N 133 
GLY C   OXT  sing N N 134 
GLY OXT HXT  sing N N 135 
GOL C1  O1   sing N N 136 
GOL C1  C2   sing N N 137 
GOL C1  H11  sing N N 138 
GOL C1  H12  sing N N 139 
GOL O1  HO1  sing N N 140 
GOL C2  O2   sing N N 141 
GOL C2  C3   sing N N 142 
GOL C2  H2   sing N N 143 
GOL O2  HO2  sing N N 144 
GOL C3  O3   sing N N 145 
GOL C3  H31  sing N N 146 
GOL C3  H32  sing N N 147 
GOL O3  HO3  sing N N 148 
HIS N   CA   sing N N 149 
HIS N   H    sing N N 150 
HIS N   H2   sing N N 151 
HIS CA  C    sing N N 152 
HIS CA  CB   sing N N 153 
HIS CA  HA   sing N N 154 
HIS C   O    doub N N 155 
HIS C   OXT  sing N N 156 
HIS CB  CG   sing N N 157 
HIS CB  HB2  sing N N 158 
HIS CB  HB3  sing N N 159 
HIS CG  ND1  sing Y N 160 
HIS CG  CD2  doub Y N 161 
HIS ND1 CE1  doub Y N 162 
HIS ND1 HD1  sing N N 163 
HIS CD2 NE2  sing Y N 164 
HIS CD2 HD2  sing N N 165 
HIS CE1 NE2  sing Y N 166 
HIS CE1 HE1  sing N N 167 
HIS NE2 HE2  sing N N 168 
HIS OXT HXT  sing N N 169 
HOH O   H1   sing N N 170 
HOH O   H2   sing N N 171 
ILE N   CA   sing N N 172 
ILE N   H    sing N N 173 
ILE N   H2   sing N N 174 
ILE CA  C    sing N N 175 
ILE CA  CB   sing N N 176 
ILE CA  HA   sing N N 177 
ILE C   O    doub N N 178 
ILE C   OXT  sing N N 179 
ILE CB  CG1  sing N N 180 
ILE CB  CG2  sing N N 181 
ILE CB  HB   sing N N 182 
ILE CG1 CD1  sing N N 183 
ILE CG1 HG12 sing N N 184 
ILE CG1 HG13 sing N N 185 
ILE CG2 HG21 sing N N 186 
ILE CG2 HG22 sing N N 187 
ILE CG2 HG23 sing N N 188 
ILE CD1 HD11 sing N N 189 
ILE CD1 HD12 sing N N 190 
ILE CD1 HD13 sing N N 191 
ILE OXT HXT  sing N N 192 
IZP O2  C1   doub N N 193 
IZP C1  C6   sing N N 194 
IZP C1  O1   sing N N 195 
IZP O1  HO1  sing N N 196 
IZP C11 C2   sing N N 197 
IZP C2  C3   sing N N 198 
IZP C2  H2   sing N N 199 
IZP C2  H2A  sing N N 200 
IZP C3  C4   sing N N 201 
IZP C3  C5   sing N N 202 
IZP C3  H3   sing N N 203 
IZP C4  H4   sing N N 204 
IZP C4  H4A  sing N N 205 
IZP C4  H4B  sing N N 206 
IZP C5  H5   sing N N 207 
IZP C5  H5A  sing N N 208 
IZP C5  H5B  sing N N 209 
IZP C7  C6   sing N N 210 
IZP C6  C8   sing N N 211 
IZP C6  H6   sing N N 212 
IZP C7  H7   sing N N 213 
IZP C7  H7A  sing N N 214 
IZP C7  H7B  sing N N 215 
IZP C8  C13  doub Y N 216 
IZP C8  C9   sing Y N 217 
IZP C9  C10  doub Y N 218 
IZP C9  H9   sing N N 219 
IZP C10 C11  sing Y N 220 
IZP C10 H10  sing N N 221 
IZP C12 C11  doub Y N 222 
IZP C13 C12  sing Y N 223 
IZP C12 H12  sing N N 224 
IZP C13 H13  sing N N 225 
LEU N   CA   sing N N 226 
LEU N   H    sing N N 227 
LEU N   H2   sing N N 228 
LEU CA  C    sing N N 229 
LEU CA  CB   sing N N 230 
LEU CA  HA   sing N N 231 
LEU C   O    doub N N 232 
LEU C   OXT  sing N N 233 
LEU CB  CG   sing N N 234 
LEU CB  HB2  sing N N 235 
LEU CB  HB3  sing N N 236 
LEU CG  CD1  sing N N 237 
LEU CG  CD2  sing N N 238 
LEU CG  HG   sing N N 239 
LEU CD1 HD11 sing N N 240 
LEU CD1 HD12 sing N N 241 
LEU CD1 HD13 sing N N 242 
LEU CD2 HD21 sing N N 243 
LEU CD2 HD22 sing N N 244 
LEU CD2 HD23 sing N N 245 
LEU OXT HXT  sing N N 246 
LYS N   CA   sing N N 247 
LYS N   H    sing N N 248 
LYS N   H2   sing N N 249 
LYS CA  C    sing N N 250 
LYS CA  CB   sing N N 251 
LYS CA  HA   sing N N 252 
LYS C   O    doub N N 253 
LYS C   OXT  sing N N 254 
LYS CB  CG   sing N N 255 
LYS CB  HB2  sing N N 256 
LYS CB  HB3  sing N N 257 
LYS CG  CD   sing N N 258 
LYS CG  HG2  sing N N 259 
LYS CG  HG3  sing N N 260 
LYS CD  CE   sing N N 261 
LYS CD  HD2  sing N N 262 
LYS CD  HD3  sing N N 263 
LYS CE  NZ   sing N N 264 
LYS CE  HE2  sing N N 265 
LYS CE  HE3  sing N N 266 
LYS NZ  HZ1  sing N N 267 
LYS NZ  HZ2  sing N N 268 
LYS NZ  HZ3  sing N N 269 
LYS OXT HXT  sing N N 270 
MET N   CA   sing N N 271 
MET N   H    sing N N 272 
MET N   H2   sing N N 273 
MET CA  C    sing N N 274 
MET CA  CB   sing N N 275 
MET CA  HA   sing N N 276 
MET C   O    doub N N 277 
MET C   OXT  sing N N 278 
MET CB  CG   sing N N 279 
MET CB  HB2  sing N N 280 
MET CB  HB3  sing N N 281 
MET CG  SD   sing N N 282 
MET CG  HG2  sing N N 283 
MET CG  HG3  sing N N 284 
MET SD  CE   sing N N 285 
MET CE  HE1  sing N N 286 
MET CE  HE2  sing N N 287 
MET CE  HE3  sing N N 288 
MET OXT HXT  sing N N 289 
PEG C1  O1   sing N N 290 
PEG C1  C2   sing N N 291 
PEG C1  H11  sing N N 292 
PEG C1  H12  sing N N 293 
PEG O1  HO1  sing N N 294 
PEG C2  O2   sing N N 295 
PEG C2  H21  sing N N 296 
PEG C2  H22  sing N N 297 
PEG O2  C3   sing N N 298 
PEG C3  C4   sing N N 299 
PEG C3  H31  sing N N 300 
PEG C3  H32  sing N N 301 
PEG C4  O4   sing N N 302 
PEG C4  H41  sing N N 303 
PEG C4  H42  sing N N 304 
PEG O4  HO4  sing N N 305 
PG4 O1  C1   sing N N 306 
PG4 O1  HO1  sing N N 307 
PG4 C1  C2   sing N N 308 
PG4 C1  H11  sing N N 309 
PG4 C1  H12  sing N N 310 
PG4 C2  O2   sing N N 311 
PG4 C2  H21  sing N N 312 
PG4 C2  H22  sing N N 313 
PG4 O2  C3   sing N N 314 
PG4 C3  C4   sing N N 315 
PG4 C3  H31  sing N N 316 
PG4 C3  H32  sing N N 317 
PG4 C4  O3   sing N N 318 
PG4 C4  H41  sing N N 319 
PG4 C4  H42  sing N N 320 
PG4 O3  C5   sing N N 321 
PG4 C5  C6   sing N N 322 
PG4 C5  H51  sing N N 323 
PG4 C5  H52  sing N N 324 
PG4 C6  O4   sing N N 325 
PG4 C6  H61  sing N N 326 
PG4 C6  H62  sing N N 327 
PG4 O4  C7   sing N N 328 
PG4 C7  C8   sing N N 329 
PG4 C7  H71  sing N N 330 
PG4 C7  H72  sing N N 331 
PG4 C8  O5   sing N N 332 
PG4 C8  H81  sing N N 333 
PG4 C8  H82  sing N N 334 
PG4 O5  HO5  sing N N 335 
PGE C1  O1   sing N N 336 
PGE C1  C2   sing N N 337 
PGE C1  H1   sing N N 338 
PGE C1  H12  sing N N 339 
PGE O1  HO1  sing N N 340 
PGE C2  O2   sing N N 341 
PGE C2  H2   sing N N 342 
PGE C2  H22  sing N N 343 
PGE O2  C3   sing N N 344 
PGE C3  C4   sing N N 345 
PGE C3  H3   sing N N 346 
PGE C3  H32  sing N N 347 
PGE C4  O3   sing N N 348 
PGE C4  H4   sing N N 349 
PGE C4  H42  sing N N 350 
PGE O4  C6   sing N N 351 
PGE O4  HO4  sing N N 352 
PGE C6  C5   sing N N 353 
PGE C6  H6   sing N N 354 
PGE C6  H62  sing N N 355 
PGE C5  O3   sing N N 356 
PGE C5  H5   sing N N 357 
PGE C5  H52  sing N N 358 
PHE N   CA   sing N N 359 
PHE N   H    sing N N 360 
PHE N   H2   sing N N 361 
PHE CA  C    sing N N 362 
PHE CA  CB   sing N N 363 
PHE CA  HA   sing N N 364 
PHE C   O    doub N N 365 
PHE C   OXT  sing N N 366 
PHE CB  CG   sing N N 367 
PHE CB  HB2  sing N N 368 
PHE CB  HB3  sing N N 369 
PHE CG  CD1  doub Y N 370 
PHE CG  CD2  sing Y N 371 
PHE CD1 CE1  sing Y N 372 
PHE CD1 HD1  sing N N 373 
PHE CD2 CE2  doub Y N 374 
PHE CD2 HD2  sing N N 375 
PHE CE1 CZ   doub Y N 376 
PHE CE1 HE1  sing N N 377 
PHE CE2 CZ   sing Y N 378 
PHE CE2 HE2  sing N N 379 
PHE CZ  HZ   sing N N 380 
PHE OXT HXT  sing N N 381 
PRO N   CA   sing N N 382 
PRO N   CD   sing N N 383 
PRO N   H    sing N N 384 
PRO CA  C    sing N N 385 
PRO CA  CB   sing N N 386 
PRO CA  HA   sing N N 387 
PRO C   O    doub N N 388 
PRO C   OXT  sing N N 389 
PRO CB  CG   sing N N 390 
PRO CB  HB2  sing N N 391 
PRO CB  HB3  sing N N 392 
PRO CG  CD   sing N N 393 
PRO CG  HG2  sing N N 394 
PRO CG  HG3  sing N N 395 
PRO CD  HD2  sing N N 396 
PRO CD  HD3  sing N N 397 
PRO OXT HXT  sing N N 398 
SER N   CA   sing N N 399 
SER N   H    sing N N 400 
SER N   H2   sing N N 401 
SER CA  C    sing N N 402 
SER CA  CB   sing N N 403 
SER CA  HA   sing N N 404 
SER C   O    doub N N 405 
SER C   OXT  sing N N 406 
SER CB  OG   sing N N 407 
SER CB  HB2  sing N N 408 
SER CB  HB3  sing N N 409 
SER OG  HG   sing N N 410 
SER OXT HXT  sing N N 411 
THR N   CA   sing N N 412 
THR N   H    sing N N 413 
THR N   H2   sing N N 414 
THR CA  C    sing N N 415 
THR CA  CB   sing N N 416 
THR CA  HA   sing N N 417 
THR C   O    doub N N 418 
THR C   OXT  sing N N 419 
THR CB  OG1  sing N N 420 
THR CB  CG2  sing N N 421 
THR CB  HB   sing N N 422 
THR OG1 HG1  sing N N 423 
THR CG2 HG21 sing N N 424 
THR CG2 HG22 sing N N 425 
THR CG2 HG23 sing N N 426 
THR OXT HXT  sing N N 427 
TRP N   CA   sing N N 428 
TRP N   H    sing N N 429 
TRP N   H2   sing N N 430 
TRP CA  C    sing N N 431 
TRP CA  CB   sing N N 432 
TRP CA  HA   sing N N 433 
TRP C   O    doub N N 434 
TRP C   OXT  sing N N 435 
TRP CB  CG   sing N N 436 
TRP CB  HB2  sing N N 437 
TRP CB  HB3  sing N N 438 
TRP CG  CD1  doub Y N 439 
TRP CG  CD2  sing Y N 440 
TRP CD1 NE1  sing Y N 441 
TRP CD1 HD1  sing N N 442 
TRP CD2 CE2  doub Y N 443 
TRP CD2 CE3  sing Y N 444 
TRP NE1 CE2  sing Y N 445 
TRP NE1 HE1  sing N N 446 
TRP CE2 CZ2  sing Y N 447 
TRP CE3 CZ3  doub Y N 448 
TRP CE3 HE3  sing N N 449 
TRP CZ2 CH2  doub Y N 450 
TRP CZ2 HZ2  sing N N 451 
TRP CZ3 CH2  sing Y N 452 
TRP CZ3 HZ3  sing N N 453 
TRP CH2 HH2  sing N N 454 
TRP OXT HXT  sing N N 455 
TYR N   CA   sing N N 456 
TYR N   H    sing N N 457 
TYR N   H2   sing N N 458 
TYR CA  C    sing N N 459 
TYR CA  CB   sing N N 460 
TYR CA  HA   sing N N 461 
TYR C   O    doub N N 462 
TYR C   OXT  sing N N 463 
TYR CB  CG   sing N N 464 
TYR CB  HB2  sing N N 465 
TYR CB  HB3  sing N N 466 
TYR CG  CD1  doub Y N 467 
TYR CG  CD2  sing Y N 468 
TYR CD1 CE1  sing Y N 469 
TYR CD1 HD1  sing N N 470 
TYR CD2 CE2  doub Y N 471 
TYR CD2 HD2  sing N N 472 
TYR CE1 CZ   doub Y N 473 
TYR CE1 HE1  sing N N 474 
TYR CE2 CZ   sing Y N 475 
TYR CE2 HE2  sing N N 476 
TYR CZ  OH   sing N N 477 
TYR OH  HH   sing N N 478 
TYR OXT HXT  sing N N 479 
VAL N   CA   sing N N 480 
VAL N   H    sing N N 481 
VAL N   H2   sing N N 482 
VAL CA  C    sing N N 483 
VAL CA  CB   sing N N 484 
VAL CA  HA   sing N N 485 
VAL C   O    doub N N 486 
VAL C   OXT  sing N N 487 
VAL CB  CG1  sing N N 488 
VAL CB  CG2  sing N N 489 
VAL CB  HB   sing N N 490 
VAL CG1 HG11 sing N N 491 
VAL CG1 HG12 sing N N 492 
VAL CG1 HG13 sing N N 493 
VAL CG2 HG21 sing N N 494 
VAL CG2 HG22 sing N N 495 
VAL CG2 HG23 sing N N 496 
VAL OXT HXT  sing N N 497 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Japan Science and Technology'                      Japan JPMJER1005 1 
'Japan Science and Technology'                      Japan JPMJTM19DC 2 
'Other private'                                     Japan 09-003-005 3 
'Japan Society for the Promotion of Science (JSPS)' Japan 19K06588   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   3WVM 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZCI 
_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]   0.014451 
_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]   0.009271 
_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]   0.020770 
_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 
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   . MET A 1 1   ? 34.106 5.652  3.518   1.00 47.10  ? 0   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 34.146 5.143  2.112   1.00 49.03  ? 0   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 32.791 5.424  1.456   1.00 38.13  ? 0   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 31.812 5.711  2.209   1.00 36.49  ? 0   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 34.512 3.673  2.098   1.00 53.78  ? 0   MET A CB  1 
ATOM   6    N N   . VAL A 1 2   ? 32.760 5.429  0.116   1.00 49.53  ? 1   VAL A N   1 
ATOM   7    C CA  . VAL A 1 2   ? 31.576 5.732  -0.761  1.00 49.84  ? 1   VAL A CA  1 
ATOM   8    C C   . VAL A 1 2   ? 30.343 4.956  -0.276  1.00 35.20  ? 1   VAL A C   1 
ATOM   9    O O   . VAL A 1 2   ? 29.190 5.408  -0.403  1.00 30.16  ? 1   VAL A O   1 
ATOM   10   C CB  . VAL A 1 2   ? 31.854 5.320  -2.219  1.00 80.58  ? 1   VAL A CB  1 
ATOM   11   C CG1 . VAL A 1 2   ? 30.891 6.016  -3.169  1.00 92.01  ? 1   VAL A CG1 1 
ATOM   12   C CG2 . VAL A 1 2   ? 33.301 5.538  -2.634  1.00 152.26 ? 1   VAL A CG2 1 
ATOM   13   N N   . ASP A 1 3   ? 30.580 3.764  0.223   1.00 26.52  ? 2   ASP A N   1 
ATOM   14   C CA  . ASP A 1 3   ? 29.513 2.839  0.659   1.00 27.91  ? 2   ASP A CA  1 
ATOM   15   C C   . ASP A 1 3   ? 28.665 3.480  1.749   1.00 23.17  ? 2   ASP A C   1 
ATOM   16   O O   . ASP A 1 3   ? 27.494 3.141  1.811   1.00 26.40  ? 2   ASP A O   1 
ATOM   17   C CB  . ASP A 1 3   ? 30.087 1.505  1.126   1.00 35.30  ? 2   ASP A CB  1 
ATOM   18   C CG  . ASP A 1 3   ? 30.819 1.550  2.463   1.00 43.90  ? 2   ASP A CG  1 
ATOM   19   O OD1 . ASP A 1 3   ? 31.875 2.210  2.544   1.00 66.90  ? 2   ASP A OD1 1 
ATOM   20   O OD2 . ASP A 1 3   ? 30.346 0.909  3.401   1.00 58.18  ? 2   ASP A OD2 1 
ATOM   21   N N   . ALA A 1 4   ? 29.212 4.400  2.546   1.00 21.64  ? 3   ALA A N   1 
ATOM   22   C CA  . ALA A 1 4   ? 28.451 5.023  3.648   1.00 22.66  ? 3   ALA A CA  1 
ATOM   23   C C   . ALA A 1 4   ? 27.317 5.917  3.111   1.00 18.13  ? 3   ALA A C   1 
ATOM   24   O O   . ALA A 1 4   ? 26.405 6.186  3.850   1.00 20.06  ? 3   ALA A O   1 
ATOM   25   C CB  . ALA A 1 4   ? 29.392 5.762  4.542   1.00 28.10  ? 3   ALA A CB  1 
ATOM   26   N N   . PHE A 1 5   ? 27.351 6.306  1.851   1.00 16.93  ? 4   PHE A N   1 
ATOM   27   C CA  . PHE A 1 5   ? 26.237 7.061  1.243   1.00 16.40  ? 4   PHE A CA  1 
ATOM   28   C C   . PHE A 1 5   ? 25.069 6.149  0.867   1.00 17.15  ? 4   PHE A C   1 
ATOM   29   O O   . PHE A 1 5   ? 23.961 6.641  0.656   1.00 17.04  ? 4   PHE A O   1 
ATOM   30   C CB  . PHE A 1 5   ? 26.692 7.810  -0.011  1.00 15.30  ? 4   PHE A CB  1 
ATOM   31   C CG  . PHE A 1 5   ? 27.626 8.953  0.278   1.00 14.98  ? 4   PHE A CG  1 
ATOM   32   C CD1 . PHE A 1 5   ? 27.137 10.112 0.822   1.00 16.84  ? 4   PHE A CD1 1 
ATOM   33   C CD2 . PHE A 1 5   ? 28.970 8.887  0.007   1.00 18.07  ? 4   PHE A CD2 1 
ATOM   34   C CE1 . PHE A 1 5   ? 27.963 11.176 1.099   1.00 16.86  ? 4   PHE A CE1 1 
ATOM   35   C CE2 . PHE A 1 5   ? 29.807 9.964  0.300   1.00 18.42  ? 4   PHE A CE2 1 
ATOM   36   C CZ  . PHE A 1 5   ? 29.302 11.093 0.861   1.00 16.48  ? 4   PHE A CZ  1 
ATOM   37   N N   . LEU A 1 6   ? 25.330 4.847  0.679   1.00 16.92  ? 5   LEU A N   1 
ATOM   38   C CA  . LEU A 1 6   ? 24.282 3.931  0.182   1.00 17.78  ? 5   LEU A CA  1 
ATOM   39   C C   . LEU A 1 6   ? 23.203 3.755  1.235   1.00 19.94  ? 5   LEU A C   1 
ATOM   40   O O   . LEU A 1 6   ? 23.506 3.631  2.422   1.00 20.84  ? 5   LEU A O   1 
ATOM   41   C CB  . LEU A 1 6   ? 24.892 2.594  -0.215  1.00 18.77  ? 5   LEU A CB  1 
ATOM   42   C CG  . LEU A 1 6   ? 25.996 2.663  -1.263  1.00 19.40  ? 5   LEU A CG  1 
ATOM   43   C CD1 . LEU A 1 6   ? 26.579 1.292  -1.477  1.00 23.95  ? 5   LEU A CD1 1 
ATOM   44   C CD2 . LEU A 1 6   ? 25.440 3.263  -2.560  1.00 24.66  ? 5   LEU A CD2 1 
ATOM   45   N N   . GLY A 1 7   ? 21.970 3.715  0.760   1.00 18.96  ? 6   GLY A N   1 
ATOM   46   C CA  . GLY A 1 7   ? 20.807 3.443  1.602   1.00 20.42  ? 6   GLY A CA  1 
ATOM   47   C C   . GLY A 1 7   ? 19.730 4.479  1.406   1.00 18.48  ? 6   GLY A C   1 
ATOM   48   O O   . GLY A 1 7   ? 19.707 5.163  0.377   1.00 19.33  ? 6   GLY A O   1 
ATOM   49   N N   . THR A 1 8   ? 18.840 4.557  2.380   1.00 19.89  ? 7   THR A N   1 
ATOM   50   C CA  . THR A 1 8   ? 17.583 5.330  2.295   1.00 18.45  ? 7   THR A CA  1 
ATOM   51   C C   . THR A 1 8   ? 17.663 6.419  3.352   1.00 19.98  ? 7   THR A C   1 
ATOM   52   O O   . THR A 1 8   ? 17.945 6.127  4.521   1.00 23.13  ? 7   THR A O   1 
ATOM   53   C CB  . THR A 1 8   ? 16.351 4.442  2.454   1.00 21.09  ? 7   THR A CB  1 
ATOM   54   O OG1 . THR A 1 8   ? 16.292 3.436  1.446   1.00 22.69  ? 7   THR A OG1 1 
ATOM   55   C CG2 . THR A 1 8   ? 15.069 5.247  2.372   1.00 23.43  ? 7   THR A CG2 1 
ATOM   56   N N   . TRP A 1 9   ? 17.471 7.655  2.900   1.00 19.91  ? 8   TRP A N   1 
ATOM   57   C CA  . TRP A 1 9   ? 17.659 8.855  3.721   1.00 19.14  ? 8   TRP A CA  1 
ATOM   58   C C   . TRP A 1 9   ? 16.376 9.685  3.724   1.00 18.86  ? 8   TRP A C   1 
ATOM   59   O O   . TRP A 1 9   ? 15.759 9.882  2.638   1.00 21.87  ? 8   TRP A O   1 
ATOM   60   C CB  . TRP A 1 9   ? 18.792 9.657  3.125   1.00 18.93  ? 8   TRP A CB  1 
ATOM   61   C CG  . TRP A 1 9   ? 20.098 8.930  3.049   1.00 18.22  ? 8   TRP A CG  1 
ATOM   62   C CD1 . TRP A 1 9   ? 20.591 8.218  1.998   1.00 17.74  ? 8   TRP A CD1 1 
ATOM   63   C CD2 . TRP A 1 9   ? 21.098 8.881  4.070   1.00 17.37  ? 8   TRP A CD2 1 
ATOM   64   N NE1 . TRP A 1 9   ? 21.840 7.734  2.298   1.00 18.77  ? 8   TRP A NE1 1 
ATOM   65   C CE2 . TRP A 1 9   ? 22.166 8.093  3.580   1.00 18.15  ? 8   TRP A CE2 1 
ATOM   66   C CE3 . TRP A 1 9   ? 21.176 9.401  5.356   1.00 20.11  ? 8   TRP A CE3 1 
ATOM   67   C CZ2 . TRP A 1 9   ? 23.323 7.875  4.318   1.00 20.11  ? 8   TRP A CZ2 1 
ATOM   68   C CZ3 . TRP A 1 9   ? 22.310 9.158  6.106   1.00 20.05  ? 8   TRP A CZ3 1 
ATOM   69   C CH2 . TRP A 1 9   ? 23.377 8.427  5.583   1.00 20.05  ? 8   TRP A CH2 1 
ATOM   70   N N   A LYS A 1 10  ? 16.029 10.208 4.897   0.60 18.21  ? 9   LYS A N   1 
ATOM   71   N N   B LYS A 1 10  ? 15.933 10.142 4.897   0.20 18.19  ? 9   LYS A N   1 
ATOM   72   C CA  A LYS A 1 10  ? 14.796 10.998 5.083   0.60 19.25  ? 9   LYS A CA  1 
ATOM   73   C CA  B LYS A 1 10  ? 14.721 10.995 4.996   0.20 18.25  ? 9   LYS A CA  1 
ATOM   74   C C   A LYS A 1 10  ? 15.167 12.413 5.522   0.60 16.70  ? 9   LYS A C   1 
ATOM   75   C C   B LYS A 1 10  ? 15.109 12.375 5.524   0.20 17.65  ? 9   LYS A C   1 
ATOM   76   O O   A LYS A 1 10  ? 15.999 12.578 6.413   0.60 17.29  ? 9   LYS A O   1 
ATOM   77   O O   B LYS A 1 10  ? 15.941 12.454 6.440   0.20 17.67  ? 9   LYS A O   1 
ATOM   78   C CB  A LYS A 1 10  ? 13.864 10.316 6.089   0.60 22.38  ? 9   LYS A CB  1 
ATOM   79   C CB  B LYS A 1 10  ? 13.626 10.373 5.868   0.20 17.62  ? 9   LYS A CB  1 
ATOM   80   C CG  A LYS A 1 10  ? 12.639 11.129 6.476   0.60 30.86  ? 9   LYS A CG  1 
ATOM   81   C CG  B LYS A 1 10  ? 12.250 10.972 5.602   0.20 18.33  ? 9   LYS A CG  1 
ATOM   82   C CD  A LYS A 1 10  ? 11.450 11.027 5.536   0.60 37.81  ? 9   LYS A CD  1 
ATOM   83   C CD  B LYS A 1 10  ? 11.154 10.619 6.590   0.20 20.25  ? 9   LYS A CD  1 
ATOM   84   C CE  A LYS A 1 10  ? 10.225 11.678 6.137   0.60 44.25  ? 9   LYS A CE  1 
ATOM   85   C CE  B LYS A 1 10  ? 9.944  11.504 6.394   0.20 21.27  ? 9   LYS A CE  1 
ATOM   86   N NZ  A LYS A 1 10  ? 9.032  11.525 5.272   0.60 55.78  ? 9   LYS A NZ  1 
ATOM   87   N NZ  B LYS A 1 10  ? 9.583  11.608 4.959   0.20 22.24  ? 9   LYS A NZ  1 
ATOM   88   N N   . LEU A 1 11  ? 14.488 13.423 4.974   1.00 20.27  ? 10  LEU A N   1 
ATOM   89   C CA  . LEU A 1 11  ? 14.802 14.820 5.356   1.00 18.69  ? 10  LEU A CA  1 
ATOM   90   C C   . LEU A 1 11  ? 14.347 15.061 6.796   1.00 19.72  ? 10  LEU A C   1 
ATOM   91   O O   . LEU A 1 11  ? 13.189 14.725 7.133   1.00 22.86  ? 10  LEU A O   1 
ATOM   92   C CB  . LEU A 1 11  ? 14.068 15.782 4.433   1.00 19.73  ? 10  LEU A CB  1 
ATOM   93   C CG  . LEU A 1 11  ? 14.415 17.245 4.668   1.00 19.02  ? 10  LEU A CG  1 
ATOM   94   C CD1 . LEU A 1 11  ? 15.719 17.594 3.966   1.00 19.55  ? 10  LEU A CD1 1 
ATOM   95   C CD2 . LEU A 1 11  ? 13.278 18.177 4.206   1.00 19.68  ? 10  LEU A CD2 1 
ATOM   96   N N   . VAL A 1 12  ? 15.224 15.611 7.627   1.00 20.04  ? 11  VAL A N   1 
ATOM   97   C CA  . VAL A 1 12  ? 14.867 16.006 9.016   1.00 23.23  ? 11  VAL A CA  1 
ATOM   98   C C   . VAL A 1 12  ? 15.075 17.504 9.266   1.00 22.05  ? 11  VAL A C   1 
ATOM   99   O O   . VAL A 1 12  ? 14.582 17.988 10.277  1.00 25.48  ? 11  VAL A O   1 
ATOM   100  C CB  . VAL A 1 12  ? 15.631 15.156 10.036  1.00 22.53  ? 11  VAL A CB  1 
ATOM   101  C CG1 . VAL A 1 12  ? 15.290 13.679 9.895   1.00 25.76  ? 11  VAL A CG1 1 
ATOM   102  C CG2 . VAL A 1 12  ? 17.126 15.383 9.962   1.00 25.15  ? 11  VAL A CG2 1 
ATOM   103  N N   . ASP A 1 13  ? 15.774 18.245 8.414   1.00 18.78  ? 12  ASP A N   1 
ATOM   104  C CA  . ASP A 1 13  ? 15.912 19.704 8.617   1.00 20.16  ? 12  ASP A CA  1 
ATOM   105  C C   . ASP A 1 13  ? 16.210 20.370 7.280   1.00 17.08  ? 12  ASP A C   1 
ATOM   106  O O   . ASP A 1 13  ? 16.677 19.716 6.355   1.00 16.79  ? 12  ASP A O   1 
ATOM   107  C CB  . ASP A 1 13  ? 16.991 20.032 9.644   1.00 21.49  ? 12  ASP A CB  1 
ATOM   108  C CG  . ASP A 1 13  ? 16.839 21.384 10.314  1.00 26.82  ? 12  ASP A CG  1 
ATOM   109  O OD1 . ASP A 1 13  ? 15.810 22.079 10.046  1.00 26.71  ? 12  ASP A OD1 1 
ATOM   110  O OD2 . ASP A 1 13  ? 17.782 21.757 11.054  1.00 28.99  ? 12  ASP A OD2 1 
ATOM   111  N N   . SER A 1 14  ? 15.915 21.658 7.206   1.00 18.48  ? 13  SER A N   1 
ATOM   112  C CA  . SER A 1 14  ? 16.213 22.456 6.002   1.00 16.64  ? 13  SER A CA  1 
ATOM   113  C C   . SER A 1 14  ? 16.431 23.911 6.400   1.00 17.65  ? 13  SER A C   1 
ATOM   114  O O   . SER A 1 14  ? 15.713 24.420 7.275   1.00 18.51  ? 13  SER A O   1 
ATOM   115  C CB  . SER A 1 14  ? 15.049 22.354 5.065   1.00 17.56  ? 13  SER A CB  1 
ATOM   116  O OG  . SER A 1 14  ? 15.317 23.014 3.840   1.00 17.81  ? 13  SER A OG  1 
ATOM   117  N N   . LYS A 1 15  ? 17.362 24.547 5.718   1.00 15.88  ? 14  LYS A N   1 
ATOM   118  C CA  . LYS A 1 15  ? 17.626 26.000 5.788   1.00 17.13  ? 14  LYS A CA  1 
ATOM   119  C C   . LYS A 1 15  ? 17.886 26.513 4.377   1.00 15.19  ? 14  LYS A C   1 
ATOM   120  O O   . LYS A 1 15  ? 18.651 25.884 3.642   1.00 15.17  ? 14  LYS A O   1 
ATOM   121  C CB  . LYS A 1 15  ? 18.820 26.062 6.734   1.00 26.88  ? 14  LYS A CB  1 
ATOM   122  C CG  . LYS A 1 15  ? 19.753 27.203 6.637   1.00 30.41  ? 14  LYS A CG  1 
ATOM   123  C CD  . LYS A 1 15  ? 20.760 27.127 7.742   1.00 26.09  ? 14  LYS A CD  1 
ATOM   124  C CE  . LYS A 1 15  ? 21.381 28.466 7.955   1.00 26.55  ? 14  LYS A CE  1 
ATOM   125  N NZ  . LYS A 1 15  ? 22.473 28.328 8.909   1.00 26.93  ? 14  LYS A NZ  1 
ATOM   126  N N   . ASN A 1 16  ? 17.258 27.622 4.001   1.00 14.97  ? 15  ASN A N   1 
ATOM   127  C CA  . ASN A 1 16  ? 17.564 28.386 2.775   1.00 13.92  ? 15  ASN A CA  1 
ATOM   128  C C   . ASN A 1 16  ? 17.152 27.624 1.507   1.00 14.27  ? 15  ASN A C   1 
ATOM   129  O O   . ASN A 1 16  ? 17.576 28.028 0.444   1.00 14.18  ? 15  ASN A O   1 
ATOM   130  C CB  . ASN A 1 16  ? 18.999 28.892 2.796   1.00 14.74  ? 15  ASN A CB  1 
ATOM   131  C CG  . ASN A 1 16  ? 19.252 29.842 3.943   1.00 17.05  ? 15  ASN A CG  1 
ATOM   132  O OD1 . ASN A 1 16  ? 18.348 30.576 4.339   1.00 18.72  ? 15  ASN A OD1 1 
ATOM   133  N ND2 . ASN A 1 16  ? 20.478 29.867 4.415   1.00 20.67  ? 15  ASN A ND2 1 
ATOM   134  N N   . PHE A 1 17  ? 16.254 26.656 1.585   1.00 14.56  ? 16  PHE A N   1 
ATOM   135  C CA  . PHE A 1 17  ? 15.753 25.940 0.368   1.00 12.43  ? 16  PHE A CA  1 
ATOM   136  C C   . PHE A 1 17  ? 14.852 26.787 -0.597  1.00 16.13  ? 16  PHE A C   1 
ATOM   137  O O   . PHE A 1 17  ? 15.079 26.828 -1.726  1.00 16.75  ? 16  PHE A O   1 
ATOM   138  C CB  . PHE A 1 17  ? 15.122 24.635 0.767   1.00 14.00  ? 16  PHE A CB  1 
ATOM   139  C CG  . PHE A 1 17  ? 14.751 23.733 -0.382  1.00 14.63  ? 16  PHE A CG  1 
ATOM   140  C CD1 . PHE A 1 17  ? 15.693 23.394 -1.332  1.00 17.46  ? 16  PHE A CD1 1 
ATOM   141  C CD2 . PHE A 1 17  ? 13.484 23.211 -0.490  1.00 17.59  ? 16  PHE A CD2 1 
ATOM   142  C CE1 . PHE A 1 17  ? 15.373 22.594 -2.401  1.00 19.15  ? 16  PHE A CE1 1 
ATOM   143  C CE2 . PHE A 1 17  ? 13.192 22.347 -1.532  1.00 19.01  ? 16  PHE A CE2 1 
ATOM   144  C CZ  . PHE A 1 17  ? 14.120 22.057 -2.488  1.00 19.24  ? 16  PHE A CZ  1 
ATOM   145  N N   . ASP A 1 18  ? 13.996 27.623 0.133   1.00 17.46  ? 17  ASP A N   1 
ATOM   146  C CA  . ASP A 1 18  ? 13.052 28.456 -0.638  1.00 17.31  ? 17  ASP A CA  1 
ATOM   147  C C   . ASP A 1 18  ? 13.973 29.421 -1.366  1.00 15.51  ? 17  ASP A C   1 
ATOM   148  O O   . ASP A 1 18  ? 13.723 29.764 -2.546  1.00 18.79  ? 17  ASP A O   1 
ATOM   149  C CB  . ASP A 1 18  ? 12.033 29.136 0.260   1.00 17.89  ? 17  ASP A CB  1 
ATOM   150  C CG  . ASP A 1 18  ? 10.936 28.225 0.790   0.80 21.33  ? 17  ASP A CG  1 
ATOM   151  O OD1 . ASP A 1 18  ? 10.598 27.362 0.064   1.00 34.72  ? 17  ASP A OD1 1 
ATOM   152  O OD2 . ASP A 1 18  ? 10.369 28.452 1.901   1.00 19.57  ? 17  ASP A OD2 1 
ATOM   153  N N   . ASP A 1 19  ? 14.983 29.920 -0.651  1.00 17.11  ? 18  ASP A N   1 
ATOM   154  C CA  . ASP A 1 19  ? 15.887 30.934 -1.237  1.00 18.21  ? 18  ASP A CA  1 
ATOM   155  C C   . ASP A 1 19  ? 16.676 30.342 -2.414  1.00 17.95  ? 18  ASP A C   1 
ATOM   156  O O   . ASP A 1 19  ? 16.782 30.995 -3.496  1.00 20.27  ? 18  ASP A O   1 
ATOM   157  C CB  . ASP A 1 19  ? 16.806 31.507 -0.159  1.00 21.49  ? 18  ASP A CB  1 
ATOM   158  C CG  . ASP A 1 19  ? 17.675 32.604 -0.727  1.00 23.42  ? 18  ASP A CG  1 
ATOM   159  O OD1 . ASP A 1 19  ? 17.104 33.690 -1.039  1.00 27.07  ? 18  ASP A OD1 1 
ATOM   160  O OD2 . ASP A 1 19  ? 18.913 32.397 -0.832  1.00 30.23  ? 18  ASP A OD2 1 
ATOM   161  N N   . TYR A 1 20  ? 17.187 29.138 -2.238  1.00 16.39  ? 19  TYR A N   1 
ATOM   162  C CA  . TYR A 1 20  ? 17.913 28.437 -3.324  1.00 16.63  ? 19  TYR A CA  1 
ATOM   163  C C   . TYR A 1 20  ? 16.996 28.243 -4.527  1.00 17.94  ? 19  TYR A C   1 
ATOM   164  O O   . TYR A 1 20  ? 17.435 28.512 -5.663  1.00 18.02  ? 19  TYR A O   1 
ATOM   165  C CB  . TYR A 1 20  ? 18.452 27.120 -2.776  1.00 15.92  ? 19  TYR A CB  1 
ATOM   166  C CG  . TYR A 1 20  ? 19.087 26.222 -3.802  1.00 13.73  ? 19  TYR A CG  1 
ATOM   167  C CD1 . TYR A 1 20  ? 20.396 26.408 -4.216  1.00 13.40  ? 19  TYR A CD1 1 
ATOM   168  C CD2 . TYR A 1 20  ? 18.358 25.183 -4.362  1.00 14.31  ? 19  TYR A CD2 1 
ATOM   169  C CE1 . TYR A 1 20  ? 20.985 25.581 -5.160  1.00 12.34  ? 19  TYR A CE1 1 
ATOM   170  C CE2 . TYR A 1 20  ? 18.927 24.365 -5.324  1.00 13.57  ? 19  TYR A CE2 1 
ATOM   171  C CZ  . TYR A 1 20  ? 20.243 24.543 -5.720  1.00 13.67  ? 19  TYR A CZ  1 
ATOM   172  O OH  . TYR A 1 20  ? 20.818 23.712 -6.653  1.00 14.30  ? 19  TYR A OH  1 
ATOM   173  N N   . MET A 1 21  ? 15.766 27.771 -4.311  1.00 17.55  ? 20  MET A N   1 
ATOM   174  C CA  . MET A 1 21  ? 14.829 27.555 -5.440  1.00 17.56  ? 20  MET A CA  1 
ATOM   175  C C   . MET A 1 21  ? 14.500 28.874 -6.148  1.00 19.59  ? 20  MET A C   1 
ATOM   176  O O   . MET A 1 21  ? 14.484 28.910 -7.393  1.00 19.52  ? 20  MET A O   1 
ATOM   177  C CB  . MET A 1 21  ? 13.531 26.905 -4.973  1.00 17.97  ? 20  MET A CB  1 
ATOM   178  C CG  . MET A 1 21  ? 13.678 25.457 -4.568  1.00 17.96  ? 20  MET A CG  1 
ATOM   179  S SD  . MET A 1 21  ? 12.102 24.678 -4.227  1.00 19.42  ? 20  MET A SD  1 
ATOM   180  C CE  . MET A 1 21  ? 11.688 25.409 -2.638  1.00 18.58  ? 20  MET A CE  1 
ATOM   181  N N   . LYS A 1 22  ? 14.311 29.940 -5.381  1.00 19.52  ? 21  LYS A N   1 
ATOM   182  C CA  . LYS A 1 22  ? 14.047 31.268 -5.975  1.00 21.97  ? 21  LYS A CA  1 
ATOM   183  C C   . LYS A 1 22  ? 15.235 31.665 -6.856  1.00 20.10  ? 21  LYS A C   1 
ATOM   184  O O   . LYS A 1 22  ? 15.030 32.174 -7.975  1.00 23.63  ? 21  LYS A O   1 
ATOM   185  C CB  . LYS A 1 22  ? 13.755 32.306 -4.882  1.00 22.66  ? 21  LYS A CB  1 
ATOM   186  C CG  . LYS A 1 22  ? 13.464 33.692 -5.411  1.00 26.34  ? 21  LYS A CG  1 
ATOM   187  C CD  . LYS A 1 22  ? 13.058 34.723 -4.373  1.00 30.75  ? 21  LYS A CD  1 
ATOM   188  C CE  . LYS A 1 22  ? 12.965 36.119 -4.961  0.80 40.73  ? 21  LYS A CE  1 
ATOM   189  N NZ  . LYS A 1 22  ? 12.781 37.164 -3.920  0.60 49.83  ? 21  LYS A NZ  1 
ATOM   190  N N   . SER A 1 23  ? 16.438 31.340 -6.429  1.00 22.09  ? 22  SER A N   1 
ATOM   191  C CA  . SER A 1 23  ? 17.684 31.715 -7.147  1.00 22.81  ? 22  SER A CA  1 
ATOM   192  C C   . SER A 1 23  ? 17.755 30.991 -8.500  1.00 23.85  ? 22  SER A C   1 
ATOM   193  O O   . SER A 1 23  ? 18.422 31.498 -9.388  1.00 25.50  ? 22  SER A O   1 
ATOM   194  C CB  . SER A 1 23  ? 18.904 31.445 -6.326  1.00 24.24  ? 22  SER A CB  1 
ATOM   195  O OG  . SER A 1 23  ? 19.310 30.088 -6.451  1.00 20.94  ? 22  SER A OG  1 
ATOM   196  N N   . LEU A 1 24  ? 17.061 29.864 -8.645  1.00 21.62  ? 23  LEU A N   1 
ATOM   197  C CA  . LEU A 1 24  ? 16.999 29.055 -9.889  1.00 23.78  ? 23  LEU A CA  1 
ATOM   198  C C   . LEU A 1 24  ? 15.767 29.384 -10.747 1.00 23.89  ? 23  LEU A C   1 
ATOM   199  O O   . LEU A 1 24  ? 15.550 28.726 -11.776 1.00 27.00  ? 23  LEU A O   1 
ATOM   200  C CB  . LEU A 1 24  ? 16.967 27.583 -9.509  1.00 22.30  ? 23  LEU A CB  1 
ATOM   201  C CG  . LEU A 1 24  ? 18.265 27.036 -8.950  1.00 22.62  ? 23  LEU A CG  1 
ATOM   202  C CD1 . LEU A 1 24  ? 18.039 25.653 -8.364  1.00 25.44  ? 23  LEU A CD1 1 
ATOM   203  C CD2 . LEU A 1 24  ? 19.357 27.008 -9.981  1.00 21.85  ? 23  LEU A CD2 1 
ATOM   204  N N   . GLY A 1 25  ? 14.960 30.351 -10.345 1.00 25.34  ? 24  GLY A N   1 
ATOM   205  C CA  . GLY A 1 25  ? 13.813 30.756 -11.160 1.00 26.35  ? 24  GLY A CA  1 
ATOM   206  C C   . GLY A 1 25  ? 12.602 29.883 -10.913 1.00 22.68  ? 24  GLY A C   1 
ATOM   207  O O   . GLY A 1 25  ? 11.690 29.910 -11.737 1.00 27.66  ? 24  GLY A O   1 
ATOM   208  N N   . VAL A 1 26  ? 12.569 29.167 -9.799  1.00 21.64  ? 25  VAL A N   1 
ATOM   209  C CA  . VAL A 1 26  ? 11.383 28.340 -9.462  1.00 23.25  ? 25  VAL A CA  1 
ATOM   210  C C   . VAL A 1 26  ? 10.300 29.275 -8.926  1.00 24.40  ? 25  VAL A C   1 
ATOM   211  O O   . VAL A 1 26  ? 10.577 30.018 -7.984  1.00 24.76  ? 25  VAL A O   1 
ATOM   212  C CB  . VAL A 1 26  ? 11.701 27.240 -8.446  1.00 21.31  ? 25  VAL A CB  1 
ATOM   213  C CG1 . VAL A 1 26  ? 10.454 26.446 -8.104  1.00 24.50  ? 25  VAL A CG1 1 
ATOM   214  C CG2 . VAL A 1 26  ? 12.857 26.347 -8.905  1.00 24.05  ? 25  VAL A CG2 1 
ATOM   215  N N   . GLY A 1 27  ? 9.107  29.215 -9.500  1.00 31.18  ? 26  GLY A N   1 
ATOM   216  C CA  . GLY A 1 27  ? 8.010  30.121 -9.133  1.00 32.76  ? 26  GLY A CA  1 
ATOM   217  C C   . GLY A 1 27  ? 7.475  29.818 -7.748  1.00 27.71  ? 26  GLY A C   1 
ATOM   218  O O   . GLY A 1 27  ? 7.631  28.697 -7.261  1.00 28.67  ? 26  GLY A O   1 
ATOM   219  N N   . PHE A 1 28  ? 6.826  30.797 -7.137  1.00 28.38  ? 27  PHE A N   1 
ATOM   220  C CA  . PHE A 1 28  ? 6.382  30.736 -5.725  1.00 25.05  ? 27  PHE A CA  1 
ATOM   221  C C   . PHE A 1 28  ? 5.448  29.536 -5.519  1.00 27.78  ? 27  PHE A C   1 
ATOM   222  O O   . PHE A 1 28  ? 5.579  28.813 -4.522  1.00 29.41  ? 27  PHE A O   1 
ATOM   223  C CB  . PHE A 1 28  ? 5.696  32.061 -5.347  1.00 33.58  ? 27  PHE A CB  1 
ATOM   224  C CG  . PHE A 1 28  ? 5.242  32.147 -3.910  1.00 37.61  ? 27  PHE A CG  1 
ATOM   225  C CD1 . PHE A 1 28  ? 6.087  31.788 -2.871  1.00 34.35  ? 27  PHE A CD1 1 
ATOM   226  C CD2 . PHE A 1 28  ? 3.981  32.611 -3.585  1.00 41.44  ? 27  PHE A CD2 1 
ATOM   227  C CE1 . PHE A 1 28  ? 5.682  31.870 -1.550  1.00 34.38  ? 27  PHE A CE1 1 
ATOM   228  C CE2 . PHE A 1 28  ? 3.573  32.699 -2.263  1.00 51.28  ? 27  PHE A CE2 1 
ATOM   229  C CZ  . PHE A 1 28  ? 4.426  32.325 -1.250  1.00 39.20  ? 27  PHE A CZ  1 
ATOM   230  N N   . ALA A 1 29  ? 4.513  29.322 -6.429  1.00 29.85  ? 28  ALA A N   1 
ATOM   231  C CA  . ALA A 1 29  ? 3.536  28.218 -6.310  1.00 34.12  ? 28  ALA A CA  1 
ATOM   232  C C   . ALA A 1 29  ? 4.263  26.874 -6.229  1.00 33.38  ? 28  ALA A C   1 
ATOM   233  O O   . ALA A 1 29  ? 3.884  26.050 -5.373  1.00 34.67  ? 28  ALA A O   1 
ATOM   234  C CB  . ALA A 1 29  ? 2.521  28.275 -7.433  1.00 38.79  ? 28  ALA A CB  1 
ATOM   235  N N   . THR A 1 30  ? 5.292  26.682 -7.050  1.00 30.71  ? 29  THR A N   1 
ATOM   236  C CA  . THR A 1 30  ? 6.104  25.443 -7.102  1.00 29.35  ? 29  THR A CA  1 
ATOM   237  C C   . THR A 1 30  ? 6.978  25.369 -5.842  1.00 26.99  ? 29  THR A C   1 
ATOM   238  O O   . THR A 1 30  ? 7.104  24.293 -5.264  1.00 25.46  ? 29  THR A O   1 
ATOM   239  C CB  . THR A 1 30  ? 6.918  25.386 -8.402  1.00 33.18  ? 29  THR A CB  1 
ATOM   240  O OG1 . THR A 1 30  ? 6.020  25.366 -9.511  1.00 35.60  ? 29  THR A OG1 1 
ATOM   241  C CG2 . THR A 1 30  ? 7.798  24.157 -8.504  1.00 37.03  ? 29  THR A CG2 1 
ATOM   242  N N   . ARG A 1 31  ? 7.559  26.483 -5.394  1.00 25.09  ? 30  ARG A N   1 
ATOM   243  C CA  . ARG A 1 31  ? 8.356  26.471 -4.152  1.00 20.40  ? 30  ARG A CA  1 
ATOM   244  C C   . ARG A 1 31  ? 7.486  26.003 -2.983  1.00 22.44  ? 30  ARG A C   1 
ATOM   245  O O   . ARG A 1 31  ? 7.990  25.219 -2.159  1.00 22.58  ? 30  ARG A O   1 
ATOM   246  C CB  . ARG A 1 31  ? 8.948  27.840 -3.862  1.00 19.45  ? 30  ARG A CB  1 
ATOM   247  C CG  . ARG A 1 31  ? 9.891  28.348 -4.928  1.00 20.70  ? 30  ARG A CG  1 
ATOM   248  C CD  . ARG A 1 31  ? 10.736 29.490 -4.426  1.00 22.37  ? 30  ARG A CD  1 
ATOM   249  N NE  . ARG A 1 31  ? 10.015 30.684 -3.980  1.00 22.61  ? 30  ARG A NE  1 
ATOM   250  C CZ  . ARG A 1 31  ? 9.727  31.761 -4.688  1.00 23.13  ? 30  ARG A CZ  1 
ATOM   251  N NH1 . ARG A 1 31  ? 9.976  31.838 -5.981  1.00 26.35  ? 30  ARG A NH1 1 
ATOM   252  N NH2 . ARG A 1 31  ? 9.164  32.787 -4.081  1.00 26.82  ? 30  ARG A NH2 1 
ATOM   253  N N   . GLN A 1 32  ? 6.230  26.452 -2.906  1.00 23.33  ? 31  GLN A N   1 
ATOM   254  C CA  . GLN A 1 32  ? 5.358  26.114 -1.763  1.00 25.94  ? 31  GLN A CA  1 
ATOM   255  C C   . GLN A 1 32  ? 5.177  24.595 -1.692  1.00 24.53  ? 31  GLN A C   1 
ATOM   256  O O   . GLN A 1 32  ? 5.298  24.052 -0.601  1.00 30.06  ? 31  GLN A O   1 
ATOM   257  C CB  . GLN A 1 32  ? 4.061  26.906 -1.871  1.00 31.55  ? 31  GLN A CB  1 
ATOM   258  C CG  . GLN A 1 32  ? 4.297  28.393 -1.638  1.00 32.02  ? 31  GLN A CG  1 
ATOM   259  C CD  . GLN A 1 32  ? 3.021  29.188 -1.618  0.50 39.91  ? 31  GLN A CD  1 
ATOM   260  O OE1 . GLN A 1 32  ? 2.609  29.683 -0.576  1.00 57.03  ? 31  GLN A OE1 1 
ATOM   261  N NE2 . GLN A 1 32  ? 2.390  29.316 -2.772  1.00 53.51  ? 31  GLN A NE2 1 
ATOM   262  N N   . VAL A 1 33  ? 4.929  23.964 -2.836  1.00 26.44  ? 32  VAL A N   1 
ATOM   263  C CA  . VAL A 1 33  ? 4.716  22.499 -2.946  1.00 29.21  ? 32  VAL A CA  1 
ATOM   264  C C   . VAL A 1 33  ? 6.021  21.791 -2.553  1.00 27.44  ? 32  VAL A C   1 
ATOM   265  O O   . VAL A 1 33  ? 5.983  20.846 -1.729  1.00 31.50  ? 32  VAL A O   1 
ATOM   266  C CB  . VAL A 1 33  ? 4.223  22.119 -4.357  1.00 32.96  ? 32  VAL A CB  1 
ATOM   267  C CG1 . VAL A 1 33  ? 4.094  20.622 -4.501  1.00 41.25  ? 32  VAL A CG1 1 
ATOM   268  C CG2 . VAL A 1 33  ? 2.916  22.817 -4.648  1.00 35.66  ? 32  VAL A CG2 1 
ATOM   269  N N   . ALA A 1 34  ? 7.151  22.253 -3.094  1.00 24.89  ? 33  ALA A N   1 
ATOM   270  C CA  . ALA A 1 34  ? 8.464  21.604 -2.908  1.00 21.98  ? 33  ALA A CA  1 
ATOM   271  C C   . ALA A 1 34  ? 8.825  21.646 -1.420  1.00 24.81  ? 33  ALA A C   1 
ATOM   272  O O   . ALA A 1 34  ? 9.382  20.675 -0.932  1.00 26.51  ? 33  ALA A O   1 
ATOM   273  C CB  . ALA A 1 34  ? 9.510  22.227 -3.791  1.00 24.66  ? 33  ALA A CB  1 
ATOM   274  N N   A SER A 1 35  ? 8.495  22.734 -0.719  0.10 25.20  ? 34  SER A N   1 
ATOM   275  N N   B SER A 1 35  ? 8.468  22.736 -0.720  0.90 24.06  ? 34  SER A N   1 
ATOM   276  C CA  A SER A 1 35  ? 8.928  22.976 0.683   0.10 24.03  ? 34  SER A CA  1 
ATOM   277  C CA  B SER A 1 35  ? 8.896  22.934 0.686   0.90 24.67  ? 34  SER A CA  1 
ATOM   278  C C   A SER A 1 35  ? 7.951  22.371 1.700   0.10 24.01  ? 34  SER A C   1 
ATOM   279  C C   B SER A 1 35  ? 8.010  22.235 1.690   0.90 26.87  ? 34  SER A C   1 
ATOM   280  O O   A SER A 1 35  ? 8.276  22.443 2.897   0.10 23.51  ? 34  SER A O   1 
ATOM   281  O O   B SER A 1 35  ? 8.527  22.035 2.813   0.90 28.49  ? 34  SER A O   1 
ATOM   282  C CB  A SER A 1 35  ? 9.124  24.446 0.928   0.10 23.33  ? 34  SER A CB  1 
ATOM   283  C CB  B SER A 1 35  ? 9.038  24.367 0.991   0.90 24.02  ? 34  SER A CB  1 
ATOM   284  O OG  A SER A 1 35  ? 7.983  25.174 0.516   0.10 23.20  ? 34  SER A OG  1 
ATOM   285  O OG  B SER A 1 35  ? 10.334 24.681 0.594   0.90 23.30  ? 34  SER A OG  1 
ATOM   286  N N   . MET A 1 36  ? 6.809  21.804 1.278   1.00 23.93  ? 35  MET A N   1 
ATOM   287  C CA  . MET A 1 36  ? 5.795  21.327 2.242   1.00 31.55  ? 35  MET A CA  1 
ATOM   288  C C   . MET A 1 36  ? 5.830  19.799 2.371   1.00 32.98  ? 35  MET A C   1 
ATOM   289  O O   . MET A 1 36  ? 4.918  19.259 3.042   1.00 51.77  ? 35  MET A O   1 
ATOM   290  C CB  . MET A 1 36  ? 4.388  21.864 1.929   1.00 43.25  ? 35  MET A CB  1 
ATOM   291  C CG  . MET A 1 36  ? 3.705  21.378 0.658   0.50 44.23  ? 35  MET A CG  1 
ATOM   292  S SD  . MET A 1 36  ? 1.994  22.064 0.533   1.00 73.22  ? 35  MET A SD  1 
ATOM   293  C CE  . MET A 1 36  ? 2.297  23.824 0.702   0.50 60.61  ? 35  MET A CE  1 
ATOM   294  N N   . THR A 1 37  ? 6.840  19.140 1.808   1.00 34.51  ? 36  THR A N   1 
ATOM   295  C CA  . THR A 1 37  ? 7.042  17.671 1.942   1.00 38.95  ? 36  THR A CA  1 
ATOM   296  C C   . THR A 1 37  ? 8.430  17.384 2.521   1.00 31.08  ? 36  THR A C   1 
ATOM   297  O O   . THR A 1 37  ? 9.305  18.193 2.332   1.00 26.66  ? 36  THR A O   1 
ATOM   298  C CB  . THR A 1 37  ? 6.874  16.913 0.613   1.00 51.04  ? 36  THR A CB  1 
ATOM   299  O OG1 . THR A 1 37  ? 7.873  17.290 -0.345  1.00 61.97  ? 36  THR A OG1 1 
ATOM   300  C CG2 . THR A 1 37  ? 5.508  17.123 -0.002  0.50 49.65  ? 36  THR A CG2 1 
ATOM   301  N N   . LYS A 1 38  ? 8.588  16.249 3.202   1.00 30.51  ? 37  LYS A N   1 
ATOM   302  C CA  . LYS A 1 38  ? 9.916  15.708 3.609   1.00 28.45  ? 37  LYS A CA  1 
ATOM   303  C C   . LYS A 1 38  ? 10.249 14.580 2.640   1.00 25.32  ? 37  LYS A C   1 
ATOM   304  O O   . LYS A 1 38  ? 9.716  13.472 2.764   1.00 29.99  ? 37  LYS A O   1 
ATOM   305  C CB  . LYS A 1 38  ? 9.946  15.255 5.077   1.00 30.37  ? 37  LYS A CB  1 
ATOM   306  C CG  . LYS A 1 38  ? 9.866  16.381 6.110   1.00 31.89  ? 37  LYS A CG  1 
ATOM   307  C CD  . LYS A 1 38  ? 9.904  15.885 7.542   1.00 34.30  ? 37  LYS A CD  1 
ATOM   308  C CE  . LYS A 1 38  ? 10.099 16.977 8.574   1.00 34.17  ? 37  LYS A CE  1 
ATOM   309  N NZ  . LYS A 1 38  ? 9.174  18.110 8.337   1.00 34.64  ? 37  LYS A NZ  1 
ATOM   310  N N   . PRO A 1 39  ? 11.097 14.856 1.628   1.00 24.59  ? 38  PRO A N   1 
ATOM   311  C CA  . PRO A 1 39  ? 11.479 13.851 0.645   1.00 22.80  ? 38  PRO A CA  1 
ATOM   312  C C   . PRO A 1 39  ? 12.350 12.742 1.235   1.00 22.44  ? 38  PRO A C   1 
ATOM   313  O O   . PRO A 1 39  ? 12.963 12.872 2.300   1.00 21.41  ? 38  PRO A O   1 
ATOM   314  C CB  . PRO A 1 39  ? 12.296 14.574 -0.430  1.00 27.48  ? 38  PRO A CB  1 
ATOM   315  C CG  . PRO A 1 39  ? 12.217 16.021 -0.050  1.00 28.31  ? 38  PRO A CG  1 
ATOM   316  C CD  . PRO A 1 39  ? 11.732 16.147 1.368   1.00 25.29  ? 38  PRO A CD  1 
ATOM   317  N N   . THR A 1 40  ? 12.366 11.644 0.496   1.00 20.57  ? 39  THR A N   1 
ATOM   318  C CA  . THR A 1 40  ? 13.234 10.476 0.743   1.00 21.96  ? 39  THR A CA  1 
ATOM   319  C C   . THR A 1 40  ? 14.195 10.393 -0.423  1.00 20.82  ? 39  THR A C   1 
ATOM   320  O O   . THR A 1 40  ? 13.764 10.490 -1.569  1.00 23.96  ? 39  THR A O   1 
ATOM   321  C CB  . THR A 1 40  ? 12.400 9.195  0.923   1.00 24.49  ? 39  THR A CB  1 
ATOM   322  O OG1 . THR A 1 40  ? 11.560 9.380  2.061   1.00 27.35  ? 39  THR A OG1 1 
ATOM   323  C CG2 . THR A 1 40  ? 13.260 7.979  1.147   1.00 25.97  ? 39  THR A CG2 1 
ATOM   324  N N   A THR A 1 41  ? 15.483 10.225 -0.134  0.50 20.03  ? 40  THR A N   1 
ATOM   325  N N   B THR A 1 41  ? 15.467 10.176 -0.132  0.50 21.04  ? 40  THR A N   1 
ATOM   326  C CA  A THR A 1 41  ? 16.525 9.962  -1.154  0.50 19.95  ? 40  THR A CA  1 
ATOM   327  C CA  B THR A 1 41  ? 16.454 9.911  -1.190  0.50 20.51  ? 40  THR A CA  1 
ATOM   328  C C   A THR A 1 41  ? 17.078 8.547  -0.949  0.50 18.81  ? 40  THR A C   1 
ATOM   329  C C   B THR A 1 41  ? 17.088 8.546  -0.954  0.50 19.53  ? 40  THR A C   1 
ATOM   330  O O   A THR A 1 41  ? 17.435 8.193  0.192   0.50 19.93  ? 40  THR A O   1 
ATOM   331  O O   B THR A 1 41  ? 17.476 8.224  0.186   0.50 20.22  ? 40  THR A O   1 
ATOM   332  C CB  A THR A 1 41  ? 17.649 11.006 -1.123  0.50 19.83  ? 40  THR A CB  1 
ATOM   333  C CB  B THR A 1 41  ? 17.437 11.067 -1.366  0.50 24.77  ? 40  THR A CB  1 
ATOM   334  O OG1 A THR A 1 41  ? 17.123 12.273 -1.525  0.50 25.05  ? 40  THR A OG1 1 
ATOM   335  O OG1 B THR A 1 41  ? 18.110 11.388 -0.141  0.50 32.91  ? 40  THR A OG1 1 
ATOM   336  C CG2 A THR A 1 41  ? 18.828 10.666 -2.013  0.50 17.59  ? 40  THR A CG2 1 
ATOM   337  C CG2 B THR A 1 41  ? 16.696 12.267 -1.908  0.50 21.94  ? 40  THR A CG2 1 
ATOM   338  N N   . ILE A 1 42  ? 17.122 7.784  -2.035  1.00 18.19  ? 41  ILE A N   1 
ATOM   339  C CA  . ILE A 1 42  ? 17.707 6.432  -2.066  1.00 17.70  ? 41  ILE A CA  1 
ATOM   340  C C   . ILE A 1 42  ? 18.946 6.486  -2.929  1.00 15.89  ? 41  ILE A C   1 
ATOM   341  O O   . ILE A 1 42  ? 18.851 6.960  -4.071  1.00 19.30  ? 41  ILE A O   1 
ATOM   342  C CB  . ILE A 1 42  ? 16.667 5.408  -2.564  1.00 22.80  ? 41  ILE A CB  1 
ATOM   343  C CG1 . ILE A 1 42  ? 15.389 5.503  -1.730  1.00 23.65  ? 41  ILE A CG1 1 
ATOM   344  C CG2 . ILE A 1 42  ? 17.293 4.016  -2.636  1.00 24.86  ? 41  ILE A CG2 1 
ATOM   345  C CD1 . ILE A 1 42  ? 14.248 4.692  -2.293  1.00 32.14  ? 41  ILE A CD1 1 
ATOM   346  N N   . ILE A 1 43  ? 20.069 6.064  -2.351  1.00 15.51  ? 42  ILE A N   1 
ATOM   347  C CA  . ILE A 1 43  ? 21.354 6.008  -3.081  1.00 15.93  ? 42  ILE A CA  1 
ATOM   348  C C   . ILE A 1 43  ? 21.723 4.530  -3.166  1.00 15.65  ? 42  ILE A C   1 
ATOM   349  O O   . ILE A 1 43  ? 21.821 3.840  -2.109  1.00 17.72  ? 42  ILE A O   1 
ATOM   350  C CB  . ILE A 1 43  ? 22.431 6.876  -2.422  1.00 16.84  ? 42  ILE A CB  1 
ATOM   351  C CG1 . ILE A 1 43  ? 21.924 8.298  -2.185  1.00 18.53  ? 42  ILE A CG1 1 
ATOM   352  C CG2 . ILE A 1 43  ? 23.688 6.801  -3.260  1.00 20.05  ? 42  ILE A CG2 1 
ATOM   353  C CD1 . ILE A 1 43  ? 22.939 9.220  -1.532  1.00 20.33  ? 42  ILE A CD1 1 
ATOM   354  N N   A GLU A 1 44  ? 21.949 4.081  -4.394  0.50 16.57  ? 43  GLU A N   1 
ATOM   355  N N   B GLU A 1 44  ? 21.851 4.026  -4.387  0.50 15.88  ? 43  GLU A N   1 
ATOM   356  C CA  A GLU A 1 44  ? 22.152 2.655  -4.717  0.50 17.78  ? 43  GLU A CA  1 
ATOM   357  C CA  B GLU A 1 44  ? 22.165 2.598  -4.621  0.50 16.86  ? 43  GLU A CA  1 
ATOM   358  C C   A GLU A 1 44  ? 23.335 2.522  -5.673  0.50 17.52  ? 43  GLU A C   1 
ATOM   359  C C   B GLU A 1 44  ? 23.286 2.498  -5.661  0.50 17.10  ? 43  GLU A C   1 
ATOM   360  O O   A GLU A 1 44  ? 23.716 3.502  -6.341  0.50 17.06  ? 43  GLU A O   1 
ATOM   361  O O   B GLU A 1 44  ? 23.567 3.473  -6.375  0.50 17.33  ? 43  GLU A O   1 
ATOM   362  C CB  A GLU A 1 44  ? 20.851 2.092  -5.286  0.50 19.36  ? 43  GLU A CB  1 
ATOM   363  C CB  B GLU A 1 44  ? 20.898 1.836  -5.023  0.50 18.90  ? 43  GLU A CB  1 
ATOM   364  C CG  A GLU A 1 44  ? 19.807 1.917  -4.201  0.50 24.74  ? 43  GLU A CG  1 
ATOM   365  C CG  B GLU A 1 44  ? 20.314 2.257  -6.352  0.50 19.94  ? 43  GLU A CG  1 
ATOM   366  C CD  A GLU A 1 44  ? 18.463 1.368  -4.634  0.50 27.17  ? 43  GLU A CD  1 
ATOM   367  C CD  B GLU A 1 44  ? 18.989 1.623  -6.743  0.50 22.31  ? 43  GLU A CD  1 
ATOM   368  O OE1 A GLU A 1 44  ? 17.922 1.844  -5.665  0.50 25.44  ? 43  GLU A OE1 1 
ATOM   369  O OE1 B GLU A 1 44  ? 18.255 1.161  -5.850  0.50 26.30  ? 43  GLU A OE1 1 
ATOM   370  O OE2 A GLU A 1 44  ? 17.963 0.471  -3.924  0.50 37.78  ? 43  GLU A OE2 1 
ATOM   371  O OE2 B GLU A 1 44  ? 18.680 1.618  -7.963  0.50 27.33  ? 43  GLU A OE2 1 
ATOM   372  N N   . LYS A 1 45  ? 23.895 1.326  -5.738  1.00 17.75  ? 44  LYS A N   1 
ATOM   373  C CA  . LYS A 1 45  ? 25.043 1.076  -6.631  1.00 18.31  ? 44  LYS A CA  1 
ATOM   374  C C   . LYS A 1 45  ? 24.921 -0.336 -7.173  1.00 20.60  ? 44  LYS A C   1 
ATOM   375  O O   . LYS A 1 45  ? 24.602 -1.263 -6.394  1.00 22.85  ? 44  LYS A O   1 
ATOM   376  C CB  . LYS A 1 45  ? 26.370 1.308  -5.910  1.00 21.62  ? 44  LYS A CB  1 
ATOM   377  C CG  . LYS A 1 45  ? 27.599 1.263  -6.814  1.00 24.32  ? 44  LYS A CG  1 
ATOM   378  C CD  . LYS A 1 45  ? 28.870 1.777  -6.135  1.00 26.03  ? 44  LYS A CD  1 
ATOM   379  C CE  . LYS A 1 45  ? 30.130 1.612  -6.951  1.00 36.60  ? 44  LYS A CE  1 
ATOM   380  N NZ  . LYS A 1 45  ? 30.610 0.213  -6.914  1.00 38.25  ? 44  LYS A NZ  1 
ATOM   381  N N   . ASN A 1 46  ? 25.192 -0.480 -8.462  1.00 19.42  ? 45  ASN A N   1 
ATOM   382  C CA  . ASN A 1 46  ? 25.230 -1.805 -9.109  1.00 20.71  ? 45  ASN A CA  1 
ATOM   383  C C   . ASN A 1 46  ? 26.427 -1.768 -10.062 1.00 19.92  ? 45  ASN A C   1 
ATOM   384  O O   . ASN A 1 46  ? 26.371 -1.029 -11.060 1.00 22.45  ? 45  ASN A O   1 
ATOM   385  C CB  . ASN A 1 46  ? 23.899 -2.169 -9.777  1.00 24.71  ? 45  ASN A CB  1 
ATOM   386  C CG  . ASN A 1 46  ? 23.784 -3.671 -9.997  1.00 32.46  ? 45  ASN A CG  1 
ATOM   387  O OD1 . ASN A 1 46  ? 24.763 -4.393 -9.832  1.00 41.15  ? 45  ASN A OD1 1 
ATOM   388  N ND2 . ASN A 1 46  ? 22.609 -4.169 -10.338 1.00 37.70  ? 45  ASN A ND2 1 
ATOM   389  N N   . GLY A 1 47  ? 27.489 -2.499 -9.731  1.00 22.86  ? 46  GLY A N   1 
ATOM   390  C CA  . GLY A 1 47  ? 28.779 -2.352 -10.408 1.00 25.91  ? 46  GLY A CA  1 
ATOM   391  C C   . GLY A 1 47  ? 29.282 -0.936 -10.265 1.00 23.96  ? 46  GLY A C   1 
ATOM   392  O O   . GLY A 1 47  ? 29.281 -0.405 -9.144  1.00 26.40  ? 46  GLY A O   1 
ATOM   393  N N   . ASP A 1 48  ? 29.631 -0.302 -11.371 1.00 22.32  ? 47  ASP A N   1 
ATOM   394  C CA  . ASP A 1 48  ? 30.127 1.091  -11.300 1.00 22.39  ? 47  ASP A CA  1 
ATOM   395  C C   . ASP A 1 48  ? 29.009 2.083  -11.590 1.00 18.31  ? 47  ASP A C   1 
ATOM   396  O O   . ASP A 1 48  ? 29.312 3.253  -11.737 1.00 19.78  ? 47  ASP A O   1 
ATOM   397  C CB  . ASP A 1 48  ? 31.348 1.339  -12.187 1.00 25.78  ? 47  ASP A CB  1 
ATOM   398  C CG  . ASP A 1 48  ? 31.113 1.116  -13.658 1.00 31.22  ? 47  ASP A CG  1 
ATOM   399  O OD1 . ASP A 1 48  ? 29.964 0.760  -14.013 1.00 29.66  ? 47  ASP A OD1 1 
ATOM   400  O OD2 . ASP A 1 48  ? 32.099 1.286  -14.432 1.00 36.04  ? 47  ASP A OD2 1 
ATOM   401  N N   A ILE A 1 49  ? 27.755 1.629  -11.633 0.50 17.61  ? 48  ILE A N   1 
ATOM   402  N N   B ILE A 1 49  ? 27.754 1.646  -11.642 0.50 16.90  ? 48  ILE A N   1 
ATOM   403  C CA  A ILE A 1 49  ? 26.586 2.517  -11.878 0.50 17.62  ? 48  ILE A CA  1 
ATOM   404  C CA  B ILE A 1 49  ? 26.628 2.580  -11.907 0.50 15.72  ? 48  ILE A CA  1 
ATOM   405  C C   A ILE A 1 49  ? 25.957 2.874  -10.535 0.50 14.87  ? 48  ILE A C   1 
ATOM   406  C C   B ILE A 1 49  ? 25.929 2.887  -10.585 0.50 14.80  ? 48  ILE A C   1 
ATOM   407  O O   A ILE A 1 49  ? 25.457 1.978  -9.830  0.50 16.10  ? 48  ILE A O   1 
ATOM   408  O O   B ILE A 1 49  ? 25.372 1.978  -9.947  0.50 16.00  ? 48  ILE A O   1 
ATOM   409  C CB  A ILE A 1 49  ? 25.548 1.885  -12.819 0.50 20.00  ? 48  ILE A CB  1 
ATOM   410  C CB  B ILE A 1 49  ? 25.650 2.056  -12.969 0.50 15.14  ? 48  ILE A CB  1 
ATOM   411  C CG1 A ILE A 1 49  ? 26.196 1.328  -14.085 0.50 22.96  ? 48  ILE A CG1 1 
ATOM   412  C CG1 B ILE A 1 49  ? 26.330 1.892  -14.330 0.50 16.45  ? 48  ILE A CG1 1 
ATOM   413  C CG2 A ILE A 1 49  ? 24.449 2.892  -13.129 0.50 21.01  ? 48  ILE A CG2 1 
ATOM   414  C CG2 B ILE A 1 49  ? 24.427 2.962  -13.026 0.50 16.84  ? 48  ILE A CG2 1 
ATOM   415  C CD1 A ILE A 1 49  ? 26.825 2.388  -14.927 0.50 26.59  ? 48  ILE A CD1 1 
ATOM   416  C CD1 B ILE A 1 49  ? 25.511 1.093  -15.336 0.50 19.60  ? 48  ILE A CD1 1 
ATOM   417  N N   . LEU A 1 50  ? 25.924 4.164  -10.236 1.00 15.85  ? 49  LEU A N   1 
ATOM   418  C CA  . LEU A 1 50  ? 25.225 4.681  -9.069  1.00 15.80  ? 49  LEU A CA  1 
ATOM   419  C C   . LEU A 1 50  ? 23.850 5.157  -9.530  1.00 15.55  ? 49  LEU A C   1 
ATOM   420  O O   . LEU A 1 50  ? 23.710 5.677  -10.653 1.00 15.90  ? 49  LEU A O   1 
ATOM   421  C CB  . LEU A 1 50  ? 26.021 5.802  -8.420  1.00 16.15  ? 49  LEU A CB  1 
ATOM   422  C CG  . LEU A 1 50  ? 27.260 5.418  -7.653  1.00 20.96  ? 49  LEU A CG  1 
ATOM   423  C CD1 . LEU A 1 50  ? 28.386 5.090  -8.606  1.00 29.50  ? 49  LEU A CD1 1 
ATOM   424  C CD2 . LEU A 1 50  ? 27.738 6.562  -6.777  1.00 29.80  ? 49  LEU A CD2 1 
ATOM   425  N N   . THR A 1 51  ? 22.866 5.011  -8.656  1.00 15.39  ? 50  THR A N   1 
ATOM   426  C CA  . THR A 1 51  ? 21.504 5.542  -8.890  1.00 15.58  ? 50  THR A CA  1 
ATOM   427  C C   . THR A 1 51  ? 21.092 6.342  -7.671  1.00 16.79  ? 50  THR A C   1 
ATOM   428  O O   . THR A 1 51  ? 21.259 5.888  -6.537  1.00 18.17  ? 50  THR A O   1 
ATOM   429  C CB  . THR A 1 51  ? 20.507 4.433  -9.224  1.00 17.70  ? 50  THR A CB  1 
ATOM   430  O OG1 . THR A 1 51  ? 20.927 3.738  -10.407 1.00 20.23  ? 50  THR A OG1 1 
ATOM   431  C CG2 . THR A 1 51  ? 19.094 4.946  -9.411  1.00 21.37  ? 50  THR A CG2 1 
ATOM   432  N N   . LEU A 1 52  ? 20.521 7.515  -7.931  1.00 15.25  ? 51  LEU A N   1 
ATOM   433  C CA  . LEU A 1 52  ? 19.971 8.367  -6.877  1.00 16.88  ? 51  LEU A CA  1 
ATOM   434  C C   . LEU A 1 52  ? 18.521 8.618  -7.237  1.00 17.93  ? 51  LEU A C   1 
ATOM   435  O O   . LEU A 1 52  ? 18.220 9.112  -8.337  1.00 17.94  ? 51  LEU A O   1 
ATOM   436  C CB  . LEU A 1 52  ? 20.795 9.651  -6.807  1.00 20.83  ? 51  LEU A CB  1 
ATOM   437  C CG  . LEU A 1 52  ? 20.491 10.517 -5.605  1.00 24.84  ? 51  LEU A CG  1 
ATOM   438  C CD1 . LEU A 1 52  ? 21.740 11.237 -5.099  1.00 29.49  ? 51  LEU A CD1 1 
ATOM   439  C CD2 . LEU A 1 52  ? 19.406 11.495 -5.968  1.00 29.23  ? 51  LEU A CD2 1 
ATOM   440  N N   . LYS A 1 53  ? 17.666 8.248  -6.315  1.00 17.98  ? 52  LYS A N   1 
ATOM   441  C CA  . LYS A 1 53  ? 16.207 8.386  -6.420  1.00 20.08  ? 52  LYS A CA  1 
ATOM   442  C C   . LYS A 1 53  ? 15.757 9.381  -5.365  1.00 21.08  ? 52  LYS A C   1 
ATOM   443  O O   . LYS A 1 53  ? 16.164 9.254  -4.218  1.00 24.53  ? 52  LYS A O   1 
ATOM   444  C CB  . LYS A 1 53  ? 15.530 7.051  -6.182  1.00 23.86  ? 52  LYS A CB  1 
ATOM   445  C CG  . LYS A 1 53  ? 15.921 5.955  -7.157  1.00 26.70  ? 52  LYS A CG  1 
ATOM   446  C CD  . LYS A 1 53  ? 15.371 4.620  -6.712  1.00 30.81  ? 52  LYS A CD  1 
ATOM   447  C CE  . LYS A 1 53  ? 15.611 3.495  -7.686  1.00 35.73  ? 52  LYS A CE  1 
ATOM   448  N NZ  . LYS A 1 53  ? 15.298 2.184  -7.060  1.00 39.64  ? 52  LYS A NZ  1 
ATOM   449  N N   . THR A 1 54  ? 14.890 10.294 -5.763  1.00 20.46  ? 53  THR A N   1 
ATOM   450  C CA  . THR A 1 54  ? 14.219 11.168 -4.801  1.00 20.34  ? 53  THR A CA  1 
ATOM   451  C C   . THR A 1 54  ? 12.724 10.951 -4.933  1.00 21.15  ? 53  THR A C   1 
ATOM   452  O O   . THR A 1 54  ? 12.185 11.061 -6.045  1.00 22.92  ? 53  THR A O   1 
ATOM   453  C CB  . THR A 1 54  ? 14.684 12.615 -4.975  1.00 20.75  ? 53  THR A CB  1 
ATOM   454  O OG1 . THR A 1 54  ? 16.111 12.594 -4.831  1.00 28.19  ? 53  THR A OG1 1 
ATOM   455  C CG2 . THR A 1 54  ? 13.991 13.497 -3.976  1.00 26.06  ? 53  THR A CG2 1 
ATOM   456  N N   . HIS A 1 55  ? 12.101 10.673 -3.802  1.00 21.38  ? 54  HIS A N   1 
ATOM   457  C CA  . HIS A 1 55  ? 10.665 10.399 -3.711  1.00 25.88  ? 54  HIS A CA  1 
ATOM   458  C C   . HIS A 1 55  ? 10.068 11.554 -2.926  1.00 25.56  ? 54  HIS A C   1 
ATOM   459  O O   . HIS A 1 55  ? 10.488 11.776 -1.780  1.00 26.37  ? 54  HIS A O   1 
ATOM   460  C CB  . HIS A 1 55  ? 10.414 9.007  -3.096  1.00 30.89  ? 54  HIS A CB  1 
ATOM   461  C CG  . HIS A 1 55  ? 10.880 7.866  -3.949  1.00 34.78  ? 54  HIS A CG  1 
ATOM   462  N ND1 . HIS A 1 55  ? 11.061 6.579  -3.449  1.00 36.29  ? 54  HIS A ND1 1 
ATOM   463  C CD2 . HIS A 1 55  ? 11.218 7.802  -5.260  1.00 34.28  ? 54  HIS A CD2 1 
ATOM   464  C CE1 . HIS A 1 55  ? 11.492 5.787  -4.419  1.00 40.92  ? 54  HIS A CE1 1 
ATOM   465  N NE2 . HIS A 1 55  ? 11.573 6.504  -5.550  1.00 34.50  ? 54  HIS A NE2 1 
ATOM   466  N N   . SER A 1 56  ? 9.096  12.233 -3.510  1.00 34.21  ? 55  SER A N   1 
ATOM   467  C CA  . SER A 1 56  ? 8.337  13.264 -2.768  1.00 41.95  ? 55  SER A CA  1 
ATOM   468  C C   . SER A 1 56  ? 6.965  13.424 -3.403  1.00 46.36  ? 55  SER A C   1 
ATOM   469  O O   . SER A 1 56  ? 6.716  12.764 -4.423  1.00 53.46  ? 55  SER A O   1 
ATOM   470  C CB  . SER A 1 56  ? 9.100  14.572 -2.722  1.00 46.67  ? 55  SER A CB  1 
ATOM   471  O OG  . SER A 1 56  ? 9.043  15.251 -3.964  1.00 51.87  ? 55  SER A OG  1 
ATOM   472  N N   . THR A 1 57  ? 6.118  14.236 -2.778  1.00 54.58  ? 56  THR A N   1 
ATOM   473  C CA  . THR A 1 57  ? 4.811  14.677 -3.326  1.00 56.17  ? 56  THR A CA  1 
ATOM   474  C C   . THR A 1 57  ? 5.038  15.716 -4.434  1.00 49.79  ? 56  THR A C   1 
ATOM   475  O O   . THR A 1 57  ? 4.179  15.770 -5.286  1.00 56.03  ? 56  THR A O   1 
ATOM   476  C CB  . THR A 1 57  ? 3.902  15.223 -2.222  0.70 56.45  ? 56  THR A CB  1 
ATOM   477  O OG1 . THR A 1 57  ? 3.961  14.310 -1.125  0.80 59.07  ? 56  THR A OG1 1 
ATOM   478  C CG2 . THR A 1 57  ? 2.472  15.409 -2.671  0.50 63.48  ? 56  THR A CG2 1 
ATOM   479  N N   . PHE A 1 58  ? 6.145  16.493 -4.423  0.50 40.60  ? 57  PHE A N   1 
ATOM   480  C CA  . PHE A 1 58  ? 6.496  17.465 -5.506  0.50 30.86  ? 57  PHE A CA  1 
ATOM   481  C C   . PHE A 1 58  ? 6.774  16.682 -6.802  0.50 31.56  ? 57  PHE A C   1 
ATOM   482  O O   . PHE A 1 58  ? 5.952  16.730 -7.744  0.50 33.71  ? 57  PHE A O   1 
ATOM   483  C CB  . PHE A 1 58  ? 7.659  18.375 -5.096  0.50 35.47  ? 57  PHE A CB  1 
ATOM   484  C CG  . PHE A 1 58  ? 8.260  19.222 -6.195  0.50 33.89  ? 57  PHE A CG  1 
ATOM   485  C CD1 . PHE A 1 58  ? 7.461  19.969 -7.047  0.50 42.36  ? 57  PHE A CD1 1 
ATOM   486  C CD2 . PHE A 1 58  ? 9.637  19.279 -6.369  0.50 41.48  ? 57  PHE A CD2 1 
ATOM   487  C CE1 . PHE A 1 58  ? 8.023  20.739 -8.056  0.50 41.81  ? 57  PHE A CE1 1 
ATOM   488  C CE2 . PHE A 1 58  ? 10.202 20.062 -7.365  0.50 43.31  ? 57  PHE A CE2 1 
ATOM   489  C CZ  . PHE A 1 58  ? 9.390  20.796 -8.204  0.50 46.39  ? 57  PHE A CZ  1 
ATOM   490  N N   . LYS A 1 59  ? 7.847  15.902 -6.832  1.00 38.60  ? 58  LYS A N   1 
ATOM   491  C CA  . LYS A 1 59  ? 8.219  15.118 -8.031  1.00 38.94  ? 58  LYS A CA  1 
ATOM   492  C C   . LYS A 1 59  ? 9.009  13.883 -7.572  1.00 43.04  ? 58  LYS A C   1 
ATOM   493  O O   . LYS A 1 59  ? 9.757  13.972 -6.570  1.00 52.36  ? 58  LYS A O   1 
ATOM   494  C CB  . LYS A 1 59  ? 9.005  16.023 -8.993  1.00 40.95  ? 58  LYS A CB  1 
ATOM   495  C CG  . LYS A 1 59  ? 8.866  15.718 -10.482 1.00 49.94  ? 58  LYS A CG  1 
ATOM   496  C CD  . LYS A 1 59  ? 7.771  16.499 -11.182 0.50 49.10  ? 58  LYS A CD  1 
ATOM   497  C CE  . LYS A 1 59  ? 7.902  16.476 -12.690 0.50 54.71  ? 58  LYS A CE  1 
ATOM   498  N NZ  . LYS A 1 59  ? 8.938  17.429 -13.159 0.50 55.84  ? 58  LYS A NZ  1 
ATOM   499  N N   . ASN A 1 60  ? 8.832  12.754 -8.250  1.00 29.15  ? 59  ASN A N   1 
ATOM   500  C CA  . ASN A 1 60  ? 9.772  11.612 -8.129  1.00 25.32  ? 59  ASN A CA  1 
ATOM   501  C C   . ASN A 1 60  ? 10.825 11.787 -9.221  1.00 25.84  ? 59  ASN A C   1 
ATOM   502  O O   . ASN A 1 60  ? 10.466 12.073 -10.367 1.00 29.23  ? 59  ASN A O   1 
ATOM   503  C CB  . ASN A 1 60  ? 9.057  10.273 -8.269  1.00 31.92  ? 59  ASN A CB  1 
ATOM   504  C CG  . ASN A 1 60  ? 8.088  10.008 -7.136  1.00 37.91  ? 59  ASN A CG  1 
ATOM   505  O OD1 . ASN A 1 60  ? 8.363  10.366 -5.984  1.00 31.38  ? 59  ASN A OD1 1 
ATOM   506  N ND2 . ASN A 1 60  ? 6.945  9.408  -7.453  1.00 46.55  ? 59  ASN A ND2 1 
ATOM   507  N N   . THR A 1 61  ? 12.096 11.629 -8.892  1.00 20.81  ? 60  THR A N   1 
ATOM   508  C CA  . THR A 1 61  ? 13.187 11.702 -9.878  1.00 19.92  ? 60  THR A CA  1 
ATOM   509  C C   . THR A 1 61  ? 14.088 10.484 -9.696  1.00 19.10  ? 60  THR A C   1 
ATOM   510  O O   . THR A 1 61  ? 14.197 9.922  -8.566  1.00 19.54  ? 60  THR A O   1 
ATOM   511  C CB  . THR A 1 61  ? 13.986 13.010 -9.805  1.00 21.19  ? 60  THR A CB  1 
ATOM   512  O OG1 . THR A 1 61  ? 14.631 13.053 -8.522  1.00 21.84  ? 60  THR A OG1 1 
ATOM   513  C CG2 . THR A 1 61  ? 13.131 14.232 -10.063 1.00 25.31  ? 60  THR A CG2 1 
ATOM   514  N N   . GLU A 1 62  ? 14.788 10.142 -10.758 1.00 20.51  ? 61  GLU A N   1 
ATOM   515  C CA  . GLU A 1 62  ? 15.829 9.086  -10.697 1.00 21.45  ? 61  GLU A CA  1 
ATOM   516  C C   . GLU A 1 62  ? 16.906 9.472  -11.692 1.00 20.27  ? 61  GLU A C   1 
ATOM   517  O O   . GLU A 1 62  ? 16.588 9.745  -12.833 1.00 22.45  ? 61  GLU A O   1 
ATOM   518  C CB  . GLU A 1 62  ? 15.227 7.706  -10.978 1.00 25.18  ? 61  GLU A CB  1 
ATOM   519  C CG  . GLU A 1 62  ? 16.239 6.595  -11.017 1.00 29.28  ? 61  GLU A CG  1 
ATOM   520  C CD  . GLU A 1 62  ? 15.600 5.247  -11.238 1.00 33.71  ? 61  GLU A CD  1 
ATOM   521  O OE1 . GLU A 1 62  ? 14.565 4.974  -10.608 1.00 38.39  ? 61  GLU A OE1 1 
ATOM   522  O OE2 . GLU A 1 62  ? 16.102 4.507  -12.087 1.00 40.85  ? 61  GLU A OE2 1 
ATOM   523  N N   . ILE A 1 63  ? 18.154 9.433  -11.248 1.00 17.57  ? 62  ILE A N   1 
ATOM   524  C CA  . ILE A 1 63  ? 19.322 9.563  -12.147 1.00 17.28  ? 62  ILE A CA  1 
ATOM   525  C C   . ILE A 1 63  ? 20.243 8.386  -11.910 1.00 15.78  ? 62  ILE A C   1 
ATOM   526  O O   . ILE A 1 63  ? 20.390 7.926  -10.758 1.00 15.99  ? 62  ILE A O   1 
ATOM   527  C CB  . ILE A 1 63  ? 20.036 10.894 -11.929 1.00 18.21  ? 62  ILE A CB  1 
ATOM   528  C CG1 . ILE A 1 63  ? 20.523 11.082 -10.488 1.00 17.03  ? 62  ILE A CG1 1 
ATOM   529  C CG2 . ILE A 1 63  ? 19.108 12.034 -12.328 1.00 22.16  ? 62  ILE A CG2 1 
ATOM   530  C CD1 . ILE A 1 63  ? 21.372 12.308 -10.268 1.00 19.00  ? 62  ILE A CD1 1 
ATOM   531  N N   . SER A 1 64  ? 20.911 7.990  -12.967 1.00 14.74  ? 63  SER A N   1 
ATOM   532  C CA  . SER A 1 64  ? 21.944 6.950  -12.910 1.00 14.89  ? 63  SER A CA  1 
ATOM   533  C C   . SER A 1 64  ? 23.175 7.512  -13.590 1.00 14.76  ? 63  SER A C   1 
ATOM   534  O O   . SER A 1 64  ? 23.078 8.160  -14.644 1.00 16.31  ? 63  SER A O   1 
ATOM   535  C CB  . SER A 1 64  ? 21.490 5.660  -13.536 1.00 18.31  ? 63  SER A CB  1 
ATOM   536  O OG  . SER A 1 64  ? 20.398 5.077  -12.802 1.00 21.15  ? 63  SER A OG  1 
ATOM   537  N N   . PHE A 1 65  ? 24.323 7.112  -13.079 1.00 13.37  ? 64  PHE A N   1 
ATOM   538  C CA  . PHE A 1 65  ? 25.595 7.694  -13.531 1.00 13.47  ? 64  PHE A CA  1 
ATOM   539  C C   . PHE A 1 65  ? 26.764 6.838  -13.048 1.00 13.93  ? 64  PHE A C   1 
ATOM   540  O O   . PHE A 1 65  ? 26.663 6.078  -12.091 1.00 15.12  ? 64  PHE A O   1 
ATOM   541  C CB  . PHE A 1 65  ? 25.690 9.152  -13.046 1.00 14.86  ? 64  PHE A CB  1 
ATOM   542  C CG  . PHE A 1 65  ? 25.559 9.289  -11.550 1.00 14.46  ? 64  PHE A CG  1 
ATOM   543  C CD1 . PHE A 1 65  ? 26.654 9.115  -10.718 1.00 14.23  ? 64  PHE A CD1 1 
ATOM   544  C CD2 . PHE A 1 65  ? 24.326 9.529  -10.970 1.00 15.32  ? 64  PHE A CD2 1 
ATOM   545  C CE1 . PHE A 1 65  ? 26.532 9.184  -9.337  1.00 15.41  ? 64  PHE A CE1 1 
ATOM   546  C CE2 . PHE A 1 65  ? 24.193 9.557  -9.599  1.00 17.63  ? 64  PHE A CE2 1 
ATOM   547  C CZ  . PHE A 1 65  ? 25.293 9.420  -8.783  1.00 16.16  ? 64  PHE A CZ  1 
ATOM   548  N N   . LYS A 1 66  ? 27.884 7.043  -13.711 1.00 12.99  ? 65  LYS A N   1 
ATOM   549  C CA  . LYS A 1 66  ? 29.184 6.568  -13.272 1.00 12.94  ? 65  LYS A CA  1 
ATOM   550  C C   . LYS A 1 66  ? 29.962 7.748  -12.727 1.00 11.56  ? 65  LYS A C   1 
ATOM   551  O O   . LYS A 1 66  ? 29.857 8.850  -13.258 1.00 11.49  ? 65  LYS A O   1 
ATOM   552  C CB  . LYS A 1 66  ? 29.964 5.954  -14.443 1.00 13.98  ? 65  LYS A CB  1 
ATOM   553  C CG  . LYS A 1 66  ? 29.305 4.730  -15.031 1.00 16.65  ? 65  LYS A CG  1 
ATOM   554  C CD  . LYS A 1 66  ? 30.058 4.150  -16.170 1.00 20.87  ? 65  LYS A CD  1 
ATOM   555  C CE  . LYS A 1 66  ? 29.401 2.974  -16.826 1.00 29.30  ? 65  LYS A CE  1 
ATOM   556  N NZ  . LYS A 1 66  ? 30.164 2.531  -18.012 1.00 38.54  ? 65  LYS A NZ  1 
ATOM   557  N N   . LEU A 1 67  ? 30.676 7.560  -11.636 1.00 12.15  ? 66  LEU A N   1 
ATOM   558  C CA  . LEU A 1 67  ? 31.527 8.635  -11.092 1.00 12.05  ? 66  LEU A CA  1 
ATOM   559  C C   . LEU A 1 67  ? 32.412 9.153  -12.221 1.00 11.16  ? 66  LEU A C   1 
ATOM   560  O O   . LEU A 1 67  ? 33.081 8.398  -12.940 1.00 12.07  ? 66  LEU A O   1 
ATOM   561  C CB  . LEU A 1 67  ? 32.404 8.142  -9.945  1.00 14.84  ? 66  LEU A CB  1 
ATOM   562  C CG  . LEU A 1 67  ? 31.742 7.822  -8.629  1.00 17.21  ? 66  LEU A CG  1 
ATOM   563  C CD1 . LEU A 1 67  ? 32.754 7.310  -7.621  1.00 20.32  ? 66  LEU A CD1 1 
ATOM   564  C CD2 . LEU A 1 67  ? 30.989 9.039  -8.089  1.00 18.21  ? 66  LEU A CD2 1 
ATOM   565  N N   . GLY A 1 68  ? 32.467 10.481 -12.335 1.00 10.41  ? 67  GLY A N   1 
ATOM   566  C CA  . GLY A 1 68  ? 33.424 11.090 -13.250 1.00 10.90  ? 67  GLY A CA  1 
ATOM   567  C C   . GLY A 1 68  ? 33.057 11.021 -14.706 1.00 10.03  ? 67  GLY A C   1 
ATOM   568  O O   . GLY A 1 68  ? 33.919 11.384 -15.514 1.00 12.63  ? 67  GLY A O   1 
ATOM   569  N N   . VAL A 1 69  ? 31.823 10.643 -15.058 1.00 9.76   ? 68  VAL A N   1 
ATOM   570  C CA  . VAL A 1 69  ? 31.375 10.587 -16.468 1.00 9.98   ? 68  VAL A CA  1 
ATOM   571  C C   . VAL A 1 69  ? 30.161 11.500 -16.620 1.00 9.73   ? 68  VAL A C   1 
ATOM   572  O O   . VAL A 1 69  ? 29.122 11.308 -15.971 1.00 10.46  ? 68  VAL A O   1 
ATOM   573  C CB  . VAL A 1 69  ? 31.057 9.151  -16.913 1.00 11.47  ? 68  VAL A CB  1 
ATOM   574  C CG1 . VAL A 1 69  ? 30.638 9.111  -18.358 1.00 12.54  ? 68  VAL A CG1 1 
ATOM   575  C CG2 . VAL A 1 69  ? 32.259 8.232  -16.712 1.00 12.73  ? 68  VAL A CG2 1 
ATOM   576  N N   . GLU A 1 70  ? 30.291 12.514 -17.465 1.00 10.08  ? 69  GLU A N   1 
ATOM   577  C CA  . GLU A 1 70  ? 29.219 13.496 -17.666 1.00 10.54  ? 69  GLU A CA  1 
ATOM   578  C C   . GLU A 1 70  ? 27.972 12.800 -18.193 1.00 10.75  ? 69  GLU A C   1 
ATOM   579  O O   . GLU A 1 70  ? 28.080 11.889 -19.016 1.00 12.31  ? 69  GLU A O   1 
ATOM   580  C CB  . GLU A 1 70  ? 29.698 14.580 -18.614 1.00 12.19  ? 69  GLU A CB  1 
ATOM   581  C CG  . GLU A 1 70  ? 28.813 15.799 -18.773 1.00 13.00  ? 69  GLU A CG  1 
ATOM   582  C CD  . GLU A 1 70  ? 29.360 16.815 -19.776 0.70 19.27  ? 69  GLU A CD  1 
ATOM   583  O OE1 . GLU A 1 70  ? 30.317 16.496 -20.535 0.70 21.71  ? 69  GLU A OE1 1 
ATOM   584  O OE2 . GLU A 1 70  ? 28.863 17.934 -19.771 0.70 29.54  ? 69  GLU A OE2 1 
ATOM   585  N N   . PHE A 1 71  ? 26.808 13.287 -17.786 1.00 11.67  ? 70  PHE A N   1 
ATOM   586  C CA  . PHE A 1 71  ? 25.495 12.756 -18.209 1.00 11.45  ? 70  PHE A CA  1 
ATOM   587  C C   . PHE A 1 71  ? 24.496 13.889 -18.347 1.00 11.59  ? 70  PHE A C   1 
ATOM   588  O O   . PHE A 1 71  ? 24.603 14.921 -17.683 1.00 13.95  ? 70  PHE A O   1 
ATOM   589  C CB  . PHE A 1 71  ? 25.052 11.656 -17.251 1.00 11.68  ? 70  PHE A CB  1 
ATOM   590  C CG  . PHE A 1 71  ? 24.772 12.071 -15.840 1.00 11.56  ? 70  PHE A CG  1 
ATOM   591  C CD1 . PHE A 1 71  ? 25.813 12.217 -14.943 1.00 11.62  ? 70  PHE A CD1 1 
ATOM   592  C CD2 . PHE A 1 71  ? 23.478 12.290 -15.403 1.00 13.35  ? 70  PHE A CD2 1 
ATOM   593  C CE1 . PHE A 1 71  ? 25.576 12.553 -13.623 1.00 11.82  ? 70  PHE A CE1 1 
ATOM   594  C CE2 . PHE A 1 71  ? 23.245 12.638 -14.072 1.00 13.48  ? 70  PHE A CE2 1 
ATOM   595  C CZ  . PHE A 1 71  ? 24.277 12.752 -13.192 1.00 12.74  ? 70  PHE A CZ  1 
ATOM   596  N N   . ASP A 1 72  ? 23.495 13.639 -19.168 1.00 12.73  ? 71  ASP A N   1 
ATOM   597  C CA  . ASP A 1 72  ? 22.341 14.530 -19.325 1.00 13.91  ? 71  ASP A CA  1 
ATOM   598  C C   . ASP A 1 72  ? 21.358 14.272 -18.188 1.00 12.96  ? 71  ASP A C   1 
ATOM   599  O O   . ASP A 1 72  ? 21.086 13.097 -17.848 1.00 14.81  ? 71  ASP A O   1 
ATOM   600  C CB  . ASP A 1 72  ? 21.648 14.236 -20.657 1.00 15.86  ? 71  ASP A CB  1 
ATOM   601  C CG  . ASP A 1 72  ? 22.456 14.742 -21.830 1.00 19.93  ? 71  ASP A CG  1 
ATOM   602  O OD1 . ASP A 1 72  ? 22.760 15.902 -21.829 1.00 28.11  ? 71  ASP A OD1 1 
ATOM   603  O OD2 . ASP A 1 72  ? 22.697 13.995 -22.767 1.00 28.64  ? 71  ASP A OD2 1 
ATOM   604  N N   . GLU A 1 73  ? 20.826 15.346 -17.627 1.00 13.01  ? 72  GLU A N   1 
ATOM   605  C CA  . GLU A 1 73  ? 19.854 15.287 -16.533 1.00 13.30  ? 72  GLU A CA  1 
ATOM   606  C C   . GLU A 1 73  ? 18.768 16.322 -16.789 1.00 13.09  ? 72  GLU A C   1 
ATOM   607  O O   . GLU A 1 73  ? 19.082 17.426 -17.245 1.00 14.14  ? 72  GLU A O   1 
ATOM   608  C CB  . GLU A 1 73  ? 20.536 15.555 -15.200 1.00 12.31  ? 72  GLU A CB  1 
ATOM   609  C CG  . GLU A 1 73  ? 19.650 15.640 -13.988 1.00 13.00  ? 72  GLU A CG  1 
ATOM   610  C CD  . GLU A 1 73  ? 20.397 15.961 -12.704 1.00 12.96  ? 72  GLU A CD  1 
ATOM   611  O OE1 . GLU A 1 73  ? 21.589 16.327 -12.789 1.00 15.55  ? 72  GLU A OE1 1 
ATOM   612  O OE2 . GLU A 1 73  ? 19.842 15.834 -11.609 1.00 14.85  ? 72  GLU A OE2 1 
ATOM   613  N N   . THR A 1 74  ? 17.534 15.955 -16.482 1.00 12.94  ? 73  THR A N   1 
ATOM   614  C CA  . THR A 1 74  ? 16.405 16.905 -16.424 1.00 12.89  ? 73  THR A CA  1 
ATOM   615  C C   . THR A 1 74  ? 15.973 16.988 -14.971 1.00 13.66  ? 73  THR A C   1 
ATOM   616  O O   . THR A 1 74  ? 15.479 16.000 -14.418 1.00 15.39  ? 73  THR A O   1 
ATOM   617  C CB  . THR A 1 74  ? 15.262 16.532 -17.353 1.00 15.36  ? 73  THR A CB  1 
ATOM   618  O OG1 . THR A 1 74  ? 15.762 16.466 -18.688 1.00 17.61  ? 73  THR A OG1 1 
ATOM   619  C CG2 . THR A 1 74  ? 14.145 17.557 -17.279 1.00 20.43  ? 73  THR A CG2 1 
ATOM   620  N N   . THR A 1 75  ? 16.198 18.134 -14.357 1.00 13.96  ? 74  THR A N   1 
ATOM   621  C CA  . THR A 1 75  ? 16.003 18.288 -12.907 1.00 14.28  ? 74  THR A CA  1 
ATOM   622  C C   . THR A 1 75  ? 14.502 18.308 -12.571 1.00 15.06  ? 74  THR A C   1 
ATOM   623  O O   . THR A 1 75  ? 13.650 18.466 -13.452 1.00 16.67  ? 74  THR A O   1 
ATOM   624  C CB  . THR A 1 75  ? 16.716 19.547 -12.430 1.00 13.25  ? 74  THR A CB  1 
ATOM   625  O OG1 . THR A 1 75  ? 16.013 20.694 -12.951 1.00 13.97  ? 74  THR A OG1 1 
ATOM   626  C CG2 . THR A 1 75  ? 18.165 19.585 -12.820 1.00 13.82  ? 74  THR A CG2 1 
ATOM   627  N N   . ALA A 1 76  ? 14.199 18.240 -11.288 1.00 15.44  ? 75  ALA A N   1 
ATOM   628  C CA  . ALA A 1 76  ? 12.812 18.235 -10.793 1.00 16.63  ? 75  ALA A CA  1 
ATOM   629  C C   . ALA A 1 76  ? 12.079 19.500 -11.255 1.00 16.34  ? 75  ALA A C   1 
ATOM   630  O O   . ALA A 1 76  ? 10.860 19.419 -11.533 1.00 20.18  ? 75  ALA A O   1 
ATOM   631  C CB  . ALA A 1 76  ? 12.782 18.121 -9.292  1.00 18.01  ? 75  ALA A CB  1 
ATOM   632  N N   . ASP A 1 77  ? 12.794 20.628 -11.316 1.00 16.57  ? 76  ASP A N   1 
ATOM   633  C CA  . ASP A 1 77  ? 12.254 21.937 -11.748 1.00 17.69  ? 76  ASP A CA  1 
ATOM   634  C C   . ASP A 1 77  ? 12.393 22.132 -13.280 1.00 18.24  ? 76  ASP A C   1 
ATOM   635  O O   . ASP A 1 77  ? 12.187 23.243 -13.746 1.00 19.66  ? 76  ASP A O   1 
ATOM   636  C CB  . ASP A 1 77  ? 12.889 23.088 -10.967 1.00 17.38  ? 76  ASP A CB  1 
ATOM   637  C CG  . ASP A 1 77  ? 14.382 23.190 -11.120 1.00 16.96  ? 76  ASP A CG  1 
ATOM   638  O OD1 . ASP A 1 77  ? 15.067 22.126 -10.939 1.00 16.10  ? 76  ASP A OD1 1 
ATOM   639  O OD2 . ASP A 1 77  ? 14.852 24.295 -11.464 1.00 18.72  ? 76  ASP A OD2 1 
ATOM   640  N N   A ASP A 1 78  ? 12.678 21.057 -14.012 0.70 18.44  ? 77  ASP A N   1 
ATOM   641  N N   B ASP A 1 78  ? 12.639 21.057 -14.035 0.30 16.49  ? 77  ASP A N   1 
ATOM   642  C CA  A ASP A 1 78  ? 12.669 21.000 -15.501 0.70 17.20  ? 77  ASP A CA  1 
ATOM   643  C CA  B ASP A 1 78  ? 12.646 21.049 -15.527 0.30 16.32  ? 77  ASP A CA  1 
ATOM   644  C C   A ASP A 1 78  ? 13.816 21.802 -16.117 0.70 17.21  ? 77  ASP A C   1 
ATOM   645  C C   B ASP A 1 78  ? 13.775 21.930 -16.071 0.30 16.72  ? 77  ASP A C   1 
ATOM   646  O O   A ASP A 1 78  ? 13.714 22.203 -17.271 0.70 21.77  ? 77  ASP A O   1 
ATOM   647  O O   B ASP A 1 78  ? 13.558 22.596 -17.097 0.30 21.03  ? 77  ASP A O   1 
ATOM   648  C CB  A ASP A 1 78  ? 11.317 21.410 -16.090 0.70 22.12  ? 77  ASP A CB  1 
ATOM   649  C CB  B ASP A 1 78  ? 11.291 21.462 -16.112 0.30 18.06  ? 77  ASP A CB  1 
ATOM   650  C CG  A ASP A 1 78  ? 11.201 21.086 -17.565 0.70 31.89  ? 77  ASP A CG  1 
ATOM   651  C CG  B ASP A 1 78  ? 10.151 20.585 -15.636 0.30 22.34  ? 77  ASP A CG  1 
ATOM   652  O OD1 A ASP A 1 78  ? 11.706 20.027 -17.972 0.70 39.37  ? 77  ASP A OD1 1 
ATOM   653  O OD1 B ASP A 1 78  ? 10.289 19.359 -15.761 0.30 24.73  ? 77  ASP A OD1 1 
ATOM   654  O OD2 A ASP A 1 78  ? 10.599 21.893 -18.290 0.70 43.01  ? 77  ASP A OD2 1 
ATOM   655  O OD2 B ASP A 1 78  ? 9.169  21.128 -15.107 0.30 28.23  ? 77  ASP A OD2 1 
ATOM   656  N N   . ARG A 1 79  ? 14.948 21.929 -15.428 1.00 15.50  ? 78  ARG A N   1 
ATOM   657  C CA  . ARG A 1 79  ? 16.184 22.364 -16.105 1.00 14.66  ? 78  ARG A CA  1 
ATOM   658  C C   . ARG A 1 79  ? 16.823 21.156 -16.804 1.00 13.45  ? 78  ARG A C   1 
ATOM   659  O O   . ARG A 1 79  ? 17.161 20.168 -16.131 1.00 14.06  ? 78  ARG A O   1 
ATOM   660  C CB  . ARG A 1 79  ? 17.194 22.949 -15.135 1.00 15.33  ? 78  ARG A CB  1 
ATOM   661  C CG  . ARG A 1 79  ? 16.841 24.325 -14.592 1.00 16.16  ? 78  ARG A CG  1 
ATOM   662  C CD  . ARG A 1 79  ? 17.797 24.793 -13.511 1.00 14.65  ? 78  ARG A CD  1 
ATOM   663  N NE  . ARG A 1 79  ? 17.541 24.057 -12.280 1.00 14.02  ? 78  ARG A NE  1 
ATOM   664  C CZ  . ARG A 1 79  ? 18.360 23.271 -11.601 1.00 13.78  ? 78  ARG A CZ  1 
ATOM   665  N NH1 . ARG A 1 79  ? 19.657 23.257 -11.854 1.00 14.76  ? 78  ARG A NH1 1 
ATOM   666  N NH2 . ARG A 1 79  ? 17.877 22.545 -10.616 1.00 15.46  ? 78  ARG A NH2 1 
ATOM   667  N N   . LYS A 1 80  ? 17.095 21.291 -18.088 1.00 13.52  ? 79  LYS A N   1 
ATOM   668  C CA  . LYS A 1 80  ? 17.972 20.365 -18.819 1.00 13.59  ? 79  LYS A CA  1 
ATOM   669  C C   . LYS A 1 80  ? 19.409 20.809 -18.562 1.00 13.31  ? 79  LYS A C   1 
ATOM   670  O O   . LYS A 1 80  ? 19.770 21.931 -18.892 1.00 15.45  ? 79  LYS A O   1 
ATOM   671  C CB  . LYS A 1 80  ? 17.620 20.305 -20.308 1.00 14.99  ? 79  LYS A CB  1 
ATOM   672  C CG  . LYS A 1 80  ? 16.249 19.701 -20.624 1.00 20.49  ? 79  LYS A CG  1 
ATOM   673  C CD  . LYS A 1 80  ? 15.807 19.864 -22.030 0.70 24.53  ? 79  LYS A CD  1 
ATOM   674  C CE  . LYS A 1 80  ? 14.365 19.433 -22.215 1.00 35.54  ? 79  LYS A CE  1 
ATOM   675  N NZ  . LYS A 1 80  ? 13.452 20.122 -21.268 0.70 44.41  ? 79  LYS A NZ  1 
ATOM   676  N N   . VAL A 1 81  ? 20.188 19.945 -17.921 1.00 12.93  ? 80  VAL A N   1 
ATOM   677  C CA  . VAL A 1 81  ? 21.541 20.299 -17.472 1.00 13.02  ? 80  VAL A CA  1 
ATOM   678  C C   . VAL A 1 81  ? 22.523 19.212 -17.937 1.00 13.27  ? 80  VAL A C   1 
ATOM   679  O O   . VAL A 1 81  ? 22.143 18.062 -18.205 1.00 13.10  ? 80  VAL A O   1 
ATOM   680  C CB  . VAL A 1 81  ? 21.571 20.524 -15.947 1.00 12.11  ? 80  VAL A CB  1 
ATOM   681  C CG1 . VAL A 1 81  ? 20.565 21.567 -15.517 1.00 13.90  ? 80  VAL A CG1 1 
ATOM   682  C CG2 . VAL A 1 81  ? 21.351 19.229 -15.170 1.00 12.34  ? 80  VAL A CG2 1 
ATOM   683  N N   . LYS A 1 82  ? 23.782 19.592 -17.898 1.00 12.94  ? 81  LYS A N   1 
ATOM   684  C CA  . LYS A 1 82  ? 24.944 18.686 -18.067 1.00 12.14  ? 81  LYS A CA  1 
ATOM   685  C C   . LYS A 1 82  ? 25.507 18.452 -16.680 1.00 12.44  ? 81  LYS A C   1 
ATOM   686  O O   . LYS A 1 82  ? 25.889 19.401 -15.990 1.00 12.53  ? 81  LYS A O   1 
ATOM   687  C CB  . LYS A 1 82  ? 25.985 19.261 -19.007 1.00 14.67  ? 81  LYS A CB  1 
ATOM   688  C CG  . LYS A 1 82  ? 25.506 19.465 -20.435 1.00 16.44  ? 81  LYS A CG  1 
ATOM   689  C CD  . LYS A 1 82  ? 25.378 18.094 -21.152 1.00 20.33  ? 81  LYS A CD  1 
ATOM   690  C CE  . LYS A 1 82  ? 25.084 18.243 -22.637 1.00 24.65  ? 81  LYS A CE  1 
ATOM   691  N NZ  . LYS A 1 82  ? 24.966 16.934 -23.313 1.00 24.81  ? 81  LYS A NZ  1 
ATOM   692  N N   . SER A 1 83  ? 25.563 17.195 -16.279 1.00 11.84  ? 82  SER A N   1 
ATOM   693  C CA  . SER A 1 83  ? 25.868 16.834 -14.883 1.00 11.07  ? 82  SER A CA  1 
ATOM   694  C C   . SER A 1 83  ? 27.076 15.922 -14.792 1.00 10.34  ? 82  SER A C   1 
ATOM   695  O O   . SER A 1 83  ? 27.361 15.140 -15.698 1.00 11.46  ? 82  SER A O   1 
ATOM   696  C CB  . SER A 1 83  ? 24.693 16.173 -14.224 1.00 11.93  ? 82  SER A CB  1 
ATOM   697  O OG  . SER A 1 83  ? 23.643 17.111 -13.980 1.00 15.65  ? 82  SER A OG  1 
ATOM   698  N N   A ILE A 1 84  ? 27.686 16.001 -13.629 0.90 10.26  ? 83  ILE A N   1 
ATOM   699  N N   B ILE A 1 84  ? 27.835 16.071 -13.712 0.10 8.94   ? 83  ILE A N   1 
ATOM   700  C CA  A ILE A 1 84  ? 28.753 15.050 -13.289 0.90 10.41  ? 83  ILE A CA  1 
ATOM   701  C CA  B ILE A 1 84  ? 28.879 15.087 -13.317 0.10 8.15   ? 83  ILE A CA  1 
ATOM   702  C C   A ILE A 1 84  ? 28.789 14.904 -11.787 0.90 10.51  ? 83  ILE A C   1 
ATOM   703  C C   B ILE A 1 84  ? 28.781 14.897 -11.812 0.10 8.76   ? 83  ILE A C   1 
ATOM   704  O O   A ILE A 1 84  ? 28.595 15.864 -11.055 0.90 12.05  ? 83  ILE A O   1 
ATOM   705  O O   B ILE A 1 84  ? 28.485 15.875 -11.104 0.10 8.83   ? 83  ILE A O   1 
ATOM   706  C CB  A ILE A 1 84  ? 30.100 15.466 -13.915 0.90 12.89  ? 83  ILE A CB  1 
ATOM   707  C CB  B ILE A 1 84  ? 30.299 15.525 -13.717 0.10 7.21   ? 83  ILE A CB  1 
ATOM   708  C CG1 A ILE A 1 84  ? 31.106 14.313 -13.926 0.90 15.15  ? 83  ILE A CG1 1 
ATOM   709  C CG1 B ILE A 1 84  ? 30.356 16.129 -15.120 0.10 6.45   ? 83  ILE A CG1 1 
ATOM   710  C CG2 A ILE A 1 84  ? 30.620 16.719 -13.250 0.90 15.54  ? 83  ILE A CG2 1 
ATOM   711  C CG2 B ILE A 1 84  ? 31.281 14.369 -13.570 0.10 7.30   ? 83  ILE A CG2 1 
ATOM   712  C CD1 A ILE A 1 84  ? 32.223 14.475 -14.884 0.90 17.38  ? 83  ILE A CD1 1 
ATOM   713  C CD1 B ILE A 1 84  ? 31.701 16.717 -15.415 0.10 6.58   ? 83  ILE A CD1 1 
ATOM   714  N N   . VAL A 1 85  ? 29.033 13.672 -11.362 1.00 10.33  ? 84  VAL A N   1 
ATOM   715  C CA  . VAL A 1 85  ? 29.142 13.358 -9.927  1.00 11.00  ? 84  VAL A CA  1 
ATOM   716  C C   . VAL A 1 85  ? 30.536 12.837 -9.714  1.00 10.96  ? 84  VAL A C   1 
ATOM   717  O O   . VAL A 1 85  ? 31.009 11.940 -10.417 1.00 11.58  ? 84  VAL A O   1 
ATOM   718  C CB  . VAL A 1 85  ? 28.085 12.341 -9.479  1.00 10.55  ? 84  VAL A CB  1 
ATOM   719  C CG1 . VAL A 1 85  ? 28.229 12.033 -7.985  1.00 12.64  ? 84  VAL A CG1 1 
ATOM   720  C CG2 . VAL A 1 85  ? 26.679 12.865 -9.787  1.00 11.75  ? 84  VAL A CG2 1 
ATOM   721  N N   . THR A 1 86  ? 31.184 13.423 -8.704  1.00 10.93  ? 85  THR A N   1 
ATOM   722  C CA  . THR A 1 86  ? 32.554 13.104 -8.320  1.00 10.77  ? 85  THR A CA  1 
ATOM   723  C C   . THR A 1 86  ? 32.634 12.878 -6.809  1.00 11.34  ? 85  THR A C   1 
ATOM   724  O O   . THR A 1 86  ? 31.738 13.254 -6.060  1.00 12.53  ? 85  THR A O   1 
ATOM   725  C CB  . THR A 1 86  ? 33.511 14.204 -8.755  1.00 12.91  ? 85  THR A CB  1 
ATOM   726  O OG1 . THR A 1 86  ? 33.104 15.442 -8.151  1.00 14.69  ? 85  THR A OG1 1 
ATOM   727  C CG2 . THR A 1 86  ? 33.573 14.365 -10.255 1.00 13.65  ? 85  THR A CG2 1 
ATOM   728  N N   A LEU A 1 87  ? 33.746 12.313 -6.390  0.90 11.80  ? 86  LEU A N   1 
ATOM   729  N N   B LEU A 1 87  ? 33.717 12.234 -6.358  0.10 9.39   ? 86  LEU A N   1 
ATOM   730  C CA  A LEU A 1 87  ? 34.060 12.108 -4.966  0.90 11.97  ? 86  LEU A CA  1 
ATOM   731  C CA  B LEU A 1 87  ? 34.070 12.066 -4.919  0.10 7.69   ? 86  LEU A CA  1 
ATOM   732  C C   A LEU A 1 87  ? 35.332 12.906 -4.688  0.90 12.07  ? 86  LEU A C   1 
ATOM   733  C C   B LEU A 1 87  ? 35.311 12.916 -4.620  0.10 8.70   ? 86  LEU A C   1 
ATOM   734  O O   A LEU A 1 87  ? 36.417 12.688 -5.267  0.90 13.91  ? 86  LEU A O   1 
ATOM   735  O O   B LEU A 1 87  ? 36.398 12.617 -5.165  0.10 9.38   ? 86  LEU A O   1 
ATOM   736  C CB  A LEU A 1 87  ? 34.293 10.617 -4.724  0.90 14.81  ? 86  LEU A CB  1 
ATOM   737  C CB  B LEU A 1 87  ? 34.370 10.593 -4.615  0.10 6.83   ? 86  LEU A CB  1 
ATOM   738  C CG  A LEU A 1 87  ? 34.488 10.230 -3.285  0.90 18.22  ? 86  LEU A CG  1 
ATOM   739  C CG  B LEU A 1 87  ? 33.177 9.680  -4.337  0.10 5.95   ? 86  LEU A CG  1 
ATOM   740  C CD1 A LEU A 1 87  ? 33.188 10.457 -2.520  0.90 19.47  ? 86  LEU A CD1 1 
ATOM   741  C CD1 B LEU A 1 87  ? 33.645 8.233  -4.340  0.10 5.72   ? 86  LEU A CD1 1 
ATOM   742  C CD2 A LEU A 1 87  ? 34.896 8.780  -3.232  0.90 23.47  ? 86  LEU A CD2 1 
ATOM   743  C CD2 B LEU A 1 87  ? 32.527 10.003 -3.005  0.10 6.04   ? 86  LEU A CD2 1 
ATOM   744  N N   A ASP A 1 88  ? 35.191 13.876 -3.805  0.80 14.74  ? 87  ASP A N   1 
ATOM   745  N N   B ASP A 1 88  ? 35.177 13.927 -3.764  0.20 9.74   ? 87  ASP A N   1 
ATOM   746  C CA  A ASP A 1 88  ? 36.245 14.852 -3.462  0.80 15.84  ? 87  ASP A CA  1 
ATOM   747  C CA  B ASP A 1 88  ? 36.277 14.866 -3.469  0.20 11.20  ? 87  ASP A CA  1 
ATOM   748  C C   A ASP A 1 88  ? 36.472 14.649 -1.961  0.80 16.06  ? 87  ASP A C   1 
ATOM   749  C C   B ASP A 1 88  ? 36.548 14.739 -1.971  0.20 13.50  ? 87  ASP A C   1 
ATOM   750  O O   A ASP A 1 88  ? 35.667 15.155 -1.159  0.80 18.86  ? 87  ASP A O   1 
ATOM   751  O O   B ASP A 1 88  ? 35.916 15.462 -1.180  0.20 15.52  ? 87  ASP A O   1 
ATOM   752  C CB  A ASP A 1 88  ? 35.796 16.292 -3.719  0.80 19.40  ? 87  ASP A CB  1 
ATOM   753  C CB  B ASP A 1 88  ? 35.925 16.257 -3.980  0.20 10.64  ? 87  ASP A CB  1 
ATOM   754  C CG  A ASP A 1 88  ? 35.630 16.722 -5.158  0.80 28.46  ? 87  ASP A CG  1 
ATOM   755  C CG  B ASP A 1 88  ? 37.090 17.205 -3.804  0.20 12.62  ? 87  ASP A CG  1 
ATOM   756  O OD1 A ASP A 1 88  ? 35.871 15.912 -6.024  0.80 34.60  ? 87  ASP A OD1 1 
ATOM   757  O OD1 B ASP A 1 88  ? 38.056 16.799 -3.133  0.20 12.68  ? 87  ASP A OD1 1 
ATOM   758  O OD2 A ASP A 1 88  ? 35.242 17.910 -5.389  0.80 30.38  ? 87  ASP A OD2 1 
ATOM   759  O OD2 B ASP A 1 88  ? 37.015 18.337 -4.329  0.20 16.52  ? 87  ASP A OD2 1 
ATOM   760  N N   . GLY A 1 89  ? 37.409 13.786 -1.613  1.00 16.71  ? 88  GLY A N   1 
ATOM   761  C CA  . GLY A 1 89  ? 37.583 13.366 -0.210  1.00 19.49  ? 88  GLY A CA  1 
ATOM   762  C C   . GLY A 1 89  ? 36.317 12.692 0.266   1.00 18.25  ? 88  GLY A C   1 
ATOM   763  O O   . GLY A 1 89  ? 35.879 11.727 -0.338  1.00 22.37  ? 88  GLY A O   1 
ATOM   764  N N   . GLY A 1 90  ? 35.717 13.206 1.308   1.00 23.61  ? 89  GLY A N   1 
ATOM   765  C CA  . GLY A 1 90  ? 34.458 12.607 1.787   1.00 25.62  ? 89  GLY A CA  1 
ATOM   766  C C   . GLY A 1 90  ? 33.196 13.188 1.184   1.00 20.54  ? 89  GLY A C   1 
ATOM   767  O O   . GLY A 1 90  ? 32.114 12.811 1.594   1.00 25.06  ? 89  GLY A O   1 
ATOM   768  N N   . LYS A 1 91  ? 33.303 14.044 0.187   1.00 17.25  ? 90  LYS A N   1 
ATOM   769  C CA  . LYS A 1 91  ? 32.157 14.786 -0.377  1.00 17.99  ? 90  LYS A CA  1 
ATOM   770  C C   . LYS A 1 91  ? 31.768 14.110 -1.699  1.00 14.82  ? 90  LYS A C   1 
ATOM   771  O O   . LYS A 1 91  ? 32.616 13.984 -2.599  1.00 16.60  ? 90  LYS A O   1 
ATOM   772  C CB  . LYS A 1 91  ? 32.503 16.263 -0.589  1.00 19.46  ? 90  LYS A CB  1 
ATOM   773  C CG  . LYS A 1 91  ? 32.707 17.100 0.684   1.00 27.21  ? 90  LYS A CG  1 
ATOM   774  C CD  . LYS A 1 91  ? 33.214 18.504 0.355   1.00 34.03  ? 90  LYS A CD  1 
ATOM   775  C CE  . LYS A 1 91  ? 33.528 19.393 1.533   1.00 41.46  ? 90  LYS A CE  1 
ATOM   776  N NZ  . LYS A 1 91  ? 33.669 20.812 1.106   1.00 50.56  ? 90  LYS A NZ  1 
ATOM   777  N N   . LEU A 1 92  ? 30.492 13.738 -1.821  1.00 14.52  ? 91  LEU A N   1 
ATOM   778  C CA  . LEU A 1 92  ? 29.921 13.305 -3.097  1.00 13.22  ? 91  LEU A CA  1 
ATOM   779  C C   . LEU A 1 92  ? 29.333 14.544 -3.763  1.00 11.31  ? 91  LEU A C   1 
ATOM   780  O O   . LEU A 1 92  ? 28.341 15.103 -3.247  1.00 12.01  ? 91  LEU A O   1 
ATOM   781  C CB  . LEU A 1 92  ? 28.873 12.244 -2.816  1.00 14.40  ? 91  LEU A CB  1 
ATOM   782  C CG  . LEU A 1 92  ? 28.288 11.581 -4.052  1.00 13.86  ? 91  LEU A CG  1 
ATOM   783  C CD1 . LEU A 1 92  ? 29.332 10.726 -4.766  1.00 15.83  ? 91  LEU A CD1 1 
ATOM   784  C CD2 . LEU A 1 92  ? 27.056 10.759 -3.669  1.00 17.79  ? 91  LEU A CD2 1 
ATOM   785  N N   . VAL A 1 93  ? 29.953 14.984 -4.818  1.00 11.38  ? 92  VAL A N   1 
ATOM   786  C CA  . VAL A 1 93  ? 29.682 16.305 -5.439  1.00 11.86  ? 92  VAL A CA  1 
ATOM   787  C C   . VAL A 1 93  ? 28.916 16.100 -6.739  1.00 11.39  ? 92  VAL A C   1 
ATOM   788  O O   . VAL A 1 93  ? 29.456 15.487 -7.666  1.00 13.61  ? 92  VAL A O   1 
ATOM   789  C CB  . VAL A 1 93  ? 30.971 17.093 -5.693  1.00 14.08  ? 92  VAL A CB  1 
ATOM   790  C CG1 . VAL A 1 93  ? 30.658 18.431 -6.339  1.00 14.93  ? 92  VAL A CG1 1 
ATOM   791  C CG2 . VAL A 1 93  ? 31.736 17.253 -4.409  1.00 15.38  ? 92  VAL A CG2 1 
ATOM   792  N N   . HIS A 1 94  ? 27.686 16.604 -6.806  1.00 10.81  ? 93  HIS A N   1 
ATOM   793  C CA  . HIS A 1 94  ? 26.875 16.595 -8.040  1.00 11.41  ? 93  HIS A CA  1 
ATOM   794  C C   . HIS A 1 94  ? 26.915 18.002 -8.609  1.00 10.93  ? 93  HIS A C   1 
ATOM   795  O O   . HIS A 1 94  ? 26.302 18.885 -8.003  1.00 12.07  ? 93  HIS A O   1 
ATOM   796  C CB  . HIS A 1 94  ? 25.488 16.073 -7.713  1.00 11.55  ? 93  HIS A CB  1 
ATOM   797  C CG  . HIS A 1 94  ? 24.581 16.053 -8.871  1.00 11.61  ? 93  HIS A CG  1 
ATOM   798  N ND1 . HIS A 1 94  ? 23.263 15.754 -8.710  1.00 13.20  ? 93  HIS A ND1 1 
ATOM   799  C CD2 . HIS A 1 94  ? 24.786 16.263 -10.188 1.00 12.72  ? 93  HIS A CD2 1 
ATOM   800  C CE1 . HIS A 1 94  ? 22.671 15.798 -9.925  1.00 13.91  ? 93  HIS A CE1 1 
ATOM   801  N NE2 . HIS A 1 94  ? 23.574 16.122 -10.831 1.00 14.27  ? 93  HIS A NE2 1 
ATOM   802  N N   . LEU A 1 95  ? 27.576 18.175 -9.729  1.00 11.12  ? 94  LEU A N   1 
ATOM   803  C CA  . LEU A 1 95  ? 27.621 19.453 -10.464 1.00 11.70  ? 94  LEU A CA  1 
ATOM   804  C C   . LEU A 1 95  ? 26.612 19.405 -11.592 1.00 12.01  ? 94  LEU A C   1 
ATOM   805  O O   . LEU A 1 95  ? 26.601 18.463 -12.330 1.00 13.28  ? 94  LEU A O   1 
ATOM   806  C CB  . LEU A 1 95  ? 29.033 19.649 -10.983 1.00 13.37  ? 94  LEU A CB  1 
ATOM   807  C CG  . LEU A 1 95  ? 29.232 20.856 -11.903 1.00 15.71  ? 94  LEU A CG  1 
ATOM   808  C CD1 . LEU A 1 95  ? 29.051 22.157 -11.158 1.00 17.13  ? 94  LEU A CD1 1 
ATOM   809  C CD2 . LEU A 1 95  ? 30.592 20.792 -12.545 1.00 18.32  ? 94  LEU A CD2 1 
ATOM   810  N N   . GLN A 1 96  ? 25.818 20.481 -11.696 1.00 11.32  ? 95  GLN A N   1 
ATOM   811  C CA  . GLN A 1 96  ? 24.893 20.712 -12.823 1.00 11.88  ? 95  GLN A CA  1 
ATOM   812  C C   . GLN A 1 96  ? 25.311 22.000 -13.529 1.00 12.11  ? 95  GLN A C   1 
ATOM   813  O O   . GLN A 1 96  ? 25.425 23.033 -12.854 1.00 14.02  ? 95  GLN A O   1 
ATOM   814  C CB  . GLN A 1 96  ? 23.474 20.829 -12.296 1.00 12.17  ? 95  GLN A CB  1 
ATOM   815  C CG  . GLN A 1 96  ? 22.911 19.618 -11.571 1.00 12.10  ? 95  GLN A CG  1 
ATOM   816  C CD  . GLN A 1 96  ? 21.566 19.825 -10.939 1.00 11.70  ? 95  GLN A CD  1 
ATOM   817  O OE1 . GLN A 1 96  ? 21.213 20.986 -10.632 1.00 13.78  ? 95  GLN A OE1 1 
ATOM   818  N NE2 . GLN A 1 96  ? 20.806 18.755 -10.742 1.00 13.16  ? 95  GLN A NE2 1 
ATOM   819  N N   . LYS A 1 97  ? 25.468 21.930 -14.827 1.00 12.17  ? 96  LYS A N   1 
ATOM   820  C CA  . LYS A 1 97  ? 25.818 23.104 -15.660 1.00 13.28  ? 96  LYS A CA  1 
ATOM   821  C C   . LYS A 1 97  ? 24.788 23.314 -16.741 1.00 12.98  ? 96  LYS A C   1 
ATOM   822  O O   . LYS A 1 97  ? 24.292 22.358 -17.347 1.00 13.44  ? 96  LYS A O   1 
ATOM   823  C CB  . LYS A 1 97  ? 27.190 22.909 -16.297 1.00 15.95  ? 96  LYS A CB  1 
ATOM   824  C CG  . LYS A 1 97  ? 28.353 22.774 -15.351 1.00 19.37  ? 96  LYS A CG  1 
ATOM   825  C CD  . LYS A 1 97  ? 29.671 22.767 -16.090 1.00 28.18  ? 96  LYS A CD  1 
ATOM   826  C CE  . LYS A 1 97  ? 30.349 24.122 -16.160 0.80 41.40  ? 96  LYS A CE  1 
ATOM   827  N NZ  . LYS A 1 97  ? 30.468 24.787 -14.830 0.80 46.80  ? 96  LYS A NZ  1 
ATOM   828  N N   . TRP A 1 98  ? 24.464 24.577 -16.979 1.00 13.58  ? 97  TRP A N   1 
ATOM   829  C CA  . TRP A 1 98  ? 23.555 24.923 -18.101 1.00 13.79  ? 97  TRP A CA  1 
ATOM   830  C C   . TRP A 1 98  ? 23.698 26.422 -18.385 1.00 14.25  ? 97  TRP A C   1 
ATOM   831  O O   . TRP A 1 98  ? 23.822 27.199 -17.398 1.00 15.21  ? 97  TRP A O   1 
ATOM   832  C CB  . TRP A 1 98  ? 22.082 24.584 -17.823 1.00 14.01  ? 97  TRP A CB  1 
ATOM   833  C CG  . TRP A 1 98  ? 21.444 25.435 -16.782 1.00 14.19  ? 97  TRP A CG  1 
ATOM   834  C CD1 . TRP A 1 98  ? 20.571 26.465 -17.023 1.00 15.17  ? 97  TRP A CD1 1 
ATOM   835  C CD2 . TRP A 1 98  ? 21.655 25.413 -15.364 1.00 14.20  ? 97  TRP A CD2 1 
ATOM   836  N NE1 . TRP A 1 98  ? 20.235 27.074 -15.848 1.00 16.49  ? 97  TRP A NE1 1 
ATOM   837  C CE2 . TRP A 1 98  ? 20.897 26.469 -14.819 1.00 14.96  ? 97  TRP A CE2 1 
ATOM   838  C CE3 . TRP A 1 98  ? 22.428 24.643 -14.502 1.00 13.94  ? 97  TRP A CE3 1 
ATOM   839  C CZ2 . TRP A 1 98  ? 20.901 26.768 -13.462 1.00 14.61  ? 97  TRP A CZ2 1 
ATOM   840  C CZ3 . TRP A 1 98  ? 22.465 24.952 -13.163 1.00 14.52  ? 97  TRP A CZ3 1 
ATOM   841  C CH2 . TRP A 1 98  ? 21.710 26.011 -12.649 1.00 15.82  ? 97  TRP A CH2 1 
ATOM   842  N N   . ASP A 1 99  ? 23.661 26.794 -19.653 1.00 15.36  ? 98  ASP A N   1 
ATOM   843  C CA  . ASP A 1 99  ? 23.418 28.200 -20.056 1.00 15.76  ? 98  ASP A CA  1 
ATOM   844  C C   . ASP A 1 99  ? 24.431 29.121 -19.381 1.00 15.67  ? 98  ASP A C   1 
ATOM   845  O O   . ASP A 1 99  ? 24.075 30.223 -18.994 1.00 19.84  ? 98  ASP A O   1 
ATOM   846  C CB  . ASP A 1 99  ? 21.993 28.642 -19.714 1.00 16.55  ? 98  ASP A CB  1 
ATOM   847  C CG  . ASP A 1 99  ? 20.888 27.843 -20.369 1.00 15.60  ? 98  ASP A CG  1 
ATOM   848  O OD1 . ASP A 1 99  ? 21.203 26.832 -21.131 1.00 16.89  ? 98  ASP A OD1 1 
ATOM   849  O OD2 . ASP A 1 99  ? 19.734 28.258 -20.204 1.00 15.75  ? 98  ASP A OD2 1 
ATOM   850  N N   . GLY A 1 100 ? 25.679 28.661 -19.270 1.00 16.30  ? 99  GLY A N   1 
ATOM   851  C CA  . GLY A 1 100 ? 26.791 29.442 -18.728 1.00 18.34  ? 99  GLY A CA  1 
ATOM   852  C C   . GLY A 1 100 ? 26.764 29.575 -17.209 1.00 16.93  ? 99  GLY A C   1 
ATOM   853  O O   . GLY A 1 100 ? 27.572 30.344 -16.667 1.00 21.20  ? 99  GLY A O   1 
ATOM   854  N N   . GLN A 1 101 ? 25.905 28.831 -16.510 1.00 15.38  ? 100 GLN A N   1 
ATOM   855  C CA  . GLN A 1 101 ? 25.876 28.863 -15.047 1.00 15.99  ? 100 GLN A CA  1 
ATOM   856  C C   . GLN A 1 101 ? 25.971 27.447 -14.477 1.00 15.12  ? 100 GLN A C   1 
ATOM   857  O O   . GLN A 1 101 ? 25.998 26.476 -15.229 1.00 15.11  ? 100 GLN A O   1 
ATOM   858  C CB  . GLN A 1 101 ? 24.685 29.651 -14.527 1.00 19.63  ? 100 GLN A CB  1 
ATOM   859  C CG  . GLN A 1 101 ? 23.323 29.105 -14.885 1.00 20.94  ? 100 GLN A CG  1 
ATOM   860  C CD  . GLN A 1 101 ? 22.193 29.969 -14.359 1.00 17.78  ? 100 GLN A CD  1 
ATOM   861  O OE1 . GLN A 1 101 ? 21.159 30.151 -15.017 1.00 25.72  ? 100 GLN A OE1 1 
ATOM   862  N NE2 . GLN A 1 101 ? 22.306 30.367 -13.109 1.00 18.03  ? 100 GLN A NE2 1 
ATOM   863  N N   . GLU A 1 102 ? 25.953 27.345 -13.172 1.00 14.16  ? 101 GLU A N   1 
ATOM   864  C CA  . GLU A 1 102 ? 26.068 26.037 -12.523 1.00 14.56  ? 101 GLU A CA  1 
ATOM   865  C C   . GLU A 1 102 ? 25.494 26.065 -11.115 1.00 13.29  ? 101 GLU A C   1 
ATOM   866  O O   . GLU A 1 102 ? 25.360 27.127 -10.494 1.00 15.87  ? 101 GLU A O   1 
ATOM   867  C CB  . GLU A 1 102 ? 27.505 25.556 -12.471 1.00 16.31  ? 101 GLU A CB  1 
ATOM   868  C CG  . GLU A 1 102 ? 28.442 26.433 -11.667 1.00 20.14  ? 101 GLU A CG  1 
ATOM   869  C CD  . GLU A 1 102 ? 29.794 25.810 -11.387 1.00 24.50  ? 101 GLU A CD  1 
ATOM   870  O OE1 . GLU A 1 102 ? 30.517 25.516 -12.335 1.00 29.98  ? 101 GLU A OE1 1 
ATOM   871  O OE2 . GLU A 1 102 ? 30.091 25.567 -10.189 1.00 32.01  ? 101 GLU A OE2 1 
ATOM   872  N N   . THR A 1 103 ? 25.279 24.867 -10.579 1.00 13.26  ? 102 THR A N   1 
ATOM   873  C CA  . THR A 1 103 ? 24.933 24.667 -9.168  1.00 12.16  ? 102 THR A CA  1 
ATOM   874  C C   . THR A 1 103 ? 25.624 23.385 -8.730  1.00 11.73  ? 102 THR A C   1 
ATOM   875  O O   . THR A 1 103 ? 25.713 22.445 -9.523  1.00 12.69  ? 102 THR A O   1 
ATOM   876  C CB  . THR A 1 103 ? 23.416 24.722 -8.952  1.00 12.90  ? 102 THR A CB  1 
ATOM   877  O OG1 . THR A 1 103 ? 23.169 24.724 -7.547  1.00 13.66  ? 102 THR A OG1 1 
ATOM   878  C CG2 . THR A 1 103 ? 22.672 23.584 -9.616  1.00 13.04  ? 102 THR A CG2 1 
ATOM   879  N N   . THR A 1 104 ? 25.989 23.345 -7.468  1.00 12.29  ? 103 THR A N   1 
ATOM   880  C CA  . THR A 1 104 ? 26.491 22.101 -6.867  1.00 13.56  ? 103 THR A CA  1 
ATOM   881  C C   . THR A 1 104 ? 25.549 21.627 -5.769  1.00 13.25  ? 103 THR A C   1 
ATOM   882  O O   . THR A 1 104 ? 25.033 22.417 -4.973  1.00 15.60  ? 103 THR A O   1 
ATOM   883  C CB  . THR A 1 104 ? 27.913 22.255 -6.360  1.00 16.65  ? 103 THR A CB  1 
ATOM   884  O OG1 . THR A 1 104 ? 27.924 23.248 -5.329  1.00 17.97  ? 103 THR A OG1 1 
ATOM   885  C CG2 . THR A 1 104 ? 28.866 22.535 -7.489  1.00 20.43  ? 103 THR A CG2 1 
ATOM   886  N N   . LEU A 1 105 ? 25.433 20.301 -5.722  1.00 12.49  ? 104 LEU A N   1 
ATOM   887  C CA  . LEU A 1 105 ? 24.662 19.567 -4.708  1.00 13.05  ? 104 LEU A CA  1 
ATOM   888  C C   . LEU A 1 105 ? 25.677 18.625 -4.059  1.00 13.81  ? 104 LEU A C   1 
ATOM   889  O O   . LEU A 1 105 ? 26.089 17.649 -4.677  1.00 13.99  ? 104 LEU A O   1 
ATOM   890  C CB  . LEU A 1 105 ? 23.464 18.846 -5.339  1.00 14.44  ? 104 LEU A CB  1 
ATOM   891  C CG  . LEU A 1 105 ? 22.451 19.680 -6.130  1.00 16.54  ? 104 LEU A CG  1 
ATOM   892  C CD1 . LEU A 1 105 ? 22.893 19.759 -7.599  1.00 21.48  ? 104 LEU A CD1 1 
ATOM   893  C CD2 . LEU A 1 105 ? 21.071 19.079 -6.104  1.00 21.55  ? 104 LEU A CD2 1 
ATOM   894  N N   . VAL A 1 106 ? 26.126 18.971 -2.858  1.00 13.00  ? 105 VAL A N   1 
ATOM   895  C CA  . VAL A 1 106 ? 27.260 18.292 -2.196  1.00 13.18  ? 105 VAL A CA  1 
ATOM   896  C C   . VAL A 1 106 ? 26.712 17.511 -1.024  1.00 12.02  ? 105 VAL A C   1 
ATOM   897  O O   . VAL A 1 106 ? 26.057 18.088 -0.179  1.00 13.54  ? 105 VAL A O   1 
ATOM   898  C CB  . VAL A 1 106 ? 28.329 19.297 -1.752  1.00 15.40  ? 105 VAL A CB  1 
ATOM   899  C CG1 . VAL A 1 106 ? 29.404 18.638 -0.912  1.00 17.58  ? 105 VAL A CG1 1 
ATOM   900  C CG2 . VAL A 1 106 ? 28.943 20.016 -2.943  1.00 16.77  ? 105 VAL A CG2 1 
ATOM   901  N N   . ARG A 1 107 ? 27.066 16.226 -0.961  1.00 12.19  ? 106 ARG A N   1 
ATOM   902  C CA  . ARG A 1 107 ? 26.671 15.361 0.169   1.00 12.08  ? 106 ARG A CA  1 
ATOM   903  C C   . ARG A 1 107 ? 27.884 14.948 0.983   1.00 13.00  ? 106 ARG A C   1 
ATOM   904  O O   . ARG A 1 107 ? 28.906 14.548 0.399   1.00 13.46  ? 106 ARG A O   1 
ATOM   905  C CB  . ARG A 1 107 ? 25.908 14.164 -0.367  1.00 12.34  ? 106 ARG A CB  1 
ATOM   906  C CG  . ARG A 1 107 ? 24.549 14.520 -0.923  1.00 12.32  ? 106 ARG A CG  1 
ATOM   907  C CD  . ARG A 1 107 ? 23.836 13.340 -1.547  1.00 14.37  ? 106 ARG A CD  1 
ATOM   908  N NE  . ARG A 1 107 ? 22.447 13.628 -1.881  1.00 15.09  ? 106 ARG A NE  1 
ATOM   909  C CZ  . ARG A 1 107 ? 22.034 14.148 -3.032  1.00 14.01  ? 106 ARG A CZ  1 
ATOM   910  N NH1 . ARG A 1 107 ? 22.865 14.403 -4.018  1.00 14.05  ? 106 ARG A NH1 1 
ATOM   911  N NH2 . ARG A 1 107 ? 20.754 14.362 -3.250  1.00 15.69  ? 106 ARG A NH2 1 
ATOM   912  N N   . GLU A 1 108 ? 27.781 15.072 2.295   1.00 14.17  ? 107 GLU A N   1 
ATOM   913  C CA  . GLU A 1 108 ? 28.855 14.724 3.219   1.00 14.96  ? 107 GLU A CA  1 
ATOM   914  C C   . GLU A 1 108 ? 28.193 14.039 4.416   1.00 15.38  ? 107 GLU A C   1 
ATOM   915  O O   . GLU A 1 108 ? 27.129 14.443 4.827   1.00 18.30  ? 107 GLU A O   1 
ATOM   916  C CB  . GLU A 1 108 ? 29.636 15.983 3.619   1.00 21.59  ? 107 GLU A CB  1 
ATOM   917  C CG  . GLU A 1 108 ? 30.908 15.686 4.356   1.00 26.65  ? 107 GLU A CG  1 
ATOM   918  C CD  . GLU A 1 108 ? 31.834 16.881 4.544   1.00 27.05  ? 107 GLU A CD  1 
ATOM   919  O OE1 . GLU A 1 108 ? 31.342 18.047 4.393   1.00 31.52  ? 107 GLU A OE1 1 
ATOM   920  O OE2 . GLU A 1 108 ? 33.037 16.641 4.838   1.00 38.24  ? 107 GLU A OE2 1 
ATOM   921  N N   . LEU A 1 109 ? 28.872 13.069 5.002   1.00 16.44  ? 108 LEU A N   1 
ATOM   922  C CA  . LEU A 1 109 ? 28.389 12.394 6.212   1.00 19.24  ? 108 LEU A CA  1 
ATOM   923  C C   . LEU A 1 109 ? 29.093 13.040 7.401   1.00 19.91  ? 108 LEU A C   1 
ATOM   924  O O   . LEU A 1 109 ? 30.337 13.085 7.438   1.00 22.81  ? 108 LEU A O   1 
ATOM   925  C CB  . LEU A 1 109 ? 28.693 10.911 6.080   1.00 21.78  ? 108 LEU A CB  1 
ATOM   926  C CG  . LEU A 1 109 ? 28.069 10.242 4.862   1.00 25.56  ? 108 LEU A CG  1 
ATOM   927  C CD1 . LEU A 1 109 ? 28.542 8.816  4.724   1.00 38.98  ? 108 LEU A CD1 1 
ATOM   928  C CD2 . LEU A 1 109 ? 26.563 10.283 4.933   1.00 31.08  ? 108 LEU A CD2 1 
ATOM   929  N N   . ILE A 1 110 ? 28.293 13.527 8.334   1.00 21.94  ? 109 ILE A N   1 
ATOM   930  C CA  . ILE A 1 110 ? 28.756 14.185 9.573   1.00 25.17  ? 109 ILE A CA  1 
ATOM   931  C C   . ILE A 1 110 ? 27.933 13.574 10.706  1.00 27.52  ? 109 ILE A C   1 
ATOM   932  O O   . ILE A 1 110 ? 26.680 13.693 10.680  1.00 27.67  ? 109 ILE A O   1 
ATOM   933  C CB  . ILE A 1 110 ? 28.615 15.715 9.432   1.00 29.61  ? 109 ILE A CB  1 
ATOM   934  C CG1 . ILE A 1 110 ? 29.341 16.233 8.180   1.00 33.67  ? 109 ILE A CG1 1 
ATOM   935  C CG2 . ILE A 1 110 ? 29.099 16.444 10.670  1.00 35.05  ? 109 ILE A CG2 1 
ATOM   936  C CD1 . ILE A 1 110 ? 29.253 17.726 8.014   1.00 42.93  ? 109 ILE A CD1 1 
ATOM   937  N N   . ASP A 1 111 ? 28.606 12.901 11.640  1.00 31.18  ? 110 ASP A N   1 
ATOM   938  C CA  . ASP A 1 111 ? 27.940 12.291 12.816  1.00 36.04  ? 110 ASP A CA  1 
ATOM   939  C C   . ASP A 1 111 ? 26.798 11.367 12.361  1.00 31.40  ? 110 ASP A C   1 
ATOM   940  O O   . ASP A 1 111 ? 25.753 11.361 13.012  1.00 36.27  ? 110 ASP A O   1 
ATOM   941  C CB  . ASP A 1 111 ? 27.375 13.381 13.728  1.00 42.29  ? 110 ASP A CB  1 
ATOM   942  C CG  . ASP A 1 111 ? 28.431 14.288 14.343  1.00 52.45  ? 110 ASP A CG  1 
ATOM   943  O OD1 . ASP A 1 111 ? 29.623 13.879 14.371  1.00 48.11  ? 110 ASP A OD1 1 
ATOM   944  O OD2 . ASP A 1 111 ? 28.059 15.397 14.809  1.00 66.73  ? 110 ASP A OD2 1 
ATOM   945  N N   . GLY A 1 112 ? 26.983 10.625 11.275  1.00 30.65  ? 111 GLY A N   1 
ATOM   946  C CA  . GLY A 1 112 ? 26.013 9.637  10.773  1.00 29.97  ? 111 GLY A CA  1 
ATOM   947  C C   . GLY A 1 112 ? 24.874 10.255 9.981   1.00 30.90  ? 111 GLY A C   1 
ATOM   948  O O   . GLY A 1 112 ? 24.063 9.487  9.436   1.00 28.50  ? 111 GLY A O   1 
ATOM   949  N N   . LYS A 1 113 ? 24.791 11.584 9.899   1.00 23.22  ? 112 LYS A N   1 
ATOM   950  C CA  . LYS A 1 113 ? 23.724 12.272 9.137   1.00 22.39  ? 112 LYS A CA  1 
ATOM   951  C C   . LYS A 1 113 ? 24.310 12.623 7.787   1.00 20.62  ? 112 LYS A C   1 
ATOM   952  O O   . LYS A 1 113 ? 25.549 12.864 7.660   1.00 22.53  ? 112 LYS A O   1 
ATOM   953  C CB  . LYS A 1 113 ? 23.227 13.552 9.797   1.00 26.03  ? 112 LYS A CB  1 
ATOM   954  C CG  . LYS A 1 113 ? 22.594 13.333 11.171  1.00 34.80  ? 112 LYS A CG  1 
ATOM   955  C CD  . LYS A 1 113 ? 22.044 14.589 11.757  1.00 38.22  ? 112 LYS A CD  1 
ATOM   956  C CE  . LYS A 1 113 ? 21.719 14.482 13.229  1.00 55.86  ? 112 LYS A CE  1 
ATOM   957  N NZ  . LYS A 1 113 ? 21.497 15.833 13.782  1.00 68.62  ? 112 LYS A NZ  1 
ATOM   958  N N   A LEU A 1 114 ? 23.454 12.653 6.779   0.35 17.96  ? 113 LEU A N   1 
ATOM   959  N N   B LEU A 1 114 ? 23.417 12.711 6.818   0.65 19.17  ? 113 LEU A N   1 
ATOM   960  C CA  A LEU A 1 114 ? 23.869 13.093 5.435   0.35 15.21  ? 113 LEU A CA  1 
ATOM   961  C CA  B LEU A 1 114 ? 23.757 13.095 5.435   0.65 17.63  ? 113 LEU A CA  1 
ATOM   962  C C   A LEU A 1 114 ? 23.458 14.561 5.276   0.35 16.29  ? 113 LEU A C   1 
ATOM   963  C C   B LEU A 1 114 ? 23.428 14.588 5.276   0.65 18.05  ? 113 LEU A C   1 
ATOM   964  O O   A LEU A 1 114 ? 22.275 14.886 5.408   0.35 18.31  ? 113 LEU A O   1 
ATOM   965  O O   B LEU A 1 114 ? 22.266 14.967 5.392   0.65 19.64  ? 113 LEU A O   1 
ATOM   966  C CB  A LEU A 1 114 ? 23.257 12.184 4.372   0.35 13.73  ? 113 LEU A CB  1 
ATOM   967  C CB  B LEU A 1 114 ? 22.988 12.202 4.456   0.65 21.32  ? 113 LEU A CB  1 
ATOM   968  C CG  A LEU A 1 114 ? 23.649 12.498 2.935   0.35 12.76  ? 113 LEU A CG  1 
ATOM   969  C CG  B LEU A 1 114 ? 23.195 12.488 2.972   0.65 21.73  ? 113 LEU A CG  1 
ATOM   970  C CD1 A LEU A 1 114 ? 23.373 11.286 2.064   0.35 12.48  ? 113 LEU A CD1 1 
ATOM   971  C CD1 B LEU A 1 114 ? 24.611 12.172 2.575   0.65 26.18  ? 113 LEU A CD1 1 
ATOM   972  C CD2 A LEU A 1 114 ? 22.921 13.741 2.423   0.35 11.57  ? 113 LEU A CD2 1 
ATOM   973  C CD2 B LEU A 1 114 ? 22.233 11.688 2.108   0.65 26.76  ? 113 LEU A CD2 1 
ATOM   974  N N   . ILE A 1 115 ? 24.463 15.416 5.095   1.00 15.80  ? 114 ILE A N   1 
ATOM   975  C CA  . ILE A 1 115 ? 24.302 16.875 4.939   1.00 15.86  ? 114 ILE A CA  1 
ATOM   976  C C   . ILE A 1 115 ? 24.381 17.153 3.443   1.00 13.81  ? 114 ILE A C   1 
ATOM   977  O O   . ILE A 1 115 ? 25.441 16.883 2.841   1.00 14.37  ? 114 ILE A O   1 
ATOM   978  C CB  . ILE A 1 115 ? 25.351 17.654 5.730   1.00 17.24  ? 114 ILE A CB  1 
ATOM   979  C CG1 . ILE A 1 115 ? 25.406 17.184 7.191   1.00 21.36  ? 114 ILE A CG1 1 
ATOM   980  C CG2 . ILE A 1 115 ? 25.101 19.155 5.612   1.00 20.67  ? 114 ILE A CG2 1 
ATOM   981  C CD1 . ILE A 1 115 ? 24.069 17.189 7.895   1.00 25.20  ? 114 ILE A CD1 1 
ATOM   982  N N   . LEU A 1 116 ? 23.323 17.704 2.877   1.00 14.12  ? 115 LEU A N   1 
ATOM   983  C CA  . LEU A 1 116 ? 23.254 18.094 1.459   1.00 13.71  ? 115 LEU A CA  1 
ATOM   984  C C   . LEU A 1 116 ? 23.353 19.616 1.401   1.00 13.57  ? 115 LEU A C   1 
ATOM   985  O O   . LEU A 1 116 ? 22.467 20.303 1.957   1.00 15.68  ? 115 LEU A O   1 
ATOM   986  C CB  . LEU A 1 116 ? 21.942 17.588 0.845   1.00 15.18  ? 115 LEU A CB  1 
ATOM   987  C CG  . LEU A 1 116 ? 21.627 18.127 -0.556  1.00 14.93  ? 115 LEU A CG  1 
ATOM   988  C CD1 . LEU A 1 116 ? 22.683 17.690 -1.558  1.00 14.43  ? 115 LEU A CD1 1 
ATOM   989  C CD2 . LEU A 1 116 ? 20.223 17.699 -0.960  1.00 17.93  ? 115 LEU A CD2 1 
ATOM   990  N N   . THR A 1 117 ? 24.434 20.113 0.810   1.00 12.65  ? 116 THR A N   1 
ATOM   991  C CA  . THR A 1 117 ? 24.648 21.567 0.633   1.00 12.38  ? 116 THR A CA  1 
ATOM   992  C C   . THR A 1 117 ? 24.419 21.890 -0.829  1.00 11.62  ? 116 THR A C   1 
ATOM   993  O O   . THR A 1 117 ? 25.099 21.330 -1.677  1.00 13.21  ? 116 THR A O   1 
ATOM   994  C CB  . THR A 1 117 ? 26.020 22.007 1.127   1.00 13.85  ? 116 THR A CB  1 
ATOM   995  O OG1 . THR A 1 117 ? 26.203 21.613 2.482   1.00 16.44  ? 116 THR A OG1 1 
ATOM   996  C CG2 . THR A 1 117 ? 26.183 23.515 1.027   1.00 15.21  ? 116 THR A CG2 1 
ATOM   997  N N   A LEU A 1 118 ? 23.446 22.753 -1.109  0.40 12.47  ? 117 LEU A N   1 
ATOM   998  N N   B LEU A 1 118 ? 23.489 22.797 -1.097  0.60 11.96  ? 117 LEU A N   1 
ATOM   999  C CA  A LEU A 1 118 ? 23.117 23.196 -2.482  0.40 13.26  ? 117 LEU A CA  1 
ATOM   1000 C CA  B LEU A 1 118 ? 23.110 23.198 -2.466  0.60 12.57  ? 117 LEU A CA  1 
ATOM   1001 C C   A LEU A 1 118 ? 23.585 24.638 -2.616  0.40 12.89  ? 117 LEU A C   1 
ATOM   1002 C C   B LEU A 1 118 ? 23.575 24.644 -2.627  0.60 12.89  ? 117 LEU A C   1 
ATOM   1003 O O   A LEU A 1 118 ? 23.113 25.486 -1.840  0.40 14.43  ? 117 LEU A O   1 
ATOM   1004 O O   B LEU A 1 118 ? 23.102 25.500 -1.868  0.60 14.32  ? 117 LEU A O   1 
ATOM   1005 C CB  A LEU A 1 118 ? 21.615 23.101 -2.761  0.40 14.43  ? 117 LEU A CB  1 
ATOM   1006 C CB  B LEU A 1 118 ? 21.597 23.085 -2.708  0.60 14.44  ? 117 LEU A CB  1 
ATOM   1007 C CG  A LEU A 1 118 ? 21.005 21.708 -2.679  0.40 15.15  ? 117 LEU A CG  1 
ATOM   1008 C CG  B LEU A 1 118 ? 20.843 21.908 -2.084  0.60 13.72  ? 117 LEU A CG  1 
ATOM   1009 C CD1 A LEU A 1 118 ? 22.062 20.687 -3.023  0.40 18.42  ? 117 LEU A CD1 1 
ATOM   1010 C CD1 B LEU A 1 118 ? 19.343 22.064 -2.236  0.60 14.13  ? 117 LEU A CD1 1 
ATOM   1011 C CD2 A LEU A 1 118 ? 20.422 21.477 -1.298  0.40 13.41  ? 117 LEU A CD2 1 
ATOM   1012 C CD2 B LEU A 1 118 ? 21.252 20.633 -2.729  0.60 16.08  ? 117 LEU A CD2 1 
ATOM   1013 N N   . THR A 1 119 ? 24.459 24.879 -3.580  1.00 12.29  ? 118 THR A N   1 
ATOM   1014 C CA  . THR A 1 119 ? 25.059 26.207 -3.804  1.00 13.16  ? 118 THR A CA  1 
ATOM   1015 C C   . THR A 1 119 ? 24.705 26.653 -5.216  1.00 14.38  ? 118 THR A C   1 
ATOM   1016 O O   . THR A 1 119 ? 25.056 25.954 -6.175  1.00 15.13  ? 118 THR A O   1 
ATOM   1017 C CB  . THR A 1 119 ? 26.565 26.192 -3.581  1.00 15.05  ? 118 THR A CB  1 
ATOM   1018 O OG1 . THR A 1 119 ? 26.815 25.720 -2.252  1.00 16.50  ? 118 THR A OG1 1 
ATOM   1019 C CG2 . THR A 1 119 ? 27.153 27.568 -3.763  1.00 17.53  ? 118 THR A CG2 1 
ATOM   1020 N N   . HIS A 1 120 ? 24.151 27.857 -5.319  1.00 14.74  ? 119 HIS A N   1 
ATOM   1021 C CA  . HIS A 1 120 ? 23.908 28.497 -6.619  1.00 15.10  ? 119 HIS A CA  1 
ATOM   1022 C C   . HIS A 1 120 ? 24.236 29.966 -6.433  1.00 17.94  ? 119 HIS A C   1 
ATOM   1023 O O   . HIS A 1 120 ? 23.481 30.659 -5.749  1.00 20.72  ? 119 HIS A O   1 
ATOM   1024 C CB  . HIS A 1 120 ? 22.448 28.298 -7.075  1.00 15.17  ? 119 HIS A CB  1 
ATOM   1025 C CG  . HIS A 1 120 ? 22.192 28.952 -8.379  1.00 17.07  ? 119 HIS A CG  1 
ATOM   1026 N ND1 . HIS A 1 120 ? 21.114 29.761 -8.603  1.00 21.51  ? 119 HIS A ND1 1 
ATOM   1027 C CD2 . HIS A 1 120 ? 22.880 28.909 -9.544  1.00 18.04  ? 119 HIS A CD2 1 
ATOM   1028 C CE1 . HIS A 1 120 ? 21.150 30.193 -9.858  1.00 23.57  ? 119 HIS A CE1 1 
ATOM   1029 N NE2 . HIS A 1 120 ? 22.215 29.691 -10.462 1.00 20.01  ? 119 HIS A NE2 1 
ATOM   1030 N N   . GLY A 1 121 ? 25.421 30.367 -6.880  1.00 20.44  ? 120 GLY A N   1 
ATOM   1031 C CA  . GLY A 1 121 ? 25.951 31.690 -6.563  1.00 26.61  ? 120 GLY A CA  1 
ATOM   1032 C C   . GLY A 1 121 ? 26.039 31.899 -5.068  1.00 25.17  ? 120 GLY A C   1 
ATOM   1033 O O   . GLY A 1 121 ? 26.611 31.038 -4.375  1.00 28.79  ? 120 GLY A O   1 
ATOM   1034 N N   . THR A 1 122 ? 25.445 32.980 -4.569  1.00 29.23  ? 121 THR A N   1 
ATOM   1035 C CA  . THR A 1 122 ? 25.448 33.291 -3.110  1.00 29.22  ? 121 THR A CA  1 
ATOM   1036 C C   . THR A 1 122 ? 24.318 32.563 -2.375  1.00 24.75  ? 121 THR A C   1 
ATOM   1037 O O   . THR A 1 122 ? 24.226 32.705 -1.146  1.00 28.29  ? 121 THR A O   1 
ATOM   1038 C CB  . THR A 1 122 ? 25.340 34.796 -2.872  1.00 34.43  ? 121 THR A CB  1 
ATOM   1039 O OG1 . THR A 1 122 ? 24.097 35.233 -3.427  1.00 39.62  ? 121 THR A OG1 1 
ATOM   1040 C CG2 . THR A 1 122 ? 26.508 35.555 -3.469  1.00 38.55  ? 121 THR A CG2 1 
ATOM   1041 N N   . ALA A 1 123 ? 23.462 31.815 -3.075  1.00 21.21  ? 122 ALA A N   1 
ATOM   1042 C CA  . ALA A 1 123 ? 22.387 31.052 -2.413  1.00 21.74  ? 122 ALA A CA  1 
ATOM   1043 C C   . ALA A 1 123 ? 22.995 29.722 -1.953  1.00 18.03  ? 122 ALA A C   1 
ATOM   1044 O O   . ALA A 1 123 ? 23.441 28.930 -2.783  1.00 20.98  ? 122 ALA A O   1 
ATOM   1045 C CB  . ALA A 1 123 ? 21.206 30.863 -3.309  1.00 22.21  ? 122 ALA A CB  1 
ATOM   1046 N N   . VAL A 1 124 ? 22.992 29.492 -0.647  1.00 17.57  ? 123 VAL A N   1 
ATOM   1047 C CA  . VAL A 1 124 ? 23.490 28.243 -0.033  1.00 15.53  ? 123 VAL A CA  1 
ATOM   1048 C C   . VAL A 1 124 ? 22.395 27.654 0.867   1.00 13.61  ? 123 VAL A C   1 
ATOM   1049 O O   . VAL A 1 124 ? 22.095 28.250 1.923   1.00 18.01  ? 123 VAL A O   1 
ATOM   1050 C CB  . VAL A 1 124 ? 24.805 28.492 0.730   1.00 19.14  ? 123 VAL A CB  1 
ATOM   1051 C CG1 . VAL A 1 124 ? 25.340 27.187 1.307   1.00 19.43  ? 123 VAL A CG1 1 
ATOM   1052 C CG2 . VAL A 1 124 ? 25.852 29.165 -0.135  1.00 20.98  ? 123 VAL A CG2 1 
ATOM   1053 N N   . CYS A 1 125 ? 21.980 26.424 0.594   1.00 14.02  ? 124 CYS A N   1 
ATOM   1054 C CA  . CYS A 1 125 ? 20.922 25.705 1.251   1.00 14.56  ? 124 CYS A CA  1 
ATOM   1055 C C   . CYS A 1 125 ? 21.578 24.507 1.929   1.00 14.99  ? 124 CYS A C   1 
ATOM   1056 O O   . CYS A 1 125 ? 22.407 23.862 1.303   1.00 15.66  ? 124 CYS A O   1 
ATOM   1057 C CB  . CYS A 1 125 ? 19.867 25.347 0.219   1.00 15.18  ? 124 CYS A CB  1 
ATOM   1058 S SG  . CYS A 1 125 ? 18.745 24.052 0.807   1.00 15.49  ? 124 CYS A SG  1 
ATOM   1059 N N   . THR A 1 126 ? 21.137 24.221 3.141   1.00 14.85  ? 125 THR A N   1 
ATOM   1060 C CA  . THR A 1 126 ? 21.529 23.006 3.843   1.00 15.58  ? 125 THR A CA  1 
ATOM   1061 C C   . THR A 1 126 ? 20.275 22.155 4.078   1.00 16.20  ? 125 THR A C   1 
ATOM   1062 O O   . THR A 1 126 ? 19.333 22.629 4.757   1.00 17.62  ? 125 THR A O   1 
ATOM   1063 C CB  . THR A 1 126 ? 22.260 23.343 5.137   1.00 18.15  ? 125 THR A CB  1 
ATOM   1064 O OG1 . THR A 1 126 ? 23.328 24.270 4.884   1.00 19.91  ? 125 THR A OG1 1 
ATOM   1065 C CG2 . THR A 1 126 ? 22.764 22.093 5.800   1.00 21.98  ? 125 THR A CG2 1 
ATOM   1066 N N   . ARG A 1 127 ? 20.303 20.927 3.577   1.00 15.32  ? 126 ARG A N   1 
ATOM   1067 C CA  . ARG A 1 127 ? 19.210 19.930 3.741   1.00 16.82  ? 126 ARG A CA  1 
ATOM   1068 C C   . ARG A 1 127 ? 19.830 18.786 4.559   1.00 17.04  ? 126 ARG A C   1 
ATOM   1069 O O   . ARG A 1 127 ? 20.870 18.234 4.148   1.00 17.61  ? 126 ARG A O   1 
ATOM   1070 C CB  . ARG A 1 127 ? 18.689 19.426 2.395   1.00 18.47  ? 126 ARG A CB  1 
ATOM   1071 C CG  . ARG A 1 127 ? 18.318 20.461 1.343   1.00 23.50  ? 126 ARG A CG  1 
ATOM   1072 C CD  . ARG A 1 127 ? 16.958 20.962 1.521   1.00 20.05  ? 126 ARG A CD  1 
ATOM   1073 N NE  . ARG A 1 127 ? 15.956 20.002 1.049   1.00 16.57  ? 126 ARG A NE  1 
ATOM   1074 C CZ  . ARG A 1 127 ? 14.648 20.163 1.242   1.00 16.37  ? 126 ARG A CZ  1 
ATOM   1075 N NH1 . ARG A 1 127 ? 14.202 21.119 2.045   1.00 19.16  ? 126 ARG A NH1 1 
ATOM   1076 N NH2 . ARG A 1 127 ? 13.804 19.284 0.719   1.00 19.75  ? 126 ARG A NH2 1 
ATOM   1077 N N   . THR A 1 128 ? 19.250 18.465 5.698   1.00 16.95  ? 127 THR A N   1 
ATOM   1078 C CA  . THR A 1 128 ? 19.822 17.457 6.613   1.00 17.00  ? 127 THR A CA  1 
ATOM   1079 C C   . THR A 1 128 ? 18.967 16.204 6.527   1.00 16.83  ? 127 THR A C   1 
ATOM   1080 O O   . THR A 1 128 ? 17.743 16.299 6.679   1.00 18.12  ? 127 THR A O   1 
ATOM   1081 C CB  . THR A 1 128 ? 19.884 17.975 8.049   1.00 19.71  ? 127 THR A CB  1 
ATOM   1082 O OG1 . THR A 1 128 ? 20.672 19.163 8.078   1.00 20.69  ? 127 THR A OG1 1 
ATOM   1083 C CG2 . THR A 1 128 ? 20.509 16.958 8.970   1.00 21.40  ? 127 THR A CG2 1 
ATOM   1084 N N   . TYR A 1 129 ? 19.624 15.066 6.293   1.00 16.60  ? 128 TYR A N   1 
ATOM   1085 C CA  . TYR A 1 129 ? 18.953 13.765 6.114   1.00 17.71  ? 128 TYR A CA  1 
ATOM   1086 C C   . TYR A 1 129 ? 19.441 12.793 7.164   1.00 18.74  ? 128 TYR A C   1 
ATOM   1087 O O   . TYR A 1 129 ? 20.617 12.817 7.562   1.00 20.96  ? 128 TYR A O   1 
ATOM   1088 C CB  . TYR A 1 129 ? 19.250 13.208 4.729   1.00 18.00  ? 128 TYR A CB  1 
ATOM   1089 C CG  . TYR A 1 129 ? 18.490 13.864 3.611   1.00 17.37  ? 128 TYR A CG  1 
ATOM   1090 C CD1 . TYR A 1 129 ? 18.911 15.055 3.041   1.00 18.95  ? 128 TYR A CD1 1 
ATOM   1091 C CD2 . TYR A 1 129 ? 17.331 13.304 3.143   1.00 18.74  ? 128 TYR A CD2 1 
ATOM   1092 C CE1 . TYR A 1 129 ? 18.179 15.638 2.010   1.00 17.73  ? 128 TYR A CE1 1 
ATOM   1093 C CE2 . TYR A 1 129 ? 16.600 13.850 2.129   1.00 19.14  ? 128 TYR A CE2 1 
ATOM   1094 C CZ  . TYR A 1 129 ? 17.000 15.045 1.570   1.00 17.99  ? 128 TYR A CZ  1 
ATOM   1095 O OH  . TYR A 1 129 ? 16.188 15.553 0.577   1.00 20.56  ? 128 TYR A OH  1 
ATOM   1096 N N   A GLU A 1 130 ? 18.531 11.944 7.607   0.90 20.92  ? 129 GLU A N   1 
ATOM   1097 N N   B GLU A 1 130 ? 18.523 11.927 7.595   0.10 18.50  ? 129 GLU A N   1 
ATOM   1098 C CA  A GLU A 1 130 ? 18.853 10.814 8.522   0.90 22.10  ? 129 GLU A CA  1 
ATOM   1099 C CA  B GLU A 1 130 ? 18.746 10.839 8.583   0.10 17.72  ? 129 GLU A CA  1 
ATOM   1100 C C   A GLU A 1 130 ? 18.606 9.489  7.827   0.90 21.35  ? 129 GLU A C   1 
ATOM   1101 C C   B GLU A 1 130 ? 18.573 9.491  7.876   0.10 19.76  ? 129 GLU A C   1 
ATOM   1102 O O   A GLU A 1 130 ? 17.637 9.362  7.073   0.90 22.21  ? 129 GLU A O   1 
ATOM   1103 O O   B GLU A 1 130 ? 17.644 9.383  7.053   0.10 19.84  ? 129 GLU A O   1 
ATOM   1104 C CB  A GLU A 1 130 ? 18.041 10.905 9.810   0.90 30.94  ? 129 GLU A CB  1 
ATOM   1105 C CB  B GLU A 1 130 ? 17.751 10.992 9.734   0.10 16.44  ? 129 GLU A CB  1 
ATOM   1106 C CG  A GLU A 1 130 ? 18.564 11.992 10.714  0.90 39.55  ? 129 GLU A CG  1 
ATOM   1107 C CG  B GLU A 1 130 ? 17.758 9.823  10.696  0.10 15.44  ? 129 GLU A CG  1 
ATOM   1108 C CD  A GLU A 1 130 ? 17.944 12.039 12.089  0.90 44.64  ? 129 GLU A CD  1 
ATOM   1109 C CD  B GLU A 1 130 ? 16.553 9.762  11.618  0.10 16.02  ? 129 GLU A CD  1 
ATOM   1110 O OE1 A GLU A 1 130 ? 17.035 11.208 12.378  0.90 50.15  ? 129 GLU A OE1 1 
ATOM   1111 O OE1 B GLU A 1 130 ? 16.604 8.991  12.579  0.10 17.28  ? 129 GLU A OE1 1 
ATOM   1112 O OE2 A GLU A 1 130 ? 18.394 12.896 12.862  0.90 55.72  ? 129 GLU A OE2 1 
ATOM   1113 O OE2 B GLU A 1 130 ? 15.570 10.490 11.362  0.10 17.79  ? 129 GLU A OE2 1 
ATOM   1114 N N   . LYS A 1 131 ? 19.420 8.504  8.192   1.00 21.02  ? 130 LYS A N   1 
ATOM   1115 C CA  . LYS A 1 131 ? 19.358 7.175  7.562   1.00 22.40  ? 130 LYS A CA  1 
ATOM   1116 C C   . LYS A 1 131 ? 18.138 6.462  8.140   1.00 23.61  ? 130 LYS A C   1 
ATOM   1117 O O   . LYS A 1 131 ? 17.920 6.513  9.388   1.00 29.04  ? 130 LYS A O   1 
ATOM   1118 C CB  . LYS A 1 131 ? 20.665 6.407  7.745   1.00 24.74  ? 130 LYS A CB  1 
ATOM   1119 C CG  . LYS A 1 131 ? 20.921 5.449  6.575   1.00 27.49  ? 130 LYS A CG  1 
ATOM   1120 C CD  . LYS A 1 131 ? 22.298 4.894  6.563   1.00 26.71  ? 130 LYS A CD  1 
ATOM   1121 C CE  . LYS A 1 131 ? 22.683 4.347  5.220   1.00 29.90  ? 130 LYS A CE  1 
ATOM   1122 N NZ  . LYS A 1 131 ? 24.017 3.723  5.313   1.00 40.21  ? 130 LYS A NZ  1 
ATOM   1123 N N   . GLU A 1 132 ? 17.358 5.845  7.251   1.00 25.14  ? 131 GLU A N   1 
ATOM   1124 C CA  . GLU A 1 132 ? 16.289 4.890  7.629   1.00 28.24  ? 131 GLU A CA  1 
ATOM   1125 C C   . GLU A 1 132 ? 16.913 3.515  7.923   1.00 33.08  ? 131 GLU A C   1 
ATOM   1126 O O   . GLU A 1 132 ? 17.853 3.097  7.193   1.00 39.95  ? 131 GLU A O   1 
ATOM   1127 C CB  . GLU A 1 132 ? 15.246 4.780  6.528   1.00 28.74  ? 131 GLU A CB  1 
ATOM   1128 C CG  . GLU A 1 132 ? 14.504 6.046  6.306   1.00 33.54  ? 131 GLU A CG  1 
ATOM   1129 C CD  . GLU A 1 132 ? 13.246 5.887  5.481   1.00 39.19  ? 131 GLU A CD  1 
ATOM   1130 O OE1 . GLU A 1 132 ? 12.692 6.919  5.144   1.00 46.03  ? 131 GLU A OE1 1 
ATOM   1131 O OE2 . GLU A 1 132 ? 12.816 4.726  5.220   1.00 49.11  ? 131 GLU A OE2 1 
ATOM   1132 N N   . ALA A 1 133 ? 16.389 2.872  8.961   1.00 38.43  ? 132 ALA A N   1 
ATOM   1133 C CA  . ALA A 1 133 ? 16.747 1.531  9.480   1.00 48.50  ? 132 ALA A CA  1 
ATOM   1134 C C   . ALA A 1 133 ? 16.005 0.467  8.672   1.00 53.72  ? 132 ALA A C   1 
ATOM   1135 O O   . ALA A 1 133 ? 15.020 0.791  8.019   1.00 58.13  ? 132 ALA A O   1 
ATOM   1136 C CB  . ALA A 1 133 ? 16.392 1.434  10.947  1.00 57.89  ? 132 ALA A CB  1 
ATOM   1137 O OXT . ALA A 1 133 ? 16.354 -0.698 8.674   1.00 46.74  ? 132 ALA A OXT 1 
HETATM 1138 C C1  . IZP B 2 .   ? 15.711 17.757 -1.653  1.00 33.50  ? 200 IZP A C1  1 
HETATM 1139 O O1  . IZP B 2 .   ? 14.507 18.156 -1.579  0.80 35.55  ? 200 IZP A O1  1 
HETATM 1140 C C2  . IZP B 2 .   ? 16.076 21.142 -7.183  1.00 25.35  ? 200 IZP A C2  1 
HETATM 1141 O O2  . IZP B 2 .   ? 16.590 17.837 -0.719  1.00 18.41  ? 200 IZP A O2  1 
HETATM 1142 C C3  . IZP B 2 .   ? 15.073 22.221 -6.834  1.00 26.10  ? 200 IZP A C3  1 
HETATM 1143 C C4  . IZP B 2 .   ? 13.570 21.825 -7.029  1.00 27.29  ? 200 IZP A C4  1 
HETATM 1144 C C5  . IZP B 2 .   ? 15.375 23.492 -7.598  0.80 28.20  ? 200 IZP A C5  1 
HETATM 1145 C C6  . IZP B 2 .   ? 16.072 17.098 -2.940  0.80 27.30  ? 200 IZP A C6  1 
HETATM 1146 C C7  . IZP B 2 .   ? 17.290 16.490 -2.610  1.00 20.93  ? 200 IZP A C7  1 
HETATM 1147 C C8  . IZP B 2 .   ? 16.136 18.106 -4.029  0.80 24.99  ? 200 IZP A C8  1 
HETATM 1148 C C9  . IZP B 2 .   ? 15.272 18.003 -5.112  0.60 27.03  ? 200 IZP A C9  1 
HETATM 1149 C C10 . IZP B 2 .   ? 15.263 18.967 -6.138  0.80 27.87  ? 200 IZP A C10 1 
HETATM 1150 C C11 . IZP B 2 .   ? 16.096 20.083 -6.076  1.00 25.20  ? 200 IZP A C11 1 
HETATM 1151 C C12 . IZP B 2 .   ? 16.980 20.130 -4.991  0.80 26.76  ? 200 IZP A C12 1 
HETATM 1152 C C13 . IZP B 2 .   ? 16.985 19.177 -3.946  1.00 32.43  ? 200 IZP A C13 1 
HETATM 1153 O O1  . PG4 C 3 .   ? 6.447  17.622 7.894   1.00 62.88  ? 201 PG4 A O1  1 
HETATM 1154 C C1  . PG4 C 3 .   ? 6.202  19.005 8.107   1.00 66.88  ? 201 PG4 A C1  1 
HETATM 1155 C C2  . PG4 C 3 .   ? 6.636  19.840 6.945   1.00 54.43  ? 201 PG4 A C2  1 
HETATM 1156 O O2  . PG4 C 3 .   ? 7.874  19.368 6.409   1.00 42.83  ? 201 PG4 A O2  1 
HETATM 1157 C C3  . PG4 C 3 .   ? 8.309  20.182 5.337   1.00 41.85  ? 201 PG4 A C3  1 
HETATM 1158 C C4  . PG4 C 3 .   ? 9.768  20.089 5.141   1.00 36.37  ? 201 PG4 A C4  1 
HETATM 1159 O O3  . PG4 C 3 .   ? 10.470 19.812 6.348   1.00 35.81  ? 201 PG4 A O3  1 
HETATM 1160 C C5  . PG4 C 3 .   ? 11.399 20.837 6.628   1.00 33.17  ? 201 PG4 A C5  1 
HETATM 1161 C C6  . PG4 C 3 .   ? 12.227 20.422 7.788   1.00 38.00  ? 201 PG4 A C6  1 
HETATM 1162 O O4  . PG4 C 3 .   ? 11.401 20.390 8.946   1.00 38.95  ? 201 PG4 A O4  1 
HETATM 1163 C C7  . PG4 C 3 .   ? 12.137 20.335 10.157  1.00 36.35  ? 201 PG4 A C7  1 
HETATM 1164 C C8  . PG4 C 3 .   ? 11.185 20.326 11.289  1.00 40.66  ? 201 PG4 A C8  1 
HETATM 1165 O O5  . PG4 C 3 .   ? 10.161 19.409 11.065  1.00 46.92  ? 201 PG4 A O5  1 
HETATM 1166 C C1  . PEG D 4 .   ? 28.895 16.526 -23.511 0.80 31.52  ? 202 PEG A C1  1 
HETATM 1167 O O1  . PEG D 4 .   ? 27.968 17.061 -24.486 1.00 35.14  ? 202 PEG A O1  1 
HETATM 1168 C C2  . PEG D 4 .   ? 28.482 15.162 -22.955 1.00 34.47  ? 202 PEG A C2  1 
HETATM 1169 O O2  . PEG D 4 .   ? 27.148 15.227 -22.461 0.80 23.94  ? 202 PEG A O2  1 
HETATM 1170 C C3  . PEG D 4 .   ? 26.730 14.126 -21.652 1.00 32.64  ? 202 PEG A C3  1 
HETATM 1171 C C4  . PEG D 4 .   ? 26.351 12.987 -22.526 1.00 31.90  ? 202 PEG A C4  1 
HETATM 1172 O O4  . PEG D 4 .   ? 27.524 12.287 -23.011 1.00 35.40  ? 202 PEG A O4  1 
HETATM 1173 C C   . ACY E 5 .   ? 20.558 15.408 -6.655  1.00 18.57  ? 203 ACY A C   1 
HETATM 1174 O O   . ACY E 5 .   ? 19.813 15.266 -5.698  1.00 19.59  ? 203 ACY A O   1 
HETATM 1175 O OXT . ACY E 5 .   ? 21.810 15.299 -6.578  1.00 15.59  ? 203 ACY A OXT 1 
HETATM 1176 C CH3 . ACY E 5 .   ? 19.912 15.833 -7.960  1.00 23.29  ? 203 ACY A CH3 1 
HETATM 1177 C C1  . PGE F 6 .   ? 31.819 22.365 -2.884  1.00 42.01  ? 204 PGE A C1  1 
HETATM 1178 O O1  . PGE F 6 .   ? 32.830 21.367 -3.158  1.00 58.38  ? 204 PGE A O1  1 
HETATM 1179 C C2  . PGE F 6 .   ? 31.439 22.372 -1.436  1.00 49.50  ? 204 PGE A C2  1 
HETATM 1180 O O2  . PGE F 6 .   ? 30.163 22.973 -1.200  1.00 48.31  ? 204 PGE A O2  1 
HETATM 1181 C C3  . PGE F 6 .   ? 29.575 22.525 0.017   1.00 41.00  ? 204 PGE A C3  1 
HETATM 1182 C C4  . PGE F 6 .   ? 30.635 21.939 0.967   1.00 39.37  ? 204 PGE A C4  1 
HETATM 1183 O O4  . PGE F 6 .   ? 30.442 22.930 5.243   1.00 63.29  ? 204 PGE A O4  1 
HETATM 1184 C C6  . PGE F 6 .   ? 30.755 22.675 3.891   1.00 44.32  ? 204 PGE A C6  1 
HETATM 1185 C C5  . PGE F 6 .   ? 29.572 22.219 3.099   1.00 46.50  ? 204 PGE A C5  1 
HETATM 1186 O O3  . PGE F 6 .   ? 29.991 21.313 2.072   1.00 44.77  ? 204 PGE A O3  1 
HETATM 1187 C C1  . GOL G 7 .   ? 24.833 5.904  -16.864 1.00 40.26  ? 205 GOL A C1  1 
HETATM 1188 O O1  . GOL G 7 .   ? 26.185 6.349  -16.918 1.00 47.72  ? 205 GOL A O1  1 
HETATM 1189 C C2  . GOL G 7 .   ? 24.774 4.411  -17.001 1.00 49.34  ? 205 GOL A C2  1 
HETATM 1190 O O2  . GOL G 7 .   ? 23.473 4.051  -17.475 1.00 66.64  ? 205 GOL A O2  1 
HETATM 1191 C C3  . GOL G 7 .   ? 25.876 3.894  -17.910 1.00 52.66  ? 205 GOL A C3  1 
HETATM 1192 O O3  . GOL G 7 .   ? 25.516 2.708  -18.623 1.00 63.32  ? 205 GOL A O3  1 
HETATM 1193 O O   . HOH H 8 .   ? 12.666 20.541 -19.767 0.30 27.16  ? 301 HOH A O   1 
HETATM 1194 O O   . HOH H 8 .   ? 32.307 1.181  -16.700 1.00 51.28  ? 302 HOH A O   1 
HETATM 1195 O O   . HOH H 8 .   ? 28.044 6.234  -18.414 1.00 46.18  ? 303 HOH A O   1 
HETATM 1196 O O   A HOH H 8 .   ? 10.971 16.922 -14.331 0.50 42.64  ? 304 HOH A O   1 
HETATM 1197 O O   B HOH H 8 .   ? 12.283 15.764 -14.180 0.50 29.08  ? 304 HOH A O   1 
HETATM 1198 O O   . HOH H 8 .   ? 10.798 7.303  3.700   1.00 42.03  ? 305 HOH A O   1 
HETATM 1199 O O   . HOH H 8 .   ? 29.408 19.411 -21.649 1.00 47.22  ? 306 HOH A O   1 
HETATM 1200 O O   . HOH H 8 .   ? 13.327 36.481 -1.629  1.00 53.47  ? 307 HOH A O   1 
HETATM 1201 O O   . HOH H 8 .   ? 12.426 5.977  -9.768  1.00 50.26  ? 308 HOH A O   1 
HETATM 1202 O O   . HOH H 8 .   ? 18.429 14.443 -1.603  1.00 25.98  ? 309 HOH A O   1 
HETATM 1203 O O   . HOH H 8 .   ? 17.937 1.673  0.648   1.00 38.40  ? 310 HOH A O   1 
HETATM 1204 O O   . HOH H 8 .   ? 22.333 20.261 9.711   1.00 42.55  ? 311 HOH A O   1 
HETATM 1205 O O   . HOH H 8 .   ? 21.524 5.663  -17.972 1.00 70.83  ? 312 HOH A O   1 
HETATM 1206 O O   . HOH H 8 .   ? 14.126 2.452  0.450   1.00 50.46  ? 313 HOH A O   1 
HETATM 1207 O O   . HOH H 8 .   ? 20.545 34.234 -1.624  1.00 58.45  ? 314 HOH A O   1 
HETATM 1208 O O   A HOH H 8 .   ? 18.046 5.682  -13.680 0.70 36.91  ? 315 HOH A O   1 
HETATM 1209 O O   B HOH H 8 .   ? 17.617 6.311  -15.379 0.30 43.53  ? 315 HOH A O   1 
HETATM 1210 O O   . HOH H 8 .   ? 31.399 12.171 3.993   1.00 24.48  ? 316 HOH A O   1 
HETATM 1211 O O   . HOH H 8 .   ? 8.545  9.138  4.411   1.00 54.83  ? 317 HOH A O   1 
HETATM 1212 O O   . HOH H 8 .   ? 17.293 14.437 -6.213  1.00 32.18  ? 318 HOH A O   1 
HETATM 1213 O O   . HOH H 8 .   ? 15.661 24.121 11.645  1.00 38.85  ? 319 HOH A O   1 
HETATM 1214 O O   . HOH H 8 .   ? 23.609 14.886 -25.034 1.00 51.34  ? 320 HOH A O   1 
HETATM 1215 O O   . HOH H 8 .   ? 10.975 19.881 1.266   1.00 20.88  ? 321 HOH A O   1 
HETATM 1216 O O   . HOH H 8 .   ? 28.283 17.957 -26.923 1.00 51.23  ? 322 HOH A O   1 
HETATM 1217 O O   . HOH H 8 .   ? 28.798 26.552 -0.763  1.00 26.43  ? 323 HOH A O   1 
HETATM 1218 O O   . HOH H 8 .   ? 25.961 5.586  6.362   1.00 29.68  ? 324 HOH A O   1 
HETATM 1219 O O   . HOH H 8 .   ? 32.171 24.145 -9.468  1.00 46.30  ? 325 HOH A O   1 
HETATM 1220 O O   . HOH H 8 .   ? 28.948 19.082 4.681   1.00 38.28  ? 326 HOH A O   1 
HETATM 1221 O O   . HOH H 8 .   ? 32.678 24.017 -12.353 1.00 51.08  ? 327 HOH A O   1 
HETATM 1222 O O   . HOH H 8 .   ? 34.561 17.622 -7.944  1.00 33.50  ? 328 HOH A O   1 
HETATM 1223 O O   . HOH H 8 .   ? 19.706 29.904 -0.507  1.00 33.15  ? 329 HOH A O   1 
HETATM 1224 O O   . HOH H 8 .   ? 13.881 16.137 -20.513 1.00 41.92  ? 330 HOH A O   1 
HETATM 1225 O O   . HOH H 8 .   ? 19.608 20.062 11.940  1.00 38.19  ? 331 HOH A O   1 
HETATM 1226 O O   . HOH H 8 .   ? 36.844 15.078 2.805   1.00 48.59  ? 332 HOH A O   1 
HETATM 1227 O O   . HOH H 8 .   ? 21.512 9.155  10.096  1.00 27.70  ? 333 HOH A O   1 
HETATM 1228 O O   . HOH H 8 .   ? 32.611 20.142 5.427   1.00 48.58  ? 334 HOH A O   1 
HETATM 1229 O O   . HOH H 8 .   ? 17.432 15.001 -10.841 1.00 19.54  ? 335 HOH A O   1 
HETATM 1230 O O   . HOH H 8 .   ? 9.400  10.909 1.757   1.00 43.81  ? 336 HOH A O   1 
HETATM 1231 O O   . HOH H 8 .   ? 21.515 22.246 -20.885 1.00 19.59  ? 337 HOH A O   1 
HETATM 1232 O O   . HOH H 8 .   ? 22.419 8.480  -17.210 1.00 43.09  ? 338 HOH A O   1 
HETATM 1233 O O   A HOH H 8 .   ? 13.401 26.188 -12.662 0.50 18.35  ? 339 HOH A O   1 
HETATM 1234 O O   B HOH H 8 .   ? 14.037 26.722 -12.544 0.50 20.90  ? 339 HOH A O   1 
HETATM 1235 O O   . HOH H 8 .   ? 29.925 25.022 -5.443  1.00 42.80  ? 340 HOH A O   1 
HETATM 1236 O O   . HOH H 8 .   ? 31.353 4.803  -10.940 1.00 18.16  ? 341 HOH A O   1 
HETATM 1237 O O   . HOH H 8 .   ? 14.511 34.245 -0.620  1.00 34.50  ? 342 HOH A O   1 
HETATM 1238 O O   . HOH H 8 .   ? 8.080  27.456 2.897   1.00 29.28  ? 343 HOH A O   1 
HETATM 1239 O O   . HOH H 8 .   ? 27.271 19.134 2.506   1.00 16.09  ? 344 HOH A O   1 
HETATM 1240 O O   A HOH H 8 .   ? 14.976 15.526 -7.495  0.50 18.96  ? 345 HOH A O   1 
HETATM 1241 O O   B HOH H 8 .   ? 15.641 16.034 -7.100  0.50 25.81  ? 345 HOH A O   1 
HETATM 1242 O O   . HOH H 8 .   ? 16.052 13.794 -12.955 1.00 19.87  ? 346 HOH A O   1 
HETATM 1243 O O   . HOH H 8 .   ? 21.599 10.608 -18.785 1.00 35.33  ? 347 HOH A O   1 
HETATM 1244 O O   . HOH H 8 .   ? 6.626  12.362 -9.773  1.00 54.49  ? 348 HOH A O   1 
HETATM 1245 O O   A HOH H 8 .   ? 22.994 31.984 -20.752 0.50 19.73  ? 349 HOH A O   1 
HETATM 1246 O O   B HOH H 8 .   ? 22.907 31.604 -21.531 0.50 21.63  ? 349 HOH A O   1 
HETATM 1247 O O   . HOH H 8 .   ? 7.443  12.862 7.022   1.00 68.03  ? 350 HOH A O   1 
HETATM 1248 O O   . HOH H 8 .   ? 28.268 31.081 -2.220  1.00 44.08  ? 351 HOH A O   1 
HETATM 1249 O O   . HOH H 8 .   ? 25.876 23.390 4.514   1.00 22.56  ? 352 HOH A O   1 
HETATM 1250 O O   A HOH H 8 .   ? 22.779 1.624  -9.512  0.50 19.77  ? 353 HOH A O   1 
HETATM 1251 O O   B HOH H 8 .   ? 22.498 1.594  -10.234 0.50 22.93  ? 353 HOH A O   1 
HETATM 1252 O O   . HOH H 8 .   ? 36.793 17.694 0.106   1.00 38.48  ? 354 HOH A O   1 
HETATM 1253 O O   . HOH H 8 .   ? 13.431 2.132  -5.078  1.00 58.47  ? 355 HOH A O   1 
HETATM 1254 O O   . HOH H 8 .   ? 18.229 36.078 -0.360  1.00 48.12  ? 356 HOH A O   1 
HETATM 1255 O O   . HOH H 8 .   ? 7.244  9.468  -3.664  1.00 47.67  ? 357 HOH A O   1 
HETATM 1256 O O   . HOH H 8 .   ? 10.430 31.035 2.781   1.00 20.21  ? 358 HOH A O   1 
HETATM 1257 O O   . HOH H 8 .   ? 10.576 6.196  -0.790  1.00 54.15  ? 359 HOH A O   1 
HETATM 1258 O O   A HOH H 8 .   ? 17.121 11.937 -8.423  0.50 22.12  ? 360 HOH A O   1 
HETATM 1259 O O   B HOH H 8 .   ? 17.874 13.651 -8.696  0.50 33.10  ? 360 HOH A O   1 
HETATM 1260 O O   . HOH H 8 .   ? 33.404 5.691  -12.751 1.00 17.88  ? 361 HOH A O   1 
HETATM 1261 O O   . HOH H 8 .   ? 11.344 17.891 -19.649 1.00 67.91  ? 362 HOH A O   1 
HETATM 1262 O O   . HOH H 8 .   ? 22.583 11.255 -22.917 1.00 36.02  ? 363 HOH A O   1 
HETATM 1263 O O   . HOH H 8 .   ? 13.192 33.697 -9.368  1.00 52.45  ? 364 HOH A O   1 
HETATM 1264 O O   . HOH H 8 .   ? 27.194 23.005 -2.606  1.00 15.52  ? 365 HOH A O   1 
HETATM 1265 O O   . HOH H 8 .   ? 19.812 11.995 -15.652 1.00 20.51  ? 366 HOH A O   1 
HETATM 1266 O O   . HOH H 8 .   ? 11.584 13.053 8.672   1.00 41.08  ? 367 HOH A O   1 
HETATM 1267 O O   . HOH H 8 .   ? 28.910 11.466 -13.177 1.00 11.23  ? 368 HOH A O   1 
HETATM 1268 O O   . HOH H 8 .   ? 26.544 9.905  -20.225 1.00 26.74  ? 369 HOH A O   1 
HETATM 1269 O O   . HOH H 8 .   ? 37.626 10.151 -1.841  1.00 28.67  ? 370 HOH A O   1 
HETATM 1270 O O   A HOH H 8 .   ? 21.687 1.133  -1.426  0.30 16.24  ? 371 HOH A O   1 
HETATM 1271 O O   B HOH H 8 .   ? 22.085 0.001  -1.154  0.50 21.75  ? 371 HOH A O   1 
HETATM 1272 O O   . HOH H 8 .   ? 19.259 21.458 7.329   1.00 19.03  ? 372 HOH A O   1 
HETATM 1273 O O   . HOH H 8 .   ? 12.679 16.659 11.843  1.00 45.63  ? 373 HOH A O   1 
HETATM 1274 O O   . HOH H 8 .   ? 5.342  28.076 -9.715  1.00 47.55  ? 374 HOH A O   1 
HETATM 1275 O O   . HOH H 8 .   ? 29.333 10.051 9.861   1.00 38.43  ? 375 HOH A O   1 
HETATM 1276 O O   . HOH H 8 .   ? 29.933 11.937 -21.121 1.00 18.93  ? 376 HOH A O   1 
HETATM 1277 O O   . HOH H 8 .   ? 27.984 26.447 -17.212 1.00 29.02  ? 377 HOH A O   1 
HETATM 1278 O O   . HOH H 8 .   ? 25.710 14.889 -4.208  1.00 12.76  ? 378 HOH A O   1 
HETATM 1279 O O   . HOH H 8 .   ? 31.261 16.924 -9.668  1.00 17.38  ? 379 HOH A O   1 
HETATM 1280 O O   . HOH H 8 .   ? 22.576 26.948 4.444   1.00 22.20  ? 380 HOH A O   1 
HETATM 1281 O O   . HOH H 8 .   ? 13.902 2.184  4.674   1.00 56.24  ? 381 HOH A O   1 
HETATM 1282 O O   . HOH H 8 .   ? 19.619 21.692 -8.409  1.00 15.50  ? 382 HOH A O   1 
HETATM 1283 O O   . HOH H 8 .   ? 19.334 23.383 9.338   1.00 30.26  ? 383 HOH A O   1 
HETATM 1284 O O   . HOH H 8 .   ? 1.366  26.379 -4.124  1.00 46.79  ? 384 HOH A O   1 
HETATM 1285 O O   . HOH H 8 .   ? 9.896  33.369 -1.404  1.00 33.59  ? 385 HOH A O   1 
HETATM 1286 O O   . HOH H 8 .   ? 28.639 19.102 -15.339 1.00 43.49  ? 386 HOH A O   1 
HETATM 1287 O O   . HOH H 8 .   ? 27.853 -3.848 -7.252  1.00 33.84  ? 387 HOH A O   1 
HETATM 1288 O O   . HOH H 8 .   ? 24.061 17.909 -25.833 1.00 31.93  ? 388 HOH A O   1 
HETATM 1289 O O   . HOH H 8 .   ? 8.534  27.405 -11.629 1.00 43.14  ? 389 HOH A O   1 
HETATM 1290 O O   . HOH H 8 .   ? 7.912  28.094 -0.563  1.00 27.34  ? 390 HOH A O   1 
HETATM 1291 O O   . HOH H 8 .   ? 18.937 2.615  4.587   1.00 26.12  ? 391 HOH A O   1 
HETATM 1292 O O   . HOH H 8 .   ? 25.603 1.906  3.581   1.00 27.25  ? 392 HOH A O   1 
HETATM 1293 O O   . HOH H 8 .   ? 27.588 8.881  -15.995 1.00 13.27  ? 393 HOH A O   1 
HETATM 1294 O O   A HOH H 8 .   ? 20.311 17.633 -20.393 0.50 20.42  ? 394 HOH A O   1 
HETATM 1295 O O   B HOH H 8 .   ? 21.066 17.685 -20.747 0.50 20.77  ? 394 HOH A O   1 
HETATM 1296 O O   . HOH H 8 .   ? 19.903 24.324 -21.732 1.00 18.17  ? 395 HOH A O   1 
HETATM 1297 O O   . HOH H 8 .   ? 26.997 28.470 -8.391  1.00 28.34  ? 396 HOH A O   1 
HETATM 1298 O O   . HOH H 8 .   ? 9.273  34.557 -6.682  1.00 70.40  ? 397 HOH A O   1 
HETATM 1299 O O   A HOH H 8 .   ? 20.000 1.696  -1.405  0.50 23.02  ? 398 HOH A O   1 
HETATM 1300 O O   B HOH H 8 .   ? 19.019 0.518  -1.230  0.50 32.48  ? 398 HOH A O   1 
HETATM 1301 O O   . HOH H 8 .   ? 25.026 6.898  8.536   1.00 33.40  ? 399 HOH A O   1 
HETATM 1302 O O   . HOH H 8 .   ? 22.177 32.917 -7.041  1.00 50.56  ? 400 HOH A O   1 
HETATM 1303 O O   . HOH H 8 .   ? 18.245 16.196 -20.190 1.00 27.61  ? 401 HOH A O   1 
HETATM 1304 O O   . HOH H 8 .   ? 18.305 19.134 -9.289  1.00 17.04  ? 402 HOH A O   1 
HETATM 1305 O O   . HOH H 8 .   ? 23.696 11.073 -20.555 1.00 22.79  ? 403 HOH A O   1 
HETATM 1306 O O   . HOH H 8 .   ? 8.963  30.405 -1.265  1.00 27.31  ? 404 HOH A O   1 
HETATM 1307 O O   . HOH H 8 .   ? 9.485  31.824 -11.972 1.00 68.10  ? 405 HOH A O   1 
HETATM 1308 O O   . HOH H 8 .   ? 6.985  33.478 -8.319  1.00 54.17  ? 406 HOH A O   1 
HETATM 1309 O O   . HOH H 8 .   ? 20.205 13.727 0.016   1.00 22.13  ? 407 HOH A O   1 
HETATM 1310 O O   . HOH H 8 .   ? 16.265 17.127 -9.510  1.00 16.87  ? 408 HOH A O   1 
HETATM 1311 O O   . HOH H 8 .   ? 14.139 11.797 -13.111 1.00 24.70  ? 409 HOH A O   1 
HETATM 1312 O O   . HOH H 8 .   ? 12.029 7.971  -8.093  1.00 38.09  ? 410 HOH A O   1 
HETATM 1313 O O   . HOH H 8 .   ? 16.105 29.504 5.969   1.00 16.20  ? 411 HOH A O   1 
HETATM 1314 O O   . HOH H 8 .   ? 30.077 -2.251 -13.555 1.00 65.87  ? 412 HOH A O   1 
HETATM 1315 O O   A HOH H 8 .   ? 19.831 9.052  -15.512 0.50 17.94  ? 413 HOH A O   1 
HETATM 1316 O O   B HOH H 8 .   ? 20.379 9.463  -15.502 0.50 24.52  ? 413 HOH A O   1 
HETATM 1317 O O   . HOH H 8 .   ? 28.946 -0.434 -16.532 1.00 60.10  ? 414 HOH A O   1 
HETATM 1318 O O   . HOH H 8 .   ? 26.710 29.866 -11.791 1.00 28.62  ? 415 HOH A O   1 
HETATM 1319 O O   . HOH H 8 .   ? 23.129 -0.514 -3.530  1.00 19.68  ? 416 HOH A O   1 
HETATM 1320 O O   . HOH H 8 .   ? 31.559 12.703 11.322  1.00 44.41  ? 417 HOH A O   1 
HETATM 1321 O O   . HOH H 8 .   ? 21.380 31.241 1.147   1.00 31.34  ? 418 HOH A O   1 
HETATM 1322 O O   . HOH H 8 .   ? 17.266 13.139 -15.530 1.00 17.00  ? 419 HOH A O   1 
HETATM 1323 O O   . HOH H 8 .   ? 3.938  30.889 -8.909  1.00 55.23  ? 420 HOH A O   1 
HETATM 1324 O O   A HOH H 8 .   ? 29.177 11.025 -25.167 0.50 45.52  ? 421 HOH A O   1 
HETATM 1325 O O   B HOH H 8 .   ? 30.694 11.416 -26.555 0.50 44.35  ? 421 HOH A O   1 
HETATM 1326 O O   A HOH H 8 .   ? 17.207 33.898 -4.116  0.50 31.23  ? 422 HOH A O   1 
HETATM 1327 O O   B HOH H 8 .   ? 19.035 33.916 -3.490  0.50 42.44  ? 422 HOH A O   1 
HETATM 1328 O O   . HOH H 8 .   ? 35.966 21.313 -0.760  1.00 66.73  ? 423 HOH A O   1 
HETATM 1329 O O   . HOH H 8 .   ? 25.384 16.305 11.432  1.00 44.24  ? 424 HOH A O   1 
HETATM 1330 O O   . HOH H 8 .   ? 32.766 0.977  -8.879  1.00 38.05  ? 425 HOH A O   1 
HETATM 1331 O O   . HOH H 8 .   ? 26.168 -2.397 -13.744 1.00 53.48  ? 426 HOH A O   1 
HETATM 1332 O O   A HOH H 8 .   ? 23.914 34.801 -6.564  0.50 33.98  ? 427 HOH A O   1 
HETATM 1333 O O   B HOH H 8 .   ? 25.310 34.820 -6.653  0.50 37.11  ? 427 HOH A O   1 
HETATM 1334 O O   . HOH H 8 .   ? 28.209 26.120 -7.764  1.00 34.67  ? 428 HOH A O   1 
HETATM 1335 O O   . HOH H 8 .   ? 9.118  24.253 -15.232 1.00 51.46  ? 429 HOH A O   1 
HETATM 1336 O O   . HOH H 8 .   ? 17.458 8.144  -15.379 0.70 38.81  ? 430 HOH A O   1 
HETATM 1337 O O   . HOH H 8 .   ? 12.585 30.556 -14.669 1.00 35.01  ? 431 HOH A O   1 
HETATM 1338 O O   . HOH H 8 .   ? 15.393 0.996  -2.197  1.00 63.72  ? 432 HOH A O   1 
HETATM 1339 O O   . HOH H 8 .   ? 36.935 19.348 -1.350  1.00 48.70  ? 433 HOH A O   1 
HETATM 1340 O O   . HOH H 8 .   ? 12.328 32.417 -1.519  1.00 30.95  ? 434 HOH A O   1 
HETATM 1341 O O   . HOH H 8 .   ? 18.844 1.456  -11.336 1.00 64.04  ? 435 HOH A O   1 
HETATM 1342 O O   . HOH H 8 .   ? 18.984 17.265 12.335  1.00 54.88  ? 436 HOH A O   1 
HETATM 1343 O O   . HOH H 8 .   ? 21.568 1.590  5.380   1.00 28.48  ? 437 HOH A O   1 
HETATM 1344 O O   A HOH H 8 .   ? 11.270 17.516 -4.664  0.50 32.84  ? 438 HOH A O   1 
HETATM 1345 O O   B HOH H 8 .   ? 12.622 17.324 -3.450  0.50 34.79  ? 438 HOH A O   1 
HETATM 1346 O O   . HOH H 8 .   ? 12.427 15.866 -6.453  1.00 41.27  ? 439 HOH A O   1 
HETATM 1347 O O   . HOH H 8 .   ? 11.721 13.171 -13.188 1.00 55.79  ? 440 HOH A O   1 
HETATM 1348 O O   . HOH H 8 .   ? 28.666 20.655 6.845   1.00 52.84  ? 441 HOH A O   1 
HETATM 1349 O O   . HOH H 8 .   ? 32.118 8.922  2.949   1.00 47.44  ? 442 HOH A O   1 
HETATM 1350 O O   A HOH H 8 .   ? 35.034 21.181 4.118   0.50 44.73  ? 443 HOH A O   1 
HETATM 1351 O O   B HOH H 8 .   ? 33.816 22.342 2.989   0.50 55.01  ? 443 HOH A O   1 
HETATM 1352 O O   . HOH H 8 .   ? 33.863 4.087  -14.896 1.00 31.85  ? 444 HOH A O   1 
HETATM 1353 O O   . HOH H 8 .   ? 9.185  23.707 -12.321 1.00 47.01  ? 445 HOH A O   1 
HETATM 1354 O O   . HOH H 8 .   ? 30.674 25.854 -2.858  1.00 50.05  ? 446 HOH A O   1 
HETATM 1355 O O   . HOH H 8 .   ? 7.068  13.483 0.373   1.00 60.23  ? 447 HOH A O   1 
HETATM 1356 O O   . HOH H 8 .   ? 6.127  27.801 1.588   1.00 38.65  ? 448 HOH A O   1 
HETATM 1357 O O   . HOH H 8 .   ? 17.201 25.479 10.139  1.00 33.19  ? 449 HOH A O   1 
HETATM 1358 O O   . HOH H 8 .   ? 26.549 22.849 -19.838 1.00 24.50  ? 450 HOH A O   1 
HETATM 1359 O O   . HOH H 8 .   ? 32.336 7.977  5.256   1.00 60.05  ? 451 HOH A O   1 
HETATM 1360 O O   . HOH H 8 .   ? 10.392 25.586 -12.050 1.00 34.99  ? 452 HOH A O   1 
HETATM 1361 O O   . HOH H 8 .   ? 23.525 31.154 3.424   1.00 47.32  ? 453 HOH A O   1 
HETATM 1362 O O   . HOH H 8 .   ? 33.811 8.490  1.560   1.00 50.38  ? 454 HOH A O   1 
HETATM 1363 O O   . HOH H 8 .   ? 21.543 -0.403 -8.155  1.00 32.93  ? 455 HOH A O   1 
HETATM 1364 O O   . HOH H 8 .   ? 27.874 -1.709 -5.002  1.00 52.74  ? 456 HOH A O   1 
HETATM 1365 O O   . HOH H 8 .   ? 17.903 12.561 -19.565 1.00 69.14  ? 457 HOH A O   1 
HETATM 1366 O O   . HOH H 8 .   ? 23.602 -1.551 -13.417 1.00 55.41  ? 458 HOH A O   1 
HETATM 1367 O O   . HOH H 8 .   ? 25.984 14.408 -26.083 1.00 61.47  ? 459 HOH A O   1 
HETATM 1368 O O   . HOH H 8 .   ? 17.228 34.999 -6.216  1.00 56.91  ? 460 HOH A O   1 
HETATM 1369 O O   . HOH H 8 .   ? 29.581 -5.556 -8.873  1.00 70.03  ? 461 HOH A O   1 
HETATM 1370 O O   A HOH H 8 .   ? 12.459 14.148 -15.808 0.50 42.38  ? 462 HOH A O   1 
HETATM 1371 O O   B HOH H 8 .   ? 12.864 12.460 -17.188 0.50 42.39  ? 462 HOH A O   1 
HETATM 1372 O O   . HOH H 8 .   ? 18.994 10.317 -19.407 1.00 69.19  ? 463 HOH A O   1 
HETATM 1373 O O   . HOH H 8 .   ? 32.221 5.331  -19.610 1.00 48.41  ? 464 HOH A O   1 
HETATM 1374 O O   . HOH H 8 .   ? 24.213 8.686  -19.413 1.00 42.98  ? 465 HOH A O   1 
HETATM 1375 O O   . HOH H 8 .   ? 27.616 25.194 -19.484 1.00 43.27  ? 466 HOH A O   1 
HETATM 1376 O O   . HOH H 8 .   ? 7.181  30.004 -12.970 1.00 65.38  ? 467 HOH A O   1 
HETATM 1377 O O   . HOH H 8 .   ? 33.641 4.606  -18.085 1.00 49.98  ? 468 HOH A O   1 
HETATM 1378 O O   . HOH H 8 .   ? 24.861 27.979 5.507   1.00 73.67  ? 469 HOH A O   1 
HETATM 1379 O O   . HOH H 8 .   ? 21.889 0.246  -12.360 1.00 47.98  ? 470 HOH A O   1 
HETATM 1380 O O   . HOH H 8 .   ? 27.431 25.564 4.237   1.00 37.28  ? 471 HOH A O   1 
HETATM 1381 O O   . HOH H 8 .   ? 21.195 19.897 -22.193 1.00 28.59  ? 472 HOH A O   1 
HETATM 1382 O O   . HOH H 8 .   ? 21.921 6.616  11.548  1.00 53.71  ? 473 HOH A O   1 
HETATM 1383 O O   . HOH H 8 .   ? 4.901  22.663 5.460   1.00 40.82  ? 474 HOH A O   1 
HETATM 1384 O O   . HOH H 8 .   ? 32.469 19.427 -9.369  1.00 32.66  ? 475 HOH A O   1 
HETATM 1385 O O   . HOH H 8 .   ? 26.586 22.433 6.993   1.00 40.52  ? 476 HOH A O   1 
HETATM 1386 O O   . HOH H 8 .   ? 33.391 21.698 -14.488 1.00 59.46  ? 477 HOH A O   1 
HETATM 1387 O O   . HOH H 8 .   ? 32.256 24.119 -6.792  1.00 54.83  ? 478 HOH A O   1 
HETATM 1388 O O   . HOH H 8 .   ? 24.538 7.287  13.619  1.00 64.98  ? 479 HOH A O   1 
HETATM 1389 O O   . HOH H 8 .   ? 17.000 37.414 1.244   1.00 58.71  ? 480 HOH A O   1 
HETATM 1390 O O   . HOH H 8 .   ? 30.904 19.241 -16.125 1.00 40.89  ? 481 HOH A O   1 
HETATM 1391 O O   . HOH H 8 .   ? 29.125 25.876 1.917   1.00 40.17  ? 482 HOH A O   1 
HETATM 1392 O O   . HOH H 8 .   ? 27.925 7.548  -20.770 1.00 47.55  ? 483 HOH A O   1 
HETATM 1393 O O   . HOH H 8 .   ? 30.097 29.616 -20.208 1.00 54.05  ? 484 HOH A O   1 
HETATM 1394 O O   . HOH H 8 .   ? 32.617 3.800  -8.706  1.00 27.92  ? 485 HOH A O   1 
HETATM 1395 O O   . HOH H 8 .   ? 29.545 29.314 -1.057  1.00 43.01  ? 486 HOH A O   1 
HETATM 1396 O O   . HOH H 8 .   ? 10.081 26.697 -16.170 1.00 60.08  ? 487 HOH A O   1 
HETATM 1397 O O   . HOH H 8 .   ? 23.444 6.892  -21.259 1.00 57.91  ? 488 HOH A O   1 
HETATM 1398 O O   . HOH H 8 .   ? 34.274 25.441 -5.113  1.00 62.36  ? 489 HOH A O   1 
HETATM 1399 O O   . HOH H 8 .   ? 28.560 17.291 -29.200 1.00 72.29  ? 490 HOH A O   1 
HETATM 1400 O O   . HOH H 8 .   ? 25.859 21.730 -23.406 1.00 29.24  ? 491 HOH A O   1 
HETATM 1401 O O   . HOH H 8 .   ? 25.130 21.025 9.149   1.00 51.43  ? 492 HOH A O   1 
HETATM 1402 O O   . HOH H 8 .   ? 6.378  32.192 2.027   1.00 34.69  ? 493 HOH A O   1 
HETATM 1403 O O   . HOH H 8 .   ? 33.157 19.135 -14.307 1.00 43.85  ? 494 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET A 1   ? 0.5045 0.4340 0.8508 0.1259  -0.0606 -0.0105 0   MET A N   
2    C CA  . MET A 1   ? 0.5403 0.4640 0.8584 -0.0184 -0.0169 -0.0185 0   MET A CA  
3    C C   . MET A 1   ? 0.4857 0.2566 0.7064 0.0165  0.0667  0.1027  0   MET A C   
4    O O   . MET A 1   ? 0.2876 0.4123 0.6863 -0.0096 -0.0277 -0.0217 0   MET A O   
5    C CB  . MET A 1   ? 0.6335 0.4522 0.9574 -0.0293 0.1550  -0.0500 0   MET A CB  
6    N N   . VAL A 2   ? 0.5721 0.6138 0.6957 0.0155  0.1518  0.0330  1   VAL A N   
7    C CA  . VAL A 2   ? 0.6561 0.5263 0.7111 0.1328  0.2318  0.3378  1   VAL A CA  
8    C C   . VAL A 2   ? 0.4737 0.3643 0.4992 0.1863  0.1344  0.1960  1   VAL A C   
9    O O   . VAL A 2   ? 0.4377 0.3155 0.3927 0.1289  0.0752  0.0867  1   VAL A O   
10   C CB  . VAL A 2   ? 1.4417 0.9627 0.6569 0.1369  0.5200  0.4864  1   VAL A CB  
11   C CG1 . VAL A 2   ? 1.6050 1.3792 0.5116 0.2737  0.4614  0.5097  1   VAL A CG1 
12   C CG2 . VAL A 2   ? 1.4926 2.0839 2.2084 0.1498  0.5897  0.5817  1   VAL A CG2 
13   N N   . ASP A 3   ? 0.2782 0.2620 0.4673 0.1236  0.0602  0.0688  2   ASP A N   
14   C CA  . ASP A 3   ? 0.3222 0.2428 0.4951 0.0583  0.0370  0.0029  2   ASP A CA  
15   C C   . ASP A 3   ? 0.3252 0.1730 0.3820 0.0887  -0.0515 0.0360  2   ASP A C   
16   O O   . ASP A 3   ? 0.3329 0.2130 0.4571 0.0562  -0.0422 0.0838  2   ASP A O   
17   C CB  . ASP A 3   ? 0.4147 0.1562 0.7704 0.0556  0.0131  -0.0171 2   ASP A CB  
18   C CG  . ASP A 3   ? 0.5116 0.2818 0.8743 0.1601  -0.1314 0.1578  2   ASP A CG  
19   O OD1 . ASP A 3   ? 0.8431 0.5122 1.1863 -0.1311 -0.1471 0.1122  2   ASP A OD1 
20   O OD2 . ASP A 3   ? 0.6831 0.5183 1.0089 -0.1488 -0.2156 0.2246  2   ASP A OD2 
21   N N   . ALA A 4   ? 0.2472 0.2240 0.3510 0.0464  -0.0034 0.0327  3   ALA A N   
22   C CA  . ALA A 4   ? 0.2800 0.2497 0.3310 0.0532  0.0036  0.0585  3   ALA A CA  
23   C C   . ALA A 4   ? 0.2538 0.1938 0.2413 0.0193  0.0210  0.0524  3   ALA A C   
24   O O   . ALA A 4   ? 0.2499 0.2470 0.2652 0.0161  0.0216  0.0409  3   ALA A O   
25   C CB  . ALA A 4   ? 0.3113 0.3229 0.4332 0.0526  -0.0469 -0.0094 3   ALA A CB  
26   N N   . PHE A 5   ? 0.2277 0.1794 0.2362 0.0034  0.0250  0.0429  4   PHE A N   
27   C CA  . PHE A 5   ? 0.2448 0.1491 0.2292 0.0048  -0.0020 0.0358  4   PHE A CA  
28   C C   . PHE A 5   ? 0.2224 0.1344 0.2948 0.0186  0.0354  0.0229  4   PHE A C   
29   O O   . PHE A 5   ? 0.2109 0.1643 0.2719 0.0133  0.0277  0.0270  4   PHE A O   
30   C CB  . PHE A 5   ? 0.2073 0.1398 0.2341 0.0148  0.0252  0.0336  4   PHE A CB  
31   C CG  . PHE A 5   ? 0.1890 0.1603 0.2196 0.0137  0.0130  0.0417  4   PHE A CG  
32   C CD1 . PHE A 5   ? 0.2150 0.1589 0.2658 0.0252  -0.0111 0.0196  4   PHE A CD1 
33   C CD2 . PHE A 5   ? 0.1956 0.1941 0.2967 0.0651  0.0293  0.0427  4   PHE A CD2 
34   C CE1 . PHE A 5   ? 0.2024 0.1875 0.2504 0.0011  -0.0210 0.0300  4   PHE A CE1 
35   C CE2 . PHE A 5   ? 0.2002 0.2229 0.2765 0.0484  0.0030  0.0584  4   PHE A CE2 
36   C CZ  . PHE A 5   ? 0.2143 0.1880 0.2238 0.0000  -0.0053 0.0702  4   PHE A CZ  
37   N N   . LEU A 6   ? 0.2221 0.1344 0.2861 0.0346  0.0084  0.0217  5   LEU A N   
38   C CA  . LEU A 6   ? 0.2543 0.1604 0.2609 0.0154  0.0107  0.0294  5   LEU A CA  
39   C C   . LEU A 6   ? 0.3078 0.1871 0.2627 0.0058  0.0223  0.0417  5   LEU A C   
40   O O   . LEU A 6   ? 0.2465 0.2697 0.2755 -0.0130 -0.0043 0.0355  5   LEU A O   
41   C CB  . LEU A 6   ? 0.2838 0.1371 0.2921 0.0140  0.0237  0.0329  5   LEU A CB  
42   C CG  . LEU A 6   ? 0.2841 0.1465 0.3062 0.0344  0.0480  0.0204  5   LEU A CG  
43   C CD1 . LEU A 6   ? 0.3218 0.1767 0.4113 0.0623  0.0853  0.0081  5   LEU A CD1 
44   C CD2 . LEU A 6   ? 0.3206 0.2989 0.3173 0.0345  0.0278  0.0242  5   LEU A CD2 
45   N N   . GLY A 7   ? 0.2696 0.1663 0.2842 0.0350  0.0585  0.0519  6   GLY A N   
46   C CA  . GLY A 7   ? 0.2984 0.1780 0.2994 0.0184  0.0796  0.0563  6   GLY A CA  
47   C C   . GLY A 7   ? 0.2541 0.1893 0.2587 0.0095  0.0740  0.0399  6   GLY A C   
48   O O   . GLY A 7   ? 0.2624 0.1940 0.2779 0.0212  0.0718  0.0645  6   GLY A O   
49   N N   . THR A 8   ? 0.2675 0.1860 0.3021 0.0217  0.1049  0.0665  7   THR A N   
50   C CA  . THR A 8   ? 0.2239 0.2078 0.2692 0.0020  0.0691  0.0371  7   THR A CA  
51   C C   . THR A 8   ? 0.2848 0.1750 0.2993 0.0023  0.0412  0.0453  7   THR A C   
52   O O   . THR A 8   ? 0.3756 0.2009 0.3022 0.0300  0.0752  0.0620  7   THR A O   
53   C CB  . THR A 8   ? 0.2560 0.1903 0.3549 -0.0125 0.0550  0.0342  7   THR A CB  
54   O OG1 . THR A 8   ? 0.2968 0.1942 0.3710 -0.0471 0.0639  0.0044  7   THR A OG1 
55   C CG2 . THR A 8   ? 0.2647 0.2319 0.3934 0.0019  0.0980  0.0648  7   THR A CG2 
56   N N   . TRP A 9   ? 0.2815 0.1918 0.2832 0.0070  0.0503  0.0617  8   TRP A N   
57   C CA  . TRP A 9   ? 0.2350 0.1930 0.2992 0.0338  0.0721  0.0423  8   TRP A CA  
58   C C   . TRP A 9   ? 0.2056 0.2159 0.2949 0.0242  0.0785  0.0421  8   TRP A C   
59   O O   . TRP A 9   ? 0.2709 0.2347 0.3252 0.0583  0.0343  0.0340  8   TRP A O   
60   C CB  . TRP A 9   ? 0.2220 0.1948 0.3023 0.0035  0.0557  0.0310  8   TRP A CB  
61   C CG  . TRP A 9   ? 0.2349 0.1914 0.2658 0.0220  0.0554  0.0409  8   TRP A CG  
62   C CD1 . TRP A 9   ? 0.2044 0.1973 0.2723 0.0174  0.0593  0.0395  8   TRP A CD1 
63   C CD2 . TRP A 9   ? 0.2496 0.1587 0.2517 0.0434  0.0529  0.0580  8   TRP A CD2 
64   N NE1 . TRP A 9   ? 0.2373 0.1726 0.3031 0.0441  0.0365  0.0351  8   TRP A NE1 
65   C CE2 . TRP A 9   ? 0.2431 0.1441 0.3023 0.0314  0.0415  0.0498  8   TRP A CE2 
66   C CE3 . TRP A 9   ? 0.2935 0.2158 0.2545 0.0440  0.0517  0.0551  8   TRP A CE3 
67   C CZ2 . TRP A 9   ? 0.2767 0.2098 0.2773 0.0269  0.0377  0.0733  8   TRP A CZ2 
68   C CZ3 . TRP A 9   ? 0.3082 0.2079 0.2454 0.0485  0.0413  0.0579  8   TRP A CZ3 
69   C CH2 . TRP A 9   ? 0.2844 0.2033 0.2741 0.0651  0.0324  0.0766  8   TRP A CH2 
70   N N   A LYS A 10  ? 0.2296 0.1610 0.3012 0.0341  0.1183  0.0701  9   LYS A N   
71   N N   B LYS A 10  ? 0.2296 0.1614 0.3002 0.0202  0.0876  0.0507  9   LYS A N   
72   C CA  A LYS A 10  ? 0.2020 0.1876 0.3417 0.0271  0.0933  0.0421  9   LYS A CA  
73   C CA  B LYS A 10  ? 0.2053 0.1638 0.3242 0.0056  0.0719  0.0404  9   LYS A CA  
74   C C   A LYS A 10  ? 0.1469 0.1746 0.3129 0.0166  0.1016  0.0665  9   LYS A C   
75   C C   B LYS A 10  ? 0.1964 0.1537 0.3203 0.0125  0.0896  0.0462  9   LYS A C   
76   O O   A LYS A 10  ? 0.2411 0.1704 0.2453 0.0495  0.0750  0.0444  9   LYS A O   
77   O O   B LYS A 10  ? 0.2048 0.1700 0.2966 0.0266  0.0942  0.0461  9   LYS A O   
78   C CB  A LYS A 10  ? 0.1994 0.1755 0.4752 -0.0016 0.1364  0.0615  9   LYS A CB  
79   C CB  B LYS A 10  ? 0.2116 0.1046 0.3532 -0.0271 0.0626  0.0278  9   LYS A CB  
80   C CG  A LYS A 10  ? 0.2893 0.3272 0.5560 0.0910  0.1433  0.0304  9   LYS A CG  
81   C CG  B LYS A 10  ? 0.2165 0.1296 0.3501 -0.0420 0.0325  0.0409  9   LYS A CG  
82   C CD  A LYS A 10  ? 0.4179 0.3995 0.6191 0.1354  0.0404  0.0511  9   LYS A CD  
83   C CD  B LYS A 10  ? 0.2426 0.1384 0.3884 -0.0802 0.0512  0.0338  9   LYS A CD  
84   C CE  A LYS A 10  ? 0.4274 0.5291 0.7248 0.1042  0.1066  0.0105  9   LYS A CE  
85   C CE  B LYS A 10  ? 0.2071 0.1845 0.4165 -0.1081 0.0172  0.0412  9   LYS A CE  
86   N NZ  A LYS A 10  ? 0.5815 0.6902 0.8475 0.0789  -0.0231 -0.0356 9   LYS A NZ  
87   N NZ  B LYS A 10  ? 0.2391 0.2056 0.4001 -0.0659 0.0507  0.0460  9   LYS A NZ  
88   N N   . LEU A 11  ? 0.2110 0.2155 0.3435 0.0583  0.0892  0.0569  10  LEU A N   
89   C CA  . LEU A 11  ? 0.2266 0.2110 0.2725 0.0267  0.0906  0.0499  10  LEU A CA  
90   C C   . LEU A 11  ? 0.2317 0.2389 0.2785 0.0390  0.1131  0.0532  10  LEU A C   
91   O O   . LEU A 11  ? 0.2565 0.2721 0.3398 0.0243  0.1377  0.0337  10  LEU A O   
92   C CB  . LEU A 11  ? 0.2100 0.2364 0.3029 0.0146  0.0300  0.0397  10  LEU A CB  
93   C CG  . LEU A 11  ? 0.2125 0.2199 0.2901 0.0218  0.0628  0.0191  10  LEU A CG  
94   C CD1 . LEU A 11  ? 0.1981 0.2521 0.2925 0.0549  0.0585  0.0365  10  LEU A CD1 
95   C CD2 . LEU A 11  ? 0.1655 0.2493 0.3329 0.0148  0.0504  -0.0205 10  LEU A CD2 
96   N N   . VAL A 12  ? 0.2873 0.2190 0.2551 0.0971  0.0612  0.0505  11  VAL A N   
97   C CA  . VAL A 12  ? 0.3045 0.2949 0.2833 0.0930  0.1025  0.0608  11  VAL A CA  
98   C C   . VAL A 12  ? 0.3177 0.2663 0.2537 0.0975  0.1365  0.0732  11  VAL A C   
99   O O   . VAL A 12  ? 0.4166 0.2791 0.2725 0.0969  0.1697  0.0506  11  VAL A O   
100  C CB  . VAL A 12  ? 0.3058 0.2934 0.2566 0.0951  0.0730  0.0388  11  VAL A CB  
101  C CG1 . VAL A 12  ? 0.3544 0.2804 0.3436 0.0573  0.0903  0.0564  11  VAL A CG1 
102  C CG2 . VAL A 12  ? 0.2735 0.3462 0.3355 0.1183  0.0782  0.0723  11  VAL A CG2 
103  N N   . ASP A 13  ? 0.2454 0.2301 0.2379 0.0871  0.0942  0.0519  12  ASP A N   
104  C CA  . ASP A 13  ? 0.2998 0.2282 0.2377 0.0999  0.0775  0.0491  12  ASP A CA  
105  C C   . ASP A 13  ? 0.1968 0.2192 0.2330 0.0735  0.0640  0.0325  12  ASP A C   
106  O O   . ASP A 13  ? 0.1997 0.2199 0.2181 0.0806  0.0490  0.0190  12  ASP A O   
107  C CB  . ASP A 13  ? 0.3155 0.2539 0.2471 0.0958  0.0549  0.0408  12  ASP A CB  
108  C CG  . ASP A 13  ? 0.4184 0.2666 0.3340 0.0867  -0.0392 -0.0097 12  ASP A CG  
109  O OD1 . ASP A 13  ? 0.3377 0.3822 0.2950 0.0855  0.0251  -0.0236 12  ASP A OD1 
110  O OD2 . ASP A 13  ? 0.3980 0.3711 0.3322 0.0926  0.0028  -0.0394 12  ASP A OD2 
111  N N   . SER A 14  ? 0.2478 0.2117 0.2427 0.0913  0.0830  0.0128  13  SER A N   
112  C CA  . SER A 14  ? 0.1760 0.2269 0.2293 0.0662  0.0758  0.0153  13  SER A CA  
113  C C   . SER A 14  ? 0.2109 0.2280 0.2316 0.0572  0.0802  0.0165  13  SER A C   
114  O O   . SER A 14  ? 0.2473 0.2149 0.2409 0.0805  0.0784  0.0117  13  SER A O   
115  C CB  . SER A 14  ? 0.2243 0.1888 0.2541 0.0429  0.0509  0.0008  13  SER A CB  
116  O OG  . SER A 14  ? 0.2392 0.2025 0.2350 0.0695  0.0678  0.0077  13  SER A OG  
117  N N   . LYS A 15  ? 0.1891 0.1821 0.2321 0.0731  0.0604  0.0172  14  LYS A N   
118  C CA  . LYS A 15  ? 0.2665 0.1777 0.2065 0.0439  0.0371  0.0244  14  LYS A CA  
119  C C   . LYS A 15  ? 0.2044 0.1811 0.1914 0.0774  0.0388  -0.0031 14  LYS A C   
120  O O   . LYS A 15  ? 0.2123 0.1718 0.1921 0.0835  0.0332  -0.0170 14  LYS A O   
121  C CB  . LYS A 15  ? 0.4630 0.3738 0.1845 0.0028  -0.0413 0.0454  14  LYS A CB  
122  C CG  . LYS A 15  ? 0.4437 0.4730 0.2385 0.0063  -0.0275 -0.0509 14  LYS A CG  
123  C CD  . LYS A 15  ? 0.4163 0.3866 0.1882 0.0169  -0.0111 -0.0606 14  LYS A CD  
124  C CE  . LYS A 15  ? 0.3751 0.3482 0.2854 0.1075  -0.0071 -0.0438 14  LYS A CE  
125  N NZ  . LYS A 15  ? 0.3655 0.3161 0.3414 0.0838  -0.0717 -0.0469 14  LYS A NZ  
126  N N   . ASN A 16  ? 0.1796 0.2003 0.1886 0.0882  0.0394  -0.0150 15  ASN A N   
127  C CA  . ASN A 16  ? 0.1633 0.1597 0.2059 0.0574  0.0049  -0.0119 15  ASN A CA  
128  C C   . ASN A 16  ? 0.1732 0.1492 0.2198 0.0392  0.0122  -0.0059 15  ASN A C   
129  O O   . ASN A 16  ? 0.2013 0.1270 0.2102 0.0411  0.0260  -0.0219 15  ASN A O   
130  C CB  . ASN A 16  ? 0.1657 0.1595 0.2346 0.0541  0.0072  -0.0411 15  ASN A CB  
131  C CG  . ASN A 16  ? 0.1924 0.1974 0.2579 0.0281  0.0299  -0.0685 15  ASN A CG  
132  O OD1 . ASN A 16  ? 0.2358 0.2333 0.2422 0.0845  0.0069  -0.0742 15  ASN A OD1 
133  N ND2 . ASN A 16  ? 0.1873 0.2748 0.3231 0.0399  0.0060  -0.0703 15  ASN A ND2 
134  N N   . PHE A 17  ? 0.1751 0.1473 0.2309 0.0391  0.0249  -0.0312 16  PHE A N   
135  C CA  . PHE A 17  ? 0.1784 0.0932 0.2006 0.0362  0.0192  -0.0011 16  PHE A CA  
136  C C   . PHE A 17  ? 0.2604 0.1972 0.1552 0.0907  -0.0202 -0.1050 16  PHE A C   
137  O O   . PHE A 17  ? 0.2151 0.2008 0.2203 0.0818  0.0140  -0.0543 16  PHE A O   
138  C CB  . PHE A 17  ? 0.1719 0.1189 0.2410 0.0603  0.0427  -0.0002 16  PHE A CB  
139  C CG  . PHE A 17  ? 0.1409 0.1669 0.2477 0.0658  0.0075  -0.0110 16  PHE A CG  
140  C CD1 . PHE A 17  ? 0.2205 0.1926 0.2501 0.0308  0.0350  -0.0387 16  PHE A CD1 
141  C CD2 . PHE A 17  ? 0.1808 0.2233 0.2642 0.0300  -0.0347 0.0007  16  PHE A CD2 
142  C CE1 . PHE A 17  ? 0.2605 0.2198 0.2473 0.0504  0.0312  -0.0581 16  PHE A CE1 
143  C CE2 . PHE A 17  ? 0.2235 0.2129 0.2856 0.0262  -0.0282 -0.0034 16  PHE A CE2 
144  C CZ  . PHE A 17  ? 0.2888 0.1959 0.2461 0.0227  -0.0224 -0.0430 16  PHE A CZ  
145  N N   . ASP A 18  ? 0.2118 0.1482 0.3032 0.0758  -0.0166 -0.1273 17  ASP A N   
146  C CA  . ASP A 18  ? 0.2107 0.2291 0.2178 0.0834  0.0256  -0.0308 17  ASP A CA  
147  C C   . ASP A 18  ? 0.1917 0.1891 0.2083 0.1045  0.0200  -0.0224 17  ASP A C   
148  O O   . ASP A 18  ? 0.2920 0.1953 0.2265 0.1054  -0.0125 0.0050  17  ASP A O   
149  C CB  . ASP A 18  ? 0.2304 0.2333 0.2160 0.1074  0.0420  -0.0049 17  ASP A CB  
150  C CG  . ASP A 18  ? 0.2834 0.3574 0.1696 0.0555  0.0266  0.0565  17  ASP A CG  
151  O OD1 . ASP A 18  ? 0.2440 0.4425 0.6326 0.0878  0.0123  -0.0756 17  ASP A OD1 
152  O OD2 . ASP A 18  ? 0.2555 0.2688 0.2190 0.0665  0.0241  -0.0206 17  ASP A OD2 
153  N N   . ASP A 19  ? 0.2249 0.2084 0.2164 0.0680  0.0175  -0.0314 18  ASP A N   
154  C CA  . ASP A 19  ? 0.2762 0.1532 0.2625 0.1204  0.0596  -0.0005 18  ASP A CA  
155  C C   . ASP A 19  ? 0.2508 0.1580 0.2731 0.0805  0.0714  -0.0036 18  ASP A C   
156  O O   . ASP A 19  ? 0.3118 0.1555 0.3026 0.0681  0.0386  0.0157  18  ASP A O   
157  C CB  . ASP A 19  ? 0.3063 0.2276 0.2826 0.0217  0.0603  -0.0086 18  ASP A CB  
158  C CG  . ASP A 19  ? 0.3798 0.1777 0.3323 0.0174  0.0680  -0.0014 18  ASP A CG  
159  O OD1 . ASP A 19  ? 0.4236 0.1938 0.4110 0.0366  0.0619  -0.0264 18  ASP A OD1 
160  O OD2 . ASP A 19  ? 0.4186 0.2282 0.5015 -0.0052 0.1334  -0.0499 18  ASP A OD2 
161  N N   . TYR A 20  ? 0.2355 0.1519 0.2353 0.0744  0.0661  0.0069  19  TYR A N   
162  C CA  . TYR A 20  ? 0.2586 0.1550 0.2183 0.0755  0.0520  0.0022  19  TYR A CA  
163  C C   . TYR A 20  ? 0.2632 0.1708 0.2476 0.0996  0.0450  0.0047  19  TYR A C   
164  O O   . TYR A 20  ? 0.2747 0.1885 0.2214 0.1087  0.0401  0.0228  19  TYR A O   
165  C CB  . TYR A 20  ? 0.2191 0.1766 0.2091 0.0888  0.0414  0.0026  19  TYR A CB  
166  C CG  . TYR A 20  ? 0.1731 0.1517 0.1966 0.0629  0.0321  0.0072  19  TYR A CG  
167  C CD1 . TYR A 20  ? 0.1705 0.1377 0.2007 0.0357  0.0158  0.0037  19  TYR A CD1 
168  C CD2 . TYR A 20  ? 0.1649 0.1695 0.2092 0.0481  0.0351  0.0097  19  TYR A CD2 
169  C CE1 . TYR A 20  ? 0.1350 0.1438 0.1900 0.0229  0.0200  0.0054  19  TYR A CE1 
170  C CE2 . TYR A 20  ? 0.1517 0.1451 0.2187 0.0347  0.0072  -0.0128 19  TYR A CE2 
171  C CZ  . TYR A 20  ? 0.1594 0.1325 0.2274 0.0286  0.0203  0.0102  19  TYR A CZ  
172  O OH  . TYR A 20  ? 0.1713 0.1531 0.2188 0.0345  0.0158  -0.0049 19  TYR A OH  
173  N N   . MET A 21  ? 0.2451 0.2119 0.2096 0.0941  0.0299  -0.0038 20  MET A N   
174  C CA  . MET A 21  ? 0.2835 0.1991 0.1845 0.0961  0.0197  -0.0024 20  MET A CA  
175  C C   . MET A 21  ? 0.3139 0.2105 0.2196 0.1009  0.0247  -0.0022 20  MET A C   
176  O O   . MET A 21  ? 0.2795 0.2516 0.2103 0.1152  0.0309  0.0168  20  MET A O   
177  C CB  . MET A 21  ? 0.2533 0.2191 0.2103 0.1038  0.0292  -0.0052 20  MET A CB  
178  C CG  . MET A 21  ? 0.2596 0.2123 0.2104 0.0769  0.0313  -0.0207 20  MET A CG  
179  S SD  . MET A 21  ? 0.2836 0.2308 0.2234 0.0536  0.0010  -0.0221 20  MET A SD  
180  C CE  . MET A 21  ? 0.2371 0.2340 0.2347 0.0323  0.0175  -0.0398 20  MET A CE  
181  N N   . LYS A 22  ? 0.3087 0.2162 0.2167 0.1336  0.0318  -0.0083 21  LYS A N   
182  C CA  . LYS A 22  ? 0.2956 0.2586 0.2802 0.1482  0.0361  0.0556  21  LYS A CA  
183  C C   . LYS A 22  ? 0.3087 0.1915 0.2633 0.1449  0.0537  0.0388  21  LYS A C   
184  O O   . LYS A 22  ? 0.3572 0.2585 0.2821 0.1577  0.0378  0.0673  21  LYS A O   
185  C CB  . LYS A 22  ? 0.3298 0.2434 0.2876 0.1172  0.0431  0.0278  21  LYS A CB  
186  C CG  . LYS A 22  ? 0.3716 0.2596 0.3694 0.1200  0.0915  0.0504  21  LYS A CG  
187  C CD  . LYS A 22  ? 0.4379 0.2822 0.4481 0.1756  0.1226  -0.0025 21  LYS A CD  
188  C CE  . LYS A 22  ? 0.6830 0.2767 0.5877 0.2219  0.0510  -0.0159 21  LYS A CE  
189  N NZ  . LYS A 22  ? 0.7934 0.4293 0.6705 0.1395  -0.0536 -0.1562 21  LYS A NZ  
190  N N   . SER A 23  ? 0.3355 0.2004 0.3033 0.1495  0.0408  0.0501  22  SER A N   
191  C CA  . SER A 23  ? 0.3742 0.1905 0.3017 0.1162  0.0906  0.0643  22  SER A CA  
192  C C   . SER A 23  ? 0.3742 0.2092 0.3224 0.1279  0.0809  0.0624  22  SER A C   
193  O O   . SER A 23  ? 0.3496 0.2862 0.3328 0.1304  0.0805  0.0955  22  SER A O   
194  C CB  . SER A 23  ? 0.4039 0.2111 0.3060 0.1296  0.0856  0.0553  22  SER A CB  
195  O OG  . SER A 23  ? 0.2853 0.2067 0.3033 0.0975  0.0571  0.0354  22  SER A OG  
196  N N   . LEU A 24  ? 0.3330 0.2216 0.2668 0.1079  0.0398  0.0299  23  LEU A N   
197  C CA  . LEU A 24  ? 0.3453 0.3123 0.2458 0.1296  0.0381  0.0264  23  LEU A CA  
198  C C   . LEU A 24  ? 0.3817 0.3049 0.2211 0.1616  0.0488  0.0407  23  LEU A C   
199  O O   . LEU A 24  ? 0.4231 0.3718 0.2307 0.1649  -0.0220 0.0193  23  LEU A O   
200  C CB  . LEU A 24  ? 0.3095 0.2978 0.2399 0.1351  0.0455  0.0266  23  LEU A CB  
201  C CG  . LEU A 24  ? 0.2916 0.3055 0.2620 0.1373  0.0245  -0.0348 23  LEU A CG  
202  C CD1 . LEU A 24  ? 0.4212 0.2909 0.2544 0.1382  0.0214  -0.0024 23  LEU A CD1 
203  C CD2 . LEU A 24  ? 0.2717 0.2455 0.3128 0.0952  0.0356  -0.0291 23  LEU A CD2 
204  N N   . GLY A 25  ? 0.4068 0.2882 0.2676 0.1713  0.0358  0.0161  24  GLY A N   
205  C CA  . GLY A 25  ? 0.3891 0.3023 0.3095 0.1519  0.0263  0.0321  24  GLY A CA  
206  C C   . GLY A 25  ? 0.3642 0.2905 0.2070 0.1499  -0.0040 0.0271  24  GLY A C   
207  O O   . GLY A 25  ? 0.3705 0.4215 0.2590 0.0884  -0.0338 0.0536  24  GLY A O   
208  N N   . VAL A 26  ? 0.3140 0.2918 0.2162 0.1539  0.0028  0.0284  25  VAL A N   
209  C CA  . VAL A 26  ? 0.3334 0.3278 0.2219 0.1004  -0.0198 -0.0138 25  VAL A CA  
210  C C   . VAL A 26  ? 0.3260 0.3364 0.2647 0.1117  0.0038  0.0267  25  VAL A C   
211  O O   . VAL A 26  ? 0.3294 0.3239 0.2871 0.1571  0.0328  -0.0064 25  VAL A O   
212  C CB  . VAL A 26  ? 0.2899 0.2799 0.2398 0.1264  -0.0272 -0.0301 25  VAL A CB  
213  C CG1 . VAL A 26  ? 0.3460 0.3225 0.2622 0.0724  -0.0224 -0.0339 25  VAL A CG1 
214  C CG2 . VAL A 26  ? 0.3103 0.3378 0.2655 0.1484  -0.0085 -0.0438 25  VAL A CG2 
215  N N   . GLY A 27  ? 0.3676 0.4476 0.3696 0.1469  -0.0537 0.0354  26  GLY A N   
216  C CA  . GLY A 27  ? 0.3584 0.5107 0.3753 0.1628  -0.0087 0.0490  26  GLY A CA  
217  C C   . GLY A 27  ? 0.3818 0.3758 0.2950 0.1578  -0.0602 -0.0245 26  GLY A C   
218  O O   . GLY A 27  ? 0.3608 0.3689 0.3597 0.1476  -0.0588 0.0266  26  GLY A O   
219  N N   . PHE A 28  ? 0.3699 0.3605 0.3479 0.1685  -0.0251 -0.0059 27  PHE A N   
220  C CA  . PHE A 28  ? 0.2268 0.3745 0.3501 0.1247  -0.0233 -0.0254 27  PHE A CA  
221  C C   . PHE A 28  ? 0.2811 0.3875 0.3868 0.0916  -0.0733 -0.0410 27  PHE A C   
222  O O   . PHE A 28  ? 0.2872 0.4230 0.4072 0.1046  -0.0146 0.0057  27  PHE A O   
223  C CB  . PHE A 28  ? 0.3993 0.4015 0.4750 0.1986  -0.0671 -0.0390 27  PHE A CB  
224  C CG  . PHE A 28  ? 0.4386 0.5095 0.4809 0.2320  -0.0317 -0.0113 27  PHE A CG  
225  C CD1 . PHE A 28  ? 0.4140 0.4839 0.4073 0.0978  -0.0202 0.0094  27  PHE A CD1 
226  C CD2 . PHE A 28  ? 0.3707 0.7945 0.4093 0.2219  -0.0358 0.1370  27  PHE A CD2 
227  C CE1 . PHE A 28  ? 0.3332 0.5401 0.4329 0.0921  0.0043  -0.0717 27  PHE A CE1 
228  C CE2 . PHE A 28  ? 0.6347 0.8901 0.4235 0.2429  -0.0493 0.0145  27  PHE A CE2 
229  C CZ  . PHE A 28  ? 0.3998 0.6649 0.4245 0.2078  -0.0182 -0.1084 27  PHE A CZ  
230  N N   . ALA A 29  ? 0.3336 0.4408 0.3594 0.1234  -0.0890 -0.0302 28  ALA A N   
231  C CA  . ALA A 29  ? 0.2731 0.4789 0.5442 0.1119  -0.1348 -0.0963 28  ALA A CA  
232  C C   . ALA A 29  ? 0.3257 0.4447 0.4978 0.1031  -0.0605 -0.0635 28  ALA A C   
233  O O   . ALA A 29  ? 0.2589 0.5256 0.5325 0.0418  -0.1016 -0.0340 28  ALA A O   
234  C CB  . ALA A 29  ? 0.3194 0.5225 0.6317 0.0627  -0.2111 -0.1195 28  ALA A CB  
235  N N   . THR A 30  ? 0.3310 0.4611 0.3744 0.0644  -0.1207 -0.0385 29  THR A N   
236  C CA  . THR A 30  ? 0.3699 0.3738 0.3712 0.0392  -0.1242 -0.0491 29  THR A CA  
237  C C   . THR A 30  ? 0.3708 0.3486 0.3060 -0.0047 -0.0769 -0.0129 29  THR A C   
238  O O   . THR A 30  ? 0.3452 0.3116 0.3106 0.0065  -0.0612 -0.0550 29  THR A O   
239  C CB  . THR A 30  ? 0.4016 0.4995 0.3595 0.0848  -0.1490 -0.0797 29  THR A CB  
240  O OG1 . THR A 30  ? 0.4066 0.6198 0.3260 0.0729  -0.1307 -0.0751 29  THR A OG1 
241  C CG2 . THR A 30  ? 0.4812 0.4253 0.5004 0.0766  -0.1632 -0.1326 29  THR A CG2 
242  N N   . ARG A 31  ? 0.3448 0.3254 0.2830 0.0743  -0.0500 -0.0198 30  ARG A N   
243  C CA  . ARG A 31  ? 0.2372 0.2777 0.2601 0.0587  -0.0069 -0.0556 30  ARG A CA  
244  C C   . ARG A 31  ? 0.2226 0.3271 0.3026 0.0459  0.0000  -0.0332 30  ARG A C   
245  O O   . ARG A 31  ? 0.2569 0.3092 0.2918 0.0489  -0.0090 -0.0429 30  ARG A O   
246  C CB  . ARG A 31  ? 0.1846 0.2805 0.2736 0.0964  -0.0171 -0.0354 30  ARG A CB  
247  C CG  . ARG A 31  ? 0.2411 0.2834 0.2619 0.0923  0.0108  -0.0351 30  ARG A CG  
248  C CD  . ARG A 31  ? 0.2668 0.2699 0.3132 0.1055  -0.0371 -0.0323 30  ARG A CD  
249  N NE  . ARG A 31  ? 0.2838 0.2833 0.2920 0.1127  -0.0124 -0.0132 30  ARG A NE  
250  C CZ  . ARG A 31  ? 0.2917 0.2782 0.3087 0.1037  -0.0278 -0.0095 30  ARG A CZ  
251  N NH1 . ARG A 31  ? 0.3785 0.3168 0.3059 0.1918  0.0069  -0.0272 30  ARG A NH1 
252  N NH2 . ARG A 31  ? 0.3771 0.3315 0.3104 0.1585  -0.0284 -0.0331 30  ARG A NH2 
253  N N   . GLN A 32  ? 0.2112 0.3226 0.3525 0.0190  -0.0223 -0.0465 31  GLN A N   
254  C CA  . GLN A 32  ? 0.2853 0.3018 0.3983 0.0128  0.0234  -0.0246 31  GLN A CA  
255  C C   . GLN A 32  ? 0.2621 0.3042 0.3656 0.0502  -0.0057 -0.0201 31  GLN A C   
256  O O   . GLN A 32  ? 0.4428 0.3592 0.3401 0.0222  0.0146  -0.0134 31  GLN A O   
257  C CB  . GLN A 32  ? 0.3171 0.4324 0.4490 0.0975  0.0268  -0.0616 31  GLN A CB  
258  C CG  . GLN A 32  ? 0.3165 0.4867 0.4133 0.0785  0.0375  -0.0731 31  GLN A CG  
259  C CD  . GLN A 32  ? 0.4634 0.5368 0.5159 0.2323  -0.0633 -0.0306 31  GLN A CD  
260  O OE1 . GLN A 32  ? 0.4812 0.9458 0.7397 0.1805  0.1495  -0.1793 31  GLN A OE1 
261  N NE2 . GLN A 32  ? 0.4743 0.9137 0.6450 0.2994  -0.2182 -0.1586 31  GLN A NE2 
262  N N   . VAL A 33  ? 0.2238 0.3582 0.4223 0.0058  -0.0073 -0.0644 32  VAL A N   
263  C CA  . VAL A 33  ? 0.2883 0.3654 0.4560 -0.0654 -0.0772 -0.0267 32  VAL A CA  
264  C C   . VAL A 33  ? 0.3242 0.3597 0.3584 -0.0294 -0.0639 -0.0481 32  VAL A C   
265  O O   . VAL A 33  ? 0.4272 0.3605 0.4091 -0.0346 -0.0355 -0.0362 32  VAL A O   
266  C CB  . VAL A 33  ? 0.2674 0.4558 0.5290 -0.0356 -0.1358 -0.0847 32  VAL A CB  
267  C CG1 . VAL A 33  ? 0.4817 0.4583 0.6270 -0.0744 -0.1958 -0.0379 32  VAL A CG1 
268  C CG2 . VAL A 33  ? 0.4005 0.3886 0.5656 0.0508  -0.1751 -0.0776 32  VAL A CG2 
269  N N   . ALA A 34  ? 0.2646 0.3108 0.3703 0.0467  -0.0747 -0.0685 33  ALA A N   
270  C CA  . ALA A 34  ? 0.2793 0.2619 0.2938 0.0427  -0.0659 -0.0863 33  ALA A CA  
271  C C   . ALA A 34  ? 0.3879 0.2700 0.2846 0.0226  -0.0359 -0.0582 33  ALA A C   
272  O O   . ALA A 34  ? 0.4071 0.2789 0.3213 0.0646  -0.0699 -0.0764 33  ALA A O   
273  C CB  . ALA A 34  ? 0.3447 0.2834 0.3088 0.0844  -0.0487 -0.0341 33  ALA A CB  
274  N N   A SER A 35  ? 0.3718 0.2665 0.3189 0.0582  -0.0352 -0.0507 34  SER A N   
275  N N   B SER A 35  ? 0.3059 0.3019 0.3063 0.0365  -0.0601 -0.0767 34  SER A N   
276  C CA  A SER A 35  ? 0.3907 0.2193 0.3030 0.0873  -0.0124 -0.0496 34  SER A CA  
277  C CA  B SER A 35  ? 0.3766 0.2777 0.2828 0.0398  -0.0295 -0.0516 34  SER A CA  
278  C C   A SER A 35  ? 0.4074 0.1905 0.3141 0.0864  -0.0110 -0.0440 34  SER A C   
279  C C   B SER A 35  ? 0.4351 0.2499 0.3356 -0.0003 -0.0613 -0.0477 34  SER A C   
280  O O   A SER A 35  ? 0.5614 0.0166 0.3150 0.0739  -0.0378 -0.0165 34  SER A O   
281  O O   B SER A 35  ? 0.4325 0.3451 0.3048 0.0315  -0.0129 -0.0514 34  SER A O   
282  C CB  A SER A 35  ? 0.3791 0.2194 0.2879 0.0825  -0.0142 -0.0444 34  SER A CB  
283  C CB  B SER A 35  ? 0.3742 0.2904 0.2478 -0.0869 -0.0051 -0.0434 34  SER A CB  
284  O OG  A SER A 35  ? 0.3760 0.2340 0.2712 0.1172  0.0119  -0.0816 34  SER A OG  
285  O OG  B SER A 35  ? 0.3047 0.2947 0.2857 0.0295  0.0009  -0.0238 34  SER A OG  
286  N N   . MET A 36  ? 0.3229 0.2919 0.2942 0.1147  0.0230  -0.0390 35  MET A N   
287  C CA  . MET A 36  ? 0.4266 0.3919 0.3800 0.1414  0.1394  -0.0022 35  MET A CA  
288  C C   . MET A 36  ? 0.4083 0.3892 0.4555 0.0278  0.1146  0.0342  35  MET A C   
289  O O   . MET A 36  ? 0.6270 0.6270 0.7128 -0.0947 0.2120  0.1705  35  MET A O   
290  C CB  . MET A 36  ? 0.4294 0.6411 0.5725 0.1470  0.0358  0.1280  35  MET A CB  
291  C CG  . MET A 36  ? 0.4124 0.6247 0.6433 -0.0823 0.1109  0.0506  35  MET A CG  
292  S SD  . MET A 36  ? 0.6120 0.9404 1.2296 0.1532  0.1223  0.2967  35  MET A SD  
293  C CE  . MET A 36  ? 0.4248 0.9212 0.9569 -0.0358 0.3143  0.3320  35  MET A CE  
294  N N   . THR A 37  ? 0.3056 0.2853 0.7203 0.0766  -0.0414 -0.0100 36  THR A N   
295  C CA  . THR A 37  ? 0.4440 0.3072 0.7287 0.1322  -0.0505 -0.0479 36  THR A CA  
296  C C   . THR A 37  ? 0.3839 0.2211 0.5759 0.0324  0.0133  -0.0263 36  THR A C   
297  O O   . THR A 37  ? 0.3367 0.2090 0.4672 0.0534  0.0990  -0.0301 36  THR A O   
298  C CB  . THR A 37  ? 0.5112 0.6293 0.7988 0.0563  -0.0318 -0.1795 36  THR A CB  
299  O OG1 . THR A 37  ? 0.7333 0.9216 0.6996 0.1024  0.1156  -0.2534 36  THR A OG1 
300  C CG2 . THR A 37  ? 0.4765 0.5690 0.8409 0.1424  0.0461  -0.0743 36  THR A CG2 
301  N N   . LYS A 38  ? 0.2860 0.2683 0.6047 -0.0278 0.0923  0.0670  37  LYS A N   
302  C CA  . LYS A 38  ? 0.3156 0.2720 0.4932 0.0600  0.1249  -0.0089 37  LYS A CA  
303  C C   . LYS A 38  ? 0.2521 0.2559 0.4541 -0.0090 0.1266  -0.0050 37  LYS A C   
304  O O   . LYS A 38  ? 0.3339 0.2588 0.5464 -0.0400 0.1382  -0.0118 37  LYS A O   
305  C CB  . LYS A 38  ? 0.3273 0.3257 0.5008 0.0039  0.1995  0.0168  37  LYS A CB  
306  C CG  . LYS A 38  ? 0.3936 0.3703 0.4478 0.0426  0.2074  0.0304  37  LYS A CG  
307  C CD  . LYS A 38  ? 0.4682 0.3715 0.4635 0.1425  0.1981  0.0585  37  LYS A CD  
308  C CE  . LYS A 38  ? 0.5193 0.3242 0.4548 0.0660  0.1839  0.0885  37  LYS A CE  
309  N NZ  . LYS A 38  ? 0.5307 0.2979 0.4874 0.0198  0.1159  0.0040  37  LYS A NZ  
310  N N   . PRO A 39  ? 0.2839 0.2339 0.4164 0.0475  0.1161  0.0144  38  PRO A N   
311  C CA  . PRO A 39  ? 0.2559 0.2358 0.3744 0.0043  0.0732  0.0156  38  PRO A CA  
312  C C   . PRO A 39  ? 0.2919 0.2643 0.2961 0.0012  0.0500  0.0301  38  PRO A C   
313  O O   . PRO A 39  ? 0.2578 0.2327 0.3230 0.0157  0.0427  0.0076  38  PRO A O   
314  C CB  . PRO A 39  ? 0.3662 0.2798 0.3981 0.0227  0.1014  0.0634  38  PRO A CB  
315  C CG  . PRO A 39  ? 0.3865 0.2839 0.4052 -0.0142 0.1246  -0.0007 38  PRO A CG  
316  C CD  . PRO A 39  ? 0.3305 0.2337 0.3965 0.0407  0.0765  0.0120  38  PRO A CD  
317  N N   . THR A 40  ? 0.1861 0.2903 0.3051 -0.0073 0.0509  0.0153  39  THR A N   
318  C CA  . THR A 40  ? 0.2602 0.2721 0.3019 0.0055  0.0582  0.0503  39  THR A CA  
319  C C   . THR A 40  ? 0.2811 0.1974 0.3124 0.0279  0.0568  0.0224  39  THR A C   
320  O O   . THR A 40  ? 0.2836 0.3131 0.3135 0.0378  0.0685  0.0251  39  THR A O   
321  C CB  . THR A 40  ? 0.2863 0.2818 0.3623 -0.0020 0.0827  0.0893  39  THR A CB  
322  O OG1 . THR A 40  ? 0.3211 0.2906 0.4275 -0.0343 0.1356  0.0560  39  THR A OG1 
323  C CG2 . THR A 40  ? 0.2898 0.2651 0.4318 -0.0095 0.0873  0.0450  39  THR A CG2 
324  N N   A THR A 41  ? 0.2844 0.1708 0.3058 0.0337  0.0670  0.0564  40  THR A N   
325  N N   B THR A 41  ? 0.2736 0.2239 0.3019 0.0022  0.0658  0.0404  40  THR A N   
326  C CA  A THR A 41  ? 0.2477 0.1614 0.3488 0.0403  0.0700  0.0333  40  THR A CA  
327  C CA  B THR A 41  ? 0.2111 0.2200 0.3480 0.0135  0.0628  0.0291  40  THR A CA  
328  C C   A THR A 41  ? 0.2535 0.1601 0.3010 0.0278  0.0441  0.0463  40  THR A C   
329  C C   B THR A 41  ? 0.2491 0.2009 0.2920 -0.0047 0.0411  0.0377  40  THR A C   
330  O O   A THR A 41  ? 0.2758 0.1870 0.2945 0.0435  0.0362  0.0286  40  THR A O   
331  O O   B THR A 41  ? 0.2700 0.2040 0.2941 0.0419  0.0364  0.0264  40  THR A O   
332  C CB  A THR A 41  ? 0.2440 0.1124 0.3969 0.0563  0.1134  0.0450  40  THR A CB  
333  C CB  B THR A 41  ? 0.2129 0.3131 0.4148 -0.0463 0.0545  0.0353  40  THR A CB  
334  O OG1 A THR A 41  ? 0.3041 0.1332 0.5142 0.0937  0.1533  0.0908  40  THR A OG1 
335  O OG1 B THR A 41  ? 0.3224 0.5316 0.3963 0.0146  0.0535  -0.0013 40  THR A OG1 
336  C CG2 A THR A 41  ? 0.1629 0.1236 0.3815 0.0129  0.0939  0.0901  40  THR A CG2 
337  C CG2 B THR A 41  ? 0.0649 0.3045 0.4641 -0.0896 0.0544  0.0451  40  THR A CG2 
338  N N   . ILE A 42  ? 0.2424 0.1827 0.2659 0.0263  0.0510  0.0435  41  ILE A N   
339  C CA  . ILE A 42  ? 0.2027 0.1723 0.2973 0.0219  0.0647  0.0409  41  ILE A CA  
340  C C   . ILE A 42  ? 0.1667 0.1710 0.2659 0.0112  0.0185  0.0449  41  ILE A C   
341  O O   . ILE A 42  ? 0.2249 0.2093 0.2989 0.0254  0.0246  0.0650  41  ILE A O   
342  C CB  . ILE A 42  ? 0.2118 0.2254 0.4288 0.0035  0.0564  0.0190  41  ILE A CB  
343  C CG1 . ILE A 42  ? 0.2484 0.2262 0.4239 -0.0243 0.0812  0.0683  41  ILE A CG1 
344  C CG2 . ILE A 42  ? 0.2361 0.2252 0.4832 -0.0004 0.0898  0.0181  41  ILE A CG2 
345  C CD1 . ILE A 42  ? 0.2912 0.3926 0.5373 -0.0920 0.0756  0.0251  41  ILE A CD1 
346  N N   . ILE A 43  ? 0.1749 0.1655 0.2489 0.0219  0.0292  0.0615  42  ILE A N   
347  C CA  . ILE A 43  ? 0.2038 0.1388 0.2625 0.0358  0.0494  0.0443  42  ILE A CA  
348  C C   . ILE A 43  ? 0.2044 0.1302 0.2600 0.0088  0.0366  0.0275  42  ILE A C   
349  O O   . ILE A 43  ? 0.2536 0.1493 0.2701 0.0108  0.0423  0.0610  42  ILE A O   
350  C CB  . ILE A 43  ? 0.2279 0.1248 0.2871 0.0220  0.0362  0.0544  42  ILE A CB  
351  C CG1 . ILE A 43  ? 0.2355 0.1383 0.3303 0.0308  0.0423  0.0569  42  ILE A CG1 
352  C CG2 . ILE A 43  ? 0.2527 0.1867 0.3224 0.0152  0.0468  0.0323  42  ILE A CG2 
353  C CD1 . ILE A 43  ? 0.2682 0.1425 0.3614 0.0124  0.0435  0.0435  42  ILE A CD1 
354  N N   A GLU A 44  ? 0.2370 0.1316 0.2606 0.0143  0.0563  0.0491  43  GLU A N   
355  N N   B GLU A 44  ? 0.2029 0.1404 0.2597 0.0000  0.0533  0.0423  43  GLU A N   
356  C CA  A GLU A 44  ? 0.2489 0.1300 0.2965 0.0190  0.0426  0.0392  43  GLU A CA  
357  C CA  B GLU A 44  ? 0.2159 0.1405 0.2839 0.0083  0.0293  0.0274  43  GLU A CA  
358  C C   A GLU A 44  ? 0.2673 0.1314 0.2667 0.0299  0.0434  0.0490  43  GLU A C   
359  C C   B GLU A 44  ? 0.2570 0.1342 0.2583 0.0277  0.0401  0.0475  43  GLU A C   
360  O O   A GLU A 44  ? 0.2334 0.1405 0.2743 0.0540  0.0543  0.0620  43  GLU A O   
361  O O   B GLU A 44  ? 0.2793 0.1238 0.2552 0.0335  0.0149  0.0492  43  GLU A O   
362  C CB  A GLU A 44  ? 0.2886 0.1099 0.3371 -0.0155 0.0175  0.0544  43  GLU A CB  
363  C CB  B GLU A 44  ? 0.2089 0.1757 0.3336 -0.0023 0.0194  0.0345  43  GLU A CB  
364  C CG  A GLU A 44  ? 0.2940 0.2331 0.4126 0.0032  0.0626  -0.0003 43  GLU A CG  
365  C CG  B GLU A 44  ? 0.2658 0.1503 0.3414 -0.0229 0.0046  0.0477  43  GLU A CG  
366  C CD  A GLU A 44  ? 0.3400 0.2027 0.4893 -0.0018 -0.0241 -0.0159 43  GLU A CD  
367  C CD  B GLU A 44  ? 0.2062 0.2473 0.3940 -0.0215 0.0218  0.0759  43  GLU A CD  
368  O OE1 A GLU A 44  ? 0.2734 0.2008 0.4924 0.0135  -0.0482 -0.0555 43  GLU A OE1 
369  O OE1 B GLU A 44  ? 0.2844 0.3701 0.3447 0.0176  0.0813  0.0187  43  GLU A OE1 
370  O OE2 A GLU A 44  ? 0.3967 0.4017 0.6368 -0.1514 -0.0170 0.0610  43  GLU A OE2 
371  O OE2 B GLU A 44  ? 0.3247 0.2751 0.4385 -0.1082 -0.0642 0.1383  43  GLU A OE2 
372  N N   . LYS A 45  ? 0.2615 0.1182 0.2947 0.0210  0.0733  0.0591  44  LYS A N   
373  C CA  . LYS A 45  ? 0.2532 0.1401 0.3022 0.0463  0.0647  0.0483  44  LYS A CA  
374  C C   . LYS A 45  ? 0.3463 0.1533 0.2829 0.0332  0.0763  0.0393  44  LYS A C   
375  O O   . LYS A 45  ? 0.4030 0.1557 0.3095 -0.0043 0.0762  0.0500  44  LYS A O   
376  C CB  . LYS A 45  ? 0.2942 0.1811 0.3461 0.0110  0.0543  -0.0021 44  LYS A CB  
377  C CG  . LYS A 45  ? 0.3321 0.2551 0.3367 -0.0414 0.0831  -0.0102 44  LYS A CG  
378  C CD  . LYS A 45  ? 0.3257 0.2954 0.3680 0.0184  0.0512  -0.0625 44  LYS A CD  
379  C CE  . LYS A 45  ? 0.4409 0.4470 0.5027 0.0392  0.1566  -0.0010 44  LYS A CE  
380  N NZ  . LYS A 45  ? 0.4326 0.4406 0.5800 0.0724  -0.0310 -0.0160 44  LYS A NZ  
381  N N   . ASN A 46  ? 0.3512 0.1178 0.2688 0.0013  0.0508  0.0323  45  ASN A N   
382  C CA  . ASN A 46  ? 0.3490 0.1391 0.2986 -0.0003 0.0436  -0.0050 45  ASN A CA  
383  C C   . ASN A 46  ? 0.3080 0.1798 0.2692 0.0604  0.0212  0.0065  45  ASN A C   
384  O O   . ASN A 46  ? 0.3975 0.1879 0.2674 0.0394  0.0214  0.0229  45  ASN A O   
385  C CB  . ASN A 46  ? 0.3781 0.1961 0.3645 -0.0450 -0.0132 0.0027  45  ASN A CB  
386  C CG  . ASN A 46  ? 0.4426 0.1956 0.5949 -0.0962 -0.1012 0.0039  45  ASN A CG  
387  O OD1 . ASN A 46  ? 0.6508 0.3251 0.5874 0.0688  -0.1090 -0.0366 45  ASN A OD1 
388  N ND2 . ASN A 46  ? 0.4554 0.4411 0.5357 -0.1294 -0.1323 0.0476  45  ASN A ND2 
389  N N   . GLY A 47  ? 0.3202 0.1562 0.3921 0.0701  0.0684  0.0543  46  GLY A N   
390  C CA  . GLY A 47  ? 0.3410 0.2351 0.4082 0.0810  0.0948  0.0236  46  GLY A CA  
391  C C   . GLY A 47  ? 0.3107 0.2403 0.3590 0.0727  0.0568  0.0391  46  GLY A C   
392  O O   . GLY A 47  ? 0.3399 0.2942 0.3689 0.0421  0.0514  0.0536  46  GLY A O   
393  N N   . ASP A 48  ? 0.3035 0.2142 0.3304 0.0884  0.0555  0.0015  47  ASP A N   
394  C CA  . ASP A 48  ? 0.2712 0.2100 0.3693 0.0715  0.0408  0.0258  47  ASP A CA  
395  C C   . ASP A 48  ? 0.2100 0.1997 0.2859 0.0357  0.0339  0.0351  47  ASP A C   
396  O O   . ASP A 48  ? 0.2279 0.1998 0.3238 0.0203  0.0460  0.0500  47  ASP A O   
397  C CB  . ASP A 48  ? 0.3268 0.2409 0.4117 0.0638  0.0915  0.0705  47  ASP A CB  
398  C CG  . ASP A 48  ? 0.3461 0.3770 0.4630 0.1409  0.0721  -0.0484 47  ASP A CG  
399  O OD1 . ASP A 48  ? 0.3486 0.3603 0.4179 0.0508  0.1145  0.0085  47  ASP A OD1 
400  O OD2 . ASP A 48  ? 0.3753 0.4943 0.4996 0.0972  0.1034  -0.0213 47  ASP A OD2 
401  N N   A ILE A 49  ? 0.2278 0.1547 0.2865 0.0302  0.0477  0.0353  48  ILE A N   
402  N N   B ILE A 49  ? 0.2288 0.1378 0.2753 0.0252  0.0475  0.0318  48  ILE A N   
403  C CA  A ILE A 49  ? 0.2475 0.1516 0.2704 0.0372  0.0424  0.0372  48  ILE A CA  
404  C CA  B ILE A 49  ? 0.2313 0.1238 0.2421 0.0167  0.0383  0.0249  48  ILE A CA  
405  C C   A ILE A 49  ? 0.1623 0.1394 0.2632 -0.0034 0.0394  0.0477  48  ILE A C   
406  C C   B ILE A 49  ? 0.1666 0.1457 0.2501 -0.0090 0.0445  0.0362  48  ILE A C   
407  O O   A ILE A 49  ? 0.1908 0.1213 0.2994 -0.0144 0.0322  0.0460  48  ILE A O   
408  O O   B ILE A 49  ? 0.2161 0.1314 0.2604 -0.0171 0.0373  0.0323  48  ILE A O   
409  C CB  A ILE A 49  ? 0.2709 0.1847 0.3043 0.0196  0.0232  0.0264  48  ILE A CB  
410  C CB  B ILE A 49  ? 0.2221 0.0886 0.2643 -0.0166 0.0411  0.0229  48  ILE A CB  
411  C CG1 A ILE A 49  ? 0.2749 0.2702 0.3272 0.0875  0.0527  0.0577  48  ILE A CG1 
412  C CG1 B ILE A 49  ? 0.2475 0.1163 0.2609 -0.0342 0.0453  0.0425  48  ILE A CG1 
413  C CG2 A ILE A 49  ? 0.2754 0.2133 0.3093 0.0334  0.0002  0.0112  48  ILE A CG2 
414  C CG2 B ILE A 49  ? 0.2351 0.1342 0.2705 0.0082  0.0324  0.0190  48  ILE A CG2 
415  C CD1 A ILE A 49  ? 0.3268 0.2541 0.4291 0.0686  0.0809  0.0621  48  ILE A CD1 
416  C CD1 B ILE A 49  ? 0.3135 0.1391 0.2918 -0.0119 -0.0081 0.0204  48  ILE A CD1 
417  N N   . LEU A 50  ? 0.2032 0.1370 0.2618 -0.0024 0.0384  0.0528  49  LEU A N   
418  C CA  . LEU A 50  ? 0.2012 0.1397 0.2595 -0.0120 0.0398  0.0540  49  LEU A CA  
419  C C   . LEU A 50  ? 0.2096 0.1316 0.2497 -0.0008 0.0241  0.0332  49  LEU A C   
420  O O   . LEU A 50  ? 0.1763 0.1568 0.2709 0.0237  0.0133  0.0393  49  LEU A O   
421  C CB  . LEU A 50  ? 0.2042 0.1250 0.2842 0.0216  0.0285  0.0161  49  LEU A CB  
422  C CG  . LEU A 50  ? 0.2513 0.1625 0.3825 0.0169  -0.0394 0.0302  49  LEU A CG  
423  C CD1 . LEU A 50  ? 0.2829 0.4376 0.4003 -0.0169 0.0337  0.0538  49  LEU A CD1 
424  C CD2 . LEU A 50  ? 0.4487 0.2281 0.4553 0.0650  -0.1288 -0.0391 49  LEU A CD2 
425  N N   . THR A 51  ? 0.1905 0.1376 0.2566 0.0235  0.0303  0.0533  50  THR A N   
426  C CA  . THR A 51  ? 0.1714 0.1580 0.2622 0.0007  0.0202  0.0412  50  THR A CA  
427  C C   . THR A 51  ? 0.1944 0.1744 0.2691 0.0371  0.0140  0.0575  50  THR A C   
428  O O   . THR A 51  ? 0.2301 0.1743 0.2857 0.0572  0.0382  0.0609  50  THR A O   
429  C CB  . THR A 51  ? 0.1567 0.2083 0.3076 -0.0248 0.0327  0.0143  50  THR A CB  
430  O OG1 . THR A 51  ? 0.2452 0.1879 0.3353 -0.0338 0.0482  0.0012  50  THR A OG1 
431  C CG2 . THR A 51  ? 0.1499 0.2901 0.3717 -0.0241 0.0510  -0.0044 50  THR A CG2 
432  N N   . LEU A 52  ? 0.1971 0.1515 0.2305 0.0213  0.0203  0.0551  51  LEU A N   
433  C CA  . LEU A 52  ? 0.2374 0.1712 0.2326 0.0129  0.0410  0.0444  51  LEU A CA  
434  C C   . LEU A 52  ? 0.2665 0.2010 0.2135 0.0377  0.0446  0.0092  51  LEU A C   
435  O O   . LEU A 52  ? 0.1969 0.2283 0.2561 0.0438  0.0257  0.0475  51  LEU A O   
436  C CB  . LEU A 52  ? 0.2931 0.1887 0.3094 -0.0105 0.0284  0.0316  51  LEU A CB  
437  C CG  . LEU A 52  ? 0.4057 0.1549 0.3830 -0.0661 0.0628  0.0310  51  LEU A CG  
438  C CD1 . LEU A 52  ? 0.4103 0.2670 0.4430 -0.0427 0.0157  -0.0019 51  LEU A CD1 
439  C CD2 . LEU A 52  ? 0.4764 0.3401 0.2940 0.0447  -0.0367 -0.0066 51  LEU A CD2 
440  N N   . LYS A 53  ? 0.2171 0.2336 0.2323 0.0578  0.0342  0.0637  52  LYS A N   
441  C CA  . LYS A 53  ? 0.2018 0.2776 0.2834 0.0563  0.0447  0.0464  52  LYS A CA  
442  C C   . LYS A 53  ? 0.2360 0.2744 0.2905 0.0737  0.0533  0.0741  52  LYS A C   
443  O O   . LYS A 53  ? 0.2994 0.3282 0.3041 0.1517  0.0436  0.0719  52  LYS A O   
444  C CB  . LYS A 53  ? 0.2008 0.3342 0.3715 0.0174  0.0828  0.0447  52  LYS A CB  
445  C CG  . LYS A 53  ? 0.2662 0.3338 0.4144 0.0313  0.0935  0.0244  52  LYS A CG  
446  C CD  . LYS A 53  ? 0.3750 0.3388 0.4567 -0.0525 0.1145  0.0145  52  LYS A CD  
447  C CE  . LYS A 53  ? 0.4506 0.3557 0.5510 -0.0295 0.1140  -0.0055 52  LYS A CE  
448  N NZ  . LYS A 53  ? 0.4407 0.3456 0.7196 -0.1528 0.1286  -0.0617 52  LYS A NZ  
449  N N   . THR A 54  ? 0.2359 0.2709 0.2706 0.0750  0.0562  0.0732  53  THR A N   
450  C CA  . THR A 54  ? 0.1960 0.2656 0.3113 0.0205  0.0798  0.0409  53  THR A CA  
451  C C   . THR A 54  ? 0.2239 0.2468 0.3329 -0.0018 0.0513  0.0234  53  THR A C   
452  O O   . THR A 54  ? 0.1697 0.3419 0.3590 0.0253  0.0444  -0.0008 53  THR A O   
453  C CB  . THR A 54  ? 0.2144 0.2645 0.3095 0.0045  0.0361  0.0652  53  THR A CB  
454  O OG1 . THR A 54  ? 0.2058 0.3745 0.4905 -0.0073 -0.0226 0.0677  53  THR A OG1 
455  C CG2 . THR A 54  ? 0.3719 0.2295 0.3888 0.0377  0.0756  0.0546  53  THR A CG2 
456  N N   . HIS A 55  ? 0.2567 0.2511 0.3046 -0.0218 0.0462  0.0232  54  HIS A N   
457  C CA  . HIS A 55  ? 0.2577 0.3295 0.3958 -0.0464 0.0753  -0.0443 54  HIS A CA  
458  C C   . HIS A 55  ? 0.1978 0.3528 0.4205 -0.0290 0.0258  -0.0613 54  HIS A C   
459  O O   . HIS A 55  ? 0.1969 0.4207 0.3840 0.0259  0.0363  -0.0572 54  HIS A O   
460  C CB  . HIS A 55  ? 0.3046 0.3291 0.5399 -0.1201 0.1029  -0.0068 54  HIS A CB  
461  C CG  . HIS A 55  ? 0.3835 0.3642 0.5737 -0.0169 0.0160  -0.0437 54  HIS A CG  
462  N ND1 . HIS A 55  ? 0.3351 0.3490 0.6946 0.0167  0.0141  -0.0532 54  HIS A ND1 
463  C CD2 . HIS A 55  ? 0.3060 0.3929 0.6034 0.1298  0.0241  -0.0779 54  HIS A CD2 
464  C CE1 . HIS A 55  ? 0.5404 0.2794 0.7349 0.1021  0.0268  -0.0218 54  HIS A CE1 
465  N NE2 . HIS A 55  ? 0.3718 0.3686 0.5703 0.1035  -0.0565 -0.0943 54  HIS A NE2 
466  N N   . SER A 56  ? 0.3141 0.5390 0.4465 0.1396  0.0299  -0.0876 55  SER A N   
467  C CA  . SER A 56  ? 0.3991 0.6295 0.5652 0.2053  -0.0420 -0.2023 55  SER A CA  
468  C C   . SER A 56  ? 0.3995 0.8326 0.5293 0.2763  -0.0428 -0.1945 55  SER A C   
469  O O   . SER A 56  ? 0.3572 1.0139 0.6602 0.2432  -0.0683 -0.3629 55  SER A O   
470  C CB  . SER A 56  ? 0.5873 0.6105 0.5753 0.1378  -0.1116 -0.2073 55  SER A CB  
471  O OG  . SER A 56  ? 0.6922 0.6594 0.6190 0.2133  -0.1482 -0.1144 55  SER A OG  
472  N N   . THR A 57  ? 0.6522 0.8788 0.5425 0.3439  0.0725  -0.2140 56  THR A N   
473  C CA  . THR A 57  ? 0.4183 0.9609 0.7547 0.2290  0.1948  -0.0735 56  THR A CA  
474  C C   . THR A 57  ? 0.1038 0.9776 0.8103 0.0487  0.0983  -0.0263 56  THR A C   
475  O O   . THR A 57  ? 0.3454 1.0472 0.7360 0.1970  0.0275  0.0413  56  THR A O   
476  C CB  . THR A 57  ? 0.4674 0.8255 0.8518 0.3713  0.1745  -0.1011 56  THR A CB  
477  O OG1 . THR A 57  ? 0.4802 1.0061 0.7579 0.3888  0.0578  -0.0747 56  THR A OG1 
478  C CG2 . THR A 57  ? 0.3504 1.0830 0.9784 0.3588  0.3163  -0.1488 56  THR A CG2 
479  N N   . PHE A 58  ? 0.1005 0.7714 0.6708 0.1262  -0.0265 0.0265  57  PHE A N   
480  C CA  . PHE A 58  ? 0.1697 0.4433 0.5592 0.0900  0.0119  -0.1662 57  PHE A CA  
481  C C   . PHE A 58  ? 0.1137 0.5970 0.4882 0.1076  0.1280  -0.1082 57  PHE A C   
482  O O   . PHE A 58  ? 0.4760 0.4124 0.3922 0.1602  0.0326  -0.0916 57  PHE A O   
483  C CB  . PHE A 58  ? 0.2185 0.4817 0.6472 0.0826  -0.0405 -0.1861 57  PHE A CB  
484  C CG  . PHE A 58  ? 0.2780 0.3193 0.6900 0.0020  -0.0362 -0.2532 57  PHE A CG  
485  C CD1 . PHE A 58  ? 0.3491 0.3935 0.8669 0.0429  -0.0196 -0.1405 57  PHE A CD1 
486  C CD2 . PHE A 58  ? 0.3030 0.5291 0.7438 -0.0047 0.0512  -0.1786 57  PHE A CD2 
487  C CE1 . PHE A 58  ? 0.3810 0.3204 0.8869 0.2106  0.0493  -0.1262 57  PHE A CE1 
488  C CE2 . PHE A 58  ? 0.4389 0.4921 0.7145 0.1878  0.2369  -0.1920 57  PHE A CE2 
489  C CZ  . PHE A 58  ? 0.4033 0.5192 0.8399 0.1946  0.1919  -0.1762 57  PHE A CZ  
490  N N   . LYS A 59  ? 0.3939 0.5352 0.5374 0.2587  0.0109  -0.0818 58  LYS A N   
491  C CA  . LYS A 59  ? 0.4790 0.4274 0.5728 0.1584  0.0029  -0.1577 58  LYS A CA  
492  C C   . LYS A 59  ? 0.5382 0.4561 0.6409 0.1595  -0.1114 -0.1504 58  LYS A C   
493  O O   . LYS A 59  ? 0.8512 0.5468 0.5914 0.3428  -0.1756 -0.2407 58  LYS A O   
494  C CB  . LYS A 59  ? 0.5105 0.3980 0.6475 0.1148  -0.1454 -0.0708 58  LYS A CB  
495  C CG  . LYS A 59  ? 0.6471 0.5930 0.6571 0.0747  0.0136  -0.1250 58  LYS A CG  
496  C CD  . LYS A 59  ? 0.7062 0.5025 0.6566 -0.0128 0.0162  0.0341  58  LYS A CD  
497  C CE  . LYS A 59  ? 0.8358 0.5642 0.6785 -0.1065 0.0987  0.0234  58  LYS A CE  
498  N NZ  . LYS A 59  ? 0.8105 0.4176 0.8934 -0.1322 -0.0269 -0.0077 58  LYS A NZ  
499  N N   . ASN A 60  ? 0.1802 0.3731 0.5540 0.0355  -0.0120 -0.0440 59  ASN A N   
500  C CA  . ASN A 60  ? 0.2109 0.3371 0.4138 0.0105  -0.0474 -0.0238 59  ASN A CA  
501  C C   . ASN A 60  ? 0.2054 0.3518 0.4244 0.0731  -0.0280 -0.0168 59  ASN A C   
502  O O   . ASN A 60  ? 0.1875 0.5022 0.4206 0.0691  -0.0283 -0.0423 59  ASN A O   
503  C CB  . ASN A 60  ? 0.2249 0.4598 0.5280 -0.1305 -0.0348 0.0022  59  ASN A CB  
504  C CG  . ASN A 60  ? 0.3133 0.6567 0.4704 -0.1285 0.0038  -0.0309 59  ASN A CG  
505  O OD1 . ASN A 60  ? 0.2614 0.4423 0.4885 -0.0966 0.0510  -0.0374 59  ASN A OD1 
506  N ND2 . ASN A 60  ? 0.3267 0.7452 0.6966 -0.1032 -0.0593 -0.0170 59  ASN A ND2 
507  N N   . THR A 61  ? 0.1873 0.2671 0.3364 0.0149  -0.0037 -0.0320 60  THR A N   
508  C CA  . THR A 61  ? 0.1678 0.2496 0.3393 0.0371  -0.0055 0.0050  60  THR A CA  
509  C C   . THR A 61  ? 0.1935 0.2163 0.3157 0.0140  -0.0072 0.0230  60  THR A C   
510  O O   . THR A 61  ? 0.1845 0.2543 0.3036 0.0111  0.0296  0.0185  60  THR A O   
511  C CB  . THR A 61  ? 0.2233 0.2593 0.3222 0.0241  0.0136  0.0092  60  THR A CB  
512  O OG1 . THR A 61  ? 0.2516 0.2650 0.3129 -0.0040 0.0034  -0.0159 60  THR A OG1 
513  C CG2 . THR A 61  ? 0.3007 0.2343 0.4264 0.0428  0.0019  -0.0207 60  THR A CG2 
514  N N   . GLU A 62  ? 0.1893 0.2715 0.3183 0.0053  0.0076  0.0113  61  GLU A N   
515  C CA  . GLU A 62  ? 0.2338 0.2811 0.3002 0.0190  0.0109  0.0087  61  GLU A CA  
516  C C   . GLU A 62  ? 0.1985 0.2934 0.2783 0.0956  0.0005  0.0202  61  GLU A C   
517  O O   . GLU A 62  ? 0.2493 0.3098 0.2938 0.0990  -0.0283 0.0330  61  GLU A O   
518  C CB  . GLU A 62  ? 0.3110 0.2375 0.4079 0.0229  0.0582  -0.0073 61  GLU A CB  
519  C CG  . GLU A 62  ? 0.3414 0.3241 0.4471 0.0539  0.0646  -0.0282 61  GLU A CG  
520  C CD  . GLU A 62  ? 0.3431 0.3279 0.6095 0.0288  0.0731  -0.0331 61  GLU A CD  
521  O OE1 . GLU A 62  ? 0.4436 0.4051 0.6098 -0.0561 0.0920  0.0159  61  GLU A OE1 
522  O OE2 . GLU A 62  ? 0.4125 0.3713 0.7682 -0.0806 0.1553  -0.1529 61  GLU A OE2 
523  N N   . ILE A 63  ? 0.1845 0.2305 0.2526 0.0479  0.0166  0.0432  62  ILE A N   
524  C CA  . ILE A 63  ? 0.2273 0.1852 0.2440 0.0393  0.0308  0.0418  62  ILE A CA  
525  C C   . ILE A 63  ? 0.1730 0.1831 0.2434 0.0127  0.0147  0.0231  62  ILE A C   
526  O O   . ILE A 63  ? 0.1960 0.1470 0.2644 0.0159  0.0264  0.0290  62  ILE A O   
527  C CB  . ILE A 63  ? 0.2660 0.1632 0.2627 0.0322  0.0429  0.0473  62  ILE A CB  
528  C CG1 . ILE A 63  ? 0.2042 0.1654 0.2771 0.0002  0.0407  0.0410  62  ILE A CG1 
529  C CG2 . ILE A 63  ? 0.3655 0.1922 0.2841 0.0575  -0.0325 0.0419  62  ILE A CG2 
530  C CD1 . ILE A 63  ? 0.2716 0.1675 0.2825 -0.0189 0.0641  0.0169  62  ILE A CD1 
531  N N   . SER A 64  ? 0.1941 0.1508 0.2150 -0.0160 0.0205  0.0379  63  SER A N   
532  C CA  . SER A 64  ? 0.1707 0.1415 0.2534 -0.0212 -0.0004 0.0161  63  SER A CA  
533  C C   . SER A 64  ? 0.1627 0.1617 0.2362 0.0004  -0.0048 0.0114  63  SER A C   
534  O O   . SER A 64  ? 0.1536 0.1985 0.2676 -0.0013 -0.0041 0.0327  63  SER A O   
535  C CB  . SER A 64  ? 0.1799 0.1998 0.3160 -0.0669 0.0209  -0.0314 63  SER A CB  
536  O OG  . SER A 64  ? 0.2126 0.1852 0.4056 -0.0536 0.0435  -0.0154 63  SER A OG  
537  N N   . PHE A 65  ? 0.1483 0.1071 0.2526 -0.0076 0.0067  0.0342  64  PHE A N   
538  C CA  . PHE A 65  ? 0.1409 0.1327 0.2382 -0.0188 0.0027  0.0478  64  PHE A CA  
539  C C   . PHE A 65  ? 0.1606 0.1146 0.2541 -0.0029 0.0181  0.0290  64  PHE A C   
540  O O   . PHE A 65  ? 0.1521 0.1483 0.2740 0.0055  0.0182  0.0536  64  PHE A O   
541  C CB  . PHE A 65  ? 0.1673 0.1371 0.2601 -0.0152 0.0320  0.0424  64  PHE A CB  
542  C CG  . PHE A 65  ? 0.1633 0.1260 0.2602 -0.0148 0.0202  0.0463  64  PHE A CG  
543  C CD1 . PHE A 65  ? 0.1661 0.1143 0.2600 0.0068  0.0245  0.0163  64  PHE A CD1 
544  C CD2 . PHE A 65  ? 0.1816 0.1487 0.2516 -0.0186 0.0378  0.0365  64  PHE A CD2 
545  C CE1 . PHE A 65  ? 0.2057 0.1198 0.2598 0.0420  -0.0016 0.0229  64  PHE A CE1 
546  C CE2 . PHE A 65  ? 0.2518 0.1715 0.2464 -0.0163 0.0279  0.0487  64  PHE A CE2 
547  C CZ  . PHE A 65  ? 0.2363 0.1572 0.2202 0.0095  0.0310  -0.0094 64  PHE A CZ  
548  N N   . LYS A 66  ? 0.1589 0.1296 0.2049 -0.0280 0.0095  0.0376  65  LYS A N   
549  C CA  . LYS A 66  ? 0.1601 0.1147 0.2168 -0.0115 0.0124  0.0296  65  LYS A CA  
550  C C   . LYS A 66  ? 0.1210 0.1217 0.1962 0.0037  0.0166  0.0229  65  LYS A C   
551  O O   . LYS A 66  ? 0.1248 0.1185 0.1931 0.0065  -0.0032 0.0222  65  LYS A O   
552  C CB  . LYS A 66  ? 0.1660 0.1437 0.2212 -0.0127 0.0192  0.0011  65  LYS A CB  
553  C CG  . LYS A 66  ? 0.1823 0.1669 0.2833 -0.0172 -0.0146 0.0006  65  LYS A CG  
554  C CD  . LYS A 66  ? 0.2510 0.2357 0.3062 -0.0312 0.0124  -0.0549 65  LYS A CD  
555  C CE  . LYS A 66  ? 0.4340 0.2628 0.4162 -0.0622 -0.0034 -0.1074 65  LYS A CE  
556  N NZ  . LYS A 66  ? 0.6169 0.4035 0.4438 -0.0506 0.0541  -0.1803 65  LYS A NZ  
557  N N   . LEU A 67  ? 0.1422 0.1262 0.1932 -0.0008 0.0056  0.0365  66  LEU A N   
558  C CA  . LEU A 67  ? 0.1132 0.1436 0.2009 0.0125  -0.0007 0.0118  66  LEU A CA  
559  C C   . LEU A 67  ? 0.1116 0.1256 0.1866 0.0204  0.0002  0.0061  66  LEU A C   
560  O O   . LEU A 67  ? 0.1433 0.1210 0.1941 0.0089  0.0178  -0.0096 66  LEU A O   
561  C CB  . LEU A 67  ? 0.1284 0.2028 0.2326 0.0103  -0.0099 0.0592  66  LEU A CB  
562  C CG  . LEU A 67  ? 0.1732 0.2383 0.2423 0.0254  0.0155  0.0300  66  LEU A CG  
563  C CD1 . LEU A 67  ? 0.2766 0.2515 0.2439 0.0465  -0.0326 0.0249  66  LEU A CD1 
564  C CD2 . LEU A 67  ? 0.2443 0.2501 0.1975 0.0579  0.0353  0.0179  66  LEU A CD2 
565  N N   . GLY A 68  ? 0.1101 0.1140 0.1713 0.0155  0.0011  0.0052  67  GLY A N   
566  C CA  . GLY A 68  ? 0.1310 0.1152 0.1679 0.0103  0.0148  0.0055  67  GLY A CA  
567  C C   . GLY A 68  ? 0.1053 0.1026 0.1732 -0.0162 0.0071  -0.0004 67  GLY A C   
568  O O   . GLY A 68  ? 0.1284 0.1893 0.1620 -0.0466 0.0068  0.0000  67  GLY A O   
569  N N   . VAL A 69  ? 0.0896 0.1192 0.1620 0.0089  -0.0007 0.0065  68  VAL A N   
570  C CA  . VAL A 69  ? 0.0858 0.1202 0.1731 -0.0016 0.0005  -0.0005 68  VAL A CA  
571  C C   . VAL A 69  ? 0.0997 0.1113 0.1584 0.0073  0.0107  0.0014  68  VAL A C   
572  O O   . VAL A 69  ? 0.0934 0.1381 0.1657 0.0000  0.0123  -0.0022 68  VAL A O   
573  C CB  . VAL A 69  ? 0.1389 0.1097 0.1869 -0.0003 0.0006  0.0035  68  VAL A CB  
574  C CG1 . VAL A 69  ? 0.1570 0.1124 0.2070 0.0009  -0.0223 -0.0295 68  VAL A CG1 
575  C CG2 . VAL A 69  ? 0.1526 0.1260 0.2048 0.0149  0.0043  -0.0106 68  VAL A CG2 
576  N N   . GLU A 70  ? 0.0908 0.1235 0.1686 -0.0005 0.0181  0.0141  69  GLU A N   
577  C CA  . GLU A 70  ? 0.0889 0.1488 0.1628 0.0156  -0.0011 -0.0041 69  GLU A CA  
578  C C   . GLU A 70  ? 0.0903 0.1517 0.1662 0.0167  -0.0076 0.0012  69  GLU A C   
579  O O   . GLU A 70  ? 0.1008 0.1685 0.1984 0.0161  0.0055  -0.0187 69  GLU A O   
580  C CB  . GLU A 70  ? 0.1258 0.1485 0.1888 0.0233  0.0132  0.0117  69  GLU A CB  
581  C CG  . GLU A 70  ? 0.1232 0.1624 0.2081 0.0315  0.0105  0.0029  69  GLU A CG  
582  C CD  . GLU A 70  ? 0.2252 0.1843 0.3223 0.0355  0.0526  0.0665  69  GLU A CD  
583  O OE1 . GLU A 70  ? 0.2864 0.2521 0.2863 0.0432  0.0486  0.0733  69  GLU A OE1 
584  O OE2 . GLU A 70  ? 0.2872 0.2488 0.5864 0.1173  0.0803  0.0639  69  GLU A OE2 
585  N N   . PHE A 71  ? 0.1112 0.1417 0.1904 0.0146  0.0076  -0.0162 70  PHE A N   
586  C CA  . PHE A 71  ? 0.1133 0.1221 0.1994 0.0120  0.0050  -0.0138 70  PHE A CA  
587  C C   . PHE A 71  ? 0.1059 0.1446 0.1898 0.0167  -0.0044 -0.0079 70  PHE A C   
588  O O   . PHE A 71  ? 0.1375 0.1342 0.2583 0.0249  -0.0395 -0.0266 70  PHE A O   
589  C CB  . PHE A 71  ? 0.1043 0.1286 0.2109 0.0133  -0.0129 -0.0111 70  PHE A CB  
590  C CG  . PHE A 71  ? 0.1101 0.1308 0.1983 0.0125  -0.0050 0.0244  70  PHE A CG  
591  C CD1 . PHE A 71  ? 0.0916 0.1306 0.2192 0.0021  -0.0046 0.0226  70  PHE A CD1 
592  C CD2 . PHE A 71  ? 0.1036 0.1597 0.2440 0.0052  -0.0009 0.0152  70  PHE A CD2 
593  C CE1 . PHE A 71  ? 0.1134 0.1363 0.1992 -0.0021 -0.0097 0.0287  70  PHE A CE1 
594  C CE2 . PHE A 71  ? 0.1248 0.1548 0.2325 0.0234  0.0074  0.0426  70  PHE A CE2 
595  C CZ  . PHE A 71  ? 0.1424 0.1356 0.2059 0.0193  0.0110  0.0278  70  PHE A CZ  
596  N N   . ASP A 72  ? 0.1440 0.1553 0.1843 0.0179  -0.0187 -0.0178 71  ASP A N   
597  C CA  . ASP A 72  ? 0.1467 0.1771 0.2047 0.0380  -0.0149 -0.0072 71  ASP A CA  
598  C C   . ASP A 72  ? 0.1142 0.1689 0.2093 0.0313  -0.0277 -0.0083 71  ASP A C   
599  O O   . ASP A 72  ? 0.1535 0.1690 0.2399 0.0118  -0.0206 0.0030  71  ASP A O   
600  C CB  . ASP A 72  ? 0.1890 0.2026 0.2107 0.0433  -0.0384 -0.0046 71  ASP A CB  
601  C CG  . ASP A 72  ? 0.2746 0.2670 0.2155 0.0183  -0.0234 0.0078  71  ASP A CG  
602  O OD1 . ASP A 72  ? 0.4958 0.2969 0.2754 -0.0897 0.0464  -0.0015 71  ASP A OD1 
603  O OD2 . ASP A 72  ? 0.4410 0.3926 0.2546 -0.0218 0.0298  -0.0572 71  ASP A OD2 
604  N N   . GLU A 73  ? 0.1428 0.1540 0.1973 0.0298  -0.0163 0.0029  72  GLU A N   
605  C CA  . GLU A 73  ? 0.1480 0.1604 0.1967 0.0062  -0.0106 0.0133  72  GLU A CA  
606  C C   . GLU A 73  ? 0.1278 0.1976 0.1720 0.0094  -0.0181 0.0140  72  GLU A C   
607  O O   . GLU A 73  ? 0.1165 0.1982 0.2224 0.0332  0.0021  0.0429  72  GLU A O   
608  C CB  . GLU A 73  ? 0.1375 0.1449 0.1852 0.0265  -0.0171 0.0248  72  GLU A CB  
609  C CG  . GLU A 73  ? 0.1514 0.1528 0.1895 0.0101  -0.0100 0.0292  72  GLU A CG  
610  C CD  . GLU A 73  ? 0.1414 0.1487 0.2021 0.0247  -0.0160 0.0274  72  GLU A CD  
611  O OE1 . GLU A 73  ? 0.1651 0.2170 0.2085 -0.0341 -0.0366 0.0242  72  GLU A OE1 
612  O OE2 . GLU A 73  ? 0.1908 0.1742 0.1991 -0.0069 -0.0084 0.0072  72  GLU A OE2 
613  N N   . THR A 74  ? 0.1109 0.1604 0.2202 0.0189  -0.0163 0.0040  73  THR A N   
614  C CA  . THR A 74  ? 0.0923 0.1889 0.2083 0.0239  -0.0120 0.0190  73  THR A CA  
615  C C   . THR A 74  ? 0.1147 0.1986 0.2056 0.0419  -0.0205 0.0092  73  THR A C   
616  O O   . THR A 74  ? 0.1445 0.1892 0.2509 0.0043  0.0033  0.0040  73  THR A O   
617  C CB  . THR A 74  ? 0.1384 0.2109 0.2342 0.0176  -0.0461 0.0156  73  THR A CB  
618  O OG1 . THR A 74  ? 0.1430 0.2736 0.2522 0.0488  -0.0021 -0.0200 73  THR A OG1 
619  C CG2 . THR A 74  ? 0.1468 0.3035 0.3257 0.0692  -0.0693 0.0314  73  THR A CG2 
620  N N   . THR A 75  ? 0.1289 0.1874 0.2140 0.0087  -0.0185 0.0159  74  THR A N   
621  C CA  . THR A 75  ? 0.1434 0.1877 0.2111 0.0077  0.0122  0.0246  74  THR A CA  
622  C C   . THR A 75  ? 0.1562 0.2028 0.2132 0.0276  0.0091  0.0188  74  THR A C   
623  O O   . THR A 75  ? 0.1541 0.2522 0.2268 0.0328  0.0036  0.0052  74  THR A O   
624  C CB  . THR A 75  ? 0.1442 0.1724 0.1867 0.0391  -0.0129 0.0150  74  THR A CB  
625  O OG1 . THR A 75  ? 0.1286 0.1925 0.2096 0.0309  -0.0176 0.0347  74  THR A OG1 
626  C CG2 . THR A 75  ? 0.1496 0.1642 0.2110 0.0134  -0.0031 0.0196  74  THR A CG2 
627  N N   . ALA A 76  ? 0.1388 0.2418 0.2061 -0.0010 0.0055  0.0270  75  ALA A N   
628  C CA  . ALA A 76  ? 0.1403 0.2319 0.2595 -0.0020 0.0262  0.0168  75  ALA A CA  
629  C C   . ALA A 76  ? 0.1328 0.2400 0.2480 0.0158  -0.0014 0.0082  75  ALA A C   
630  O O   . ALA A 76  ? 0.1251 0.3236 0.3180 0.0291  -0.0041 0.0347  75  ALA A O   
631  C CB  . ALA A 76  ? 0.1893 0.2419 0.2528 -0.0019 0.0096  0.0123  75  ALA A CB  
632  N N   . ASP A 77  ? 0.1278 0.2438 0.2580 0.0198  0.0163  0.0066  76  ASP A N   
633  C CA  . ASP A 77  ? 0.1539 0.2621 0.2560 0.0664  0.0047  0.0047  76  ASP A CA  
634  C C   . ASP A 77  ? 0.1528 0.2827 0.2575 0.0358  0.0184  0.0184  76  ASP A C   
635  O O   . ASP A 77  ? 0.1858 0.2750 0.2860 0.0666  0.0098  0.0300  76  ASP A O   
636  C CB  . ASP A 77  ? 0.1895 0.2238 0.2467 0.0825  0.0110  0.0092  76  ASP A CB  
637  C CG  . ASP A 77  ? 0.1888 0.2334 0.2221 0.0776  0.0022  0.0117  76  ASP A CG  
638  O OD1 . ASP A 77  ? 0.1681 0.1978 0.2456 0.0504  -0.0020 0.0030  76  ASP A OD1 
639  O OD2 . ASP A 77  ? 0.2140 0.2204 0.2769 0.0983  0.0242  0.0321  76  ASP A OD2 
640  N N   A ASP A 78  ? 0.1621 0.2931 0.2454 0.0373  -0.0036 0.0126  77  ASP A N   
641  N N   B ASP A 78  ? 0.0878 0.2743 0.2641 0.0283  0.0018  0.0199  77  ASP A N   
642  C CA  A ASP A 78  ? 0.1122 0.2909 0.2501 0.0535  -0.0212 -0.0211 77  ASP A CA  
643  C CA  B ASP A 78  ? 0.1040 0.2529 0.2630 0.0406  -0.0247 0.0291  77  ASP A CA  
644  C C   A ASP A 78  ? 0.1774 0.2395 0.2370 0.0422  -0.0298 0.0356  77  ASP A C   
645  C C   B ASP A 78  ? 0.1396 0.2513 0.2443 0.0472  -0.0002 0.0513  77  ASP A C   
646  O O   A ASP A 78  ? 0.1516 0.4165 0.2589 0.0480  -0.0221 0.0820  77  ASP A O   
647  O O   B ASP A 78  ? 0.1487 0.3878 0.2625 0.0476  0.0169  0.1107  77  ASP A O   
648  C CB  A ASP A 78  ? 0.1398 0.3645 0.3361 0.1163  -0.0257 0.0084  77  ASP A CB  
649  C CB  B ASP A 78  ? 0.1190 0.2713 0.2957 0.0371  -0.0484 0.0423  77  ASP A CB  
650  C CG  A ASP A 78  ? 0.3251 0.5384 0.3478 0.1586  -0.0305 -0.0119 77  ASP A CG  
651  C CG  B ASP A 78  ? 0.1927 0.3090 0.3471 -0.0120 -0.0576 0.0891  77  ASP A CG  
652  O OD1 A ASP A 78  ? 0.3628 0.6629 0.4702 0.2537  -0.1311 -0.1083 77  ASP A OD1 
653  O OD1 B ASP A 78  ? 0.2729 0.3004 0.3662 -0.0583 -0.1450 0.0508  77  ASP A OD1 
654  O OD2 A ASP A 78  ? 0.4401 0.6888 0.5050 0.2376  -0.1091 0.0501  77  ASP A OD2 
655  O OD2 B ASP A 78  ? 0.1651 0.4079 0.4996 -0.0517 0.0226  0.1111  77  ASP A OD2 
656  N N   . ARG A 79  ? 0.1599 0.2327 0.1960 0.0517  -0.0020 0.0205  78  ARG A N   
657  C CA  . ARG A 79  ? 0.1662 0.1921 0.1987 0.0596  -0.0003 0.0339  78  ARG A CA  
658  C C   . ARG A 79  ? 0.1578 0.1846 0.1683 0.0286  -0.0110 0.0158  78  ARG A C   
659  O O   . ARG A 79  ? 0.1614 0.1781 0.1945 0.0437  -0.0054 0.0284  78  ARG A O   
660  C CB  . ARG A 79  ? 0.2037 0.1839 0.1948 0.0546  -0.0149 0.0052  78  ARG A CB  
661  C CG  . ARG A 79  ? 0.1901 0.1720 0.2517 0.0562  0.0021  0.0139  78  ARG A CG  
662  C CD  . ARG A 79  ? 0.1794 0.1400 0.2372 0.0532  -0.0057 0.0143  78  ARG A CD  
663  N NE  . ARG A 79  ? 0.1481 0.1499 0.2343 0.0405  0.0017  0.0169  78  ARG A NE  
664  C CZ  . ARG A 79  ? 0.1434 0.1727 0.2071 0.0219  -0.0083 0.0220  78  ARG A CZ  
665  N NH1 . ARG A 79  ? 0.1484 0.1846 0.2278 0.0136  -0.0148 0.0315  78  ARG A NH1 
666  N NH2 . ARG A 79  ? 0.1849 0.1932 0.2093 0.0254  0.0005  0.0213  78  ARG A NH2 
667  N N   . LYS A 80  ? 0.1588 0.1794 0.1753 0.0479  -0.0233 0.0391  79  LYS A N   
668  C CA  . LYS A 80  ? 0.1419 0.1791 0.1951 0.0434  -0.0059 0.0262  79  LYS A CA  
669  C C   . LYS A 80  ? 0.1490 0.1765 0.1802 0.0341  -0.0054 0.0195  79  LYS A C   
670  O O   . LYS A 80  ? 0.1809 0.1783 0.2275 0.0297  -0.0254 0.0315  79  LYS A O   
671  C CB  . LYS A 80  ? 0.1779 0.1931 0.1984 0.0437  -0.0133 0.0041  79  LYS A CB  
672  C CG  . LYS A 80  ? 0.1986 0.3025 0.2774 -0.0113 -0.0342 0.0441  79  LYS A CG  
673  C CD  . LYS A 80  ? 0.3059 0.3576 0.2685 -0.0676 -0.0357 0.0146  79  LYS A CD  
674  C CE  . LYS A 80  ? 0.3572 0.3864 0.6065 -0.1480 -0.0343 -0.0369 79  LYS A CE  
675  N NZ  . LYS A 80  ? 0.5611 0.5545 0.5714 -0.1685 0.0442  -0.0668 79  LYS A NZ  
676  N N   . VAL A 81  ? 0.1343 0.1627 0.1941 0.0237  -0.0046 0.0337  80  VAL A N   
677  C CA  . VAL A 81  ? 0.1450 0.1547 0.1949 0.0180  0.0101  0.0085  80  VAL A CA  
678  C C   . VAL A 81  ? 0.1622 0.1696 0.1722 0.0367  -0.0031 0.0088  80  VAL A C   
679  O O   . VAL A 81  ? 0.1194 0.1723 0.2057 0.0194  -0.0079 0.0213  80  VAL A O   
680  C CB  . VAL A 81  ? 0.1134 0.1535 0.1932 0.0248  0.0025  0.0128  80  VAL A CB  
681  C CG1 . VAL A 81  ? 0.1442 0.1647 0.2190 0.0603  0.0000  0.0276  80  VAL A CG1 
682  C CG2 . VAL A 81  ? 0.1357 0.1365 0.1965 0.0342  -0.0012 0.0141  80  VAL A CG2 
683  N N   . LYS A 82  ? 0.1476 0.1518 0.1921 0.0463  -0.0170 0.0370  81  LYS A N   
684  C CA  . LYS A 82  ? 0.1304 0.1427 0.1880 0.0340  -0.0019 0.0357  81  LYS A CA  
685  C C   . LYS A 82  ? 0.1479 0.1479 0.1765 0.0440  0.0012  0.0034  81  LYS A C   
686  O O   . LYS A 82  ? 0.1443 0.1399 0.1917 0.0212  -0.0050 0.0166  81  LYS A O   
687  C CB  . LYS A 82  ? 0.1541 0.1850 0.2184 0.0343  0.0201  0.0554  81  LYS A CB  
688  C CG  . LYS A 82  ? 0.2149 0.2175 0.1922 0.0542  0.0451  0.0525  81  LYS A CG  
689  C CD  . LYS A 82  ? 0.3043 0.2414 0.2265 0.0113  0.0149  0.0187  81  LYS A CD  
690  C CE  . LYS A 82  ? 0.4476 0.2623 0.2265 0.0085  -0.0007 0.0146  81  LYS A CE  
691  N NZ  . LYS A 82  ? 0.4066 0.3102 0.2259 -0.0057 0.0090  0.0035  81  LYS A NZ  
692  N N   . SER A 83  ? 0.1341 0.1280 0.1875 0.0173  -0.0104 0.0009  82  SER A N   
693  C CA  . SER A 83  ? 0.1035 0.1371 0.1799 0.0109  -0.0124 0.0019  82  SER A CA  
694  C C   . SER A 83  ? 0.1143 0.1224 0.1561 -0.0018 -0.0089 0.0093  82  SER A C   
695  O O   . SER A 83  ? 0.1318 0.1334 0.1701 0.0135  -0.0065 -0.0012 82  SER A O   
696  C CB  . SER A 83  ? 0.1145 0.1526 0.1859 0.0149  0.0086  0.0010  82  SER A CB  
697  O OG  . SER A 83  ? 0.1286 0.1772 0.2887 0.0227  0.0173  -0.0583 82  SER A OG  
698  N N   A ILE A 84  ? 0.1261 0.1104 0.1531 0.0238  -0.0177 -0.0117 83  ILE A N   
699  N N   B ILE A 84  ? 0.0787 0.1121 0.1489 0.0229  0.0028  0.0085  83  ILE A N   
700  C CA  A ILE A 84  ? 0.1154 0.1182 0.1616 0.0360  0.0093  -0.0034 83  ILE A CA  
701  C CA  B ILE A 84  ? 0.0587 0.1132 0.1375 0.0177  0.0112  0.0058  83  ILE A CA  
702  C C   A ILE A 84  ? 0.1180 0.1142 0.1670 0.0184  0.0025  0.0029  83  ILE A C   
703  C C   B ILE A 84  ? 0.0808 0.1129 0.1392 0.0199  0.0068  0.0041  83  ILE A C   
704  O O   A ILE A 84  ? 0.1757 0.1142 0.1677 0.0259  -0.0093 -0.0088 83  ILE A O   
705  O O   B ILE A 84  ? 0.0783 0.1073 0.1497 0.0219  -0.0005 0.0018  83  ILE A O   
706  C CB  A ILE A 84  ? 0.1238 0.1701 0.1958 0.0355  0.0134  0.0139  83  ILE A CB  
707  C CB  B ILE A 84  ? 0.0523 0.1145 0.1071 0.0300  0.0100  0.0121  83  ILE A CB  
708  C CG1 A ILE A 84  ? 0.1620 0.1838 0.2296 0.0592  0.0302  0.0440  83  ILE A CG1 
709  C CG1 B ILE A 84  ? 0.0275 0.1159 0.1016 0.0316  0.0110  0.0102  83  ILE A CG1 
710  C CG2 A ILE A 84  ? 0.1555 0.2145 0.2202 -0.0026 0.0256  0.0172  83  ILE A CG2 
711  C CG2 B ILE A 84  ? 0.0363 0.1203 0.1207 0.0279  0.0181  0.0094  83  ILE A CG2 
712  C CD1 A ILE A 84  ? 0.2050 0.2197 0.2353 0.0463  0.0356  0.0021  83  ILE A CD1 
713  C CD1 B ILE A 84  ? 0.0251 0.1209 0.1038 0.0354  0.0121  0.0175  83  ILE A CD1 
714  N N   . VAL A 85  ? 0.1192 0.1067 0.1666 0.0284  0.0064  -0.0020 84  VAL A N   
715  C CA  . VAL A 85  ? 0.1245 0.1309 0.1623 -0.0019 0.0046  0.0031  84  VAL A CA  
716  C C   . VAL A 85  ? 0.1374 0.1306 0.1483 0.0091  0.0183  0.0014  84  VAL A C   
717  O O   . VAL A 85  ? 0.1458 0.1241 0.1699 0.0274  0.0144  -0.0006 84  VAL A O   
718  C CB  . VAL A 85  ? 0.1125 0.1227 0.1655 0.0098  -0.0039 -0.0072 84  VAL A CB  
719  C CG1 . VAL A 85  ? 0.1283 0.1751 0.1768 0.0281  0.0015  0.0204  84  VAL A CG1 
720  C CG2 . VAL A 85  ? 0.1144 0.1487 0.1831 0.0191  -0.0053 0.0135  84  VAL A CG2 
721  N N   . THR A 86  ? 0.1260 0.1414 0.1476 0.0559  -0.0034 -0.0196 85  THR A N   
722  C CA  . THR A 86  ? 0.1110 0.1541 0.1442 0.0447  0.0098  -0.0055 85  THR A CA  
723  C C   . THR A 86  ? 0.1176 0.1706 0.1424 0.0395  -0.0030 -0.0034 85  THR A C   
724  O O   . THR A 86  ? 0.1413 0.1730 0.1615 0.0442  0.0176  -0.0045 85  THR A O   
725  C CB  . THR A 86  ? 0.1433 0.1720 0.1750 0.0270  0.0196  0.0023  85  THR A CB  
726  O OG1 . THR A 86  ? 0.1942 0.1704 0.1933 0.0300  0.0132  -0.0191 85  THR A OG1 
727  C CG2 . THR A 86  ? 0.1770 0.1660 0.1755 0.0203  0.0054  -0.0107 85  THR A CG2 
728  N N   A LEU A 87  ? 0.1034 0.1785 0.1663 0.0255  -0.0134 -0.0046 86  LEU A N   
729  N N   B LEU A 87  ? 0.0580 0.1540 0.1446 -0.0007 0.0039  -0.0128 86  LEU A N   
730  C CA  A LEU A 87  ? 0.1105 0.1776 0.1665 0.0427  -0.0079 -0.0017 86  LEU A CA  
731  C CA  B LEU A 87  ? 0.0074 0.1332 0.1512 0.0024  -0.0064 -0.0114 86  LEU A CA  
732  C C   A LEU A 87  ? 0.1058 0.1750 0.1775 0.0293  0.0075  -0.0011 86  LEU A C   
733  C C   B LEU A 87  ? 0.0063 0.1559 0.1680 0.0012  0.0027  -0.0174 86  LEU A C   
734  O O   A LEU A 87  ? 0.1091 0.2157 0.2034 0.0141  0.0129  -0.0284 86  LEU A O   
735  O O   B LEU A 87  ? 0.0071 0.1642 0.1851 0.0104  0.0023  -0.0242 86  LEU A O   
736  C CB  A LEU A 87  ? 0.1772 0.1773 0.2080 0.0635  0.0298  -0.0036 86  LEU A CB  
737  C CB  B LEU A 87  ? 0.0084 0.1267 0.1242 -0.0074 -0.0133 -0.0106 86  LEU A CB  
738  C CG  A LEU A 87  ? 0.2193 0.2371 0.2358 0.0354  0.0201  0.0198  86  LEU A CG  
739  C CG  B LEU A 87  ? 0.0132 0.1066 0.1060 -0.0059 -0.0248 -0.0084 86  LEU A CG  
740  C CD1 A LEU A 87  ? 0.2778 0.2353 0.2264 0.0619  0.0662  0.0422  86  LEU A CD1 
741  C CD1 B LEU A 87  ? 0.0146 0.1033 0.0994 -0.0093 -0.0253 -0.0080 86  LEU A CD1 
742  C CD2 A LEU A 87  ? 0.3291 0.2616 0.3011 0.0784  0.0238  0.0634  86  LEU A CD2 
743  C CD2 B LEU A 87  ? 0.0132 0.1088 0.1072 -0.0042 -0.0256 -0.0083 86  LEU A CD2 
744  N N   A ASP A 88  ? 0.1652 0.1966 0.1979 0.0281  0.0140  -0.0259 87  ASP A N   
745  N N   B ASP A 88  ? 0.0075 0.1748 0.1875 0.0081  0.0105  -0.0336 87  ASP A N   
746  C CA  A ASP A 88  ? 0.1556 0.2377 0.2083 0.0023  0.0058  -0.0238 87  ASP A CA  
747  C CA  B ASP A 88  ? 0.0263 0.1905 0.2088 -0.0136 0.0135  -0.0352 87  ASP A CA  
748  C C   A ASP A 88  ? 0.1657 0.2288 0.2155 0.0038  -0.0233 -0.0011 87  ASP A C   
749  C C   B ASP A 88  ? 0.0729 0.2291 0.2110 -0.0157 0.0094  -0.0218 87  ASP A C   
750  O O   A ASP A 88  ? 0.2484 0.2786 0.1894 0.0034  -0.0041 -0.0313 87  ASP A O   
751  O O   B ASP A 88  ? 0.0707 0.2592 0.2596 -0.0019 0.0039  -0.0553 87  ASP A O   
752  C CB  A ASP A 88  ? 0.2081 0.2375 0.2915 -0.0046 0.0172  0.0245  87  ASP A CB  
753  C CB  B ASP A 88  ? 0.0108 0.1837 0.2097 -0.0105 0.0297  -0.0389 87  ASP A CB  
754  C CG  A ASP A 88  ? 0.4161 0.3636 0.3013 0.0914  -0.0155 0.0075  87  ASP A CG  
755  C CG  B ASP A 88  ? 0.0455 0.1930 0.2409 -0.0352 0.0325  -0.0591 87  ASP A CG  
756  O OD1 A ASP A 88  ? 0.6593 0.3167 0.3386 0.1041  -0.0318 0.0098  87  ASP A OD1 
757  O OD1 B ASP A 88  ? 0.0992 0.1583 0.2239 -0.0047 0.0224  -0.0820 87  ASP A OD1 
758  O OD2 A ASP A 88  ? 0.4104 0.3375 0.4065 0.0768  0.0838  0.0391  87  ASP A OD2 
759  O OD2 B ASP A 88  ? 0.1491 0.1795 0.2991 -0.0277 0.0388  -0.0623 87  ASP A OD2 
760  N N   . GLY A 89  ? 0.1458 0.2710 0.2179 0.0206  -0.0111 0.0005  88  GLY A N   
761  C CA  . GLY A 89  ? 0.1074 0.3972 0.2358 0.0069  -0.0177 0.0320  88  GLY A CA  
762  C C   . GLY A 89  ? 0.1365 0.3458 0.2109 -0.0042 -0.0213 0.0517  88  GLY A C   
763  O O   . GLY A 89  ? 0.2407 0.3074 0.3017 -0.0063 0.0041  0.0143  88  GLY A O   
764  N N   . GLY A 90  ? 0.1963 0.4355 0.2650 0.0776  0.0201  0.0548  89  GLY A N   
765  C CA  . GLY A 90  ? 0.2027 0.4774 0.2933 0.0090  -0.0343 0.1020  89  GLY A CA  
766  C C   . GLY A 90  ? 0.1666 0.4068 0.2070 0.0160  0.0067  0.0488  89  GLY A C   
767  O O   . GLY A 90  ? 0.1907 0.4864 0.2748 -0.0336 0.0061  0.0644  89  GLY A O   
768  N N   . LYS A 91  ? 0.1229 0.3628 0.1694 0.0072  0.0129  0.0026  90  LYS A N   
769  C CA  . LYS A 91  ? 0.1216 0.3801 0.1818 0.0214  -0.0220 -0.0378 90  LYS A CA  
770  C C   . LYS A 91  ? 0.1433 0.2616 0.1580 0.0420  0.0104  -0.0054 90  LYS A C   
771  O O   . LYS A 91  ? 0.1372 0.3142 0.1791 0.0489  0.0086  -0.0376 90  LYS A O   
772  C CB  . LYS A 91  ? 0.1215 0.3477 0.2701 0.0589  -0.0304 -0.0674 90  LYS A CB  
773  C CG  . LYS A 91  ? 0.2495 0.4540 0.3303 -0.0076 -0.0017 -0.1356 90  LYS A CG  
774  C CD  . LYS A 91  ? 0.3690 0.4524 0.4714 -0.0464 -0.0123 -0.1585 90  LYS A CD  
775  C CE  . LYS A 91  ? 0.5522 0.4946 0.5283 -0.0467 0.1035  -0.2343 90  LYS A CE  
776  N NZ  . LYS A 91  ? 0.4609 0.5054 0.9546 -0.0464 0.1771  -0.1462 90  LYS A NZ  
777  N N   . LEU A 92  ? 0.1382 0.2497 0.1636 0.0553  0.0035  -0.0078 91  LEU A N   
778  C CA  . LEU A 92  ? 0.1273 0.1912 0.1835 0.0445  0.0047  -0.0037 91  LEU A CA  
779  C C   . LEU A 92  ? 0.0960 0.1712 0.1623 0.0273  0.0090  0.0007  91  LEU A C   
780  O O   . LEU A 92  ? 0.1214 0.1574 0.1774 0.0286  0.0211  -0.0125 91  LEU A O   
781  C CB  . LEU A 92  ? 0.1527 0.1812 0.2131 0.0554  0.0363  0.0181  91  LEU A CB  
782  C CG  . LEU A 92  ? 0.1599 0.1735 0.1932 0.0441  0.0040  0.0361  91  LEU A CG  
783  C CD1 . LEU A 92  ? 0.2307 0.1752 0.1954 0.0382  0.0329  0.0064  91  LEU A CD1 
784  C CD2 . LEU A 92  ? 0.1901 0.2481 0.2375 0.0149  0.0455  -0.0083 91  LEU A CD2 
785  N N   . VAL A 93  ? 0.1274 0.1454 0.1593 0.0452  0.0166  -0.0142 92  VAL A N   
786  C CA  . VAL A 93  ? 0.1557 0.1385 0.1564 0.0442  0.0087  -0.0164 92  VAL A CA  
787  C C   . VAL A 93  ? 0.1048 0.1623 0.1655 0.0290  0.0081  0.0025  92  VAL A C   
788  O O   . VAL A 93  ? 0.1389 0.2000 0.1783 0.0584  0.0005  -0.0198 92  VAL A O   
789  C CB  . VAL A 93  ? 0.1839 0.1644 0.1864 0.0139  0.0180  -0.0236 92  VAL A CB  
790  C CG1 . VAL A 93  ? 0.1784 0.1590 0.2296 -0.0031 0.0177  -0.0137 92  VAL A CG1 
791  C CG2 . VAL A 93  ? 0.1677 0.1861 0.2305 0.0253  -0.0108 -0.0443 92  VAL A CG2 
792  N N   . HIS A 94  ? 0.1247 0.1228 0.1629 0.0418  0.0056  -0.0023 93  HIS A N   
793  C CA  . HIS A 94  ? 0.1590 0.1090 0.1652 0.0382  0.0024  0.0016  93  HIS A CA  
794  C C   . HIS A 94  ? 0.1536 0.1130 0.1484 0.0359  0.0114  0.0034  93  HIS A C   
795  O O   . HIS A 94  ? 0.1659 0.1255 0.1671 0.0452  0.0219  0.0055  93  HIS A O   
796  C CB  . HIS A 94  ? 0.1776 0.1072 0.1540 0.0059  -0.0099 0.0145  93  HIS A CB  
797  C CG  . HIS A 94  ? 0.1406 0.1284 0.1719 0.0204  -0.0123 0.0025  93  HIS A CG  
798  N ND1 . HIS A 94  ? 0.1304 0.1392 0.2316 0.0300  -0.0407 0.0046  93  HIS A ND1 
799  C CD2 . HIS A 94  ? 0.1630 0.1475 0.1726 0.0602  -0.0125 -0.0043 93  HIS A CD2 
800  C CE1 . HIS A 94  ? 0.1749 0.1344 0.2191 0.0370  -0.0333 -0.0135 93  HIS A CE1 
801  N NE2 . HIS A 94  ? 0.1832 0.1535 0.2053 0.0710  -0.0325 -0.0063 93  HIS A NE2 
802  N N   . LEU A 95  ? 0.1439 0.1284 0.1500 0.0370  -0.0033 0.0083  94  LEU A N   
803  C CA  . LEU A 95  ? 0.1468 0.1296 0.1680 0.0379  0.0159  0.0055  94  LEU A CA  
804  C C   . LEU A 95  ? 0.1687 0.1229 0.1645 0.0382  0.0101  0.0137  94  LEU A C   
805  O O   . LEU A 95  ? 0.2010 0.1424 0.1611 0.0576  -0.0092 -0.0042 94  LEU A O   
806  C CB  . LEU A 95  ? 0.1513 0.1585 0.1981 0.0302  0.0292  -0.0037 94  LEU A CB  
807  C CG  . LEU A 95  ? 0.1816 0.1753 0.2397 0.0307  0.0421  0.0292  94  LEU A CG  
808  C CD1 . LEU A 95  ? 0.2148 0.1597 0.2764 0.0033  0.0482  0.0369  94  LEU A CD1 
809  C CD2 . LEU A 95  ? 0.1898 0.2145 0.2916 0.0468  0.0600  0.0555  94  LEU A CD2 
810  N N   . GLN A 96  ? 0.1628 0.1038 0.1633 0.0256  -0.0008 0.0051  95  GLN A N   
811  C CA  . GLN A 96  ? 0.1485 0.1399 0.1627 0.0235  0.0027  0.0195  95  GLN A CA  
812  C C   . GLN A 96  ? 0.1537 0.1391 0.1672 0.0267  -0.0055 0.0177  95  GLN A C   
813  O O   . GLN A 96  ? 0.2005 0.1427 0.1893 0.0094  0.0095  0.0148  95  GLN A O   
814  C CB  . GLN A 96  ? 0.1438 0.1289 0.1897 0.0175  0.0063  0.0091  95  GLN A CB  
815  C CG  . GLN A 96  ? 0.1365 0.1312 0.1920 0.0151  -0.0035 0.0184  95  GLN A CG  
816  C CD  . GLN A 96  ? 0.1258 0.1238 0.1949 0.0108  -0.0067 0.0185  95  GLN A CD  
817  O OE1 . GLN A 96  ? 0.1466 0.1350 0.2419 0.0287  0.0006  0.0122  95  GLN A OE1 
818  N NE2 . GLN A 96  ? 0.1649 0.1331 0.2018 -0.0074 -0.0163 0.0305  95  GLN A NE2 
819  N N   . LYS A 97  ? 0.1652 0.1381 0.1590 0.0330  0.0023  0.0187  96  LYS A N   
820  C CA  . LYS A 97  ? 0.1755 0.1461 0.1829 0.0189  -0.0063 0.0310  96  LYS A CA  
821  C C   . LYS A 97  ? 0.1728 0.1284 0.1918 0.0131  -0.0059 0.0411  96  LYS A C   
822  O O   . LYS A 97  ? 0.1751 0.1437 0.1916 0.0246  0.0014  0.0277  96  LYS A O   
823  C CB  . LYS A 97  ? 0.1894 0.1908 0.2256 0.0319  0.0294  0.0846  96  LYS A CB  
824  C CG  . LYS A 97  ? 0.2096 0.2767 0.2494 0.0692  0.0123  0.0650  96  LYS A CG  
825  C CD  . LYS A 97  ? 0.1687 0.4874 0.4144 0.0574  0.0312  0.1247  96  LYS A CD  
826  C CE  . LYS A 97  ? 0.4816 0.5338 0.5576 0.0237  0.0858  0.0580  96  LYS A CE  
827  N NZ  . LYS A 97  ? 0.3365 0.9392 0.5024 0.0159  0.1388  0.0203  96  LYS A NZ  
828  N N   . TRP A 98  ? 0.1867 0.1250 0.2040 0.0225  -0.0122 0.0347  97  TRP A N   
829  C CA  . TRP A 98  ? 0.1735 0.1418 0.2085 0.0294  -0.0115 0.0311  97  TRP A CA  
830  C C   . TRP A 98  ? 0.1684 0.1570 0.2160 0.0328  -0.0072 0.0514  97  TRP A C   
831  O O   . TRP A 98  ? 0.2115 0.1495 0.2167 0.0162  -0.0172 0.0394  97  TRP A O   
832  C CB  . TRP A 98  ? 0.1600 0.1623 0.2099 0.0227  -0.0124 0.0346  97  TRP A CB  
833  C CG  . TRP A 98  ? 0.1650 0.1618 0.2123 0.0223  -0.0163 0.0238  97  TRP A CG  
834  C CD1 . TRP A 98  ? 0.1758 0.2014 0.1990 0.0410  -0.0412 0.0391  97  TRP A CD1 
835  C CD2 . TRP A 98  ? 0.1637 0.1710 0.2047 0.0395  0.0035  0.0339  97  TRP A CD2 
836  N NE1 . TRP A 98  ? 0.2040 0.1861 0.2363 0.0493  -0.0129 0.0343  97  TRP A NE1 
837  C CE2 . TRP A 98  ? 0.1924 0.1613 0.2148 0.0329  0.0037  0.0344  97  TRP A CE2 
838  C CE3 . TRP A 98  ? 0.1383 0.1726 0.2187 0.0199  0.0122  0.0444  97  TRP A CE3 
839  C CZ2 . TRP A 98  ? 0.1817 0.1528 0.2203 0.0151  0.0059  0.0190  97  TRP A CZ2 
840  C CZ3 . TRP A 98  ? 0.1587 0.1802 0.2127 0.0089  -0.0034 0.0496  97  TRP A CZ3 
841  C CH2 . TRP A 98  ? 0.2207 0.1824 0.1978 0.0148  -0.0004 0.0236  97  TRP A CH2 
842  N N   . ASP A 99  ? 0.2154 0.1750 0.1931 0.0611  -0.0205 0.0211  98  ASP A N   
843  C CA  . ASP A 99  ? 0.2238 0.1697 0.2052 0.0463  -0.0146 0.0330  98  ASP A CA  
844  C C   . ASP A 99  ? 0.2046 0.1742 0.2165 0.0577  -0.0364 0.0775  98  ASP A C   
845  O O   . ASP A 99  ? 0.2350 0.1655 0.3530 0.0253  -0.0236 0.0493  98  ASP A O   
846  C CB  . ASP A 99  ? 0.2323 0.1804 0.2158 0.0586  -0.0189 0.0435  98  ASP A CB  
847  C CG  . ASP A 99  ? 0.1959 0.2412 0.1555 0.0777  -0.0304 0.0168  98  ASP A CG  
848  O OD1 . ASP A 99  ? 0.1953 0.2359 0.2106 0.0643  -0.0080 0.0149  98  ASP A OD1 
849  O OD2 . ASP A 99  ? 0.1965 0.1911 0.2107 0.0698  -0.0452 0.0084  98  ASP A OD2 
850  N N   . GLY A 100 ? 0.1850 0.1839 0.2502 0.0445  -0.0294 0.0803  99  GLY A N   
851  C CA  . GLY A 100 ? 0.2070 0.2280 0.2618 -0.0020 -0.0254 0.0868  99  GLY A CA  
852  C C   . GLY A 100 ? 0.1896 0.1962 0.2575 -0.0106 -0.0042 0.0422  99  GLY A C   
853  O O   . GLY A 100 ? 0.2386 0.2370 0.3296 -0.0495 -0.0544 0.0583  99  GLY A O   
854  N N   . GLN A 101 ? 0.1819 0.1648 0.2376 0.0126  -0.0087 0.0540  100 GLN A N   
855  C CA  . GLN A 101 ? 0.1979 0.1638 0.2456 0.0016  -0.0096 0.0459  100 GLN A CA  
856  C C   . GLN A 101 ? 0.2090 0.1587 0.2067 -0.0315 0.0238  0.0406  100 GLN A C   
857  O O   . GLN A 101 ? 0.2067 0.1647 0.2025 0.0071  -0.0085 0.0405  100 GLN A O   
858  C CB  . GLN A 101 ? 0.2576 0.2174 0.2705 0.0196  0.0139  0.0278  100 GLN A CB  
859  C CG  . GLN A 101 ? 0.2702 0.2243 0.3009 -0.0037 0.0075  -0.0445 100 GLN A CG  
860  C CD  . GLN A 101 ? 0.1984 0.2086 0.2686 0.0043  -0.0652 -0.0294 100 GLN A CD  
861  O OE1 . GLN A 101 ? 0.2807 0.3214 0.3748 0.0387  -0.1318 0.0472  100 GLN A OE1 
862  N NE2 . GLN A 101 ? 0.2407 0.2021 0.2422 0.0074  -0.0485 0.0184  100 GLN A NE2 
863  N N   . GLU A 102 ? 0.2005 0.1204 0.2170 -0.0043 0.0426  0.0303  101 GLU A N   
864  C CA  . GLU A 102 ? 0.1918 0.1340 0.2274 0.0034  0.0462  0.0496  101 GLU A CA  
865  C C   . GLU A 102 ? 0.1973 0.1126 0.1950 -0.0001 0.0177  0.0121  101 GLU A C   
866  O O   . GLU A 102 ? 0.2333 0.1240 0.2455 0.0054  0.0293  -0.0015 101 GLU A O   
867  C CB  . GLU A 102 ? 0.1702 0.1857 0.2635 -0.0078 0.0744  0.0402  101 GLU A CB  
868  C CG  . GLU A 102 ? 0.1941 0.2351 0.3359 0.0241  0.0155  0.0387  101 GLU A CG  
869  C CD  . GLU A 102 ? 0.2037 0.2839 0.4431 0.0550  0.0570  0.0426  101 GLU A CD  
870  O OE1 . GLU A 102 ? 0.2213 0.3910 0.5266 0.0053  0.1650  0.0459  101 GLU A OE1 
871  O OE2 . GLU A 102 ? 0.3652 0.3629 0.4881 0.0214  -0.0751 -0.0024 101 GLU A OE2 
872  N N   . THR A 103 ? 0.1942 0.0974 0.2122 0.0176  0.0128  0.0102  102 THR A N   
873  C CA  . THR A 103 ? 0.1490 0.1098 0.2030 0.0131  0.0049  -0.0075 102 THR A CA  
874  C C   . THR A 103 ? 0.1060 0.1528 0.1868 0.0338  0.0176  -0.0024 102 THR A C   
875  O O   . THR A 103 ? 0.1594 0.1345 0.1881 0.0333  0.0129  0.0045  102 THR A O   
876  C CB  . THR A 103 ? 0.1456 0.1507 0.1936 0.0114  -0.0053 0.0044  102 THR A CB  
877  O OG1 . THR A 103 ? 0.1539 0.1711 0.1939 0.0117  0.0224  -0.0084 102 THR A OG1 
878  C CG2 . THR A 103 ? 0.1508 0.1313 0.2133 0.0146  0.0067  -0.0101 102 THR A CG2 
879  N N   . THR A 104 ? 0.1680 0.1332 0.1657 0.0286  0.0202  -0.0006 103 THR A N   
880  C CA  . THR A 104 ? 0.2097 0.1434 0.1619 0.0414  0.0115  0.0050  103 THR A CA  
881  C C   . THR A 104 ? 0.2354 0.1177 0.1501 0.0246  0.0106  -0.0057 103 THR A C   
882  O O   . THR A 104 ? 0.2689 0.1319 0.1919 0.0419  0.0365  -0.0147 103 THR A O   
883  C CB  . THR A 104 ? 0.1977 0.2067 0.2282 0.0383  0.0167  -0.0112 103 THR A CB  
884  O OG1 . THR A 104 ? 0.2023 0.2372 0.2430 0.0274  0.0038  -0.0116 103 THR A OG1 
885  C CG2 . THR A 104 ? 0.2113 0.3519 0.2130 0.0216  0.0158  -0.0195 103 THR A CG2 
886  N N   . LEU A 105 ? 0.1826 0.1065 0.1853 0.0518  0.0283  -0.0025 104 LEU A N   
887  C CA  . LEU A 105 ? 0.1688 0.1553 0.1716 0.0488  0.0225  0.0173  104 LEU A CA  
888  C C   . LEU A 105 ? 0.2004 0.1588 0.1653 0.0741  0.0362  0.0053  104 LEU A C   
889  O O   . LEU A 105 ? 0.2213 0.1369 0.1731 0.0754  0.0343  -0.0021 104 LEU A O   
890  C CB  . LEU A 105 ? 0.1845 0.1669 0.1969 0.0274  0.0077  0.0197  104 LEU A CB  
891  C CG  . LEU A 105 ? 0.1396 0.2324 0.2565 0.0636  0.0070  -0.0078 104 LEU A CG  
892  C CD1 . LEU A 105 ? 0.2261 0.3352 0.2546 0.0508  -0.0328 0.0549  104 LEU A CD1 
893  C CD2 . LEU A 105 ? 0.2498 0.2941 0.2746 -0.0559 0.0057  0.0324  104 LEU A CD2 
894  N N   . VAL A 106 ? 0.1917 0.1382 0.1637 0.0617  0.0253  -0.0002 105 VAL A N   
895  C CA  . VAL A 106 ? 0.1930 0.1416 0.1661 0.0657  0.0296  0.0055  105 VAL A CA  
896  C C   . VAL A 106 ? 0.1599 0.1408 0.1558 0.0455  0.0059  -0.0024 105 VAL A C   
897  O O   . VAL A 106 ? 0.1971 0.1472 0.1702 0.0425  0.0367  0.0101  105 VAL A O   
898  C CB  . VAL A 106 ? 0.2032 0.1387 0.2431 0.0505  0.0580  0.0023  105 VAL A CB  
899  C CG1 . VAL A 106 ? 0.1929 0.1850 0.2901 0.0070  0.0067  0.0119  105 VAL A CG1 
900  C CG2 . VAL A 106 ? 0.1929 0.1707 0.2736 0.0391  0.0649  0.0174  105 VAL A CG2 
901  N N   . ARG A 107 ? 0.1410 0.1416 0.1804 0.0517  0.0248  0.0099  106 ARG A N   
902  C CA  . ARG A 107 ? 0.1469 0.1374 0.1747 0.0512  0.0273  0.0065  106 ARG A CA  
903  C C   . ARG A 107 ? 0.1587 0.1688 0.1663 0.0358  0.0233  0.0262  106 ARG A C   
904  O O   . ARG A 107 ? 0.1631 0.1729 0.1751 0.0483  0.0152  0.0062  106 ARG A O   
905  C CB  . ARG A 107 ? 0.1253 0.1531 0.1902 0.0399  0.0092  0.0202  106 ARG A CB  
906  C CG  . ARG A 107 ? 0.1029 0.1735 0.1915 0.0285  0.0172  0.0158  106 ARG A CG  
907  C CD  . ARG A 107 ? 0.1719 0.1669 0.2070 0.0187  -0.0204 0.0287  106 ARG A CD  
908  N NE  . ARG A 107 ? 0.1473 0.2148 0.2110 0.0074  0.0151  0.0182  106 ARG A NE  
909  C CZ  . ARG A 107 ? 0.1480 0.1825 0.2017 0.0158  -0.0111 0.0020  106 ARG A CZ  
910  N NH1 . ARG A 107 ? 0.1550 0.1775 0.2011 0.0540  -0.0166 0.0132  106 ARG A NH1 
911  N NH2 . ARG A 107 ? 0.1446 0.2270 0.2242 0.0223  0.0067  0.0137  106 ARG A NH2 
912  N N   . GLU A 108 ? 0.1643 0.2009 0.1731 0.0732  0.0354  0.0382  107 GLU A N   
913  C CA  . GLU A 108 ? 0.1614 0.2263 0.1804 0.0969  0.0331  0.0492  107 GLU A CA  
914  C C   . GLU A 108 ? 0.1932 0.2308 0.1601 0.0700  0.0267  0.0195  107 GLU A C   
915  O O   . GLU A 108 ? 0.2268 0.2717 0.1967 0.1205  0.0589  0.0527  107 GLU A O   
916  C CB  . GLU A 108 ? 0.2538 0.2920 0.2746 0.0467  -0.0400 0.0193  107 GLU A CB  
917  C CG  . GLU A 108 ? 0.3093 0.3438 0.3594 0.0440  -0.0896 0.0019  107 GLU A CG  
918  C CD  . GLU A 108 ? 0.2043 0.3955 0.4278 0.0436  -0.0851 -0.0103 107 GLU A CD  
919  O OE1 . GLU A 108 ? 0.3875 0.3004 0.5095 0.0081  -0.1547 0.0163  107 GLU A OE1 
920  O OE2 . GLU A 108 ? 0.2271 0.4989 0.7267 0.0661  -0.1671 -0.0599 107 GLU A OE2 
921  N N   . LEU A 109 ? 0.2158 0.2160 0.1929 0.0761  -0.0068 0.0132  108 LEU A N   
922  C CA  . LEU A 109 ? 0.3083 0.2487 0.1739 0.0864  -0.0044 0.0274  108 LEU A CA  
923  C C   . LEU A 109 ? 0.2724 0.2846 0.1994 0.0643  -0.0003 0.0271  108 LEU A C   
924  O O   . LEU A 109 ? 0.2808 0.3696 0.2160 0.0513  -0.0193 0.0055  108 LEU A O   
925  C CB  . LEU A 109 ? 0.3154 0.2463 0.2658 0.0908  -0.0233 0.0672  108 LEU A CB  
926  C CG  . LEU A 109 ? 0.2849 0.2963 0.3898 0.0821  -0.0668 -0.0166 108 LEU A CG  
927  C CD1 . LEU A 109 ? 0.5269 0.2682 0.6859 0.0161  -0.1156 -0.0963 108 LEU A CD1 
928  C CD2 . LEU A 109 ? 0.3036 0.3426 0.5345 0.0696  -0.1078 -0.0821 108 LEU A CD2 
929  N N   . ILE A 110 ? 0.3371 0.2961 0.2003 0.0897  -0.0116 0.0074  109 ILE A N   
930  C CA  . ILE A 110 ? 0.4132 0.3476 0.1952 0.0576  -0.0254 -0.0132 109 ILE A CA  
931  C C   . ILE A 110 ? 0.4253 0.3873 0.2327 0.0347  -0.0027 -0.0019 109 ILE A C   
932  O O   . ILE A 110 ? 0.4201 0.4173 0.2138 0.0701  0.0004  -0.0104 109 ILE A O   
933  C CB  . ILE A 110 ? 0.5497 0.3240 0.2511 0.0698  -0.0670 -0.0259 109 ILE A CB  
934  C CG1 . ILE A 110 ? 0.6215 0.3766 0.2812 0.0355  -0.0700 -0.0522 109 ILE A CG1 
935  C CG2 . ILE A 110 ? 0.5954 0.4502 0.2860 0.0426  -0.0388 -0.0815 109 ILE A CG2 
936  C CD1 . ILE A 110 ? 0.7486 0.4253 0.4572 0.0284  -0.0557 -0.0087 109 ILE A CD1 
937  N N   . ASP A 111 ? 0.4728 0.4609 0.2510 0.0174  -0.0329 0.0197  110 ASP A N   
938  C CA  . ASP A 111 ? 0.6095 0.4833 0.2765 -0.0987 -0.0461 0.0796  110 ASP A CA  
939  C C   . ASP A 111 ? 0.4910 0.4700 0.2319 -0.0315 -0.0308 0.0374  110 ASP A C   
940  O O   . ASP A 111 ? 0.5682 0.5654 0.2443 -0.0321 0.0225  0.0695  110 ASP A O   
941  C CB  . ASP A 111 ? 0.8097 0.4570 0.3399 -0.1446 0.0353  0.0179  110 ASP A CB  
942  C CG  . ASP A 111 ? 0.6886 0.8261 0.4781 -0.1582 0.0422  -0.1073 110 ASP A CG  
943  O OD1 . ASP A 111 ? 0.6331 0.9132 0.2815 -0.1758 0.0269  -0.0367 110 ASP A OD1 
944  O OD2 . ASP A 111 ? 1.0317 0.9941 0.5095 0.0611  -0.1457 -0.2482 110 ASP A OD2 
945  N N   . GLY A 112 ? 0.5074 0.3986 0.2584 0.0100  -0.0458 0.0837  111 GLY A N   
946  C CA  . GLY A 112 ? 0.4865 0.3096 0.3425 0.0597  -0.0490 0.0826  111 GLY A CA  
947  C C   . GLY A 112 ? 0.4795 0.3444 0.3501 0.0397  -0.0504 0.1004  111 GLY A C   
948  O O   . GLY A 112 ? 0.4427 0.3090 0.3311 0.0723  0.0118  0.0495  111 GLY A O   
949  N N   . LYS A 113 ? 0.3335 0.3353 0.2134 0.0319  -0.0057 0.0448  112 LYS A N   
950  C CA  . LYS A 113 ? 0.3050 0.3397 0.2060 0.0423  0.0426  0.0645  112 LYS A CA  
951  C C   . LYS A 113 ? 0.3150 0.2601 0.2083 0.0698  0.0524  0.0376  112 LYS A C   
952  O O   . LYS A 113 ? 0.3000 0.3491 0.2068 0.0613  0.0284  0.0319  112 LYS A O   
953  C CB  . LYS A 113 ? 0.3667 0.4066 0.2156 0.0522  0.0238  -0.0005 112 LYS A CB  
954  C CG  . LYS A 113 ? 0.5535 0.5219 0.2468 0.0725  0.0958  0.0147  112 LYS A CG  
955  C CD  . LYS A 113 ? 0.5590 0.5743 0.3187 0.1264  0.1028  -0.0133 112 LYS A CD  
956  C CE  . LYS A 113 ? 0.8657 0.8897 0.3669 0.1803  0.2285  -0.1289 112 LYS A CE  
957  N NZ  . LYS A 113 ? 1.2204 0.9521 0.4344 0.2069  0.1870  -0.2110 112 LYS A NZ  
958  N N   A LEU A 114 ? 0.2512 0.2076 0.2235 0.0892  0.0635  0.0666  113 LEU A N   
959  N N   B LEU A 114 ? 0.2874 0.2264 0.2143 0.0755  0.0514  0.0696  113 LEU A N   
960  C CA  A LEU A 114 ? 0.1873 0.1761 0.2145 0.0967  0.0550  0.0613  113 LEU A CA  
961  C CA  B LEU A 114 ? 0.2303 0.2229 0.2164 0.0629  0.0649  0.0725  113 LEU A CA  
962  C C   A LEU A 114 ? 0.2229 0.1713 0.2247 0.0927  0.0651  0.0534  113 LEU A C   
963  C C   B LEU A 114 ? 0.2450 0.2212 0.2196 0.0597  0.0626  0.0505  113 LEU A C   
964  O O   A LEU A 114 ? 0.2445 0.1699 0.2812 0.1204  0.0873  0.0666  113 LEU A O   
965  O O   B LEU A 114 ? 0.2651 0.2248 0.2562 0.0818  0.0670  0.0461  113 LEU A O   
966  C CB  A LEU A 114 ? 0.1810 0.1391 0.2013 0.0786  0.0835  0.0649  113 LEU A CB  
967  C CB  B LEU A 114 ? 0.3207 0.2369 0.2523 0.0323  0.0525  0.0593  113 LEU A CB  
968  C CG  A LEU A 114 ? 0.1830 0.1178 0.1839 0.0861  0.0753  0.0439  113 LEU A CG  
969  C CG  B LEU A 114 ? 0.3070 0.2816 0.2369 0.0019  0.0714  0.0174  113 LEU A CG  
970  C CD1 A LEU A 114 ? 0.1733 0.1068 0.1940 0.0718  0.0912  0.0501  113 LEU A CD1 
971  C CD1 B LEU A 114 ? 0.3102 0.4165 0.2681 0.0630  0.0543  0.0833  113 LEU A CD1 
972  C CD2 A LEU A 114 ? 0.1958 0.1088 0.1348 0.0678  0.0870  0.0620  113 LEU A CD2 
973  C CD2 B LEU A 114 ? 0.3967 0.3356 0.2842 -0.0360 0.0532  -0.0075 113 LEU A CD2 
974  N N   . ILE A 115 ? 0.1692 0.2127 0.2183 0.0924  0.0492  0.0403  114 ILE A N   
975  C CA  . ILE A 115 ? 0.2278 0.2001 0.1747 0.0850  0.0398  0.0234  114 ILE A CA  
976  C C   . ILE A 115 ? 0.1946 0.1626 0.1671 0.0667  0.0329  0.0069  114 ILE A C   
977  O O   . ILE A 115 ? 0.1795 0.1844 0.1818 0.0777  0.0169  -0.0002 114 ILE A O   
978  C CB  . ILE A 115 ? 0.2315 0.2394 0.1838 0.0865  0.0242  -0.0025 114 ILE A CB  
979  C CG1 . ILE A 115 ? 0.3397 0.2844 0.1875 0.0615  0.0131  0.0051  114 ILE A CG1 
980  C CG2 . ILE A 115 ? 0.3171 0.2447 0.2233 0.0993  0.0188  -0.0040 114 ILE A CG2 
981  C CD1 . ILE A 115 ? 0.4046 0.3403 0.2123 0.0651  0.0437  0.0269  114 ILE A CD1 
982  N N   . LEU A 116 ? 0.1723 0.1760 0.1881 0.0596  0.0450  0.0352  115 LEU A N   
983  C CA  . LEU A 116 ? 0.1689 0.1634 0.1885 0.0532  0.0255  0.0257  115 LEU A CA  
984  C C   . LEU A 116 ? 0.1724 0.1697 0.1734 0.0426  0.0372  0.0071  115 LEU A C   
985  O O   . LEU A 116 ? 0.1977 0.1896 0.2083 0.0615  0.0601  0.0133  115 LEU A O   
986  C CB  . LEU A 116 ? 0.1449 0.2003 0.2315 0.0438  0.0178  0.0312  115 LEU A CB  
987  C CG  . LEU A 116 ? 0.1540 0.1756 0.2374 0.0717  0.0118  0.0232  115 LEU A CG  
988  C CD1 . LEU A 116 ? 0.1846 0.1466 0.2168 0.0656  0.0036  -0.0081 115 LEU A CD1 
989  C CD2 . LEU A 116 ? 0.2098 0.1813 0.2902 0.0381  -0.0134 0.0471  115 LEU A CD2 
990  N N   . THR A 117 ? 0.1471 0.1508 0.1827 0.0526  0.0234  0.0047  116 THR A N   
991  C CA  . THR A 117 ? 0.1508 0.1487 0.1706 0.0362  0.0090  -0.0073 116 THR A CA  
992  C C   . THR A 117 ? 0.1245 0.1420 0.1747 0.0392  0.0129  -0.0034 116 THR A C   
993  O O   . THR A 117 ? 0.1743 0.1440 0.1833 0.0465  0.0333  -0.0071 116 THR A O   
994  C CB  . THR A 117 ? 0.1527 0.1733 0.2001 0.0512  -0.0176 -0.0209 116 THR A CB  
995  O OG1 . THR A 117 ? 0.2202 0.2175 0.1867 0.0434  -0.0146 -0.0172 116 THR A OG1 
996  C CG2 . THR A 117 ? 0.1887 0.1713 0.2177 0.0372  -0.0136 -0.0170 116 THR A CG2 
997  N N   A LEU A 118 ? 0.1590 0.1213 0.1933 0.0590  0.0215  -0.0142 117 LEU A N   
998  N N   B LEU A 118 ? 0.1456 0.1304 0.1782 0.0567  0.0180  -0.0253 117 LEU A N   
999  C CA  A LEU A 118 ? 0.1896 0.1195 0.1948 0.0188  0.0319  0.0043  117 LEU A CA  
1000 C CA  B LEU A 118 ? 0.1686 0.1331 0.1758 0.0054  0.0207  -0.0153 117 LEU A CA  
1001 C C   A LEU A 118 ? 0.1839 0.1169 0.1889 0.0212  0.0430  -0.0080 117 LEU A C   
1002 C C   B LEU A 118 ? 0.1801 0.1287 0.1808 0.0119  0.0380  -0.0143 117 LEU A C   
1003 O O   A LEU A 118 ? 0.2053 0.1387 0.2041 0.0427  0.0356  -0.0248 117 LEU A O   
1004 O O   B LEU A 118 ? 0.2037 0.1489 0.1915 0.0369  0.0268  -0.0302 117 LEU A O   
1005 C CB  A LEU A 118 ? 0.1966 0.1244 0.2270 0.0153  0.0180  0.0289  117 LEU A CB  
1006 C CB  B LEU A 118 ? 0.1742 0.1590 0.2155 0.0089  0.0006  -0.0082 117 LEU A CB  
1007 C CG  A LEU A 118 ? 0.2240 0.1245 0.2268 0.0165  0.0191  0.0827  117 LEU A CG  
1008 C CG  B LEU A 118 ? 0.1561 0.1699 0.1952 -0.0070 -0.0197 -0.0191 117 LEU A CG  
1009 C CD1 A LEU A 118 ? 0.2002 0.2117 0.2877 0.0136  0.0388  0.0527  117 LEU A CD1 
1010 C CD1 B LEU A 118 ? 0.1534 0.1600 0.2231 -0.0132 0.0289  -0.0370 117 LEU A CD1 
1011 C CD2 A LEU A 118 ? 0.1494 0.1205 0.2394 0.0581  0.0389  0.0560  117 LEU A CD2 
1012 C CD2 B LEU A 118 ? 0.1100 0.2498 0.2511 0.0331  0.0778  -0.0414 117 LEU A CD2 
1013 N N   . THR A 119 ? 0.1668 0.1244 0.1755 0.0344  0.0294  -0.0081 118 THR A N   
1014 C CA  . THR A 119 ? 0.1664 0.1278 0.2055 0.0190  0.0358  -0.0025 118 THR A CA  
1015 C C   . THR A 119 ? 0.1865 0.1409 0.2187 0.0251  0.0297  0.0190  118 THR A C   
1016 O O   . THR A 119 ? 0.2135 0.1509 0.2103 0.0250  0.0280  0.0158  118 THR A O   
1017 C CB  . THR A 119 ? 0.1627 0.1805 0.2283 -0.0004 0.0115  -0.0135 118 THR A CB  
1018 O OG1 . THR A 119 ? 0.2052 0.1996 0.2220 -0.0040 0.0013  -0.0327 118 THR A OG1 
1019 C CG2 . THR A 119 ? 0.1795 0.1943 0.2920 -0.0207 -0.0076 -0.0162 118 THR A CG2 
1020 N N   . HIS A 120 ? 0.2120 0.1333 0.2148 0.0266  -0.0006 -0.0111 119 HIS A N   
1021 C CA  . HIS A 120 ? 0.2071 0.1550 0.2116 0.0277  0.0189  0.0131  119 HIS A CA  
1022 C C   . HIS A 120 ? 0.2373 0.1807 0.2636 -0.0105 0.0015  0.0231  119 HIS A C   
1023 O O   . HIS A 120 ? 0.3186 0.1482 0.3203 0.0307  0.0109  -0.0058 119 HIS A O   
1024 C CB  . HIS A 120 ? 0.1965 0.1451 0.2347 0.0458  0.0128  0.0272  119 HIS A CB  
1025 C CG  . HIS A 120 ? 0.2346 0.1748 0.2390 0.0789  0.0080  0.0301  119 HIS A CG  
1026 N ND1 . HIS A 120 ? 0.3241 0.2229 0.2700 0.1458  -0.0458 0.0312  119 HIS A ND1 
1027 C CD2 . HIS A 120 ? 0.2772 0.1701 0.2381 0.0653  0.0146  0.0273  119 HIS A CD2 
1028 C CE1 . HIS A 120 ? 0.3344 0.2550 0.3059 0.1569  -0.0251 0.0375  119 HIS A CE1 
1029 N NE2 . HIS A 120 ? 0.3317 0.1956 0.2328 0.0652  0.0079  0.0332  119 HIS A NE2 
1030 N N   . GLY A 121 ? 0.2541 0.1948 0.3276 -0.0322 0.0462  0.0079  120 GLY A N   
1031 C CA  . GLY A 121 ? 0.4152 0.1936 0.4022 -0.0842 0.0342  0.0362  120 GLY A CA  
1032 C C   . GLY A 121 ? 0.3403 0.2118 0.4043 -0.0902 0.0502  -0.0135 120 GLY A C   
1033 O O   . GLY A 121 ? 0.4135 0.2230 0.4572 -0.0414 -0.0299 -0.0559 120 GLY A O   
1034 N N   . THR A 122 ? 0.4931 0.1735 0.4441 -0.0557 0.0475  -0.0150 121 THR A N   
1035 C CA  . THR A 122 ? 0.4659 0.2043 0.4400 -0.0765 -0.0160 -0.0272 121 THR A CA  
1036 C C   . THR A 122 ? 0.4484 0.1888 0.3032 -0.0291 0.0155  -0.0595 121 THR A C   
1037 O O   . THR A 122 ? 0.5528 0.2191 0.3028 -0.0633 0.0066  -0.0781 121 THR A O   
1038 C CB  . THR A 122 ? 0.5808 0.2076 0.5194 -0.1478 0.0134  -0.0912 121 THR A CB  
1039 O OG1 . THR A 122 ? 0.7138 0.2127 0.5786 0.0177  -0.0020 -0.0503 121 THR A OG1 
1040 C CG2 . THR A 122 ? 0.5958 0.2757 0.5932 -0.1617 0.0735  -0.1219 121 THR A CG2 
1041 N N   . ALA A 123 ? 0.3631 0.1387 0.3041 0.0525  -0.0172 -0.0326 122 ALA A N   
1042 C CA  . ALA A 123 ? 0.3410 0.1613 0.3236 0.0767  -0.0012 -0.0295 122 ALA A CA  
1043 C C   . ALA A 123 ? 0.2531 0.1660 0.2660 0.0567  0.0440  -0.0163 122 ALA A C   
1044 O O   . ALA A 123 ? 0.3576 0.1666 0.2729 0.0930  0.0610  -0.0109 122 ALA A O   
1045 C CB  . ALA A 123 ? 0.3107 0.2063 0.3267 0.0853  0.0092  -0.0292 122 ALA A CB  
1046 N N   . VAL A 124 ? 0.2785 0.1298 0.2590 0.0327  0.0430  -0.0341 123 VAL A N   
1047 C CA  . VAL A 124 ? 0.2282 0.1212 0.2404 0.0322  0.0491  -0.0306 123 VAL A CA  
1048 C C   . VAL A 124 ? 0.2399 0.1093 0.1677 0.0556  0.0376  -0.0237 123 VAL A C   
1049 O O   . VAL A 124 ? 0.2246 0.2116 0.2481 0.0315  0.0415  -0.1145 123 VAL A O   
1050 C CB  . VAL A 124 ? 0.2089 0.2295 0.2887 0.0487  0.0279  -0.0267 123 VAL A CB  
1051 C CG1 . VAL A 124 ? 0.2544 0.2332 0.2507 0.0459  0.0174  -0.0337 123 VAL A CG1 
1052 C CG2 . VAL A 124 ? 0.2293 0.2466 0.3210 0.0094  0.0010  -0.0396 123 VAL A CG2 
1053 N N   . CYS A 125 ? 0.2348 0.1047 0.1929 0.0704  0.0665  0.0342  124 CYS A N   
1054 C CA  . CYS A 125 ? 0.1689 0.1649 0.2191 0.0435  0.0476  -0.0059 124 CYS A CA  
1055 C C   . CYS A 125 ? 0.2021 0.1897 0.1775 0.0654  0.0293  -0.0315 124 CYS A C   
1056 O O   . CYS A 125 ? 0.2211 0.1706 0.2033 0.0617  0.0493  -0.0158 124 CYS A O   
1057 C CB  . CYS A 125 ? 0.1795 0.1821 0.2148 0.0434  0.0367  -0.0066 124 CYS A CB  
1058 S SG  . CYS A 125 ? 0.1789 0.1830 0.2265 0.0545  0.0394  -0.0173 124 CYS A SG  
1059 N N   . THR A 126 ? 0.1896 0.1835 0.1910 0.0860  0.0482  -0.0286 125 THR A N   
1060 C CA  . THR A 126 ? 0.1824 0.1875 0.2218 0.0726  0.0259  -0.0213 125 THR A CA  
1061 C C   . THR A 126 ? 0.2005 0.2172 0.1978 0.0627  0.0650  -0.0108 125 THR A C   
1062 O O   . THR A 126 ? 0.2345 0.1961 0.2388 0.0955  0.0930  0.0085  125 THR A O   
1063 C CB  . THR A 126 ? 0.2183 0.2310 0.2402 0.0741  0.0009  -0.0203 125 THR A CB  
1064 O OG1 . THR A 126 ? 0.2591 0.2432 0.2539 0.0335  -0.0150 -0.0233 125 THR A OG1 
1065 C CG2 . THR A 126 ? 0.3075 0.3132 0.2144 0.1504  0.0021  -0.0005 125 THR A CG2 
1066 N N   . ARG A 127 ? 0.1633 0.1818 0.2369 0.0610  0.0689  0.0117  126 ARG A N   
1067 C CA  . ARG A 127 ? 0.1840 0.1686 0.2863 0.0620  0.0876  0.0491  126 ARG A CA  
1068 C C   . ARG A 127 ? 0.1887 0.2085 0.2502 0.0642  0.0778  0.0546  126 ARG A C   
1069 O O   . ARG A 127 ? 0.2005 0.2289 0.2395 0.0864  0.0671  0.0500  126 ARG A O   
1070 C CB  . ARG A 127 ? 0.1795 0.1875 0.3346 0.0484  0.0521  0.0432  126 ARG A CB  
1071 C CG  . ARG A 127 ? 0.2963 0.2173 0.3793 0.0246  0.0172  0.0317  126 ARG A CG  
1072 C CD  . ARG A 127 ? 0.2678 0.1230 0.3708 0.0159  0.0280  -0.0055 126 ARG A CD  
1073 N NE  . ARG A 127 ? 0.1785 0.1792 0.2717 0.0494  0.0133  0.0150  126 ARG A NE  
1074 C CZ  . ARG A 127 ? 0.1750 0.1913 0.2554 0.0358  0.0224  0.0200  126 ARG A CZ  
1075 N NH1 . ARG A 127 ? 0.2154 0.2345 0.2781 0.0573  0.0361  0.0012  126 ARG A NH1 
1076 N NH2 . ARG A 127 ? 0.2084 0.2109 0.3310 0.0098  0.0413  -0.0027 126 ARG A NH2 
1077 N N   . THR A 128 ? 0.2266 0.1894 0.2279 0.0810  0.0848  0.0289  127 THR A N   
1078 C CA  . THR A 128 ? 0.2265 0.2151 0.2040 0.0538  0.0532  0.0325  127 THR A CA  
1079 C C   . THR A 128 ? 0.2143 0.2077 0.2175 0.0697  0.0569  0.0248  127 THR A C   
1080 O O   . THR A 128 ? 0.2169 0.2115 0.2601 0.0657  0.0813  0.0338  127 THR A O   
1081 C CB  . THR A 128 ? 0.3092 0.2301 0.2094 0.0374  0.0543  0.0086  127 THR A CB  
1082 O OG1 . THR A 128 ? 0.3087 0.2255 0.2520 0.0453  0.0500  -0.0177 127 THR A OG1 
1083 C CG2 . THR A 128 ? 0.3391 0.2905 0.1833 0.0781  0.0318  -0.0056 127 THR A CG2 
1084 N N   . TYR A 129 ? 0.2126 0.2038 0.2141 0.0614  0.0623  0.0140  128 TYR A N   
1085 C CA  . TYR A 129 ? 0.2387 0.1861 0.2479 0.0543  0.0396  0.0252  128 TYR A CA  
1086 C C   . TYR A 129 ? 0.2867 0.2101 0.2150 0.0281  0.0401  0.0277  128 TYR A C   
1087 O O   . TYR A 129 ? 0.2924 0.2687 0.2352 0.0807  0.0565  0.0751  128 TYR A O   
1088 C CB  . TYR A 129 ? 0.2684 0.1683 0.2472 0.0571  0.0414  0.0217  128 TYR A CB  
1089 C CG  . TYR A 129 ? 0.2353 0.1873 0.2372 0.0602  0.0785  0.0380  128 TYR A CG  
1090 C CD1 . TYR A 129 ? 0.2484 0.1947 0.2769 0.0628  0.0801  0.0546  128 TYR A CD1 
1091 C CD2 . TYR A 129 ? 0.2530 0.1880 0.2709 0.0625  0.0718  0.0468  128 TYR A CD2 
1092 C CE1 . TYR A 129 ? 0.2418 0.1945 0.2374 0.0580  0.0717  0.0246  128 TYR A CE1 
1093 C CE2 . TYR A 129 ? 0.2008 0.2459 0.2805 0.0420  0.0581  0.0560  128 TYR A CE2 
1094 C CZ  . TYR A 129 ? 0.2168 0.2035 0.2631 0.0435  0.0589  0.0367  128 TYR A CZ  
1095 O OH  . TYR A 129 ? 0.2685 0.2115 0.3012 0.0646  0.0081  0.0102  128 TYR A OH  
1096 N N   A GLU A 130 ? 0.2685 0.2274 0.2989 0.0495  0.0781  0.0685  129 GLU A N   
1097 N N   B GLU A 130 ? 0.2843 0.1949 0.2235 0.0656  0.0742  0.0688  129 GLU A N   
1098 C CA  A GLU A 130 ? 0.3240 0.2225 0.2929 0.0834  0.0571  0.0555  129 GLU A CA  
1099 C CA  B GLU A 130 ? 0.2700 0.1929 0.2103 0.0562  0.1056  0.0722  129 GLU A CA  
1100 C C   A GLU A 130 ? 0.3302 0.2410 0.2400 0.0723  0.0665  0.0692  129 GLU A C   
1101 C C   B GLU A 130 ? 0.3053 0.2038 0.2417 0.0488  0.0867  0.0618  129 GLU A C   
1102 O O   A GLU A 130 ? 0.3462 0.2224 0.2751 0.0811  0.0624  0.0609  129 GLU A O   
1103 O O   B GLU A 130 ? 0.2955 0.1975 0.2607 0.0651  0.0845  0.0670  129 GLU A O   
1104 C CB  A GLU A 130 ? 0.5520 0.3231 0.3004 0.1061  0.1232  0.0095  129 GLU A CB  
1105 C CB  B GLU A 130 ? 0.2975 0.1498 0.1773 0.0619  0.1062  0.1171  129 GLU A CB  
1106 C CG  A GLU A 130 ? 0.7311 0.3963 0.3749 0.0466  0.0933  -0.0112 129 GLU A CG  
1107 C CG  B GLU A 130 ? 0.2669 0.1679 0.1519 0.0614  0.1388  0.1184  129 GLU A CG  
1108 C CD  A GLU A 130 ? 0.7999 0.6249 0.2713 0.1968  0.0184  0.0602  129 GLU A CD  
1109 C CD  B GLU A 130 ? 0.2565 0.1722 0.1798 0.0714  0.1442  0.0954  129 GLU A CD  
1110 O OE1 A GLU A 130 ? 0.8571 0.6804 0.3677 0.2274  0.2212  0.0253  129 GLU A OE1 
1111 O OE1 B GLU A 130 ? 0.2538 0.1906 0.2120 0.0487  0.1498  0.1238  129 GLU A OE1 
1112 O OE2 A GLU A 130 ? 0.9031 0.8626 0.3512 0.0620  -0.0268 -0.0179 129 GLU A OE2 
1113 O OE2 B GLU A 130 ? 0.2798 0.1753 0.2207 0.0747  0.1449  0.1622  129 GLU A OE2 
1114 N N   . LYS A 131 ? 0.2945 0.2291 0.2752 0.0493  0.0648  0.0658  130 LYS A N   
1115 C CA  . LYS A 131 ? 0.3192 0.2356 0.2962 0.0388  0.0621  0.0401  130 LYS A CA  
1116 C C   . LYS A 131 ? 0.3261 0.2679 0.3031 0.0287  0.0602  0.0380  130 LYS A C   
1117 O O   . LYS A 131 ? 0.4968 0.3008 0.3056 0.0016  0.0815  0.0672  130 LYS A O   
1118 C CB  . LYS A 131 ? 0.3776 0.2082 0.3542 0.0736  0.0275  0.0286  130 LYS A CB  
1119 C CG  . LYS A 131 ? 0.3636 0.2686 0.4121 0.0174  0.0275  -0.0187 130 LYS A CG  
1120 C CD  . LYS A 131 ? 0.3429 0.2658 0.4060 -0.0209 0.0712  0.0478  130 LYS A CD  
1121 C CE  . LYS A 131 ? 0.4361 0.2543 0.4457 -0.0141 0.0111  -0.0053 130 LYS A CE  
1122 N NZ  . LYS A 131 ? 0.7095 0.1994 0.6189 0.2060  -0.1572 -0.0162 130 LYS A NZ  
1123 N N   . GLU A 132 ? 0.4039 0.2467 0.3044 -0.0098 0.0480  0.0729  131 GLU A N   
1124 C CA  . GLU A 132 ? 0.3941 0.2573 0.4216 -0.0008 0.0819  0.0538  131 GLU A CA  
1125 C C   . GLU A 132 ? 0.3799 0.3132 0.5636 0.0886  0.1073  0.0886  131 GLU A C   
1126 O O   . GLU A 132 ? 0.4931 0.3849 0.6397 0.1303  0.1921  0.1650  131 GLU A O   
1127 C CB  . GLU A 132 ? 0.4022 0.3052 0.3846 0.0301  0.0618  0.0758  131 GLU A CB  
1128 C CG  . GLU A 132 ? 0.3800 0.3207 0.5734 0.0279  0.1276  0.0653  131 GLU A CG  
1129 C CD  . GLU A 132 ? 0.4217 0.4300 0.6371 0.0659  0.0683  0.1473  131 GLU A CD  
1130 O OE1 . GLU A 132 ? 0.5131 0.2528 0.9828 0.0803  0.1271  0.0710  131 GLU A OE1 
1131 O OE2 . GLU A 132 ? 0.6186 0.6126 0.6347 -0.1336 0.1282  -0.0052 131 GLU A OE2 
1132 N N   . ALA A 133 ? 0.4434 0.3669 0.6496 -0.0076 0.1306  0.1123  132 ALA A N   
1133 C CA  . ALA A 133 ? 0.7539 0.3190 0.7696 0.0292  0.0749  0.0339  132 ALA A CA  
1134 C C   . ALA A 133 ? 0.9162 0.2961 0.8285 0.0944  0.1734  -0.1823 132 ALA A C   
1135 O O   . ALA A 133 ? 0.9687 0.4548 0.7851 -0.1675 0.1359  0.0511  132 ALA A O   
1136 C CB  . ALA A 133 ? 0.9229 0.4601 0.8164 -0.0334 0.1825  0.0640  132 ALA A CB  
1137 O OXT . ALA A 133 ? 0.5850 0.3165 0.8743 0.1015  0.2742  0.0220  132 ALA A OXT 
1138 C C1  . IZP B .   ? 0.5501 0.3980 0.3247 0.0309  -0.1479 -0.0262 200 IZP A C1  
1139 O O1  . IZP B .   ? 0.5030 0.2530 0.5947 -0.0609 0.1499  -0.0492 200 IZP A O1  
1140 C C2  . IZP B .   ? 0.3043 0.3450 0.3137 0.0517  0.0407  -0.0311 200 IZP A C2  
1141 O O2  . IZP B .   ? 0.2070 0.1751 0.3171 0.0591  -0.0177 0.0088  200 IZP A O2  
1142 C C3  . IZP B .   ? 0.3454 0.3061 0.3401 0.0508  0.0430  -0.0067 200 IZP A C3  
1143 C C4  . IZP B .   ? 0.2944 0.2911 0.4512 0.1072  0.0719  -0.0140 200 IZP A C4  
1144 C C5  . IZP B .   ? 0.4537 0.3468 0.2707 0.0590  0.0613  -0.0273 200 IZP A C5  
1145 C C6  . IZP B .   ? 0.3825 0.2742 0.3805 0.0562  0.0366  0.0427  200 IZP A C6  
1146 C C7  . IZP B .   ? 0.3515 0.2388 0.2048 0.0022  -0.0268 0.0355  200 IZP A C7  
1147 C C8  . IZP B .   ? 0.3511 0.2036 0.3945 -0.0037 -0.0490 0.0354  200 IZP A C8  
1148 C C9  . IZP B .   ? 0.3632 0.2494 0.4143 -0.0259 -0.0733 -0.0703 200 IZP A C9  
1149 C C10 . IZP B .   ? 0.3457 0.3158 0.3971 -0.0155 0.0198  -0.0671 200 IZP A C10 
1150 C C11 . IZP B .   ? 0.2834 0.3568 0.3173 -0.0258 0.0377  -0.0120 200 IZP A C11 
1151 C C12 . IZP B .   ? 0.3161 0.2890 0.4117 0.0316  -0.0309 -0.0866 200 IZP A C12 
1152 C C13 . IZP B .   ? 0.3254 0.1851 0.7214 0.0227  -0.0884 -0.0011 200 IZP A C13 
1153 O O1  . PG4 C .   ? 0.4605 0.7232 1.2053 -0.1151 0.2231  -0.4752 201 PG4 A O1  
1154 C C1  . PG4 C .   ? 0.8159 0.6980 1.0272 0.0156  0.2336  -0.0563 201 PG4 A C1  
1155 C C2  . PG4 C .   ? 0.5083 0.5810 0.9785 0.0008  0.2829  -0.1344 201 PG4 A C2  
1156 O O2  . PG4 C .   ? 0.5216 0.5562 0.5494 0.0926  0.1282  -0.0947 201 PG4 A O2  
1157 C C3  . PG4 C .   ? 0.6371 0.3651 0.5876 0.1242  0.1118  -0.0818 201 PG4 A C3  
1158 C C4  . PG4 C .   ? 0.5838 0.3137 0.4841 -0.0358 -0.0465 -0.1085 201 PG4 A C4  
1159 O O3  . PG4 C .   ? 0.4840 0.4981 0.3785 -0.0592 0.0650  -0.0645 201 PG4 A O3  
1160 C C5  . PG4 C .   ? 0.2542 0.5259 0.4801 0.0548  0.0504  -0.0475 201 PG4 A C5  
1161 C C6  . PG4 C .   ? 0.3805 0.6392 0.4238 -0.0405 0.0144  0.0113  201 PG4 A C6  
1162 O O4  . PG4 C .   ? 0.5373 0.5637 0.3788 -0.0660 0.0199  -0.0689 201 PG4 A O4  
1163 C C7  . PG4 C .   ? 0.5364 0.4688 0.3759 0.0106  0.0490  -0.1303 201 PG4 A C7  
1164 C C8  . PG4 C .   ? 0.6624 0.4461 0.4362 -0.1103 0.1517  -0.0852 201 PG4 A C8  
1165 O O5  . PG4 C .   ? 0.7499 0.4801 0.5526 -0.1582 0.0537  -0.1283 201 PG4 A O5  
1166 C C1  . PEG D .   ? 0.3621 0.4560 0.3792 0.1448  -0.0272 0.0360  202 PEG A C1  
1167 O O1  . PEG D .   ? 0.3283 0.5918 0.4150 0.1433  -0.0687 0.0135  202 PEG A O1  
1168 C C2  . PEG D .   ? 0.4711 0.4820 0.3564 0.1184  0.0747  -0.0115 202 PEG A C2  
1169 O O2  . PEG D .   ? 0.3961 0.2426 0.2705 0.0215  -0.0162 -0.0162 202 PEG A O2  
1170 C C3  . PEG D .   ? 0.4818 0.2434 0.5150 0.0884  0.0591  0.0872  202 PEG A C3  
1171 C C4  . PEG D .   ? 0.3893 0.3758 0.4466 0.0421  -0.0481 0.0599  202 PEG A C4  
1172 O O4  . PEG D .   ? 0.4747 0.4560 0.4143 0.1230  -0.0470 0.0834  202 PEG A O4  
1173 C C   . ACY E .   ? 0.1675 0.2484 0.2897 0.0384  0.0045  0.0807  203 ACY A C   
1174 O O   . ACY E .   ? 0.1628 0.2853 0.2959 0.0649  0.0260  0.0867  203 ACY A O   
1175 O OXT . ACY E .   ? 0.1596 0.1764 0.2563 0.0149  -0.0045 0.0409  203 ACY A OXT 
1176 C CH3 . ACY E .   ? 0.2348 0.3625 0.2876 0.0849  -0.0269 0.0353  203 ACY A CH3 
1177 C C1  . PGE F .   ? 0.3513 0.4790 0.7658 -0.0121 -0.0470 -0.3165 204 PGE A C1  
1178 O O1  . PGE F .   ? 0.6047 0.5704 1.0427 0.0728  0.2971  -0.2942 204 PGE A O1  
1179 C C2  . PGE F .   ? 0.2427 0.8317 0.8061 -0.1316 0.0156  -0.1854 204 PGE A C2  
1180 O O2  . PGE F .   ? 0.5651 0.5516 0.7187 0.0156  0.0732  -0.0758 204 PGE A O2  
1181 C C3  . PGE F .   ? 0.3928 0.4487 0.7163 -0.0912 0.1204  -0.2652 204 PGE A C3  
1182 C C4  . PGE F .   ? 0.4604 0.4036 0.6315 -0.1538 0.0705  -0.1489 204 PGE A C4  
1183 O O4  . PGE F .   ? 0.9113 0.9579 0.5355 0.2162  0.1715  0.1192  204 PGE A O4  
1184 C C6  . PGE F .   ? 0.7735 0.3991 0.5111 0.0208  0.0926  -0.0186 204 PGE A C6  
1185 C C5  . PGE F .   ? 0.6781 0.4310 0.6576 0.0194  0.1373  -0.0512 204 PGE A C5  
1186 O O3  . PGE F .   ? 0.6177 0.3628 0.7204 0.0945  0.1187  0.0056  204 PGE A O3  
1187 C C1  . GOL G .   ? 0.4803 0.5268 0.5224 -0.2659 -0.0352 -0.0108 205 GOL A C1  
1188 O O1  . GOL G .   ? 0.4253 0.5331 0.8547 -0.1149 -0.0480 0.3809  205 GOL A O1  
1189 C C2  . GOL G .   ? 0.8097 0.5186 0.5462 -0.1821 -0.0145 0.0269  205 GOL A C2  
1190 O O2  . GOL G .   ? 0.7239 0.8673 0.9405 -0.0387 -0.0680 0.0913  205 GOL A O2  
1191 C C3  . GOL G .   ? 0.6789 0.6753 0.6466 -0.1951 -0.0400 -0.0230 205 GOL A C3  
1192 O O3  . GOL G .   ? 1.0270 0.6780 0.7005 -0.2562 -0.1974 -0.0358 205 GOL A O3  
1193 O O   . HOH H .   ? 0.0560 0.4941 0.4817 0.0957  -0.0804 -0.1326 301 HOH A O   
1194 O O   . HOH H .   ? 0.6738 0.7388 0.5357 0.2690  0.1362  -0.0363 302 HOH A O   
1195 O O   . HOH H .   ? 0.3611 0.6408 0.7526 0.0690  0.1236  0.2473  303 HOH A O   
1196 O O   A HOH H .   ? 0.3288 0.4945 0.7965 -0.0622 -0.2000 -0.1891 304 HOH A O   
1197 O O   B HOH H .   ? 0.2996 0.2782 0.5270 -0.0436 0.0794  0.0111  304 HOH A O   
1198 O O   . HOH H .   ? 0.4410 0.3340 0.8217 0.0052  0.2195  0.1207  305 HOH A O   
1199 O O   . HOH H .   ? 0.4846 0.5398 0.7695 -0.0014 0.1748  0.0739  306 HOH A O   
1200 O O   . HOH H .   ? 0.6723 0.5520 0.8071 -0.0176 -0.0335 0.2068  307 HOH A O   
1201 O O   . HOH H .   ? 0.6685 0.5184 0.7226 -0.2205 0.0553  -0.0630 308 HOH A O   
1202 O O   . HOH H .   ? 0.2631 0.3072 0.4165 0.0147  0.0828  -0.0187 309 HOH A O   
1203 O O   . HOH H .   ? 0.3642 0.2249 0.8699 0.0077  0.0952  -0.0707 310 HOH A O   
1204 O O   . HOH H .   ? 0.5486 0.5583 0.5098 0.0909  -0.1696 -0.1630 311 HOH A O   
1205 O O   . HOH H .   ? 1.0632 0.6556 0.9722 0.1099  0.1171  -0.4625 312 HOH A O   
1206 O O   . HOH H .   ? 0.6938 0.5310 0.6922 0.1008  0.1874  0.0029  313 HOH A O   
1207 O O   . HOH H .   ? 0.5534 0.2980 1.3693 0.0118  0.3166  -0.0228 314 HOH A O   
1208 O O   A HOH H .   ? 0.1720 0.4861 0.7443 -0.0566 0.0456  0.1576  315 HOH A O   
1209 O O   B HOH H .   ? 0.4978 0.4790 0.6770 -0.2100 -0.2445 0.3221  315 HOH A O   
1210 O O   . HOH H .   ? 0.2343 0.4102 0.2855 0.1250  0.0098  0.0629  316 HOH A O   
1211 O O   . HOH H .   ? 0.6474 0.6601 0.7754 -0.0074 0.1659  -0.0726 317 HOH A O   
1212 O O   . HOH H .   ? 0.2644 0.4985 0.4596 -0.0489 -0.0180 0.1711  318 HOH A O   
1213 O O   . HOH H .   ? 0.4985 0.5038 0.4739 0.2691  -0.0695 -0.1899 319 HOH A O   
1214 O O   . HOH H .   ? 0.8815 0.7646 0.3045 -0.1761 0.0357  -0.0074 320 HOH A O   
1215 O O   . HOH H .   ? 0.1905 0.2552 0.3476 0.0243  -0.0078 -0.0714 321 HOH A O   
1216 O O   . HOH H .   ? 0.6629 0.6212 0.6624 0.1379  -0.1277 0.1511  322 HOH A O   
1217 O O   . HOH H .   ? 0.2705 0.4019 0.3315 -0.0123 -0.0453 -0.1202 323 HOH A O   
1218 O O   . HOH H .   ? 0.4128 0.3720 0.3428 0.0984  0.0745  0.1075  324 HOH A O   
1219 O O   . HOH H .   ? 0.4199 0.4070 0.9323 -0.0322 -0.1798 -0.0126 325 HOH A O   
1220 O O   . HOH H .   ? 0.6087 0.3094 0.5364 -0.0517 -0.3261 0.0289  326 HOH A O   
1221 O O   . HOH H .   ? 0.3069 0.4800 1.1539 0.0269  -0.0170 -0.2147 327 HOH A O   
1222 O O   . HOH H .   ? 0.3892 0.4501 0.4333 -0.1954 -0.0041 -0.0405 328 HOH A O   
1223 O O   . HOH H .   ? 0.4437 0.3501 0.4656 -0.0907 0.0751  0.0293  329 HOH A O   
1224 O O   . HOH H .   ? 0.3279 0.8293 0.4355 -0.0359 -0.1643 -0.1291 330 HOH A O   
1225 O O   . HOH H .   ? 0.6355 0.3920 0.4234 0.0448  -0.1270 -0.0930 331 HOH A O   
1226 O O   . HOH H .   ? 0.9125 0.5403 0.3930 -0.1627 0.0938  -0.0870 332 HOH A O   
1227 O O   . HOH H .   ? 0.4210 0.2708 0.3604 0.0077  -0.0174 0.0059  333 HOH A O   
1228 O O   . HOH H .   ? 0.3689 0.5482 0.9286 -0.1241 -0.0510 -0.2330 334 HOH A O   
1229 O O   . HOH H .   ? 0.1326 0.3298 0.2797 0.0210  0.0141  -0.0147 335 HOH A O   
1230 O O   . HOH H .   ? 0.3982 0.3897 0.8767 0.0473  0.2477  0.1127  336 HOH A O   
1231 O O   . HOH H .   ? 0.2527 0.2390 0.2525 0.0505  0.0082  0.0391  337 HOH A O   
1232 O O   . HOH H .   ? 0.9007 0.3667 0.3698 0.0642  -0.0606 -0.0582 338 HOH A O   
1233 O O   A HOH H .   ? 0.1960 0.2296 0.2713 0.1192  0.0383  0.0551  339 HOH A O   
1234 O O   B HOH H .   ? 0.2945 0.2862 0.2133 0.0095  -0.0225 0.0116  339 HOH A O   
1235 O O   . HOH H .   ? 0.4482 0.4857 0.6923 -0.1774 0.1435  -0.1098 340 HOH A O   
1236 O O   . HOH H .   ? 0.2378 0.1477 0.3044 0.0279  0.0215  0.0426  341 HOH A O   
1237 O O   . HOH H .   ? 0.5662 0.3674 0.3771 0.1706  0.0775  -0.0198 342 HOH A O   
1238 O O   . HOH H .   ? 0.3118 0.3583 0.4423 0.0540  -0.0094 0.0132  343 HOH A O   
1239 O O   . HOH H .   ? 0.1734 0.2066 0.2314 0.0364  0.0019  -0.0006 344 HOH A O   
1240 O O   A HOH H .   ? 0.2443 0.2092 0.2669 -0.0212 -0.0228 -0.0053 345 HOH A O   
1241 O O   B HOH H .   ? 0.3334 0.3885 0.2587 0.1311  0.1071  0.0777  345 HOH A O   
1242 O O   . HOH H .   ? 0.1979 0.2928 0.2641 -0.0220 -0.0163 0.0500  346 HOH A O   
1243 O O   . HOH H .   ? 0.4198 0.3577 0.5649 -0.0449 -0.0321 -0.0901 347 HOH A O   
1244 O O   . HOH H .   ? 0.4054 0.4784 1.1863 -0.0117 -0.3406 0.0091  348 HOH A O   
1245 O O   A HOH H .   ? 0.2617 0.2003 0.2877 -0.0190 -0.0449 0.0743  349 HOH A O   
1246 O O   B HOH H .   ? 0.1127 0.3273 0.3817 0.0035  -0.0836 0.1093  349 HOH A O   
1247 O O   . HOH H .   ? 0.8392 0.5763 1.1690 -0.2055 0.4382  0.1636  350 HOH A O   
1248 O O   . HOH H .   ? 0.4826 0.4251 0.7669 -0.1380 -0.0193 0.0982  351 HOH A O   
1249 O O   . HOH H .   ? 0.3053 0.3004 0.2511 0.0421  0.0046  -0.0584 352 HOH A O   
1250 O O   A HOH H .   ? 0.2984 0.1657 0.2867 0.0068  -0.0323 0.0467  353 HOH A O   
1251 O O   B HOH H .   ? 0.1825 0.1546 0.5341 -0.0413 -0.0058 -0.0189 353 HOH A O   
1252 O O   . HOH H .   ? 0.3791 0.5243 0.5583 0.0293  -0.0402 -0.1740 354 HOH A O   
1253 O O   . HOH H .   ? 0.8664 0.3674 0.9877 -0.1833 0.3017  -0.0241 355 HOH A O   
1254 O O   . HOH H .   ? 0.8898 0.3847 0.5538 0.0280  0.2338  -0.0518 356 HOH A O   
1255 O O   . HOH H .   ? 0.6873 0.6162 0.5076 0.0617  0.0994  0.0751  357 HOH A O   
1256 O O   . HOH H .   ? 0.2267 0.3005 0.2405 0.0504  0.0251  -0.0414 358 HOH A O   
1257 O O   . HOH H .   ? 0.7249 0.6411 0.6913 -0.2597 -0.0159 0.1561  359 HOH A O   
1258 O O   A HOH H .   ? 0.2623 0.2134 0.3647 0.1251  -0.1087 -0.0999 360 HOH A O   
1259 O O   B HOH H .   ? 0.6145 0.3867 0.2562 0.2407  0.0751  0.0999  360 HOH A O   
1260 O O   . HOH H .   ? 0.1772 0.1440 0.3578 0.0067  0.0122  0.0026  361 HOH A O   
1261 O O   . HOH H .   ? 0.4461 1.1297 1.0042 -0.0453 -0.4209 0.1495  362 HOH A O   
1262 O O   . HOH H .   ? 0.5817 0.4305 0.3563 0.0209  -0.1292 -0.0519 363 HOH A O   
1263 O O   . HOH H .   ? 0.7161 0.7776 0.4990 0.3975  -0.1148 0.0018  364 HOH A O   
1264 O O   . HOH H .   ? 0.1791 0.1794 0.2312 0.0563  0.0336  -0.0036 365 HOH A O   
1265 O O   . HOH H .   ? 0.2135 0.2384 0.3273 0.0340  0.0329  0.0496  366 HOH A O   
1266 O O   . HOH H .   ? 0.4785 0.4187 0.6634 0.0496  0.1254  0.2081  367 HOH A O   
1267 O O   . HOH H .   ? 0.1290 0.1227 0.1749 0.0117  -0.0022 -0.0027 368 HOH A O   
1268 O O   . HOH H .   ? 0.2764 0.3265 0.4129 -0.0700 0.0178  -0.1127 369 HOH A O   
1269 O O   . HOH H .   ? 0.3644 0.3188 0.4060 -0.0434 0.1206  0.0383  370 HOH A O   
1270 O O   A HOH H .   ? 0.3625 0.0608 0.1936 0.0101  0.0030  0.0572  371 HOH A O   
1271 O O   B HOH H .   ? 0.1590 0.3298 0.3373 0.0259  0.0334  0.0163  371 HOH A O   
1272 O O   . HOH H .   ? 0.2567 0.2369 0.2293 0.0496  0.0353  -0.0141 372 HOH A O   
1273 O O   . HOH H .   ? 0.6659 0.5310 0.5366 0.1093  0.3369  0.0958  373 HOH A O   
1274 O O   . HOH H .   ? 0.6232 0.6610 0.5223 -0.1233 -0.1940 0.1468  374 HOH A O   
1275 O O   . HOH H .   ? 0.4700 0.5464 0.4436 0.1520  -0.0307 0.0610  375 HOH A O   
1276 O O   . HOH H .   ? 0.2378 0.2243 0.2571 -0.0356 0.0525  -0.0256 376 HOH A O   
1277 O O   . HOH H .   ? 0.3658 0.2456 0.4912 0.0481  0.1715  0.0751  377 HOH A O   
1278 O O   . HOH H .   ? 0.1362 0.1575 0.1911 0.0317  0.0171  0.0043  378 HOH A O   
1279 O O   . HOH H .   ? 0.2254 0.1985 0.2362 0.0436  0.0121  0.0113  379 HOH A O   
1280 O O   . HOH H .   ? 0.2713 0.2747 0.2973 0.0251  0.0172  -0.0802 380 HOH A O   
1281 O O   . HOH H .   ? 0.9473 0.6089 0.5805 -0.3737 0.1809  0.0119  381 HOH A O   
1282 O O   . HOH H .   ? 0.1695 0.1623 0.2568 0.0269  -0.0014 -0.0032 382 HOH A O   
1283 O O   . HOH H .   ? 0.4556 0.3712 0.3226 0.1311  -0.0372 -0.0727 383 HOH A O   
1284 O O   . HOH H .   ? 0.3104 0.6294 0.8379 0.0317  -0.1315 0.0106  384 HOH A O   
1285 O O   . HOH H .   ? 0.5288 0.4733 0.2739 0.2482  -0.0567 -0.0589 385 HOH A O   
1286 O O   . HOH H .   ? 0.3639 0.4245 0.8640 -0.0500 -0.2292 0.1946  386 HOH A O   
1287 O O   . HOH H .   ? 0.4069 0.3646 0.5140 -0.0605 -0.0169 0.2256  387 HOH A O   
1288 O O   . HOH H .   ? 0.4421 0.4409 0.3298 0.1095  -0.0608 0.0079  388 HOH A O   
1289 O O   . HOH H .   ? 0.5418 0.6541 0.4432 -0.0096 -0.1573 -0.0114 389 HOH A O   
1290 O O   . HOH H .   ? 0.3955 0.2915 0.3515 0.0195  -0.0415 0.0144  390 HOH A O   
1291 O O   . HOH H .   ? 0.3415 0.2630 0.3876 0.0164  0.0562  0.1375  391 HOH A O   
1292 O O   . HOH H .   ? 0.3457 0.3415 0.3480 -0.0430 0.0078  0.0646  392 HOH A O   
1293 O O   . HOH H .   ? 0.1049 0.1468 0.2526 0.0019  0.0026  0.0310  393 HOH A O   
1294 O O   A HOH H .   ? 0.2345 0.3049 0.2365 0.0906  -0.0256 0.0542  394 HOH A O   
1295 O O   B HOH H .   ? 0.3497 0.1916 0.2478 -0.0021 -0.0649 0.0348  394 HOH A O   
1296 O O   . HOH H .   ? 0.1890 0.2750 0.2261 0.0679  0.0018  0.0544  395 HOH A O   
1297 O O   . HOH H .   ? 0.2501 0.3693 0.4572 -0.0710 0.0702  -0.0988 396 HOH A O   
1298 O O   . HOH H .   ? 0.7400 0.6696 1.2653 0.0718  -0.1870 0.6747  397 HOH A O   
1299 O O   A HOH H .   ? 0.3302 0.1701 0.3742 0.0056  0.0601  0.0857  398 HOH A O   
1300 O O   B HOH H .   ? 0.3953 0.2604 0.5785 -0.1370 0.2257  -0.0614 398 HOH A O   
1301 O O   . HOH H .   ? 0.6159 0.2821 0.3709 0.0740  -0.0164 0.0153  399 HOH A O   
1302 O O   . HOH H .   ? 0.6994 0.5861 0.6355 0.1704  -0.0749 0.1372  400 HOH A O   
1303 O O   . HOH H .   ? 0.2052 0.4897 0.3539 0.0500  -0.0230 -0.0914 401 HOH A O   
1304 O O   . HOH H .   ? 0.1853 0.2106 0.2515 0.0289  -0.0007 0.0132  402 HOH A O   
1305 O O   . HOH H .   ? 0.3263 0.2538 0.2858 0.0109  -0.0224 -0.0838 403 HOH A O   
1306 O O   . HOH H .   ? 0.3456 0.3929 0.2988 0.0907  -0.0478 -0.0304 404 HOH A O   
1307 O O   . HOH H .   ? 0.5994 1.0732 0.9149 0.5081  0.3676  0.6944  405 HOH A O   
1308 O O   . HOH H .   ? 0.8248 0.3968 0.8362 0.2645  0.3066  0.1602  406 HOH A O   
1309 O O   . HOH H .   ? 0.2769 0.2958 0.2679 0.0657  0.0846  0.0488  407 HOH A O   
1310 O O   . HOH H .   ? 0.1555 0.2428 0.2425 0.0116  -0.0085 0.0222  408 HOH A O   
1311 O O   . HOH H .   ? 0.2822 0.3225 0.3337 0.0143  -0.0142 0.0414  409 HOH A O   
1312 O O   . HOH H .   ? 0.3901 0.4026 0.6544 -0.0991 0.0356  0.0062  410 HOH A O   
1313 O O   . HOH H .   ? 0.1942 0.1862 0.2351 0.0733  0.0121  -0.0351 411 HOH A O   
1314 O O   . HOH H .   ? 1.5241 0.4286 0.5498 -0.2270 0.4447  -0.0990 412 HOH A O   
1315 O O   A HOH H .   ? 0.1503 0.2023 0.3289 -0.0045 -0.0092 0.0036  413 HOH A O   
1316 O O   B HOH H .   ? 0.4661 0.2144 0.2511 0.0457  -0.0303 0.0598  413 HOH A O   
1317 O O   . HOH H .   ? 0.6200 0.4994 1.1641 -0.0392 0.1626  -0.4017 414 HOH A O   
1318 O O   . HOH H .   ? 0.4815 0.1787 0.4269 -0.0583 -0.1139 0.0252  415 HOH A O   
1319 O O   . HOH H .   ? 0.3086 0.1465 0.2925 -0.0031 0.0210  0.0574  416 HOH A O   
1320 O O   . HOH H .   ? 0.4325 0.7604 0.4943 -0.0127 -0.1096 0.1718  417 HOH A O   
1321 O O   . HOH H .   ? 0.5541 0.2575 0.3790 0.1115  0.1721  -0.0403 418 HOH A O   
1322 O O   . HOH H .   ? 0.1605 0.1987 0.2867 0.0026  0.0094  0.0105  419 HOH A O   
1323 O O   . HOH H .   ? 0.6204 0.6736 0.8044 0.2296  -0.4331 -0.0841 420 HOH A O   
1324 O O   A HOH H .   ? 0.2923 0.9707 0.4664 -0.2213 -0.0198 -0.2643 421 HOH A O   
1325 O O   B HOH H .   ? 0.3210 0.7103 0.6536 -0.0396 -0.1478 -0.2740 421 HOH A O   
1326 O O   A HOH H .   ? 0.5707 0.2454 0.3704 0.1413  0.0649  0.0646  422 HOH A O   
1327 O O   B HOH H .   ? 0.6737 0.5183 0.4205 -0.0467 0.2527  -0.1095 422 HOH A O   
1328 O O   . HOH H .   ? 0.3886 1.0384 1.1084 0.3297  0.0480  0.0888  423 HOH A O   
1329 O O   . HOH H .   ? 0.5665 0.7225 0.3919 0.0752  0.0498  -0.1571 424 HOH A O   
1330 O O   . HOH H .   ? 0.3781 0.5499 0.5177 0.0830  0.0464  0.0395  425 HOH A O   
1331 O O   . HOH H .   ? 0.9249 0.5831 0.5236 -0.0236 -0.1788 -0.0070 426 HOH A O   
1332 O O   A HOH H .   ? 0.3339 0.3790 0.5781 0.1851  0.0422  0.0291  427 HOH A O   
1333 O O   B HOH H .   ? 0.4387 0.3019 0.6691 0.1571  0.1653  0.1383  427 HOH A O   
1334 O O   . HOH H .   ? 0.3405 0.2913 0.6852 -0.0231 0.0286  0.0241  428 HOH A O   
1335 O O   . HOH H .   ? 0.5732 0.5234 0.8586 0.0175  -0.0444 0.0831  429 HOH A O   
1336 O O   . HOH H .   ? 0.5047 0.5092 0.4607 -0.1371 -0.1647 0.0333  430 HOH A O   
1337 O O   . HOH H .   ? 0.4367 0.4531 0.4401 0.0602  -0.1176 0.0616  431 HOH A O   
1338 O O   . HOH H .   ? 0.9332 0.3596 1.1280 -0.1216 -0.0241 0.0316  432 HOH A O   
1339 O O   . HOH H .   ? 0.8255 0.4718 0.5530 -0.0959 -0.0904 0.0510  433 HOH A O   
1340 O O   . HOH H .   ? 0.4088 0.3771 0.3898 0.1238  0.0032  -0.0371 434 HOH A O   
1341 O O   . HOH H .   ? 0.5372 0.4213 1.4747 0.0113  0.0002  0.2173  435 HOH A O   
1342 O O   . HOH H .   ? 0.9673 0.6087 0.5089 0.3195  0.1364  0.0068  436 HOH A O   
1343 O O   . HOH H .   ? 0.3742 0.3001 0.4075 0.0700  -0.0068 0.0333  437 HOH A O   
1344 O O   A HOH H .   ? 0.1745 0.4246 0.6485 0.0523  -0.0669 -0.1434 438 HOH A O   
1345 O O   B HOH H .   ? 0.4492 0.4029 0.4697 -0.1926 0.0839  -0.1016 438 HOH A O   
1346 O O   . HOH H .   ? 0.4078 0.6815 0.4788 0.0503  0.0404  0.1659  439 HOH A O   
1347 O O   . HOH H .   ? 0.4260 0.7416 0.9520 0.1693  -0.1403 -0.1655 440 HOH A O   
1348 O O   . HOH H .   ? 0.6041 0.5528 0.8508 0.0771  -0.2826 -0.0620 441 HOH A O   
1349 O O   . HOH H .   ? 0.4908 0.4446 0.8670 0.1636  -0.1662 -0.0189 442 HOH A O   
1350 O O   A HOH H .   ? 0.4545 0.4991 0.7459 -0.0074 -0.3461 -0.1527 443 HOH A O   
1351 O O   B HOH H .   ? 0.8225 0.5143 0.7531 0.0236  0.1247  -0.3320 443 HOH A O   
1352 O O   . HOH H .   ? 0.4103 0.3204 0.4793 0.0043  -0.0041 -0.1683 444 HOH A O   
1353 O O   . HOH H .   ? 0.3462 0.6598 0.7801 0.2111  -0.0046 -0.0211 445 HOH A O   
1354 O O   . HOH H .   ? 0.3402 0.6539 0.9074 -0.0621 -0.0041 -0.3738 446 HOH A O   
1355 O O   . HOH H .   ? 0.7021 0.9680 0.6184 -0.0483 0.1543  -0.3807 447 HOH A O   
1356 O O   . HOH H .   ? 0.5007 0.3899 0.5778 -0.0110 0.0864  -0.0579 448 HOH A O   
1357 O O   . HOH H .   ? 0.6200 0.3073 0.3337 0.1538  -0.0679 -0.0271 449 HOH A O   
1358 O O   . HOH H .   ? 0.2544 0.3910 0.2854 0.0077  -0.0364 0.0440  450 HOH A O   
1359 O O   . HOH H .   ? 0.4462 0.4470 1.3883 0.0742  -0.2078 -0.1392 451 HOH A O   
1360 O O   . HOH H .   ? 0.4004 0.5038 0.4253 0.1233  -0.0743 -0.0471 452 HOH A O   
1361 O O   . HOH H .   ? 0.5474 0.5521 0.6983 -0.0542 0.2412  -0.1716 453 HOH A O   
1362 O O   . HOH H .   ? 0.6212 0.3985 0.8942 -0.0240 -0.3094 0.1651  454 HOH A O   
1363 O O   . HOH H .   ? 0.2712 0.3522 0.6277 -0.1165 -0.0311 0.1539  455 HOH A O   
1364 O O   . HOH H .   ? 0.5867 0.3094 1.1077 -0.0178 -0.0811 0.2292  456 HOH A O   
1365 O O   . HOH H .   ? 0.6581 1.3783 0.5903 0.2023  -0.1914 -0.3775 457 HOH A O   
1366 O O   . HOH H .   ? 1.2076 0.3639 0.5338 0.0460  0.1153  -0.0397 458 HOH A O   
1367 O O   . HOH H .   ? 0.9621 1.0297 0.3435 0.1533  0.0596  0.1147  459 HOH A O   
1368 O O   . HOH H .   ? 0.6997 0.3735 1.0891 0.1116  0.0228  -0.0976 460 HOH A O   
1369 O O   . HOH H .   ? 0.8463 0.6311 1.1833 0.3310  0.4076  0.4295  461 HOH A O   
1370 O O   A HOH H .   ? 0.4819 0.5214 0.6068 -0.0148 0.1785  0.1163  462 HOH A O   
1371 O O   B HOH H .   ? 0.3443 0.9297 0.3363 -0.0334 -0.0428 0.0299  462 HOH A O   
1372 O O   . HOH H .   ? 0.9530 1.1168 0.5587 0.4435  -0.1548 -0.2268 463 HOH A O   
1373 O O   . HOH H .   ? 0.7167 0.5407 0.5818 -0.0499 0.1556  -0.2380 464 HOH A O   
1374 O O   . HOH H .   ? 0.6609 0.4561 0.5157 0.0012  -0.1680 -0.0165 465 HOH A O   
1375 O O   . HOH H .   ? 0.6689 0.6293 0.3456 -0.2274 -0.0083 0.0718  466 HOH A O   
1376 O O   . HOH H .   ? 0.5149 1.4502 0.5189 0.2177  0.0550  0.3519  467 HOH A O   
1377 O O   . HOH H .   ? 0.5241 0.7625 0.6120 0.1430  -0.0384 -0.0746 468 HOH A O   
1378 O O   . HOH H .   ? 1.2578 0.6372 0.9041 -0.3915 -0.5106 0.0655  469 HOH A O   
1379 O O   . HOH H .   ? 0.6975 0.4582 0.6670 -0.1574 0.0375  0.0296  470 HOH A O   
1380 O O   . HOH H .   ? 0.6056 0.4216 0.3893 -0.1775 -0.0654 -0.0198 471 HOH A O   
1381 O O   . HOH H .   ? 0.4458 0.3316 0.3087 0.0030  0.0404  0.0231  472 HOH A O   
1382 O O   . HOH H .   ? 1.2334 0.3265 0.4807 0.0678  0.2272  0.0183  473 HOH A O   
1383 O O   . HOH H .   ? 0.2905 0.4171 0.8431 -0.0664 -0.0020 -0.0749 474 HOH A O   
1384 O O   . HOH H .   ? 0.2689 0.4578 0.5140 -0.0689 -0.0108 0.1735  475 HOH A O   
1385 O O   . HOH H .   ? 0.6283 0.5648 0.3464 0.0236  -0.1688 0.0196  476 HOH A O   
1386 O O   . HOH H .   ? 0.4528 0.7786 1.0277 0.0237  0.3398  0.3719  477 HOH A O   
1387 O O   . HOH H .   ? 0.5682 0.6039 0.9111 0.1371  0.2229  0.2399  478 HOH A O   
1388 O O   . HOH H .   ? 1.1025 0.8184 0.5477 0.0273  0.0810  0.2044  479 HOH A O   
1389 O O   . HOH H .   ? 0.4639 1.2622 0.5043 0.0457  0.0462  0.2604  480 HOH A O   
1390 O O   . HOH H .   ? 0.3517 0.6669 0.5347 0.0542  -0.0519 0.0644  481 HOH A O   
1391 O O   . HOH H .   ? 0.3202 0.6474 0.5585 -0.1961 -0.1184 0.1160  482 HOH A O   
1392 O O   . HOH H .   ? 0.6324 0.5168 0.6572 0.0670  -0.2022 -0.2389 483 HOH A O   
1393 O O   . HOH H .   ? 0.5460 1.1295 0.3782 -0.1500 0.0691  -0.0741 484 HOH A O   
1394 O O   . HOH H .   ? 0.2989 0.3383 0.4235 -0.0564 -0.0519 0.1308  485 HOH A O   
1395 O O   . HOH H .   ? 0.4146 0.4733 0.7460 -0.2043 0.0003  -0.0959 486 HOH A O   
1396 O O   . HOH H .   ? 0.3592 1.1500 0.7733 0.2339  -0.1535 -0.1054 487 HOH A O   
1397 O O   . HOH H .   ? 0.7947 0.7252 0.6802 -0.2298 -0.0015 -0.2789 488 HOH A O   
1398 O O   . HOH H .   ? 0.5870 0.7930 0.9893 -0.0252 0.0125  0.3254  489 HOH A O   
1399 O O   . HOH H .   ? 0.6838 1.5450 0.5180 -0.0224 -0.0879 0.2201  490 HOH A O   
1400 O O   . HOH H .   ? 0.3933 0.3313 0.3862 0.0829  0.0032  0.0130  491 HOH A O   
1401 O O   . HOH H .   ? 0.6470 0.9048 0.4020 0.0701  -0.0638 -0.1582 492 HOH A O   
1402 O O   . HOH H .   ? 0.3624 0.4544 0.5011 0.0045  -0.0682 -0.0547 493 HOH A O   
1403 O O   . HOH H .   ? 0.4904 0.3947 0.7806 -0.0995 0.2436  -0.1897 494 HOH A O   
# 
