data_7GUX
# 
_entry.id   7GUX 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   7GUX         pdb_00007gux 10.2210/pdb7gux/pdb 
WWPDB D_1001406668 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-12-04 
2 'Structure model' 1 1 2025-01-01 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.country'                 
2 2 'Structure model' '_citation.journal_id_CSD'          
3 2 'Structure model' '_citation.journal_id_ISSN'         
4 2 'Structure model' '_citation.journal_volume'          
5 2 'Structure model' '_citation.page_first'              
6 2 'Structure model' '_citation.page_last'               
7 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8 2 'Structure model' '_citation.title'                   
9 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.entry_id                        7GUX 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-09 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              Rob.vanMontfort@icr.ac.uk 
_pdbx_contact_author.name_first         Rob 
_pdbx_contact_author.name_last          'van Montfort' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rodrigues, M.J.'      1 0000-0003-1243-903X 
'Le Bihan, Y.V.'       2 0000-0002-6850-9706 
'van Montfort, R.L.M.' 3 0000-0002-5688-3450 
# 
_citation.id                        primary 
_citation.title                     
'Specific radiation damage to halogenated inhibitors and ligands in protein-ligand crystal structures.' 
_citation.journal_abbrev            J.Appl.Crystallogr. 
_citation.journal_volume            57 
_citation.page_first                1951 
_citation.page_last                 1965 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39628887 
_citation.pdbx_database_id_DOI      10.1107/S1600576724010549 
_citation.journal_id_ASTM           JACGAR 
_citation.country                   DK 
_citation.journal_id_ISSN           0021-8898 
_citation.journal_id_CSD            0228 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rodrigues, M.J.'      1 0000-0003-1243-903X 
primary 'Cabry, M.'            2 0000-0002-9070-5498 
primary 'Collie, G.'           3 0000-0002-0406-922X 
primary 'Carter, M.'           4 ?                   
primary 'McAndrew, C.'         5 0000-0002-1366-088X 
primary 'Owen, R.L.'           6 0000-0002-2104-7057 
primary 'Bellenie, B.R.'       7 0000-0001-9987-3079 
primary 'Le Bihan, Y.V.'       8 0000-0002-6850-9706 
primary 'van Montfort, R.L.M.' 9 0000-0002-5688-3450 
# 
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 'B-cell lymphoma 6 protein'                                            14536.915 1   ? ? ? ? 
2 polymer     syn 'WVIP tetrapeptide'                                                    610.744   1   ? ? ? ? 
3 non-polymer syn '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' 339.575   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                         35.453    1   ? ? ? ? 
5 non-polymer nat 'DIMETHYL SULFOXIDE'                                                   78.133    1   ? ? ? ? 
6 water       nat water                                                                  18.015    185 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'BCL-6,B-cell lymphoma 5 protein,BCL-5,Protein LAZ-3,Zinc finger and BTB domain-containing protein 27,Zinc finger protein 51' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
A ? 
2 'polypeptide(L)' no yes '(ACE)WVIPA' XWVIPA D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' A1ACA 
4 'CHLORIDE ION'                                                         CL    
5 'DIMETHYL SULFOXIDE'                                                   DMS   
6 water                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   ALA n 
1 5   ASP n 
1 6   SER n 
1 7   CYS n 
1 8   ILE n 
1 9   GLN n 
1 10  PHE n 
1 11  THR n 
1 12  ARG n 
1 13  HIS n 
1 14  ALA n 
1 15  SER n 
1 16  ASP n 
1 17  VAL n 
1 18  LEU n 
1 19  LEU n 
1 20  ASN n 
1 21  LEU n 
1 22  ASN n 
1 23  ARG n 
1 24  LEU n 
1 25  ARG n 
1 26  SER n 
1 27  ARG n 
1 28  ASP n 
1 29  ILE n 
1 30  LEU n 
1 31  THR n 
1 32  ASP n 
1 33  VAL n 
1 34  VAL n 
1 35  ILE n 
1 36  VAL n 
1 37  VAL n 
1 38  SER n 
1 39  ARG n 
1 40  GLU n 
1 41  GLN n 
1 42  PHE n 
1 43  ARG n 
1 44  ALA n 
1 45  HIS n 
1 46  LYS n 
1 47  THR n 
1 48  VAL n 
1 49  LEU n 
1 50  MET n 
1 51  ALA n 
1 52  CYS n 
1 53  SER n 
1 54  GLY n 
1 55  LEU n 
1 56  PHE n 
1 57  TYR n 
1 58  SER n 
1 59  ILE n 
1 60  PHE n 
1 61  THR n 
1 62  ASP n 
1 63  GLN n 
1 64  LEU n 
1 65  LYS n 
1 66  CYS n 
1 67  ASN n 
1 68  LEU n 
1 69  SER n 
1 70  VAL n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ASP n 
1 75  PRO n 
1 76  GLU n 
1 77  ILE n 
1 78  ASN n 
1 79  PRO n 
1 80  GLU n 
1 81  GLY n 
1 82  PHE n 
1 83  CYS n 
1 84  ILE n 
1 85  LEU n 
1 86  LEU n 
1 87  ASP n 
1 88  PHE n 
1 89  MET n 
1 90  TYR n 
1 91  THR n 
1 92  SER n 
1 93  ARG n 
1 94  LEU n 
1 95  ASN n 
1 96  LEU n 
1 97  ARG n 
1 98  GLU n 
1 99  GLY n 
1 100 ASN n 
1 101 ILE n 
1 102 MET n 
1 103 ALA n 
1 104 VAL n 
1 105 MET n 
1 106 ALA n 
1 107 THR n 
1 108 ALA n 
1 109 MET n 
1 110 TYR n 
1 111 LEU n 
1 112 GLN n 
1 113 MET n 
1 114 GLU n 
1 115 HIS n 
1 116 VAL n 
1 117 VAL n 
1 118 ASP n 
1 119 THR n 
1 120 CYS n 
1 121 ARG n 
1 122 LYS n 
1 123 PHE n 
1 124 ILE n 
1 125 LYS n 
1 126 ALA n 
1 127 SER n 
1 128 GLU n 
2 1   ACE n 
2 2   TRP n 
2 3   VAL n 
2 4   ILE n 
2 5   PRO n 
2 6   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                   128 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'BCL6, BCL5, LAZ3, ZBTB27, ZNF51' 
_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               BL21-AI 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               pET48b 
_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_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1 6 'synthetic construct' ? 32630 ? 
3 2 sample ? ? 'synthetic construct' ? 32630 ? 
# 
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 
A1ACA non-polymer         . '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' ? 'C12 H8 Br Cl N4 O' 339.575 
ACE   non-polymer         . 'ACETYL GROUP'                                                         ? 'C2 H4 O'           44.053  
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 
CL    non-polymer         . 'CHLORIDE ION'                                                         ? 'Cl -1'             35.453  
CYS   'L-peptide linking' y CYSTEINE                                                               ? 'C3 H7 N O2 S'      121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                   ? 'C2 H6 O S'         78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                              ? 'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                        ? 'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE                                                                ? 'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE                                                              ? 'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER                                                                  ? 'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                             ? 'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE                                                                ? 'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE                                                                 ? 'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE                                                             ? 'C5 H11 N O2 S'     149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                          ? 'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE                                                                ? 'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE                                                                 ? 'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE                                                              ? 'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                             ? 'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE                                                               ? 'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE                                                                 ? 'C5 H11 N O2'       117.146 
# 
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   GLY 1   2   ?   ?   ?   A . n 
A 1 2   PRO 2   3   ?   ?   ?   A . n 
A 1 3   GLY 3   4   ?   ?   ?   A . n 
A 1 4   ALA 4   5   ?   ?   ?   A . n 
A 1 5   ASP 5   6   6   ASP ASP A . n 
A 1 6   SER 6   7   7   SER SER A . n 
A 1 7   CYS 7   8   8   CYS CYS A . n 
A 1 8   ILE 8   9   9   ILE ILE A . n 
A 1 9   GLN 9   10  10  GLN GLN A . n 
A 1 10  PHE 10  11  11  PHE PHE A . n 
A 1 11  THR 11  12  12  THR THR A . n 
A 1 12  ARG 12  13  13  ARG ARG A . n 
A 1 13  HIS 13  14  14  HIS HIS A . n 
A 1 14  ALA 14  15  15  ALA ALA A . n 
A 1 15  SER 15  16  16  SER SER A . n 
A 1 16  ASP 16  17  17  ASP ASP A . n 
A 1 17  VAL 17  18  18  VAL VAL A . n 
A 1 18  LEU 18  19  19  LEU LEU A . n 
A 1 19  LEU 19  20  20  LEU LEU A . n 
A 1 20  ASN 20  21  21  ASN ASN A . n 
A 1 21  LEU 21  22  22  LEU LEU A . n 
A 1 22  ASN 22  23  23  ASN ASN A . n 
A 1 23  ARG 23  24  24  ARG ARG A . n 
A 1 24  LEU 24  25  25  LEU LEU A . n 
A 1 25  ARG 25  26  26  ARG ARG A . n 
A 1 26  SER 26  27  27  SER SER A . n 
A 1 27  ARG 27  28  28  ARG ARG A . n 
A 1 28  ASP 28  29  29  ASP ASP A . n 
A 1 29  ILE 29  30  30  ILE ILE A . n 
A 1 30  LEU 30  31  31  LEU LEU A . n 
A 1 31  THR 31  32  32  THR THR A . n 
A 1 32  ASP 32  33  33  ASP ASP A . n 
A 1 33  VAL 33  34  34  VAL VAL A . n 
A 1 34  VAL 34  35  35  VAL VAL A . n 
A 1 35  ILE 35  36  36  ILE ILE A . n 
A 1 36  VAL 36  37  37  VAL VAL A . n 
A 1 37  VAL 37  38  38  VAL VAL A . n 
A 1 38  SER 38  39  39  SER SER A . n 
A 1 39  ARG 39  40  40  ARG ARG A . n 
A 1 40  GLU 40  41  41  GLU GLU A . n 
A 1 41  GLN 41  42  42  GLN GLN A . n 
A 1 42  PHE 42  43  43  PHE PHE A . n 
A 1 43  ARG 43  44  44  ARG ARG A . n 
A 1 44  ALA 44  45  45  ALA ALA A . n 
A 1 45  HIS 45  46  46  HIS HIS A . n 
A 1 46  LYS 46  47  47  LYS LYS A . n 
A 1 47  THR 47  48  48  THR THR A . n 
A 1 48  VAL 48  49  49  VAL VAL A . n 
A 1 49  LEU 49  50  50  LEU LEU A . n 
A 1 50  MET 50  51  51  MET MET A . n 
A 1 51  ALA 51  52  52  ALA ALA A . n 
A 1 52  CYS 52  53  53  CYS CYS A . n 
A 1 53  SER 53  54  54  SER SER A . n 
A 1 54  GLY 54  55  55  GLY GLY A . n 
A 1 55  LEU 55  56  56  LEU LEU A . n 
A 1 56  PHE 56  57  57  PHE PHE A . n 
A 1 57  TYR 57  58  58  TYR TYR A . n 
A 1 58  SER 58  59  59  SER SER A . n 
A 1 59  ILE 59  60  60  ILE ILE A . n 
A 1 60  PHE 60  61  61  PHE PHE A . n 
A 1 61  THR 61  62  62  THR THR A . n 
A 1 62  ASP 62  63  63  ASP ASP A . n 
A 1 63  GLN 63  64  64  GLN GLN A . n 
A 1 64  LEU 64  65  65  LEU LEU A . n 
A 1 65  LYS 65  66  66  LYS LYS A . n 
A 1 66  CYS 66  67  67  CYS CYS A . n 
A 1 67  ASN 67  68  68  ASN ASN A . n 
A 1 68  LEU 68  69  69  LEU LEU A . n 
A 1 69  SER 69  70  70  SER SER A . n 
A 1 70  VAL 70  71  71  VAL VAL A . n 
A 1 71  ILE 71  72  72  ILE ILE A . n 
A 1 72  ASN 72  73  73  ASN ASN A . n 
A 1 73  LEU 73  74  74  LEU LEU A . n 
A 1 74  ASP 74  75  75  ASP ASP A . n 
A 1 75  PRO 75  76  76  PRO PRO A . n 
A 1 76  GLU 76  77  77  GLU GLU A . n 
A 1 77  ILE 77  78  78  ILE ILE A . n 
A 1 78  ASN 78  79  79  ASN ASN A . n 
A 1 79  PRO 79  80  80  PRO PRO A . n 
A 1 80  GLU 80  81  81  GLU GLU A . n 
A 1 81  GLY 81  82  82  GLY GLY A . n 
A 1 82  PHE 82  83  83  PHE PHE A . n 
A 1 83  CYS 83  84  84  CYS CYS A . n 
A 1 84  ILE 84  85  85  ILE ILE A . n 
A 1 85  LEU 85  86  86  LEU LEU A . n 
A 1 86  LEU 86  87  87  LEU LEU A . n 
A 1 87  ASP 87  88  88  ASP ASP A . n 
A 1 88  PHE 88  89  89  PHE PHE A . n 
A 1 89  MET 89  90  90  MET MET A . n 
A 1 90  TYR 90  91  91  TYR TYR A . n 
A 1 91  THR 91  92  92  THR THR A . n 
A 1 92  SER 92  93  93  SER SER A . n 
A 1 93  ARG 93  94  94  ARG ARG A . n 
A 1 94  LEU 94  95  95  LEU LEU A . n 
A 1 95  ASN 95  96  96  ASN ASN A . n 
A 1 96  LEU 96  97  97  LEU LEU A . n 
A 1 97  ARG 97  98  98  ARG ARG A . n 
A 1 98  GLU 98  99  99  GLU GLU A . n 
A 1 99  GLY 99  100 100 GLY GLY A . n 
A 1 100 ASN 100 101 101 ASN ASN A . n 
A 1 101 ILE 101 102 102 ILE ILE A . n 
A 1 102 MET 102 103 103 MET MET A . n 
A 1 103 ALA 103 104 104 ALA ALA A . n 
A 1 104 VAL 104 105 105 VAL VAL A . n 
A 1 105 MET 105 106 106 MET MET A . n 
A 1 106 ALA 106 107 107 ALA ALA A . n 
A 1 107 THR 107 108 108 THR THR A . n 
A 1 108 ALA 108 109 109 ALA ALA A . n 
A 1 109 MET 109 110 110 MET MET A . n 
A 1 110 TYR 110 111 111 TYR TYR A . n 
A 1 111 LEU 111 112 112 LEU LEU A . n 
A 1 112 GLN 112 113 113 GLN GLN A . n 
A 1 113 MET 113 114 114 MET MET A . n 
A 1 114 GLU 114 115 115 GLU GLU A . n 
A 1 115 HIS 115 116 116 HIS HIS A . n 
A 1 116 VAL 116 117 117 VAL VAL A . n 
A 1 117 VAL 117 118 118 VAL VAL A . n 
A 1 118 ASP 118 119 119 ASP ASP A . n 
A 1 119 THR 119 120 120 THR THR A . n 
A 1 120 CYS 120 121 121 CYS CYS A . n 
A 1 121 ARG 121 122 122 ARG ARG A . n 
A 1 122 LYS 122 123 123 LYS LYS A . n 
A 1 123 PHE 123 124 124 PHE PHE A . n 
A 1 124 ILE 124 125 125 ILE ILE A . n 
A 1 125 LYS 125 126 126 LYS LYS A . n 
A 1 126 ALA 126 127 127 ALA ALA A . n 
A 1 127 SER 127 128 128 SER SER A . n 
A 1 128 GLU 128 129 129 GLU GLU A . n 
B 2 1   ACE 1   0   0   ACE ACE D . n 
B 2 2   TRP 2   1   1   TRP TRP D . n 
B 2 3   VAL 3   2   2   VAL VAL D . n 
B 2 4   ILE 4   3   3   ILE ILE D . n 
B 2 5   PRO 5   4   4   PRO PRO D . n 
B 2 6   ALA 6   5   5   ALA ALA D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 A1ACA 1   201 1   A1ACA 763 A . 
D 4 CL    1   202 1   CL    CL  A . 
E 5 DMS   1   101 1   DMS   DMS D . 
F 6 HOH   1   301 178 HOH   HOH A . 
F 6 HOH   2   302 7   HOH   HOH A . 
F 6 HOH   3   303 166 HOH   HOH A . 
F 6 HOH   4   304 140 HOH   HOH A . 
F 6 HOH   5   305 29  HOH   HOH A . 
F 6 HOH   6   306 19  HOH   HOH A . 
F 6 HOH   7   307 94  HOH   HOH A . 
F 6 HOH   8   308 45  HOH   HOH A . 
F 6 HOH   9   309 173 HOH   HOH A . 
F 6 HOH   10  310 202 HOH   HOH A . 
F 6 HOH   11  311 100 HOH   HOH A . 
F 6 HOH   12  312 106 HOH   HOH A . 
F 6 HOH   13  313 47  HOH   HOH A . 
F 6 HOH   14  314 90  HOH   HOH A . 
F 6 HOH   15  315 247 HOH   HOH A . 
F 6 HOH   16  316 99  HOH   HOH A . 
F 6 HOH   17  317 83  HOH   HOH A . 
F 6 HOH   18  318 179 HOH   HOH A . 
F 6 HOH   19  319 75  HOH   HOH A . 
F 6 HOH   20  320 84  HOH   HOH A . 
F 6 HOH   21  321 37  HOH   HOH A . 
F 6 HOH   22  322 142 HOH   HOH A . 
F 6 HOH   23  323 101 HOH   HOH A . 
F 6 HOH   24  324 193 HOH   HOH A . 
F 6 HOH   25  325 119 HOH   HOH A . 
F 6 HOH   26  326 87  HOH   HOH A . 
F 6 HOH   27  327 91  HOH   HOH A . 
F 6 HOH   28  328 132 HOH   HOH A . 
F 6 HOH   29  329 139 HOH   HOH A . 
F 6 HOH   30  330 27  HOH   HOH A . 
F 6 HOH   31  331 40  HOH   HOH A . 
F 6 HOH   32  332 237 HOH   HOH A . 
F 6 HOH   33  333 117 HOH   HOH A . 
F 6 HOH   34  334 14  HOH   HOH A . 
F 6 HOH   35  335 6   HOH   HOH A . 
F 6 HOH   36  336 242 HOH   HOH A . 
F 6 HOH   37  337 20  HOH   HOH A . 
F 6 HOH   38  338 243 HOH   HOH A . 
F 6 HOH   39  339 239 HOH   HOH A . 
F 6 HOH   40  340 4   HOH   HOH A . 
F 6 HOH   41  341 17  HOH   HOH A . 
F 6 HOH   42  342 196 HOH   HOH A . 
F 6 HOH   43  343 42  HOH   HOH A . 
F 6 HOH   44  344 144 HOH   HOH A . 
F 6 HOH   45  345 5   HOH   HOH A . 
F 6 HOH   46  346 44  HOH   HOH A . 
F 6 HOH   47  347 151 HOH   HOH A . 
F 6 HOH   48  348 34  HOH   HOH A . 
F 6 HOH   49  349 89  HOH   HOH A . 
F 6 HOH   50  350 50  HOH   HOH A . 
F 6 HOH   51  351 86  HOH   HOH A . 
F 6 HOH   52  352 85  HOH   HOH A . 
F 6 HOH   53  353 244 HOH   HOH A . 
F 6 HOH   54  354 96  HOH   HOH A . 
F 6 HOH   55  355 12  HOH   HOH A . 
F 6 HOH   56  356 175 HOH   HOH A . 
F 6 HOH   57  357 124 HOH   HOH A . 
F 6 HOH   58  358 51  HOH   HOH A . 
F 6 HOH   59  359 141 HOH   HOH A . 
F 6 HOH   60  360 97  HOH   HOH A . 
F 6 HOH   61  361 24  HOH   HOH A . 
F 6 HOH   62  362 30  HOH   HOH A . 
F 6 HOH   63  363 55  HOH   HOH A . 
F 6 HOH   64  364 93  HOH   HOH A . 
F 6 HOH   65  365 145 HOH   HOH A . 
F 6 HOH   66  366 103 HOH   HOH A . 
F 6 HOH   67  367 186 HOH   HOH A . 
F 6 HOH   68  368 131 HOH   HOH A . 
F 6 HOH   69  369 207 HOH   HOH A . 
F 6 HOH   70  370 15  HOH   HOH A . 
F 6 HOH   71  371 229 HOH   HOH A . 
F 6 HOH   72  372 177 HOH   HOH A . 
F 6 HOH   73  373 133 HOH   HOH A . 
F 6 HOH   74  374 180 HOH   HOH A . 
F 6 HOH   75  375 122 HOH   HOH A . 
F 6 HOH   76  376 170 HOH   HOH A . 
F 6 HOH   77  377 39  HOH   HOH A . 
F 6 HOH   78  378 192 HOH   HOH A . 
F 6 HOH   79  379 245 HOH   HOH A . 
F 6 HOH   80  380 169 HOH   HOH A . 
F 6 HOH   81  381 28  HOH   HOH A . 
F 6 HOH   82  382 21  HOH   HOH A . 
F 6 HOH   83  383 70  HOH   HOH A . 
F 6 HOH   84  384 105 HOH   HOH A . 
F 6 HOH   85  385 167 HOH   HOH A . 
F 6 HOH   86  386 25  HOH   HOH A . 
F 6 HOH   87  387 74  HOH   HOH A . 
F 6 HOH   88  388 76  HOH   HOH A . 
F 6 HOH   89  389 194 HOH   HOH A . 
F 6 HOH   90  390 16  HOH   HOH A . 
F 6 HOH   91  391 32  HOH   HOH A . 
F 6 HOH   92  392 191 HOH   HOH A . 
F 6 HOH   93  393 241 HOH   HOH A . 
F 6 HOH   94  394 22  HOH   HOH A . 
F 6 HOH   95  395 205 HOH   HOH A . 
F 6 HOH   96  396 212 HOH   HOH A . 
F 6 HOH   97  397 69  HOH   HOH A . 
F 6 HOH   98  398 165 HOH   HOH A . 
F 6 HOH   99  399 157 HOH   HOH A . 
F 6 HOH   100 400 108 HOH   HOH A . 
F 6 HOH   101 401 92  HOH   HOH A . 
F 6 HOH   102 402 64  HOH   HOH A . 
F 6 HOH   103 403 174 HOH   HOH A . 
F 6 HOH   104 404 35  HOH   HOH A . 
F 6 HOH   105 405 185 HOH   HOH A . 
F 6 HOH   106 406 82  HOH   HOH A . 
F 6 HOH   107 407 129 HOH   HOH A . 
F 6 HOH   108 408 43  HOH   HOH A . 
F 6 HOH   109 409 223 HOH   HOH A . 
F 6 HOH   110 410 176 HOH   HOH A . 
F 6 HOH   111 411 120 HOH   HOH A . 
F 6 HOH   112 412 67  HOH   HOH A . 
F 6 HOH   113 413 60  HOH   HOH A . 
F 6 HOH   114 414 215 HOH   HOH A . 
F 6 HOH   115 415 190 HOH   HOH A . 
F 6 HOH   116 416 26  HOH   HOH A . 
F 6 HOH   117 417 61  HOH   HOH A . 
F 6 HOH   118 418 36  HOH   HOH A . 
F 6 HOH   119 419 46  HOH   HOH A . 
F 6 HOH   120 420 88  HOH   HOH A . 
F 6 HOH   121 421 236 HOH   HOH A . 
F 6 HOH   122 422 110 HOH   HOH A . 
F 6 HOH   123 423 204 HOH   HOH A . 
F 6 HOH   124 424 56  HOH   HOH A . 
F 6 HOH   125 425 57  HOH   HOH A . 
F 6 HOH   126 426 68  HOH   HOH A . 
F 6 HOH   127 427 65  HOH   HOH A . 
F 6 HOH   128 428 95  HOH   HOH A . 
F 6 HOH   129 429 41  HOH   HOH A . 
F 6 HOH   130 430 116 HOH   HOH A . 
F 6 HOH   131 431 187 HOH   HOH A . 
F 6 HOH   132 432 147 HOH   HOH A . 
F 6 HOH   133 433 135 HOH   HOH A . 
F 6 HOH   134 434 168 HOH   HOH A . 
F 6 HOH   135 435 227 HOH   HOH A . 
F 6 HOH   136 436 214 HOH   HOH A . 
F 6 HOH   137 437 200 HOH   HOH A . 
F 6 HOH   138 438 248 HOH   HOH A . 
F 6 HOH   139 439 123 HOH   HOH A . 
F 6 HOH   140 440 228 HOH   HOH A . 
F 6 HOH   141 441 231 HOH   HOH A . 
F 6 HOH   142 442 63  HOH   HOH A . 
F 6 HOH   143 443 71  HOH   HOH A . 
F 6 HOH   144 444 225 HOH   HOH A . 
F 6 HOH   145 445 121 HOH   HOH A . 
F 6 HOH   146 446 171 HOH   HOH A . 
F 6 HOH   147 447 203 HOH   HOH A . 
F 6 HOH   148 448 234 HOH   HOH A . 
F 6 HOH   149 449 220 HOH   HOH A . 
F 6 HOH   150 450 114 HOH   HOH A . 
F 6 HOH   151 451 125 HOH   HOH A . 
F 6 HOH   152 452 238 HOH   HOH A . 
F 6 HOH   153 453 181 HOH   HOH A . 
F 6 HOH   154 454 158 HOH   HOH A . 
F 6 HOH   155 455 79  HOH   HOH A . 
F 6 HOH   156 456 217 HOH   HOH A . 
F 6 HOH   157 457 235 HOH   HOH A . 
F 6 HOH   158 458 246 HOH   HOH A . 
F 6 HOH   159 459 81  HOH   HOH A . 
F 6 HOH   160 460 221 HOH   HOH A . 
F 6 HOH   161 461 115 HOH   HOH A . 
F 6 HOH   162 462 107 HOH   HOH A . 
F 6 HOH   163 463 216 HOH   HOH A . 
F 6 HOH   164 464 230 HOH   HOH A . 
F 6 HOH   165 465 182 HOH   HOH A . 
F 6 HOH   166 466 188 HOH   HOH A . 
F 6 HOH   167 467 183 HOH   HOH A . 
F 6 HOH   168 468 201 HOH   HOH A . 
F 6 HOH   169 469 213 HOH   HOH A . 
F 6 HOH   170 470 148 HOH   HOH A . 
F 6 HOH   171 471 48  HOH   HOH A . 
F 6 HOH   172 472 113 HOH   HOH A . 
F 6 HOH   173 473 206 HOH   HOH A . 
F 6 HOH   174 474 172 HOH   HOH A . 
F 6 HOH   175 475 211 HOH   HOH A . 
G 6 HOH   1   201 62  HOH   HOH D . 
G 6 HOH   2   202 78  HOH   HOH D . 
G 6 HOH   3   203 23  HOH   HOH D . 
G 6 HOH   4   204 38  HOH   HOH D . 
G 6 HOH   5   205 53  HOH   HOH D . 
G 6 HOH   6   206 73  HOH   HOH D . 
G 6 HOH   7   207 240 HOH   HOH D . 
G 6 HOH   8   208 49  HOH   HOH D . 
G 6 HOH   9   209 58  HOH   HOH D . 
G 6 HOH   10  210 195 HOH   HOH D . 
# 
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 GLN 64  ? CD  ? A GLN 63  CD  
2  1 Y 1 A GLN 64  ? OE1 ? A GLN 63  OE1 
3  1 Y 1 A GLN 64  ? NE2 ? A GLN 63  NE2 
4  1 Y 1 A GLU 115 ? CD  ? A GLU 114 CD  
5  1 Y 1 A GLU 115 ? OE1 ? A GLU 114 OE1 
6  1 Y 1 A GLU 115 ? OE2 ? A GLU 114 OE2 
7  1 Y 1 A LYS 126 ? CG  ? A LYS 125 CG  
8  1 Y 1 A LYS 126 ? CD  ? A LYS 125 CD  
9  1 Y 1 A LYS 126 ? CE  ? A LYS 125 CE  
10 1 Y 1 A LYS 126 ? NZ  ? A LYS 125 NZ  
11 1 Y 1 D ALA 5   ? CA  ? B ALA 6   CA  
12 1 Y 1 D ALA 5   ? C   ? B ALA 6   C   
13 1 Y 1 D ALA 5   ? O   ? B ALA 6   O   
14 1 Y 1 D ALA 5   ? CB  ? B ALA 6   CB  
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
4 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com phasing           
http://www.globalphasing.com/buster/                ?   ? 
5 PDB_EXTRACT 3.24   'Sep. 1, 2017' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.entry_id           7GUX 
_cell.length_a           67.610 
_cell.length_b           67.610 
_cell.length_c           166.570 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        120.000 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7GUX 
_symmetry.Int_Tables_number                178 
_symmetry.space_group_name_H-M             'P 61 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.entry_id          7GUX 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.63 
_exptl_crystal.density_percent_sol   66.09 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    '1.0 M K2HPO4, 0.7 M NaH2PO4, 75 mM sodium acetate pH 4.5, 2% DMSO' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2017-07-31 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9686 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I24' 
_diffrn_source.pdbx_wavelength_list        0.9686 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7GUX 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.940 
_reflns.d_resolution_high            1.750 
_reflns.number_obs                   23650 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.067 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15.100 
_reflns.B_iso_Wilson_estimate        30.950 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.071 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     214786 
_reflns.pdbx_scaling_rejects         1202 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 1.750 1.780  ? 12037 1290 ? 1.536 ? ? ? 9.300 ? 1.800  ? ? ? ? ? ? 100.000 1.623 0.521 0.684 ? 
1 2 9.090 33.940 ? 1496  228  ? 0.033 ? ? ? 6.600 ? 40.200 ? ? ? ? ? ? 98.800  0.036 0.013 0.998 ? 
# 
_refine.entry_id                                 7GUX 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.7500 
_refine.ls_d_res_low                             33.9400 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    100.0000 
_refine.ls_number_reflns_obs                     23585 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1810 
_refine.ls_R_factor_R_work                       0.1800 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2040 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1400 
_refine.ls_number_reflns_R_free                  1212 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               35.0800 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.0793 
_refine.aniso_B[2][2]                            0.0793 
_refine.aniso_B[3][3]                            -0.1587 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9610 
_refine.correlation_coeff_Fo_to_Fc_free          0.9440 
_refine.overall_SU_R_Cruickshank_DPI             0.0870 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0860 
_refine.pdbx_overall_SU_R_Blow_DPI               0.0990 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.0950 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                123.420 
_refine.B_iso_min                                17.070 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_analyze.entry_id                        7GUX 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.230 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.7500 
_refine_hist.d_res_low                        33.9400 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.number_atoms_solvent             185 
_refine_hist.number_atoms_total               1231 
_refine_hist.pdbx_number_residues_total       130 
_refine_hist.pdbx_B_iso_mean_ligand           30.02 
_refine_hist.pdbx_B_iso_mean_solvent          52.01 
_refine_hist.pdbx_number_atoms_protein        1022 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' t_dihedral_angle_d        445  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              235  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1233 ?      ? 20.000 HARMONIC     
'X-RAY DIFFRACTION' t_nbd                     ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_improper_torsion        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_pseud_angle             ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_chiral_improper_torsion 162  ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_sum_occupancies         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_distance        8    ?      ? 1.000  HARMONIC     
'X-RAY DIFFRACTION' t_utility_angle           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_torsion         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_ideal_dist_contact      1651 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1233 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1689 0.880  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.330  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    14.600 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       1.7500 
_refine_ls_shell.d_res_low                        1.8300 
_refine_ls_shell.pdbx_total_number_of_bins_used   12 
_refine_ls_shell.percent_reflns_obs               99.8900 
_refine_ls_shell.number_reflns_R_work             2699 
_refine_ls_shell.R_factor_all                     0.3415 
_refine_ls_shell.R_factor_R_work                  0.3417 
_refine_ls_shell.R_factor_R_free                  0.3356 
_refine_ls_shell.percent_reflns_R_free            4.4900 
_refine_ls_shell.number_reflns_R_free             127 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2826 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUX 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 at 7.50 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUX 
_struct_keywords.text            'transcription factor, radiation damage, ligand, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
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 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP BCL6_HUMAN P41182 ? 1 
;ADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPEGFC
ILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
5 
2 PDB 7GUX       7GUX   ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7GUX A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUX D 1 ? 6   ? 7GUX   0 ? 5   ? 0 5   
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7GUX GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUX PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUX GLY A 3 ? UNP P41182 ? ? 'expression tag' 4 3 
# 
_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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 7390  ? 
1 MORE         -64   ? 
1 'SSA (A^2)'  12970 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z          1.0000000000 0.0000000000 0.0000000000 0.0000000000  0.0000000000 
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 12_545 x,x-y-1,-z+1/6 0.5000000000 0.8660254038 0.0000000000 33.8050000000 0.8660254038 
-0.5000000000 0.0000000000 -58.5519775499 0.0000000000 0.0000000000 -1.0000000000 27.7616666667 
# 
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 ARG A 12  ? ARG A 27  ? ARG A 13  ARG A 28  1 ? 16 
HELX_P HELX_P2 AA2 HIS A 45  ? SER A 53  ? HIS A 46  SER A 54  1 ? 9  
HELX_P HELX_P3 AA3 SER A 53  ? THR A 61  ? SER A 54  THR A 62  1 ? 9  
HELX_P HELX_P4 AA4 LEU A 64  ? LEU A 68  ? LEU A 65  LEU A 69  5 ? 5  
HELX_P HELX_P5 AA5 ASN A 78  ? SER A 92  ? ASN A 79  SER A 93  1 ? 15 
HELX_P HELX_P6 AA6 ASN A 100 ? GLN A 112 ? ASN A 101 GLN A 113 1 ? 13 
HELX_P HELX_P7 AA7 MET A 113 ? GLU A 128 ? MET A 114 GLU A 129 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N A ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 ACE B 1 ? TRP B 2 A ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
2 ACE B 1 ? TRP B 2 B ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_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 ? 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 GLU A 40 ? ALA A 44 ? GLU A 41 ALA A 45 
AA1 2 VAL A 33 ? VAL A 37 ? VAL A 34 VAL A 38 
AA1 3 VAL A 70 ? ASN A 72 ? VAL A 71 ASN 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 42 ? O PHE A 43 N ILE A 35 ? N ILE A 36 
AA1 2 3 N VAL A 36 ? N VAL A 37 O ILE A 71 ? O ILE A 72 
# 
_pdbx_entry_details.entry_id                   7GUX 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 39  ? A 61.91 -118.00 
2 1 SER A 39  ? B 38.95 65.65   
3 1 ARG A 40  ? B 74.88 -23.43  
4 1 SER A 93  ? A 76.27 -3.09   
5 1 GLN A 113 ? ? 62.32 60.29   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 376 ? F HOH . 
2 1 A HOH 380 ? F HOH . 
3 1 A HOH 457 ? F HOH . 
4 1 A HOH 464 ? F HOH . 
5 1 A HOH 467 ? F HOH . 
6 1 A HOH 468 ? F HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 29.2144 -16.5503 24.6837 0.0161  -0.0478 -0.0738 -0.0421 0.0289  -0.0213 0.9698 1.7105  1.9196 
0.4179 -0.3121 1.1369 0.1333 -0.0701 -0.0631 -0.0505 0.1022 0.0893 0.2367  -0.0101 -0.0054 
'X-RAY DIFFRACTION' 2 ? refined 18.9076 -32.4261 1.8469  -0.1134 0.1276  -0.0487 -0.0368 -0.0088 -0.0851 1.0111 -0.2973 0.0000 
0.0344 0.0132  0.4170 0.0288 -0.0121 -0.0167 -0.0152 0.0059 0.0379 -0.0269 0.0095  -0.0073 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 6 A 129 '{A|6 - 129}' ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 D 1 D 5   '{D|1 - 5}'   ? ? ? ? ? 
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY 2 ? A GLY 1 
2 1 Y 1 A PRO 3 ? A PRO 2 
3 1 Y 1 A GLY 4 ? A GLY 3 
4 1 Y 1 A ALA 5 ? A ALA 4 
# 
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 
A1ACA C4   C  Y N 1   
A1ACA C5   C  Y N 2   
A1ACA C6   C  Y N 3   
A1ACA C7   C  Y N 4   
A1ACA C8   C  N N 5   
A1ACA C10  C  Y N 6   
A1ACA C1   C  Y N 7   
A1ACA C2   C  Y N 8   
A1ACA C3   C  Y N 9   
A1ACA C9   C  N N 10  
A1ACA O    O  N N 11  
A1ACA N2   N  N N 12  
A1ACA C11  C  Y N 13  
A1ACA N1   N  N N 14  
A1ACA N3   N  Y N 15  
A1ACA C    C  Y N 16  
A1ACA CL   CL N N 17  
A1ACA BR   BR N N 18  
A1ACA N    N  Y N 19  
A1ACA H1   H  N N 20  
A1ACA H2   H  N N 21  
A1ACA H3   H  N N 22  
A1ACA H4   H  N N 23  
A1ACA H5   H  N N 24  
A1ACA H6   H  N N 25  
A1ACA H7   H  N N 26  
A1ACA H8   H  N N 27  
ACE   C    C  N N 28  
ACE   O    O  N N 29  
ACE   CH3  C  N N 30  
ACE   H    H  N N 31  
ACE   H1   H  N N 32  
ACE   H2   H  N N 33  
ACE   H3   H  N N 34  
ALA   N    N  N N 35  
ALA   CA   C  N S 36  
ALA   C    C  N N 37  
ALA   O    O  N N 38  
ALA   CB   C  N N 39  
ALA   OXT  O  N N 40  
ALA   H    H  N N 41  
ALA   H2   H  N N 42  
ALA   HA   H  N N 43  
ALA   HB1  H  N N 44  
ALA   HB2  H  N N 45  
ALA   HB3  H  N N 46  
ALA   HXT  H  N N 47  
ARG   N    N  N N 48  
ARG   CA   C  N S 49  
ARG   C    C  N N 50  
ARG   O    O  N N 51  
ARG   CB   C  N N 52  
ARG   CG   C  N N 53  
ARG   CD   C  N N 54  
ARG   NE   N  N N 55  
ARG   CZ   C  N N 56  
ARG   NH1  N  N N 57  
ARG   NH2  N  N N 58  
ARG   OXT  O  N N 59  
ARG   H    H  N N 60  
ARG   H2   H  N N 61  
ARG   HA   H  N N 62  
ARG   HB2  H  N N 63  
ARG   HB3  H  N N 64  
ARG   HG2  H  N N 65  
ARG   HG3  H  N N 66  
ARG   HD2  H  N N 67  
ARG   HD3  H  N N 68  
ARG   HE   H  N N 69  
ARG   HH11 H  N N 70  
ARG   HH12 H  N N 71  
ARG   HH21 H  N N 72  
ARG   HH22 H  N N 73  
ARG   HXT  H  N N 74  
ASN   N    N  N N 75  
ASN   CA   C  N S 76  
ASN   C    C  N N 77  
ASN   O    O  N N 78  
ASN   CB   C  N N 79  
ASN   CG   C  N N 80  
ASN   OD1  O  N N 81  
ASN   ND2  N  N N 82  
ASN   OXT  O  N N 83  
ASN   H    H  N N 84  
ASN   H2   H  N N 85  
ASN   HA   H  N N 86  
ASN   HB2  H  N N 87  
ASN   HB3  H  N N 88  
ASN   HD21 H  N N 89  
ASN   HD22 H  N N 90  
ASN   HXT  H  N N 91  
ASP   N    N  N N 92  
ASP   CA   C  N S 93  
ASP   C    C  N N 94  
ASP   O    O  N N 95  
ASP   CB   C  N N 96  
ASP   CG   C  N N 97  
ASP   OD1  O  N N 98  
ASP   OD2  O  N N 99  
ASP   OXT  O  N N 100 
ASP   H    H  N N 101 
ASP   H2   H  N N 102 
ASP   HA   H  N N 103 
ASP   HB2  H  N N 104 
ASP   HB3  H  N N 105 
ASP   HD2  H  N N 106 
ASP   HXT  H  N N 107 
CL    CL   CL N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
DMS   S    S  N N 123 
DMS   O    O  N N 124 
DMS   C1   C  N N 125 
DMS   C2   C  N N 126 
DMS   H11  H  N N 127 
DMS   H12  H  N N 128 
DMS   H13  H  N N 129 
DMS   H21  H  N N 130 
DMS   H22  H  N N 131 
DMS   H23  H  N N 132 
GLN   N    N  N N 133 
GLN   CA   C  N S 134 
GLN   C    C  N N 135 
GLN   O    O  N N 136 
GLN   CB   C  N N 137 
GLN   CG   C  N N 138 
GLN   CD   C  N N 139 
GLN   OE1  O  N N 140 
GLN   NE2  N  N N 141 
GLN   OXT  O  N N 142 
GLN   H    H  N N 143 
GLN   H2   H  N N 144 
GLN   HA   H  N N 145 
GLN   HB2  H  N N 146 
GLN   HB3  H  N N 147 
GLN   HG2  H  N N 148 
GLN   HG3  H  N N 149 
GLN   HE21 H  N N 150 
GLN   HE22 H  N N 151 
GLN   HXT  H  N N 152 
GLU   N    N  N N 153 
GLU   CA   C  N S 154 
GLU   C    C  N N 155 
GLU   O    O  N N 156 
GLU   CB   C  N N 157 
GLU   CG   C  N N 158 
GLU   CD   C  N N 159 
GLU   OE1  O  N N 160 
GLU   OE2  O  N N 161 
GLU   OXT  O  N N 162 
GLU   H    H  N N 163 
GLU   H2   H  N N 164 
GLU   HA   H  N N 165 
GLU   HB2  H  N N 166 
GLU   HB3  H  N N 167 
GLU   HG2  H  N N 168 
GLU   HG3  H  N N 169 
GLU   HE2  H  N N 170 
GLU   HXT  H  N N 171 
GLY   N    N  N N 172 
GLY   CA   C  N N 173 
GLY   C    C  N N 174 
GLY   O    O  N N 175 
GLY   OXT  O  N N 176 
GLY   H    H  N N 177 
GLY   H2   H  N N 178 
GLY   HA2  H  N N 179 
GLY   HA3  H  N N 180 
GLY   HXT  H  N N 181 
HIS   N    N  N N 182 
HIS   CA   C  N S 183 
HIS   C    C  N N 184 
HIS   O    O  N N 185 
HIS   CB   C  N N 186 
HIS   CG   C  Y N 187 
HIS   ND1  N  Y N 188 
HIS   CD2  C  Y N 189 
HIS   CE1  C  Y N 190 
HIS   NE2  N  Y N 191 
HIS   OXT  O  N N 192 
HIS   H    H  N N 193 
HIS   H2   H  N N 194 
HIS   HA   H  N N 195 
HIS   HB2  H  N N 196 
HIS   HB3  H  N N 197 
HIS   HD1  H  N N 198 
HIS   HD2  H  N N 199 
HIS   HE1  H  N N 200 
HIS   HE2  H  N N 201 
HIS   HXT  H  N N 202 
HOH   O    O  N N 203 
HOH   H1   H  N N 204 
HOH   H2   H  N N 205 
ILE   N    N  N N 206 
ILE   CA   C  N S 207 
ILE   C    C  N N 208 
ILE   O    O  N N 209 
ILE   CB   C  N S 210 
ILE   CG1  C  N N 211 
ILE   CG2  C  N N 212 
ILE   CD1  C  N N 213 
ILE   OXT  O  N N 214 
ILE   H    H  N N 215 
ILE   H2   H  N N 216 
ILE   HA   H  N N 217 
ILE   HB   H  N N 218 
ILE   HG12 H  N N 219 
ILE   HG13 H  N N 220 
ILE   HG21 H  N N 221 
ILE   HG22 H  N N 222 
ILE   HG23 H  N N 223 
ILE   HD11 H  N N 224 
ILE   HD12 H  N N 225 
ILE   HD13 H  N N 226 
ILE   HXT  H  N N 227 
LEU   N    N  N N 228 
LEU   CA   C  N S 229 
LEU   C    C  N N 230 
LEU   O    O  N N 231 
LEU   CB   C  N N 232 
LEU   CG   C  N N 233 
LEU   CD1  C  N N 234 
LEU   CD2  C  N N 235 
LEU   OXT  O  N N 236 
LEU   H    H  N N 237 
LEU   H2   H  N N 238 
LEU   HA   H  N N 239 
LEU   HB2  H  N N 240 
LEU   HB3  H  N N 241 
LEU   HG   H  N N 242 
LEU   HD11 H  N N 243 
LEU   HD12 H  N N 244 
LEU   HD13 H  N N 245 
LEU   HD21 H  N N 246 
LEU   HD22 H  N N 247 
LEU   HD23 H  N N 248 
LEU   HXT  H  N N 249 
LYS   N    N  N N 250 
LYS   CA   C  N S 251 
LYS   C    C  N N 252 
LYS   O    O  N N 253 
LYS   CB   C  N N 254 
LYS   CG   C  N N 255 
LYS   CD   C  N N 256 
LYS   CE   C  N N 257 
LYS   NZ   N  N N 258 
LYS   OXT  O  N N 259 
LYS   H    H  N N 260 
LYS   H2   H  N N 261 
LYS   HA   H  N N 262 
LYS   HB2  H  N N 263 
LYS   HB3  H  N N 264 
LYS   HG2  H  N N 265 
LYS   HG3  H  N N 266 
LYS   HD2  H  N N 267 
LYS   HD3  H  N N 268 
LYS   HE2  H  N N 269 
LYS   HE3  H  N N 270 
LYS   HZ1  H  N N 271 
LYS   HZ2  H  N N 272 
LYS   HZ3  H  N N 273 
LYS   HXT  H  N N 274 
MET   N    N  N N 275 
MET   CA   C  N S 276 
MET   C    C  N N 277 
MET   O    O  N N 278 
MET   CB   C  N N 279 
MET   CG   C  N N 280 
MET   SD   S  N N 281 
MET   CE   C  N N 282 
MET   OXT  O  N N 283 
MET   H    H  N N 284 
MET   H2   H  N N 285 
MET   HA   H  N N 286 
MET   HB2  H  N N 287 
MET   HB3  H  N N 288 
MET   HG2  H  N N 289 
MET   HG3  H  N N 290 
MET   HE1  H  N N 291 
MET   HE2  H  N N 292 
MET   HE3  H  N N 293 
MET   HXT  H  N N 294 
PHE   N    N  N N 295 
PHE   CA   C  N S 296 
PHE   C    C  N N 297 
PHE   O    O  N N 298 
PHE   CB   C  N N 299 
PHE   CG   C  Y N 300 
PHE   CD1  C  Y N 301 
PHE   CD2  C  Y N 302 
PHE   CE1  C  Y N 303 
PHE   CE2  C  Y N 304 
PHE   CZ   C  Y N 305 
PHE   OXT  O  N N 306 
PHE   H    H  N N 307 
PHE   H2   H  N N 308 
PHE   HA   H  N N 309 
PHE   HB2  H  N N 310 
PHE   HB3  H  N N 311 
PHE   HD1  H  N N 312 
PHE   HD2  H  N N 313 
PHE   HE1  H  N N 314 
PHE   HE2  H  N N 315 
PHE   HZ   H  N N 316 
PHE   HXT  H  N N 317 
PRO   N    N  N N 318 
PRO   CA   C  N S 319 
PRO   C    C  N N 320 
PRO   O    O  N N 321 
PRO   CB   C  N N 322 
PRO   CG   C  N N 323 
PRO   CD   C  N N 324 
PRO   OXT  O  N N 325 
PRO   H    H  N N 326 
PRO   HA   H  N N 327 
PRO   HB2  H  N N 328 
PRO   HB3  H  N N 329 
PRO   HG2  H  N N 330 
PRO   HG3  H  N N 331 
PRO   HD2  H  N N 332 
PRO   HD3  H  N N 333 
PRO   HXT  H  N N 334 
SER   N    N  N N 335 
SER   CA   C  N S 336 
SER   C    C  N N 337 
SER   O    O  N N 338 
SER   CB   C  N N 339 
SER   OG   O  N N 340 
SER   OXT  O  N N 341 
SER   H    H  N N 342 
SER   H2   H  N N 343 
SER   HA   H  N N 344 
SER   HB2  H  N N 345 
SER   HB3  H  N N 346 
SER   HG   H  N N 347 
SER   HXT  H  N N 348 
THR   N    N  N N 349 
THR   CA   C  N S 350 
THR   C    C  N N 351 
THR   O    O  N N 352 
THR   CB   C  N R 353 
THR   OG1  O  N N 354 
THR   CG2  C  N N 355 
THR   OXT  O  N N 356 
THR   H    H  N N 357 
THR   H2   H  N N 358 
THR   HA   H  N N 359 
THR   HB   H  N N 360 
THR   HG1  H  N N 361 
THR   HG21 H  N N 362 
THR   HG22 H  N N 363 
THR   HG23 H  N N 364 
THR   HXT  H  N N 365 
TRP   N    N  N N 366 
TRP   CA   C  N S 367 
TRP   C    C  N N 368 
TRP   O    O  N N 369 
TRP   CB   C  N N 370 
TRP   CG   C  Y N 371 
TRP   CD1  C  Y N 372 
TRP   CD2  C  Y N 373 
TRP   NE1  N  Y N 374 
TRP   CE2  C  Y N 375 
TRP   CE3  C  Y N 376 
TRP   CZ2  C  Y N 377 
TRP   CZ3  C  Y N 378 
TRP   CH2  C  Y N 379 
TRP   OXT  O  N N 380 
TRP   H    H  N N 381 
TRP   H2   H  N N 382 
TRP   HA   H  N N 383 
TRP   HB2  H  N N 384 
TRP   HB3  H  N N 385 
TRP   HD1  H  N N 386 
TRP   HE1  H  N N 387 
TRP   HE3  H  N N 388 
TRP   HZ2  H  N N 389 
TRP   HZ3  H  N N 390 
TRP   HH2  H  N N 391 
TRP   HXT  H  N N 392 
TYR   N    N  N N 393 
TYR   CA   C  N S 394 
TYR   C    C  N N 395 
TYR   O    O  N N 396 
TYR   CB   C  N N 397 
TYR   CG   C  Y N 398 
TYR   CD1  C  Y N 399 
TYR   CD2  C  Y N 400 
TYR   CE1  C  Y N 401 
TYR   CE2  C  Y N 402 
TYR   CZ   C  Y N 403 
TYR   OH   O  N N 404 
TYR   OXT  O  N N 405 
TYR   H    H  N N 406 
TYR   H2   H  N N 407 
TYR   HA   H  N N 408 
TYR   HB2  H  N N 409 
TYR   HB3  H  N N 410 
TYR   HD1  H  N N 411 
TYR   HD2  H  N N 412 
TYR   HE1  H  N N 413 
TYR   HE2  H  N N 414 
TYR   HH   H  N N 415 
TYR   HXT  H  N N 416 
VAL   N    N  N N 417 
VAL   CA   C  N S 418 
VAL   C    C  N N 419 
VAL   O    O  N N 420 
VAL   CB   C  N N 421 
VAL   CG1  C  N N 422 
VAL   CG2  C  N N 423 
VAL   OXT  O  N N 424 
VAL   H    H  N N 425 
VAL   H2   H  N N 426 
VAL   HA   H  N N 427 
VAL   HB   H  N N 428 
VAL   HG11 H  N N 429 
VAL   HG12 H  N N 430 
VAL   HG13 H  N N 431 
VAL   HG21 H  N N 432 
VAL   HG22 H  N N 433 
VAL   HG23 H  N N 434 
VAL   HXT  H  N N 435 
# 
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 
A1ACA N   C1   doub Y N 1   
A1ACA N   C    sing Y N 2   
A1ACA CL  C    sing N N 3   
A1ACA C1  C2   sing Y N 4   
A1ACA C   N3   doub Y N 5   
A1ACA C2  BR   sing N N 6   
A1ACA C2  C3   doub Y N 7   
A1ACA N3  C3   sing Y N 8   
A1ACA C3  N1   sing N N 9   
A1ACA N1  C4   sing N N 10  
A1ACA C4  C5   doub Y N 11  
A1ACA C4  C11  sing Y N 12  
A1ACA C5  C6   sing Y N 13  
A1ACA C11 C10  doub Y N 14  
A1ACA C6  C7   doub Y N 15  
A1ACA C10 C7   sing Y N 16  
A1ACA C10 C9   sing N N 17  
A1ACA C7  N2   sing N N 18  
A1ACA C9  C8   sing N N 19  
A1ACA N2  C8   sing N N 20  
A1ACA C8  O    doub N N 21  
A1ACA C5  H1   sing N N 22  
A1ACA C6  H2   sing N N 23  
A1ACA C1  H3   sing N N 24  
A1ACA C9  H4   sing N N 25  
A1ACA C9  H5   sing N N 26  
A1ACA N2  H6   sing N N 27  
A1ACA C11 H7   sing N N 28  
A1ACA N1  H8   sing N N 29  
ACE   C   O    doub N N 30  
ACE   C   CH3  sing N N 31  
ACE   C   H    sing N N 32  
ACE   CH3 H1   sing N N 33  
ACE   CH3 H2   sing N N 34  
ACE   CH3 H3   sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
DMS   S   O    doub N N 118 
DMS   S   C1   sing N N 119 
DMS   S   C2   sing N N 120 
DMS   C1  H11  sing N N 121 
DMS   C1  H12  sing N N 122 
DMS   C1  H13  sing N N 123 
DMS   C2  H21  sing N N 124 
DMS   C2  H22  sing N N 125 
DMS   C2  H23  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
HIS   N   CA   sing N N 173 
HIS   N   H    sing N N 174 
HIS   N   H2   sing N N 175 
HIS   CA  C    sing N N 176 
HIS   CA  CB   sing N N 177 
HIS   CA  HA   sing N N 178 
HIS   C   O    doub N N 179 
HIS   C   OXT  sing N N 180 
HIS   CB  CG   sing N N 181 
HIS   CB  HB2  sing N N 182 
HIS   CB  HB3  sing N N 183 
HIS   CG  ND1  sing Y N 184 
HIS   CG  CD2  doub Y N 185 
HIS   ND1 CE1  doub Y N 186 
HIS   ND1 HD1  sing N N 187 
HIS   CD2 NE2  sing Y N 188 
HIS   CD2 HD2  sing N N 189 
HIS   CE1 NE2  sing Y N 190 
HIS   CE1 HE1  sing N N 191 
HIS   NE2 HE2  sing N N 192 
HIS   OXT HXT  sing N N 193 
HOH   O   H1   sing N N 194 
HOH   O   H2   sing N N 195 
ILE   N   CA   sing N N 196 
ILE   N   H    sing N N 197 
ILE   N   H2   sing N N 198 
ILE   CA  C    sing N N 199 
ILE   CA  CB   sing N N 200 
ILE   CA  HA   sing N N 201 
ILE   C   O    doub N N 202 
ILE   C   OXT  sing N N 203 
ILE   CB  CG1  sing N N 204 
ILE   CB  CG2  sing N N 205 
ILE   CB  HB   sing N N 206 
ILE   CG1 CD1  sing N N 207 
ILE   CG1 HG12 sing N N 208 
ILE   CG1 HG13 sing N N 209 
ILE   CG2 HG21 sing N N 210 
ILE   CG2 HG22 sing N N 211 
ILE   CG2 HG23 sing N N 212 
ILE   CD1 HD11 sing N N 213 
ILE   CD1 HD12 sing N N 214 
ILE   CD1 HD13 sing N N 215 
ILE   OXT HXT  sing N N 216 
LEU   N   CA   sing N N 217 
LEU   N   H    sing N N 218 
LEU   N   H2   sing N N 219 
LEU   CA  C    sing N N 220 
LEU   CA  CB   sing N N 221 
LEU   CA  HA   sing N N 222 
LEU   C   O    doub N N 223 
LEU   C   OXT  sing N N 224 
LEU   CB  CG   sing N N 225 
LEU   CB  HB2  sing N N 226 
LEU   CB  HB3  sing N N 227 
LEU   CG  CD1  sing N N 228 
LEU   CG  CD2  sing N N 229 
LEU   CG  HG   sing N N 230 
LEU   CD1 HD11 sing N N 231 
LEU   CD1 HD12 sing N N 232 
LEU   CD1 HD13 sing N N 233 
LEU   CD2 HD21 sing N N 234 
LEU   CD2 HD22 sing N N 235 
LEU   CD2 HD23 sing N N 236 
LEU   OXT HXT  sing N N 237 
LYS   N   CA   sing N N 238 
LYS   N   H    sing N N 239 
LYS   N   H2   sing N N 240 
LYS   CA  C    sing N N 241 
LYS   CA  CB   sing N N 242 
LYS   CA  HA   sing N N 243 
LYS   C   O    doub N N 244 
LYS   C   OXT  sing N N 245 
LYS   CB  CG   sing N N 246 
LYS   CB  HB2  sing N N 247 
LYS   CB  HB3  sing N N 248 
LYS   CG  CD   sing N N 249 
LYS   CG  HG2  sing N N 250 
LYS   CG  HG3  sing N N 251 
LYS   CD  CE   sing N N 252 
LYS   CD  HD2  sing N N 253 
LYS   CD  HD3  sing N N 254 
LYS   CE  NZ   sing N N 255 
LYS   CE  HE2  sing N N 256 
LYS   CE  HE3  sing N N 257 
LYS   NZ  HZ1  sing N N 258 
LYS   NZ  HZ2  sing N N 259 
LYS   NZ  HZ3  sing N N 260 
LYS   OXT HXT  sing N N 261 
MET   N   CA   sing N N 262 
MET   N   H    sing N N 263 
MET   N   H2   sing N N 264 
MET   CA  C    sing N N 265 
MET   CA  CB   sing N N 266 
MET   CA  HA   sing N N 267 
MET   C   O    doub N N 268 
MET   C   OXT  sing N N 269 
MET   CB  CG   sing N N 270 
MET   CB  HB2  sing N N 271 
MET   CB  HB3  sing N N 272 
MET   CG  SD   sing N N 273 
MET   CG  HG2  sing N N 274 
MET   CG  HG3  sing N N 275 
MET   SD  CE   sing N N 276 
MET   CE  HE1  sing N N 277 
MET   CE  HE2  sing N N 278 
MET   CE  HE3  sing N N 279 
MET   OXT HXT  sing N N 280 
PHE   N   CA   sing N N 281 
PHE   N   H    sing N N 282 
PHE   N   H2   sing N N 283 
PHE   CA  C    sing N N 284 
PHE   CA  CB   sing N N 285 
PHE   CA  HA   sing N N 286 
PHE   C   O    doub N N 287 
PHE   C   OXT  sing N N 288 
PHE   CB  CG   sing N N 289 
PHE   CB  HB2  sing N N 290 
PHE   CB  HB3  sing N N 291 
PHE   CG  CD1  doub Y N 292 
PHE   CG  CD2  sing Y N 293 
PHE   CD1 CE1  sing Y N 294 
PHE   CD1 HD1  sing N N 295 
PHE   CD2 CE2  doub Y N 296 
PHE   CD2 HD2  sing N N 297 
PHE   CE1 CZ   doub Y N 298 
PHE   CE1 HE1  sing N N 299 
PHE   CE2 CZ   sing Y N 300 
PHE   CE2 HE2  sing N N 301 
PHE   CZ  HZ   sing N N 302 
PHE   OXT HXT  sing N N 303 
PRO   N   CA   sing N N 304 
PRO   N   CD   sing N N 305 
PRO   N   H    sing N N 306 
PRO   CA  C    sing N N 307 
PRO   CA  CB   sing N N 308 
PRO   CA  HA   sing N N 309 
PRO   C   O    doub N N 310 
PRO   C   OXT  sing N N 311 
PRO   CB  CG   sing N N 312 
PRO   CB  HB2  sing N N 313 
PRO   CB  HB3  sing N N 314 
PRO   CG  CD   sing N N 315 
PRO   CG  HG2  sing N N 316 
PRO   CG  HG3  sing N N 317 
PRO   CD  HD2  sing N N 318 
PRO   CD  HD3  sing N N 319 
PRO   OXT HXT  sing N N 320 
SER   N   CA   sing N N 321 
SER   N   H    sing N N 322 
SER   N   H2   sing N N 323 
SER   CA  C    sing N N 324 
SER   CA  CB   sing N N 325 
SER   CA  HA   sing N N 326 
SER   C   O    doub N N 327 
SER   C   OXT  sing N N 328 
SER   CB  OG   sing N N 329 
SER   CB  HB2  sing N N 330 
SER   CB  HB3  sing N N 331 
SER   OG  HG   sing N N 332 
SER   OXT HXT  sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TRP   N   CA   sing N N 350 
TRP   N   H    sing N N 351 
TRP   N   H2   sing N N 352 
TRP   CA  C    sing N N 353 
TRP   CA  CB   sing N N 354 
TRP   CA  HA   sing N N 355 
TRP   C   O    doub N N 356 
TRP   C   OXT  sing N N 357 
TRP   CB  CG   sing N N 358 
TRP   CB  HB2  sing N N 359 
TRP   CB  HB3  sing N N 360 
TRP   CG  CD1  doub Y N 361 
TRP   CG  CD2  sing Y N 362 
TRP   CD1 NE1  sing Y N 363 
TRP   CD1 HD1  sing N N 364 
TRP   CD2 CE2  doub Y N 365 
TRP   CD2 CE3  sing Y N 366 
TRP   NE1 CE2  sing Y N 367 
TRP   NE1 HE1  sing N N 368 
TRP   CE2 CZ2  sing Y N 369 
TRP   CE3 CZ3  doub Y N 370 
TRP   CE3 HE3  sing N N 371 
TRP   CZ2 CH2  doub Y N 372 
TRP   CZ2 HZ2  sing N N 373 
TRP   CZ3 CH2  sing Y N 374 
TRP   CZ3 HZ3  sing N N 375 
TRP   CH2 HH2  sing N N 376 
TRP   OXT HXT  sing N N 377 
TYR   N   CA   sing N N 378 
TYR   N   H    sing N N 379 
TYR   N   H2   sing N N 380 
TYR   CA  C    sing N N 381 
TYR   CA  CB   sing N N 382 
TYR   CA  HA   sing N N 383 
TYR   C   O    doub N N 384 
TYR   C   OXT  sing N N 385 
TYR   CB  CG   sing N N 386 
TYR   CB  HB2  sing N N 387 
TYR   CB  HB3  sing N N 388 
TYR   CG  CD1  doub Y N 389 
TYR   CG  CD2  sing Y N 390 
TYR   CD1 CE1  sing Y N 391 
TYR   CD1 HD1  sing N N 392 
TYR   CD2 CE2  doub Y N 393 
TYR   CD2 HD2  sing N N 394 
TYR   CE1 CZ   doub Y N 395 
TYR   CE1 HE1  sing N N 396 
TYR   CE2 CZ   sing Y N 397 
TYR   CE2 HE2  sing N N 398 
TYR   CZ  OH   sing N N 399 
TYR   OH  HH   sing N N 400 
TYR   OXT HXT  sing N N 401 
VAL   N   CA   sing N N 402 
VAL   N   H    sing N N 403 
VAL   N   H2   sing N N 404 
VAL   CA  C    sing N N 405 
VAL   CA  CB   sing N N 406 
VAL   CA  HA   sing N N 407 
VAL   C   O    doub N N 408 
VAL   C   OXT  sing N N 409 
VAL   CB  CG1  sing N N 410 
VAL   CB  CG2  sing N N 411 
VAL   CB  HB   sing N N 412 
VAL   CG1 HG11 sing N N 413 
VAL   CG1 HG12 sing N N 414 
VAL   CG1 HG13 sing N N 415 
VAL   CG2 HG21 sing N N 416 
VAL   CG2 HG22 sing N N 417 
VAL   CG2 HG23 sing N N 418 
VAL   OXT HXT  sing N N 419 
# 
_pdbx_deposit_group.group_id            G_1002065 
_pdbx_deposit_group.group_title         'X-ray dose series of B-cell lymphoma 6 protein BTB domain in complex with ligand 2' 
_pdbx_deposit_group.group_description   
;Crystal structures of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 solved at increasing X-ray dose using Many Structures One Crystal (MSOX) crystallography.
;
_pdbx_deposit_group.group_type          undefined 
# 
_atom_sites.entry_id                    7GUX 
_atom_sites.fract_transf_matrix[1][1]   0.014791 
_atom_sites.fract_transf_matrix[1][2]   0.008539 
_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]   0.017079 
_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]   0.006003 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
BR 
C  
CL 
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   . ASP   A 1 5   ? 17.296 -21.198 -4.820 1.00 65.29  ? 6   ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 5   ? 18.211 -22.088 -5.536 1.00 64.13  ? 6   ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 5   ? 17.748 -23.563 -5.463 1.00 63.63  ? 6   ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 5   ? 16.700 -23.862 -4.880 1.00 64.41  ? 6   ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 5   ? 19.645 -21.936 -4.974 1.00 65.02  ? 6   ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 5   ? 20.739 -22.001 -6.030 1.00 79.02  ? 6   ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 5   ? 20.874 -23.065 -6.688 1.00 79.18  ? 6   ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 5   ? 21.469 -20.996 -6.191 1.00 86.46  ? 6   ASP   A OD2 1 
ATOM   9    N  N   . SER   A 1 6   ? 18.525 -24.471 -6.073 1.00 54.72  ? 7   SER   A N   1 
ATOM   10   C  CA  . SER   A 1 6   ? 18.268 -25.908 -6.066 1.00 52.04  ? 7   SER   A CA  1 
ATOM   11   C  C   . SER   A 1 6   ? 19.259 -26.626 -5.098 1.00 47.71  ? 7   SER   A C   1 
ATOM   12   O  O   . SER   A 1 6   ? 19.548 -27.808 -5.278 1.00 46.83  ? 7   SER   A O   1 
ATOM   13   C  CB  . SER   A 1 6   ? 18.375 -26.465 -7.482 1.00 57.90  ? 7   SER   A CB  1 
ATOM   14   O  OG  . SER   A 1 6   ? 19.660 -26.236 -8.038 1.00 69.47  ? 7   SER   A OG  1 
ATOM   15   N  N   . CYS   A 1 7   ? 19.744 -25.917 -4.058 1.00 38.74  ? 8   CYS   A N   1 
ATOM   16   C  CA  . CYS   A 1 7   ? 20.690 -26.485 -3.093 1.00 35.55  ? 8   CYS   A CA  1 
ATOM   17   C  C   . CYS   A 1 7   ? 20.075 -27.640 -2.286 1.00 35.74  ? 8   CYS   A C   1 
ATOM   18   O  O   . CYS   A 1 7   ? 18.856 -27.698 -2.117 1.00 35.88  ? 8   CYS   A O   1 
ATOM   19   C  CB  . CYS   A 1 7   ? 21.201 -25.396 -2.146 1.00 36.38  ? 8   CYS   A CB  1 
ATOM   20   S  SG  . CYS   A 1 7   ? 22.358 -24.211 -2.894 1.00 41.68  ? 8   CYS   A SG  1 
ATOM   21   N  N   . ILE   A 1 8   ? 20.918 -28.544 -1.786 1.00 27.41  ? 9   ILE   A N   1 
ATOM   22   C  CA  . ILE   A 1 8   ? 20.545 -29.542 -0.780 1.00 24.70  ? 9   ILE   A CA  1 
ATOM   23   C  C   . ILE   A 1 8   ? 21.157 -29.010 0.516  1.00 26.77  ? 9   ILE   A C   1 
ATOM   24   O  O   . ILE   A 1 8   ? 22.113 -28.223 0.462  1.00 25.36  ? 9   ILE   A O   1 
ATOM   25   C  CB  . ILE   A 1 8   ? 20.894 -31.021 -1.086 1.00 27.88  ? 9   ILE   A CB  1 
ATOM   26   C  CG1 . ILE   A 1 8   ? 22.412 -31.211 -1.349 1.00 27.97  ? 9   ILE   A CG1 1 
ATOM   27   C  CG2 . ILE   A 1 8   ? 20.049 -31.541 -2.261 1.00 27.44  ? 9   ILE   A CG2 1 
ATOM   28   C  CD1 . ILE   A 1 8   ? 22.913 -32.659 -1.487 1.00 32.83  ? 9   ILE   A CD1 1 
ATOM   29   N  N   A GLN   A 1 9   ? 20.674 -29.446 1.683  0.66 21.93  ? 10  GLN   A N   1 
ATOM   30   N  N   B GLN   A 1 9   ? 20.570 -29.380 1.653  0.34 22.77  ? 10  GLN   A N   1 
ATOM   31   C  CA  A GLN   A 1 9   ? 21.223 -28.956 2.953  0.66 21.32  ? 10  GLN   A CA  1 
ATOM   32   C  CA  B GLN   A 1 9   ? 20.988 -28.885 2.952  0.34 21.92  ? 10  GLN   A CA  1 
ATOM   33   C  C   A GLN   A 1 9   ? 21.560 -30.104 3.889  0.66 24.21  ? 10  GLN   A C   1 
ATOM   34   C  C   B GLN   A 1 9   ? 21.387 -30.012 3.885  0.34 25.54  ? 10  GLN   A C   1 
ATOM   35   O  O   A GLN   A 1 9   ? 20.788 -31.058 3.983  0.66 25.01  ? 10  GLN   A O   1 
ATOM   36   O  O   B GLN   A 1 9   ? 20.682 -31.015 3.980  0.34 25.88  ? 10  GLN   A O   1 
ATOM   37   C  CB  A GLN   A 1 9   ? 20.237 -27.961 3.621  0.66 23.16  ? 10  GLN   A CB  1 
ATOM   38   C  CB  B GLN   A 1 9   ? 19.849 -28.059 3.564  0.34 23.20  ? 10  GLN   A CB  1 
ATOM   39   C  CG  A GLN   A 1 9   ? 20.517 -27.684 5.117  0.66 29.43  ? 10  GLN   A CG  1 
ATOM   40   C  CG  B GLN   A 1 9   ? 20.318 -27.067 4.622  0.34 22.35  ? 10  GLN   A CG  1 
ATOM   41   C  CD  A GLN   A 1 9   ? 20.062 -26.336 5.608  0.66 47.95  ? 10  GLN   A CD  1 
ATOM   42   C  CD  B GLN   A 1 9   ? 19.559 -27.198 5.920  0.34 37.36  ? 10  GLN   A CD  1 
ATOM   43   O  OE1 A GLN   A 1 9   ? 19.503 -25.524 4.867  0.66 41.19  ? 10  GLN   A OE1 1 
ATOM   44   O  OE1 B GLN   A 1 9   ? 18.336 -27.376 5.945  0.34 30.85  ? 10  GLN   A OE1 1 
ATOM   45   N  NE2 A GLN   A 1 9   ? 20.322 -26.056 6.880  0.66 40.46  ? 10  GLN   A NE2 1 
ATOM   46   N  NE2 B GLN   A 1 9   ? 20.272 -27.088 7.032  0.34 35.54  ? 10  GLN   A NE2 1 
ATOM   47   N  N   A PHE   A 1 10  ? 22.703 -30.010 4.584  0.66 21.40  ? 11  PHE   A N   1 
ATOM   48   N  N   B PHE   A 1 10  ? 22.513 -29.835 4.579  0.34 22.45  ? 11  PHE   A N   1 
ATOM   49   C  CA  A PHE   A 1 10  ? 23.075 -31.028 5.558  0.66 20.41  ? 11  PHE   A CA  1 
ATOM   50   C  CA  B PHE   A 1 10  ? 23.017 -30.810 5.538  0.34 21.81  ? 11  PHE   A CA  1 
ATOM   51   C  C   A PHE   A 1 10  ? 22.626 -30.531 6.923  0.66 23.18  ? 11  PHE   A C   1 
ATOM   52   C  C   B PHE   A 1 10  ? 22.516 -30.373 6.893  0.34 24.37  ? 11  PHE   A C   1 
ATOM   53   O  O   A PHE   A 1 10  ? 23.222 -29.594 7.482  0.66 22.43  ? 11  PHE   A O   1 
ATOM   54   O  O   B PHE   A 1 10  ? 22.941 -29.327 7.406  0.34 23.80  ? 11  PHE   A O   1 
ATOM   55   C  CB  A PHE   A 1 10  ? 24.584 -31.345 5.503  0.66 21.50  ? 11  PHE   A CB  1 
ATOM   56   C  CB  B PHE   A 1 10  ? 24.551 -30.904 5.449  0.34 23.25  ? 11  PHE   A CB  1 
ATOM   57   C  CG  A PHE   A 1 10  ? 24.955 -32.543 6.341  0.66 22.46  ? 11  PHE   A CG  1 
ATOM   58   C  CG  B PHE   A 1 10  ? 25.014 -31.682 4.237  0.34 25.39  ? 11  PHE   A CG  1 
ATOM   59   C  CD1 A PHE   A 1 10  ? 24.592 -33.828 5.948  0.66 24.46  ? 11  PHE   A CD1 1 
ATOM   60   C  CD1 B PHE   A 1 10  ? 24.728 -31.237 2.949  0.34 29.12  ? 11  PHE   A CD1 1 
ATOM   61   C  CD2 A PHE   A 1 10  ? 25.740 -32.399 7.481  0.66 23.24  ? 11  PHE   A CD2 1 
ATOM   62   C  CD2 B PHE   A 1 10  ? 25.739 -32.857 4.381  0.34 28.66  ? 11  PHE   A CD2 1 
ATOM   63   C  CE1 A PHE   A 1 10  ? 24.939 -34.939 6.730  0.66 25.65  ? 11  PHE   A CE1 1 
ATOM   64   C  CE1 B PHE   A 1 10  ? 25.151 -31.957 1.830  0.34 30.45  ? 11  PHE   A CE1 1 
ATOM   65   C  CE2 A PHE   A 1 10  ? 26.067 -33.503 8.271  0.66 25.00  ? 11  PHE   A CE2 1 
ATOM   66   C  CE2 B PHE   A 1 10  ? 26.164 -33.578 3.256  0.34 32.29  ? 11  PHE   A CE2 1 
ATOM   67   C  CZ  A PHE   A 1 10  ? 25.676 -34.767 7.886  0.66 23.63  ? 11  PHE   A CZ  1 
ATOM   68   C  CZ  B PHE   A 1 10  ? 25.867 -33.122 1.990  0.34 30.32  ? 11  PHE   A CZ  1 
ATOM   69   N  N   . THR   A 1 11  ? 21.533 -31.123 7.426  1.00 20.91  ? 12  THR   A N   1 
ATOM   70   C  CA  . THR   A 1 11  ? 20.868 -30.757 8.692  1.00 21.48  ? 12  THR   A CA  1 
ATOM   71   C  C   . THR   A 1 11  ? 21.831 -30.511 9.877  1.00 23.56  ? 12  THR   A C   1 
ATOM   72   O  O   . THR   A 1 11  ? 21.713 -29.490 10.572 1.00 23.80  ? 12  THR   A O   1 
ATOM   73   C  CB  . THR   A 1 11  ? 19.803 -31.795 9.052  1.00 28.56  ? 12  THR   A CB  1 
ATOM   74   O  OG1 . THR   A 1 11  ? 18.896 -31.931 7.938  1.00 29.24  ? 12  THR   A OG1 1 
ATOM   75   C  CG2 . THR   A 1 11  ? 19.017 -31.417 10.325 1.00 31.99  ? 12  THR   A CG2 1 
ATOM   76   N  N   . ARG   A 1 12  ? 22.768 -31.446 10.089 1.00 20.99  ? 13  ARG   A N   1 
ATOM   77   C  CA  . ARG   A 1 12  ? 23.676 -31.358 11.243 1.00 21.09  ? 13  ARG   A CA  1 
ATOM   78   C  C   . ARG   A 1 12  ? 24.914 -30.462 11.034 1.00 22.62  ? 13  ARG   A C   1 
ATOM   79   O  O   . ARG   A 1 12  ? 25.747 -30.381 11.949 1.00 21.51  ? 13  ARG   A O   1 
ATOM   80   C  CB  . ARG   A 1 12  ? 24.136 -32.776 11.656 1.00 26.43  ? 13  ARG   A CB  1 
ATOM   81   C  CG  . ARG   A 1 12  ? 23.035 -33.716 12.191 1.00 36.81  ? 13  ARG   A CG  1 
ATOM   82   C  CD  . ARG   A 1 12  ? 22.473 -33.285 13.534 1.00 58.44  ? 13  ARG   A CD  1 
ATOM   83   N  NE  . ARG   A 1 12  ? 23.455 -33.369 14.619 1.00 70.91  ? 13  ARG   A NE  1 
ATOM   84   C  CZ  . ARG   A 1 12  ? 23.318 -32.772 15.799 1.00 82.25  ? 13  ARG   A CZ  1 
ATOM   85   N  NH1 . ARG   A 1 12  ? 24.253 -32.906 16.729 1.00 70.97  ? 13  ARG   A NH1 1 
ATOM   86   N  NH2 . ARG   A 1 12  ? 22.251 -32.022 16.053 1.00 64.79  ? 13  ARG   A NH2 1 
ATOM   87   N  N   . HIS   A 1 13  ? 25.057 -29.812 9.862  1.00 18.54  ? 14  HIS   A N   1 
ATOM   88   C  CA  . HIS   A 1 13  ? 26.284 -29.068 9.577  1.00 19.47  ? 14  HIS   A CA  1 
ATOM   89   C  C   . HIS   A 1 13  ? 26.588 -27.970 10.597 1.00 21.81  ? 14  HIS   A C   1 
ATOM   90   O  O   . HIS   A 1 13  ? 27.725 -27.903 11.095 1.00 20.96  ? 14  HIS   A O   1 
ATOM   91   C  CB  . HIS   A 1 13  ? 26.276 -28.501 8.141  1.00 19.28  ? 14  HIS   A CB  1 
ATOM   92   C  CG  . HIS   A 1 13  ? 27.538 -27.752 7.839  1.00 21.22  ? 14  HIS   A CG  1 
ATOM   93   N  ND1 . HIS   A 1 13  ? 28.716 -28.426 7.625  1.00 21.71  ? 14  HIS   A ND1 1 
ATOM   94   C  CD2 . HIS   A 1 13  ? 27.753 -26.422 7.689  1.00 21.64  ? 14  HIS   A CD2 1 
ATOM   95   C  CE1 . HIS   A 1 13  ? 29.628 -27.499 7.368  1.00 21.18  ? 14  HIS   A CE1 1 
ATOM   96   N  NE2 . HIS   A 1 13  ? 29.100 -26.273 7.396  1.00 20.45  ? 14  HIS   A NE2 1 
ATOM   97   N  N   . ALA   A 1 14  ? 25.604 -27.091 10.876 1.00 19.00  ? 15  ALA   A N   1 
ATOM   98   C  CA  . ALA   A 1 14  ? 25.836 -25.961 11.811 1.00 19.23  ? 15  ALA   A CA  1 
ATOM   99   C  C   . ALA   A 1 14  ? 26.248 -26.470 13.209 1.00 20.77  ? 15  ALA   A C   1 
ATOM   100  O  O   . ALA   A 1 14  ? 27.168 -25.915 13.809 1.00 18.68  ? 15  ALA   A O   1 
ATOM   101  C  CB  . ALA   A 1 14  ? 24.594 -25.072 11.888 1.00 20.24  ? 15  ALA   A CB  1 
ATOM   102  N  N   A SER   A 1 15  ? 25.590 -27.530 13.696 0.42 19.92  ? 16  SER   A N   1 
ATOM   103  N  N   B SER   A 1 15  ? 25.588 -27.535 13.698 0.30 19.39  ? 16  SER   A N   1 
ATOM   104  N  N   C SER   A 1 15  ? 25.585 -27.526 13.716 0.28 18.97  ? 16  SER   A N   1 
ATOM   105  C  CA  A SER   A 1 15  ? 25.887 -28.112 15.004 0.42 19.71  ? 16  SER   A CA  1 
ATOM   106  C  CA  B SER   A 1 15  ? 25.879 -28.137 15.002 0.30 19.21  ? 16  SER   A CA  1 
ATOM   107  C  CA  C SER   A 1 15  ? 25.910 -28.084 15.033 0.28 18.55  ? 16  SER   A CA  1 
ATOM   108  C  C   A SER   A 1 15  ? 27.298 -28.703 15.029 0.42 23.50  ? 16  SER   A C   1 
ATOM   109  C  C   B SER   A 1 15  ? 27.288 -28.720 15.034 0.30 23.49  ? 16  SER   A C   1 
ATOM   110  C  C   C SER   A 1 15  ? 27.301 -28.722 15.047 0.28 23.22  ? 16  SER   A C   1 
ATOM   111  O  O   A SER   A 1 15  ? 28.022 -28.516 16.015 0.42 21.21  ? 16  SER   A O   1 
ATOM   112  O  O   B SER   A 1 15  ? 28.002 -28.546 16.027 0.30 21.78  ? 16  SER   A O   1 
ATOM   113  O  O   C SER   A 1 15  ? 28.021 -28.580 16.040 0.28 21.56  ? 16  SER   A O   1 
ATOM   114  C  CB  A SER   A 1 15  ? 24.851 -29.173 15.365 0.42 23.50  ? 16  SER   A CB  1 
ATOM   115  C  CB  B SER   A 1 15  ? 24.857 -29.220 15.331 0.30 22.55  ? 16  SER   A CB  1 
ATOM   116  C  CB  C SER   A 1 15  ? 24.841 -29.070 15.494 0.28 21.17  ? 16  SER   A CB  1 
ATOM   117  O  OG  A SER   A 1 15  ? 25.097 -29.700 16.658 0.42 27.02  ? 16  SER   A OG  1 
ATOM   118  O  OG  B SER   A 1 15  ? 23.555 -28.672 15.437 0.30 25.36  ? 16  SER   A OG  1 
ATOM   119  O  OG  C SER   A 1 15  ? 24.746 -30.181 14.620 0.28 21.36  ? 16  SER   A OG  1 
ATOM   120  N  N   . ASP   A 1 16  ? 27.692 -29.389 13.936 1.00 21.20  ? 17  ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 16  ? 29.020 -30.009 13.801 1.00 21.52  ? 17  ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 16  ? 30.090 -28.915 13.766 1.00 21.65  ? 17  ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 16  ? 31.133 -29.073 14.397 1.00 21.53  ? 17  ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 16  ? 29.094 -30.875 12.537 1.00 23.51  ? 17  ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 16  ? 28.305 -32.187 12.621 1.00 31.95  ? 17  ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 16  ? 27.769 -32.500 13.718 1.00 30.18  ? 17  ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 16  ? 28.213 -32.891 11.591 1.00 34.83  ? 17  ASP   A OD2 1 
ATOM   128  N  N   . VAL   A 1 17  ? 29.822 -27.798 13.055 1.00 17.69  ? 18  VAL   A N   1 
ATOM   129  C  CA  . VAL   A 1 17  ? 30.790 -26.687 13.015 1.00 17.07  ? 18  VAL   A CA  1 
ATOM   130  C  C   . VAL   A 1 17  ? 31.012 -26.155 14.449 1.00 21.53  ? 18  VAL   A C   1 
ATOM   131  O  O   . VAL   A 1 17  ? 32.145 -26.000 14.895 1.00 19.46  ? 18  VAL   A O   1 
ATOM   132  C  CB  . VAL   A 1 17  ? 30.315 -25.567 12.045 1.00 19.10  ? 18  VAL   A CB  1 
ATOM   133  C  CG1 . VAL   A 1 17  ? 31.086 -24.261 12.265 1.00 19.32  ? 18  VAL   A CG1 1 
ATOM   134  C  CG2 . VAL   A 1 17  ? 30.390 -26.020 10.581 1.00 19.08  ? 18  VAL   A CG2 1 
ATOM   135  N  N   . LEU   A 1 18  ? 29.920 -25.902 15.163 1.00 18.67  ? 19  LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 18  ? 30.012 -25.350 16.517 1.00 19.71  ? 19  LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 18  ? 30.737 -26.304 17.478 1.00 20.13  ? 19  LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 18  ? 31.588 -25.850 18.263 1.00 18.80  ? 19  LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 18  ? 28.623 -24.968 17.031 1.00 20.35  ? 19  LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 18  ? 28.634 -24.093 18.299 1.00 23.98  ? 19  LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 18  ? 29.205 -22.710 18.004 1.00 23.72  ? 19  LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 18  ? 27.230 -23.953 18.862 1.00 27.72  ? 19  LEU   A CD2 1 
ATOM   143  N  N   . LEU   A 1 19  ? 30.455 -27.604 17.360 1.00 19.21  ? 20  LEU   A N   1 
ATOM   144  C  CA  . LEU   A 1 19  ? 31.123 -28.638 18.155 1.00 20.11  ? 20  LEU   A CA  1 
ATOM   145  C  C   . LEU   A 1 19  ? 32.639 -28.555 17.904 1.00 22.75  ? 20  LEU   A C   1 
ATOM   146  O  O   . LEU   A 1 19  ? 33.423 -28.547 18.867 1.00 22.11  ? 20  LEU   A O   1 
ATOM   147  C  CB  . LEU   A 1 19  ? 30.588 -30.015 17.762 1.00 22.23  ? 20  LEU   A CB  1 
ATOM   148  C  CG  . LEU   A 1 19  ? 31.161 -31.203 18.539 1.00 30.51  ? 20  LEU   A CG  1 
ATOM   149  C  CD1 . LEU   A 1 19  ? 30.760 -31.122 20.018 1.00 33.27  ? 20  LEU   A CD1 1 
ATOM   150  C  CD2 . LEU   A 1 19  ? 30.620 -32.510 17.974 1.00 35.30  ? 20  LEU   A CD2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 33.048 -28.424 16.622 1.00 19.54  ? 21  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 34.474 -28.307 16.295 1.00 18.60  ? 21  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 35.088 -27.003 16.799 1.00 21.19  ? 21  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 36.213 -27.006 17.284 1.00 20.95  ? 21  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 34.703 -28.519 14.809 1.00 20.40  ? 21  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.662 -29.985 14.432 1.00 30.24  ? 21  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.884 -30.877 15.265 1.00 26.45  ? 21  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.386 -30.267 13.166 1.00 25.24  ? 21  ASN   A ND2 1 
ATOM   159  N  N   . LEU   A 1 21  ? 34.345 -25.894 16.718 1.00 19.62  ? 22  LEU   A N   1 
ATOM   160  C  CA  . LEU   A 1 21  ? 34.847 -24.623 17.257 1.00 19.44  ? 22  LEU   A CA  1 
ATOM   161  C  C   . LEU   A 1 21  ? 35.071 -24.773 18.773 1.00 21.27  ? 22  LEU   A C   1 
ATOM   162  O  O   . LEU   A 1 21  ? 36.049 -24.228 19.311 1.00 20.92  ? 22  LEU   A O   1 
ATOM   163  C  CB  . LEU   A 1 21  ? 33.873 -23.479 16.946 1.00 19.43  ? 22  LEU   A CB  1 
ATOM   164  C  CG  . LEU   A 1 21  ? 33.762 -23.132 15.448 1.00 20.82  ? 22  LEU   A CG  1 
ATOM   165  C  CD1 . LEU   A 1 21  ? 32.635 -22.116 15.214 1.00 22.15  ? 22  LEU   A CD1 1 
ATOM   166  C  CD2 . LEU   A 1 21  ? 35.122 -22.670 14.847 1.00 24.73  ? 22  LEU   A CD2 1 
ATOM   167  N  N   . ASN   A 1 22  ? 34.152 -25.488 19.468 1.00 19.60  ? 23  ASN   A N   1 
ATOM   168  C  CA  . ASN   A 1 22  ? 34.307 -25.697 20.920 1.00 19.93  ? 23  ASN   A CA  1 
ATOM   169  C  C   . ASN   A 1 22  ? 35.543 -26.568 21.225 1.00 24.17  ? 23  ASN   A C   1 
ATOM   170  O  O   . ASN   A 1 22  ? 36.248 -26.314 22.207 1.00 24.82  ? 23  ASN   A O   1 
ATOM   171  C  CB  . ASN   A 1 22  ? 33.053 -26.309 21.543 1.00 21.21  ? 23  ASN   A CB  1 
ATOM   172  C  CG  . ASN   A 1 22  ? 33.062 -26.179 23.056 1.00 28.06  ? 23  ASN   A CG  1 
ATOM   173  O  OD1 . ASN   A 1 22  ? 33.580 -25.207 23.617 1.00 25.93  ? 23  ASN   A OD1 1 
ATOM   174  N  ND2 . ASN   A 1 22  ? 32.500 -27.156 23.727 1.00 30.21  ? 23  ASN   A ND2 1 
ATOM   175  N  N   . ARG   A 1 23  ? 35.823 -27.567 20.361 1.00 22.19  ? 24  ARG   A N   1 
ATOM   176  C  CA  . ARG   A 1 23  ? 37.010 -28.428 20.483 1.00 22.97  ? 24  ARG   A CA  1 
ATOM   177  C  C   . ARG   A 1 23  ? 38.271 -27.578 20.335 1.00 26.35  ? 24  ARG   A C   1 
ATOM   178  O  O   . ARG   A 1 23  ? 39.218 -27.759 21.099 1.00 25.78  ? 24  ARG   A O   1 
ATOM   179  C  CB  . ARG   A 1 23  ? 36.991 -29.540 19.429 1.00 23.23  ? 24  ARG   A CB  1 
ATOM   180  C  CG  . ARG   A 1 23  ? 35.977 -30.627 19.763 1.00 26.22  ? 24  ARG   A CG  1 
ATOM   181  C  CD  . ARG   A 1 23  ? 35.784 -31.564 18.580 1.00 28.50  ? 24  ARG   A CD  1 
ATOM   182  N  NE  . ARG   A 1 23  ? 34.933 -32.692 18.945 1.00 36.61  ? 24  ARG   A NE  1 
ATOM   183  C  CZ  . ARG   A 1 23  ? 34.285 -33.461 18.077 1.00 51.12  ? 24  ARG   A CZ  1 
ATOM   184  N  NH1 . ARG   A 1 23  ? 34.332 -33.195 16.776 1.00 38.51  ? 24  ARG   A NH1 1 
ATOM   185  N  NH2 . ARG   A 1 23  ? 33.560 -34.482 18.505 1.00 44.01  ? 24  ARG   A NH2 1 
ATOM   186  N  N   . LEU   A 1 24  ? 38.269 -26.611 19.386 1.00 22.57  ? 25  LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 24  ? 39.409 -25.704 19.225 1.00 22.57  ? 25  LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 24  ? 39.554 -24.851 20.483 1.00 26.09  ? 25  LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 24  ? 40.679 -24.681 20.982 1.00 26.64  ? 25  LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 24  ? 39.220 -24.785 18.023 1.00 22.26  ? 25  LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 24  ? 39.221 -25.478 16.649 1.00 26.55  ? 25  LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 24  ? 39.096 -24.444 15.539 1.00 26.61  ? 25  LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 24  ? 40.487 -26.328 16.465 1.00 27.39  ? 25  LEU   A CD2 1 
ATOM   194  N  N   . ARG   A 1 25  ? 38.414 -24.335 21.015 1.00 22.40  ? 26  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 25  ? 38.462 -23.554 22.251 1.00 22.92  ? 26  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 25  ? 39.092 -24.367 23.422 1.00 28.21  ? 26  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 25  ? 39.979 -23.846 24.120 1.00 28.49  ? 26  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 25  ? 37.068 -23.050 22.656 1.00 23.46  ? 26  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 25  ? 37.201 -22.158 23.897 1.00 26.44  ? 26  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 25  ? 35.912 -21.514 24.288 1.00 31.64  ? 26  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 25  ? 34.899 -22.497 24.652 1.00 27.72  ? 26  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 25  ? 34.279 -22.550 25.829 1.00 38.16  ? 26  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 25  ? 34.622 -21.718 26.809 1.00 32.92  ? 26  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 25  ? 33.331 -23.446 26.042 1.00 29.29  ? 26  ARG   A NH2 1 
ATOM   205  N  N   A SER   A 1 26  ? 38.624 -25.609 23.633 0.39 25.94  ? 27  SER   A N   1 
ATOM   206  N  N   B SER   A 1 26  ? 38.626 -25.619 23.613 0.28 25.81  ? 27  SER   A N   1 
ATOM   207  N  N   C SER   A 1 26  ? 38.623 -25.610 23.630 0.33 26.14  ? 27  SER   A N   1 
ATOM   208  C  CA  A SER   A 1 26  ? 39.097 -26.497 24.704 0.39 27.15  ? 27  SER   A CA  1 
ATOM   209  C  CA  B SER   A 1 26  ? 39.075 -26.564 24.645 0.28 26.99  ? 27  SER   A CA  1 
ATOM   210  C  CA  C SER   A 1 26  ? 39.089 -26.514 24.691 0.33 27.47  ? 27  SER   A CA  1 
ATOM   211  C  C   A SER   A 1 26  ? 40.608 -26.773 24.630 0.39 32.89  ? 27  SER   A C   1 
ATOM   212  C  C   B SER   A 1 26  ? 40.588 -26.780 24.616 0.28 32.67  ? 27  SER   A C   1 
ATOM   213  C  C   C SER   A 1 26  ? 40.602 -26.776 24.625 0.33 32.96  ? 27  SER   A C   1 
ATOM   214  O  O   A SER   A 1 26  ? 41.258 -26.888 25.672 0.39 34.30  ? 27  SER   A O   1 
ATOM   215  O  O   B SER   A 1 26  ? 41.217 -26.884 25.672 0.28 33.89  ? 27  SER   A O   1 
ATOM   216  O  O   C SER   A 1 26  ? 41.247 -26.893 25.671 0.33 34.26  ? 27  SER   A O   1 
ATOM   217  C  CB  A SER   A 1 26  ? 38.308 -27.803 24.708 0.39 30.30  ? 27  SER   A CB  1 
ATOM   218  C  CB  B SER   A 1 26  ? 38.387 -27.913 24.459 0.28 30.24  ? 27  SER   A CB  1 
ATOM   219  C  CB  C SER   A 1 26  ? 38.321 -27.830 24.641 0.33 31.20  ? 27  SER   A CB  1 
ATOM   220  O  OG  A SER   A 1 26  ? 38.656 -28.647 23.622 0.39 35.82  ? 27  SER   A OG  1 
ATOM   221  O  OG  B SER   A 1 26  ? 37.026 -27.887 24.848 0.28 36.26  ? 27  SER   A OG  1 
ATOM   222  O  OG  C SER   A 1 26  ? 38.751 -28.727 25.653 0.33 40.47  ? 27  SER   A OG  1 
ATOM   223  N  N   . ARG   A 1 27  ? 41.163 -26.844 23.404 1.00 28.92  ? 28  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 27  ? 42.594 -27.089 23.181 1.00 30.76  ? 28  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 27  ? 43.380 -25.797 22.980 1.00 32.99  ? 28  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 27  ? 44.586 -25.841 22.717 1.00 34.30  ? 28  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 27  ? 42.762 -28.051 22.001 1.00 32.55  ? 28  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 27  ? 42.038 -29.380 22.209 1.00 39.32  ? 28  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 27  ? 42.017 -30.210 20.951 1.00 44.45  ? 28  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 27  ? 43.375 -30.567 20.538 1.00 54.95  ? 28  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 27  ? 43.731 -30.791 19.281 1.00 69.20  ? 28  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 27  ? 44.989 -31.093 18.985 1.00 58.75  ? 28  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 27  ? 42.843 -30.688 18.306 1.00 52.46  ? 28  ARG   A NH2 1 
ATOM   234  N  N   . ASP   A 1 28  ? 42.697 -24.647 23.128 1.00 27.44  ? 29  ASP   A N   1 
ATOM   235  C  CA  . ASP   A 1 28  ? 43.249 -23.304 22.984 1.00 27.91  ? 29  ASP   A CA  1 
ATOM   236  C  C   . ASP   A 1 28  ? 43.881 -23.075 21.586 1.00 32.40  ? 29  ASP   A C   1 
ATOM   237  O  O   . ASP   A 1 28  ? 44.941 -22.451 21.459 1.00 34.12  ? 29  ASP   A O   1 
ATOM   238  C  CB  . ASP   A 1 28  ? 44.243 -22.996 24.132 1.00 30.86  ? 29  ASP   A CB  1 
ATOM   239  C  CG  . ASP   A 1 28  ? 44.549 -21.521 24.285 1.00 40.88  ? 29  ASP   A CG  1 
ATOM   240  O  OD1 . ASP   A 1 28  ? 43.622 -20.699 24.090 1.00 40.46  ? 29  ASP   A OD1 1 
ATOM   241  O  OD2 . ASP   A 1 28  ? 45.711 -21.188 24.596 1.00 45.52  ? 29  ASP   A OD2 1 
ATOM   242  N  N   . ILE   A 1 29  ? 43.240 -23.613 20.550 1.00 26.43  ? 30  ILE   A N   1 
ATOM   243  C  CA  . ILE   A 1 29  ? 43.736 -23.518 19.175 1.00 26.44  ? 30  ILE   A CA  1 
ATOM   244  C  C   . ILE   A 1 29  ? 43.133 -22.312 18.470 1.00 28.46  ? 30  ILE   A C   1 
ATOM   245  O  O   . ILE   A 1 29  ? 41.902 -22.174 18.389 1.00 24.56  ? 30  ILE   A O   1 
ATOM   246  C  CB  . ILE   A 1 29  ? 43.508 -24.830 18.379 1.00 29.18  ? 30  ILE   A CB  1 
ATOM   247  C  CG1 . ILE   A 1 29  ? 44.301 -26.019 19.002 1.00 31.00  ? 30  ILE   A CG1 1 
ATOM   248  C  CG2 . ILE   A 1 29  ? 43.832 -24.642 16.866 1.00 28.08  ? 30  ILE   A CG2 1 
ATOM   249  C  CD1 . ILE   A 1 29  ? 43.803 -27.384 18.518 1.00 34.52  ? 30  ILE   A CD1 1 
ATOM   250  N  N   . LEU   A 1 30  ? 44.020 -21.424 17.979 1.00 27.27  ? 31  LEU   A N   1 
ATOM   251  C  CA  . LEU   A 1 30  ? 43.659 -20.226 17.216 1.00 27.66  ? 31  LEU   A CA  1 
ATOM   252  C  C   . LEU   A 1 30  ? 42.747 -19.238 17.970 1.00 28.24  ? 31  LEU   A C   1 
ATOM   253  O  O   . LEU   A 1 30  ? 42.173 -18.352 17.342 1.00 25.70  ? 31  LEU   A O   1 
ATOM   254  C  CB  . LEU   A 1 30  ? 43.088 -20.556 15.835 1.00 28.06  ? 31  LEU   A CB  1 
ATOM   255  C  CG  . LEU   A 1 30  ? 44.124 -21.090 14.801 1.00 35.25  ? 31  LEU   A CG  1 
ATOM   256  C  CD1 . LEU   A 1 30  ? 43.503 -21.174 13.455 1.00 35.91  ? 31  LEU   A CD1 1 
ATOM   257  C  CD2 . LEU   A 1 30  ? 45.337 -20.209 14.702 1.00 42.57  ? 31  LEU   A CD2 1 
ATOM   258  N  N   . THR   A 1 31  ? 42.734 -19.305 19.307 1.00 25.51  ? 32  THR   A N   1 
ATOM   259  C  CA  . THR   A 1 31  ? 42.061 -18.298 20.131 1.00 24.22  ? 32  THR   A CA  1 
ATOM   260  C  C   . THR   A 1 31  ? 42.877 -17.013 19.935 1.00 29.84  ? 32  THR   A C   1 
ATOM   261  O  O   . THR   A 1 31  ? 44.109 -17.070 19.789 1.00 29.77  ? 32  THR   A O   1 
ATOM   262  C  CB  . THR   A 1 31  ? 41.989 -18.735 21.593 1.00 28.71  ? 32  THR   A CB  1 
ATOM   263  O  OG1 . THR   A 1 31  ? 43.313 -19.060 22.020 1.00 31.28  ? 32  THR   A OG1 1 
ATOM   264  C  CG2 . THR   A 1 31  ? 41.040 -19.948 21.794 1.00 27.36  ? 32  THR   A CG2 1 
ATOM   265  N  N   . ASP   A 1 32  ? 42.196 -15.881 19.801 1.00 26.66  ? 33  ASP   A N   1 
ATOM   266  C  CA  . ASP   A 1 32  ? 42.870 -14.628 19.461 1.00 26.77  ? 33  ASP   A CA  1 
ATOM   267  C  C   . ASP   A 1 32  ? 42.536 -13.480 20.370 1.00 28.57  ? 33  ASP   A C   1 
ATOM   268  O  O   . ASP   A 1 32  ? 42.896 -12.340 20.078 1.00 28.29  ? 33  ASP   A O   1 
ATOM   269  C  CB  . ASP   A 1 32  ? 42.572 -14.265 17.993 1.00 28.01  ? 33  ASP   A CB  1 
ATOM   270  C  CG  . ASP   A 1 32  ? 41.092 -14.259 17.612 1.00 37.12  ? 33  ASP   A CG  1 
ATOM   271  O  OD1 . ASP   A 1 32  ? 40.237 -14.394 18.519 1.00 32.18  ? 33  ASP   A OD1 1 
ATOM   272  O  OD2 . ASP   A 1 32  ? 40.795 -14.122 16.413 1.00 46.33  ? 33  ASP   A OD2 1 
ATOM   273  N  N   . VAL   A 1 33  ? 41.864 -13.764 21.483 1.00 23.40  ? 34  VAL   A N   1 
ATOM   274  C  CA  . VAL   A 1 33  ? 41.550 -12.715 22.453 1.00 23.11  ? 34  VAL   A CA  1 
ATOM   275  C  C   . VAL   A 1 33  ? 41.384 -13.319 23.835 1.00 27.01  ? 34  VAL   A C   1 
ATOM   276  O  O   . VAL   A 1 33  ? 40.979 -14.489 23.970 1.00 26.30  ? 34  VAL   A O   1 
ATOM   277  C  CB  . VAL   A 1 33  ? 40.274 -11.898 22.015 1.00 25.67  ? 34  VAL   A CB  1 
ATOM   278  C  CG1 . VAL   A 1 33  ? 38.977 -12.713 22.168 1.00 23.49  ? 34  VAL   A CG1 1 
ATOM   279  C  CG2 . VAL   A 1 33  ? 40.156 -10.554 22.758 1.00 26.37  ? 34  VAL   A CG2 1 
ATOM   280  N  N   A VAL   A 1 34  ? 41.677 -12.508 24.855 0.60 24.51  ? 35  VAL   A N   1 
ATOM   281  N  N   B VAL   A 1 34  ? 41.674 -12.522 24.868 0.40 23.76  ? 35  VAL   A N   1 
ATOM   282  C  CA  A VAL   A 1 34  ? 41.460 -12.823 26.260 0.60 24.57  ? 35  VAL   A CA  1 
ATOM   283  C  CA  B VAL   A 1 34  ? 41.421 -12.894 26.252 0.40 23.44  ? 35  VAL   A CA  1 
ATOM   284  C  C   A VAL   A 1 34  ? 40.375 -11.842 26.719 0.60 27.14  ? 35  VAL   A C   1 
ATOM   285  C  C   B VAL   A 1 34  ? 40.450 -11.864 26.844 0.40 27.05  ? 35  VAL   A C   1 
ATOM   286  O  O   A VAL   A 1 34  ? 40.482 -10.640 26.450 0.60 27.17  ? 35  VAL   A O   1 
ATOM   287  O  O   B VAL   A 1 34  ? 40.680 -10.655 26.743 0.40 27.61  ? 35  VAL   A O   1 
ATOM   288  C  CB  A VAL   A 1 34  ? 42.752 -12.668 27.122 0.60 29.92  ? 35  VAL   A CB  1 
ATOM   289  C  CB  B VAL   A 1 34  ? 42.678 -13.192 27.124 0.40 28.02  ? 35  VAL   A CB  1 
ATOM   290  C  CG1 A VAL   A 1 34  ? 42.483 -12.952 28.601 0.60 30.28  ? 35  VAL   A CG1 1 
ATOM   291  C  CG1 B VAL   A 1 34  ? 43.559 -11.963 27.317 0.40 28.49  ? 35  VAL   A CG1 1 
ATOM   292  C  CG2 A VAL   A 1 34  ? 43.875 -13.558 26.610 0.60 30.44  ? 35  VAL   A CG2 1 
ATOM   293  C  CG2 B VAL   A 1 34  ? 42.291 -13.798 28.471 0.40 28.02  ? 35  VAL   A CG2 1 
ATOM   294  N  N   . ILE   A 1 35  ? 39.331 -12.353 27.378 1.00 22.41  ? 36  ILE   A N   1 
ATOM   295  C  CA  . ILE   A 1 35  ? 38.274 -11.539 27.978 1.00 23.01  ? 36  ILE   A CA  1 
ATOM   296  C  C   . ILE   A 1 35  ? 38.557 -11.559 29.468 1.00 28.13  ? 36  ILE   A C   1 
ATOM   297  O  O   . ILE   A 1 35  ? 38.581 -12.640 30.079 1.00 27.44  ? 36  ILE   A O   1 
ATOM   298  C  CB  . ILE   A 1 35  ? 36.840 -12.056 27.662 1.00 24.42  ? 36  ILE   A CB  1 
ATOM   299  C  CG1 . ILE   A 1 35  ? 36.607 -12.233 26.134 1.00 23.90  ? 36  ILE   A CG1 1 
ATOM   300  C  CG2 . ILE   A 1 35  ? 35.788 -11.137 28.292 1.00 26.20  ? 36  ILE   A CG2 1 
ATOM   301  C  CD1 . ILE   A 1 35  ? 36.876 -10.948 25.239 1.00 23.08  ? 36  ILE   A CD1 1 
ATOM   302  N  N   . VAL   A 1 36  ? 38.790 -10.374 30.038 1.00 24.76  ? 37  VAL   A N   1 
ATOM   303  C  CA  . VAL   A 1 36  ? 39.101 -10.243 31.462 1.00 24.83  ? 37  VAL   A CA  1 
ATOM   304  C  C   . VAL   A 1 36  ? 37.847 -9.812  32.208 1.00 30.23  ? 37  VAL   A C   1 
ATOM   305  O  O   . VAL   A 1 36  ? 37.260 -8.769  31.900 1.00 28.53  ? 37  VAL   A O   1 
ATOM   306  C  CB  . VAL   A 1 36  ? 40.312 -9.295  31.708 1.00 29.56  ? 37  VAL   A CB  1 
ATOM   307  C  CG1 . VAL   A 1 36  ? 40.604 -9.146  33.208 1.00 30.44  ? 37  VAL   A CG1 1 
ATOM   308  C  CG2 . VAL   A 1 36  ? 41.559 -9.807  30.985 1.00 30.35  ? 37  VAL   A CG2 1 
ATOM   309  N  N   . VAL   A 1 37  ? 37.453 -10.613 33.207 1.00 27.25  ? 38  VAL   A N   1 
ATOM   310  C  CA  . VAL   A 1 37  ? 36.264 -10.381 34.021 1.00 27.08  ? 38  VAL   A CA  1 
ATOM   311  C  C   . VAL   A 1 37  ? 36.767 -10.421 35.449 1.00 34.49  ? 38  VAL   A C   1 
ATOM   312  O  O   . VAL   A 1 37  ? 36.932 -11.503 36.021 1.00 31.49  ? 38  VAL   A O   1 
ATOM   313  C  CB  . VAL   A 1 37  ? 35.158 -11.433 33.734 1.00 30.14  ? 38  VAL   A CB  1 
ATOM   314  C  CG1 . VAL   A 1 37  ? 33.836 -11.005 34.362 1.00 30.29  ? 38  VAL   A CG1 1 
ATOM   315  C  CG2 . VAL   A 1 37  ? 34.992 -11.655 32.229 1.00 28.78  ? 38  VAL   A CG2 1 
ATOM   316  N  N   A SER   A 1 38  ? 37.140 -9.242  35.979 0.54 35.24  ? 39  SER   A N   1 
ATOM   317  N  N   B SER   A 1 38  ? 37.000 -9.220  36.012 0.46 34.20  ? 39  SER   A N   1 
ATOM   318  C  CA  A SER   A 1 38  ? 37.735 -9.064  37.309 0.54 36.81  ? 39  SER   A CA  1 
ATOM   319  C  CA  B SER   A 1 38  ? 37.531 -8.977  37.353 0.46 35.36  ? 39  SER   A CA  1 
ATOM   320  C  C   A SER   A 1 38  ? 39.086 -9.824  37.381 0.54 38.44  ? 39  SER   A C   1 
ATOM   321  C  C   B SER   A 1 38  ? 38.630 -9.990  37.710 0.46 37.86  ? 39  SER   A C   1 
ATOM   322  O  O   A SER   A 1 38  ? 39.982 -9.521  36.594 0.54 37.90  ? 39  SER   A O   1 
ATOM   323  O  O   B SER   A 1 38  ? 38.446 -10.884 38.543 0.46 37.41  ? 39  SER   A O   1 
ATOM   324  C  CB  A SER   A 1 38  ? 36.765 -9.485  38.417 0.54 42.66  ? 39  SER   A CB  1 
ATOM   325  C  CB  B SER   A 1 38  ? 36.413 -8.896  38.385 0.46 39.86  ? 39  SER   A CB  1 
ATOM   326  O  OG  A SER   A 1 38  ? 35.521 -8.811  38.319 0.54 57.44  ? 39  SER   A OG  1 
ATOM   327  O  OG  B SER   A 1 38  ? 35.725 -7.663  38.243 0.46 47.83  ? 39  SER   A OG  1 
ATOM   328  N  N   A ARG   A 1 39  ? 39.207 -10.827 38.279 0.54 34.29  ? 40  ARG   A N   1 
ATOM   329  N  N   B ARG   A 1 39  ? 39.735 -9.882  36.953 0.46 32.85  ? 40  ARG   A N   1 
ATOM   330  C  CA  A ARG   A 1 39  ? 40.420 -11.627 38.475 0.54 34.20  ? 40  ARG   A CA  1 
ATOM   331  C  CA  B ARG   A 1 39  ? 40.981 -10.655 36.996 0.46 33.17  ? 40  ARG   A CA  1 
ATOM   332  C  C   A ARG   A 1 39  ? 40.529 -12.810 37.509 0.54 36.17  ? 40  ARG   A C   1 
ATOM   333  C  C   B ARG   A 1 39  ? 40.850 -12.073 36.403 0.46 35.20  ? 40  ARG   A C   1 
ATOM   334  O  O   A ARG   A 1 39  ? 41.570 -13.476 37.484 0.54 35.75  ? 40  ARG   A O   1 
ATOM   335  O  O   B ARG   A 1 39  ? 41.867 -12.593 35.934 0.46 35.27  ? 40  ARG   A O   1 
ATOM   336  C  CB  A ARG   A 1 39  ? 40.520 -12.120 39.935 0.54 34.45  ? 40  ARG   A CB  1 
ATOM   337  C  CB  B ARG   A 1 39  ? 41.640 -10.671 38.387 0.46 34.62  ? 40  ARG   A CB  1 
ATOM   338  C  CG  A ARG   A 1 39  ? 40.961 -11.055 40.929 0.54 41.36  ? 40  ARG   A CG  1 
ATOM   339  C  CG  B ARG   A 1 39  ? 42.164 -9.291  38.792 0.46 44.97  ? 40  ARG   A CG  1 
ATOM   340  C  CD  A ARG   A 1 39  ? 41.304 -11.678 42.268 0.54 40.23  ? 40  ARG   A CD  1 
ATOM   341  C  CD  B ARG   A 1 39  ? 43.164 -9.347  39.926 0.46 51.89  ? 40  ARG   A CD  1 
ATOM   342  N  NE  A ARG   A 1 39  ? 41.538 -10.675 43.306 0.54 43.18  ? 40  ARG   A NE  1 
ATOM   343  N  NE  B ARG   A 1 39  ? 43.604 -8.009  40.329 0.46 58.93  ? 40  ARG   A NE  1 
ATOM   344  C  CZ  A ARG   A 1 39  ? 42.725 -10.155 43.608 0.54 57.91  ? 40  ARG   A CZ  1 
ATOM   345  C  CZ  B ARG   A 1 39  ? 43.010 -7.270  41.262 0.46 69.88  ? 40  ARG   A CZ  1 
ATOM   346  N  NH1 A ARG   A 1 39  ? 42.833 -9.259  44.578 0.54 47.28  ? 40  ARG   A NH1 1 
ATOM   347  N  NH1 B ARG   A 1 39  ? 41.936 -7.725  41.896 0.46 53.17  ? 40  ARG   A NH1 1 
ATOM   348  N  NH2 A ARG   A 1 39  ? 43.810 -10.520 42.937 0.54 44.71  ? 40  ARG   A NH2 1 
ATOM   349  N  NH2 B ARG   A 1 39  ? 43.482 -6.067  41.564 0.46 57.73  ? 40  ARG   A NH2 1 
ATOM   350  N  N   A GLU   A 1 40  ? 39.459 -13.086 36.729 0.54 30.55  ? 41  GLU   A N   1 
ATOM   351  N  N   B GLU   A 1 40  ? 39.621 -12.668 36.353 0.46 30.90  ? 41  GLU   A N   1 
ATOM   352  C  CA  A GLU   A 1 40  ? 39.440 -14.212 35.793 0.54 29.61  ? 41  GLU   A CA  1 
ATOM   353  C  CA  B GLU   A 1 40  ? 39.382 -13.990 35.739 0.46 30.18  ? 41  GLU   A CA  1 
ATOM   354  C  C   A GLU   A 1 40  ? 39.717 -13.797 34.353 0.54 32.18  ? 41  GLU   A C   1 
ATOM   355  C  C   B GLU   A 1 40  ? 39.525 -13.838 34.223 0.46 32.49  ? 41  GLU   A C   1 
ATOM   356  O  O   A GLU   A 1 40  ? 39.391 -12.683 33.944 0.54 30.29  ? 41  GLU   A O   1 
ATOM   357  O  O   B GLU   A 1 40  ? 38.946 -12.916 33.646 0.46 30.54  ? 41  GLU   A O   1 
ATOM   358  C  CB  A GLU   A 1 40  ? 38.109 -14.990 35.888 0.54 30.52  ? 41  GLU   A CB  1 
ATOM   359  C  CB  B GLU   A 1 40  ? 37.991 -14.544 36.107 0.46 31.32  ? 41  GLU   A CB  1 
ATOM   360  C  CG  A GLU   A 1 40  ? 37.830 -15.569 37.269 0.54 46.20  ? 41  GLU   A CG  1 
ATOM   361  C  CG  B GLU   A 1 40  ? 37.900 -15.075 37.529 0.46 44.42  ? 41  GLU   A CG  1 
ATOM   362  C  CD  A GLU   A 1 40  ? 38.169 -17.038 37.426 0.54 82.81  ? 41  GLU   A CD  1 
ATOM   363  C  CD  B GLU   A 1 40  ? 38.150 -16.564 37.653 0.46 79.04  ? 41  GLU   A CD  1 
ATOM   364  O  OE1 A GLU   A 1 40  ? 37.436 -17.884 36.862 0.54 83.74  ? 41  GLU   A OE1 1 
ATOM   365  O  OE1 B GLU   A 1 40  ? 39.215 -16.942 38.192 0.46 81.02  ? 41  GLU   A OE1 1 
ATOM   366  O  OE2 A GLU   A 1 40  ? 39.164 -17.345 38.123 0.54 83.49  ? 41  GLU   A OE2 1 
ATOM   367  O  OE2 B GLU   A 1 40  ? 37.284 -17.353 37.209 0.46 79.90  ? 41  GLU   A OE2 1 
ATOM   368  N  N   . GLN   A 1 41  ? 40.308 -14.725 33.582 1.00 28.71  ? 42  GLN   A N   1 
ATOM   369  C  CA  . GLN   A 1 41  ? 40.636 -14.592 32.168 1.00 27.96  ? 42  GLN   A CA  1 
ATOM   370  C  C   . GLN   A 1 41  ? 40.002 -15.721 31.379 1.00 30.45  ? 42  GLN   A C   1 
ATOM   371  O  O   . GLN   A 1 41  ? 40.067 -16.871 31.818 1.00 30.37  ? 42  GLN   A O   1 
ATOM   372  C  CB  . GLN   A 1 41  ? 42.161 -14.634 31.998 1.00 30.47  ? 42  GLN   A CB  1 
ATOM   373  C  CG  . GLN   A 1 41  ? 42.872 -13.400 32.548 1.00 46.30  ? 42  GLN   A CG  1 
ATOM   374  C  CD  . GLN   A 1 41  ? 44.343 -13.330 32.211 1.00 66.25  ? 42  GLN   A CD  1 
ATOM   375  O  OE1 . GLN   A 1 41  ? 44.917 -14.193 31.529 1.00 60.21  ? 42  GLN   A OE1 1 
ATOM   376  N  NE2 . GLN   A 1 41  ? 44.989 -12.283 32.692 1.00 68.20  ? 42  GLN   A NE2 1 
ATOM   377  N  N   . PHE   A 1 42  ? 39.411 -15.402 30.209 1.00 24.43  ? 43  PHE   A N   1 
ATOM   378  C  CA  . PHE   A 1 42  ? 38.750 -16.392 29.344 1.00 24.56  ? 43  PHE   A CA  1 
ATOM   379  C  C   . PHE   A 1 42  ? 39.260 -16.213 27.939 1.00 28.30  ? 43  PHE   A C   1 
ATOM   380  O  O   . PHE   A 1 42  ? 39.106 -15.124 27.376 1.00 28.62  ? 43  PHE   A O   1 
ATOM   381  C  CB  . PHE   A 1 42  ? 37.224 -16.188 29.352 1.00 25.19  ? 43  PHE   A CB  1 
ATOM   382  C  CG  . PHE   A 1 42  ? 36.607 -16.310 30.720 1.00 26.93  ? 43  PHE   A CG  1 
ATOM   383  C  CD1 . PHE   A 1 42  ? 36.492 -15.199 31.554 1.00 28.90  ? 43  PHE   A CD1 1 
ATOM   384  C  CD2 . PHE   A 1 42  ? 36.123 -17.534 31.174 1.00 29.75  ? 43  PHE   A CD2 1 
ATOM   385  C  CE1 . PHE   A 1 42  ? 35.928 -15.316 32.827 1.00 30.78  ? 43  PHE   A CE1 1 
ATOM   386  C  CE2 . PHE   A 1 42  ? 35.566 -17.650 32.454 1.00 32.89  ? 43  PHE   A CE2 1 
ATOM   387  C  CZ  . PHE   A 1 42  ? 35.474 -16.540 33.270 1.00 30.76  ? 43  PHE   A CZ  1 
ATOM   388  N  N   . ARG   A 1 43  ? 39.899 -17.247 27.384 1.00 25.38  ? 44  ARG   A N   1 
ATOM   389  C  CA  . ARG   A 1 43  ? 40.405 -17.200 26.012 1.00 24.30  ? 44  ARG   A CA  1 
ATOM   390  C  C   . ARG   A 1 43  ? 39.262 -17.588 25.057 1.00 27.21  ? 44  ARG   A C   1 
ATOM   391  O  O   . ARG   A 1 43  ? 38.457 -18.480 25.363 1.00 26.22  ? 44  ARG   A O   1 
ATOM   392  C  CB  . ARG   A 1 43  ? 41.616 -18.137 25.834 1.00 25.72  ? 44  ARG   A CB  1 
ATOM   393  C  CG  . ARG   A 1 43  ? 42.844 -17.702 26.684 1.00 33.34  ? 44  ARG   A CG  1 
ATOM   394  C  CD  . ARG   A 1 43  ? 44.162 -18.135 26.049 1.00 39.22  ? 44  ARG   A CD  1 
ATOM   395  N  NE  . ARG   A 1 43  ? 44.192 -17.770 24.628 1.00 52.01  ? 44  ARG   A NE  1 
ATOM   396  C  CZ  . ARG   A 1 43  ? 44.714 -16.652 24.134 1.00 64.95  ? 44  ARG   A CZ  1 
ATOM   397  N  NH1 . ARG   A 1 43  ? 45.355 -15.804 24.926 1.00 58.12  ? 44  ARG   A NH1 1 
ATOM   398  N  NH2 . ARG   A 1 43  ? 44.643 -16.398 22.836 1.00 47.29  ? 44  ARG   A NH2 1 
ATOM   399  N  N   . ALA   A 1 44  ? 39.178 -16.928 23.898 1.00 24.08  ? 45  ALA   A N   1 
ATOM   400  C  CA  . ALA   A 1 44  ? 38.094 -17.235 22.945 1.00 23.30  ? 45  ALA   A CA  1 
ATOM   401  C  C   . ALA   A 1 44  ? 38.486 -16.827 21.540 1.00 24.80  ? 45  ALA   A C   1 
ATOM   402  O  O   . ALA   A 1 44  ? 39.580 -16.294 21.327 1.00 23.52  ? 45  ALA   A O   1 
ATOM   403  C  CB  . ALA   A 1 44  ? 36.804 -16.511 23.352 1.00 24.09  ? 45  ALA   A CB  1 
ATOM   404  N  N   . HIS   A 1 45  ? 37.592 -17.104 20.585 1.00 21.75  ? 46  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 45  ? 37.737 -16.700 19.196 1.00 20.88  ? 46  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 45  ? 36.850 -15.458 19.013 1.00 22.94  ? 46  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 45  ? 35.636 -15.508 19.302 1.00 21.90  ? 46  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 45  ? 37.260 -17.822 18.258 1.00 20.75  ? 46  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 45  ? 38.034 -19.090 18.428 1.00 23.52  ? 46  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 45  ? 37.564 -20.126 19.235 1.00 25.09  ? 46  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 45  ? 39.272 -19.413 17.974 1.00 24.73  ? 46  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 45  ? 38.505 -21.064 19.194 1.00 24.87  ? 46  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 45  ? 39.558 -20.671 18.463 1.00 24.74  ? 46  HIS   A NE2 1 
ATOM   414  N  N   . LYS   A 1 46  ? 37.452 -14.354 18.555 1.00 22.00  ? 47  LYS   A N   1 
ATOM   415  C  CA  . LYS   A 1 46  ? 36.717 -13.093 18.292 1.00 21.61  ? 47  LYS   A CA  1 
ATOM   416  C  C   . LYS   A 1 46  ? 35.472 -13.361 17.424 1.00 23.60  ? 47  LYS   A C   1 
ATOM   417  O  O   . LYS   A 1 46  ? 34.391 -12.874 17.748 1.00 21.17  ? 47  LYS   A O   1 
ATOM   418  C  CB  . LYS   A 1 46  ? 37.629 -12.082 17.566 1.00 23.91  ? 47  LYS   A CB  1 
ATOM   419  C  CG  . LYS   A 1 46  ? 38.628 -11.454 18.524 1.00 25.89  ? 47  LYS   A CG  1 
ATOM   420  C  CD  . LYS   A 1 46  ? 39.571 -10.551 17.745 1.00 24.75  ? 47  LYS   A CD  1 
ATOM   421  C  CE  . LYS   A 1 46  ? 40.644 -10.037 18.650 1.00 31.70  ? 47  LYS   A CE  1 
ATOM   422  N  NZ  . LYS   A 1 46  ? 41.617 -9.261  17.865 1.00 30.35  ? 47  LYS   A NZ  1 
ATOM   423  N  N   . THR   A 1 47  ? 35.615 -14.141 16.347 1.00 21.03  ? 48  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 47  ? 34.483 -14.389 15.442 1.00 21.35  ? 48  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 47  ? 33.300 -15.043 16.141 1.00 21.92  ? 48  THR   A C   1 
ATOM   426  O  O   . THR   A 1 47  ? 32.164 -14.648 15.889 1.00 22.31  ? 48  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 47  ? 34.918 -15.156 14.203 1.00 26.73  ? 48  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 47  ? 35.529 -16.366 14.637 1.00 28.63  ? 48  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 47  ? 35.824 -14.310 13.289 1.00 28.57  ? 48  THR   A CG2 1 
ATOM   430  N  N   . VAL   A 1 48  ? 33.551 -16.021 17.022 1.00 18.94  ? 49  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 48  ? 32.469 -16.708 17.750 1.00 18.76  ? 49  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 48  ? 31.800 -15.722 18.708 1.00 21.09  ? 49  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 48  ? 30.563 -15.675 18.783 1.00 19.61  ? 49  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 48  ? 32.992 -17.963 18.496 1.00 20.24  ? 49  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 48  ? 31.869 -18.586 19.345 1.00 20.77  ? 49  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 48  ? 33.521 -18.995 17.481 1.00 20.17  ? 49  VAL   A CG2 1 
ATOM   437  N  N   . LEU   A 1 49  ? 32.609 -14.920 19.433 1.00 20.00  ? 50  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 49  ? 32.035 -13.919 20.335 1.00 19.32  ? 50  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 49  ? 31.135 -12.926 19.581 1.00 21.83  ? 50  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 49  ? 30.018 -12.649 20.031 1.00 22.22  ? 50  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 49  ? 33.141 -13.146 21.079 1.00 18.85  ? 50  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 49  ? 34.123 -13.945 21.967 1.00 21.74  ? 50  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 49  ? 35.175 -13.007 22.582 1.00 21.95  ? 50  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 49  ? 33.382 -14.730 23.059 1.00 23.72  ? 50  LEU   A CD2 1 
ATOM   445  N  N   . MET   A 1 50  ? 31.584 -12.449 18.408 1.00 18.97  ? 51  MET   A N   1 
ATOM   446  C  CA  . MET   A 1 50  ? 30.795 -11.520 17.588 1.00 20.37  ? 51  MET   A CA  1 
ATOM   447  C  C   . MET   A 1 50  ? 29.508 -12.169 17.095 1.00 24.22  ? 51  MET   A C   1 
ATOM   448  O  O   . MET   A 1 50  ? 28.451 -11.532 17.112 1.00 24.17  ? 51  MET   A O   1 
ATOM   449  C  CB  . MET   A 1 50  ? 31.600 -11.051 16.381 1.00 22.14  ? 51  MET   A CB  1 
ATOM   450  C  CG  . MET   A 1 50  ? 32.830 -10.264 16.768 1.00 24.09  ? 51  MET   A CG  1 
ATOM   451  S  SD  . MET   A 1 50  ? 33.888 -10.169 15.314 1.00 28.45  ? 51  MET   A SD  1 
ATOM   452  C  CE  . MET   A 1 50  ? 33.117 -8.830  14.505 1.00 25.24  ? 51  MET   A CE  1 
ATOM   453  N  N   . ALA   A 1 51  ? 29.586 -13.456 16.700 1.00 20.89  ? 52  ALA   A N   1 
ATOM   454  C  CA  . ALA   A 1 51  ? 28.423 -14.196 16.190 1.00 20.52  ? 52  ALA   A CA  1 
ATOM   455  C  C   . ALA   A 1 51  ? 27.339 -14.390 17.278 1.00 24.10  ? 52  ALA   A C   1 
ATOM   456  O  O   . ALA   A 1 51  ? 26.180 -14.613 16.937 1.00 24.67  ? 52  ALA   A O   1 
ATOM   457  C  CB  . ALA   A 1 51  ? 28.867 -15.565 15.645 1.00 20.61  ? 52  ALA   A CB  1 
ATOM   458  N  N   . CYS   A 1 52  ? 27.727 -14.337 18.574 1.00 20.08  ? 53  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 52  ? 26.812 -14.591 19.690 1.00 20.50  ? 53  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 52  ? 26.347 -13.379 20.484 1.00 23.66  ? 53  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 52  ? 25.393 -13.520 21.252 1.00 22.63  ? 53  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 52  ? 27.464 -15.590 20.641 1.00 20.36  ? 53  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 52  ? 27.819 -17.186 19.893 1.00 22.89  ? 53  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 53  ? 27.097 -12.266 20.421 1.00 20.79  ? 54  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 53  ? 26.892 -11.126 21.315 1.00 20.46  ? 54  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 53  ? 26.892 -9.820  20.553 1.00 24.38  ? 54  SER   A C   1 
ATOM   467  O  O   . SER   A 1 53  ? 27.865 -9.522  19.842 1.00 22.31  ? 54  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 53  ? 28.030 -11.142 22.337 1.00 21.23  ? 54  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 53  ? 28.332 -9.896  22.947 1.00 24.30  ? 54  SER   A OG  1 
ATOM   470  N  N   . GLY   A 1 54  ? 25.845 -9.009  20.762 1.00 23.07  ? 55  GLY   A N   1 
ATOM   471  C  CA  . GLY   A 1 54  ? 25.772 -7.675  20.170 1.00 22.57  ? 55  GLY   A CA  1 
ATOM   472  C  C   . GLY   A 1 54  ? 26.897 -6.784  20.670 1.00 25.32  ? 55  GLY   A C   1 
ATOM   473  O  O   . GLY   A 1 54  ? 27.454 -5.989  19.899 1.00 24.32  ? 55  GLY   A O   1 
ATOM   474  N  N   . LEU   A 1 55  ? 27.306 -6.969  21.949 1.00 22.52  ? 56  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 55  ? 28.422 -6.173  22.492 1.00 22.76  ? 56  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 55  ? 29.762 -6.523  21.797 1.00 25.59  ? 56  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 55  ? 30.463 -5.610  21.340 1.00 23.95  ? 56  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 55  ? 28.523 -6.369  24.019 1.00 22.85  ? 56  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 55  ? 29.589 -5.487  24.698 1.00 28.03  ? 56  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 55  ? 29.170 -3.995  24.711 1.00 29.49  ? 56  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 55  ? 29.872 -5.979  26.099 1.00 26.29  ? 56  LEU   A CD2 1 
ATOM   482  N  N   . PHE   A 1 56  ? 30.093 -7.825  21.682 1.00 21.53  ? 57  PHE   A N   1 
ATOM   483  C  CA  . PHE   A 1 56  ? 31.350 -8.222  21.010 1.00 20.56  ? 57  PHE   A CA  1 
ATOM   484  C  C   . PHE   A 1 56  ? 31.325 -7.872  19.543 1.00 24.29  ? 57  PHE   A C   1 
ATOM   485  O  O   . PHE   A 1 56  ? 32.354 -7.477  19.009 1.00 23.02  ? 57  PHE   A O   1 
ATOM   486  C  CB  . PHE   A 1 56  ? 31.715 -9.694  21.258 1.00 21.51  ? 57  PHE   A CB  1 
ATOM   487  C  CG  . PHE   A 1 56  ? 32.142 -9.922  22.694 1.00 22.43  ? 57  PHE   A CG  1 
ATOM   488  C  CD1 . PHE   A 1 56  ? 33.206 -9.207  23.249 1.00 24.64  ? 57  PHE   A CD1 1 
ATOM   489  C  CD2 . PHE   A 1 56  ? 31.498 -10.870 23.485 1.00 23.33  ? 57  PHE   A CD2 1 
ATOM   490  C  CE1 . PHE   A 1 56  ? 33.575 -9.388  24.599 1.00 24.81  ? 57  PHE   A CE1 1 
ATOM   491  C  CE2 . PHE   A 1 56  ? 31.905 -11.094 24.812 1.00 25.23  ? 57  PHE   A CE2 1 
ATOM   492  C  CZ  . PHE   A 1 56  ? 32.933 -10.351 25.361 1.00 23.10  ? 57  PHE   A CZ  1 
ATOM   493  N  N   . TYR   A 1 57  ? 30.142 -7.946  18.900 1.00 21.33  ? 58  TYR   A N   1 
ATOM   494  C  CA  . TYR   A 1 57  ? 30.014 -7.552  17.484 1.00 22.13  ? 58  TYR   A CA  1 
ATOM   495  C  C   . TYR   A 1 57  ? 30.445 -6.081  17.322 1.00 26.56  ? 58  TYR   A C   1 
ATOM   496  O  O   . TYR   A 1 57  ? 31.243 -5.769  16.431 1.00 24.62  ? 58  TYR   A O   1 
ATOM   497  C  CB  . TYR   A 1 57  ? 28.560 -7.766  17.033 1.00 23.89  ? 58  TYR   A CB  1 
ATOM   498  C  CG  . TYR   A 1 57  ? 28.294 -7.254  15.642 1.00 27.76  ? 58  TYR   A CG  1 
ATOM   499  C  CD1 . TYR   A 1 57  ? 28.947 -7.799  14.540 1.00 29.08  ? 58  TYR   A CD1 1 
ATOM   500  C  CD2 . TYR   A 1 57  ? 27.402 -6.209  15.427 1.00 31.82  ? 58  TYR   A CD2 1 
ATOM   501  C  CE1 . TYR   A 1 57  ? 28.704 -7.322  13.248 1.00 31.49  ? 58  TYR   A CE1 1 
ATOM   502  C  CE2 . TYR   A 1 57  ? 27.151 -5.728  14.147 1.00 35.30  ? 58  TYR   A CE2 1 
ATOM   503  C  CZ  . TYR   A 1 57  ? 27.793 -6.298  13.062 1.00 42.14  ? 58  TYR   A CZ  1 
ATOM   504  O  OH  . TYR   A 1 57  ? 27.522 -5.813  11.816 1.00 48.08  ? 58  TYR   A OH  1 
ATOM   505  N  N   A SER   A 1 58  ? 29.919 -5.193  18.188 0.53 24.54  ? 59  SER   A N   1 
ATOM   506  N  N   B SER   A 1 58  ? 29.919 -5.197  18.190 0.47 24.58  ? 59  SER   A N   1 
ATOM   507  C  CA  A SER   A 1 58  ? 30.238 -3.764  18.189 0.53 25.30  ? 59  SER   A CA  1 
ATOM   508  C  CA  B SER   A 1 58  ? 30.243 -3.772  18.199 0.47 25.42  ? 59  SER   A CA  1 
ATOM   509  C  C   A SER   A 1 58  ? 31.727 -3.524  18.506 0.53 30.39  ? 59  SER   A C   1 
ATOM   510  C  C   B SER   A 1 58  ? 31.740 -3.562  18.473 0.47 30.19  ? 59  SER   A C   1 
ATOM   511  O  O   A SER   A 1 58  ? 32.362 -2.715  17.835 0.53 31.87  ? 59  SER   A O   1 
ATOM   512  O  O   B SER   A 1 58  ? 32.386 -2.808  17.749 0.47 31.35  ? 59  SER   A O   1 
ATOM   513  C  CB  A SER   A 1 58  ? 29.340 -3.023  19.176 0.53 27.53  ? 59  SER   A CB  1 
ATOM   514  C  CB  B SER   A 1 58  ? 29.410 -3.050  19.255 0.47 28.07  ? 59  SER   A CB  1 
ATOM   515  O  OG  A SER   A 1 58  ? 27.996 -3.017  18.719 0.53 30.03  ? 59  SER   A OG  1 
ATOM   516  O  OG  B SER   A 1 58  ? 29.746 -1.674  19.290 0.47 33.68  ? 59  SER   A OG  1 
ATOM   517  N  N   . ILE   A 1 59  ? 32.284 -4.252  19.497 1.00 26.15  ? 60  ILE   A N   1 
ATOM   518  C  CA  . ILE   A 1 59  ? 33.702 -4.136  19.900 1.00 25.52  ? 60  ILE   A CA  1 
ATOM   519  C  C   . ILE   A 1 59  ? 34.651 -4.516  18.762 1.00 28.53  ? 60  ILE   A C   1 
ATOM   520  O  O   . ILE   A 1 59  ? 35.533 -3.728  18.407 1.00 29.96  ? 60  ILE   A O   1 
ATOM   521  C  CB  . ILE   A 1 59  ? 34.030 -4.965  21.201 1.00 27.37  ? 60  ILE   A CB  1 
ATOM   522  C  CG1 . ILE   A 1 59  ? 33.284 -4.416  22.441 1.00 27.58  ? 60  ILE   A CG1 1 
ATOM   523  C  CG2 . ILE   A 1 59  ? 35.563 -5.016  21.464 1.00 25.77  ? 60  ILE   A CG2 1 
ATOM   524  C  CD1 . ILE   A 1 59  ? 33.354 -5.373  23.650 1.00 30.12  ? 60  ILE   A CD1 1 
ATOM   525  N  N   . PHE   A 1 60  ? 34.466 -5.706  18.182 1.00 24.12  ? 61  PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 60  ? 35.447 -6.144  17.206 1.00 24.12  ? 61  PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 60  ? 35.222 -5.612  15.794 1.00 28.11  ? 61  PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 60  ? 36.060 -5.880  14.927 1.00 29.20  ? 61  PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 60  ? 35.612 -7.670  17.241 1.00 24.25  ? 61  PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 60  ? 36.027 -8.160  18.620 1.00 24.92  ? 61  PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 60  ? 37.236 -7.761  19.187 1.00 28.52  ? 61  PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 60  ? 35.222 -9.039  19.333 1.00 25.17  ? 61  PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 60  ? 37.613 -8.209  20.465 1.00 29.03  ? 61  PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 60  ? 35.614 -9.512  20.594 1.00 27.98  ? 61  PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 60  ? 36.802 -9.091  21.153 1.00 27.04  ? 61  PHE   A CZ  1 
ATOM   536  N  N   . THR   A 1 61  ? 34.153 -4.823  15.560 1.00 26.13  ? 62  THR   A N   1 
ATOM   537  C  CA  . THR   A 1 61  ? 33.997 -4.140  14.259 1.00 26.54  ? 62  THR   A CA  1 
ATOM   538  C  C   . THR   A 1 61  ? 34.535 -2.715  14.388 1.00 33.19  ? 62  THR   A C   1 
ATOM   539  O  O   . THR   A 1 61  ? 34.614 -1.987  13.391 1.00 32.86  ? 62  THR   A O   1 
ATOM   540  C  CB  . THR   A 1 61  ? 32.571 -4.169  13.702 1.00 34.37  ? 62  THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 61  ? 31.669 -3.640  14.669 1.00 31.54  ? 62  THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 61  ? 32.142 -5.562  13.224 1.00 30.80  ? 62  THR   A CG2 1 
ATOM   543  N  N   . ASP   A 1 62  ? 34.939 -2.319  15.615 1.00 29.93  ? 63  ASP   A N   1 
ATOM   544  C  CA  . ASP   A 1 62  ? 35.551 -1.006  15.819 1.00 31.54  ? 63  ASP   A CA  1 
ATOM   545  C  C   . ASP   A 1 62  ? 36.976 -1.066  15.261 1.00 37.06  ? 63  ASP   A C   1 
ATOM   546  O  O   . ASP   A 1 62  ? 37.724 -1.978  15.608 1.00 34.83  ? 63  ASP   A O   1 
ATOM   547  C  CB  . ASP   A 1 62  ? 35.555 -0.616  17.308 1.00 33.13  ? 63  ASP   A CB  1 
ATOM   548  C  CG  . ASP   A 1 62  ? 36.287 0.689   17.529 1.00 44.15  ? 63  ASP   A CG  1 
ATOM   549  O  OD1 . ASP   A 1 62  ? 35.664 1.751   17.351 1.00 49.24  ? 63  ASP   A OD1 1 
ATOM   550  O  OD2 . ASP   A 1 62  ? 37.504 0.645   17.810 1.00 44.00  ? 63  ASP   A OD2 1 
ATOM   551  N  N   . GLN   A 1 63  ? 37.353 -0.077  14.419 1.00 37.81  ? 64  GLN   A N   1 
ATOM   552  C  CA  . GLN   A 1 63  ? 38.653 -0.009  13.743 1.00 39.08  ? 64  GLN   A CA  1 
ATOM   553  C  C   . GLN   A 1 63  ? 39.864 -0.039  14.685 1.00 42.52  ? 64  GLN   A C   1 
ATOM   554  O  O   . GLN   A 1 63  ? 40.935 -0.461  14.246 1.00 44.77  ? 64  GLN   A O   1 
ATOM   555  C  CB  . GLN   A 1 63  ? 38.729 1.195   12.787 1.00 42.74  ? 64  GLN   A CB  1 
ATOM   556  C  CG  . GLN   A 1 63  ? 37.905 1.003   11.515 1.00 59.35  ? 64  GLN   A CG  1 
ATOM   557  N  N   . LEU   A 1 64  ? 39.717 0.411   15.954 1.00 35.37  ? 65  LEU   A N   1 
ATOM   558  C  CA  . LEU   A 1 64  ? 40.807 0.325   16.926 1.00 34.92  ? 65  LEU   A CA  1 
ATOM   559  C  C   . LEU   A 1 64  ? 40.710 -0.936  17.776 1.00 38.57  ? 65  LEU   A C   1 
ATOM   560  O  O   . LEU   A 1 64  ? 41.724 -1.591  18.006 1.00 40.09  ? 65  LEU   A O   1 
ATOM   561  C  CB  . LEU   A 1 64  ? 40.832 1.545   17.879 1.00 35.86  ? 65  LEU   A CB  1 
ATOM   562  C  CG  . LEU   A 1 64  ? 41.430 2.831   17.345 1.00 43.01  ? 65  LEU   A CG  1 
ATOM   563  C  CD1 . LEU   A 1 64  ? 41.336 3.928   18.386 1.00 44.20  ? 65  LEU   A CD1 1 
ATOM   564  C  CD2 . LEU   A 1 64  ? 42.892 2.652   16.922 1.00 47.53  ? 65  LEU   A CD2 1 
ATOM   565  N  N   . LYS   A 1 65  ? 39.512 -1.243  18.311 1.00 31.70  ? 66  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 65  ? 39.350 -2.369  19.230 1.00 30.14  ? 66  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 65  ? 39.486 -3.731  18.550 1.00 35.79  ? 66  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 65  ? 39.858 -4.692  19.218 1.00 35.48  ? 66  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 65  ? 38.035 -2.275  20.031 1.00 30.16  ? 66  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 65  ? 37.932 -1.019  20.911 1.00 30.11  ? 66  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 65  ? 36.647 -1.057  21.732 1.00 29.68  ? 66  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 65  ? 36.336 0.273   22.391 1.00 34.85  ? 66  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 65  ? 35.799 1.275   21.446 1.00 37.49  ? 66  LYS   A NZ  1 
ATOM   574  N  N   . CYS   A 1 66  ? 39.237 -3.802  17.226 1.00 35.03  ? 67  CYS   A N   1 
ATOM   575  C  CA  . CYS   A 1 66  ? 39.368 -5.051  16.448 1.00 35.19  ? 67  CYS   A CA  1 
ATOM   576  C  C   . CYS   A 1 66  ? 40.765 -5.669  16.600 1.00 39.39  ? 67  CYS   A C   1 
ATOM   577  O  O   . CYS   A 1 66  ? 40.910 -6.885  16.439 1.00 39.69  ? 67  CYS   A O   1 
ATOM   578  C  CB  . CYS   A 1 66  ? 39.016 -4.828  14.977 1.00 37.33  ? 67  CYS   A CB  1 
ATOM   579  S  SG  . CYS   A 1 66  ? 40.157 -3.734  14.076 1.00 43.75  ? 67  CYS   A SG  1 
ATOM   580  N  N   . ASN   A 1 67  ? 41.788 -4.818  16.881 1.00 35.29  ? 68  ASN   A N   1 
ATOM   581  C  CA  . ASN   A 1 67  ? 43.189 -5.210  17.004 1.00 36.00  ? 68  ASN   A CA  1 
ATOM   582  C  C   . ASN   A 1 67  ? 43.664 -5.503  18.426 1.00 38.86  ? 68  ASN   A C   1 
ATOM   583  O  O   . ASN   A 1 67  ? 44.831 -5.863  18.621 1.00 37.70  ? 68  ASN   A O   1 
ATOM   584  C  CB  . ASN   A 1 67  ? 44.090 -4.159  16.330 1.00 37.51  ? 68  ASN   A CB  1 
ATOM   585  C  CG  . ASN   A 1 67  ? 43.842 -4.087  14.834 1.00 53.26  ? 68  ASN   A CG  1 
ATOM   586  O  OD1 . ASN   A 1 67  ? 43.732 -3.008  14.252 1.00 52.94  ? 68  ASN   A OD1 1 
ATOM   587  N  ND2 . ASN   A 1 67  ? 43.689 -5.237  14.182 1.00 42.57  ? 68  ASN   A ND2 1 
ATOM   588  N  N   . LEU   A 1 68  ? 42.779 -5.353  19.422 1.00 35.15  ? 69  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 68  ? 43.170 -5.620  20.800 1.00 34.17  ? 69  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 68  ? 43.172 -7.118  21.077 1.00 36.63  ? 69  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 68  ? 42.286 -7.835  20.585 1.00 35.17  ? 69  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 68  ? 42.225 -4.909  21.788 1.00 34.24  ? 69  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 68  ? 42.206 -3.374  21.715 1.00 39.00  ? 69  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 68  ? 41.132 -2.821  22.629 1.00 38.92  ? 69  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 68  ? 43.575 -2.772  22.076 1.00 40.92  ? 69  LEU   A CD2 1 
ATOM   596  N  N   A SER   A 1 69  ? 44.156 -7.592  21.859 0.51 33.69  ? 70  SER   A N   1 
ATOM   597  N  N   B SER   A 1 69  ? 44.159 -7.579  21.863 0.49 33.51  ? 70  SER   A N   1 
ATOM   598  C  CA  A SER   A 1 69  ? 44.253 -9.007  22.233 0.51 33.24  ? 70  SER   A CA  1 
ATOM   599  C  CA  B SER   A 1 69  ? 44.306 -8.983  22.258 0.49 33.03  ? 70  SER   A CA  1 
ATOM   600  C  C   A SER   A 1 69  ? 43.638 -9.239  23.621 0.51 34.02  ? 70  SER   A C   1 
ATOM   601  C  C   B SER   A 1 69  ? 43.663 -9.230  23.627 0.49 33.95  ? 70  SER   A C   1 
ATOM   602  O  O   A SER   A 1 69  ? 43.446 -10.385 24.023 0.51 31.84  ? 70  SER   A O   1 
ATOM   603  O  O   B SER   A 1 69  ? 43.478 -10.381 24.022 0.49 31.77  ? 70  SER   A O   1 
ATOM   604  C  CB  A SER   A 1 69  ? 45.704 -9.481  22.194 0.51 38.27  ? 70  SER   A CB  1 
ATOM   605  C  CB  B SER   A 1 69  ? 45.781 -9.372  22.295 0.49 37.71  ? 70  SER   A CB  1 
ATOM   606  O  OG  A SER   A 1 69  ? 46.504 -8.764  23.118 0.51 47.19  ? 70  SER   A OG  1 
ATOM   607  O  OG  B SER   A 1 69  ? 46.329 -9.384  20.988 0.49 44.76  ? 70  SER   A OG  1 
ATOM   608  N  N   . VAL   A 1 70  ? 43.353 -8.142  24.358 1.00 31.07  ? 71  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 70  ? 42.744 -8.181  25.695 1.00 30.71  ? 71  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 70  ? 41.554 -7.212  25.733 1.00 31.71  ? 71  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 70  ? 41.688 -6.048  25.327 1.00 31.58  ? 71  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 70  ? 43.763 -7.848  26.831 1.00 36.25  ? 71  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 70  ? 43.095 -7.883  28.211 1.00 36.40  ? 71  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 70  ? 44.983 -8.774  26.798 1.00 36.88  ? 71  VAL   A CG2 1 
ATOM   615  N  N   . ILE   A 1 71  ? 40.406 -7.696  26.228 1.00 24.85  ? 72  ILE   A N   1 
ATOM   616  C  CA  . ILE   A 1 71  ? 39.201 -6.888  26.422 1.00 24.82  ? 72  ILE   A CA  1 
ATOM   617  C  C   . ILE   A 1 71  ? 38.806 -7.005  27.888 1.00 28.16  ? 72  ILE   A C   1 
ATOM   618  O  O   . ILE   A 1 71  ? 38.562 -8.119  28.367 1.00 27.99  ? 72  ILE   A O   1 
ATOM   619  C  CB  . ILE   A 1 71  ? 38.036 -7.267  25.460 1.00 26.62  ? 72  ILE   A CB  1 
ATOM   620  C  CG1 . ILE   A 1 71  ? 38.427 -7.102  23.947 1.00 27.75  ? 72  ILE   A CG1 1 
ATOM   621  C  CG2 . ILE   A 1 71  ? 36.732 -6.522  25.808 1.00 27.48  ? 72  ILE   A CG2 1 
ATOM   622  C  CD1 . ILE   A 1 71  ? 38.825 -5.647  23.470 1.00 30.41  ? 72  ILE   A CD1 1 
ATOM   623  N  N   . ASN   A 1 72  ? 38.702 -5.858  28.588 1.00 26.22  ? 73  ASN   A N   1 
ATOM   624  C  CA  . ASN   A 1 72  ? 38.309 -5.823  29.990 1.00 26.35  ? 73  ASN   A CA  1 
ATOM   625  C  C   . ASN   A 1 72  ? 36.826 -5.507  30.107 1.00 28.32  ? 73  ASN   A C   1 
ATOM   626  O  O   . ASN   A 1 72  ? 36.391 -4.440  29.662 1.00 26.86  ? 73  ASN   A O   1 
ATOM   627  C  CB  . ASN   A 1 72  ? 39.123 -4.773  30.771 1.00 31.22  ? 73  ASN   A CB  1 
ATOM   628  C  CG  . ASN   A 1 72  ? 40.603 -4.967  30.695 1.00 48.80  ? 73  ASN   A CG  1 
ATOM   629  O  OD1 . ASN   A 1 72  ? 41.139 -6.001  31.081 1.00 39.31  ? 73  ASN   A OD1 1 
ATOM   630  N  ND2 . ASN   A 1 72  ? 41.297 -3.958  30.214 1.00 44.44  ? 73  ASN   A ND2 1 
ATOM   631  N  N   . LEU   A 1 73  ? 36.054 -6.410  30.717 1.00 24.53  ? 74  LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 73  ? 34.628 -6.168  30.902 1.00 24.28  ? 74  LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 73  ? 34.388 -5.260  32.115 1.00 28.11  ? 74  LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 73  ? 35.258 -5.120  32.988 1.00 28.40  ? 74  LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 73  ? 33.822 -7.477  31.061 1.00 23.51  ? 74  LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 73  ? 33.870 -8.504  29.896 1.00 26.62  ? 74  LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 73  ? 32.742 -9.544  30.047 1.00 27.40  ? 74  LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 73  ? 33.814 -7.829  28.514 1.00 25.84  ? 74  LEU   A CD2 1 
ATOM   639  N  N   . ASP   A 1 74  ? 33.192 -4.680  32.185 1.00 25.48  ? 75  ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 74  ? 32.769 -3.809  33.289 1.00 25.85  ? 75  ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 74  ? 32.978 -4.563  34.626 1.00 30.02  ? 75  ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 74  ? 32.649 -5.754  34.690 1.00 28.94  ? 75  ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 74  ? 31.290 -3.444  33.089 1.00 26.98  ? 75  ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 74  ? 30.740 -2.425  34.071 1.00 37.05  ? 75  ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 74  ? 30.622 -2.756  35.274 1.00 38.56  ? 75  ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 74  ? 30.394 -1.317  33.635 1.00 37.93  ? 75  ASP   A OD2 1 
ATOM   647  N  N   . PRO   A 1 75  ? 33.526 -3.913  35.678 1.00 31.54  ? 76  PRO   A N   1 
ATOM   648  C  CA  . PRO   A 1 75  ? 33.766 -4.639  36.949 1.00 32.32  ? 76  PRO   A CA  1 
ATOM   649  C  C   . PRO   A 1 75  ? 32.533 -5.230  37.623 1.00 35.44  ? 76  PRO   A C   1 
ATOM   650  O  O   . PRO   A 1 75  ? 32.688 -6.108  38.468 1.00 36.46  ? 76  PRO   A O   1 
ATOM   651  C  CB  . PRO   A 1 75  ? 34.458 -3.603  37.849 1.00 35.30  ? 76  PRO   A CB  1 
ATOM   652  C  CG  . PRO   A 1 75  ? 34.167 -2.275  37.228 1.00 40.18  ? 76  PRO   A CG  1 
ATOM   653  C  CD  . PRO   A 1 75  ? 34.005 -2.513  35.755 1.00 34.24  ? 76  PRO   A CD  1 
ATOM   654  N  N   . GLU   A 1 76  ? 31.321 -4.786  37.254 1.00 32.25  ? 77  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 76  ? 30.080 -5.316  37.827 1.00 33.67  ? 77  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 76  ? 29.790 -6.734  37.276 1.00 33.13  ? 77  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 76  ? 28.967 -7.447  37.842 1.00 32.43  ? 77  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 76  ? 28.895 -4.381  37.501 1.00 36.35  ? 77  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 76  ? 27.760 -4.414  38.510 1.00 56.51  ? 77  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 76  ? 27.975 -3.538  39.730 1.00 85.83  ? 77  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 76  ? 28.031 -2.297  39.569 1.00 86.86  ? 77  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 76  ? 28.082 -4.093  40.848 1.00 80.74  ? 77  GLU   A OE2 1 
ATOM   663  N  N   . ILE   A 1 77  ? 30.444 -7.126  36.170 1.00 27.65  ? 78  ILE   A N   1 
ATOM   664  C  CA  . ILE   A 1 77  ? 30.193 -8.436  35.556 1.00 26.93  ? 78  ILE   A CA  1 
ATOM   665  C  C   . ILE   A 1 77  ? 30.774 -9.563  36.375 1.00 30.30  ? 78  ILE   A C   1 
ATOM   666  O  O   . ILE   A 1 77  ? 31.943 -9.534  36.762 1.00 29.24  ? 78  ILE   A O   1 
ATOM   667  C  CB  . ILE   A 1 77  ? 30.653 -8.463  34.078 1.00 29.09  ? 78  ILE   A CB  1 
ATOM   668  C  CG1 . ILE   A 1 77  ? 29.956 -7.334  33.269 1.00 29.78  ? 78  ILE   A CG1 1 
ATOM   669  C  CG2 . ILE   A 1 77  ? 30.415 -9.849  33.446 1.00 26.44  ? 78  ILE   A CG2 1 
ATOM   670  C  CD1 . ILE   A 1 77  ? 28.363 -7.330  33.290 1.00 35.15  ? 78  ILE   A CD1 1 
ATOM   671  N  N   . ASN   A 1 78  ? 29.935 -10.549 36.627 1.00 31.10  ? 79  ASN   A N   1 
ATOM   672  C  CA  . ASN   A 1 78  ? 30.253 -11.736 37.404 1.00 31.58  ? 79  ASN   A CA  1 
ATOM   673  C  C   . ASN   A 1 78  ? 31.007 -12.770 36.544 1.00 31.47  ? 79  ASN   A C   1 
ATOM   674  O  O   . ASN   A 1 78  ? 30.497 -13.159 35.493 1.00 28.98  ? 79  ASN   A O   1 
ATOM   675  C  CB  . ASN   A 1 78  ? 28.957 -12.310 37.982 1.00 32.81  ? 79  ASN   A CB  1 
ATOM   676  C  CG  . ASN   A 1 78  ? 29.171 -13.581 38.745 1.00 48.49  ? 79  ASN   A CG  1 
ATOM   677  O  OD1 . ASN   A 1 78  ? 28.887 -14.656 38.241 1.00 37.83  ? 79  ASN   A OD1 1 
ATOM   678  N  ND2 . ASN   A 1 78  ? 29.700 -13.483 39.963 1.00 40.63  ? 79  ASN   A ND2 1 
ATOM   679  N  N   . PRO   A 1 79  ? 32.222 -13.221 36.961 1.00 29.70  ? 80  PRO   A N   1 
ATOM   680  C  CA  . PRO   A 1 79  ? 32.972 -14.207 36.153 1.00 28.78  ? 80  PRO   A CA  1 
ATOM   681  C  C   . PRO   A 1 79  ? 32.222 -15.520 35.894 1.00 31.58  ? 80  PRO   A C   1 
ATOM   682  O  O   . PRO   A 1 79  ? 32.319 -16.063 34.789 1.00 29.81  ? 80  PRO   A O   1 
ATOM   683  C  CB  . PRO   A 1 79  ? 34.246 -14.439 36.976 1.00 32.20  ? 80  PRO   A CB  1 
ATOM   684  C  CG  . PRO   A 1 79  ? 34.379 -13.212 37.832 1.00 37.17  ? 80  PRO   A CG  1 
ATOM   685  C  CD  . PRO   A 1 79  ? 32.975 -12.845 38.176 1.00 32.96  ? 80  PRO   A CD  1 
ATOM   686  N  N   . GLU   A 1 80  ? 31.449 -16.014 36.890 1.00 28.74  ? 81  GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 80  ? 30.680 -17.244 36.697 1.00 28.45  ? 81  GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 80  ? 29.583 -17.052 35.624 1.00 29.92  ? 81  GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 80  ? 29.435 -17.912 34.763 1.00 28.42  ? 81  GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 80  ? 30.096 -17.773 38.014 1.00 31.02  ? 81  GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 80  ? 29.513 -19.166 37.811 1.00 38.62  ? 81  GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 80  ? 28.698 -19.774 38.938 1.00 63.16  ? 81  GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 80  ? 28.705 -21.020 39.049 1.00 61.82  ? 81  GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 80  ? 28.040 -19.022 39.692 1.00 54.86  ? 81  GLU   A OE2 1 
ATOM   695  N  N   . GLY   A 1 81  ? 28.856 -15.925 35.683 1.00 27.70  ? 82  GLY   A N   1 
ATOM   696  C  CA  . GLY   A 1 81  ? 27.844 -15.584 34.689 1.00 26.65  ? 82  GLY   A CA  1 
ATOM   697  C  C   . GLY   A 1 81  ? 28.469 -15.532 33.304 1.00 27.39  ? 82  GLY   A C   1 
ATOM   698  O  O   . GLY   A 1 81  ? 27.916 -16.074 32.332 1.00 24.81  ? 82  GLY   A O   1 
ATOM   699  N  N   . PHE   A 1 82  ? 29.655 -14.909 33.211 1.00 23.44  ? 83  PHE   A N   1 
ATOM   700  C  CA  . PHE   A 1 82  ? 30.347 -14.848 31.919 1.00 21.79  ? 83  PHE   A CA  1 
ATOM   701  C  C   . PHE   A 1 82  ? 30.730 -16.264 31.453 1.00 24.59  ? 83  PHE   A C   1 
ATOM   702  O  O   . PHE   A 1 82  ? 30.530 -16.606 30.286 1.00 23.39  ? 83  PHE   A O   1 
ATOM   703  C  CB  . PHE   A 1 82  ? 31.598 -13.930 31.982 1.00 23.34  ? 83  PHE   A CB  1 
ATOM   704  C  CG  . PHE   A 1 82  ? 32.212 -13.812 30.604 1.00 23.91  ? 83  PHE   A CG  1 
ATOM   705  C  CD1 . PHE   A 1 82  ? 31.639 -12.985 29.637 1.00 26.95  ? 83  PHE   A CD1 1 
ATOM   706  C  CD2 . PHE   A 1 82  ? 33.271 -14.632 30.224 1.00 24.72  ? 83  PHE   A CD2 1 
ATOM   707  C  CE1 . PHE   A 1 82  ? 32.141 -12.950 28.334 1.00 27.98  ? 83  PHE   A CE1 1 
ATOM   708  C  CE2 . PHE   A 1 82  ? 33.782 -14.585 28.926 1.00 26.33  ? 83  PHE   A CE2 1 
ATOM   709  C  CZ  . PHE   A 1 82  ? 33.199 -13.764 27.980 1.00 25.22  ? 83  PHE   A CZ  1 
ATOM   710  N  N   . CYS   A 1 83  ? 31.291 -17.071 32.354 1.00 25.16  ? 84  CYS   A N   1 
ATOM   711  C  CA  . CYS   A 1 83  ? 31.694 -18.440 32.022 1.00 27.10  ? 84  CYS   A CA  1 
ATOM   712  C  C   . CYS   A 1 83  ? 30.521 -19.268 31.445 1.00 27.61  ? 84  CYS   A C   1 
ATOM   713  O  O   . CYS   A 1 83  ? 30.676 -19.955 30.420 1.00 25.88  ? 84  CYS   A O   1 
ATOM   714  C  CB  . CYS   A 1 83  ? 32.308 -19.122 33.240 1.00 30.66  ? 84  CYS   A CB  1 
ATOM   715  S  SG  . CYS   A 1 83  ? 33.017 -20.747 32.868 1.00 36.32  ? 84  CYS   A SG  1 
ATOM   716  N  N   . ILE   A 1 84  ? 29.339 -19.168 32.099 1.00 24.70  ? 85  ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 84  ? 28.120 -19.872 31.693 1.00 22.95  ? 85  ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 84  ? 27.721 -19.416 30.292 1.00 23.70  ? 85  ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 84  ? 27.368 -20.242 29.435 1.00 22.66  ? 85  ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 84  ? 26.998 -19.635 32.738 1.00 25.64  ? 85  ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 84  ? 27.311 -20.428 34.052 1.00 26.87  ? 85  ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 84  ? 25.592 -19.979 32.164 1.00 25.70  ? 85  ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 84  ? 26.563 -19.948 35.245 1.00 33.15  ? 85  ILE   A CD1 1 
ATOM   724  N  N   . LEU   A 1 85  ? 27.795 -18.110 30.060 1.00 20.44  ? 86  LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 85  ? 27.444 -17.576 28.737 1.00 20.45  ? 86  LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 85  ? 28.455 -17.929 27.660 1.00 23.96  ? 86  LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 85  ? 28.058 -18.200 26.527 1.00 22.18  ? 86  LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 85  ? 27.173 -16.083 28.810 1.00 21.09  ? 86  LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 85  ? 25.888 -15.722 29.591 1.00 26.32  ? 86  LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 85  ? 25.796 -14.253 29.742 1.00 26.73  ? 86  LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 85  ? 24.613 -16.223 28.881 1.00 26.80  ? 86  LEU   A CD2 1 
ATOM   732  N  N   . LEU   A 1 86  ? 29.760 -17.945 27.995 1.00 21.21  ? 87  LEU   A N   1 
ATOM   733  C  CA  . LEU   A 1 86  ? 30.789 -18.343 27.027 1.00 20.83  ? 87  LEU   A CA  1 
ATOM   734  C  C   . LEU   A 1 86  ? 30.555 -19.819 26.624 1.00 23.42  ? 87  LEU   A C   1 
ATOM   735  O  O   . LEU   A 1 86  ? 30.568 -20.159 25.440 1.00 21.66  ? 87  LEU   A O   1 
ATOM   736  C  CB  . LEU   A 1 86  ? 32.178 -18.128 27.638 1.00 21.06  ? 87  LEU   A CB  1 
ATOM   737  C  CG  . LEU   A 1 86  ? 33.345 -18.430 26.683 1.00 25.51  ? 87  LEU   A CG  1 
ATOM   738  C  CD1 . LEU   A 1 86  ? 33.302 -17.517 25.440 1.00 25.41  ? 87  LEU   A CD1 1 
ATOM   739  C  CD2 . LEU   A 1 86  ? 34.701 -18.292 27.421 1.00 27.19  ? 87  LEU   A CD2 1 
ATOM   740  N  N   . ASP   A 1 87  ? 30.289 -20.683 27.610 1.00 21.60  ? 88  ASP   A N   1 
ATOM   741  C  CA  . ASP   A 1 87  ? 29.947 -22.077 27.332 1.00 21.32  ? 88  ASP   A CA  1 
ATOM   742  C  C   . ASP   A 1 87  ? 28.727 -22.164 26.404 1.00 23.09  ? 88  ASP   A C   1 
ATOM   743  O  O   . ASP   A 1 87  ? 28.753 -22.942 25.459 1.00 23.19  ? 88  ASP   A O   1 
ATOM   744  C  CB  . ASP   A 1 87  ? 29.653 -22.800 28.644 1.00 24.56  ? 88  ASP   A CB  1 
ATOM   745  C  CG  . ASP   A 1 87  ? 30.896 -23.166 29.438 1.00 38.12  ? 88  ASP   A CG  1 
ATOM   746  O  OD1 . ASP   A 1 87  ? 32.014 -23.095 28.868 1.00 38.65  ? 88  ASP   A OD1 1 
ATOM   747  O  OD2 . ASP   A 1 87  ? 30.752 -23.529 30.627 1.00 38.36  ? 88  ASP   A OD2 1 
ATOM   748  N  N   . PHE   A 1 88  ? 27.661 -21.396 26.688 1.00 21.33  ? 89  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 88  ? 26.472 -21.342 25.821 1.00 19.43  ? 89  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 88  ? 26.854 -20.955 24.383 1.00 20.15  ? 89  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 88  ? 26.373 -21.572 23.416 1.00 18.95  ? 89  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 88  ? 25.425 -20.357 26.370 1.00 20.24  ? 89  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 88  ? 24.315 -20.088 25.378 1.00 20.47  ? 89  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 88  ? 23.363 -21.061 25.094 1.00 22.95  ? 89  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 88  ? 24.288 -18.902 24.641 1.00 23.08  ? 89  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 88  ? 22.369 -20.834 24.140 1.00 22.35  ? 89  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 88  ? 23.293 -18.683 23.672 1.00 25.71  ? 89  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 88  ? 22.340 -19.647 23.437 1.00 23.74  ? 89  PHE   A CZ  1 
ATOM   759  N  N   . MET   A 1 89  ? 27.677 -19.910 24.228 1.00 18.04  ? 90  MET   A N   1 
ATOM   760  C  CA  . MET   A 1 89  ? 28.071 -19.485 22.866 1.00 17.72  ? 90  MET   A CA  1 
ATOM   761  C  C   . MET   A 1 89  ? 28.634 -20.627 22.048 1.00 21.37  ? 90  MET   A C   1 
ATOM   762  O  O   . MET   A 1 89  ? 28.319 -20.747 20.863 1.00 21.09  ? 90  MET   A O   1 
ATOM   763  C  CB  . MET   A 1 89  ? 29.155 -18.400 22.963 1.00 18.32  ? 90  MET   A CB  1 
ATOM   764  C  CG  . MET   A 1 89  ? 28.638 -17.113 23.561 1.00 19.86  ? 90  MET   A CG  1 
ATOM   765  S  SD  . MET   A 1 89  ? 29.983 -15.871 23.482 1.00 23.82  ? 90  MET   A SD  1 
ATOM   766  C  CE  . MET   A 1 89  ? 29.282 -14.605 24.608 1.00 24.30  ? 90  MET   A CE  1 
ATOM   767  N  N   . TYR   A 1 90  ? 29.492 -21.453 22.673 1.00 18.08  ? 91  TYR   A N   1 
ATOM   768  C  CA  . TYR   A 1 90  ? 30.174 -22.547 21.971 1.00 18.20  ? 91  TYR   A CA  1 
ATOM   769  C  C   . TYR   A 1 90  ? 29.429 -23.863 21.944 1.00 22.64  ? 91  TYR   A C   1 
ATOM   770  O  O   . TYR   A 1 90  ? 29.914 -24.826 21.337 1.00 21.52  ? 91  TYR   A O   1 
ATOM   771  C  CB  . TYR   A 1 90  ? 31.562 -22.775 22.589 1.00 19.78  ? 91  TYR   A CB  1 
ATOM   772  C  CG  . TYR   A 1 90  ? 32.605 -21.787 22.107 1.00 21.15  ? 91  TYR   A CG  1 
ATOM   773  C  CD1 . TYR   A 1 90  ? 32.754 -20.540 22.720 1.00 22.69  ? 91  TYR   A CD1 1 
ATOM   774  C  CD2 . TYR   A 1 90  ? 33.463 -22.107 21.049 1.00 21.99  ? 91  TYR   A CD2 1 
ATOM   775  C  CE1 . TYR   A 1 90  ? 33.725 -19.627 22.283 1.00 23.30  ? 91  TYR   A CE1 1 
ATOM   776  C  CE2 . TYR   A 1 90  ? 34.478 -21.231 20.649 1.00 22.83  ? 91  TYR   A CE2 1 
ATOM   777  C  CZ  . TYR   A 1 90  ? 34.574 -19.977 21.235 1.00 24.96  ? 91  TYR   A CZ  1 
ATOM   778  O  OH  . TYR   A 1 90  ? 35.604 -19.162 20.847 1.00 23.06  ? 91  TYR   A OH  1 
ATOM   779  N  N   . THR   A 1 91  ? 28.291 -23.949 22.638 1.00 19.15  ? 92  THR   A N   1 
ATOM   780  C  CA  . THR   A 1 91  ? 27.599 -25.249 22.713 1.00 20.05  ? 92  THR   A CA  1 
ATOM   781  C  C   . THR   A 1 91  ? 26.089 -25.244 22.488 1.00 22.33  ? 92  THR   A C   1 
ATOM   782  O  O   . THR   A 1 91  ? 25.531 -26.335 22.285 1.00 21.24  ? 92  THR   A O   1 
ATOM   783  C  CB  . THR   A 1 91  ? 27.803 -25.921 24.113 1.00 23.53  ? 92  THR   A CB  1 
ATOM   784  O  OG1 . THR   A 1 91  ? 27.126 -25.173 25.129 1.00 23.55  ? 92  THR   A OG1 1 
ATOM   785  C  CG2 . THR   A 1 91  ? 29.271 -26.144 24.498 1.00 24.09  ? 92  THR   A CG2 1 
ATOM   786  N  N   A SER   A 1 92  ? 25.430 -24.068 22.572 0.67 19.22  ? 93  SER   A N   1 
ATOM   787  N  N   B SER   A 1 92  ? 25.435 -24.068 22.602 0.33 18.95  ? 93  SER   A N   1 
ATOM   788  C  CA  A SER   A 1 92  ? 23.957 -23.875 22.527 0.67 19.15  ? 93  SER   A CA  1 
ATOM   789  C  CA  B SER   A 1 92  ? 23.975 -23.852 22.542 0.33 18.95  ? 93  SER   A CA  1 
ATOM   790  C  C   A SER   A 1 92  ? 23.299 -24.271 23.863 0.67 21.83  ? 93  SER   A C   1 
ATOM   791  C  C   B SER   A 1 92  ? 23.278 -24.338 23.833 0.33 22.86  ? 93  SER   A C   1 
ATOM   792  O  O   A SER   A 1 92  ? 22.099 -24.085 24.012 0.67 21.75  ? 93  SER   A O   1 
ATOM   793  O  O   B SER   A 1 92  ? 22.053 -24.299 23.914 0.33 23.11  ? 93  SER   A O   1 
ATOM   794  C  CB  A SER   A 1 92  ? 23.287 -24.674 21.403 0.67 20.00  ? 93  SER   A CB  1 
ATOM   795  C  CB  B SER   A 1 92  ? 23.349 -24.495 21.299 0.33 20.78  ? 93  SER   A CB  1 
ATOM   796  O  OG  A SER   A 1 92  ? 23.903 -24.496 20.142 0.67 17.86  ? 93  SER   A OG  1 
ATOM   797  O  OG  B SER   A 1 92  ? 23.032 -25.865 21.492 0.33 23.28  ? 93  SER   A OG  1 
ATOM   798  N  N   A ARG   A 1 93  ? 24.084 -24.781 24.839 0.67 19.74  ? 94  ARG   A N   1 
ATOM   799  N  N   B ARG   A 1 93  ? 24.071 -24.760 24.847 0.33 20.21  ? 94  ARG   A N   1 
ATOM   800  C  CA  A ARG   A 1 93  ? 23.549 -25.221 26.130 0.67 19.83  ? 94  ARG   A CA  1 
ATOM   801  C  CA  B ARG   A 1 93  ? 23.585 -25.279 26.129 0.33 20.65  ? 94  ARG   A CA  1 
ATOM   802  C  C   A ARG   A 1 93  ? 23.780 -24.180 27.193 0.67 24.51  ? 94  ARG   A C   1 
ATOM   803  C  C   B ARG   A 1 93  ? 23.800 -24.240 27.224 0.33 24.86  ? 94  ARG   A C   1 
ATOM   804  O  O   A ARG   A 1 93  ? 24.903 -23.695 27.373 0.67 22.34  ? 94  ARG   A O   1 
ATOM   805  O  O   B ARG   A 1 93  ? 24.930 -23.787 27.433 0.33 23.45  ? 94  ARG   A O   1 
ATOM   806  C  CB  A ARG   A 1 93  ? 24.152 -26.562 26.575 0.67 22.57  ? 94  ARG   A CB  1 
ATOM   807  C  CB  B ARG   A 1 93  ? 24.293 -26.606 26.493 0.33 22.43  ? 94  ARG   A CB  1 
ATOM   808  C  CG  A ARG   A 1 93  ? 23.858 -27.715 25.614 0.67 28.18  ? 94  ARG   A CG  1 
ATOM   809  C  CG  B ARG   A 1 93  ? 24.188 -27.699 25.420 0.33 29.66  ? 94  ARG   A CG  1 
ATOM   810  C  CD  A ARG   A 1 93  ? 24.840 -28.860 25.835 0.67 38.31  ? 94  ARG   A CD  1 
ATOM   811  C  CD  B ARG   A 1 93  ? 23.062 -28.675 25.696 0.33 34.90  ? 94  ARG   A CD  1 
ATOM   812  N  NE  A ARG   A 1 93  ? 24.763 -29.380 27.203 0.67 48.47  ? 94  ARG   A NE  1 
ATOM   813  N  NE  B ARG   A 1 93  ? 22.921 -29.687 24.643 0.33 35.92  ? 94  ARG   A NE  1 
ATOM   814  C  CZ  A ARG   A 1 93  ? 23.961 -30.370 27.580 0.67 60.07  ? 94  ARG   A CZ  1 
ATOM   815  C  CZ  B ARG   A 1 93  ? 23.196 -30.980 24.797 0.33 47.09  ? 94  ARG   A CZ  1 
ATOM   816  N  NH1 A ARG   A 1 93  ? 23.176 -30.970 26.695 0.67 48.03  ? 94  ARG   A NH1 1 
ATOM   817  N  NH1 B ARG   A 1 93  ? 23.019 -31.826 23.791 0.33 36.41  ? 94  ARG   A NH1 1 
ATOM   818  N  NH2 A ARG   A 1 93  ? 23.945 -30.772 28.841 0.67 45.98  ? 94  ARG   A NH2 1 
ATOM   819  N  NH2 B ARG   A 1 93  ? 23.627 -31.440 25.963 0.33 30.58  ? 94  ARG   A NH2 1 
ATOM   820  N  N   . LEU   A 1 94  ? 22.715 -23.860 27.914 1.00 22.08  ? 95  LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 94  ? 22.771 -22.849 28.967 1.00 21.50  ? 95  LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 94  ? 22.549 -23.485 30.324 1.00 26.89  ? 95  LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 94  ? 21.485 -24.077 30.559 1.00 26.21  ? 95  LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 94  ? 21.709 -21.776 28.687 1.00 22.49  ? 95  LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 94  ? 21.739 -20.568 29.638 1.00 25.71  ? 95  LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 94  ? 23.005 -19.732 29.398 1.00 23.22  ? 95  LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 94  ? 20.475 -19.719 29.488 1.00 28.00  ? 95  LEU   A CD2 1 
ATOM   828  N  N   . ASN   A 1 95  ? 23.549 -23.364 31.224 1.00 25.89  ? 96  ASN   A N   1 
ATOM   829  C  CA  . ASN   A 1 95  ? 23.443 -23.924 32.585 1.00 27.26  ? 96  ASN   A CA  1 
ATOM   830  C  C   . ASN   A 1 95  ? 22.748 -22.914 33.518 1.00 32.01  ? 96  ASN   A C   1 
ATOM   831  O  O   . ASN   A 1 95  ? 23.398 -22.221 34.307 1.00 32.08  ? 96  ASN   A O   1 
ATOM   832  C  CB  . ASN   A 1 95  ? 24.823 -24.357 33.107 1.00 31.22  ? 96  ASN   A CB  1 
ATOM   833  C  CG  . ASN   A 1 95  ? 24.787 -24.985 34.492 1.00 49.24  ? 96  ASN   A CG  1 
ATOM   834  O  OD1 . ASN   A 1 95  ? 23.778 -25.537 34.924 1.00 40.14  ? 96  ASN   A OD1 1 
ATOM   835  N  ND2 . ASN   A 1 95  ? 25.886 -24.901 35.220 1.00 43.41  ? 96  ASN   A ND2 1 
ATOM   836  N  N   . LEU   A 1 96  ? 21.437 -22.787 33.355 1.00 29.01  ? 97  LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 96  ? 20.613 -21.844 34.108 1.00 30.63  ? 97  LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 96  ? 20.083 -22.507 35.377 1.00 34.60  ? 97  LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 96  ? 19.427 -23.555 35.315 1.00 33.93  ? 97  LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 96  ? 19.492 -21.342 33.186 1.00 31.63  ? 97  LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 96  ? 18.748 -20.082 33.559 1.00 37.94  ? 97  LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 96  ? 19.719 -18.876 33.690 1.00 38.35  ? 97  LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 96  ? 17.646 -19.811 32.535 1.00 37.37  ? 97  LEU   A CD2 1 
ATOM   844  N  N   . ARG   A 1 97  ? 20.449 -21.929 36.544 1.00 31.84  ? 98  ARG   A N   1 
ATOM   845  C  CA  . ARG   A 1 97  ? 20.089 -22.456 37.867 1.00 33.85  ? 98  ARG   A CA  1 
ATOM   846  C  C   . ARG   A 1 97  ? 19.553 -21.341 38.750 1.00 35.29  ? 98  ARG   A C   1 
ATOM   847  O  O   . ARG   A 1 97  ? 19.894 -20.171 38.537 1.00 32.53  ? 98  ARG   A O   1 
ATOM   848  C  CB  . ARG   A 1 97  ? 21.315 -23.108 38.541 1.00 36.91  ? 98  ARG   A CB  1 
ATOM   849  C  CG  . ARG   A 1 97  ? 21.929 -24.274 37.757 1.00 43.34  ? 98  ARG   A CG  1 
ATOM   850  C  CD  . ARG   A 1 97  ? 23.169 -24.855 38.425 1.00 59.27  ? 98  ARG   A CD  1 
ATOM   851  N  NE  . ARG   A 1 97  ? 22.880 -25.462 39.730 1.00 78.29  ? 98  ARG   A NE  1 
ATOM   852  C  CZ  . ARG   A 1 97  ? 22.483 -26.720 39.913 1.00 99.42  ? 98  ARG   A CZ  1 
ATOM   853  N  NH1 . ARG   A 1 97  ? 22.237 -27.173 41.136 1.00 86.90  ? 98  ARG   A NH1 1 
ATOM   854  N  NH2 . ARG   A 1 97  ? 22.314 -27.530 38.873 1.00 90.24  ? 98  ARG   A NH2 1 
ATOM   855  N  N   . GLU   A 1 98  ? 18.719 -21.681 39.747 1.00 34.17  ? 99  GLU   A N   1 
ATOM   856  C  CA  . GLU   A 1 98  ? 18.180 -20.662 40.661 1.00 34.18  ? 99  GLU   A CA  1 
ATOM   857  C  C   . GLU   A 1 98  ? 19.294 -19.754 41.234 1.00 38.45  ? 99  GLU   A C   1 
ATOM   858  O  O   . GLU   A 1 98  ? 19.113 -18.538 41.309 1.00 39.17  ? 99  GLU   A O   1 
ATOM   859  C  CB  . GLU   A 1 98  ? 17.385 -21.325 41.810 1.00 37.38  ? 99  GLU   A CB  1 
ATOM   860  C  CG  . GLU   A 1 98  ? 16.758 -20.339 42.779 1.00 48.30  ? 99  GLU   A CG  1 
ATOM   861  C  CD  . GLU   A 1 98  ? 16.018 -20.972 43.944 1.00 78.14  ? 99  GLU   A CD  1 
ATOM   862  O  OE1 . GLU   A 1 98  ? 16.567 -21.904 44.579 1.00 71.59  ? 99  GLU   A OE1 1 
ATOM   863  O  OE2 . GLU   A 1 98  ? 14.885 -20.523 44.229 1.00 78.73  ? 99  GLU   A OE2 1 
ATOM   864  N  N   . GLY   A 1 99  ? 20.428 -20.355 41.592 1.00 36.32  ? 100 GLY   A N   1 
ATOM   865  C  CA  . GLY   A 1 99  ? 21.565 -19.652 42.181 1.00 37.46  ? 100 GLY   A CA  1 
ATOM   866  C  C   . GLY   A 1 99  ? 22.357 -18.762 41.240 1.00 38.39  ? 100 GLY   A C   1 
ATOM   867  O  O   . GLY   A 1 99  ? 23.104 -17.893 41.697 1.00 38.90  ? 100 GLY   A O   1 
ATOM   868  N  N   . ASN   A 1 100 ? 22.204 -18.949 39.918 1.00 33.70  ? 101 ASN   A N   1 
ATOM   869  C  CA  . ASN   A 1 100 ? 22.980 -18.142 38.976 1.00 31.39  ? 101 ASN   A CA  1 
ATOM   870  C  C   . ASN   A 1 100 ? 22.135 -17.288 38.021 1.00 33.74  ? 101 ASN   A C   1 
ATOM   871  O  O   . ASN   A 1 100 ? 22.712 -16.498 37.264 1.00 32.56  ? 101 ASN   A O   1 
ATOM   872  C  CB  . ASN   A 1 100 ? 23.960 -19.044 38.197 1.00 30.87  ? 101 ASN   A CB  1 
ATOM   873  C  CG  . ASN   A 1 100 ? 23.310 -19.982 37.198 1.00 39.17  ? 101 ASN   A CG  1 
ATOM   874  O  OD1 . ASN   A 1 100 ? 22.252 -19.691 36.637 1.00 29.05  ? 101 ASN   A OD1 1 
ATOM   875  N  ND2 . ASN   A 1 100 ? 23.949 -21.114 36.922 1.00 31.66  ? 101 ASN   A ND2 1 
ATOM   876  N  N   . ILE   A 1 101 ? 20.791 -17.487 37.999 1.00 30.71  ? 102 ILE   A N   1 
ATOM   877  C  CA  . ILE   A 1 101 ? 19.915 -16.823 37.015 1.00 30.74  ? 102 ILE   A CA  1 
ATOM   878  C  C   . ILE   A 1 101 ? 20.041 -15.298 37.004 1.00 31.51  ? 102 ILE   A C   1 
ATOM   879  O  O   . ILE   A 1 101 ? 20.059 -14.705 35.915 1.00 28.93  ? 102 ILE   A O   1 
ATOM   880  C  CB  . ILE   A 1 101 ? 18.431 -17.261 37.084 1.00 35.26  ? 102 ILE   A CB  1 
ATOM   881  C  CG1 . ILE   A 1 101 ? 17.628 -16.691 35.877 1.00 35.51  ? 102 ILE   A CG1 1 
ATOM   882  C  CG2 . ILE   A 1 101 ? 17.780 -16.958 38.437 1.00 35.74  ? 102 ILE   A CG2 1 
ATOM   883  C  CD1 . ILE   A 1 101 ? 16.458 -17.522 35.439 1.00 38.26  ? 102 ILE   A CD1 1 
ATOM   884  N  N   . MET   A 1 102 ? 20.140 -14.665 38.179 1.00 30.25  ? 103 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 102 ? 20.277 -13.209 38.214 1.00 30.94  ? 103 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 102 ? 21.576 -12.730 37.565 1.00 33.00  ? 103 MET   A C   1 
ATOM   887  O  O   . MET   A 1 102 ? 21.537 -11.786 36.770 1.00 31.01  ? 103 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 102 ? 20.110 -12.653 39.642 1.00 35.16  ? 103 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 102 ? 18.742 -12.947 40.255 1.00 42.10  ? 103 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 102 ? 17.312 -12.595 39.192 1.00 48.30  ? 103 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 102 ? 17.197 -10.821 39.366 1.00 46.62  ? 103 MET   A CE  1 
ATOM   892  N  N   . ALA   A 1 103 ? 22.718 -13.404 37.868 1.00 30.81  ? 104 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 103 ? 24.032 -13.050 37.296 1.00 30.03  ? 104 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 103 ? 24.045 -13.338 35.801 1.00 30.72  ? 104 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 103 ? 24.570 -12.541 35.025 1.00 28.65  ? 104 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 103 ? 25.147 -13.834 37.979 1.00 31.40  ? 104 ALA   A CB  1 
ATOM   897  N  N   . VAL   A 1 104 ? 23.471 -14.479 35.392 1.00 25.92  ? 105 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 104 ? 23.413 -14.841 33.966 1.00 23.77  ? 105 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 104 ? 22.599 -13.808 33.180 1.00 27.13  ? 105 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 104 ? 23.081 -13.348 32.139 1.00 25.60  ? 105 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 104 ? 22.906 -16.296 33.764 1.00 26.97  ? 105 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 104 ? 22.598 -16.587 32.286 1.00 25.13  ? 105 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 104 ? 23.938 -17.287 34.288 1.00 27.58  ? 105 VAL   A CG2 1 
ATOM   904  N  N   A MET   A 1 105 ? 21.395 -13.436 33.673 0.20 25.83  ? 106 MET   A N   1 
ATOM   905  N  N   B MET   A 1 105 ? 21.396 -13.432 33.672 0.80 26.23  ? 106 MET   A N   1 
ATOM   906  C  CA  A MET   A 1 105 ? 20.537 -12.450 33.009 0.20 26.59  ? 106 MET   A CA  1 
ATOM   907  C  CA  B MET   A 1 105 ? 20.569 -12.448 32.967 0.80 27.32  ? 106 MET   A CA  1 
ATOM   908  C  C   A MET   A 1 105 ? 21.241 -11.100 32.875 0.20 30.51  ? 106 MET   A C   1 
ATOM   909  C  C   B MET   A 1 105 ? 21.272 -11.093 32.862 0.80 30.22  ? 106 MET   A C   1 
ATOM   910  O  O   A MET   A 1 105 ? 21.226 -10.519 31.789 0.20 29.51  ? 106 MET   A O   1 
ATOM   911  O  O   B MET   A 1 105 ? 21.269 -10.493 31.788 0.80 28.45  ? 106 MET   A O   1 
ATOM   912  C  CB  A MET   A 1 105 ? 19.196 -12.284 33.736 0.20 30.33  ? 106 MET   A CB  1 
ATOM   913  C  CB  B MET   A 1 105 ? 19.194 -12.281 33.617 0.80 31.12  ? 106 MET   A CB  1 
ATOM   914  C  CG  A MET   A 1 105 ? 18.232 -11.389 32.990 0.20 34.72  ? 106 MET   A CG  1 
ATOM   915  C  CG  B MET   A 1 105 ? 18.280 -11.355 32.822 0.80 35.47  ? 106 MET   A CG  1 
ATOM   916  S  SD  A MET   A 1 105 ? 16.713 -11.093 33.897 0.20 40.64  ? 106 MET   A SD  1 
ATOM   917  S  SD  B MET   A 1 105 ? 16.597 -11.344 33.463 0.80 41.13  ? 106 MET   A SD  1 
ATOM   918  C  CE  A MET   A 1 105 ? 16.152 -9.651  33.073 0.20 38.11  ? 106 MET   A CE  1 
ATOM   919  C  CE  B MET   A 1 105 ? 16.806 -10.330 35.009 0.80 39.28  ? 106 MET   A CE  1 
ATOM   920  N  N   . ALA   A 1 106 ? 21.864 -10.616 33.969 1.00 27.95  ? 107 ALA   A N   1 
ATOM   921  C  CA  . ALA   A 1 106 ? 22.599 -9.332  33.982 1.00 28.63  ? 107 ALA   A CA  1 
ATOM   922  C  C   . ALA   A 1 106 ? 23.767 -9.374  32.966 1.00 29.18  ? 107 ALA   A C   1 
ATOM   923  O  O   . ALA   A 1 106 ? 23.957 -8.415  32.195 1.00 28.19  ? 107 ALA   A O   1 
ATOM   924  C  CB  . ALA   A 1 106 ? 23.115 -9.040  35.384 1.00 30.33  ? 107 ALA   A CB  1 
ATOM   925  N  N   . THR   A 1 107 ? 24.504 -10.510 32.923 1.00 24.93  ? 108 THR   A N   1 
ATOM   926  C  CA  . THR   A 1 107 ? 25.616 -10.671 31.979 1.00 24.43  ? 108 THR   A CA  1 
ATOM   927  C  C   . THR   A 1 107 ? 25.081 -10.702 30.532 1.00 26.50  ? 108 THR   A C   1 
ATOM   928  O  O   . THR   A 1 107 ? 25.658 -10.044 29.666 1.00 23.96  ? 108 THR   A O   1 
ATOM   929  C  CB  . THR   A 1 107 ? 26.534 -11.861 32.354 1.00 28.57  ? 108 THR   A CB  1 
ATOM   930  O  OG1 . THR   A 1 107 ? 26.834 -11.830 33.757 1.00 27.98  ? 108 THR   A OG1 1 
ATOM   931  C  CG2 . THR   A 1 107 ? 27.849 -11.861 31.564 1.00 28.08  ? 108 THR   A CG2 1 
ATOM   932  N  N   . ALA   A 1 108 ? 23.968 -11.447 30.270 1.00 23.73  ? 109 ALA   A N   1 
ATOM   933  C  CA  . ALA   A 1 108 ? 23.387 -11.523 28.919 1.00 22.60  ? 109 ALA   A CA  1 
ATOM   934  C  C   . ALA   A 1 108 ? 22.860 -10.150 28.461 1.00 26.21  ? 109 ALA   A C   1 
ATOM   935  O  O   . ALA   A 1 108 ? 23.000 -9.804  27.289 1.00 25.01  ? 109 ALA   A O   1 
ATOM   936  C  CB  . ALA   A 1 108 ? 22.285 -12.588 28.867 1.00 23.42  ? 109 ALA   A CB  1 
ATOM   937  N  N   . MET   A 1 109 ? 22.314 -9.334  29.389 1.00 24.55  ? 110 MET   A N   1 
ATOM   938  C  CA  . MET   A 1 109 ? 21.861 -7.994  28.992 1.00 24.14  ? 110 MET   A CA  1 
ATOM   939  C  C   . MET   A 1 109 ? 23.059 -7.127  28.551 1.00 26.78  ? 110 MET   A C   1 
ATOM   940  O  O   . MET   A 1 109 ? 23.025 -6.484  27.502 1.00 27.08  ? 110 MET   A O   1 
ATOM   941  C  CB  . MET   A 1 109 ? 21.082 -7.333  30.144 1.00 27.01  ? 110 MET   A CB  1 
ATOM   942  C  CG  . MET   A 1 109 ? 19.713 -7.963  30.367 1.00 31.99  ? 110 MET   A CG  1 
ATOM   943  S  SD  . MET   A 1 109 ? 18.969 -7.374  31.914 1.00 39.94  ? 110 MET   A SD  1 
ATOM   944  C  CE  . MET   A 1 109 ? 18.731 -5.628  31.502 1.00 38.04  ? 110 MET   A CE  1 
ATOM   945  N  N   . TYR   A 1 110 ? 24.129 -7.161  29.338 1.00 24.81  ? 111 TYR   A N   1 
ATOM   946  C  CA  . TYR   A 1 110 ? 25.365 -6.421  29.068 1.00 23.93  ? 111 TYR   A CA  1 
ATOM   947  C  C   . TYR   A 1 110 ? 25.982 -6.884  27.728 1.00 27.18  ? 111 TYR   A C   1 
ATOM   948  O  O   . TYR   A 1 110 ? 26.373 -6.054  26.903 1.00 25.89  ? 111 TYR   A O   1 
ATOM   949  C  CB  . TYR   A 1 110 ? 26.341 -6.688  30.213 1.00 24.82  ? 111 TYR   A CB  1 
ATOM   950  C  CG  . TYR   A 1 110 ? 27.750 -6.188  29.976 1.00 25.38  ? 111 TYR   A CG  1 
ATOM   951  C  CD1 . TYR   A 1 110 ? 28.055 -4.829  30.062 1.00 28.34  ? 111 TYR   A CD1 1 
ATOM   952  C  CD2 . TYR   A 1 110 ? 28.794 -7.081  29.726 1.00 24.94  ? 111 TYR   A CD2 1 
ATOM   953  C  CE1 . TYR   A 1 110 ? 29.360 -4.366  29.867 1.00 27.26  ? 111 TYR   A CE1 1 
ATOM   954  C  CE2 . TYR   A 1 110 ? 30.102 -6.633  29.553 1.00 25.03  ? 111 TYR   A CE2 1 
ATOM   955  C  CZ  . TYR   A 1 110 ? 30.379 -5.275  29.635 1.00 28.21  ? 111 TYR   A CZ  1 
ATOM   956  O  OH  . TYR   A 1 110 ? 31.669 -4.853  29.511 1.00 27.10  ? 111 TYR   A OH  1 
ATOM   957  N  N   . LEU   A 1 111 ? 26.049 -8.206  27.516 1.00 23.21  ? 112 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 111 ? 26.613 -8.802  26.296 1.00 21.50  ? 112 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 111 ? 25.690 -8.684  25.081 1.00 24.86  ? 112 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 111 ? 26.114 -8.967  23.954 1.00 24.70  ? 112 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 111 ? 27.005 -10.273 26.536 1.00 20.44  ? 112 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 111 ? 28.153 -10.546 27.530 1.00 23.08  ? 112 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 111 ? 28.414 -12.069 27.640 1.00 23.62  ? 112 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 111 ? 29.455 -9.826  27.104 1.00 25.04  ? 112 LEU   A CD2 1 
ATOM   965  N  N   . GLN   A 1 112 ? 24.423 -8.305  25.307 1.00 22.74  ? 113 GLN   A N   1 
ATOM   966  C  CA  . GLN   A 1 112 ? 23.420 -8.177  24.238 1.00 23.64  ? 113 GLN   A CA  1 
ATOM   967  C  C   . GLN   A 1 112 ? 23.172 -9.534  23.561 1.00 26.61  ? 113 GLN   A C   1 
ATOM   968  O  O   . GLN   A 1 112 ? 23.438 -9.726  22.374 1.00 25.53  ? 113 GLN   A O   1 
ATOM   969  C  CB  . GLN   A 1 112 ? 23.777 -7.066  23.233 1.00 24.95  ? 113 GLN   A CB  1 
ATOM   970  C  CG  . GLN   A 1 112 ? 23.933 -5.681  23.879 1.00 25.60  ? 113 GLN   A CG  1 
ATOM   971  C  CD  . GLN   A 1 112 ? 24.638 -4.714  22.956 1.00 36.38  ? 113 GLN   A CD  1 
ATOM   972  O  OE1 . GLN   A 1 112 ? 24.548 -4.807  21.737 1.00 30.88  ? 113 GLN   A OE1 1 
ATOM   973  N  NE2 . GLN   A 1 112 ? 25.372 -3.774  23.520 1.00 35.44  ? 113 GLN   A NE2 1 
ATOM   974  N  N   . MET   A 1 113 ? 22.719 -10.488 24.371 1.00 23.83  ? 114 MET   A N   1 
ATOM   975  C  CA  . MET   A 1 113 ? 22.386 -11.861 23.948 1.00 23.67  ? 114 MET   A CA  1 
ATOM   976  C  C   . MET   A 1 113 ? 20.887 -12.020 24.209 1.00 29.23  ? 114 MET   A C   1 
ATOM   977  O  O   . MET   A 1 113 ? 20.456 -12.501 25.268 1.00 26.91  ? 114 MET   A O   1 
ATOM   978  C  CB  . MET   A 1 113 ? 23.236 -12.850 24.749 1.00 24.80  ? 114 MET   A CB  1 
ATOM   979  C  CG  . MET   A 1 113 ? 24.727 -12.705 24.438 1.00 25.40  ? 114 MET   A CG  1 
ATOM   980  S  SD  . MET   A 1 113 ? 25.755 -13.762 25.458 1.00 28.04  ? 114 MET   A SD  1 
ATOM   981  C  CE  . MET   A 1 113 ? 25.440 -15.419 24.629 1.00 25.17  ? 114 MET   A CE  1 
ATOM   982  N  N   . GLU   A 1 114 ? 20.093 -11.500 23.265 1.00 29.08  ? 115 GLU   A N   1 
ATOM   983  C  CA  . GLU   A 1 114 ? 18.628 -11.372 23.376 1.00 30.64  ? 115 GLU   A CA  1 
ATOM   984  C  C   . GLU   A 1 114 ? 17.876 -12.649 23.731 1.00 31.37  ? 115 GLU   A C   1 
ATOM   985  O  O   . GLU   A 1 114 ? 16.982 -12.584 24.569 1.00 30.65  ? 115 GLU   A O   1 
ATOM   986  C  CB  . GLU   A 1 114 ? 18.020 -10.750 22.107 1.00 33.53  ? 115 GLU   A CB  1 
ATOM   987  C  CG  . GLU   A 1 114 ? 18.538 -9.348  21.830 1.00 46.56  ? 115 GLU   A CG  1 
ATOM   988  N  N   . HIS   A 1 115 ? 18.219 -13.796 23.112 1.00 28.06  ? 116 HIS   A N   1 
ATOM   989  C  CA  . HIS   A 1 115 ? 17.489 -15.038 23.409 1.00 29.55  ? 116 HIS   A CA  1 
ATOM   990  C  C   . HIS   A 1 115 ? 17.718 -15.517 24.841 1.00 30.87  ? 116 HIS   A C   1 
ATOM   991  O  O   . HIS   A 1 115 ? 16.769 -15.988 25.488 1.00 31.78  ? 116 HIS   A O   1 
ATOM   992  C  CB  . HIS   A 1 115 ? 17.799 -16.123 22.379 1.00 31.46  ? 116 HIS   A CB  1 
ATOM   993  C  CG  . HIS   A 1 115 ? 17.355 -15.763 20.997 1.00 36.49  ? 116 HIS   A CG  1 
ATOM   994  N  ND1 . HIS   A 1 115 ? 16.023 -15.519 20.711 1.00 40.12  ? 116 HIS   A ND1 1 
ATOM   995  C  CD2 . HIS   A 1 115 ? 18.075 -15.656 19.857 1.00 38.43  ? 116 HIS   A CD2 1 
ATOM   996  C  CE1 . HIS   A 1 115 ? 15.979 -15.236 19.418 1.00 40.03  ? 116 HIS   A CE1 1 
ATOM   997  N  NE2 . HIS   A 1 115 ? 17.186 -15.317 18.860 1.00 39.35  ? 116 HIS   A NE2 1 
ATOM   998  N  N   . VAL   A 1 116 ? 18.963 -15.348 25.350 1.00 25.05  ? 117 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 116 ? 19.301 -15.703 26.731 1.00 24.77  ? 117 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 116 ? 18.512 -14.797 27.686 1.00 30.33  ? 117 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 116 ? 17.897 -15.298 28.632 1.00 28.12  ? 117 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 116 ? 20.823 -15.696 27.039 1.00 27.44  ? 117 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 116 ? 21.075 -15.950 28.528 1.00 27.64  ? 117 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 116 ? 21.562 -16.719 26.179 1.00 26.92  ? 117 VAL   A CG2 1 
ATOM   1005 N  N   . VAL   A 1 117 ? 18.510 -13.468 27.427 1.00 27.23  ? 118 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 117 ? 17.752 -12.508 28.253 1.00 27.67  ? 118 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 117 ? 16.268 -12.938 28.326 1.00 33.30  ? 118 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 117 ? 15.726 -13.035 29.420 1.00 32.18  ? 118 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 117 ? 17.929 -11.038 27.777 1.00 30.50  ? 118 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 117 ? 17.072 -10.078 28.620 1.00 31.14  ? 118 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 117 ? 19.394 -10.617 27.844 1.00 29.17  ? 118 VAL   A CG2 1 
ATOM   1012 N  N   A ASP   A 1 118 ? 15.672 -13.282 27.172 0.61 31.80  ? 119 ASP   A N   1 
ATOM   1013 N  N   B ASP   A 1 118 ? 15.638 -13.181 27.159 0.39 31.60  ? 119 ASP   A N   1 
ATOM   1014 C  CA  A ASP   A 1 118 ? 14.290 -13.746 27.051 0.61 32.93  ? 119 ASP   A CA  1 
ATOM   1015 C  CA  B ASP   A 1 118 ? 14.237 -13.593 27.016 0.39 32.88  ? 119 ASP   A CA  1 
ATOM   1016 C  C   A ASP   A 1 118 ? 13.977 -14.976 27.928 0.61 35.76  ? 119 ASP   A C   1 
ATOM   1017 C  C   B ASP   A 1 118 ? 13.866 -14.801 27.884 0.39 36.79  ? 119 ASP   A C   1 
ATOM   1018 O  O   A ASP   A 1 118 ? 12.997 -14.929 28.675 0.61 36.41  ? 119 ASP   A O   1 
ATOM   1019 O  O   B ASP   A 1 118 ? 12.851 -14.757 28.579 0.39 37.75  ? 119 ASP   A O   1 
ATOM   1020 C  CB  A ASP   A 1 118 ? 13.937 -14.014 25.576 0.61 34.94  ? 119 ASP   A CB  1 
ATOM   1021 C  CB  B ASP   A 1 118 ? 13.909 -13.888 25.536 0.39 34.80  ? 119 ASP   A CB  1 
ATOM   1022 C  CG  A ASP   A 1 118 ? 12.489 -14.409 25.351 0.61 49.10  ? 119 ASP   A CG  1 
ATOM   1023 C  CG  B ASP   A 1 118 ? 13.652 -12.674 24.660 0.39 47.15  ? 119 ASP   A CG  1 
ATOM   1024 O  OD1 A ASP   A 1 118 ? 11.595 -13.602 25.682 0.61 52.63  ? 119 ASP   A OD1 1 
ATOM   1025 O  OD1 B ASP   A 1 118 ? 13.218 -11.631 25.197 0.39 50.20  ? 119 ASP   A OD1 1 
ATOM   1026 O  OD2 A ASP   A 1 118 ? 12.253 -15.523 24.839 0.61 55.12  ? 119 ASP   A OD2 1 
ATOM   1027 O  OD2 B ASP   A 1 118 ? 13.859 -12.775 23.431 0.39 52.99  ? 119 ASP   A OD2 1 
ATOM   1028 N  N   A THR   A 1 119 ? 14.798 -16.059 27.858 0.61 30.62  ? 120 THR   A N   1 
ATOM   1029 N  N   B THR   A 1 119 ? 14.695 -15.865 27.856 0.39 31.92  ? 120 THR   A N   1 
ATOM   1030 C  CA  A THR   A 1 119 ? 14.523 -17.258 28.682 0.61 30.73  ? 120 THR   A CA  1 
ATOM   1031 C  CA  B THR   A 1 119 ? 14.444 -17.097 28.616 0.39 32.10  ? 120 THR   A CA  1 
ATOM   1032 C  C   A THR   A 1 119 ? 14.719 -16.975 30.175 0.61 33.90  ? 120 THR   A C   1 
ATOM   1033 C  C   B THR   A 1 119 ? 14.640 -16.870 30.124 0.39 34.94  ? 120 THR   A C   1 
ATOM   1034 O  O   A THR   A 1 119 ? 14.022 -17.570 30.998 0.61 33.83  ? 120 THR   A O   1 
ATOM   1035 O  O   B THR   A 1 119 ? 13.850 -17.393 30.912 0.39 35.31  ? 120 THR   A O   1 
ATOM   1036 C  CB  A THR   A 1 119 ? 15.278 -18.517 28.215 0.61 31.33  ? 120 THR   A CB  1 
ATOM   1037 C  CB  B THR   A 1 119 ? 15.247 -18.270 28.046 0.39 37.07  ? 120 THR   A CB  1 
ATOM   1038 O  OG1 A THR   A 1 119 ? 14.672 -19.655 28.844 0.61 31.20  ? 120 THR   A OG1 1 
ATOM   1039 O  OG1 B THR   A 1 119 ? 15.217 -18.196 26.620 0.39 35.39  ? 120 THR   A OG1 1 
ATOM   1040 C  CG2 A THR   A 1 119 ? 16.773 -18.487 28.544 0.61 25.68  ? 120 THR   A CG2 1 
ATOM   1041 C  CG2 B THR   A 1 119 ? 14.683 -19.613 28.471 0.39 36.91  ? 120 THR   A CG2 1 
ATOM   1042 N  N   . CYS   A 1 120 ? 15.664 -16.079 30.520 1.00 30.58  ? 121 CYS   A N   1 
ATOM   1043 C  CA  . CYS   A 1 120 ? 15.913 -15.709 31.932 1.00 31.17  ? 121 CYS   A CA  1 
ATOM   1044 C  C   . CYS   A 1 120 ? 14.693 -15.000 32.487 1.00 37.30  ? 121 CYS   A C   1 
ATOM   1045 O  O   . CYS   A 1 120 ? 14.234 -15.358 33.581 1.00 35.62  ? 121 CYS   A O   1 
ATOM   1046 C  CB  . CYS   A 1 120 ? 17.154 -14.831 32.053 1.00 30.54  ? 121 CYS   A CB  1 
ATOM   1047 S  SG  . CYS   A 1 120 ? 18.705 -15.734 31.872 1.00 32.92  ? 121 CYS   A SG  1 
ATOM   1048 N  N   A ARG   A 1 121 ? 14.147 -14.023 31.720 0.48 35.41  ? 122 ARG   A N   1 
ATOM   1049 N  N   B ARG   A 1 121 ? 14.152 -14.009 31.738 0.52 35.81  ? 122 ARG   A N   1 
ATOM   1050 C  CA  A ARG   A 1 121 ? 12.946 -13.253 32.072 0.48 36.90  ? 122 ARG   A CA  1 
ATOM   1051 C  CA  B ARG   A 1 121 ? 12.955 -13.261 32.136 0.52 37.46  ? 122 ARG   A CA  1 
ATOM   1052 C  C   A ARG   A 1 121 ? 11.760 -14.187 32.339 0.48 41.00  ? 122 ARG   A C   1 
ATOM   1053 C  C   B ARG   A 1 121 ? 11.753 -14.194 32.355 0.52 41.19  ? 122 ARG   A C   1 
ATOM   1054 O  O   A ARG   A 1 121 ? 11.041 -14.008 33.325 0.48 41.39  ? 122 ARG   A O   1 
ATOM   1055 O  O   B ARG   A 1 121 ? 11.021 -14.026 33.333 0.52 41.51  ? 122 ARG   A O   1 
ATOM   1056 C  CB  A ARG   A 1 121 ? 12.582 -12.265 30.949 0.48 37.91  ? 122 ARG   A CB  1 
ATOM   1057 C  CB  B ARG   A 1 121 ? 12.619 -12.173 31.108 0.52 39.45  ? 122 ARG   A CB  1 
ATOM   1058 C  CG  A ARG   A 1 121 ? 13.540 -11.093 30.819 0.48 49.91  ? 122 ARG   A CG  1 
ATOM   1059 C  CG  B ARG   A 1 121 ? 13.391 -10.875 31.326 0.52 53.93  ? 122 ARG   A CG  1 
ATOM   1060 C  CD  A ARG   A 1 121 ? 12.942 -9.945  30.025 0.48 62.86  ? 122 ARG   A CD  1 
ATOM   1061 C  CD  B ARG   A 1 121 ? 12.682 -9.685  30.697 0.52 65.91  ? 122 ARG   A CD  1 
ATOM   1062 N  NE  A ARG   A 1 121 ? 13.954 -8.943  29.684 0.48 67.61  ? 122 ARG   A NE  1 
ATOM   1063 N  NE  B ARG   A 1 121 ? 12.822 -9.666  29.238 0.52 70.67  ? 122 ARG   A NE  1 
ATOM   1064 C  CZ  A ARG   A 1 121 ? 14.296 -7.916  30.457 0.48 78.43  ? 122 ARG   A CZ  1 
ATOM   1065 C  CZ  B ARG   A 1 121 ? 13.606 -8.828  28.567 0.52 80.54  ? 122 ARG   A CZ  1 
ATOM   1066 N  NH1 A ARG   A 1 121 ? 13.701 -7.730  31.630 0.48 69.45  ? 122 ARG   A NH1 1 
ATOM   1067 N  NH1 B ARG   A 1 121 ? 14.326 -7.917  29.213 0.52 64.59  ? 122 ARG   A NH1 1 
ATOM   1068 N  NH2 A ARG   A 1 121 ? 15.234 -7.066  30.063 0.48 60.03  ? 122 ARG   A NH2 1 
ATOM   1069 N  NH2 B ARG   A 1 121 ? 13.672 -8.888  27.244 0.52 65.46  ? 122 ARG   A NH2 1 
ATOM   1070 N  N   . LYS   A 1 122 ? 11.582 -15.195 31.467 1.00 37.14  ? 123 LYS   A N   1 
ATOM   1071 C  CA  . LYS   A 1 122 ? 10.499 -16.188 31.558 1.00 38.58  ? 123 LYS   A CA  1 
ATOM   1072 C  C   . LYS   A 1 122 ? 10.661 -17.102 32.768 1.00 41.78  ? 123 LYS   A C   1 
ATOM   1073 O  O   . LYS   A 1 122 ? 9.682  -17.323 33.486 1.00 41.96  ? 123 LYS   A O   1 
ATOM   1074 C  CB  . LYS   A 1 122 ? 10.371 -16.992 30.256 1.00 40.57  ? 123 LYS   A CB  1 
ATOM   1075 C  CG  . LYS   A 1 122 ? 9.824  -16.145 29.112 1.00 58.88  ? 123 LYS   A CG  1 
ATOM   1076 C  CD  . LYS   A 1 122 ? 9.727  -16.899 27.802 1.00 70.56  ? 123 LYS   A CD  1 
ATOM   1077 C  CE  . LYS   A 1 122 ? 9.304  -15.966 26.693 1.00 84.39  ? 123 LYS   A CE  1 
ATOM   1078 N  NZ  . LYS   A 1 122 ? 8.455  -16.650 25.685 1.00 97.20  ? 123 LYS   A NZ  1 
ATOM   1079 N  N   . PHE   A 1 123 ? 11.897 -17.594 33.025 1.00 36.50  ? 124 PHE   A N   1 
ATOM   1080 C  CA  . PHE   A 1 123 ? 12.171 -18.455 34.185 1.00 36.96  ? 124 PHE   A CA  1 
ATOM   1081 C  C   . PHE   A 1 123 ? 11.976 -17.692 35.492 1.00 42.01  ? 124 PHE   A C   1 
ATOM   1082 O  O   . PHE   A 1 123 ? 11.434 -18.255 36.450 1.00 41.45  ? 124 PHE   A O   1 
ATOM   1083 C  CB  . PHE   A 1 123 ? 13.571 -19.066 34.106 1.00 36.98  ? 124 PHE   A CB  1 
ATOM   1084 C  CG  . PHE   A 1 123 ? 13.697 -20.345 33.297 1.00 38.51  ? 124 PHE   A CG  1 
ATOM   1085 C  CD1 . PHE   A 1 123 ? 13.150 -20.442 32.019 1.00 41.57  ? 124 PHE   A CD1 1 
ATOM   1086 C  CD2 . PHE   A 1 123 ? 14.423 -21.426 33.785 1.00 41.30  ? 124 PHE   A CD2 1 
ATOM   1087 C  CE1 . PHE   A 1 123 ? 13.283 -21.618 31.268 1.00 42.58  ? 124 PHE   A CE1 1 
ATOM   1088 C  CE2 . PHE   A 1 123 ? 14.566 -22.597 33.026 1.00 43.18  ? 124 PHE   A CE2 1 
ATOM   1089 C  CZ  . PHE   A 1 123 ? 13.996 -22.683 31.775 1.00 40.82  ? 124 PHE   A CZ  1 
ATOM   1090 N  N   . ILE   A 1 124 ? 12.366 -16.401 35.519 1.00 38.22  ? 125 ILE   A N   1 
ATOM   1091 C  CA  . ILE   A 1 124 ? 12.164 -15.549 36.707 1.00 39.57  ? 125 ILE   A CA  1 
ATOM   1092 C  C   . ILE   A 1 124 ? 10.665 -15.304 36.963 1.00 46.93  ? 125 ILE   A C   1 
ATOM   1093 O  O   . ILE   A 1 124 ? 10.212 -15.464 38.105 1.00 47.59  ? 125 ILE   A O   1 
ATOM   1094 C  CB  . ILE   A 1 124 ? 13.005 -14.246 36.623 1.00 41.73  ? 125 ILE   A CB  1 
ATOM   1095 C  CG1 . ILE   A 1 124 ? 14.502 -14.585 36.764 1.00 40.30  ? 125 ILE   A CG1 1 
ATOM   1096 C  CG2 . ILE   A 1 124 ? 12.573 -13.209 37.699 1.00 44.23  ? 125 ILE   A CG2 1 
ATOM   1097 C  CD1 . ILE   A 1 124 ? 15.452 -13.547 36.218 1.00 44.08  ? 125 ILE   A CD1 1 
ATOM   1098 N  N   . LYS   A 1 125 ? 9.896  -14.969 35.896 1.00 44.97  ? 126 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 125 ? 8.453  -14.718 35.974 1.00 47.65  ? 126 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 125 ? 7.691  -15.950 36.493 1.00 52.11  ? 126 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 125 ? 6.713  -15.797 37.221 1.00 52.11  ? 126 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 125 ? 7.895  -14.270 34.616 1.00 50.98  ? 126 LYS   A CB  1 
ATOM   1103 N  N   . ALA   A 1 126 ? 8.164  -17.161 36.150 1.00 47.11  ? 127 ALA   A N   1 
ATOM   1104 C  CA  . ALA   A 1 126 ? 7.540  -18.407 36.609 1.00 48.49  ? 127 ALA   A CA  1 
ATOM   1105 C  C   . ALA   A 1 126 ? 7.711  -18.642 38.123 1.00 54.72  ? 127 ALA   A C   1 
ATOM   1106 O  O   . ALA   A 1 126 ? 6.833  -19.231 38.739 1.00 55.11  ? 127 ALA   A O   1 
ATOM   1107 C  CB  . ALA   A 1 126 ? 8.101  -19.588 35.830 1.00 47.67  ? 127 ALA   A CB  1 
ATOM   1108 N  N   . SER   A 1 127 ? 8.837  -18.206 38.710 1.00 52.87  ? 128 SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 127 ? 9.139  -18.420 40.128 1.00 55.49  ? 128 SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 127 ? 8.543  -17.370 41.083 1.00 63.65  ? 128 SER   A C   1 
ATOM   1111 O  O   . SER   A 1 127 ? 8.531  -17.607 42.295 1.00 66.05  ? 128 SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 127 ? 10.645 -18.544 40.341 1.00 59.20  ? 128 SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 127 ? 11.070 -19.889 40.184 1.00 69.92  ? 128 SER   A OG  1 
ATOM   1114 N  N   . GLU   A 1 128 ? 8.027  -16.237 40.554 1.00 60.12  ? 129 GLU   A N   1 
ATOM   1115 C  CA  . GLU   A 1 128 ? 7.440  -15.169 41.379 1.00 80.04  ? 129 GLU   A CA  1 
ATOM   1116 C  C   . GLU   A 1 128 ? 6.008  -15.478 41.847 1.00 123.42 ? 129 GLU   A C   1 
ATOM   1117 O  O   . GLU   A 1 128 ? 5.617  -16.638 41.966 1.00 91.13  ? 129 GLU   A O   1 
ATOM   1118 C  CB  . GLU   A 1 128 ? 7.521  -13.800 40.673 1.00 80.61  ? 129 GLU   A CB  1 
ATOM   1119 C  CG  . GLU   A 1 128 ? 6.496  -13.580 39.569 1.00 90.52  ? 129 GLU   A CG  1 
ATOM   1120 C  CD  . GLU   A 1 128 ? 6.661  -12.341 38.707 1.00 110.93 ? 129 GLU   A CD  1 
ATOM   1121 O  OE1 . GLU   A 1 128 ? 7.797  -11.821 38.599 1.00 102.29 ? 129 GLU   A OE1 1 
ATOM   1122 O  OE2 . GLU   A 1 128 ? 5.646  -11.899 38.121 1.00 104.46 ? 129 GLU   A OE2 1 
HETATM 1123 C  C   . ACE   B 2 1   ? 21.190 -35.065 5.835  1.00 28.04  ? 0   ACE   D C   1 
HETATM 1124 O  O   . ACE   B 2 1   ? 21.279 -33.930 6.323  1.00 29.19  ? 0   ACE   D O   1 
HETATM 1125 C  CH3 . ACE   B 2 1   ? 21.379 -36.295 6.698  1.00 27.96  ? 0   ACE   D CH3 1 
ATOM   1126 N  N   A TRP   B 2 2   ? 20.919 -35.292 4.553  0.66 25.75  ? 1   TRP   D N   1 
ATOM   1127 N  N   B TRP   B 2 2   ? 20.941 -35.293 4.545  0.34 26.93  ? 1   TRP   D N   1 
ATOM   1128 C  CA  A TRP   B 2 2   ? 20.716 -34.231 3.571  0.66 24.83  ? 1   TRP   D CA  1 
ATOM   1129 C  CA  B TRP   B 2 2   ? 20.680 -34.215 3.593  0.34 26.58  ? 1   TRP   D CA  1 
ATOM   1130 C  C   A TRP   B 2 2   ? 19.210 -34.079 3.284  0.66 29.49  ? 1   TRP   D C   1 
ATOM   1131 C  C   B TRP   B 2 2   ? 19.173 -34.058 3.421  0.34 29.18  ? 1   TRP   D C   1 
ATOM   1132 O  O   A TRP   B 2 2   ? 18.493 -35.085 3.206  0.66 29.73  ? 1   TRP   D O   1 
ATOM   1133 O  O   B TRP   B 2 2   ? 18.426 -35.041 3.516  0.34 28.54  ? 1   TRP   D O   1 
ATOM   1134 C  CB  A TRP   B 2 2   ? 21.500 -34.558 2.280  0.66 24.00  ? 1   TRP   D CB  1 
ATOM   1135 C  CB  B TRP   B 2 2   ? 21.363 -34.454 2.220  0.34 26.10  ? 1   TRP   D CB  1 
ATOM   1136 C  CG  A TRP   B 2 2   ? 22.995 -34.552 2.472  0.66 24.30  ? 1   TRP   D CG  1 
ATOM   1137 C  CG  B TRP   B 2 2   ? 20.744 -35.532 1.378  0.34 27.47  ? 1   TRP   D CG  1 
ATOM   1138 C  CD1 A TRP   B 2 2   ? 23.777 -35.591 2.888  0.66 26.84  ? 1   TRP   D CD1 1 
ATOM   1139 C  CD1 B TRP   B 2 2   ? 21.112 -36.842 1.330  0.34 30.69  ? 1   TRP   D CD1 1 
ATOM   1140 C  CD2 A TRP   B 2 2   ? 23.883 -33.444 2.256  0.66 23.84  ? 1   TRP   D CD2 1 
ATOM   1141 C  CD2 B TRP   B 2 2   ? 19.659 -35.385 0.445  0.34 27.55  ? 1   TRP   D CD2 1 
ATOM   1142 N  NE1 A TRP   B 2 2   ? 25.093 -35.192 2.969  0.66 25.92  ? 1   TRP   D NE1 1 
ATOM   1143 N  NE1 B TRP   B 2 2   ? 20.302 -37.532 0.461  0.34 30.51  ? 1   TRP   D NE1 1 
ATOM   1144 C  CE2 A TRP   B 2 2   ? 25.187 -33.882 2.580  0.66 26.94  ? 1   TRP   D CE2 1 
ATOM   1145 C  CE2 B TRP   B 2 2   ? 19.401 -36.662 -0.099 0.34 31.70  ? 1   TRP   D CE2 1 
ATOM   1146 C  CE3 A TRP   B 2 2   ? 23.697 -32.104 1.871  0.66 24.56  ? 1   TRP   D CE3 1 
ATOM   1147 C  CE3 B TRP   B 2 2   ? 18.846 -34.306 0.054  0.34 28.49  ? 1   TRP   D CE3 1 
ATOM   1148 C  CZ2 A TRP   B 2 2   ? 26.309 -33.046 2.467  0.66 26.28  ? 1   TRP   D CZ2 1 
ATOM   1149 C  CZ2 B TRP   B 2 2   ? 18.383 -36.886 -1.034 0.34 30.99  ? 1   TRP   D CZ2 1 
ATOM   1150 C  CZ3 A TRP   B 2 2   ? 24.809 -31.287 1.738  0.66 25.35  ? 1   TRP   D CZ3 1 
ATOM   1151 C  CZ3 B TRP   B 2 2   ? 17.832 -34.531 -0.865 0.34 30.12  ? 1   TRP   D CZ3 1 
ATOM   1152 C  CH2 A TRP   B 2 2   ? 26.094 -31.754 2.043  0.66 25.79  ? 1   TRP   D CH2 1 
ATOM   1153 C  CH2 B TRP   B 2 2   ? 17.613 -35.807 -1.403 0.34 30.68  ? 1   TRP   D CH2 1 
ATOM   1154 N  N   . VAL   B 2 3   ? 18.727 -32.833 3.147  1.00 24.36  ? 2   VAL   D N   1 
ATOM   1155 C  CA  . VAL   B 2 3   ? 17.296 -32.540 2.907  1.00 24.41  ? 2   VAL   D CA  1 
ATOM   1156 C  C   . VAL   B 2 3   ? 17.148 -31.485 1.803  1.00 26.67  ? 2   VAL   D C   1 
ATOM   1157 O  O   . VAL   B 2 3   ? 18.129 -30.806 1.454  1.00 25.72  ? 2   VAL   D O   1 
ATOM   1158 C  CB  . VAL   B 2 3   ? 16.591 -32.040 4.209  1.00 28.05  ? 2   VAL   D CB  1 
ATOM   1159 C  CG1 . VAL   B 2 3   ? 16.613 -33.101 5.316  1.00 28.12  ? 2   VAL   D CG1 1 
ATOM   1160 C  CG2 . VAL   B 2 3   ? 17.184 -30.706 4.705  1.00 27.42  ? 2   VAL   D CG2 1 
ATOM   1161 N  N   . ILE   B 2 4   ? 15.912 -31.313 1.324  1.00 25.06  ? 3   ILE   D N   1 
ATOM   1162 C  CA  . ILE   B 2 4   ? 15.530 -30.233 0.436  1.00 24.78  ? 3   ILE   D CA  1 
ATOM   1163 C  C   . ILE   B 2 4   ? 15.158 -29.088 1.424  1.00 29.01  ? 3   ILE   D C   1 
ATOM   1164 O  O   . ILE   B 2 4   ? 14.141 -29.200 2.124  1.00 28.90  ? 3   ILE   D O   1 
ATOM   1165 C  CB  . ILE   B 2 4   ? 14.319 -30.612 -0.467 1.00 26.67  ? 3   ILE   D CB  1 
ATOM   1166 C  CG1 . ILE   B 2 4   ? 14.630 -31.868 -1.366 1.00 24.85  ? 3   ILE   D CG1 1 
ATOM   1167 C  CG2 . ILE   B 2 4   ? 13.873 -29.377 -1.307 1.00 28.92  ? 3   ILE   D CG2 1 
ATOM   1168 C  CD1 . ILE   B 2 4   ? 15.948 -31.730 -2.308 1.00 29.08  ? 3   ILE   D CD1 1 
ATOM   1169 N  N   . PRO   B 2 5   ? 15.954 -27.994 1.510  1.00 28.48  ? 4   PRO   D N   1 
ATOM   1170 C  CA  . PRO   B 2 5   ? 15.626 -26.925 2.475  1.00 29.00  ? 4   PRO   D CA  1 
ATOM   1171 C  C   . PRO   B 2 5   ? 14.381 -26.121 2.081  1.00 32.75  ? 4   PRO   D C   1 
ATOM   1172 O  O   . PRO   B 2 5   ? 14.070 -26.004 0.895  1.00 31.15  ? 4   PRO   D O   1 
ATOM   1173 C  CB  . PRO   B 2 5   ? 16.888 -26.053 2.483  1.00 31.02  ? 4   PRO   D CB  1 
ATOM   1174 C  CG  . PRO   B 2 5   ? 17.473 -26.247 1.099  1.00 34.92  ? 4   PRO   D CG  1 
ATOM   1175 C  CD  . PRO   B 2 5   ? 17.203 -27.692 0.771  1.00 30.73  ? 4   PRO   D CD  1 
ATOM   1176 N  N   . ALA   B 2 6   ? 13.645 -25.621 3.076  1.00 32.33  ? 5   ALA   D N   1 
HETATM 1177 C  C4  . A1ACA C 3 .   ? 25.472 -10.158 16.481 1.00 24.69  ? 201 A1ACA A C4  1 
HETATM 1178 C  C5  . A1ACA C 3 .   ? 24.879 -8.892  16.518 1.00 25.16  ? 201 A1ACA A C5  1 
HETATM 1179 C  C6  . A1ACA C 3 .   ? 23.860 -8.610  17.419 1.00 28.00  ? 201 A1ACA A C6  1 
HETATM 1180 C  C7  . A1ACA C 3 .   ? 23.418 -9.623  18.264 1.00 28.26  ? 201 A1ACA A C7  1 
HETATM 1181 C  C8  . A1ACA C 3 .   ? 22.241 -10.807 19.825 1.00 32.23  ? 201 A1ACA A C8  1 
HETATM 1182 C  C10 . A1ACA C 3 .   ? 23.955 -10.905 18.199 1.00 26.66  ? 201 A1ACA A C10 1 
HETATM 1183 C  C1  . A1ACA C 3 .   ? 27.235 -10.263 11.923 1.00 28.59  ? 201 A1ACA A C1  1 
HETATM 1184 C  C2  . A1ACA C 3 .   ? 27.383 -10.591 13.259 1.00 26.71  ? 201 A1ACA A C2  1 
HETATM 1185 C  C3  . A1ACA C 3 .   ? 26.351 -10.239 14.154 1.00 25.55  ? 201 A1ACA A C3  1 
HETATM 1186 C  C9  . A1ACA C 3 .   ? 23.233 -11.764 19.197 1.00 30.25  ? 201 A1ACA A C9  1 
HETATM 1187 O  O   . A1ACA C 3 .   ? 21.416 -11.068 20.698 1.00 31.93  ? 201 A1ACA A O   1 
HETATM 1188 N  N2  . A1ACA C 3 .   ? 22.416 -9.591  19.242 1.00 29.89  ? 201 A1ACA A N2  1 
HETATM 1189 C  C11 . A1ACA C 3 .   ? 24.983 -11.180 17.303 1.00 24.90  ? 201 A1ACA A C11 1 
HETATM 1190 N  N1  . A1ACA C 3 .   ? 26.369 -10.559 15.472 1.00 22.81  ? 201 A1ACA A N1  1 
HETATM 1191 N  N3  . A1ACA C 3 .   ? 25.257 -9.624  13.674 1.00 29.29  ? 201 A1ACA A N3  1 
HETATM 1192 C  C   . A1ACA C 3 .   ? 25.237 -9.379  12.377 1.00 30.75  ? 201 A1ACA A C   1 
HETATM 1193 CL CL  . A1ACA C 3 .   ? 23.790 -8.610  11.799 0.53 31.08  ? 201 A1ACA A CL  1 
HETATM 1194 BR BR  . A1ACA C 3 .   ? 28.932 -11.492 13.841 0.71 24.99  ? 201 A1ACA A BR  1 
HETATM 1195 N  N   . A1ACA C 3 .   ? 26.143 -9.644  11.453 1.00 30.03  ? 201 A1ACA A N   1 
HETATM 1196 CL CL  . CL    D 4 .   ? 21.320 -15.336 22.691 1.00 36.93  ? 202 CL    A CL  1 
HETATM 1197 S  S   A DMS   E 5 .   ? 17.511 -35.332 -1.280 0.66 42.87  ? 101 DMS   D S   1 
HETATM 1198 O  O   A DMS   E 5 .   ? 16.198 -35.094 -0.687 0.66 44.52  ? 101 DMS   D O   1 
HETATM 1199 C  C1  A DMS   E 5 .   ? 18.607 -34.410 -0.232 0.66 41.75  ? 101 DMS   D C1  1 
HETATM 1200 C  C2  A DMS   E 5 .   ? 17.918 -36.957 -0.753 0.66 42.19  ? 101 DMS   D C2  1 
HETATM 1201 O  O   . HOH   F 6 .   ? 35.610 -25.769 25.542 1.00 39.43  ? 301 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 6 .   ? 25.750 -3.510  26.500 1.00 34.05  ? 302 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 6 .   ? 22.718 -5.487  19.931 1.00 53.35  ? 303 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 6 .   ? 41.059 -21.671 25.216 1.00 42.38  ? 304 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 6 .   ? 37.821 2.356   19.834 1.00 37.33  ? 305 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 6 .   ? 38.428 -14.941 15.485 1.00 35.35  ? 306 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 6 .   ? 20.752 -5.888  26.227 1.00 39.86  ? 307 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 6 .   ? 26.824 -32.031 16.182 1.00 42.77  ? 308 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 6 .   ? 44.318 -0.910  17.917 1.00 50.56  ? 309 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 6 .   ? 37.168 -12.478 40.290 1.00 57.75  ? 310 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 6 .   ? 45.052 -11.295 18.859 1.00 65.86  ? 311 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 6 .   ? 16.421 -27.477 -3.236 1.00 48.41  ? 312 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 6 .   ? 37.646 -20.476 26.973 1.00 34.40  ? 313 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 6 .   ? 29.800 -32.191 9.533  1.00 48.28  ? 314 HOH   A O   1 
HETATM 1215 O  O   A HOH   F 6 .   ? 19.065 -22.913 4.381  0.67 45.54  ? 315 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 6 .   ? 15.408 -10.068 25.006 1.00 48.42  ? 316 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 6 .   ? 21.652 -29.499 -5.246 1.00 36.83  ? 317 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 6 .   ? 33.282 -20.823 29.593 1.00 44.66  ? 318 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 6 .   ? 20.416 -13.574 20.545 1.00 46.68  ? 319 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 6 .   ? 19.854 -9.693  37.089 1.00 37.84  ? 320 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 6 .   ? 28.290 -8.973  39.970 1.00 44.85  ? 321 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 6 .   ? 43.590 -6.649  32.025 1.00 48.93  ? 322 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 6 .   ? 22.642 -27.753 17.813 1.00 51.49  ? 323 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 6 .   ? 32.743 -24.530 32.169 1.00 57.43  ? 324 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 6 .   ? 21.468 -27.128 14.656 0.50 37.78  ? 325 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 6 .   ? 31.636 -0.937  15.921 1.00 42.12  ? 326 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 6 .   ? 25.630 -2.946  20.087 1.00 56.78  ? 327 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 6 .   ? 30.285 1.383   33.895 1.00 64.65  ? 328 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 6 .   ? 23.357 -5.868  32.929 1.00 36.93  ? 329 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 6 .   ? 27.199 -10.220 35.916 1.00 37.34  ? 330 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 6 .   ? 17.881 -29.415 7.686  1.00 33.05  ? 331 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 6 .   ? 28.795 -21.832 41.646 1.00 71.38  ? 332 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 6 .   ? 23.218 -17.065 44.290 1.00 60.00  ? 333 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 6 .   ? 27.308 -28.205 18.644 1.00 25.65  ? 334 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 6 .   ? 22.950 -28.247 12.661 1.00 22.83  ? 335 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 6 .   ? 21.553 -30.047 14.194 1.00 67.49  ? 336 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 6 .   ? 36.811 -5.772  12.303 1.00 36.74  ? 337 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 6 .   ? 34.413 -23.936 29.870 1.00 74.41  ? 338 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 6 .   ? 41.348 -12.793 14.088 1.00 99.81  ? 339 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 6 .   ? 21.893 -24.998 18.355 1.00 22.89  ? 340 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 6 .   ? 41.226 -16.908 15.218 1.00 38.47  ? 341 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 6 .   ? 26.910 -35.302 11.613 1.00 54.82  ? 342 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 6 .   ? 28.249 -23.767 31.718 1.00 39.42  ? 343 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 6 .   ? 12.229 -18.065 25.870 1.00 56.95  ? 344 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 6 .   ? 29.368 -27.437 20.649 1.00 23.55  ? 345 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 6 .   ? 23.956 -15.872 21.320 1.00 30.21  ? 346 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 6 .   ? 41.111 -1.491  11.694 1.00 64.68  ? 347 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 6 .   ? 30.348 -0.665  37.062 1.00 51.12  ? 348 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 6 .   ? 10.756 -11.528 34.517 1.00 49.17  ? 349 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 6 .   ? 26.106 -21.903 38.658 1.00 37.38  ? 350 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 6 .   ? 24.881 -26.854 19.057 1.00 33.58  ? 351 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 6 .   ? 29.008 -31.154 7.212  1.00 34.18  ? 352 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 6 .   ? 26.916 -16.679 38.717 1.00 52.12  ? 353 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 6 .   ? 20.847 -7.377  19.834 1.00 45.97  ? 354 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 6 .   ? 26.106 -22.668 29.936 1.00 27.02  ? 355 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 6 .   ? 45.906 -14.254 21.596 1.00 55.12  ? 356 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 6 .   ? 44.316 -12.746 41.350 1.00 52.05  ? 357 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 6 .   ? 46.790 -21.577 18.165 1.00 48.07  ? 358 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 6 .   ? 28.473 -24.297 34.396 1.00 52.23  ? 359 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 6 .   ? 30.653 -28.943 22.661 1.00 39.32  ? 360 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 6 .   ? 17.995 -34.538 8.333  1.00 33.79  ? 361 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 6 .   ? 37.272 -6.446  34.385 1.00 40.95  ? 362 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 6 .   ? 41.124 -7.055  35.974 1.00 43.83  ? 363 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 6 .   ? 42.398 -10.548 15.518 1.00 49.30  ? 364 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 6 .   ? 28.866 -0.454  16.940 1.00 74.02  ? 365 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 6 .   ? 26.356 -7.812  36.884 1.00 53.91  ? 366 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 6 .   ? 21.011 -23.416 6.229  1.00 50.28  ? 367 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 6 .   ? 27.068 -2.366  16.147 1.00 59.65  ? 368 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 6 .   ? 46.158 -15.852 27.623 1.00 68.29  ? 369 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 6 .   ? 20.223 -15.979 40.903 1.00 35.47  ? 370 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 6 .   ? 45.459 -10.869 30.298 1.00 55.38  ? 371 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 6 .   ? 47.124 -25.298 21.614 1.00 50.32  ? 372 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 6 .   ? 12.734 -20.593 42.405 1.00 53.04  ? 373 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 6 .   ? 14.315 -16.902 23.485 1.00 42.07  ? 374 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 6 .   ? 43.926 -4.388  25.810 1.00 45.98  ? 375 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 6 .   ? 34.742 -18.976 13.881 0.50 21.60  ? 376 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 6 .   ? 45.179 -12.613 23.613 1.00 48.01  ? 377 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 6 .   ? 17.920 -24.404 39.700 1.00 42.43  ? 378 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 6 .   ? 11.636 -15.324 40.557 1.00 74.38  ? 379 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 6 .   ? 27.589 -23.107 13.881 0.50 27.18  ? 380 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 6 .   ? 37.945 -16.678 13.163 0.50 26.89  ? 381 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 6 .   ? 38.965 -18.899 33.488 1.00 45.82  ? 382 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 6 .   ? 46.261 -18.934 19.677 1.00 50.67  ? 383 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 6 .   ? 25.999 -19.174 41.688 1.00 58.57  ? 384 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 6 .   ? 26.147 -8.095  9.050  1.00 43.16  ? 385 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 6 .   ? 34.119 -7.974  35.740 1.00 34.45  ? 386 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 6 .   ? 44.578 -16.420 29.761 1.00 52.52  ? 387 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 6 .   ? 43.844 -10.675 35.146 1.00 70.09  ? 388 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 6 .   ? 34.735 -29.152 26.032 1.00 64.77  ? 389 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 6 .   ? 31.865 -31.859 14.531 1.00 35.83  ? 390 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 6 .   ? 23.634 -15.684 17.810 1.00 43.54  ? 391 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 6 .   ? 19.848 -25.532 41.261 1.00 76.64  ? 392 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 6 .   ? 17.336 -24.546 -2.131 1.00 61.80  ? 393 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 6 .   ? 40.335 -19.603 29.032 1.00 35.11  ? 394 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 6 .   ? 42.095 -6.009  11.870 1.00 72.34  ? 395 HOH   A O   1 
HETATM 1296 O  O   A HOH   F 6 .   ? 12.119 -20.710 27.896 0.66 45.82  ? 396 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 6 .   ? 4.282  -20.385 37.880 1.00 61.09  ? 397 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 6 .   ? 16.775 -6.517  27.631 1.00 64.67  ? 398 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 6 .   ? 29.634 -22.699 36.830 1.00 63.81  ? 399 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 6 .   ? 26.453 -30.774 19.029 1.00 61.38  ? 400 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 6 .   ? 33.079 -29.814 21.502 1.00 40.15  ? 401 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 6 .   ? 46.047 -8.980  44.109 1.00 51.72  ? 402 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 6 .   ? 47.298 -6.661  20.312 1.00 66.37  ? 403 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 6 .   ? 30.350 -10.649 40.611 1.00 43.10  ? 404 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 6 .   ? 36.952 -2.249  11.560 1.00 58.44  ? 405 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 6 .   ? 25.586 -4.626  17.974 1.00 51.30  ? 406 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 6 .   ? 44.571 -8.789  17.939 1.00 69.99  ? 407 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 6 .   ? 41.197 -17.086 35.202 1.00 42.97  ? 408 HOH   A O   1 
HETATM 1309 O  O   . HOH   F 6 .   ? 10.426 -11.706 40.040 1.00 64.18  ? 409 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 6 .   ? 46.857 -20.201 21.979 1.00 64.95  ? 410 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 6 .   ? 45.804 -17.072 17.306 1.00 67.63  ? 411 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 6 .   ? 21.081 -23.254 42.111 1.00 44.91  ? 412 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 6 .   ? 35.086 -29.710 23.387 1.00 43.68  ? 413 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 6 .   ? 19.624 -27.332 10.109 1.00 49.49  ? 414 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 6 .   ? 35.200 1.879   13.530 1.00 53.15  ? 415 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 6 .   ? 22.971 -15.028 40.428 1.00 32.66  ? 416 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 6 .   ? 27.290 -25.498 28.357 1.00 56.79  ? 417 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 6 .   ? 32.149 -15.721 39.855 1.00 35.01  ? 418 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 6 .   ? 27.009 -1.645  22.045 1.00 51.11  ? 419 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 6 .   ? 32.364 -9.038  39.767 1.00 56.45  ? 420 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 6 .   ? 33.527 -33.016 12.085 1.00 46.89  ? 421 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 6 .   ? 33.969 -32.830 21.882 1.00 61.93  ? 422 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 6 .   ? 41.990 -8.031  13.749 1.00 58.21  ? 423 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 6 .   ? 33.500 -0.371  20.129 1.00 43.45  ? 424 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 6 .   ? 25.615 -16.104 41.099 1.00 49.49  ? 425 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 6 .   ? 29.511 -0.846  22.337 1.00 57.76  ? 426 HOH   A O   1 
HETATM 1327 O  O   . HOH   F 6 .   ? 34.491 -18.874 36.243 1.00 64.97  ? 427 HOH   A O   1 
HETATM 1328 O  O   . HOH   F 6 .   ? 39.856 -5.570  33.971 1.00 39.67  ? 428 HOH   A O   1 
HETATM 1329 O  O   . HOH   F 6 .   ? 45.741 -5.519  23.760 1.00 46.00  ? 429 HOH   A O   1 
HETATM 1330 O  O   . HOH   F 6 .   ? 42.764 -18.234 30.715 1.00 48.22  ? 430 HOH   A O   1 
HETATM 1331 O  O   . HOH   F 6 .   ? 26.372 -29.456 22.657 1.00 58.24  ? 431 HOH   A O   1 
HETATM 1332 O  O   . HOH   F 6 .   ? 23.403 -30.541 19.311 1.00 65.79  ? 432 HOH   A O   1 
HETATM 1333 O  O   . HOH   F 6 .   ? 31.752 -26.106 27.125 1.00 54.74  ? 433 HOH   A O   1 
HETATM 1334 O  O   . HOH   F 6 .   ? 22.234 -10.493 14.626 1.00 44.45  ? 434 HOH   A O   1 
HETATM 1335 O  O   . HOH   F 6 .   ? 31.921 -0.042  13.352 1.00 62.69  ? 435 HOH   A O   1 
HETATM 1336 O  O   . HOH   F 6 .   ? 37.060 -31.564 23.393 1.00 77.23  ? 436 HOH   A O   1 
HETATM 1337 O  O   . HOH   F 6 .   ? 44.354 -4.270  28.918 1.00 64.50  ? 437 HOH   A O   1 
HETATM 1338 O  O   . HOH   F 6 .   ? 26.927 -34.491 17.941 1.00 63.51  ? 438 HOH   A O   1 
HETATM 1339 O  O   . HOH   F 6 .   ? 23.058 -3.149  26.839 1.00 64.46  ? 439 HOH   A O   1 
HETATM 1340 O  O   . HOH   F 6 .   ? 28.750 -2.666  13.137 1.00 74.20  ? 440 HOH   A O   1 
HETATM 1341 O  O   . HOH   F 6 .   ? 19.461 -31.776 13.920 1.00 63.83  ? 441 HOH   A O   1 
HETATM 1342 O  O   . HOH   F 6 .   ? 47.883 -23.443 19.798 1.00 59.10  ? 442 HOH   A O   1 
HETATM 1343 O  O   . HOH   F 6 .   ? 36.750 -24.470 27.635 1.00 56.75  ? 443 HOH   A O   1 
HETATM 1344 O  O   . HOH   F 6 .   ? 19.749 -8.160  24.566 1.00 52.37  ? 444 HOH   A O   1 
HETATM 1345 O  O   . HOH   F 6 .   ? 30.651 -34.334 14.896 1.00 57.62  ? 445 HOH   A O   1 
HETATM 1346 O  O   . HOH   F 6 .   ? 35.367 -4.253  10.663 1.00 45.43  ? 446 HOH   A O   1 
HETATM 1347 O  O   . HOH   F 6 .   ? 24.451 -21.708 41.080 1.00 57.19  ? 447 HOH   A O   1 
HETATM 1348 O  O   . HOH   F 6 .   ? 46.642 -14.670 18.307 1.00 66.81  ? 448 HOH   A O   1 
HETATM 1349 O  O   . HOH   F 6 .   ? 47.387 -28.407 17.637 1.00 58.37  ? 449 HOH   A O   1 
HETATM 1350 O  O   . HOH   F 6 .   ? 35.828 -21.284 30.513 1.00 62.30  ? 450 HOH   A O   1 
HETATM 1351 O  O   . HOH   F 6 .   ? 47.138 -11.911 25.373 1.00 63.59  ? 451 HOH   A O   1 
HETATM 1352 O  O   . HOH   F 6 .   ? 34.074 -17.660 39.467 1.00 64.65  ? 452 HOH   A O   1 
HETATM 1353 O  O   . HOH   F 6 .   ? 32.172 -1.137  22.363 1.00 59.17  ? 453 HOH   A O   1 
HETATM 1354 O  O   . HOH   F 6 .   ? 11.912 -18.855 22.738 1.00 66.82  ? 454 HOH   A O   1 
HETATM 1355 O  O   . HOH   F 6 .   ? 19.445 -7.730  35.284 1.00 54.59  ? 455 HOH   A O   1 
HETATM 1356 O  O   . HOH   F 6 .   ? 46.992 -12.587 28.441 1.00 59.77  ? 456 HOH   A O   1 
HETATM 1357 O  O   . HOH   F 6 .   ? 43.935 -13.669 13.881 0.50 84.25  ? 457 HOH   A O   1 
HETATM 1358 O  O   . HOH   F 6 .   ? 45.547 -8.412  31.379 1.00 63.26  ? 458 HOH   A O   1 
HETATM 1359 O  O   . HOH   F 6 .   ? 25.335 -5.762  35.051 1.00 60.36  ? 459 HOH   A O   1 
HETATM 1360 O  O   . HOH   F 6 .   ? 17.106 -8.019  25.073 1.00 62.99  ? 460 HOH   A O   1 
HETATM 1361 O  O   . HOH   F 6 .   ? 17.065 -28.097 9.889  1.00 47.39  ? 461 HOH   A O   1 
HETATM 1362 O  O   . HOH   F 6 .   ? 19.905 -14.969 43.397 1.00 54.16  ? 462 HOH   A O   1 
HETATM 1363 O  O   . HOH   F 6 .   ? 43.124 -3.045  33.950 1.00 58.21  ? 463 HOH   A O   1 
HETATM 1364 O  O   . HOH   F 6 .   ? 19.107 -28.232 13.810 0.50 68.31  ? 464 HOH   A O   1 
HETATM 1365 O  O   . HOH   F 6 .   ? 32.551 -20.657 36.964 1.00 73.38  ? 465 HOH   A O   1 
HETATM 1366 O  O   . HOH   F 6 .   ? 28.268 -29.818 24.585 1.00 65.41  ? 466 HOH   A O   1 
HETATM 1367 O  O   . HOH   F 6 .   ? 33.805 -11.135 41.642 0.50 61.06  ? 467 HOH   A O   1 
HETATM 1368 O  O   . HOH   F 6 .   ? 33.805 -14.078 41.643 0.50 41.23  ? 468 HOH   A O   1 
HETATM 1369 O  O   . HOH   F 6 .   ? 12.536 -18.261 19.974 1.00 61.09  ? 469 HOH   A O   1 
HETATM 1370 O  O   . HOH   F 6 .   ? 16.729 -6.859  34.881 1.00 68.75  ? 470 HOH   A O   1 
HETATM 1371 O  O   . HOH   F 6 .   ? 21.271 -5.771  34.761 1.00 51.27  ? 471 HOH   A O   1 
HETATM 1372 O  O   . HOH   F 6 .   ? 32.169 -23.950 34.956 1.00 66.37  ? 472 HOH   A O   1 
HETATM 1373 O  O   . HOH   F 6 .   ? 45.127 -12.304 15.922 1.00 70.74  ? 473 HOH   A O   1 
HETATM 1374 O  O   . HOH   F 6 .   ? 39.408 -5.645  11.557 1.00 65.24  ? 474 HOH   A O   1 
HETATM 1375 O  O   . HOH   F 6 .   ? 16.664 -30.129 12.435 1.00 55.06  ? 475 HOH   A O   1 
HETATM 1376 O  O   . HOH   G 6 .   ? 12.204 -24.207 0.044  1.00 50.40  ? 201 HOH   D O   1 
HETATM 1377 O  O   . HOH   G 6 .   ? 14.921 -25.750 -1.776 1.00 43.83  ? 202 HOH   D O   1 
HETATM 1378 O  O   . HOH   G 6 .   ? 22.602 -34.001 8.834  1.00 34.14  ? 203 HOH   D O   1 
HETATM 1379 O  O   . HOH   G 6 .   ? 17.688 -36.234 6.048  1.00 40.90  ? 204 HOH   D O   1 
HETATM 1380 O  O   . HOH   G 6 .   ? 20.771 -38.257 4.017  1.00 46.99  ? 205 HOH   D O   1 
HETATM 1381 O  O   . HOH   G 6 .   ? 11.399 -23.556 3.152  1.00 54.16  ? 206 HOH   D O   1 
HETATM 1382 O  O   . HOH   G 6 .   ? 20.793 -39.471 -2.140 1.00 54.84  ? 207 HOH   D O   1 
HETATM 1383 O  O   . HOH   G 6 .   ? 10.645 -24.646 5.547  1.00 56.74  ? 208 HOH   D O   1 
HETATM 1384 O  O   . HOH   G 6 .   ? 20.136 -35.330 10.130 1.00 38.12  ? 209 HOH   D O   1 
HETATM 1385 O  O   . HOH   G 6 .   ? 23.643 -36.480 9.958  1.00 49.41  ? 210 HOH   D 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   . ASP A 5   ? 0.8139 0.9816 0.6851 0.0298  -0.1284 -0.0163 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8063 0.9689 0.6614 0.0140  -0.1197 -0.0188 6   ASP A CA  
3    C C   . ASP A 5   ? 0.7821 0.9741 0.6612 0.0032  -0.1155 -0.0344 6   ASP A C   
4    O O   . ASP A 5   ? 0.7745 0.9910 0.6816 0.0072  -0.1191 -0.0434 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8296 0.9650 0.6758 0.0054  -0.1033 -0.0126 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0239 1.1404 0.8381 -0.0050 -0.0982 -0.0084 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0220 1.1511 0.8353 -0.0158 -0.0954 -0.0170 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1354 1.2243 0.9256 -0.0033 -0.0959 0.0025  6   ASP A OD2 
9    N N   . SER A 6   ? 0.6742 0.8630 0.5419 -0.0110 -0.1071 -0.0386 7   SER A N   
10   C CA  . SER A 6   ? 0.6270 0.8372 0.5129 -0.0230 -0.1009 -0.0530 7   SER A CA  
11   C C   . SER A 6   ? 0.5725 0.7704 0.4698 -0.0330 -0.0829 -0.0553 7   SER A C   
12   O O   . SER A 6   ? 0.5580 0.7614 0.4598 -0.0448 -0.0748 -0.0647 7   SER A O   
13   C CB  . SER A 6   ? 0.7064 0.9221 0.5714 -0.0311 -0.1050 -0.0573 7   SER A CB  
14   O OG  . SER A 6   ? 0.8707 1.0607 0.7083 -0.0375 -0.0975 -0.0499 7   SER A OG  
15   N N   . CYS A 7   ? 0.4630 0.6440 0.3648 -0.0277 -0.0774 -0.0474 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4236 0.5923 0.3347 -0.0349 -0.0628 -0.0487 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4127 0.5966 0.3487 -0.0407 -0.0570 -0.0601 8   CYS A C   
18   O O   . CYS A 7   ? 0.4027 0.6067 0.3540 -0.0374 -0.0632 -0.0661 8   CYS A O   
19   C CB  . CYS A 7   ? 0.4406 0.5905 0.3510 -0.0275 -0.0600 -0.0384 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5271 0.6504 0.4060 -0.0259 -0.0599 -0.0259 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3093 0.4830 0.2492 -0.0493 -0.0451 -0.0637 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2672 0.4452 0.2260 -0.0548 -0.0374 -0.0719 9   ILE A CA  
23   C C   . ILE A 8   ? 0.2981 0.4583 0.2606 -0.0503 -0.0319 -0.0645 9   ILE A C   
24   O O   . ILE A 8   ? 0.2892 0.4343 0.2400 -0.0464 -0.0316 -0.0557 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3075 0.4850 0.2670 -0.0667 -0.0292 -0.0820 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3192 0.4775 0.2662 -0.0694 -0.0226 -0.0786 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.2951 0.4940 0.2535 -0.0719 -0.0350 -0.0913 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3816 0.5350 0.3307 -0.0791 -0.0136 -0.0882 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2318 0.3925 0.2088 -0.0521 -0.0266 -0.0684 10  GLN A N   
30   N N   B GLN A 9   ? 0.2418 0.4041 0.2193 -0.0516 -0.0274 -0.0684 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2292 0.3730 0.2080 -0.0483 -0.0217 -0.0617 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2351 0.3821 0.2158 -0.0477 -0.0227 -0.0623 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2681 0.4004 0.2512 -0.0556 -0.0121 -0.0664 10  GLN A C   
34   C C   B GLN A 9   ? 0.2838 0.4185 0.2680 -0.0551 -0.0128 -0.0666 10  GLN A C   
35   O O   A GLN A 9   ? 0.2732 0.4135 0.2637 -0.0627 -0.0087 -0.0754 10  GLN A O   
36   O O   B GLN A 9   ? 0.2834 0.4254 0.2747 -0.0625 -0.0090 -0.0757 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2463 0.3984 0.2353 -0.0406 -0.0261 -0.0594 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2435 0.4019 0.2361 -0.0410 -0.0270 -0.0619 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.3290 0.4666 0.3224 -0.0393 -0.0195 -0.0558 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.2383 0.3811 0.2299 -0.0345 -0.0249 -0.0533 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5618 0.7005 0.5595 -0.0297 -0.0237 -0.0503 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4229 0.5683 0.4285 -0.0360 -0.0196 -0.0577 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4728 0.6220 0.4703 -0.0221 -0.0325 -0.0483 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3294 0.4940 0.3488 -0.0369 -0.0210 -0.0659 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.4704 0.5965 0.4703 -0.0293 -0.0178 -0.0476 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.4072 0.5339 0.4092 -0.0367 -0.0132 -0.0532 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2410 0.3537 0.2184 -0.0540 -0.0079 -0.0607 11  PHE A N   
48   N N   B PHE A 10  ? 0.2530 0.3683 0.2315 -0.0531 -0.0089 -0.0604 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2331 0.3309 0.2114 -0.0587 -0.0005 -0.0636 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2503 0.3496 0.2288 -0.0576 -0.0014 -0.0627 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2686 0.3606 0.2513 -0.0563 0.0016  -0.0604 11  PHE A C   
52   C C   B PHE A 10  ? 0.2828 0.3769 0.2663 -0.0556 0.0008  -0.0601 11  PHE A C   
53   O O   A PHE A 10  ? 0.2630 0.3465 0.2428 -0.0502 0.0002  -0.0529 11  PHE A O   
54   O O   B PHE A 10  ? 0.2783 0.3661 0.2599 -0.0492 -0.0011 -0.0527 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2548 0.3367 0.2255 -0.0577 0.0017  -0.0611 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2763 0.3604 0.2468 -0.0558 0.0001  -0.0590 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2729 0.3379 0.2425 -0.0613 0.0076  -0.0646 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.3034 0.3913 0.2701 -0.0603 0.0009  -0.0647 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.2986 0.3629 0.2681 -0.0686 0.0116  -0.0729 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3472 0.4493 0.3099 -0.0608 -0.0037 -0.0653 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.2895 0.3374 0.2559 -0.0570 0.0086  -0.0595 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3491 0.4250 0.3149 -0.0636 0.0059  -0.0696 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3220 0.3656 0.2870 -0.0712 0.0169  -0.0752 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3645 0.4700 0.3223 -0.0661 -0.0021 -0.0714 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3197 0.3486 0.2815 -0.0590 0.0125  -0.0617 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3948 0.4743 0.3580 -0.0680 0.0076  -0.0762 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3040 0.3293 0.2644 -0.0657 0.0167  -0.0691 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3661 0.4609 0.3252 -0.0700 0.0041  -0.0773 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2358 0.3332 0.2254 -0.0622 0.0056  -0.0672 12  THR A N   
70   C CA  . THR A 11  ? 0.2424 0.3369 0.2369 -0.0625 0.0093  -0.0669 12  THR A CA  
71   C C   . THR A 11  ? 0.2796 0.3507 0.2649 -0.0595 0.0120  -0.0594 12  THR A C   
72   O O   . THR A 11  ? 0.2821 0.3527 0.2695 -0.0547 0.0111  -0.0549 12  THR A O   
73   C CB  . THR A 11  ? 0.3288 0.4276 0.3286 -0.0731 0.0166  -0.0772 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3256 0.4499 0.3357 -0.0754 0.0129  -0.0853 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3711 0.4685 0.3760 -0.0752 0.0220  -0.0787 12  THR A CG2 
76   N N   . ARG A 12  ? 0.2565 0.3090 0.2321 -0.0619 0.0147  -0.0588 13  ARG A N   
77   C CA  . ARG A 12  ? 0.2681 0.2989 0.2344 -0.0589 0.0158  -0.0528 13  ARG A CA  
78   C C   . ARG A 12  ? 0.2888 0.3177 0.2532 -0.0506 0.0104  -0.0460 13  ARG A C   
79   O O   . ARG A 12  ? 0.2820 0.2954 0.2399 -0.0477 0.0101  -0.0420 13  ARG A O   
80   C CB  . ARG A 12  ? 0.3464 0.3557 0.3021 -0.0635 0.0199  -0.0552 13  ARG A CB  
81   C CG  . ARG A 12  ? 0.4812 0.4838 0.4335 -0.0738 0.0279  -0.0615 13  ARG A CG  
82   C CD  . ARG A 12  ? 0.7595 0.7536 0.7074 -0.0764 0.0322  -0.0596 13  ARG A CD  
83   N NE  . ARG A 12  ? 0.9313 0.8993 0.8637 -0.0725 0.0311  -0.0526 13  ARG A NE  
84   C CZ  . ARG A 12  ? 1.0800 1.0392 1.0061 -0.0726 0.0329  -0.0490 13  ARG A CZ  
85   N NH1 . ARG A 12  ? 0.9500 0.8859 0.8607 -0.0688 0.0304  -0.0430 13  ARG A NH1 
86   N NH2 . ARG A 12  ? 0.8506 0.8251 0.7862 -0.0761 0.0369  -0.0520 13  ARG A NH2 
87   N N   . HIS A 13  ? 0.2308 0.2743 0.1995 -0.0476 0.0062  -0.0452 14  HIS A N   
88   C CA  . HIS A 13  ? 0.2445 0.2851 0.2102 -0.0423 0.0031  -0.0404 14  HIS A CA  
89   C C   . HIS A 13  ? 0.2769 0.3106 0.2411 -0.0380 0.0026  -0.0345 14  HIS A C   
90   O O   . HIS A 13  ? 0.2707 0.2944 0.2314 -0.0357 0.0021  -0.0327 14  HIS A O   
91   C CB  . HIS A 13  ? 0.2373 0.2917 0.2034 -0.0413 -0.0002 -0.0402 14  HIS A CB  
92   C CG  . HIS A 13  ? 0.2647 0.3150 0.2265 -0.0383 -0.0011 -0.0366 14  HIS A CG  
93   N ND1 . HIS A 13  ? 0.2728 0.3181 0.2338 -0.0394 0.0004  -0.0399 14  HIS A ND1 
94   C CD2 . HIS A 13  ? 0.2711 0.3215 0.2294 -0.0350 -0.0028 -0.0310 14  HIS A CD2 
95   C CE1 . HIS A 13  ? 0.2672 0.3120 0.2255 -0.0378 0.0003  -0.0373 14  HIS A CE1 
96   N NE2 . HIS A 13  ? 0.2585 0.3046 0.2137 -0.0356 -0.0012 -0.0315 14  HIS A NE2 
97   N N   . ALA A 14  ? 0.2379 0.2781 0.2059 -0.0366 0.0024  -0.0327 15  ALA A N   
98   C CA  . ALA A 14  ? 0.2435 0.2770 0.2101 -0.0329 0.0027  -0.0277 15  ALA A CA  
99   C C   . ALA A 14  ? 0.2701 0.2881 0.2312 -0.0348 0.0055  -0.0277 15  ALA A C   
100  O O   . ALA A 14  ? 0.2476 0.2574 0.2047 -0.0323 0.0046  -0.0245 15  ALA A O   
101  C CB  . ALA A 14  ? 0.2509 0.2940 0.2241 -0.0304 0.0024  -0.0274 15  ALA A CB  
102  N N   A SER A 15  ? 0.2615 0.2747 0.2209 -0.0398 0.0089  -0.0314 16  SER A N   
103  N N   B SER A 15  ? 0.2548 0.2679 0.2141 -0.0398 0.0089  -0.0314 16  SER A N   
104  N N   C SER A 15  ? 0.2494 0.2625 0.2088 -0.0398 0.0090  -0.0314 16  SER A N   
105  C CA  A SER A 15  ? 0.2683 0.2629 0.2176 -0.0422 0.0114  -0.0308 16  SER A CA  
106  C CA  B SER A 15  ? 0.2620 0.2565 0.2113 -0.0423 0.0114  -0.0308 16  SER A CA  
107  C CA  C SER A 15  ? 0.2538 0.2481 0.2029 -0.0420 0.0113  -0.0306 16  SER A CA  
108  C C   A SER A 15  ? 0.3223 0.3054 0.2651 -0.0389 0.0075  -0.0295 16  SER A C   
109  C C   B SER A 15  ? 0.3223 0.3053 0.2650 -0.0390 0.0075  -0.0295 16  SER A C   
110  C C   C SER A 15  ? 0.3190 0.3018 0.2616 -0.0389 0.0075  -0.0295 16  SER A C   
111  O O   A SER A 15  ? 0.2998 0.2707 0.2352 -0.0365 0.0056  -0.0267 16  SER A O   
112  O O   B SER A 15  ? 0.3073 0.2779 0.2425 -0.0366 0.0057  -0.0267 16  SER A O   
113  O O   C SER A 15  ? 0.3047 0.2749 0.2396 -0.0366 0.0057  -0.0267 16  SER A O   
114  C CB  A SER A 15  ? 0.3191 0.3087 0.2653 -0.0498 0.0171  -0.0356 16  SER A CB  
115  C CB  B SER A 15  ? 0.3070 0.2966 0.2531 -0.0499 0.0171  -0.0357 16  SER A CB  
116  C CB  C SER A 15  ? 0.2899 0.2788 0.2357 -0.0497 0.0172  -0.0352 16  SER A CB  
117  O OG  A SER A 15  ? 0.3760 0.3433 0.3075 -0.0526 0.0197  -0.0339 16  SER A OG  
118  O OG  B SER A 15  ? 0.3353 0.3380 0.2903 -0.0530 0.0210  -0.0389 16  SER A OG  
119  O OG  C SER A 15  ? 0.2913 0.2822 0.2380 -0.0529 0.0177  -0.0395 16  SER A OG  
120  N N   . ASP A 16  ? 0.2903 0.2787 0.2366 -0.0385 0.0059  -0.0324 17  ASP A N   
121  C CA  . ASP A 16  ? 0.2976 0.2785 0.2417 -0.0345 0.0022  -0.0334 17  ASP A CA  
122  C C   . ASP A 16  ? 0.2958 0.2830 0.2440 -0.0297 -0.0012 -0.0312 17  ASP A C   
123  O O   . ASP A 16  ? 0.2978 0.2769 0.2434 -0.0256 -0.0048 -0.0313 17  ASP A O   
124  C CB  . ASP A 16  ? 0.3190 0.3067 0.2676 -0.0362 0.0028  -0.0385 17  ASP A CB  
125  C CG  . ASP A 16  ? 0.4310 0.4087 0.3743 -0.0416 0.0067  -0.0421 17  ASP A CG  
126  O OD1 . ASP A 16  ? 0.4166 0.3794 0.3506 -0.0444 0.0092  -0.0405 17  ASP A OD1 
127  O OD2 . ASP A 16  ? 0.4643 0.4480 0.4112 -0.0442 0.0080  -0.0472 17  ASP A OD2 
128  N N   . VAL A 17  ? 0.2394 0.2399 0.1930 -0.0301 -0.0003 -0.0296 18  VAL A N   
129  C CA  . VAL A 17  ? 0.2296 0.2339 0.1852 -0.0275 -0.0017 -0.0280 18  VAL A CA  
130  C C   . VAL A 17  ? 0.2908 0.2854 0.2419 -0.0260 -0.0026 -0.0253 18  VAL A C   
131  O O   . VAL A 17  ? 0.2652 0.2575 0.2165 -0.0235 -0.0053 -0.0265 18  VAL A O   
132  C CB  . VAL A 17  ? 0.2512 0.2659 0.2086 -0.0285 -0.0003 -0.0256 18  VAL A CB  
133  C CG1 . VAL A 17  ? 0.2547 0.2684 0.2111 -0.0274 0.0003  -0.0233 18  VAL A CG1 
134  C CG2 . VAL A 17  ? 0.2474 0.2712 0.2064 -0.0304 -0.0001 -0.0287 18  VAL A CG2 
135  N N   . LEU A 18  ? 0.2572 0.2474 0.2047 -0.0278 -0.0001 -0.0228 19  LEU A N   
136  C CA  . LEU A 18  ? 0.2755 0.2563 0.2171 -0.0276 0.0001  -0.0205 19  LEU A CA  
137  C C   . LEU A 18  ? 0.2885 0.2553 0.2212 -0.0261 -0.0035 -0.0213 19  LEU A C   
138  O O   . LEU A 18  ? 0.2741 0.2367 0.2034 -0.0239 -0.0067 -0.0209 19  LEU A O   
139  C CB  . LEU A 18  ? 0.2841 0.2641 0.2248 -0.0306 0.0048  -0.0194 19  LEU A CB  
140  C CG  . LEU A 18  ? 0.3345 0.3067 0.2697 -0.0311 0.0066  -0.0177 19  LEU A CG  
141  C CD1 . LEU A 18  ? 0.3278 0.3058 0.2676 -0.0286 0.0062  -0.0162 19  LEU A CD1 
142  C CD2 . LEU A 18  ? 0.3821 0.3537 0.3173 -0.0348 0.0124  -0.0187 19  LEU A CD2 
143  N N   . LEU A 19  ? 0.2808 0.2399 0.2091 -0.0270 -0.0037 -0.0227 20  LEU A N   
144  C CA  . LEU A 19  ? 0.3017 0.2436 0.2189 -0.0242 -0.0082 -0.0228 20  LEU A CA  
145  C C   . LEU A 19  ? 0.3308 0.2788 0.2550 -0.0174 -0.0151 -0.0254 20  LEU A C   
146  O O   . LEU A 19  ? 0.3277 0.2673 0.2453 -0.0132 -0.0209 -0.0250 20  LEU A O   
147  C CB  . LEU A 19  ? 0.3332 0.2658 0.2457 -0.0265 -0.0061 -0.0246 20  LEU A CB  
148  C CG  . LEU A 19  ? 0.4509 0.3600 0.3484 -0.0229 -0.0108 -0.0240 20  LEU A CG  
149  C CD1 . LEU A 19  ? 0.4988 0.3881 0.3771 -0.0258 -0.0100 -0.0197 20  LEU A CD1 
150  C CD2 . LEU A 19  ? 0.5160 0.4155 0.4096 -0.0261 -0.0071 -0.0265 20  LEU A CD2 
151  N N   . ASN A 20  ? 0.2803 0.2443 0.2178 -0.0168 -0.0143 -0.0290 21  ASN A N   
152  C CA  . ASN A 20  ? 0.2621 0.2354 0.2092 -0.0118 -0.0190 -0.0338 21  ASN A CA  
153  C C   . ASN A 20  ? 0.2916 0.2721 0.2416 -0.0120 -0.0198 -0.0337 21  ASN A C   
154  O O   . ASN A 20  ? 0.2866 0.2693 0.2400 -0.0075 -0.0255 -0.0375 21  ASN A O   
155  C CB  . ASN A 20  ? 0.2767 0.2636 0.2349 -0.0132 -0.0161 -0.0385 21  ASN A CB  
156  C CG  . ASN A 20  ? 0.4041 0.3835 0.3613 -0.0110 -0.0172 -0.0417 21  ASN A CG  
157  O OD1 . ASN A 20  ? 0.3641 0.3275 0.3135 -0.0062 -0.0220 -0.0413 21  ASN A OD1 
158  N ND2 . ASN A 20  ? 0.3358 0.3244 0.2987 -0.0145 -0.0130 -0.0449 21  ASN A ND2 
159  N N   . LEU A 21  ? 0.2708 0.2549 0.2199 -0.0169 -0.0143 -0.0300 22  LEU A N   
160  C CA  . LEU A 21  ? 0.2669 0.2547 0.2169 -0.0181 -0.0138 -0.0300 22  LEU A CA  
161  C C   . LEU A 21  ? 0.2973 0.2733 0.2375 -0.0158 -0.0188 -0.0289 22  LEU A C   
162  O O   . LEU A 21  ? 0.2906 0.2710 0.2333 -0.0146 -0.0223 -0.0322 22  LEU A O   
163  C CB  . LEU A 21  ? 0.2666 0.2560 0.2154 -0.0224 -0.0072 -0.0258 22  LEU A CB  
164  C CG  . LEU A 21  ? 0.2791 0.2784 0.2337 -0.0244 -0.0035 -0.0261 22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.2974 0.2953 0.2490 -0.0261 0.0008  -0.0211 22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.3233 0.3317 0.2844 -0.0258 -0.0029 -0.0315 22  LEU A CD2 
167  N N   . ASN A 22  ? 0.2852 0.2463 0.2132 -0.0163 -0.0186 -0.0249 23  ASN A N   
168  C CA  . ASN A 22  ? 0.2992 0.2453 0.2127 -0.0150 -0.0232 -0.0231 23  ASN A CA  
169  C C   . ASN A 22  ? 0.3544 0.2972 0.2669 -0.0072 -0.0336 -0.0265 23  ASN A C   
170  O O   . ASN A 22  ? 0.3656 0.3052 0.2721 -0.0044 -0.0401 -0.0274 23  ASN A O   
171  C CB  . ASN A 22  ? 0.3262 0.2551 0.2247 -0.0190 -0.0191 -0.0188 23  ASN A CB  
172  C CG  . ASN A 22  ? 0.4243 0.3372 0.3047 -0.0203 -0.0213 -0.0165 23  ASN A CG  
173  O OD1 . ASN A 22  ? 0.3954 0.3133 0.2766 -0.0204 -0.0229 -0.0176 23  ASN A OD1 
174  N ND2 . ASN A 22  ? 0.4644 0.3567 0.3266 -0.0221 -0.0210 -0.0137 23  ASN A ND2 
175  N N   . ARG A 23  ? 0.3263 0.2711 0.2456 -0.0032 -0.0357 -0.0290 24  ARG A N   
176  C CA  . ARG A 23  ? 0.3357 0.2793 0.2578 0.0061  -0.0458 -0.0336 24  ARG A CA  
177  C C   . ARG A 23  ? 0.3658 0.3307 0.3045 0.0085  -0.0495 -0.0409 24  ARG A C   
178  O O   . ARG A 23  ? 0.3590 0.3237 0.2970 0.0155  -0.0596 -0.0443 24  ARG A O   
179  C CB  . ARG A 23  ? 0.3368 0.2802 0.2656 0.0089  -0.0449 -0.0363 24  ARG A CB  
180  C CG  . ARG A 23  ? 0.3890 0.3079 0.2995 0.0073  -0.0430 -0.0308 24  ARG A CG  
181  C CD  . ARG A 23  ? 0.4146 0.3353 0.3328 0.0073  -0.0394 -0.0342 24  ARG A CD  
182  N NE  . ARG A 23  ? 0.5319 0.4272 0.4318 0.0053  -0.0373 -0.0303 24  ARG A NE  
183  C CZ  . ARG A 23  ? 0.7159 0.6090 0.6176 0.0012  -0.0312 -0.0321 24  ARG A CZ  
184  N NH1 . ARG A 23  ? 0.5428 0.4579 0.4625 -0.0012 -0.0270 -0.0370 24  ARG A NH1 
185  N NH2 . ARG A 23  ? 0.6402 0.5081 0.5237 -0.0018 -0.0285 -0.0293 24  ARG A NH2 
186  N N   . LEU A 24  ? 0.3076 0.2902 0.2598 0.0022  -0.0414 -0.0435 25  LEU A N   
187  C CA  . LEU A 24  ? 0.2962 0.2982 0.2630 0.0014  -0.0421 -0.0513 25  LEU A CA  
188  C C   . LEU A 24  ? 0.3448 0.3433 0.3032 -0.0002 -0.0450 -0.0500 25  LEU A C   
189  O O   . LEU A 24  ? 0.3460 0.3547 0.3116 0.0034  -0.0522 -0.0571 25  LEU A O   
190  C CB  . LEU A 24  ? 0.2851 0.2997 0.2610 -0.0068 -0.0315 -0.0525 25  LEU A CB  
191  C CG  . LEU A 24  ? 0.3343 0.3557 0.3188 -0.0068 -0.0279 -0.0555 25  LEU A CG  
192  C CD1 . LEU A 24  ? 0.3305 0.3616 0.3191 -0.0153 -0.0181 -0.0561 25  LEU A CD1 
193  C CD2 . LEU A 24  ? 0.3367 0.3688 0.3352 0.0003  -0.0346 -0.0658 25  LEU A CD2 
194  N N   . ARG A 25  ? 0.3072 0.2926 0.2515 -0.0057 -0.0394 -0.0421 26  ARG A N   
195  C CA  . ARG A 25  ? 0.3187 0.2989 0.2531 -0.0081 -0.0410 -0.0411 26  ARG A CA  
196  C C   . ARG A 25  ? 0.3926 0.3632 0.3160 -0.0004 -0.0539 -0.0419 26  ARG A C   
197  O O   . ARG A 25  ? 0.3928 0.3714 0.3183 0.0007  -0.0599 -0.0473 26  ARG A O   
198  C CB  . ARG A 25  ? 0.3345 0.3011 0.2558 -0.0143 -0.0327 -0.0335 26  ARG A CB  
199  C CG  . ARG A 25  ? 0.3767 0.3391 0.2887 -0.0177 -0.0333 -0.0340 26  ARG A CG  
200  C CD  . ARG A 25  ? 0.4493 0.4011 0.3518 -0.0240 -0.0240 -0.0287 26  ARG A CD  
201  N NE  . ARG A 25  ? 0.4095 0.3452 0.2984 -0.0239 -0.0233 -0.0234 26  ARG A NE  
202  C CZ  . ARG A 25  ? 0.5531 0.4730 0.4240 -0.0274 -0.0218 -0.0207 26  ARG A CZ  
203  N NH1 . ARG A 25  ? 0.4896 0.4077 0.3533 -0.0303 -0.0224 -0.0227 26  ARG A NH1 
204  N NH2 . ARG A 25  ? 0.4497 0.3549 0.3084 -0.0291 -0.0191 -0.0169 26  ARG A NH2 
205  N N   A SER A 26  ? 0.3742 0.3268 0.2847 0.0045  -0.0581 -0.0370 27  SER A N   
206  N N   B SER A 26  ? 0.3724 0.3252 0.2831 0.0045  -0.0580 -0.0370 27  SER A N   
207  N N   C SER A 26  ? 0.3767 0.3293 0.2872 0.0045  -0.0580 -0.0370 27  SER A N   
208  C CA  A SER A 26  ? 0.4002 0.3370 0.2945 0.0127  -0.0708 -0.0358 27  SER A CA  
209  C CA  B SER A 26  ? 0.3981 0.3346 0.2927 0.0129  -0.0707 -0.0357 27  SER A CA  
210  C CA  C SER A 26  ? 0.4043 0.3410 0.2986 0.0127  -0.0708 -0.0358 27  SER A CA  
211  C C   A SER A 26  ? 0.4624 0.4154 0.3720 0.0229  -0.0833 -0.0450 27  SER A C   
212  C C   B SER A 26  ? 0.4596 0.4124 0.3692 0.0229  -0.0831 -0.0449 27  SER A C   
213  C C   C SER A 26  ? 0.4632 0.4162 0.3728 0.0229  -0.0833 -0.0450 27  SER A C   
214  O O   A SER A 26  ? 0.4850 0.4333 0.3849 0.0291  -0.0952 -0.0464 27  SER A O   
215  O O   B SER A 26  ? 0.4801 0.4280 0.3796 0.0288  -0.0949 -0.0461 27  SER A O   
216  O O   C SER A 26  ? 0.4846 0.4328 0.3844 0.0290  -0.0952 -0.0463 27  SER A O   
217  C CB  A SER A 26  ? 0.4538 0.3661 0.3315 0.0151  -0.0708 -0.0292 27  SER A CB  
218  C CB  B SER A 26  ? 0.4507 0.3657 0.3324 0.0160  -0.0708 -0.0301 27  SER A CB  
219  C CB  C SER A 26  ? 0.4646 0.3776 0.3433 0.0153  -0.0707 -0.0294 27  SER A CB  
220  O OG  A SER A 26  ? 0.5167 0.4355 0.4088 0.0208  -0.0720 -0.0327 27  SER A OG  
221  O OG  B SER A 26  ? 0.5389 0.4360 0.4027 0.0073  -0.0614 -0.0227 27  SER A OG  
222  O OG  C SER A 26  ? 0.5956 0.4878 0.4542 0.0237  -0.0832 -0.0270 27  SER A OG  
223  N N   . ARG A 27  ? 0.3973 0.3705 0.3310 0.0245  -0.0807 -0.0521 28  ARG A N   
224  C CA  . ARG A 27  ? 0.4071 0.4006 0.3609 0.0336  -0.0907 -0.0636 28  ARG A CA  
225  C C   . ARG A 27  ? 0.4199 0.4407 0.3928 0.0269  -0.0867 -0.0732 28  ARG A C   
226  O O   . ARG A 27  ? 0.4222 0.4652 0.4159 0.0321  -0.0927 -0.0853 28  ARG A O   
227  C CB  . ARG A 27  ? 0.4237 0.4216 0.3914 0.0386  -0.0892 -0.0673 28  ARG A CB  
228  C CG  . ARG A 27  ? 0.5257 0.4945 0.4738 0.0446  -0.0927 -0.0588 28  ARG A CG  
229  C CD  . ARG A 27  ? 0.5851 0.5577 0.5462 0.0467  -0.0881 -0.0624 28  ARG A CD  
230  N NE  . ARG A 27  ? 0.7034 0.6964 0.6881 0.0568  -0.0962 -0.0751 28  ARG A NE  
231  C CZ  . ARG A 27  ? 0.8713 0.8813 0.8769 0.0559  -0.0900 -0.0834 28  ARG A CZ  
232  N NH1 . ARG A 27  ? 0.7245 0.7546 0.7531 0.0650  -0.0970 -0.0967 28  ARG A NH1 
233  N NH2 . ARG A 27  ? 0.6602 0.6686 0.6643 0.0456  -0.0768 -0.0796 28  ARG A NH2 
234  N N   . ASP A 28  ? 0.3527 0.3714 0.3186 0.0153  -0.0761 -0.0688 29  ASP A N   
235  C CA  . ASP A 28  ? 0.3478 0.3860 0.3265 0.0065  -0.0695 -0.0763 29  ASP A CA  
236  C C   . ASP A 28  ? 0.3897 0.4496 0.3919 0.0028  -0.0618 -0.0855 29  ASP A C   
237  O O   . ASP A 28  ? 0.3986 0.4802 0.4175 -0.0004 -0.0613 -0.0974 29  ASP A O   
238  C CB  . ASP A 28  ? 0.3817 0.4295 0.3614 0.0100  -0.0810 -0.0840 29  ASP A CB  
239  C CG  . ASP A 28  ? 0.5022 0.5630 0.4879 -0.0016 -0.0728 -0.0899 29  ASP A CG  
240  O OD1 . ASP A 28  ? 0.5035 0.5536 0.4802 -0.0112 -0.0601 -0.0829 29  ASP A OD1 
241  O OD2 . ASP A 28  ? 0.5493 0.6311 0.5491 -0.0009 -0.0790 -0.1024 29  ASP A OD2 
242  N N   . ILE A 29  ? 0.3159 0.3700 0.3184 0.0023  -0.0554 -0.0808 30  ILE A N   
243  C CA  . ILE A 29  ? 0.3044 0.3755 0.3247 -0.0018 -0.0475 -0.0886 30  ILE A CA  
244  C C   . ILE A 29  ? 0.3320 0.4014 0.3479 -0.0144 -0.0331 -0.0845 30  ILE A C   
245  O O   . ILE A 29  ? 0.2931 0.3457 0.2943 -0.0169 -0.0282 -0.0732 30  ILE A O   
246  C CB  . ILE A 29  ? 0.3395 0.4063 0.3627 0.0049  -0.0493 -0.0875 30  ILE A CB  
247  C CG1 . ILE A 29  ? 0.3603 0.4282 0.3894 0.0191  -0.0642 -0.0931 30  ILE A CG1 
248  C CG2 . ILE A 29  ? 0.3158 0.3978 0.3534 -0.0019 -0.0386 -0.0945 30  ILE A CG2 
249  C CD1 . ILE A 29  ? 0.4111 0.4648 0.4355 0.0263  -0.0664 -0.0889 30  ILE A CD1 
250  N N   . LEU A 30  ? 0.3070 0.3935 0.3356 -0.0224 -0.0263 -0.0946 31  LEU A N   
251  C CA  . LEU A 30  ? 0.3148 0.3980 0.3380 -0.0345 -0.0125 -0.0921 31  LEU A CA  
252  C C   . LEU A 30  ? 0.3335 0.3996 0.3398 -0.0386 -0.0090 -0.0822 31  LEU A C   
253  O O   . LEU A 30  ? 0.3070 0.3643 0.3052 -0.0459 0.0012  -0.0770 31  LEU A O   
254  C CB  . LEU A 30  ? 0.3221 0.4013 0.3427 -0.0369 -0.0052 -0.0878 31  LEU A CB  
255  C CG  . LEU A 30  ? 0.4011 0.4992 0.4391 -0.0382 -0.0027 -0.1005 31  LEU A CG  
256  C CD1 . LEU A 30  ? 0.4139 0.5058 0.4446 -0.0431 0.0058  -0.0957 31  LEU A CD1 
257  C CD2 . LEU A 30  ? 0.4837 0.5994 0.5342 -0.0473 0.0035  -0.1140 31  LEU A CD2 
258  N N   . THR A 31  ? 0.3020 0.3639 0.3033 -0.0342 -0.0172 -0.0811 32  THR A N   
259  C CA  . THR A 31  ? 0.2948 0.3431 0.2824 -0.0389 -0.0133 -0.0749 32  THR A CA  
260  C C   . THR A 31  ? 0.3608 0.4185 0.3546 -0.0496 -0.0047 -0.0838 32  THR A C   
261  O O   . THR A 31  ? 0.3482 0.4256 0.3574 -0.0514 -0.0064 -0.0965 32  THR A O   
262  C CB  . THR A 31  ? 0.3564 0.3987 0.3357 -0.0328 -0.0240 -0.0732 32  THR A CB  
263  O OG1 . THR A 31  ? 0.3788 0.4389 0.3706 -0.0292 -0.0334 -0.0849 32  THR A OG1 
264  C CG2 . THR A 31  ? 0.3480 0.3753 0.3164 -0.0246 -0.0299 -0.0636 32  THR A CG2 
265  N N   . ASP A 32  ? 0.3288 0.3726 0.3117 -0.0567 0.0056  -0.0779 33  ASP A N   
266  C CA  . ASP A 32  ? 0.3283 0.3754 0.3134 -0.0684 0.0162  -0.0852 33  ASP A CA  
267  C C   . ASP A 32  ? 0.3589 0.3934 0.3334 -0.0738 0.0209  -0.0835 33  ASP A C   
268  O O   . ASP A 32  ? 0.3572 0.3881 0.3295 -0.0841 0.0316  -0.0878 33  ASP A O   
269  C CB  . ASP A 32  ? 0.3479 0.3878 0.3287 -0.0735 0.0268  -0.0814 33  ASP A CB  
270  C CG  . ASP A 32  ? 0.4746 0.4946 0.4413 -0.0687 0.0282  -0.0667 33  ASP A CG  
271  O OD1 . ASP A 32  ? 0.4171 0.4281 0.3776 -0.0630 0.0235  -0.0600 33  ASP A OD1 
272  O OD2 . ASP A 32  ? 0.5948 0.6091 0.5564 -0.0710 0.0341  -0.0627 33  ASP A OD2 
273  N N   . VAL A 33  ? 0.2986 0.3250 0.2653 -0.0678 0.0141  -0.0778 34  VAL A N   
274  C CA  . VAL A 33  ? 0.3020 0.3171 0.2589 -0.0730 0.0186  -0.0774 34  VAL A CA  
275  C C   . VAL A 33  ? 0.3534 0.3681 0.3048 -0.0673 0.0080  -0.0767 34  VAL A C   
276  O O   . VAL A 33  ? 0.3454 0.3590 0.2948 -0.0585 -0.0008 -0.0713 34  VAL A O   
277  C CB  . VAL A 33  ? 0.3460 0.3388 0.2907 -0.0742 0.0286  -0.0667 34  VAL A CB  
278  C CG1 . VAL A 33  ? 0.3235 0.3071 0.2621 -0.0648 0.0237  -0.0559 34  VAL A CG1 
279  C CG2 . VAL A 33  ? 0.3616 0.3422 0.2981 -0.0817 0.0369  -0.0688 34  VAL A CG2 
280  N N   A VAL A 34  ? 0.3237 0.3371 0.2704 -0.0733 0.0095  -0.0822 35  VAL A N   
281  N N   B VAL A 34  ? 0.3143 0.3277 0.2609 -0.0732 0.0093  -0.0822 35  VAL A N   
282  C CA  A VAL A 34  ? 0.3294 0.3384 0.2656 -0.0704 0.0013  -0.0815 35  VAL A CA  
283  C CA  B VAL A 34  ? 0.3153 0.3240 0.2512 -0.0698 0.0009  -0.0810 35  VAL A CA  
284  C C   A VAL A 34  ? 0.3730 0.3621 0.2963 -0.0751 0.0118  -0.0758 35  VAL A C   
285  C C   B VAL A 34  ? 0.3716 0.3615 0.2945 -0.0752 0.0108  -0.0766 35  VAL A C   
286  O O   A VAL A 34  ? 0.3745 0.3591 0.2986 -0.0832 0.0227  -0.0792 35  VAL A O   
287  O O   B VAL A 34  ? 0.3794 0.3664 0.3031 -0.0839 0.0209  -0.0813 35  VAL A O   
288  C CB  A VAL A 34  ? 0.3897 0.4159 0.3312 -0.0737 -0.0063 -0.0945 35  VAL A CB  
289  C CB  B VAL A 34  ? 0.3657 0.3922 0.3067 -0.0694 -0.0108 -0.0923 35  VAL A CB  
290  C CG1 A VAL A 34  ? 0.4022 0.4207 0.3277 -0.0712 -0.0150 -0.0929 35  VAL A CG1 
291  C CG1 B VAL A 34  ? 0.3661 0.4028 0.3137 -0.0810 -0.0039 -0.1046 35  VAL A CG1 
292  C CG2 A VAL A 34  ? 0.3832 0.4319 0.3416 -0.0681 -0.0164 -0.1023 35  VAL A CG2 
293  C CG2 B VAL A 34  ? 0.3744 0.3914 0.2988 -0.0643 -0.0211 -0.0883 35  VAL A CG2 
294  N N   . ILE A 35  ? 0.3214 0.2975 0.2327 -0.0704 0.0093  -0.0680 36  ILE A N   
295  C CA  . ILE A 35  ? 0.3381 0.2974 0.2386 -0.0741 0.0184  -0.0644 36  ILE A CA  
296  C C   . ILE A 35  ? 0.4075 0.3653 0.2960 -0.0772 0.0131  -0.0692 36  ILE A C   
297  O O   . ILE A 35  ? 0.4015 0.3594 0.2818 -0.0722 0.0025  -0.0669 36  ILE A O   
298  C CB  . ILE A 35  ? 0.3613 0.3088 0.2578 -0.0682 0.0211  -0.0541 36  ILE A CB  
299  C CG1 . ILE A 35  ? 0.3500 0.3008 0.2572 -0.0640 0.0234  -0.0493 36  ILE A CG1 
300  C CG2 . ILE A 35  ? 0.3913 0.3240 0.2802 -0.0717 0.0311  -0.0528 36  ILE A CG2 
301  C CD1 . ILE A 35  ? 0.3389 0.2869 0.2511 -0.0689 0.0333  -0.0511 36  ILE A CD1 
302  N N   . VAL A 36  ? 0.3668 0.3216 0.2523 -0.0858 0.0204  -0.0758 37  VAL A N   
303  C CA  . VAL A 36  ? 0.3723 0.3262 0.2451 -0.0905 0.0161  -0.0817 37  VAL A CA  
304  C C   . VAL A 36  ? 0.4514 0.3864 0.3106 -0.0932 0.0251  -0.0777 37  VAL A C   
305  O O   . VAL A 36  ? 0.4320 0.3576 0.2945 -0.0969 0.0379  -0.0777 37  VAL A O   
306  C CB  . VAL A 36  ? 0.4261 0.3922 0.3050 -0.0995 0.0176  -0.0944 37  VAL A CB  
307  C CG1 . VAL A 36  ? 0.4423 0.4079 0.3064 -0.1046 0.0123  -0.1009 37  VAL A CG1 
308  C CG2 . VAL A 36  ? 0.4233 0.4115 0.3183 -0.0968 0.0088  -0.1004 37  VAL A CG2 
309  N N   . VAL A 37  ? 0.4213 0.3495 0.2644 -0.0916 0.0186  -0.0749 38  VAL A N   
310  C CA  . VAL A 37  ? 0.4294 0.3409 0.2585 -0.0951 0.0271  -0.0726 38  VAL A CA  
311  C C   . VAL A 37  ? 0.5306 0.4396 0.3404 -0.1010 0.0211  -0.0783 38  VAL A C   
312  O O   . VAL A 37  ? 0.4983 0.4047 0.2934 -0.0975 0.0096  -0.0752 38  VAL A O   
313  C CB  . VAL A 37  ? 0.4719 0.3755 0.2977 -0.0888 0.0268  -0.0632 38  VAL A CB  
314  C CG1 . VAL A 37  ? 0.4812 0.3707 0.2989 -0.0933 0.0392  -0.0629 38  VAL A CG1 
315  C CG2 . VAL A 37  ? 0.4460 0.3568 0.2907 -0.0816 0.0276  -0.0580 38  VAL A CG2 
316  N N   A SER A 38  ? 0.5402 0.4498 0.3490 -0.1099 0.0278  -0.0872 39  SER A N   
317  N N   B SER A 38  ? 0.5279 0.4357 0.3359 -0.1100 0.0290  -0.0868 39  SER A N   
318  C CA  A SER A 38  ? 0.5659 0.4754 0.3571 -0.1170 0.0224  -0.0949 39  SER A CA  
319  C CA  B SER A 38  ? 0.5490 0.4557 0.3391 -0.1177 0.0248  -0.0945 39  SER A CA  
320  C C   A SER A 38  ? 0.5807 0.5072 0.3727 -0.1123 0.0038  -0.0980 39  SER A C   
321  C C   B SER A 38  ? 0.5790 0.4973 0.3621 -0.1127 0.0052  -0.0954 39  SER A C   
322  O O   A SER A 38  ? 0.5616 0.5050 0.3732 -0.1115 0.0018  -0.1032 39  SER A O   
323  O O   B SER A 38  ? 0.5838 0.4926 0.3450 -0.1106 -0.0037 -0.0913 39  SER A O   
324  C CB  A SER A 38  ? 0.6544 0.5459 0.4208 -0.1200 0.0248  -0.0914 39  SER A CB  
325  C CB  B SER A 38  ? 0.6188 0.5069 0.3888 -0.1232 0.0333  -0.0933 39  SER A CB  
326  O OG  A SER A 38  ? 0.8445 0.7238 0.6143 -0.1233 0.0418  -0.0904 39  SER A OG  
327  O OG  B SER A 38  ? 0.7193 0.6003 0.4978 -0.1287 0.0505  -0.0971 39  SER A OG  
328  N N   A ARG A 39  ? 0.5370 0.4582 0.3077 -0.1089 -0.0096 -0.0951 40  ARG A N   
329  N N   B ARG A 39  ? 0.5025 0.4406 0.3051 -0.1101 -0.0009 -0.1006 40  ARG A N   
330  C CA  A ARG A 39  ? 0.5316 0.4670 0.3009 -0.1020 -0.0295 -0.0980 40  ARG A CA  
331  C CA  B ARG A 39  ? 0.4993 0.4553 0.3056 -0.1039 -0.0193 -0.1046 40  ARG A CA  
332  C C   A ARG A 39  ? 0.5514 0.4911 0.3317 -0.0893 -0.0386 -0.0902 40  ARG A C   
333  C C   B ARG A 39  ? 0.5249 0.4799 0.3326 -0.0910 -0.0300 -0.0948 40  ARG A C   
334  O O   A ARG A 39  ? 0.5400 0.4936 0.3248 -0.0815 -0.0550 -0.0934 40  ARG A O   
335  O O   B ARG A 39  ? 0.5152 0.4883 0.3367 -0.0842 -0.0420 -0.0986 40  ARG A O   
336  C CB  A ARG A 39  ? 0.5494 0.4731 0.2863 -0.1034 -0.0409 -0.0981 40  ARG A CB  
337  C CB  B ARG A 39  ? 0.5233 0.4818 0.3102 -0.1077 -0.0308 -0.1120 40  ARG A CB  
338  C CG  A ARG A 39  ? 0.6386 0.5666 0.3666 -0.1151 -0.0383 -0.1097 40  ARG A CG  
339  C CG  B ARG A 39  ? 0.6497 0.6172 0.4417 -0.1205 -0.0223 -0.1253 40  ARG A CG  
340  C CD  A ARG A 39  ? 0.6379 0.5573 0.3332 -0.1145 -0.0542 -0.1100 40  ARG A CD  
341  C CD  B ARG A 39  ? 0.7375 0.7169 0.5171 -0.1231 -0.0374 -0.1355 40  ARG A CD  
342  N NE  A ARG A 39  ? 0.6791 0.5996 0.3617 -0.1272 -0.0502 -0.1208 40  ARG A NE  
343  N NE  B ARG A 39  ? 0.8226 0.8099 0.6066 -0.1371 -0.0277 -0.1492 40  ARG A NE  
344  C CZ  A ARG A 39  ? 0.8556 0.7984 0.5463 -0.1301 -0.0595 -0.1337 40  ARG A CZ  
345  C CZ  B ARG A 39  ? 0.9728 0.9443 0.7378 -0.1478 -0.0175 -0.1518 40  ARG A CZ  
346  N NH1 A ARG A 39  ? 0.7259 0.6676 0.4029 -0.1428 -0.0546 -0.1436 40  ARG A NH1 
347  N NH1 B ARG A 39  ? 0.7772 0.7250 0.5179 -0.1466 -0.0151 -0.1420 40  ARG A NH1 
348  N NH2 A ARG A 39  ? 0.6724 0.6401 0.3864 -0.1210 -0.0732 -0.1382 40  ARG A NH2 
349  N NH2 B ARG A 39  ? 0.8148 0.7937 0.5850 -0.1607 -0.0085 -0.1653 40  ARG A NH2 
350  N N   A GLU A 40  ? 0.4823 0.4110 0.2676 -0.0868 -0.0284 -0.0810 41  GLU A N   
351  N N   B GLU A 40  ? 0.4809 0.4162 0.2769 -0.0882 -0.0247 -0.0836 41  GLU A N   
352  C CA  A GLU A 40  ? 0.4666 0.3974 0.2610 -0.0759 -0.0351 -0.0737 41  GLU A CA  
353  C CA  B GLU A 40  ? 0.4729 0.4044 0.2695 -0.0774 -0.0325 -0.0744 41  GLU A CA  
354  C C   A GLU A 40  ? 0.4839 0.4309 0.3078 -0.0742 -0.0288 -0.0756 41  GLU A C   
355  C C   B GLU A 40  ? 0.4883 0.4335 0.3128 -0.0739 -0.0271 -0.0741 41  GLU A C   
356  O O   A GLU A 40  ? 0.4563 0.4042 0.2904 -0.0811 -0.0150 -0.0782 41  GLU A O   
357  O O   B GLU A 40  ? 0.4607 0.4042 0.2954 -0.0791 -0.0127 -0.0740 41  GLU A O   
358  C CB  A GLU A 40  ? 0.4909 0.3995 0.2694 -0.0745 -0.0297 -0.0628 41  GLU A CB  
359  C CB  B GLU A 40  ? 0.5017 0.4094 0.2789 -0.0784 -0.0256 -0.0648 41  GLU A CB  
360  C CG  A GLU A 40  ? 0.7073 0.5960 0.4521 -0.0769 -0.0357 -0.0600 41  GLU A CG  
361  C CG  B GLU A 40  ? 0.6843 0.5748 0.4286 -0.0807 -0.0330 -0.0632 41  GLU A CG  
362  C CD  A GLU A 40  ? 1.1793 1.0586 0.9086 -0.0670 -0.0517 -0.0535 41  GLU A CD  
363  C CD  B GLU A 40  ? 1.1311 1.0119 0.8600 -0.0709 -0.0483 -0.0562 41  GLU A CD  
364  O OE1 A GLU A 40  ? 1.1948 1.0635 0.9234 -0.0632 -0.0486 -0.0457 41  GLU A OE1 
365  O OE1 B GLU A 40  ? 1.1574 1.0432 0.8778 -0.0655 -0.0651 -0.0594 41  GLU A OE1 
366  O OE2 A GLU A 40  ? 1.1909 1.0729 0.9084 -0.0627 -0.0677 -0.0568 41  GLU A OE2 
367  O OE2 B GLU A 40  ? 1.1473 1.0154 0.8729 -0.0683 -0.0438 -0.0481 41  GLU A OE2 
368  N N   . GLN A 41  ? 0.4324 0.3901 0.2682 -0.0647 -0.0389 -0.0743 42  GLN A N   
369  C CA  . GLN A 41  ? 0.4096 0.3821 0.2707 -0.0625 -0.0345 -0.0758 42  GLN A CA  
370  C C   . GLN A 41  ? 0.4430 0.4084 0.3055 -0.0541 -0.0362 -0.0663 42  GLN A C   
371  O O   . GLN A 41  ? 0.4484 0.4067 0.2988 -0.0468 -0.0478 -0.0624 42  GLN A O   
372  C CB  . GLN A 41  ? 0.4278 0.4248 0.3051 -0.0600 -0.0453 -0.0870 42  GLN A CB  
373  C CG  . GLN A 41  ? 0.6234 0.6316 0.5044 -0.0703 -0.0415 -0.0988 42  GLN A CG  
374  C CD  . GLN A 41  ? 0.8594 0.8961 0.7617 -0.0697 -0.0493 -0.1123 42  GLN A CD  
375  O OE1 . GLN A 41  ? 0.7738 0.8236 0.6902 -0.0609 -0.0579 -0.1137 42  GLN A OE1 
376  N NE2 . GLN A 41  ? 0.8792 0.9269 0.7852 -0.0799 -0.0456 -0.1241 42  GLN A NE2 
377  N N   . PHE A 42  ? 0.3621 0.3282 0.2378 -0.0552 -0.0251 -0.0628 43  PHE A N   
378  C CA  . PHE A 42  ? 0.3645 0.3257 0.2431 -0.0486 -0.0253 -0.0548 43  PHE A CA  
379  C C   . PHE A 42  ? 0.3996 0.3761 0.2995 -0.0475 -0.0221 -0.0577 43  PHE A C   
380  O O   . PHE A 42  ? 0.4006 0.3789 0.3079 -0.0536 -0.0112 -0.0592 43  PHE A O   
381  C CB  . PHE A 42  ? 0.3807 0.3257 0.2509 -0.0517 -0.0140 -0.0472 43  PHE A CB  
382  C CG  . PHE A 42  ? 0.4156 0.3442 0.2636 -0.0552 -0.0139 -0.0453 43  PHE A CG  
383  C CD1 . PHE A 42  ? 0.4440 0.3688 0.2854 -0.0630 -0.0072 -0.0496 43  PHE A CD1 
384  C CD2 . PHE A 42  ? 0.4612 0.3762 0.2930 -0.0517 -0.0194 -0.0395 43  PHE A CD2 
385  C CE1 . PHE A 42  ? 0.4803 0.3897 0.2995 -0.0674 -0.0061 -0.0485 43  PHE A CE1 
386  C CE2 . PHE A 42  ? 0.5148 0.4123 0.3225 -0.0566 -0.0181 -0.0380 43  PHE A CE2 
387  C CZ  . PHE A 42  ? 0.4905 0.3862 0.2922 -0.0645 -0.0116 -0.0427 43  PHE A CZ  
388  N N   . ARG A 43  ? 0.3567 0.3426 0.2651 -0.0400 -0.0313 -0.0588 44  ARG A N   
389  C CA  . ARG A 43  ? 0.3317 0.3321 0.2593 -0.0396 -0.0279 -0.0623 44  ARG A CA  
390  C C   . ARG A 43  ? 0.3719 0.3629 0.2989 -0.0379 -0.0211 -0.0533 44  ARG A C   
391  O O   . ARG A 43  ? 0.3671 0.3457 0.2834 -0.0337 -0.0241 -0.0464 44  ARG A O   
392  C CB  . ARG A 43  ? 0.3405 0.3570 0.2798 -0.0321 -0.0403 -0.0695 44  ARG A CB  
393  C CG  . ARG A 43  ? 0.4303 0.4618 0.3744 -0.0334 -0.0481 -0.0809 44  ARG A CG  
394  C CD  . ARG A 43  ? 0.4892 0.5453 0.4556 -0.0288 -0.0551 -0.0925 44  ARG A CD  
395  N NE  . ARG A 43  ? 0.6436 0.7079 0.6247 -0.0343 -0.0430 -0.0944 44  ARG A NE  
396  C CZ  . ARG A 43  ? 0.8003 0.8759 0.7918 -0.0450 -0.0325 -0.1025 44  ARG A CZ  
397  N NH1 . ARG A 43  ? 0.7105 0.7946 0.7033 -0.0515 -0.0327 -0.1114 44  ARG A NH1 
398  N NH2 . ARG A 43  ? 0.5733 0.6512 0.5725 -0.0499 -0.0216 -0.1025 44  ARG A NH2 
399  N N   . ALA A 44  ? 0.3273 0.3234 0.2642 -0.0417 -0.0120 -0.0535 45  ALA A N   
400  C CA  . ALA A 44  ? 0.3200 0.3090 0.2563 -0.0399 -0.0067 -0.0456 45  ALA A CA  
401  C C   . ALA A 44  ? 0.3324 0.3304 0.2796 -0.0425 -0.0009 -0.0479 45  ALA A C   
402  O O   . ALA A 44  ? 0.3099 0.3188 0.2650 -0.0469 0.0006  -0.0560 45  ALA A O   
403  C CB  . ALA A 44  ? 0.3381 0.3127 0.2646 -0.0426 0.0009  -0.0393 45  ALA A CB  
404  N N   . HIS A 45  ? 0.2955 0.2890 0.2420 -0.0406 0.0026  -0.0414 46  HIS A N   
405  C CA  . HIS A 45  ? 0.2815 0.2791 0.2329 -0.0435 0.0086  -0.0416 46  HIS A CA  
406  C C   . HIS A 45  ? 0.3144 0.2992 0.2579 -0.0466 0.0170  -0.0359 46  HIS A C   
407  O O   . HIS A 45  ? 0.3060 0.2820 0.2443 -0.0431 0.0172  -0.0295 46  HIS A O   
408  C CB  . HIS A 45  ? 0.2781 0.2783 0.2321 -0.0388 0.0058  -0.0382 46  HIS A CB  
409  C CG  . HIS A 45  ? 0.3078 0.3172 0.2689 -0.0342 -0.0024 -0.0434 46  HIS A CG  
410  N ND1 . HIS A 45  ? 0.3315 0.3342 0.2874 -0.0285 -0.0093 -0.0403 46  HIS A ND1 
411  C CD2 . HIS A 45  ? 0.3145 0.3380 0.2870 -0.0344 -0.0045 -0.0522 46  HIS A CD2 
412  C CE1 . HIS A 45  ? 0.3237 0.3345 0.2869 -0.0240 -0.0164 -0.0462 46  HIS A CE1 
413  N NE2 . HIS A 45  ? 0.3131 0.3385 0.2883 -0.0270 -0.0141 -0.0541 46  HIS A NE2 
414  N N   . LYS A 46  ? 0.3034 0.2865 0.2460 -0.0532 0.0241  -0.0390 47  LYS A N   
415  C CA  . LYS A 46  ? 0.3069 0.2742 0.2402 -0.0553 0.0320  -0.0336 47  LYS A CA  
416  C C   . LYS A 46  ? 0.3353 0.2967 0.2650 -0.0490 0.0312  -0.0248 47  LYS A C   
417  O O   . LYS A 46  ? 0.3092 0.2606 0.2348 -0.0453 0.0326  -0.0197 47  LYS A O   
418  C CB  . LYS A 46  ? 0.3380 0.3021 0.2682 -0.0640 0.0404  -0.0379 47  LYS A CB  
419  C CG  . LYS A 46  ? 0.3609 0.3288 0.2939 -0.0714 0.0431  -0.0471 47  LYS A CG  
420  C CD  . LYS A 46  ? 0.3483 0.3137 0.2784 -0.0821 0.0529  -0.0529 47  LYS A CD  
421  C CE  . LYS A 46  ? 0.4316 0.4055 0.3675 -0.0904 0.0553  -0.0644 47  LYS A CE  
422  N NZ  . LYS A 46  ? 0.4151 0.3885 0.3494 -0.1027 0.0661  -0.0720 47  LYS A NZ  
423  N N   . THR A 47  ? 0.2992 0.2683 0.2316 -0.0478 0.0288  -0.0243 48  THR A N   
424  C CA  . THR A 47  ? 0.3055 0.2711 0.2344 -0.0425 0.0273  -0.0171 48  THR A CA  
425  C C   . THR A 47  ? 0.3113 0.2780 0.2436 -0.0361 0.0227  -0.0139 48  THR A C   
426  O O   . THR A 47  ? 0.3189 0.2800 0.2488 -0.0317 0.0232  -0.0089 48  THR A O   
427  C CB  . THR A 47  ? 0.3703 0.3447 0.3007 -0.0437 0.0260  -0.0185 48  THR A CB  
428  O OG1 . THR A 47  ? 0.3866 0.3739 0.3272 -0.0429 0.0210  -0.0243 48  THR A OG1 
429  C CG2 . THR A 47  ? 0.3977 0.3671 0.3207 -0.0515 0.0331  -0.0208 48  THR A CG2 
430  N N   . VAL A 48  ? 0.2697 0.2431 0.2070 -0.0356 0.0184  -0.0174 49  VAL A N   
431  C CA  . VAL A 48  ? 0.2674 0.2398 0.2054 -0.0318 0.0158  -0.0153 49  VAL A CA  
432  C C   . VAL A 48  ? 0.3010 0.2643 0.2358 -0.0319 0.0199  -0.0141 49  VAL A C   
433  O O   . VAL A 48  ? 0.2825 0.2441 0.2187 -0.0287 0.0210  -0.0117 49  VAL A O   
434  C CB  . VAL A 48  ? 0.2845 0.2608 0.2237 -0.0316 0.0104  -0.0186 49  VAL A CB  
435  C CG1 . VAL A 48  ? 0.2941 0.2652 0.2300 -0.0302 0.0099  -0.0167 49  VAL A CG1 
436  C CG2 . VAL A 48  ? 0.2791 0.2640 0.2232 -0.0304 0.0068  -0.0204 49  VAL A CG2 
437  N N   . LEU A 49  ? 0.2898 0.2485 0.2215 -0.0360 0.0226  -0.0173 50  LEU A N   
438  C CA  . LEU A 49  ? 0.2856 0.2346 0.2138 -0.0368 0.0276  -0.0172 50  LEU A CA  
439  C C   . LEU A 49  ? 0.3199 0.2615 0.2478 -0.0330 0.0318  -0.0129 50  LEU A C   
440  O O   . LEU A 49  ? 0.3253 0.2635 0.2552 -0.0295 0.0338  -0.0120 50  LEU A O   
441  C CB  . LEU A 49  ? 0.2819 0.2277 0.2065 -0.0429 0.0302  -0.0222 50  LEU A CB  
442  C CG  . LEU A 49  ? 0.3163 0.2693 0.2405 -0.0454 0.0244  -0.0274 50  LEU A CG  
443  C CD1 . LEU A 49  ? 0.3198 0.2721 0.2421 -0.0519 0.0272  -0.0337 50  LEU A CD1 
444  C CD2 . LEU A 49  ? 0.3441 0.2937 0.2633 -0.0437 0.0214  -0.0263 50  LEU A CD2 
445  N N   . MET A 50  ? 0.2856 0.2245 0.2106 -0.0333 0.0328  -0.0106 51  MET A N   
446  C CA  . MET A 50  ? 0.3081 0.2367 0.2290 -0.0283 0.0350  -0.0054 51  MET A CA  
447  C C   . MET A 50  ? 0.3523 0.2886 0.2794 -0.0205 0.0300  -0.0023 51  MET A C   
448  O O   . MET A 50  ? 0.3527 0.2839 0.2817 -0.0141 0.0306  -0.0002 51  MET A O   
449  C CB  . MET A 50  ? 0.3355 0.2579 0.2477 -0.0315 0.0368  -0.0033 51  MET A CB  
450  C CG  . MET A 50  ? 0.3644 0.2796 0.2713 -0.0405 0.0433  -0.0080 51  MET A CG  
451  S SD  . MET A 50  ? 0.4231 0.3364 0.3214 -0.0472 0.0462  -0.0080 51  MET A SD  
452  C CE  . MET A 50  ? 0.3966 0.2842 0.2781 -0.0430 0.0501  0.0005  51  MET A CE  
453  N N   . ALA A 51  ? 0.3043 0.2536 0.2359 -0.0210 0.0252  -0.0030 52  ALA A N   
454  C CA  . ALA A 51  ? 0.2943 0.2532 0.2324 -0.0155 0.0208  -0.0017 52  ALA A CA  
455  C C   . ALA A 51  ? 0.3358 0.2982 0.2817 -0.0136 0.0222  -0.0046 52  ALA A C   
456  O O   . ALA A 51  ? 0.3380 0.3081 0.2914 -0.0085 0.0201  -0.0048 52  ALA A O   
457  C CB  . ALA A 51  ? 0.2909 0.2610 0.2310 -0.0181 0.0168  -0.0031 52  ALA A CB  
458  N N   . CYS A 52  ? 0.2870 0.2447 0.2311 -0.0183 0.0259  -0.0079 53  CYS A N   
459  C CA  . CYS A 52  ? 0.2903 0.2497 0.2388 -0.0191 0.0289  -0.0116 53  CYS A CA  
460  C C   . CYS A 52  ? 0.3330 0.2839 0.2822 -0.0179 0.0349  -0.0135 53  CYS A C   
461  O O   . CYS A 52  ? 0.3171 0.2710 0.2718 -0.0182 0.0384  -0.0176 53  CYS A O   
462  C CB  . CYS A 52  ? 0.2908 0.2494 0.2334 -0.0256 0.0284  -0.0140 53  CYS A CB  
463  S SG  . CYS A 52  ? 0.3199 0.2868 0.2628 -0.0263 0.0222  -0.0132 53  CYS A SG  
464  N N   . SER A 53  ? 0.3024 0.2420 0.2454 -0.0183 0.0372  -0.0119 54  SER A N   
465  C CA  . SER A 53  ? 0.3024 0.2312 0.2440 -0.0189 0.0438  -0.0147 54  SER A CA  
466  C C   . SER A 53  ? 0.3570 0.2735 0.2957 -0.0135 0.0454  -0.0111 54  SER A C   
467  O O   . SER A 53  ? 0.3359 0.2458 0.2661 -0.0160 0.0446  -0.0079 54  SER A O   
468  C CB  . SER A 53  ? 0.3166 0.2405 0.2494 -0.0278 0.0461  -0.0178 54  SER A CB  
469  O OG  . SER A 53  ? 0.3612 0.2726 0.2893 -0.0305 0.0525  -0.0203 54  SER A OG  
470  N N   . GLY A 54  ? 0.3401 0.2517 0.2848 -0.0066 0.0485  -0.0125 55  GLY A N   
471  C CA  . GLY A 54  ? 0.3412 0.2356 0.2806 -0.0002 0.0502  -0.0089 55  GLY A CA  
472  C C   . GLY A 54  ? 0.3858 0.2633 0.3131 -0.0084 0.0570  -0.0100 55  GLY A C   
473  O O   . GLY A 54  ? 0.3820 0.2439 0.2982 -0.0081 0.0582  -0.0056 55  GLY A O   
474  N N   . LEU A 55  ? 0.3492 0.2297 0.2766 -0.0171 0.0617  -0.0163 56  LEU A N   
475  C CA  . LEU A 55  ? 0.3599 0.2277 0.2770 -0.0262 0.0679  -0.0192 56  LEU A CA  
476  C C   . LEU A 55  ? 0.3974 0.2678 0.3071 -0.0331 0.0651  -0.0172 56  LEU A C   
477  O O   . LEU A 55  ? 0.3844 0.2405 0.2850 -0.0368 0.0696  -0.0164 56  LEU A O   
478  C CB  . LEU A 55  ? 0.3596 0.2315 0.2772 -0.0338 0.0719  -0.0267 56  LEU A CB  
479  C CG  . LEU A 55  ? 0.4320 0.2928 0.3402 -0.0436 0.0783  -0.0316 56  LEU A CG  
480  C CD1 . LEU A 55  ? 0.4585 0.2981 0.3637 -0.0407 0.0870  -0.0325 56  LEU A CD1 
481  C CD2 . LEU A 55  ? 0.4084 0.2765 0.3142 -0.0517 0.0790  -0.0382 56  LEU A CD2 
482  N N   . PHE A 56  ? 0.3388 0.2265 0.2526 -0.0348 0.0584  -0.0172 57  PHE A N   
483  C CA  . PHE A 56  ? 0.3260 0.2190 0.2361 -0.0406 0.0558  -0.0171 57  PHE A CA  
484  C C   . PHE A 56  ? 0.3774 0.2631 0.2824 -0.0370 0.0553  -0.0111 57  PHE A C   
485  O O   . PHE A 56  ? 0.3654 0.2459 0.2634 -0.0437 0.0586  -0.0120 57  PHE A O   
486  C CB  . PHE A 56  ? 0.3302 0.2413 0.2457 -0.0420 0.0486  -0.0189 57  PHE A CB  
487  C CG  . PHE A 56  ? 0.3412 0.2556 0.2556 -0.0475 0.0486  -0.0249 57  PHE A CG  
488  C CD1 . PHE A 56  ? 0.3717 0.2828 0.2817 -0.0554 0.0522  -0.0307 57  PHE A CD1 
489  C CD2 . PHE A 56  ? 0.3502 0.2703 0.2660 -0.0458 0.0451  -0.0253 57  PHE A CD2 
490  C CE1 . PHE A 56  ? 0.3739 0.2879 0.2808 -0.0602 0.0511  -0.0364 57  PHE A CE1 
491  C CE2 . PHE A 56  ? 0.3760 0.2963 0.2861 -0.0510 0.0445  -0.0301 57  PHE A CE2 
492  C CZ  . PHE A 56  ? 0.3514 0.2691 0.2571 -0.0576 0.0467  -0.0355 57  PHE A CZ  
493  N N   . TYR A 57  ? 0.3394 0.2241 0.2471 -0.0270 0.0518  -0.0055 58  TYR A N   
494  C CA  . TYR A 57  ? 0.3555 0.2305 0.2548 -0.0225 0.0501  0.0012  58  TYR A CA  
495  C C   . TYR A 57  ? 0.4249 0.2745 0.3098 -0.0254 0.0580  0.0026  58  TYR A C   
496  O O   . TYR A 57  ? 0.4077 0.2475 0.2801 -0.0309 0.0606  0.0048  58  TYR A O   
497  C CB  . TYR A 57  ? 0.3742 0.2534 0.2801 -0.0100 0.0439  0.0054  58  TYR A CB  
498  C CG  . TYR A 57  ? 0.4313 0.2980 0.3256 -0.0035 0.0406  0.0129  58  TYR A CG  
499  C CD1 . TYR A 57  ? 0.4496 0.3197 0.3358 -0.0076 0.0379  0.0158  58  TYR A CD1 
500  C CD2 . TYR A 57  ? 0.4897 0.3397 0.3798 0.0070  0.0401  0.0169  58  TYR A CD2 
501  C CE1 . TYR A 57  ? 0.4896 0.3458 0.3609 -0.0024 0.0348  0.0231  58  TYR A CE1 
502  C CE2 . TYR A 57  ? 0.5434 0.3787 0.4190 0.0140  0.0356  0.0248  58  TYR A CE2 
503  C CZ  . TYR A 57  ? 0.6327 0.4709 0.4977 0.0088  0.0329  0.0282  58  TYR A CZ  
504  O OH  . TYR A 57  ? 0.7193 0.5410 0.5663 0.0151  0.0283  0.0363  58  TYR A OH  
505  N N   A SER A 58  ? 0.4030 0.2406 0.2889 -0.0227 0.0628  0.0006  59  SER A N   
506  N N   B SER A 58  ? 0.4034 0.2411 0.2894 -0.0227 0.0628  0.0006  59  SER A N   
507  C CA  A SER A 58  ? 0.4263 0.2366 0.2984 -0.0254 0.0713  0.0012  59  SER A CA  
508  C CA  B SER A 58  ? 0.4276 0.2382 0.2999 -0.0255 0.0713  0.0011  59  SER A CA  
509  C C   A SER A 58  ? 0.4936 0.3020 0.3590 -0.0411 0.0788  -0.0050 59  SER A C   
510  C C   B SER A 58  ? 0.4909 0.2999 0.3564 -0.0411 0.0786  -0.0049 59  SER A C   
511  O O   A SER A 58  ? 0.5240 0.3128 0.3740 -0.0469 0.0850  -0.0033 59  SER A O   
512  O O   B SER A 58  ? 0.5169 0.3071 0.3671 -0.0469 0.0844  -0.0030 59  SER A O   
513  C CB  A SER A 58  ? 0.4555 0.2571 0.3335 -0.0193 0.0750  -0.0017 59  SER A CB  
514  C CB  B SER A 58  ? 0.4620 0.2645 0.3402 -0.0203 0.0753  -0.0023 59  SER A CB  
515  O OG  A SER A 58  ? 0.4851 0.2866 0.3693 -0.0041 0.0686  0.0030  59  SER A OG  
516  O OG  B SER A 58  ? 0.5472 0.3211 0.4114 -0.0233 0.0843  -0.0023 59  SER A OG  
517  N N   . ILE A 59  ? 0.4295 0.2582 0.3058 -0.0480 0.0779  -0.0126 60  ILE A N   
518  C CA  . ILE A 59  ? 0.4208 0.2541 0.2950 -0.0620 0.0830  -0.0207 60  ILE A CA  
519  C C   . ILE A 59  ? 0.4585 0.2971 0.3285 -0.0680 0.0825  -0.0202 60  ILE A C   
520  O O   . ILE A 59  ? 0.4841 0.3103 0.3439 -0.0782 0.0910  -0.0235 60  ILE A O   
521  C CB  . ILE A 59  ? 0.4330 0.2879 0.3189 -0.0656 0.0789  -0.0283 60  ILE A CB  
522  C CG1 . ILE A 59  ? 0.4378 0.2853 0.3247 -0.0638 0.0825  -0.0311 60  ILE A CG1 
523  C CG2 . ILE A 59  ? 0.4089 0.2746 0.2957 -0.0784 0.0811  -0.0375 60  ILE A CG2 
524  C CD1 . ILE A 59  ? 0.4615 0.3275 0.3556 -0.0657 0.0771  -0.0363 60  ILE A CD1 
525  N N   . PHE A 60  ? 0.3944 0.2505 0.2717 -0.0627 0.0739  -0.0171 61  PHE A N   
526  C CA  . PHE A 60  ? 0.3924 0.2563 0.2676 -0.0695 0.0743  -0.0190 61  PHE A CA  
527  C C   . PHE A 60  ? 0.4547 0.2995 0.3137 -0.0683 0.0773  -0.0112 61  PHE A C   
528  O O   . PHE A 60  ? 0.4685 0.3176 0.3234 -0.0757 0.0796  -0.0134 61  PHE A O   
529  C CB  . PHE A 60  ? 0.3804 0.2711 0.2700 -0.0665 0.0648  -0.0212 61  PHE A CB  
530  C CG  . PHE A 60  ? 0.3800 0.2859 0.2808 -0.0686 0.0616  -0.0288 61  PHE A CG  
531  C CD1 . PHE A 60  ? 0.4233 0.3343 0.3260 -0.0789 0.0659  -0.0386 61  PHE A CD1 
532  C CD2 . PHE A 60  ? 0.3779 0.2928 0.2859 -0.0608 0.0541  -0.0267 61  PHE A CD2 
533  C CE1 . PHE A 60  ? 0.4226 0.3470 0.3333 -0.0800 0.0610  -0.0453 61  PHE A CE1 
534  C CE2 . PHE A 60  ? 0.4081 0.3334 0.3215 -0.0628 0.0505  -0.0328 61  PHE A CE2 
535  C CZ  . PHE A 60  ? 0.3943 0.3244 0.3087 -0.0717 0.0531  -0.0416 61  PHE A CZ  
536  N N   . THR A 61  ? 0.4406 0.2633 0.2890 -0.0594 0.0774  -0.0029 62  THR A N   
537  C CA  . THR A 61  ? 0.4610 0.2593 0.2882 -0.0583 0.0801  0.0052  62  THR A CA  
538  C C   . THR A 61  ? 0.5609 0.3297 0.3706 -0.0672 0.0923  0.0038  62  THR A C   
539  O O   . THR A 61  ? 0.5732 0.3154 0.3600 -0.0693 0.0971  0.0099  62  THR A O   
540  C CB  . THR A 61  ? 0.5636 0.3547 0.3877 -0.0420 0.0712  0.0154  62  THR A CB  
541  O OG1 . THR A 61  ? 0.5271 0.3125 0.3588 -0.0333 0.0705  0.0154  62  THR A OG1 
542  C CG2 . THR A 61  ? 0.5054 0.3228 0.3421 -0.0361 0.0606  0.0167  62  THR A CG2 
543  N N   . ASP A 62  ? 0.5157 0.2876 0.3341 -0.0734 0.0979  -0.0046 63  ASP A N   
544  C CA  . ASP A 62  ? 0.5500 0.2954 0.3531 -0.0842 0.1110  -0.0082 63  ASP A CA  
545  C C   . ASP A 62  ? 0.6200 0.3705 0.4177 -0.1016 0.1191  -0.0157 63  ASP A C   
546  O O   . ASP A 62  ? 0.5754 0.3571 0.3910 -0.1072 0.1160  -0.0246 63  ASP A O   
547  C CB  . ASP A 62  ? 0.5648 0.3146 0.3793 -0.0866 0.1143  -0.0162 63  ASP A CB  
548  C CG  . ASP A 62  ? 0.7180 0.4421 0.5175 -0.0999 0.1287  -0.0218 63  ASP A CG  
549  O OD1 . ASP A 62  ? 0.7991 0.4896 0.5822 -0.0950 0.1338  -0.0156 63  ASP A OD1 
550  O OD2 . ASP A 62  ? 0.7103 0.4474 0.5141 -0.1154 0.1350  -0.0329 63  ASP A OD2 
551  N N   . GLN A 63  ? 0.6485 0.3673 0.4208 -0.1102 0.1299  -0.0129 64  GLN A N   
552  C CA  . GLN A 63  ? 0.6671 0.3868 0.4311 -0.1285 0.1404  -0.0206 64  GLN A CA  
553  C C   . GLN A 63  ? 0.6969 0.4400 0.4785 -0.1437 0.1472  -0.0375 64  GLN A C   
554  O O   . GLN A 63  ? 0.7177 0.4786 0.5048 -0.1561 0.1516  -0.0469 64  GLN A O   
555  C CB  . GLN A 63  ? 0.7401 0.4146 0.4690 -0.1357 0.1523  -0.0140 64  GLN A CB  
556  C CG  . GLN A 63  ? 0.9630 0.6199 0.6722 -0.1242 0.1449  0.0008  64  GLN A CG  
557  N N   . LEU A 64  ? 0.6031 0.3471 0.3937 -0.1429 0.1480  -0.0425 65  LEU A N   
558  C CA  . LEU A 64  ? 0.5832 0.3523 0.3913 -0.1558 0.1517  -0.0589 65  LEU A CA  
559  C C   . LEU A 64  ? 0.6078 0.4153 0.4424 -0.1464 0.1371  -0.0625 65  LEU A C   
560  O O   . LEU A 64  ? 0.6116 0.4491 0.4627 -0.1537 0.1349  -0.0742 65  LEU A O   
561  C CB  . LEU A 64  ? 0.6044 0.3529 0.4053 -0.1628 0.1617  -0.0641 65  LEU A CB  
562  C CG  . LEU A 64  ? 0.7141 0.4287 0.4913 -0.1792 0.1797  -0.0674 65  LEU A CG  
563  C CD1 . LEU A 64  ? 0.7373 0.4327 0.5095 -0.1843 0.1884  -0.0728 65  LEU A CD1 
564  C CD2 . LEU A 64  ? 0.7631 0.4971 0.5457 -0.1990 0.1884  -0.0820 65  LEU A CD2 
565  N N   . LYS A 65  ? 0.5199 0.3260 0.3584 -0.1307 0.1275  -0.0535 66  LYS A N   
566  C CA  . LYS A 65  ? 0.4834 0.3197 0.3422 -0.1228 0.1149  -0.0563 66  LYS A CA  
567  C C   . LYS A 65  ? 0.5433 0.4035 0.4131 -0.1171 0.1048  -0.0543 66  LYS A C   
568  O O   . LYS A 65  ? 0.5251 0.4119 0.4111 -0.1150 0.0962  -0.0602 66  LYS A O   
569  C CB  . LYS A 65  ? 0.4864 0.3137 0.3456 -0.1101 0.1100  -0.0491 66  LYS A CB  
570  C CG  . LYS A 65  ? 0.4953 0.3021 0.3466 -0.1156 0.1197  -0.0533 66  LYS A CG  
571  C CD  . LYS A 65  ? 0.4900 0.2926 0.3450 -0.1032 0.1150  -0.0482 66  LYS A CD  
572  C CE  . LYS A 65  ? 0.5673 0.3442 0.4128 -0.1063 0.1255  -0.0508 66  LYS A CE  
573  N NZ  . LYS A 65  ? 0.6175 0.3603 0.4465 -0.1019 0.1323  -0.0423 66  LYS A NZ  
574  N N   . CYS A 66  ? 0.5408 0.3901 0.4002 -0.1148 0.1061  -0.0464 67  CYS A N   
575  C CA  . CYS A 66  ? 0.5330 0.4029 0.4013 -0.1104 0.0980  -0.0450 67  CYS A CA  
576  C C   . CYS A 66  ? 0.5715 0.4695 0.4556 -0.1202 0.0981  -0.0592 67  CYS A C   
577  O O   . CYS A 66  ? 0.5632 0.4838 0.4609 -0.1146 0.0889  -0.0606 67  CYS A O   
578  C CB  . CYS A 66  ? 0.5724 0.4233 0.4229 -0.1096 0.1014  -0.0358 67  CYS A CB  
579  S SG  . CYS A 66  ? 0.6668 0.4976 0.4980 -0.1288 0.1184  -0.0418 67  CYS A SG  
580  N N   . ASN A 67  ? 0.5205 0.4170 0.4034 -0.1348 0.1086  -0.0705 68  ASN A N   
581  C CA  . ASN A 67  ? 0.5146 0.4390 0.4142 -0.1453 0.1100  -0.0866 68  ASN A CA  
582  C C   . ASN A 67  ? 0.5375 0.4845 0.4543 -0.1445 0.1025  -0.0967 68  ASN A C   
583  O O   . ASN A 67  ? 0.5086 0.4820 0.4419 -0.1512 0.1013  -0.1113 68  ASN A O   
584  C CB  . ASN A 67  ? 0.5416 0.4534 0.4301 -0.1638 0.1269  -0.0949 68  ASN A CB  
585  C CG  . ASN A 67  ? 0.7534 0.6464 0.6239 -0.1657 0.1331  -0.0865 68  ASN A CG  
586  O OD1 . ASN A 67  ? 0.7679 0.6291 0.6146 -0.1742 0.1455  -0.0821 68  ASN A OD1 
587  N ND2 . ASN A 67  ? 0.6098 0.5191 0.4886 -0.1574 0.1244  -0.0832 68  ASN A ND2 
588  N N   . LEU A 68  ? 0.4951 0.4325 0.4080 -0.1362 0.0972  -0.0900 69  LEU A N   
589  C CA  . LEU A 68  ? 0.4727 0.4285 0.3973 -0.1356 0.0896  -0.0987 69  LEU A CA  
590  C C   . LEU A 68  ? 0.4913 0.4707 0.4299 -0.1237 0.0739  -0.0978 69  LEU A C   
591  O O   . LEU A 68  ? 0.4754 0.4495 0.4112 -0.1129 0.0684  -0.0864 69  LEU A O   
592  C CB  . LEU A 68  ? 0.4839 0.4196 0.3975 -0.1325 0.0912  -0.0927 69  LEU A CB  
593  C CG  . LEU A 68  ? 0.5580 0.4671 0.4569 -0.1435 0.1066  -0.0942 69  LEU A CG  
594  C CD1 . LEU A 68  ? 0.5662 0.4563 0.4563 -0.1376 0.1072  -0.0878 69  LEU A CD1 
595  C CD2 . LEU A 68  ? 0.5762 0.4977 0.4811 -0.1602 0.1142  -0.1115 69  LEU A CD2 
596  N N   A SER A 69  ? 0.4408 0.4456 0.3938 -0.1254 0.0662  -0.1103 70  SER A N   
597  N N   B SER A 69  ? 0.4386 0.4433 0.3915 -0.1255 0.0663  -0.1104 70  SER A N   
598  C CA  A SER A 69  ? 0.4248 0.4492 0.3891 -0.1134 0.0503  -0.1101 70  SER A CA  
599  C CA  B SER A 69  ? 0.4217 0.4468 0.3864 -0.1139 0.0504  -0.1108 70  SER A CA  
600  C C   A SER A 69  ? 0.4384 0.4580 0.3960 -0.1066 0.0413  -0.1059 70  SER A C   
601  C C   B SER A 69  ? 0.4374 0.4574 0.3952 -0.1067 0.0413  -0.1062 70  SER A C   
602  O O   A SER A 69  ? 0.4076 0.4346 0.3677 -0.0959 0.0286  -0.1023 70  SER A O   
603  O O   B SER A 69  ? 0.4064 0.4339 0.3668 -0.0961 0.0285  -0.1027 70  SER A O   
604  C CB  A SER A 69  ? 0.4716 0.5267 0.4557 -0.1170 0.0454  -0.1264 70  SER A CB  
605  C CB  B SER A 69  ? 0.4643 0.5200 0.4486 -0.1182 0.0458  -0.1277 70  SER A CB  
606  O OG  A SER A 69  ? 0.5797 0.6452 0.5681 -0.1261 0.0466  -0.1395 70  SER A OG  
607  O OG  B SER A 69  ? 0.5490 0.6112 0.5404 -0.1242 0.0539  -0.1323 70  SER A OG  
608  N N   . VAL A 70  ? 0.4093 0.4147 0.3565 -0.1135 0.0487  -0.1068 71  VAL A N   
609  C CA  . VAL A 70  ? 0.4101 0.4085 0.3482 -0.1097 0.0431  -0.1038 71  VAL A CA  
610  C C   . VAL A 70  ? 0.4367 0.4074 0.3607 -0.1111 0.0542  -0.0949 71  VAL A C   
611  O O   . VAL A 70  ? 0.4405 0.3990 0.3604 -0.1201 0.0669  -0.0975 71  VAL A O   
612  C CB  . VAL A 70  ? 0.4740 0.4877 0.4157 -0.1170 0.0391  -0.1180 71  VAL A CB  
613  C CG1 . VAL A 70  ? 0.4836 0.4876 0.4119 -0.1141 0.0339  -0.1145 71  VAL A CG1 
614  C CG2 . VAL A 70  ? 0.4664 0.5099 0.4248 -0.1139 0.0266  -0.1284 71  VAL A CG2 
615  N N   . ILE A 71  ? 0.3558 0.3162 0.2723 -0.1023 0.0499  -0.0852 72  ILE A N   
616  C CA  . ILE A 71  ? 0.3664 0.3039 0.2725 -0.1015 0.0588  -0.0782 72  ILE A CA  
617  C C   . ILE A 71  ? 0.4121 0.3474 0.3106 -0.1014 0.0552  -0.0800 72  ILE A C   
618  O O   . ILE A 71  ? 0.4081 0.3501 0.3051 -0.0949 0.0450  -0.0767 72  ILE A O   
619  C CB  . ILE A 71  ? 0.3928 0.3202 0.2983 -0.0918 0.0593  -0.0658 72  ILE A CB  
620  C CG1 . ILE A 71  ? 0.4061 0.3332 0.3151 -0.0929 0.0633  -0.0637 72  ILE A CG1 
621  C CG2 . ILE A 71  ? 0.4129 0.3202 0.3109 -0.0889 0.0666  -0.0603 72  ILE A CG2 
622  C CD1 . ILE A 71  ? 0.4473 0.3585 0.3497 -0.1027 0.0766  -0.0671 72  ILE A CD1 
623  N N   . ASN A 72  ? 0.3937 0.3172 0.2854 -0.1090 0.0644  -0.0850 73  ASN A N   
624  C CA  . ASN A 72  ? 0.3999 0.3194 0.2820 -0.1109 0.0632  -0.0877 73  ASN A CA  
625  C C   . ASN A 72  ? 0.4328 0.3336 0.3095 -0.1059 0.0705  -0.0803 73  ASN A C   
626  O O   . ASN A 72  ? 0.4195 0.3050 0.2961 -0.1072 0.0816  -0.0794 73  ASN A O   
627  C CB  . ASN A 72  ? 0.4628 0.3824 0.3412 -0.1232 0.0691  -0.1000 73  ASN A CB  
628  C CG  . ASN A 72  ? 0.6753 0.6166 0.5621 -0.1290 0.0625  -0.1102 73  ASN A CG  
629  O OD1 . ASN A 72  ? 0.5486 0.5072 0.4379 -0.1247 0.0487  -0.1120 73  ASN A OD1 
630  N ND2 . ASN A 72  ? 0.6191 0.5592 0.5101 -0.1390 0.0725  -0.1179 73  ASN A ND2 
631  N N   . LEU A 73  ? 0.3863 0.2876 0.2582 -0.1005 0.0648  -0.0758 74  LEU A N   
632  C CA  . LEU A 73  ? 0.3885 0.2760 0.2581 -0.0964 0.0722  -0.0712 74  LEU A CA  
633  C C   . LEU A 73  ? 0.4436 0.3206 0.3040 -0.1042 0.0808  -0.0786 74  LEU A C   
634  O O   . LEU A 73  ? 0.4481 0.3298 0.3010 -0.1124 0.0783  -0.0864 74  LEU A O   
635  C CB  . LEU A 73  ? 0.3780 0.2694 0.2457 -0.0896 0.0652  -0.0648 74  LEU A CB  
636  C CG  . LEU A 73  ? 0.4114 0.3123 0.2877 -0.0816 0.0572  -0.0575 74  LEU A CG  
637  C CD1 . LEU A 73  ? 0.4223 0.3221 0.2966 -0.0762 0.0548  -0.0520 74  LEU A CD1 
638  C CD2 . LEU A 73  ? 0.3990 0.2973 0.2854 -0.0781 0.0619  -0.0541 74  LEU A CD2 
639  N N   . ASP A 74  ? 0.4142 0.2782 0.2759 -0.1012 0.0903  -0.0772 75  ASP A N   
640  C CA  . ASP A 74  ? 0.4251 0.2777 0.2795 -0.1078 0.1004  -0.0847 75  ASP A CA  
641  C C   . ASP A 74  ? 0.4807 0.3389 0.3209 -0.1143 0.0949  -0.0888 75  ASP A C   
642  O O   . ASP A 74  ? 0.4662 0.3303 0.3032 -0.1100 0.0870  -0.0834 75  ASP A O   
643  C CB  . ASP A 74  ? 0.4405 0.2828 0.3020 -0.1004 0.1090  -0.0820 75  ASP A CB  
644  C CG  . ASP A 74  ? 0.5738 0.4031 0.4310 -0.1058 0.1215  -0.0905 75  ASP A CG  
645  O OD1 . ASP A 74  ? 0.5960 0.4268 0.4424 -0.1130 0.1225  -0.0960 75  ASP A OD1 
646  O OD2 . ASP A 74  ? 0.5874 0.4032 0.4505 -0.1027 0.1303  -0.0917 75  ASP A OD2 
647  N N   . PRO A 75  ? 0.5047 0.3596 0.3341 -0.1247 0.0985  -0.0982 76  PRO A N   
648  C CA  . PRO A 75  ? 0.5193 0.3777 0.3310 -0.1307 0.0918  -0.1015 76  PRO A CA  
649  C C   . PRO A 75  ? 0.5643 0.4151 0.3669 -0.1299 0.0956  -0.0992 76  PRO A C   
650  O O   . PRO A 75  ? 0.5829 0.4344 0.3681 -0.1332 0.0881  -0.0988 76  PRO A O   
651  C CB  . PRO A 75  ? 0.5611 0.4163 0.3640 -0.1426 0.0973  -0.1131 76  PRO A CB  
652  C CG  . PRO A 75  ? 0.6225 0.4667 0.4373 -0.1430 0.1112  -0.1159 76  PRO A CG  
653  C CD  . PRO A 75  ? 0.5413 0.3879 0.3717 -0.1322 0.1086  -0.1064 76  PRO A CD  
654  N N   . GLU A 76  ? 0.5228 0.3661 0.3363 -0.1255 0.1068  -0.0981 77  GLU A N   
655  C CA  . GLU A 76  ? 0.5440 0.3827 0.3526 -0.1256 0.1125  -0.0979 77  GLU A CA  
656  C C   . GLU A 76  ? 0.5344 0.3802 0.3441 -0.1187 0.1028  -0.0886 77  GLU A C   
657  O O   . GLU A 76  ? 0.5297 0.3720 0.3305 -0.1211 0.1056  -0.0885 77  GLU A O   
658  C CB  . GLU A 76  ? 0.5746 0.4069 0.3996 -0.1213 0.1266  -0.1012 77  GLU A CB  
659  C CG  . GLU A 76  ? 0.8339 0.6605 0.6529 -0.1267 0.1377  -0.1081 77  GLU A CG  
660  C CD  . GLU A 76  ? 1.2131 1.0300 1.0182 -0.1385 0.1472  -0.1190 77  GLU A CD  
661  O OE1 . GLU A 76  ? 1.2253 1.0355 1.0397 -0.1380 0.1555  -0.1244 77  GLU A OE1 
662  O OE2 . GLU A 76  ? 1.1569 0.9709 0.9398 -0.1486 0.1465  -0.1222 77  GLU A OE2 
663  N N   . ILE A 77  ? 0.4585 0.3133 0.2786 -0.1112 0.0929  -0.0818 78  ILE A N   
664  C CA  . ILE A 77  ? 0.4466 0.3076 0.2689 -0.1045 0.0843  -0.0736 78  ILE A CA  
665  C C   . ILE A 77  ? 0.4970 0.3565 0.2978 -0.1084 0.0739  -0.0719 78  ILE A C   
666  O O   . ILE A 77  ? 0.4856 0.3479 0.2774 -0.1112 0.0654  -0.0740 78  ILE A O   
667  C CB  . ILE A 77  ? 0.4651 0.3353 0.3050 -0.0955 0.0782  -0.0676 78  ILE A CB  
668  C CG1 . ILE A 77  ? 0.4692 0.3362 0.3260 -0.0905 0.0880  -0.0681 78  ILE A CG1 
669  C CG2 . ILE A 77  ? 0.4287 0.3053 0.2706 -0.0892 0.0696  -0.0600 78  ILE A CG2 
670  C CD1 . ILE A 77  ? 0.5352 0.3999 0.4007 -0.0865 0.0967  -0.0688 78  ILE A CD1 
671  N N   . ASN A 78  ? 0.5115 0.3661 0.3040 -0.1086 0.0746  -0.0685 79  ASN A N   
672  C CA  . ASN A 78  ? 0.5283 0.3754 0.2963 -0.1117 0.0657  -0.0654 79  ASN A CA  
673  C C   . ASN A 78  ? 0.5230 0.3773 0.2953 -0.1029 0.0512  -0.0579 79  ASN A C   
674  O O   . ASN A 78  ? 0.4841 0.3444 0.2727 -0.0965 0.0521  -0.0535 79  ASN A O   
675  C CB  . ASN A 78  ? 0.5512 0.3875 0.3079 -0.1173 0.0755  -0.0658 79  ASN A CB  
676  C CG  . ASN A 78  ? 0.7642 0.5870 0.4912 -0.1210 0.0676  -0.0614 79  ASN A CG  
677  O OD1 . ASN A 78  ? 0.6301 0.4510 0.3565 -0.1170 0.0635  -0.0554 79  ASN A OD1 
678  N ND2 . ASN A 78  ? 0.6774 0.4889 0.3775 -0.1286 0.0647  -0.0644 79  ASN A ND2 
679  N N   . PRO A 79  ? 0.5050 0.3597 0.2638 -0.1020 0.0375  -0.0573 80  PRO A N   
680  C CA  . PRO A 79  ? 0.4888 0.3510 0.2536 -0.0928 0.0238  -0.0516 80  PRO A CA  
681  C C   . PRO A 79  ? 0.5298 0.3828 0.2873 -0.0896 0.0225  -0.0444 80  PRO A C   
682  O O   . PRO A 79  ? 0.4993 0.3608 0.2726 -0.0820 0.0183  -0.0404 80  PRO A O   
683  C CB  . PRO A 79  ? 0.5377 0.4001 0.2858 -0.0929 0.0097  -0.0541 80  PRO A CB  
684  C CG  . PRO A 79  ? 0.6026 0.4645 0.3453 -0.1021 0.0167  -0.0623 80  PRO A CG  
685  C CD  . PRO A 79  ? 0.5546 0.4045 0.2931 -0.1088 0.0331  -0.0627 80  PRO A CD  
686  N N   . GLU A 80  ? 0.5079 0.3430 0.2411 -0.0966 0.0276  -0.0436 81  GLU A N   
687  C CA  . GLU A 80  ? 0.5109 0.3350 0.2353 -0.0960 0.0286  -0.0379 81  GLU A CA  
688  C C   . GLU A 80  ? 0.5170 0.3520 0.2679 -0.0943 0.0398  -0.0383 81  GLU A C   
689  O O   . GLU A 80  ? 0.4943 0.3323 0.2532 -0.0887 0.0362  -0.0337 81  GLU A O   
690  C CB  . GLU A 80  ? 0.5629 0.3631 0.2526 -0.1061 0.0334  -0.0378 81  GLU A CB  
691  C CG  . GLU A 80  ? 0.6682 0.4540 0.3452 -0.1059 0.0331  -0.0317 81  GLU A CG  
692  C CD  . GLU A 80  ? 0.9991 0.7588 0.6417 -0.1179 0.0417  -0.0316 81  GLU A CD  
693  O OE1 . GLU A 80  ? 0.9960 0.7364 0.6164 -0.1175 0.0364  -0.0254 81  GLU A OE1 
694  O OE2 . GLU A 80  ? 0.8968 0.6539 0.5338 -0.1284 0.0547  -0.0381 81  GLU A OE2 
695  N N   . GLY A 81  ? 0.4825 0.3235 0.2466 -0.0983 0.0525  -0.0441 82  GLY A N   
696  C CA  . GLY A 81  ? 0.4564 0.3095 0.2468 -0.0949 0.0614  -0.0453 82  GLY A CA  
697  C C   . GLY A 81  ? 0.4537 0.3214 0.2657 -0.0845 0.0532  -0.0412 82  GLY A C   
698  O O   . GLY A 81  ? 0.4141 0.2889 0.2397 -0.0799 0.0532  -0.0384 82  GLY A O   
699  N N   . PHE A 82  ? 0.4011 0.2737 0.2156 -0.0820 0.0463  -0.0417 83  PHE A N   
700  C CA  . PHE A 82  ? 0.3698 0.2554 0.2027 -0.0739 0.0395  -0.0388 83  PHE A CA  
701  C C   . PHE A 82  ? 0.4065 0.2925 0.2354 -0.0691 0.0292  -0.0336 83  PHE A C   
702  O O   . PHE A 82  ? 0.3834 0.2780 0.2273 -0.0636 0.0281  -0.0307 83  PHE A O   
703  C CB  . PHE A 82  ? 0.3867 0.2778 0.2223 -0.0744 0.0355  -0.0424 83  PHE A CB  
704  C CG  . PHE A 82  ? 0.3836 0.2873 0.2376 -0.0680 0.0315  -0.0404 83  PHE A CG  
705  C CD1 . PHE A 82  ? 0.4156 0.3228 0.2853 -0.0655 0.0390  -0.0396 83  PHE A CD1 
706  C CD2 . PHE A 82  ? 0.3912 0.3020 0.2459 -0.0640 0.0200  -0.0391 83  PHE A CD2 
707  C CE1 . PHE A 82  ? 0.4214 0.3376 0.3040 -0.0606 0.0358  -0.0372 83  PHE A CE1 
708  C CE2 . PHE A 82  ? 0.4023 0.3247 0.2733 -0.0594 0.0178  -0.0382 83  PHE A CE2 
709  C CZ  . PHE A 82  ? 0.3836 0.3077 0.2669 -0.0584 0.0260  -0.0368 83  PHE A CZ  
710  N N   . CYS A 83  ? 0.4243 0.2997 0.2319 -0.0707 0.0213  -0.0325 84  CYS A N   
711  C CA  . CYS A 83  ? 0.4522 0.3240 0.2535 -0.0653 0.0110  -0.0277 84  CYS A CA  
712  C C   . CYS A 83  ? 0.4588 0.3270 0.2633 -0.0655 0.0172  -0.0246 84  CYS A C   
713  O O   . CYS A 83  ? 0.4309 0.3058 0.2465 -0.0596 0.0126  -0.0218 84  CYS A O   
714  C CB  . CYS A 83  ? 0.5119 0.3678 0.2852 -0.0667 0.0019  -0.0267 84  CYS A CB  
715  S SG  . CYS A 83  ? 0.5887 0.4375 0.3536 -0.0574 -0.0129 -0.0212 84  CYS A SG  
716  N N   . ILE A 84  ? 0.4278 0.2870 0.2239 -0.0733 0.0285  -0.0264 85  ILE A N   
717  C CA  . ILE A 84  ? 0.4049 0.2625 0.2047 -0.0759 0.0363  -0.0259 85  ILE A CA  
718  C C   . ILE A 84  ? 0.3977 0.2754 0.2271 -0.0699 0.0385  -0.0265 85  ILE A C   
719  O O   . ILE A 84  ? 0.3807 0.2627 0.2177 -0.0672 0.0372  -0.0246 85  ILE A O   
720  C CB  . ILE A 84  ? 0.4464 0.2938 0.2340 -0.0867 0.0494  -0.0305 85  ILE A CB  
721  C CG1 . ILE A 84  ? 0.4827 0.3046 0.2336 -0.0936 0.0467  -0.0284 85  ILE A CG1 
722  C CG2 . ILE A 84  ? 0.4400 0.2947 0.2419 -0.0897 0.0600  -0.0337 85  ILE A CG2 
723  C CD1 . ILE A 84  ? 0.5711 0.3823 0.3063 -0.1052 0.0589  -0.0338 85  ILE A CD1 
724  N N   . LEU A 85  ? 0.3482 0.2362 0.1923 -0.0679 0.0417  -0.0291 86  LEU A N   
725  C CA  . LEU A 85  ? 0.3350 0.2388 0.2033 -0.0615 0.0429  -0.0288 86  LEU A CA  
726  C C   . LEU A 85  ? 0.3744 0.2858 0.2499 -0.0548 0.0331  -0.0249 86  LEU A C   
727  O O   . LEU A 85  ? 0.3444 0.2653 0.2331 -0.0506 0.0325  -0.0233 86  LEU A O   
728  C CB  . LEU A 85  ? 0.3383 0.2460 0.2170 -0.0611 0.0497  -0.0324 86  LEU A CB  
729  C CG  . LEU A 85  ? 0.4054 0.3103 0.2845 -0.0664 0.0612  -0.0381 86  LEU A CG  
730  C CD1 . LEU A 85  ? 0.4074 0.3132 0.2950 -0.0650 0.0670  -0.0417 86  LEU A CD1 
731  C CD2 . LEU A 85  ? 0.4030 0.3183 0.2970 -0.0643 0.0653  -0.0397 86  LEU A CD2 
732  N N   . LEU A 86  ? 0.3433 0.2520 0.2107 -0.0540 0.0254  -0.0244 87  LEU A N   
733  C CA  . LEU A 86  ? 0.3328 0.2502 0.2082 -0.0482 0.0167  -0.0226 87  LEU A CA  
734  C C   . LEU A 86  ? 0.3678 0.2823 0.2398 -0.0460 0.0125  -0.0198 87  LEU A C   
735  O O   . LEU A 86  ? 0.3383 0.2622 0.2226 -0.0420 0.0107  -0.0186 87  LEU A O   
736  C CB  . LEU A 86  ? 0.3381 0.2552 0.2068 -0.0482 0.0093  -0.0250 87  LEU A CB  
737  C CG  . LEU A 86  ? 0.3868 0.3158 0.2667 -0.0429 0.0013  -0.0258 87  LEU A CG  
738  C CD1 . LEU A 86  ? 0.3762 0.3162 0.2729 -0.0422 0.0069  -0.0261 87  LEU A CD1 
739  C CD2 . LEU A 86  ? 0.4088 0.3405 0.2837 -0.0427 -0.0070 -0.0302 87  LEU A CD2 
740  N N   . ASP A 87  ? 0.3560 0.2554 0.2093 -0.0493 0.0117  -0.0188 88  ASP A N   
741  C CA  . ASP A 87  ? 0.3571 0.2490 0.2040 -0.0486 0.0096  -0.0163 88  ASP A CA  
742  C C   . ASP A 87  ? 0.3715 0.2727 0.2330 -0.0500 0.0175  -0.0171 88  ASP A C   
743  O O   . ASP A 87  ? 0.3689 0.2750 0.2373 -0.0468 0.0145  -0.0161 88  ASP A O   
744  C CB  . ASP A 87  ? 0.4145 0.2840 0.2347 -0.0543 0.0105  -0.0151 88  ASP A CB  
745  C CG  . ASP A 87  ? 0.5961 0.4540 0.3985 -0.0505 -0.0012 -0.0134 88  ASP A CG  
746  O OD1 . ASP A 87  ? 0.5949 0.4645 0.4090 -0.0429 -0.0105 -0.0141 88  ASP A OD1 
747  O OD2 . ASP A 87  ? 0.6144 0.4521 0.3910 -0.0552 -0.0013 -0.0120 88  ASP A OD2 
748  N N   . PHE A 88  ? 0.3464 0.2510 0.2130 -0.0545 0.0270  -0.0199 89  PHE A N   
749  C CA  . PHE A 88  ? 0.3126 0.2299 0.1960 -0.0545 0.0332  -0.0221 89  PHE A CA  
750  C C   . PHE A 88  ? 0.3104 0.2434 0.2117 -0.0470 0.0283  -0.0204 89  PHE A C   
751  O O   . PHE A 88  ? 0.2895 0.2309 0.1996 -0.0455 0.0277  -0.0206 89  PHE A O   
752  C CB  . PHE A 88  ? 0.3196 0.2405 0.2091 -0.0582 0.0430  -0.0267 89  PHE A CB  
753  C CG  . PHE A 88  ? 0.3097 0.2478 0.2205 -0.0552 0.0467  -0.0297 89  PHE A CG  
754  C CD1 . PHE A 88  ? 0.3384 0.2809 0.2527 -0.0591 0.0503  -0.0329 89  PHE A CD1 
755  C CD2 . PHE A 88  ? 0.3337 0.2829 0.2601 -0.0480 0.0455  -0.0293 89  PHE A CD2 
756  C CE1 . PHE A 88  ? 0.3175 0.2789 0.2528 -0.0555 0.0519  -0.0367 89  PHE A CE1 
757  C CE2 . PHE A 88  ? 0.3558 0.3206 0.3005 -0.0433 0.0464  -0.0316 89  PHE A CE2 
758  C CZ  . PHE A 88  ? 0.3264 0.2991 0.2766 -0.0468 0.0490  -0.0357 89  PHE A CZ  
759  N N   . MET A 89  ? 0.2811 0.2177 0.1866 -0.0435 0.0257  -0.0194 90  MET A N   
760  C CA  . MET A 89  ? 0.2689 0.2171 0.1874 -0.0379 0.0223  -0.0177 90  MET A CA  
761  C C   . MET A 89  ? 0.3137 0.2652 0.2329 -0.0358 0.0161  -0.0164 90  MET A C   
762  O O   . MET A 89  ? 0.3038 0.2650 0.2326 -0.0332 0.0154  -0.0159 90  MET A O   
763  C CB  . MET A 89  ? 0.2768 0.2243 0.1950 -0.0369 0.0208  -0.0176 90  MET A CB  
764  C CG  . MET A 89  ? 0.2972 0.2412 0.2163 -0.0383 0.0274  -0.0192 90  MET A CG  
765  S SD  . MET A 89  ? 0.3480 0.2906 0.2665 -0.0386 0.0267  -0.0198 90  MET A SD  
766  C CE  . MET A 89  ? 0.3581 0.2917 0.2736 -0.0417 0.0355  -0.0229 90  MET A CE  
767  N N   . TYR A 90  ? 0.2787 0.2214 0.1869 -0.0363 0.0111  -0.0163 91  TYR A N   
768  C CA  . TYR A 90  ? 0.2793 0.2236 0.1885 -0.0332 0.0050  -0.0160 91  TYR A CA  
769  C C   . TYR A 90  ? 0.3398 0.2771 0.2433 -0.0353 0.0060  -0.0159 91  TYR A C   
770  O O   . TYR A 90  ? 0.3254 0.2625 0.2297 -0.0326 0.0016  -0.0161 91  TYR A O   
771  C CB  . TYR A 90  ? 0.3033 0.2425 0.2055 -0.0306 -0.0026 -0.0168 91  TYR A CB  
772  C CG  . TYR A 90  ? 0.3134 0.2644 0.2259 -0.0288 -0.0044 -0.0191 91  TYR A CG  
773  C CD1 . TYR A 90  ? 0.3333 0.2842 0.2447 -0.0315 -0.0013 -0.0201 91  TYR A CD1 
774  C CD2 . TYR A 90  ? 0.3172 0.2787 0.2398 -0.0256 -0.0080 -0.0214 91  TYR A CD2 
775  C CE1 . TYR A 90  ? 0.3353 0.2954 0.2548 -0.0317 -0.0014 -0.0231 91  TYR A CE1 
776  C CE2 . TYR A 90  ? 0.3216 0.2934 0.2525 -0.0260 -0.0082 -0.0249 91  TYR A CE2 
777  C CZ  . TYR A 90  ? 0.3495 0.3202 0.2786 -0.0294 -0.0045 -0.0256 91  TYR A CZ  
778  O OH  . TYR A 90  ? 0.3201 0.2997 0.2564 -0.0314 -0.0035 -0.0301 91  TYR A OH  
779  N N   . THR A 91  ? 0.2999 0.2305 0.1972 -0.0407 0.0126  -0.0165 92  THR A N   
780  C CA  . THR A 91  ? 0.3171 0.2383 0.2063 -0.0449 0.0152  -0.0173 92  THR A CA  
781  C C   . THR A 91  ? 0.3408 0.2699 0.2379 -0.0505 0.0240  -0.0209 92  THR A C   
782  O O   . THR A 91  ? 0.3297 0.2542 0.2232 -0.0548 0.0268  -0.0228 92  THR A O   
783  C CB  . THR A 91  ? 0.3773 0.2744 0.2423 -0.0487 0.0149  -0.0157 92  THR A CB  
784  O OG1 . THR A 91  ? 0.3811 0.2740 0.2397 -0.0546 0.0219  -0.0170 92  THR A OG1 
785  C CG2 . THR A 91  ? 0.3907 0.2788 0.2460 -0.0422 0.0042  -0.0130 92  THR A CG2 
786  N N   A SER A 92  ? 0.2941 0.2342 0.2019 -0.0506 0.0285  -0.0228 93  SER A N   
787  N N   B SER A 92  ? 0.2910 0.2307 0.1984 -0.0507 0.0286  -0.0227 93  SER A N   
788  C CA  A SER A 92  ? 0.2863 0.2368 0.2046 -0.0549 0.0366  -0.0281 93  SER A CA  
789  C CA  B SER A 92  ? 0.2838 0.2342 0.2020 -0.0548 0.0366  -0.0281 93  SER A CA  
790  C C   A SER A 92  ? 0.3298 0.2659 0.2337 -0.0646 0.0453  -0.0315 93  SER A C   
791  C C   B SER A 92  ? 0.3428 0.2789 0.2467 -0.0648 0.0453  -0.0316 93  SER A C   
792  O O   A SER A 92  ? 0.3227 0.2679 0.2359 -0.0694 0.0535  -0.0379 93  SER A O   
793  O O   B SER A 92  ? 0.3400 0.2852 0.2529 -0.0700 0.0535  -0.0381 93  SER A O   
794  C CB  A SER A 92  ? 0.2891 0.2523 0.2185 -0.0555 0.0366  -0.0312 93  SER A CB  
795  C CB  B SER A 92  ? 0.2977 0.2628 0.2290 -0.0542 0.0358  -0.0308 93  SER A CB  
796  O OG  A SER A 92  ? 0.2553 0.2293 0.1940 -0.0482 0.0291  -0.0283 93  SER A OG  
797  O OG  B SER A 92  ? 0.3360 0.2910 0.2573 -0.0615 0.0392  -0.0332 93  SER A OG  
798  N N   A ARG A 93  ? 0.3185 0.2323 0.1994 -0.0674 0.0434  -0.0279 94  ARG A N   
799  N N   B ARG A 93  ? 0.3243 0.2382 0.2053 -0.0674 0.0435  -0.0279 94  ARG A N   
800  C CA  A ARG A 93  ? 0.3326 0.2276 0.1933 -0.0777 0.0516  -0.0301 94  ARG A CA  
801  C CA  B ARG A 93  ? 0.3436 0.2377 0.2034 -0.0777 0.0513  -0.0299 94  ARG A CA  
802  C C   A ARG A 93  ? 0.3962 0.2857 0.2495 -0.0787 0.0536  -0.0300 94  ARG A C   
803  C C   B ARG A 93  ? 0.4014 0.2898 0.2534 -0.0790 0.0535  -0.0299 94  ARG A C   
804  O O   A ARG A 93  ? 0.3715 0.2573 0.2198 -0.0727 0.0455  -0.0255 94  ARG A O   
805  O O   B ARG A 93  ? 0.3869 0.2709 0.2332 -0.0731 0.0454  -0.0253 94  ARG A O   
806  C CB  A ARG A 93  ? 0.3847 0.2536 0.2192 -0.0805 0.0481  -0.0258 94  ARG A CB  
807  C CB  B ARG A 93  ? 0.3829 0.2518 0.2176 -0.0793 0.0466  -0.0252 94  ARG A CB  
808  C CG  A ARG A 93  ? 0.4536 0.3242 0.2929 -0.0813 0.0480  -0.0270 94  ARG A CG  
809  C CG  B ARG A 93  ? 0.4714 0.3432 0.3122 -0.0782 0.0447  -0.0256 94  ARG A CG  
810  C CD  A ARG A 93  ? 0.5979 0.4433 0.4145 -0.0786 0.0404  -0.0213 94  ARG A CD  
811  C CD  B ARG A 93  ? 0.5446 0.4059 0.3757 -0.0905 0.0558  -0.0306 94  ARG A CD  
812  N NE  A ARG A 93  ? 0.7476 0.5621 0.5320 -0.0865 0.0444  -0.0193 94  ARG A NE  
813  N NE  B ARG A 93  ? 0.5541 0.4190 0.3919 -0.0904 0.0547  -0.0322 94  ARG A NE  
814  C CZ  A ARG A 93  ? 0.9068 0.7020 0.6735 -0.0978 0.0538  -0.0216 94  ARG A CZ  
815  C CZ  B ARG A 93  ? 0.7108 0.5506 0.5278 -0.0937 0.0545  -0.0300 94  ARG A CZ  
816  N NH1 A ARG A 93  ? 0.7462 0.5520 0.5267 -0.1024 0.0601  -0.0269 94  ARG A NH1 
817  N NH1 B ARG A 93  ? 0.5711 0.4159 0.3962 -0.0941 0.0545  -0.0327 94  ARG A NH1 
818  N NH2 A ARG A 93  ? 0.7499 0.5140 0.4833 -0.1053 0.0574  -0.0189 94  ARG A NH2 
819  N NH2 B ARG A 93  ? 0.5226 0.3305 0.3087 -0.0966 0.0541  -0.0252 94  ARG A NH2 
820  N N   . LEU A 94  ? 0.3654 0.2551 0.2183 -0.0873 0.0651  -0.0363 95  LEU A N   
821  C CA  . LEU A 94  ? 0.3620 0.2467 0.2081 -0.0898 0.0693  -0.0380 95  LEU A CA  
822  C C   . LEU A 94  ? 0.4487 0.3083 0.2645 -0.1020 0.0766  -0.0391 95  LEU A C   
823  O O   . LEU A 94  ? 0.4420 0.2989 0.2548 -0.1123 0.0877  -0.0451 95  LEU A O   
824  C CB  . LEU A 94  ? 0.3585 0.2651 0.2308 -0.0889 0.0774  -0.0457 95  LEU A CB  
825  C CG  . LEU A 94  ? 0.4011 0.3048 0.2710 -0.0904 0.0824  -0.0486 95  LEU A CG  
826  C CD1 . LEU A 94  ? 0.3695 0.2730 0.2400 -0.0811 0.0721  -0.0422 95  LEU A CD1 
827  C CD2 . LEU A 94  ? 0.4155 0.3383 0.3103 -0.0901 0.0921  -0.0581 95  LEU A CD2 
828  N N   . ASN A 95  ? 0.4502 0.2913 0.2423 -0.1016 0.0705  -0.0340 96  ASN A N   
829  C CA  . ASN A 95  ? 0.4886 0.3016 0.2456 -0.1129 0.0760  -0.0338 96  ASN A CA  
830  C C   . ASN A 95  ? 0.5479 0.3635 0.3048 -0.1214 0.0882  -0.0413 96  ASN A C   
831  O O   . ASN A 95  ? 0.5554 0.3637 0.2998 -0.1210 0.0851  -0.0401 96  ASN A O   
832  C CB  . ASN A 95  ? 0.5547 0.3467 0.2850 -0.1076 0.0619  -0.0252 96  ASN A CB  
833  C CG  . ASN A 95  ? 0.8079 0.5667 0.4964 -0.1182 0.0653  -0.0234 96  ASN A CG  
834  O OD1 . ASN A 95  ? 0.7015 0.4474 0.3763 -0.1308 0.0784  -0.0271 96  ASN A OD1 
835  N ND2 . ASN A 95  ? 0.7462 0.4905 0.4126 -0.1139 0.0537  -0.0181 96  ASN A ND2 
836  N N   . LEU A 96  ? 0.4999 0.3287 0.2738 -0.1283 0.1019  -0.0504 97  LEU A N   
837  C CA  . LEU A 96  ? 0.5162 0.3514 0.2962 -0.1358 0.1153  -0.0601 97  LEU A CA  
838  C C   . LEU A 96  ? 0.5859 0.3959 0.3326 -0.1531 0.1278  -0.0639 97  LEU A C   
839  O O   . LEU A 96  ? 0.5831 0.3849 0.3212 -0.1622 0.1350  -0.0663 97  LEU A O   
840  C CB  . LEU A 96  ? 0.5054 0.3714 0.3251 -0.1322 0.1220  -0.0691 97  LEU A CB  
841  C CG  . LEU A 96  ? 0.5736 0.4549 0.4130 -0.1329 0.1322  -0.0794 97  LEU A CG  
842  C CD1 . LEU A 96  ? 0.5786 0.4593 0.4194 -0.1235 0.1242  -0.0745 97  LEU A CD1 
843  C CD2 . LEU A 96  ? 0.5434 0.4550 0.4215 -0.1272 0.1358  -0.0878 97  LEU A CD2 
844  N N   . ARG A 97  ? 0.5634 0.3584 0.2878 -0.1586 0.1302  -0.0643 98  ARG A N   
845  C CA  . ARG A 97  ? 0.6112 0.3778 0.2970 -0.1758 0.1416  -0.0670 98  ARG A CA  
846  C C   . ARG A 97  ? 0.6265 0.3988 0.3156 -0.1837 0.1547  -0.0775 98  ARG A C   
847  O O   . ARG A 97  ? 0.5784 0.3681 0.2896 -0.1741 0.1504  -0.0789 98  ARG A O   
848  C CB  . ARG A 97  ? 0.6751 0.4092 0.3182 -0.1745 0.1281  -0.0549 98  ARG A CB  
849  C CG  . ARG A 97  ? 0.7616 0.4865 0.3987 -0.1660 0.1148  -0.0448 98  ARG A CG  
850  C CD  . ARG A 97  ? 0.9866 0.6811 0.5843 -0.1619 0.0995  -0.0336 98  ARG A CD  
851  N NE  . ARG A 97  ? 1.2557 0.9134 0.8054 -0.1773 0.1076  -0.0329 98  ARG A NE  
852  C CZ  . ARG A 97  ? 1.5426 1.1715 1.0633 -0.1863 0.1128  -0.0299 98  ARG A CZ  
853  N NH1 . ARG A 97  ? 1.4118 1.0046 0.8854 -0.2012 0.1209  -0.0291 98  ARG A NH1 
854  N NH2 . ARG A 97  ? 1.4191 1.0536 0.9560 -0.1813 0.1107  -0.0280 98  ARG A NH2 
855  N N   . GLU A 98  ? 0.6253 0.3816 0.2915 -0.2020 0.1718  -0.0855 99  GLU A N   
856  C CA  . GLU A 98  ? 0.6235 0.3840 0.2913 -0.2111 0.1861  -0.0971 99  GLU A CA  
857  C C   . GLU A 98  ? 0.6842 0.4376 0.3390 -0.2047 0.1754  -0.0916 99  GLU A C   
858  O O   . GLU A 98  ? 0.6798 0.4507 0.3577 -0.2015 0.1803  -0.0993 99  GLU A O   
859  C CB  . GLU A 98  ? 0.6840 0.4199 0.3166 -0.2340 0.2049  -0.1046 99  GLU A CB  
860  C CG  . GLU A 98  ? 0.8204 0.5607 0.4543 -0.2453 0.2220  -0.1185 99  GLU A CG  
861  C CD  . GLU A 98  ? 1.2195 0.9340 0.8154 -0.2698 0.2419  -0.1265 99  GLU A CD  
862  O OE1 . GLU A 98  ? 1.1657 0.8427 0.7115 -0.2780 0.2375  -0.1161 99  GLU A OE1 
863  O OE2 . GLU A 98  ? 1.2149 0.9458 0.8306 -0.2809 0.2622  -0.1437 99  GLU A OE2 
864  N N   . GLY A 99  ? 0.6772 0.4059 0.2968 -0.2022 0.1607  -0.0791 100 GLY A N   
865  C CA  . GLY A 99  ? 0.6993 0.4208 0.3033 -0.1972 0.1491  -0.0743 100 GLY A CA  
866  C C   . GLY A 99  ? 0.6912 0.4377 0.3299 -0.1795 0.1356  -0.0711 100 GLY A C   
867  O O   . GLY A 99  ? 0.6988 0.4459 0.3333 -0.1770 0.1303  -0.0714 100 GLY A O   
868  N N   . ASN A 100 ? 0.6139 0.3806 0.2858 -0.1681 0.1307  -0.0687 101 ASN A N   
869  C CA  . ASN A 100 ? 0.5680 0.3554 0.2691 -0.1524 0.1186  -0.0652 101 ASN A CA  
870  C C   . ASN A 100 ? 0.5740 0.3891 0.3188 -0.1457 0.1262  -0.0723 101 ASN A C   
871  O O   . ASN A 100 ? 0.5470 0.3765 0.3137 -0.1339 0.1181  -0.0698 101 ASN A O   
872  C CB  . ASN A 100 ? 0.5635 0.3481 0.2611 -0.1417 0.1009  -0.0538 101 ASN A CB  
873  C CG  . ASN A 100 ? 0.6615 0.4530 0.3739 -0.1391 0.1022  -0.0521 101 ASN A CG  
874  O OD1 . ASN A 100 ? 0.5184 0.3278 0.2577 -0.1398 0.1126  -0.0591 101 ASN A OD1 
875  N ND2 . ASN A 100 ? 0.5760 0.3545 0.2724 -0.1352 0.0908  -0.0434 101 ASN A ND2 
876  N N   . ILE A 101 ? 0.5291 0.3516 0.2861 -0.1528 0.1409  -0.0812 102 ILE A N   
877  C CA  . ILE A 101 ? 0.5063 0.3562 0.3055 -0.1445 0.1458  -0.0880 102 ILE A CA  
878  C C   . ILE A 101 ? 0.5059 0.3665 0.3247 -0.1373 0.1473  -0.0925 102 ILE A C   
879  O O   . ILE A 101 ? 0.4580 0.3356 0.3055 -0.1239 0.1412  -0.0908 102 ILE A O   
880  C CB  . ILE A 101 ? 0.5564 0.4157 0.3677 -0.1538 0.1615  -0.0996 102 ILE A CB  
881  C CG1 . ILE A 101 ? 0.5342 0.4243 0.3906 -0.1415 0.1616  -0.1053 102 ILE A CG1 
882  C CG2 . ILE A 101 ? 0.5712 0.4202 0.3665 -0.1697 0.1790  -0.1110 102 ILE A CG2 
883  C CD1 . ILE A 101 ? 0.5593 0.4635 0.4310 -0.1466 0.1695  -0.1131 102 ILE A CD1 
884  N N   . MET A 102 ? 0.4996 0.3484 0.3015 -0.1462 0.1553  -0.0982 103 MET A N   
885  C CA  . MET A 102 ? 0.5002 0.3561 0.3191 -0.1403 0.1578  -0.1031 103 MET A CA  
886  C C   . MET A 102 ? 0.5256 0.3816 0.3466 -0.1289 0.1424  -0.0931 103 MET A C   
887  O O   . MET A 102 ? 0.4879 0.3558 0.3347 -0.1180 0.1409  -0.0938 103 MET A O   
888  C CB  . MET A 102 ? 0.5646 0.4075 0.3637 -0.1537 0.1707  -0.1125 103 MET A CB  
889  C CG  . MET A 102 ? 0.6510 0.4964 0.4523 -0.1658 0.1890  -0.1253 103 MET A CG  
890  S SD  . MET A 102 ? 0.7026 0.5784 0.5540 -0.1556 0.1967  -0.1357 103 MET A SD  
891  C CE  . MET A 102 ? 0.6717 0.5540 0.5456 -0.1478 0.2029  -0.1448 103 MET A CE  
892  N N   . ALA A 103 ? 0.5112 0.3539 0.3053 -0.1312 0.1308  -0.0843 104 ALA A N   
893  C CA  . ALA A 103 ? 0.5001 0.3448 0.2962 -0.1221 0.1165  -0.0765 104 ALA A CA  
894  C C   . ALA A 103 ? 0.4959 0.3551 0.3161 -0.1097 0.1083  -0.0702 104 ALA A C   
895  O O   . ALA A 103 ? 0.4617 0.3288 0.2981 -0.1009 0.1033  -0.0679 104 ALA A O   
896  C CB  . ALA A 103 ? 0.5331 0.3629 0.2970 -0.1265 0.1053  -0.0702 104 ALA A CB  
897  N N   . VAL A 104 ? 0.4342 0.2957 0.2550 -0.1100 0.1075  -0.0676 105 VAL A N   
898  C CA  . VAL A 104 ? 0.3951 0.2707 0.2375 -0.0992 0.1001  -0.0624 105 VAL A CA  
899  C C   . VAL A 104 ? 0.4221 0.3136 0.2952 -0.0911 0.1055  -0.0672 105 VAL A C   
900  O O   . VAL A 104 ? 0.3955 0.2945 0.2826 -0.0809 0.0978  -0.0622 105 VAL A O   
901  C CB  . VAL A 104 ? 0.4386 0.3122 0.2739 -0.1028 0.0995  -0.0601 105 VAL A CB  
902  C CG1 . VAL A 104 ? 0.4013 0.2921 0.2615 -0.0928 0.0942  -0.0572 105 VAL A CG1 
903  C CG2 . VAL A 104 ? 0.4624 0.3180 0.2677 -0.1062 0.0900  -0.0528 105 VAL A CG2 
904  N N   A MET A 105 ? 0.4009 0.2969 0.2837 -0.0954 0.1185  -0.0772 106 MET A N   
905  N N   B MET A 105 ? 0.4060 0.3020 0.2888 -0.0954 0.1185  -0.0772 106 MET A N   
906  C CA  A MET A 105 ? 0.3957 0.3064 0.3082 -0.0860 0.1230  -0.0828 106 MET A CA  
907  C CA  B MET A 105 ? 0.4049 0.3157 0.3176 -0.0856 0.1225  -0.0825 106 MET A CA  
908  C C   A MET A 105 ? 0.4458 0.3515 0.3622 -0.0793 0.1207  -0.0811 106 MET A C   
909  C C   B MET A 105 ? 0.4422 0.3477 0.3584 -0.0791 0.1205  -0.0809 106 MET A C   
910  O O   A MET A 105 ? 0.4248 0.3377 0.3589 -0.0673 0.1154  -0.0777 106 MET A O   
911  O O   B MET A 105 ? 0.4115 0.3240 0.3453 -0.0673 0.1152  -0.0775 106 MET A O   
912  C CB  A MET A 105 ? 0.4378 0.3546 0.3601 -0.0926 0.1381  -0.0961 106 MET A CB  
913  C CB  B MET A 105 ? 0.4468 0.3647 0.3709 -0.0914 0.1372  -0.0956 106 MET A CB  
914  C CG  A MET A 105 ? 0.4765 0.4107 0.4322 -0.0805 0.1407  -0.1027 106 MET A CG  
915  C CG  B MET A 105 ? 0.4851 0.4202 0.4425 -0.0786 0.1392  -0.1016 106 MET A CG  
916  S SD  A MET A 105 ? 0.5428 0.4872 0.5141 -0.0877 0.1592  -0.1213 106 MET A SD  
917  S SD  B MET A 105 ? 0.5452 0.4953 0.5222 -0.0847 0.1559  -0.1196 106 MET A SD  
918  C CE  A MET A 105 ? 0.4952 0.4522 0.5005 -0.0686 0.1573  -0.1256 106 MET A CE  
919  C CE  B MET A 105 ? 0.5329 0.4656 0.4940 -0.0949 0.1694  -0.1280 106 MET A CE  
920  N N   . ALA A 106 ? 0.4241 0.3160 0.3218 -0.0875 0.1248  -0.0836 107 ALA A N   
921  C CA  . ALA A 106 ? 0.4348 0.3197 0.3333 -0.0840 0.1244  -0.0834 107 ALA A CA  
922  C C   . ALA A 106 ? 0.4419 0.3271 0.3396 -0.0770 0.1113  -0.0730 107 ALA A C   
923  O O   . ALA A 106 ? 0.4255 0.3105 0.3351 -0.0687 0.1100  -0.0711 107 ALA A O   
924  C CB  . ALA A 106 ? 0.4685 0.3398 0.3442 -0.0963 0.1302  -0.0884 107 ALA A CB  
925  N N   . THR A 107 ? 0.3930 0.2777 0.2765 -0.0801 0.1020  -0.0666 108 THR A N   
926  C CA  . THR A 107 ? 0.3855 0.2730 0.2696 -0.0744 0.0903  -0.0585 108 THR A CA  
927  C C   . THR A 107 ? 0.4013 0.2996 0.3059 -0.0634 0.0869  -0.0542 108 THR A C   
928  O O   . THR A 107 ? 0.3671 0.2654 0.2779 -0.0574 0.0830  -0.0504 108 THR A O   
929  C CB  . THR A 107 ? 0.4454 0.3296 0.3104 -0.0791 0.0810  -0.0540 108 THR A CB  
930  O OG1 . THR A 107 ? 0.4487 0.3219 0.2926 -0.0889 0.0839  -0.0583 108 THR A OG1 
931  C CG2 . THR A 107 ? 0.4374 0.3255 0.3039 -0.0744 0.0702  -0.0487 108 THR A CG2 
932  N N   . ALA A 108 ? 0.3602 0.2673 0.2741 -0.0617 0.0888  -0.0556 109 ALA A N   
933  C CA  . ALA A 108 ? 0.3356 0.2547 0.2683 -0.0514 0.0846  -0.0524 109 ALA A CA  
934  C C   . ALA A 108 ? 0.3762 0.2954 0.3244 -0.0424 0.0883  -0.0548 109 ALA A C   
935  O O   . ALA A 108 ? 0.3575 0.2791 0.3135 -0.0332 0.0822  -0.0493 109 ALA A O   
936  C CB  . ALA A 108 ? 0.3402 0.2700 0.2799 -0.0531 0.0868  -0.0557 109 ALA A CB  
937  N N   . MET A 109 ? 0.3562 0.2702 0.3065 -0.0451 0.0984  -0.0629 110 MET A N   
938  C CA  . MET A 109 ? 0.3476 0.2582 0.3114 -0.0353 0.1016  -0.0651 110 MET A CA  
939  C C   . MET A 109 ? 0.3891 0.2855 0.3430 -0.0336 0.0980  -0.0587 110 MET A C   
940  O O   . MET A 109 ? 0.3918 0.2849 0.3523 -0.0234 0.0941  -0.0539 110 MET A O   
941  C CB  . MET A 109 ? 0.3834 0.2910 0.3517 -0.0393 0.1142  -0.0765 110 MET A CB  
942  C CG  . MET A 109 ? 0.4359 0.3598 0.4197 -0.0395 0.1195  -0.0850 110 MET A CG  
943  S SD  . MET A 109 ? 0.5375 0.4576 0.5223 -0.0487 0.1364  -0.1000 110 MET A SD  
944  C CE  . MET A 109 ? 0.5109 0.4228 0.5117 -0.0342 0.1386  -0.1027 110 MET A CE  
945  N N   . TYR A 110 ? 0.3726 0.2606 0.3094 -0.0440 0.0990  -0.0589 111 TYR A N   
946  C CA  . TYR A 110 ? 0.3684 0.2451 0.2956 -0.0457 0.0970  -0.0552 111 TYR A CA  
947  C C   . TYR A 110 ? 0.4077 0.2892 0.3357 -0.0405 0.0870  -0.0463 111 TYR A C   
948  O O   . TYR A 110 ? 0.3943 0.2670 0.3222 -0.0361 0.0864  -0.0425 111 TYR A O   
949  C CB  . TYR A 110 ? 0.3865 0.2596 0.2968 -0.0583 0.0978  -0.0585 111 TYR A CB  
950  C CG  . TYR A 110 ? 0.3986 0.2656 0.3002 -0.0622 0.0946  -0.0566 111 TYR A CG  
951  C CD1 . TYR A 110 ? 0.4411 0.2948 0.3411 -0.0638 0.1018  -0.0600 111 TYR A CD1 
952  C CD2 . TYR A 110 ? 0.3926 0.2673 0.2878 -0.0652 0.0852  -0.0528 111 TYR A CD2 
953  C CE1 . TYR A 110 ? 0.4315 0.2806 0.3238 -0.0696 0.1005  -0.0600 111 TYR A CE1 
954  C CE2 . TYR A 110 ? 0.3962 0.2689 0.2860 -0.0699 0.0831  -0.0535 111 TYR A CE2 
955  C CZ  . TYR A 110 ? 0.4411 0.3015 0.3294 -0.0729 0.0911  -0.0574 111 TYR A CZ  
956  O OH  . TYR A 110 ? 0.4289 0.2887 0.3123 -0.0796 0.0903  -0.0599 111 TYR A OH  
957  N N   . LEU A 111 ? 0.3538 0.2472 0.2812 -0.0417 0.0801  -0.0432 112 LEU A N   
958  C CA  . LEU A 111 ? 0.3296 0.2292 0.2580 -0.0378 0.0712  -0.0360 112 LEU A CA  
959  C C   . LEU A 111 ? 0.3665 0.2709 0.3073 -0.0267 0.0684  -0.0322 112 LEU A C   
960  O O   . LEU A 111 ? 0.3636 0.2708 0.3040 -0.0233 0.0620  -0.0263 112 LEU A O   
961  C CB  . LEU A 111 ? 0.3151 0.2237 0.2379 -0.0425 0.0649  -0.0348 112 LEU A CB  
962  C CG  . LEU A 111 ? 0.3546 0.2593 0.2632 -0.0514 0.0632  -0.0371 112 LEU A CG  
963  C CD1 . LEU A 111 ? 0.3613 0.2722 0.2640 -0.0531 0.0557  -0.0348 112 LEU A CD1 
964  C CD2 . LEU A 111 ? 0.3813 0.2830 0.2871 -0.0531 0.0613  -0.0365 112 LEU A CD2 
965  N N   . GLN A 112 ? 0.3350 0.2417 0.2871 -0.0212 0.0729  -0.0364 113 GLN A N   
966  C CA  . GLN A 112 ? 0.3397 0.2534 0.3053 -0.0091 0.0688  -0.0342 113 GLN A CA  
967  C C   . GLN A 112 ? 0.3701 0.3004 0.3404 -0.0087 0.0616  -0.0317 113 GLN A C   
968  O O   . GLN A 112 ? 0.3561 0.2886 0.3255 -0.0037 0.0543  -0.0254 113 GLN A O   
969  C CB  . GLN A 112 ? 0.3624 0.2619 0.3238 -0.0012 0.0664  -0.0280 113 GLN A CB  
970  C CG  . GLN A 112 ? 0.3785 0.2589 0.3353 -0.0015 0.0747  -0.0312 113 GLN A CG  
971  C CD  . GLN A 112 ? 0.5253 0.3864 0.4705 0.0019  0.0735  -0.0243 113 GLN A CD  
972  O OE1 . GLN A 112 ? 0.4563 0.3171 0.3999 0.0093  0.0663  -0.0174 113 GLN A OE1 
973  N NE2 . GLN A 112 ? 0.5228 0.3662 0.4575 -0.0046 0.0810  -0.0265 113 GLN A NE2 
974  N N   . MET A 113 ? 0.3312 0.2707 0.3036 -0.0154 0.0645  -0.0370 114 MET A N   
975  C CA  . MET A 113 ? 0.3233 0.2767 0.2993 -0.0171 0.0599  -0.0364 114 MET A CA  
976  C C   . MET A 113 ? 0.3837 0.3507 0.3764 -0.0149 0.0646  -0.0448 114 MET A C   
977  O O   . MET A 113 ? 0.3542 0.3227 0.3455 -0.0236 0.0721  -0.0516 114 MET A O   
978  C CB  . MET A 113 ? 0.3445 0.2930 0.3050 -0.0282 0.0602  -0.0358 114 MET A CB  
979  C CG  . MET A 113 ? 0.3589 0.2988 0.3073 -0.0295 0.0549  -0.0298 114 MET A CG  
980  S SD  . MET A 113 ? 0.4000 0.3341 0.3311 -0.0395 0.0530  -0.0298 114 MET A SD  
981  C CE  . MET A 113 ? 0.3593 0.3037 0.2934 -0.0386 0.0468  -0.0272 114 MET A CE  
982  N N   . GLU A 114 ? 0.3735 0.3496 0.3817 -0.0031 0.0604  -0.0451 115 GLU A N   
983  C CA  . GLU A 114 ? 0.3808 0.3731 0.4104 0.0022  0.0638  -0.0547 115 GLU A CA  
984  C C   . GLU A 114 ? 0.3822 0.3909 0.4189 -0.0065 0.0676  -0.0623 115 GLU A C   
985  O O   . GLU A 114 ? 0.3670 0.3830 0.4144 -0.0103 0.0767  -0.0730 115 GLU A O   
986  C CB  . GLU A 114 ? 0.4101 0.4104 0.4534 0.0181  0.0547  -0.0524 115 GLU A CB  
987  C CG  . GLU A 114 ? 0.5844 0.5647 0.6201 0.0270  0.0530  -0.0461 115 GLU A CG  
988  N N   . HIS A 115 ? 0.3408 0.3542 0.3712 -0.0105 0.0619  -0.0578 116 HIS A N   
989  C CA  . HIS A 115 ? 0.3537 0.3801 0.3891 -0.0198 0.0665  -0.0653 116 HIS A CA  
990  C C   . HIS A 115 ? 0.3799 0.3933 0.3996 -0.0342 0.0771  -0.0689 116 HIS A C   
991  O O   . HIS A 115 ? 0.3864 0.4082 0.4129 -0.0422 0.0863  -0.0792 116 HIS A O   
992  C CB  . HIS A 115 ? 0.3770 0.4094 0.4088 -0.0205 0.0584  -0.0600 116 HIS A CB  
993  C CG  . HIS A 115 ? 0.4309 0.4782 0.4774 -0.0077 0.0485  -0.0583 116 HIS A CG  
994  N ND1 . HIS A 115 ? 0.4618 0.5306 0.5319 -0.0011 0.0482  -0.0679 116 HIS A ND1 
995  C CD2 . HIS A 115 ? 0.4592 0.5025 0.4986 -0.0010 0.0385  -0.0488 116 HIS A CD2 
996  C CE1 . HIS A 115 ? 0.4567 0.5327 0.5317 0.0105  0.0368  -0.0628 116 HIS A CE1 
997  N NE2 . HIS A 115 ? 0.4596 0.5199 0.5154 0.0101  0.0313  -0.0512 116 HIS A NE2 
998  N N   . VAL A 116 ? 0.3202 0.3133 0.3184 -0.0378 0.0759  -0.0612 117 VAL A N   
999  C CA  . VAL A 116 ? 0.3281 0.3060 0.3071 -0.0504 0.0839  -0.0633 117 VAL A CA  
1000 C C   . VAL A 116 ? 0.3955 0.3743 0.3824 -0.0525 0.0950  -0.0731 117 VAL A C   
1001 O O   . VAL A 116 ? 0.3696 0.3471 0.3516 -0.0637 0.1052  -0.0810 117 VAL A O   
1002 C CB  . VAL A 116 ? 0.3757 0.3349 0.3320 -0.0525 0.0783  -0.0541 117 VAL A CB  
1003 C CG1 . VAL A 116 ? 0.3905 0.3339 0.3257 -0.0643 0.0855  -0.0569 117 VAL A CG1 
1004 C CG2 . VAL A 116 ? 0.3712 0.3305 0.3211 -0.0511 0.0686  -0.0466 117 VAL A CG2 
1005 N N   . VAL A 117 ? 0.3525 0.3317 0.3505 -0.0423 0.0938  -0.0730 118 VAL A N   
1006 C CA  . VAL A 117 ? 0.3542 0.3345 0.3625 -0.0424 0.1043  -0.0832 118 VAL A CA  
1007 C C   . VAL A 117 ? 0.4115 0.4127 0.4411 -0.0443 0.1117  -0.0961 118 VAL A C   
1008 O O   . VAL A 117 ? 0.3983 0.3985 0.4258 -0.0550 0.1242  -0.1061 118 VAL A O   
1009 C CB  . VAL A 117 ? 0.3884 0.3644 0.4061 -0.0291 0.1009  -0.0808 118 VAL A CB  
1010 C CG1 . VAL A 117 ? 0.3917 0.3691 0.4223 -0.0283 0.1122  -0.0928 118 VAL A CG1 
1011 C CG2 . VAL A 117 ? 0.3852 0.3413 0.3816 -0.0308 0.0964  -0.0708 118 VAL A CG2 
1012 N N   A ASP A 118 ? 0.3799 0.4001 0.4283 -0.0356 0.1042  -0.0963 119 ASP A N   
1013 N N   B ASP A 118 ? 0.3768 0.3974 0.4266 -0.0346 0.1042  -0.0966 119 ASP A N   
1014 C CA  A ASP A 118 ? 0.3780 0.4229 0.4502 -0.0367 0.1093  -0.1095 119 ASP A CA  
1015 C CA  B ASP A 118 ? 0.3763 0.4221 0.4509 -0.0350 0.1091  -0.1099 119 ASP A CA  
1016 C C   A ASP A 118 ? 0.4183 0.4618 0.4786 -0.0557 0.1206  -0.1163 119 ASP A C   
1017 C C   B ASP A 118 ? 0.4292 0.4751 0.4936 -0.0537 0.1205  -0.1174 119 ASP A C   
1018 O O   A ASP A 118 ? 0.4193 0.4728 0.4914 -0.0629 0.1333  -0.1306 119 ASP A O   
1019 O O   B ASP A 118 ? 0.4331 0.4904 0.5109 -0.0604 0.1329  -0.1320 119 ASP A O   
1020 C CB  A ASP A 118 ? 0.3915 0.4553 0.4808 -0.0247 0.0966  -0.1066 119 ASP A CB  
1021 C CB  B ASP A 118 ? 0.3889 0.4533 0.4799 -0.0232 0.0962  -0.1067 119 ASP A CB  
1022 C CG  A ASP A 118 ? 0.5512 0.6452 0.6692 -0.0244 0.1003  -0.1218 119 ASP A CG  
1023 C CG  B ASP A 118 ? 0.5374 0.6082 0.6459 -0.0035 0.0867  -0.1047 119 ASP A CG  
1024 O OD1 A ASP A 118 ? 0.5841 0.6910 0.7244 -0.0184 0.1057  -0.1336 119 ASP A OD1 
1025 O OD1 B ASP A 118 ? 0.5727 0.6424 0.6922 0.0023  0.0922  -0.1115 119 ASP A OD1 
1026 O OD2 A ASP A 118 ? 0.6233 0.7285 0.7424 -0.0303 0.0981  -0.1230 119 ASP A OD2 
1027 O OD2 B ASP A 118 ? 0.6093 0.6848 0.7192 0.0062  0.0739  -0.0966 119 ASP A OD2 
1028 N N   A THR A 119 ? 0.3659 0.3955 0.4022 -0.0639 0.1166  -0.1068 120 THR A N   
1029 N N   B THR A 119 ? 0.3804 0.4119 0.4203 -0.0624 0.1170  -0.1080 120 THR A N   
1030 C CA  A THR A 119 ? 0.3751 0.3975 0.3951 -0.0820 0.1272  -0.1120 120 THR A CA  
1031 C CA  B THR A 119 ? 0.3902 0.4152 0.4142 -0.0801 0.1269  -0.1128 120 THR A CA  
1032 C C   A THR A 119 ? 0.4288 0.4314 0.4280 -0.0939 0.1392  -0.1153 120 THR A C   
1033 C C   B THR A 119 ? 0.4401 0.4450 0.4426 -0.0927 0.1392  -0.1161 120 THR A C   
1034 O O   A THR A 119 ? 0.4306 0.4316 0.4234 -0.1087 0.1526  -0.1253 120 THR A O   
1035 O O   B THR A 119 ? 0.4454 0.4513 0.4449 -0.1067 0.1529  -0.1272 120 THR A O   
1036 C CB  A THR A 119 ? 0.3932 0.4041 0.3931 -0.0864 0.1198  -0.1017 120 THR A CB  
1037 C CB  B THR A 119 ? 0.4630 0.4775 0.4682 -0.0829 0.1182  -0.1017 120 THR A CB  
1038 O OG1 A THR A 119 ? 0.3966 0.4032 0.3856 -0.1029 0.1312  -0.1092 120 THR A OG1 
1039 O OG1 B THR A 119 ? 0.4298 0.4614 0.4536 -0.0697 0.1060  -0.0976 120 THR A OG1 
1040 C CG2 A THR A 119 ? 0.3399 0.3246 0.3112 -0.0857 0.1124  -0.0878 120 THR A CG2 
1041 C CG2 B THR A 119 ? 0.4654 0.4770 0.4601 -0.0991 0.1278  -0.1081 120 THR A CG2 
1042 N N   . CYS A 120 ? 0.3960 0.3830 0.3830 -0.0886 0.1349  -0.1077 121 CYS A N   
1043 C CA  . CYS A 120 ? 0.4166 0.3850 0.3828 -0.0995 0.1452  -0.1109 121 CYS A CA  
1044 C C   . CYS A 120 ? 0.4824 0.4650 0.4698 -0.1021 0.1593  -0.1273 121 CYS A C   
1045 O O   . CYS A 120 ? 0.4679 0.4432 0.4423 -0.1177 0.1734  -0.1362 121 CYS A O   
1046 C CB  . CYS A 120 ? 0.4182 0.3710 0.3712 -0.0928 0.1371  -0.1009 121 CYS A CB  
1047 S SG  . CYS A 120 ? 0.4648 0.3982 0.3876 -0.0940 0.1235  -0.0850 121 CYS A SG  
1048 N N   A ARG A 121 ? 0.4411 0.4435 0.4609 -0.0866 0.1556  -0.1317 122 ARG A N   
1049 N N   B ARG A 121 ? 0.4463 0.4484 0.4659 -0.0867 0.1558  -0.1318 122 ARG A N   
1050 C CA  A ARG A 121 ? 0.4449 0.4650 0.4921 -0.0847 0.1671  -0.1485 122 ARG A CA  
1051 C CA  B ARG A 121 ? 0.4526 0.4719 0.4987 -0.0855 0.1677  -0.1487 122 ARG A CA  
1052 C C   A ARG A 121 ? 0.4872 0.5248 0.5457 -0.0973 0.1792  -0.1632 122 ARG A C   
1053 C C   B ARG A 121 ? 0.4897 0.5273 0.5481 -0.0976 0.1794  -0.1633 122 ARG A C   
1054 O O   A ARG A 121 ? 0.4901 0.5305 0.5520 -0.1083 0.1953  -0.1777 122 ARG A O   
1055 O O   B ARG A 121 ? 0.4916 0.5322 0.5535 -0.1086 0.1956  -0.1780 122 ARG A O   
1056 C CB  A ARG A 121 ? 0.4411 0.4791 0.5202 -0.0630 0.1568  -0.1486 122 ARG A CB  
1057 C CB  B ARG A 121 ? 0.4619 0.4976 0.5392 -0.0639 0.1582  -0.1490 122 ARG A CB  
1058 C CG  A ARG A 121 ? 0.6019 0.6219 0.6725 -0.0519 0.1494  -0.1381 122 ARG A CG  
1059 C CG  B ARG A 121 ? 0.6539 0.6716 0.7238 -0.0554 0.1555  -0.1428 122 ARG A CG  
1060 C CD  A ARG A 121 ? 0.7518 0.7848 0.8520 -0.0318 0.1437  -0.1416 122 ARG A CD  
1061 C CD  B ARG A 121 ? 0.7904 0.8219 0.8918 -0.0365 0.1523  -0.1489 122 ARG A CD  
1062 N NE  A ARG A 121 ? 0.8228 0.8352 0.9111 -0.0218 0.1357  -0.1294 122 ARG A NE  
1063 N NE  B ARG A 121 ? 0.8447 0.8842 0.9564 -0.0202 0.1356  -0.1386 122 ARG A NE  
1064 C CZ  A ARG A 121 ? 0.9678 0.9634 1.0489 -0.0226 0.1428  -0.1316 122 ARG A CZ  
1065 C CZ  B ARG A 121 ? 0.9769 1.0015 1.0817 -0.0077 0.1252  -0.1265 122 ARG A CZ  
1066 N NH1 A ARG A 121 ? 0.8523 0.8495 0.9368 -0.0325 0.1579  -0.1456 122 ARG A NH1 
1067 N NH1 B ARG A 121 ? 0.7873 0.7895 0.8772 -0.0093 0.1297  -0.1235 122 ARG A NH1 
1068 N NH2 A ARG A 121 ? 0.7448 0.7215 0.8144 -0.0149 0.1358  -0.1207 122 ARG A NH2 
1069 N NH2 B ARG A 121 ? 0.7815 0.8127 0.8929 0.0054  0.1109  -0.1178 122 ARG A NH2 
1070 N N   . LYS A 122 ? 0.4329 0.4818 0.4963 -0.0971 0.1723  -0.1601 123 LYS A N   
1071 C CA  . LYS A 122 ? 0.4419 0.5081 0.5160 -0.1100 0.1831  -0.1740 123 LYS A CA  
1072 C C   . LYS A 122 ? 0.5021 0.5442 0.5410 -0.1334 0.1974  -0.1755 123 LYS A C   
1073 O O   . LYS A 122 ? 0.4994 0.5501 0.5449 -0.1476 0.2146  -0.1922 123 LYS A O   
1074 C CB  . LYS A 122 ? 0.4576 0.5401 0.5440 -0.1036 0.1712  -0.1696 123 LYS A CB  
1075 C CG  . LYS A 122 ? 0.6673 0.7785 0.7915 -0.0822 0.1595  -0.1729 123 LYS A CG  
1076 C CD  . LYS A 122 ? 0.8064 0.9336 0.9407 -0.0759 0.1469  -0.1686 123 LYS A CD  
1077 C CE  . LYS A 122 ? 0.9634 1.1139 1.1290 -0.0534 0.1332  -0.1695 123 LYS A CE  
1078 N NZ  . LYS A 122 ? 1.1074 1.2887 1.2970 -0.0505 0.1274  -0.1776 123 LYS A NZ  
1079 N N   . PHE A 123 ? 0.4582 0.4693 0.4591 -0.1374 0.1903  -0.1588 124 PHE A N   
1080 C CA  . PHE A 123 ? 0.4870 0.4693 0.4481 -0.1578 0.2012  -0.1576 124 PHE A CA  
1081 C C   . PHE A 123 ? 0.5577 0.5299 0.5086 -0.1673 0.2154  -0.1666 124 PHE A C   
1082 O O   . PHE A 123 ? 0.5599 0.5219 0.4930 -0.1868 0.2320  -0.1761 124 PHE A O   
1083 C CB  . PHE A 123 ? 0.5084 0.4621 0.4344 -0.1561 0.1875  -0.1381 124 PHE A CB  
1084 C CG  . PHE A 123 ? 0.5303 0.4823 0.4505 -0.1574 0.1806  -0.1316 124 PHE A CG  
1085 C CD1 . PHE A 123 ? 0.5484 0.5291 0.5019 -0.1472 0.1742  -0.1348 124 PHE A CD1 
1086 C CD2 . PHE A 123 ? 0.5895 0.5100 0.4697 -0.1674 0.1792  -0.1217 124 PHE A CD2 
1087 C CE1 . PHE A 123 ? 0.5638 0.5425 0.5115 -0.1490 0.1684  -0.1296 124 PHE A CE1 
1088 C CE2 . PHE A 123 ? 0.6162 0.5333 0.4911 -0.1679 0.1730  -0.1161 124 PHE A CE2 
1089 C CZ  . PHE A 123 ? 0.5651 0.5117 0.4741 -0.1594 0.1683  -0.1204 124 PHE A CZ  
1090 N N   . ILE A 124 ? 0.5051 0.4799 0.4672 -0.1544 0.2103  -0.1646 125 ILE A N   
1091 C CA  . ILE A 124 ? 0.5270 0.4940 0.4827 -0.1622 0.2240  -0.1745 125 ILE A CA  
1092 C C   . ILE A 124 ? 0.6009 0.5939 0.5882 -0.1683 0.2417  -0.1971 125 ILE A C   
1093 O O   . ILE A 124 ? 0.6178 0.6014 0.5891 -0.1869 0.2597  -0.2084 125 ILE A O   
1094 C CB  . ILE A 124 ? 0.5550 0.5165 0.5141 -0.1474 0.2142  -0.1669 125 ILE A CB  
1095 C CG1 . ILE A 124 ? 0.5586 0.4923 0.4805 -0.1477 0.2012  -0.1483 125 ILE A CG1 
1096 C CG2 . ILE A 124 ? 0.5862 0.5459 0.5485 -0.1532 0.2295  -0.1806 125 ILE A CG2 
1097 C CD1 . ILE A 124 ? 0.6047 0.5367 0.5334 -0.1314 0.1876  -0.1383 125 ILE A CD1 
1098 N N   . LYS A 125 ? 0.5505 0.5764 0.5816 -0.1532 0.2363  -0.2042 126 LYS A N   
1099 C CA  . LYS A 125 ? 0.5615 0.6187 0.6302 -0.1555 0.2504  -0.2272 126 LYS A CA  
1100 C C   . LYS A 125 ? 0.6208 0.6799 0.6792 -0.1791 0.2671  -0.2392 126 LYS A C   
1101 O O   . LYS A 125 ? 0.6121 0.6840 0.6839 -0.1913 0.2863  -0.2596 126 LYS A O   
1102 C CB  . LYS A 125 ? 0.5775 0.6682 0.6913 -0.1330 0.2371  -0.2301 126 LYS A CB  
1103 N N   . ALA A 126 ? 0.5708 0.6151 0.6040 -0.1863 0.2609  -0.2272 127 ALA A N   
1104 C CA  . ALA A 126 ? 0.5952 0.6347 0.6125 -0.2098 0.2767  -0.2365 127 ALA A CA  
1105 C C   . ALA A 126 ? 0.6996 0.7059 0.6737 -0.2329 0.2944  -0.2390 127 ALA A C   
1106 O O   . ALA A 126 ? 0.7052 0.7135 0.6750 -0.2539 0.3146  -0.2549 127 ALA A O   
1107 C CB  . ALA A 126 ? 0.5948 0.6226 0.5940 -0.2098 0.2644  -0.2216 127 ALA A CB  
1108 N N   . SER A 127 ? 0.6974 0.6732 0.6382 -0.2300 0.2871  -0.2239 128 SER A N   
1109 C CA  . SER A 127 ? 0.7577 0.6988 0.6520 -0.2505 0.3006  -0.2238 128 SER A CA  
1110 C C   . SER A 127 ? 0.8549 0.8037 0.7600 -0.2570 0.3178  -0.2412 128 SER A C   
1111 O O   . SER A 127 ? 0.9060 0.8294 0.7742 -0.2777 0.3332  -0.2455 128 SER A O   
1112 C CB  . SER A 127 ? 0.8306 0.7363 0.6826 -0.2452 0.2838  -0.2005 128 SER A CB  
1113 O OG  . SER A 127 ? 0.9848 0.8672 0.8045 -0.2527 0.2785  -0.1886 128 SER A OG  
1114 N N   . GLU A 128 ? 0.7828 0.7649 0.7367 -0.2398 0.3157  -0.2516 129 GLU A N   
1115 C CA  . GLU A 128 ? 1.0268 1.0181 0.9962 -0.2434 0.3317  -0.2694 129 GLU A CA  
1116 C C   . GLU A 128 ? 1.5620 1.5754 1.5520 -0.2615 0.3565  -0.2960 129 GLU A C   
1117 O O   . GLU A 128 ? 1.1604 1.1683 1.1340 -0.2796 0.3660  -0.2995 129 GLU A O   
1118 C CB  . GLU A 128 ? 1.0133 1.0263 1.0233 -0.2167 0.3192  -0.2694 129 GLU A CB  
1119 C CG  . GLU A 128 ? 1.1059 1.1615 1.1721 -0.2007 0.3154  -0.2817 129 GLU A CG  
1120 C CD  . GLU A 128 ? 1.3476 1.4189 1.4482 -0.1722 0.2994  -0.2776 129 GLU A CD  
1121 O OE1 . GLU A 128 ? 1.2526 1.3011 1.3328 -0.1622 0.2859  -0.2596 129 GLU A OE1 
1122 O OE2 . GLU A 128 ? 1.2384 1.3445 1.3862 -0.1597 0.3002  -0.2930 129 GLU A OE2 
1126 N N   A TRP B 2   ? 0.2232 0.4677 0.2873 -0.0382 -0.0087 -0.0829 1   TRP D N   
1127 N N   B TRP B 2   ? 0.2382 0.4826 0.3022 -0.0382 -0.0087 -0.0829 1   TRP D N   
1128 C CA  A TRP B 2   ? 0.2124 0.4553 0.2756 -0.0376 -0.0085 -0.0844 1   TRP D CA  
1129 C CA  B TRP B 2   ? 0.2346 0.4775 0.2979 -0.0376 -0.0084 -0.0844 1   TRP D CA  
1130 C C   A TRP B 2   ? 0.2709 0.5136 0.3361 -0.0380 -0.0091 -0.0841 1   TRP D C   
1131 C C   B TRP B 2   ? 0.2668 0.5099 0.3322 -0.0381 -0.0090 -0.0841 1   TRP D C   
1132 O O   A TRP B 2   ? 0.2737 0.5158 0.3402 -0.0383 -0.0102 -0.0834 1   TRP D O   
1133 O O   B TRP B 2   ? 0.2583 0.5011 0.3251 -0.0386 -0.0100 -0.0832 1   TRP D O   
1134 C CB  A TRP B 2   ? 0.2035 0.4436 0.2647 -0.0368 -0.0097 -0.0854 1   TRP D CB  
1135 C CB  B TRP B 2   ? 0.2301 0.4702 0.2915 -0.0368 -0.0096 -0.0853 1   TRP D CB  
1136 C CG  A TRP B 2   ? 0.2083 0.4483 0.2668 -0.0365 -0.0091 -0.0866 1   TRP D CG  
1137 C CG  B TRP B 2   ? 0.2469 0.4863 0.3103 -0.0367 -0.0116 -0.0853 1   TRP D CG  
1138 C CD1 A TRP B 2   ? 0.2407 0.4805 0.2988 -0.0365 -0.0099 -0.0867 1   TRP D CD1 
1139 C CD1 B TRP B 2   ? 0.2872 0.5262 0.3526 -0.0368 -0.0130 -0.0854 1   TRP D CD1 
1140 C CD2 A TRP B 2   ? 0.2032 0.4432 0.2593 -0.0361 -0.0075 -0.0883 1   TRP D CD2 
1141 C CD2 B TRP B 2   ? 0.2474 0.4870 0.3122 -0.0362 -0.0121 -0.0856 1   TRP D CD2 
1142 N NE1 A TRP B 2   ? 0.2301 0.4700 0.2849 -0.0361 -0.0090 -0.0889 1   TRP D NE1 
1143 N NE1 B TRP B 2   ? 0.2836 0.5232 0.3525 -0.0365 -0.0143 -0.0862 1   TRP D NE1 
1144 C CE2 A TRP B 2   ? 0.2434 0.4834 0.2968 -0.0359 -0.0073 -0.0899 1   TRP D CE2 
1145 C CE2 B TRP B 2   ? 0.2987 0.5389 0.3667 -0.0360 -0.0136 -0.0864 1   TRP D CE2 
1146 C CE3 A TRP B 2   ? 0.2123 0.4522 0.2688 -0.0360 -0.0061 -0.0885 1   TRP D CE3 
1147 C CE3 B TRP B 2   ? 0.2594 0.4993 0.3238 -0.0358 -0.0115 -0.0854 1   TRP D CE3 
1148 C CZ2 A TRP B 2   ? 0.2361 0.4760 0.2865 -0.0355 -0.0056 -0.0924 1   TRP D CZ2 
1149 C CZ2 B TRP B 2   ? 0.2883 0.5304 0.3587 -0.0352 -0.0140 -0.0875 1   TRP D CZ2 
1150 C CZ3 A TRP B 2   ? 0.2230 0.4628 0.2776 -0.0357 -0.0044 -0.0902 1   TRP D CZ3 
1151 C CZ3 B TRP B 2   ? 0.2792 0.5202 0.3450 -0.0350 -0.0122 -0.0860 1   TRP D CZ3 
1152 C CH2 A TRP B 2   ? 0.2296 0.4694 0.2808 -0.0355 -0.0041 -0.0924 1   TRP D CH2 
1153 C CH2 B TRP B 2   ? 0.2849 0.5273 0.3535 -0.0347 -0.0133 -0.0873 1   TRP D CH2 
1154 N N   . VAL B 3   ? 0.2053 0.4487 0.2714 -0.0379 -0.0084 -0.0849 2   VAL D N   
1155 C CA  . VAL B 3   ? 0.2054 0.4488 0.2731 -0.0381 -0.0091 -0.0854 2   VAL D CA  
1156 C C   . VAL B 3   ? 0.2347 0.4764 0.3023 -0.0369 -0.0091 -0.0856 2   VAL D C   
1157 O O   . VAL B 3   ? 0.2230 0.4641 0.2899 -0.0364 -0.0083 -0.0853 2   VAL D O   
1158 C CB  . VAL B 3   ? 0.2492 0.4969 0.3197 -0.0396 -0.0087 -0.0863 2   VAL D CB  
1159 C CG1 . VAL B 3   ? 0.2490 0.4997 0.3198 -0.0409 -0.0087 -0.0851 2   VAL D CG1 
1160 C CG2 . VAL B 3   ? 0.2392 0.4900 0.3125 -0.0396 -0.0072 -0.0877 2   VAL D CG2 
1161 N N   . ILE B 4   ? 0.2142 0.4556 0.2826 -0.0366 -0.0100 -0.0861 3   ILE D N   
1162 C CA  . ILE B 4   ? 0.2106 0.4511 0.2797 -0.0355 -0.0102 -0.0857 3   ILE D CA  
1163 C C   . ILE B 4   ? 0.2622 0.5044 0.3354 -0.0365 -0.0097 -0.0870 3   ILE D C   
1164 O O   . ILE B 4   ? 0.2597 0.5037 0.3345 -0.0375 -0.0104 -0.0888 3   ILE D O   
1165 C CB  . ILE B 4   ? 0.2349 0.4753 0.3032 -0.0344 -0.0112 -0.0863 3   ILE D CB  
1166 C CG1 . ILE B 4   ? 0.2121 0.4532 0.2787 -0.0335 -0.0116 -0.0862 3   ILE D CG1 
1167 C CG2 . ILE B 4   ? 0.2631 0.5032 0.3325 -0.0331 -0.0115 -0.0853 3   ILE D CG2 
1168 C CD1 . ILE B 4   ? 0.2659 0.5079 0.3313 -0.0329 -0.0116 -0.0847 3   ILE D CD1 
1169 N N   . PRO B 5   ? 0.2546 0.4971 0.3305 -0.0364 -0.0086 -0.0867 4   PRO D N   
1170 C CA  . PRO B 5   ? 0.2580 0.5037 0.3403 -0.0373 -0.0082 -0.0889 4   PRO D CA  
1171 C C   . PRO B 5   ? 0.3045 0.5495 0.3902 -0.0370 -0.0097 -0.0896 4   PRO D C   
1172 O O   . PRO B 5   ? 0.2862 0.5279 0.3696 -0.0356 -0.0104 -0.0875 4   PRO D O   
1173 C CB  . PRO B 5   ? 0.2826 0.5284 0.3675 -0.0369 -0.0062 -0.0885 4   PRO D CB  
1174 C CG  . PRO B 5   ? 0.3351 0.5765 0.4150 -0.0356 -0.0063 -0.0854 4   PRO D CG  
1175 C CD  . PRO B 5   ? 0.2843 0.5249 0.3585 -0.0355 -0.0076 -0.0849 4   PRO D CD  
1176 N N   . ALA B 6   ? 0.2959 0.5451 0.3872 -0.0385 -0.0103 -0.0929 5   ALA D N   
# 
