data_7GUY
# 
_entry.id   7GUY 
# 
_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   7GUY         pdb_00007guy 10.2210/pdb7guy/pdb 
WWPDB D_1001406669 ?            ?                   
# 
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                        7GUY 
_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   304 173 HOH   HOH A . 
F 6 HOH   5   305 106 HOH   HOH A . 
F 6 HOH   6   306 140 HOH   HOH A . 
F 6 HOH   7   307 19  HOH   HOH A . 
F 6 HOH   8   308 94  HOH   HOH A . 
F 6 HOH   9   309 100 HOH   HOH A . 
F 6 HOH   10  310 90  HOH   HOH A . 
F 6 HOH   11  311 29  HOH   HOH A . 
F 6 HOH   12  312 47  HOH   HOH A . 
F 6 HOH   13  313 99  HOH   HOH A . 
F 6 HOH   14  314 202 HOH   HOH A . 
F 6 HOH   15  315 45  HOH   HOH A . 
F 6 HOH   16  316 179 HOH   HOH A . 
F 6 HOH   17  317 40  HOH   HOH A . 
F 6 HOH   18  318 247 HOH   HOH A . 
F 6 HOH   19  319 101 HOH   HOH A . 
F 6 HOH   20  320 75  HOH   HOH A . 
F 6 HOH   21  321 142 HOH   HOH A . 
F 6 HOH   22  322 193 HOH   HOH A . 
F 6 HOH   23  323 37  HOH   HOH A . 
F 6 HOH   24  324 83  HOH   HOH A . 
F 6 HOH   25  325 139 HOH   HOH A . 
F 6 HOH   26  326 87  HOH   HOH A . 
F 6 HOH   27  327 132 HOH   HOH A . 
F 6 HOH   28  328 119 HOH   HOH A . 
F 6 HOH   29  329 84  HOH   HOH A . 
F 6 HOH   30  330 6   HOH   HOH A . 
F 6 HOH   31  331 91  HOH   HOH A . 
F 6 HOH   32  332 237 HOH   HOH A . 
F 6 HOH   33  333 17  HOH   HOH A . 
F 6 HOH   34  334 14  HOH   HOH A . 
F 6 HOH   35  335 42  HOH   HOH A . 
F 6 HOH   36  336 151 HOH   HOH A . 
F 6 HOH   37  337 239 HOH   HOH A . 
F 6 HOH   38  338 27  HOH   HOH A . 
F 6 HOH   39  339 20  HOH   HOH A . 
F 6 HOH   40  340 196 HOH   HOH A . 
F 6 HOH   41  341 117 HOH   HOH A . 
F 6 HOH   42  342 244 HOH   HOH A . 
F 6 HOH   43  343 243 HOH   HOH A . 
F 6 HOH   44  344 50  HOH   HOH A . 
F 6 HOH   45  345 242 HOH   HOH A . 
F 6 HOH   46  346 44  HOH   HOH A . 
F 6 HOH   47  347 5   HOH   HOH A . 
F 6 HOH   48  348 133 HOH   HOH A . 
F 6 HOH   49  349 144 HOH   HOH A . 
F 6 HOH   50  350 15  HOH   HOH A . 
F 6 HOH   51  351 86  HOH   HOH A . 
F 6 HOH   52  352 4   HOH   HOH A . 
F 6 HOH   53  353 89  HOH   HOH A . 
F 6 HOH   54  354 122 HOH   HOH A . 
F 6 HOH   55  355 24  HOH   HOH A . 
F 6 HOH   56  356 124 HOH   HOH A . 
F 6 HOH   57  357 85  HOH   HOH A . 
F 6 HOH   58  358 96  HOH   HOH A . 
F 6 HOH   59  359 175 HOH   HOH A . 
F 6 HOH   60  360 93  HOH   HOH A . 
F 6 HOH   61  361 30  HOH   HOH A . 
F 6 HOH   62  362 145 HOH   HOH A . 
F 6 HOH   63  363 51  HOH   HOH A . 
F 6 HOH   64  364 34  HOH   HOH A . 
F 6 HOH   65  365 141 HOH   HOH A . 
F 6 HOH   66  366 97  HOH   HOH A . 
F 6 HOH   67  367 131 HOH   HOH A . 
F 6 HOH   68  368 245 HOH   HOH A . 
F 6 HOH   69  369 207 HOH   HOH A . 
F 6 HOH   70  370 103 HOH   HOH A . 
F 6 HOH   71  371 186 HOH   HOH A . 
F 6 HOH   72  372 21  HOH   HOH A . 
F 6 HOH   73  373 192 HOH   HOH A . 
F 6 HOH   74  374 12  HOH   HOH A . 
F 6 HOH   75  375 170 HOH   HOH A . 
F 6 HOH   76  376 25  HOH   HOH A . 
F 6 HOH   77  377 108 HOH   HOH A . 
F 6 HOH   78  378 180 HOH   HOH A . 
F 6 HOH   79  379 39  HOH   HOH A . 
F 6 HOH   80  380 76  HOH   HOH A . 
F 6 HOH   81  381 177 HOH   HOH A . 
F 6 HOH   82  382 55  HOH   HOH A . 
F 6 HOH   83  383 229 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 28  HOH   HOH A . 
F 6 HOH   87  387 74  HOH   HOH A . 
F 6 HOH   88  388 16  HOH   HOH A . 
F 6 HOH   89  389 70  HOH   HOH A . 
F 6 HOH   90  390 169 HOH   HOH A . 
F 6 HOH   91  391 69  HOH   HOH A . 
F 6 HOH   92  392 165 HOH   HOH A . 
F 6 HOH   93  393 129 HOH   HOH A . 
F 6 HOH   94  394 191 HOH   HOH A . 
F 6 HOH   95  395 32  HOH   HOH A . 
F 6 HOH   96  396 212 HOH   HOH A . 
F 6 HOH   97  397 174 HOH   HOH A . 
F 6 HOH   98  398 64  HOH   HOH A . 
F 6 HOH   99  399 241 HOH   HOH A . 
F 6 HOH   100 400 22  HOH   HOH A . 
F 6 HOH   101 401 194 HOH   HOH A . 
F 6 HOH   102 402 157 HOH   HOH A . 
F 6 HOH   103 403 92  HOH   HOH A . 
F 6 HOH   104 404 82  HOH   HOH A . 
F 6 HOH   105 405 185 HOH   HOH A . 
F 6 HOH   106 406 205 HOH   HOH A . 
F 6 HOH   107 407 120 HOH   HOH A . 
F 6 HOH   108 408 176 HOH   HOH A . 
F 6 HOH   109 409 43  HOH   HOH A . 
F 6 HOH   110 410 35  HOH   HOH A . 
F 6 HOH   111 411 190 HOH   HOH A . 
F 6 HOH   112 412 60  HOH   HOH A . 
F 6 HOH   113 413 46  HOH   HOH A . 
F 6 HOH   114 414 26  HOH   HOH A . 
F 6 HOH   115 415 67  HOH   HOH A . 
F 6 HOH   116 416 65  HOH   HOH A . 
F 6 HOH   117 417 36  HOH   HOH A . 
F 6 HOH   118 418 110 HOH   HOH A . 
F 6 HOH   119 419 88  HOH   HOH A . 
F 6 HOH   120 420 61  HOH   HOH A . 
F 6 HOH   121 421 204 HOH   HOH A . 
F 6 HOH   122 422 215 HOH   HOH A . 
F 6 HOH   123 423 236 HOH   HOH A . 
F 6 HOH   124 424 223 HOH   HOH A . 
F 6 HOH   125 425 68  HOH   HOH A . 
F 6 HOH   126 426 56  HOH   HOH A . 
F 6 HOH   127 427 57  HOH   HOH A . 
F 6 HOH   128 428 95  HOH   HOH A . 
F 6 HOH   129 429 41  HOH   HOH A . 
F 6 HOH   130 430 135 HOH   HOH A . 
F 6 HOH   131 431 147 HOH   HOH A . 
F 6 HOH   132 432 168 HOH   HOH A . 
F 6 HOH   133 433 214 HOH   HOH A . 
F 6 HOH   134 434 116 HOH   HOH A . 
F 6 HOH   135 435 187 HOH   HOH A . 
F 6 HOH   136 436 227 HOH   HOH A . 
F 6 HOH   137 437 200 HOH   HOH A . 
F 6 HOH   138 438 123 HOH   HOH A . 
F 6 HOH   139 439 248 HOH   HOH A . 
F 6 HOH   140 440 231 HOH   HOH A . 
F 6 HOH   141 441 121 HOH   HOH A . 
F 6 HOH   142 442 228 HOH   HOH A . 
F 6 HOH   143 443 63  HOH   HOH A . 
F 6 HOH   144 444 171 HOH   HOH A . 
F 6 HOH   145 445 71  HOH   HOH A . 
F 6 HOH   146 446 225 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   150 450 238 HOH   HOH A . 
F 6 HOH   151 451 181 HOH   HOH A . 
F 6 HOH   152 452 125 HOH   HOH A . 
F 6 HOH   153 453 114 HOH   HOH A . 
F 6 HOH   154 454 158 HOH   HOH A . 
F 6 HOH   155 455 79  HOH   HOH A . 
F 6 HOH   156 456 235 HOH   HOH A . 
F 6 HOH   157 457 217 HOH   HOH A . 
F 6 HOH   158 458 81  HOH   HOH A . 
F 6 HOH   159 459 246 HOH   HOH A . 
F 6 HOH   160 460 58  HOH   HOH A . 
F 6 HOH   161 461 107 HOH   HOH A . 
F 6 HOH   162 462 216 HOH   HOH A . 
F 6 HOH   163 463 221 HOH   HOH A . 
F 6 HOH   164 464 115 HOH   HOH A . 
F 6 HOH   165 465 230 HOH   HOH A . 
F 6 HOH   166 466 183 HOH   HOH A . 
F 6 HOH   167 467 201 HOH   HOH A . 
F 6 HOH   168 468 188 HOH   HOH A . 
F 6 HOH   169 469 113 HOH   HOH A . 
F 6 HOH   170 470 182 HOH   HOH A . 
F 6 HOH   171 471 213 HOH   HOH A . 
F 6 HOH   172 472 148 HOH   HOH A . 
F 6 HOH   173 473 48  HOH   HOH A . 
F 6 HOH   174 474 206 HOH   HOH A . 
F 6 HOH   175 475 172 HOH   HOH A . 
F 6 HOH   176 476 211 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   209 195 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           7GUY 
_cell.length_a           67.780 
_cell.length_b           67.780 
_cell.length_c           166.860 
_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                         7GUY 
_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          7GUY 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.65 
_exptl_crystal.density_percent_sol   66.32 
_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                     7GUY 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             34.000 
_reflns.d_resolution_high            1.750 
_reflns.number_obs                   23796 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.078 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.500 
_reflns.B_iso_Wilson_estimate        31.590 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.083 
_reflns.pdbx_Rpim_I_all              0.027 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     215583 
_reflns.pdbx_scaling_rejects         952 
_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  ? 11935 1282 ? 1.284 ? ? ? 9.300 ? 1.800  ? ? ? ? ? ? 100.000 1.359 0.438 0.719 ? 
1 2 9.090 34.000 ? 1507  236  ? 0.052 ? ? ? 6.400 ? 27.500 ? ? ? ? ? ? 98.800  0.056 0.022 0.996 ? 
# 
_refine.entry_id                                 7GUY 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.7500 
_refine.ls_d_res_low                             34.0000 
_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                     23731 
_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                          0.1800 
_refine.ls_R_factor_R_work                       0.1780 
_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                 5.1500 
_refine.ls_number_reflns_R_free                  1222 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               36.0000 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.4505 
_refine.aniso_B[2][2]                            -0.4505 
_refine.aniso_B[3][3]                            0.9011 
_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               0.9620 
_refine.correlation_coeff_Fo_to_Fc_free          0.9440 
_refine.overall_SU_R_Cruickshank_DPI             0.0850 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0860 
_refine.pdbx_overall_SU_R_Blow_DPI               0.0980 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.0940 
_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                                125.330 
_refine.B_iso_min                                17.480 
_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                        7GUY 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.220 
_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                        34.0000 
_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           31.17 
_refine_hist.pdbx_B_iso_mean_solvent          53.31 
_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      1628 ?      ? 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           ?    3.350  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    14.570 ? ?      ?            
# 
_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               99.8600 
_refine_ls_shell.number_reflns_R_work             2691 
_refine_ls_shell.R_factor_all                     0.3055 
_refine_ls_shell.R_factor_R_work                  0.3037 
_refine_ls_shell.R_factor_R_free                  0.3440 
_refine_ls_shell.percent_reflns_R_free            4.6400 
_refine_ls_shell.number_reflns_R_free             131 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2822 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUY 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 at 8.75 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUY 
_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 7GUY       7GUY   ? 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 7GUY A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUY D 1 ? 6   ? 7GUY   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 7GUY GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUY PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUY 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         -65   ? 
1 'SSA (A^2)'  13010 ? 
# 
_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 33.8900000000 0.8660254038 
-0.5000000000 0.0000000000 -58.6992018685 0.0000000000 0.0000000000 -1.0000000000 27.8100000000 
# 
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 ? ? ? ? ? ? ? 1.332 ? ? 
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                   7GUY 
_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 62.54 -118.35 
2 1 SER A 39 ? B 37.88 65.66   
3 1 ARG A 40 ? B 75.50 -22.66  
4 1 SER A 93 ? A 75.91 -3.29   
# 
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 375 ? F HOH . 
2 1 A HOH 390 ? F HOH . 
3 1 A HOH 456 ? F HOH . 
4 1 A HOH 465 ? F HOH . 
5 1 A HOH 466 ? F HOH . 
6 1 A HOH 467 ? 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 0.0059  -0.0638 -0.0470 -0.0420 0.0278  -0.0195 1.0538 1.7289  1.9168 
0.4681  -0.3209 1.1312 0.1433 -0.0830 -0.0603 -0.0519 0.1019 0.0907 0.2390  -0.0118 -0.0037 
'X-RAY DIFFRACTION' 2 ? refined 18.9076 -32.4261 1.8469  -0.1330 0.1159  -0.0223 -0.0438 -0.0044 -0.0843 0.7565 -0.4540 0.0000 
-0.1748 0.1249  0.6231 0.0282 -0.0041 -0.0241 -0.0031 0.0076 0.0404 -0.0418 0.0108  -0.0051 
# 
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                    7GUY 
_atom_sites.fract_transf_matrix[1][1]   0.014754 
_atom_sites.fract_transf_matrix[1][2]   0.008518 
_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]   0.017036 
_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]   0.005993 
_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   ? 17.306 -21.268 -4.802 1.00 66.05  ? 6   ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 5   ? 18.225 -22.143 -5.529 1.00 64.97  ? 6   ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 5   ? 17.762 -23.620 -5.484 1.00 64.30  ? 6   ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 5   ? 16.692 -23.921 -4.946 1.00 65.24  ? 6   ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 5   ? 19.657 -21.999 -4.955 1.00 65.85  ? 6   ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 5   ? 20.752 -22.039 -6.010 1.00 80.02  ? 6   ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 5   ? 20.921 -23.104 -6.656 1.00 80.26  ? 6   ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 5   ? 21.445 -21.011 -6.186 1.00 87.65  ? 6   ASP   A OD2 1 
ATOM   9    N  N   . SER   A 1 6   ? 18.564 -24.527 -6.066 1.00 55.15  ? 7   SER   A N   1 
ATOM   10   C  CA  . SER   A 1 6   ? 18.304 -25.964 -6.072 1.00 52.40  ? 7   SER   A CA  1 
ATOM   11   C  C   . SER   A 1 6   ? 19.299 -26.695 -5.119 1.00 48.38  ? 7   SER   A C   1 
ATOM   12   O  O   . SER   A 1 6   ? 19.594 -27.874 -5.314 1.00 47.37  ? 7   SER   A O   1 
ATOM   13   C  CB  . SER   A 1 6   ? 18.391 -26.508 -7.494 1.00 57.79  ? 7   SER   A CB  1 
ATOM   14   O  OG  . SER   A 1 6   ? 19.664 -26.264 -8.067 1.00 68.35  ? 7   SER   A OG  1 
ATOM   15   N  N   . CYS   A 1 7   ? 19.784 -25.997 -4.075 1.00 39.96  ? 8   CYS   A N   1 
ATOM   16   C  CA  . CYS   A 1 7   ? 20.726 -26.565 -3.107 1.00 36.96  ? 8   CYS   A CA  1 
ATOM   17   C  C   . CYS   A 1 7   ? 20.111 -27.727 -2.298 1.00 36.61  ? 8   CYS   A C   1 
ATOM   18   O  O   . CYS   A 1 7   ? 18.886 -27.806 -2.141 1.00 36.36  ? 8   CYS   A O   1 
ATOM   19   C  CB  . CYS   A 1 7   ? 21.235 -25.473 -2.161 1.00 37.64  ? 8   CYS   A CB  1 
ATOM   20   S  SG  . CYS   A 1 7   ? 22.417 -24.305 -2.895 1.00 42.89  ? 8   CYS   A SG  1 
ATOM   21   N  N   . ILE   A 1 8   ? 20.961 -28.625 -1.792 1.00 28.83  ? 9   ILE   A N   1 
ATOM   22   C  CA  . ILE   A 1 8   ? 20.602 -29.625 -0.787 1.00 25.72  ? 9   ILE   A CA  1 
ATOM   23   C  C   . ILE   A 1 8   ? 21.219 -29.089 0.517  1.00 27.27  ? 9   ILE   A C   1 
ATOM   24   O  O   . ILE   A 1 8   ? 22.183 -28.306 0.473  1.00 26.70  ? 9   ILE   A O   1 
ATOM   25   C  CB  . ILE   A 1 8   ? 20.953 -31.103 -1.099 1.00 28.43  ? 9   ILE   A CB  1 
ATOM   26   C  CG1 . ILE   A 1 8   ? 22.486 -31.289 -1.326 1.00 28.20  ? 9   ILE   A CG1 1 
ATOM   27   C  CG2 . ILE   A 1 8   ? 20.112 -31.628 -2.289 1.00 29.49  ? 9   ILE   A CG2 1 
ATOM   28   C  CD1 . ILE   A 1 8   ? 22.964 -32.739 -1.551 1.00 34.61  ? 9   ILE   A CD1 1 
ATOM   29   N  N   A GLN   A 1 9   ? 20.736 -29.532 1.679  0.66 23.06  ? 10  GLN   A N   1 
ATOM   30   N  N   B GLN   A 1 9   ? 20.609 -29.442 1.646  0.34 23.57  ? 10  GLN   A N   1 
ATOM   31   C  CA  A GLN   A 1 9   ? 21.274 -29.040 2.954  0.66 22.06  ? 10  GLN   A CA  1 
ATOM   32   C  CA  B GLN   A 1 9   ? 21.017 -28.949 2.951  0.34 22.51  ? 10  GLN   A CA  1 
ATOM   33   C  C   A GLN   A 1 9   ? 21.618 -30.184 3.904  0.66 25.19  ? 10  GLN   A C   1 
ATOM   34   C  C   B GLN   A 1 9   ? 21.415 -30.080 3.878  0.34 26.09  ? 10  GLN   A C   1 
ATOM   35   O  O   A GLN   A 1 9   ? 20.846 -31.137 4.009  0.66 25.90  ? 10  GLN   A O   1 
ATOM   36   O  O   B GLN   A 1 9   ? 20.718 -31.091 3.957  0.34 26.46  ? 10  GLN   A O   1 
ATOM   37   C  CB  A GLN   A 1 9   ? 20.274 -28.053 3.611  0.66 23.79  ? 10  GLN   A CB  1 
ATOM   38   C  CB  B GLN   A 1 9   ? 19.875 -28.131 3.563  0.34 23.87  ? 10  GLN   A CB  1 
ATOM   39   C  CG  A GLN   A 1 9   ? 20.490 -27.814 5.124  0.66 28.30  ? 10  GLN   A CG  1 
ATOM   40   C  CG  B GLN   A 1 9   ? 20.335 -27.154 4.641  0.34 24.54  ? 10  GLN   A CG  1 
ATOM   41   C  CD  A GLN   A 1 9   ? 20.103 -26.445 5.617  0.66 50.09  ? 10  GLN   A CD  1 
ATOM   42   C  CD  B GLN   A 1 9   ? 19.546 -27.282 5.920  0.34 38.91  ? 10  GLN   A CD  1 
ATOM   43   O  OE1 A GLN   A 1 9   ? 19.632 -25.586 4.868  0.66 42.58  ? 10  GLN   A OE1 1 
ATOM   44   O  OE1 B GLN   A 1 9   ? 18.323 -27.474 5.918  0.34 29.55  ? 10  GLN   A OE1 1 
ATOM   45   N  NE2 A GLN   A 1 9   ? 20.320 -26.202 6.905  0.66 46.50  ? 10  GLN   A NE2 1 
ATOM   46   N  NE2 B GLN   A 1 9   ? 20.233 -27.159 7.047  0.34 35.57  ? 10  GLN   A NE2 1 
ATOM   47   N  N   A PHE   A 1 10  ? 22.758 -30.082 4.604  0.66 23.11  ? 11  PHE   A N   1 
ATOM   48   N  N   B PHE   A 1 10  ? 22.530 -29.900 4.585  0.34 22.89  ? 11  PHE   A N   1 
ATOM   49   C  CA  A PHE   A 1 10  ? 23.129 -31.102 5.580  0.66 21.35  ? 11  PHE   A CA  1 
ATOM   50   C  CA  B PHE   A 1 10  ? 23.031 -30.884 5.536  0.34 21.83  ? 11  PHE   A CA  1 
ATOM   51   C  C   A PHE   A 1 10  ? 22.669 -30.607 6.946  0.66 23.41  ? 11  PHE   A C   1 
ATOM   52   C  C   B PHE   A 1 10  ? 22.544 -30.442 6.893  0.34 24.20  ? 11  PHE   A C   1 
ATOM   53   O  O   A PHE   A 1 10  ? 23.264 -29.678 7.515  0.66 21.91  ? 11  PHE   A O   1 
ATOM   54   O  O   B PHE   A 1 10  ? 22.970 -29.392 7.397  0.34 23.34  ? 11  PHE   A O   1 
ATOM   55   C  CB  A PHE   A 1 10  ? 24.644 -31.422 5.523  0.66 21.84  ? 11  PHE   A CB  1 
ATOM   56   C  CB  B PHE   A 1 10  ? 24.565 -30.990 5.439  0.34 22.91  ? 11  PHE   A CB  1 
ATOM   57   C  CG  A PHE   A 1 10  ? 25.031 -32.626 6.350  0.66 22.82  ? 11  PHE   A CG  1 
ATOM   58   C  CG  B PHE   A 1 10  ? 25.035 -31.771 4.230  0.34 25.01  ? 11  PHE   A CG  1 
ATOM   59   C  CD1 A PHE   A 1 10  ? 24.640 -33.908 5.973  0.66 26.02  ? 11  PHE   A CD1 1 
ATOM   60   C  CD1 B PHE   A 1 10  ? 24.750 -31.332 2.940  0.34 28.57  ? 11  PHE   A CD1 1 
ATOM   61   C  CD2 A PHE   A 1 10  ? 25.826 -32.487 7.486  0.66 23.61  ? 11  PHE   A CD2 1 
ATOM   62   C  CD2 B PHE   A 1 10  ? 25.798 -32.922 4.379  0.34 28.44  ? 11  PHE   A CD2 1 
ATOM   63   C  CE1 A PHE   A 1 10  ? 24.992 -35.022 6.750  0.66 26.81  ? 11  PHE   A CE1 1 
ATOM   64   C  CE1 B PHE   A 1 10  ? 25.188 -32.047 1.824  0.34 29.98  ? 11  PHE   A CE1 1 
ATOM   65   C  CE2 A PHE   A 1 10  ? 26.151 -33.594 8.274  0.66 25.52  ? 11  PHE   A CE2 1 
ATOM   66   C  CE2 B PHE   A 1 10  ? 26.239 -33.638 3.257  0.34 31.94  ? 11  PHE   A CE2 1 
ATOM   67   C  CZ  A PHE   A 1 10  ? 25.740 -34.855 7.899  0.66 24.31  ? 11  PHE   A CZ  1 
ATOM   68   C  CZ  B PHE   A 1 10  ? 25.932 -33.194 1.990  0.34 29.86  ? 11  PHE   A CZ  1 
ATOM   69   N  N   . THR   A 1 11  ? 21.578 -31.195 7.447  1.00 20.93  ? 12  THR   A N   1 
ATOM   70   C  CA  . THR   A 1 11  ? 20.923 -30.818 8.719  1.00 21.52  ? 12  THR   A CA  1 
ATOM   71   C  C   . THR   A 1 11  ? 21.877 -30.580 9.906  1.00 24.53  ? 12  THR   A C   1 
ATOM   72   O  O   . THR   A 1 11  ? 21.768 -29.540 10.579 1.00 24.22  ? 12  THR   A O   1 
ATOM   73   C  CB  . THR   A 1 11  ? 19.851 -31.854 9.087  1.00 29.43  ? 12  THR   A CB  1 
ATOM   74   O  OG1 . THR   A 1 11  ? 18.943 -31.981 7.979  1.00 32.41  ? 12  THR   A OG1 1 
ATOM   75   C  CG2 . THR   A 1 11  ? 19.071 -31.465 10.359 1.00 32.40  ? 12  THR   A CG2 1 
ATOM   76   N  N   . ARG   A 1 12  ? 22.815 -31.518 10.129 1.00 21.79  ? 13  ARG   A N   1 
ATOM   77   C  CA  . ARG   A 1 12  ? 23.721 -31.436 11.287 1.00 21.80  ? 13  ARG   A CA  1 
ATOM   78   C  C   . ARG   A 1 12  ? 24.963 -30.539 11.075 1.00 23.26  ? 13  ARG   A C   1 
ATOM   79   O  O   . ARG   A 1 12  ? 25.786 -30.439 11.996 1.00 22.42  ? 13  ARG   A O   1 
ATOM   80   C  CB  . ARG   A 1 12  ? 24.185 -32.852 11.693 1.00 26.32  ? 13  ARG   A CB  1 
ATOM   81   C  CG  . ARG   A 1 12  ? 23.077 -33.811 12.191 1.00 36.83  ? 13  ARG   A CG  1 
ATOM   82   C  CD  . ARG   A 1 12  ? 22.483 -33.396 13.528 1.00 58.21  ? 13  ARG   A CD  1 
ATOM   83   N  NE  . ARG   A 1 12  ? 23.449 -33.462 14.630 1.00 70.72  ? 13  ARG   A NE  1 
ATOM   84   C  CZ  . ARG   A 1 12  ? 23.314 -32.817 15.785 1.00 81.52  ? 13  ARG   A CZ  1 
ATOM   85   N  NH1 . ARG   A 1 12  ? 24.236 -32.938 16.730 1.00 68.89  ? 13  ARG   A NH1 1 
ATOM   86   N  NH2 . ARG   A 1 12  ? 22.266 -32.029 15.997 1.00 64.06  ? 13  ARG   A NH2 1 
ATOM   87   N  N   . HIS   A 1 13  ? 25.117 -29.914 9.893  1.00 20.10  ? 14  HIS   A N   1 
ATOM   88   C  CA  . HIS   A 1 13  ? 26.348 -29.156 9.606  1.00 20.01  ? 14  HIS   A CA  1 
ATOM   89   C  C   . HIS   A 1 13  ? 26.645 -28.050 10.626 1.00 22.32  ? 14  HIS   A C   1 
ATOM   90   O  O   . HIS   A 1 13  ? 27.779 -27.973 11.127 1.00 20.54  ? 14  HIS   A O   1 
ATOM   91   C  CB  . HIS   A 1 13  ? 26.329 -28.576 8.172  1.00 19.77  ? 14  HIS   A CB  1 
ATOM   92   C  CG  . HIS   A 1 13  ? 27.584 -27.813 7.873  1.00 21.60  ? 14  HIS   A CG  1 
ATOM   93   N  ND1 . HIS   A 1 13  ? 28.770 -28.475 7.654  1.00 21.67  ? 14  HIS   A ND1 1 
ATOM   94   C  CD2 . HIS   A 1 13  ? 27.785 -26.481 7.725  1.00 21.70  ? 14  HIS   A CD2 1 
ATOM   95   C  CE1 . HIS   A 1 13  ? 29.673 -27.536 7.402  1.00 21.46  ? 14  HIS   A CE1 1 
ATOM   96   N  NE2 . HIS   A 1 13  ? 29.131 -26.315 7.436  1.00 20.72  ? 14  HIS   A NE2 1 
ATOM   97   N  N   . ALA   A 1 14  ? 25.658 -27.166 10.897 1.00 19.27  ? 15  ALA   A N   1 
ATOM   98   C  CA  . ALA   A 1 14  ? 25.895 -26.046 11.839 1.00 19.50  ? 15  ALA   A CA  1 
ATOM   99   C  C   . ALA   A 1 14  ? 26.312 -26.546 13.244 1.00 21.24  ? 15  ALA   A C   1 
ATOM   100  O  O   . ALA   A 1 14  ? 27.237 -25.989 13.851 1.00 20.01  ? 15  ALA   A O   1 
ATOM   101  C  CB  . ALA   A 1 14  ? 24.657 -25.151 11.909 1.00 20.60  ? 15  ALA   A CB  1 
ATOM   102  N  N   A SER   A 1 15  ? 25.648 -27.602 13.734 0.42 20.52  ? 16  SER   A N   1 
ATOM   103  N  N   B SER   A 1 15  ? 25.648 -27.610 13.732 0.30 19.89  ? 16  SER   A N   1 
ATOM   104  N  N   C SER   A 1 15  ? 25.647 -27.601 13.752 0.28 19.80  ? 16  SER   A N   1 
ATOM   105  C  CA  A SER   A 1 15  ? 25.948 -28.180 15.039 0.42 20.41  ? 16  SER   A CA  1 
ATOM   106  C  CA  B SER   A 1 15  ? 25.930 -28.215 15.035 0.30 19.77  ? 16  SER   A CA  1 
ATOM   107  C  CA  C SER   A 1 15  ? 25.972 -28.153 15.070 0.28 19.64  ? 16  SER   A CA  1 
ATOM   108  C  C   A SER   A 1 15  ? 27.362 -28.761 15.050 0.42 23.60  ? 16  SER   A C   1 
ATOM   109  C  C   B SER   A 1 15  ? 27.338 -28.806 15.065 0.30 23.59  ? 16  SER   A C   1 
ATOM   110  C  C   C SER   A 1 15  ? 27.359 -28.803 15.078 0.28 23.58  ? 16  SER   A C   1 
ATOM   111  O  O   A SER   A 1 15  ? 28.099 -28.552 16.021 0.42 21.21  ? 16  SER   A O   1 
ATOM   112  O  O   B SER   A 1 15  ? 28.047 -28.655 16.066 0.30 21.89  ? 16  SER   A O   1 
ATOM   113  O  O   C SER   A 1 15  ? 28.076 -28.686 16.076 0.28 21.94  ? 16  SER   A O   1 
ATOM   114  C  CB  A SER   A 1 15  ? 24.928 -29.259 15.391 0.42 24.77  ? 16  SER   A CB  1 
ATOM   115  C  CB  B SER   A 1 15  ? 24.905 -29.299 15.352 0.30 23.48  ? 16  SER   A CB  1 
ATOM   116  C  CB  C SER   A 1 15  ? 24.901 -29.134 15.536 0.28 23.42  ? 16  SER   A CB  1 
ATOM   117  O  OG  A SER   A 1 15  ? 25.225 -29.835 16.652 0.42 27.65  ? 16  SER   A OG  1 
ATOM   118  O  OG  B SER   A 1 15  ? 23.601 -28.752 15.441 0.30 25.73  ? 16  SER   A OG  1 
ATOM   119  O  OG  C SER   A 1 15  ? 24.847 -30.276 14.699 0.28 25.86  ? 16  SER   A OG  1 
ATOM   120  N  N   . ASP   A 1 16  ? 27.748 -29.458 13.960 1.00 20.94  ? 17  ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 16  ? 29.082 -30.085 13.823 1.00 21.41  ? 17  ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 16  ? 30.152 -28.996 13.790 1.00 21.82  ? 17  ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 16  ? 31.202 -29.161 14.414 1.00 21.73  ? 17  ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 16  ? 29.162 -30.955 12.554 1.00 23.55  ? 17  ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 16  ? 28.387 -32.272 12.649 1.00 33.62  ? 17  ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 16  ? 27.860 -32.581 13.747 1.00 32.19  ? 17  ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 16  ? 28.298 -32.988 11.620 1.00 36.85  ? 17  ASP   A OD2 1 
ATOM   128  N  N   . VAL   A 1 17  ? 29.882 -27.878 13.076 1.00 18.38  ? 18  VAL   A N   1 
ATOM   129  C  CA  . VAL   A 1 17  ? 30.841 -26.751 13.039 1.00 17.48  ? 18  VAL   A CA  1 
ATOM   130  C  C   . VAL   A 1 17  ? 31.075 -26.227 14.473 1.00 22.21  ? 18  VAL   A C   1 
ATOM   131  O  O   . VAL   A 1 17  ? 32.215 -26.048 14.903 1.00 20.25  ? 18  VAL   A O   1 
ATOM   132  C  CB  . VAL   A 1 17  ? 30.373 -25.613 12.086 1.00 19.56  ? 18  VAL   A CB  1 
ATOM   133  C  CG1 . VAL   A 1 17  ? 31.170 -24.321 12.318 1.00 19.37  ? 18  VAL   A CG1 1 
ATOM   134  C  CG2 . VAL   A 1 17  ? 30.463 -26.049 10.616 1.00 19.73  ? 18  VAL   A CG2 1 
ATOM   135  N  N   . LEU   A 1 18  ? 29.989 -25.974 15.192 1.00 18.88  ? 19  LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 18  ? 30.092 -25.413 16.547 1.00 20.46  ? 19  LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 18  ? 30.814 -26.364 17.509 1.00 20.71  ? 19  LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 18  ? 31.661 -25.909 18.295 1.00 20.31  ? 19  LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 18  ? 28.712 -25.011 17.067 1.00 21.23  ? 19  LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 18  ? 28.725 -24.126 18.330 1.00 24.89  ? 19  LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 18  ? 29.307 -22.746 18.038 1.00 24.69  ? 19  LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 18  ? 27.304 -23.975 18.886 1.00 28.37  ? 19  LEU   A CD2 1 
ATOM   143  N  N   . LEU   A 1 19  ? 30.521 -27.669 17.399 1.00 19.51  ? 20  LEU   A N   1 
ATOM   144  C  CA  . LEU   A 1 19  ? 31.192 -28.703 18.190 1.00 20.69  ? 20  LEU   A CA  1 
ATOM   145  C  C   . LEU   A 1 19  ? 32.712 -28.616 17.922 1.00 23.19  ? 20  LEU   A C   1 
ATOM   146  O  O   . LEU   A 1 19  ? 33.495 -28.602 18.881 1.00 22.91  ? 20  LEU   A O   1 
ATOM   147  C  CB  . LEU   A 1 19  ? 30.667 -30.077 17.793 1.00 22.91  ? 20  LEU   A CB  1 
ATOM   148  C  CG  . LEU   A 1 19  ? 31.240 -31.263 18.567 1.00 31.24  ? 20  LEU   A CG  1 
ATOM   149  C  CD1 . LEU   A 1 19  ? 30.825 -31.193 20.043 1.00 33.48  ? 20  LEU   A CD1 1 
ATOM   150  C  CD2 . LEU   A 1 19  ? 30.706 -32.567 17.994 1.00 35.49  ? 20  LEU   A CD2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 33.114 -28.466 16.643 1.00 20.05  ? 21  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 34.543 -28.367 16.329 1.00 18.89  ? 21  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 35.167 -27.067 16.836 1.00 21.15  ? 21  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 36.306 -27.068 17.296 1.00 21.69  ? 21  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 34.798 -28.593 14.845 1.00 20.53  ? 21  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.748 -30.057 14.461 1.00 29.23  ? 21  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.952 -30.959 15.294 1.00 27.83  ? 21  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.475 -30.327 13.182 1.00 26.20  ? 21  ASN   A ND2 1 
ATOM   159  N  N   . LEU   A 1 21  ? 34.427 -25.960 16.768 1.00 20.50  ? 22  LEU   A N   1 
ATOM   160  C  CA  . LEU   A 1 21  ? 34.943 -24.690 17.291 1.00 19.77  ? 22  LEU   A CA  1 
ATOM   161  C  C   . LEU   A 1 21  ? 35.153 -24.827 18.803 1.00 21.89  ? 22  LEU   A C   1 
ATOM   162  O  O   . LEU   A 1 21  ? 36.121 -24.279 19.340 1.00 21.36  ? 22  LEU   A O   1 
ATOM   163  C  CB  . LEU   A 1 21  ? 33.977 -23.542 16.984 1.00 19.66  ? 22  LEU   A CB  1 
ATOM   164  C  CG  . LEU   A 1 21  ? 33.829 -23.203 15.482 1.00 21.84  ? 22  LEU   A CG  1 
ATOM   165  C  CD1 . LEU   A 1 21  ? 32.745 -22.134 15.277 1.00 23.30  ? 22  LEU   A CD1 1 
ATOM   166  C  CD2 . LEU   A 1 21  ? 35.181 -22.778 14.853 1.00 24.52  ? 22  LEU   A CD2 1 
ATOM   167  N  N   . ASN   A 1 22  ? 34.226 -25.524 19.498 1.00 19.38  ? 23  ASN   A N   1 
ATOM   168  C  CA  . ASN   A 1 22  ? 34.380 -25.743 20.951 1.00 20.62  ? 23  ASN   A CA  1 
ATOM   169  C  C   . ASN   A 1 22  ? 35.617 -26.623 21.252 1.00 24.68  ? 23  ASN   A C   1 
ATOM   170  O  O   . ASN   A 1 22  ? 36.325 -26.371 22.231 1.00 24.95  ? 23  ASN   A O   1 
ATOM   171  C  CB  . ASN   A 1 22  ? 33.125 -26.354 21.566 1.00 22.93  ? 23  ASN   A CB  1 
ATOM   172  C  CG  . ASN   A 1 22  ? 33.136 -26.227 23.078 1.00 29.34  ? 23  ASN   A CG  1 
ATOM   173  O  OD1 . ASN   A 1 22  ? 33.652 -25.255 23.643 1.00 26.89  ? 23  ASN   A OD1 1 
ATOM   174  N  ND2 . ASN   A 1 22  ? 32.582 -27.210 23.746 1.00 31.50  ? 23  ASN   A ND2 1 
ATOM   175  N  N   . ARG   A 1 23  ? 35.894 -27.620 20.393 1.00 22.62  ? 24  ARG   A N   1 
ATOM   176  C  CA  . ARG   A 1 23  ? 37.084 -28.479 20.509 1.00 23.19  ? 24  ARG   A CA  1 
ATOM   177  C  C   . ARG   A 1 23  ? 38.348 -27.633 20.366 1.00 27.59  ? 24  ARG   A C   1 
ATOM   178  O  O   . ARG   A 1 23  ? 39.296 -27.820 21.132 1.00 27.03  ? 24  ARG   A O   1 
ATOM   179  C  CB  . ARG   A 1 23  ? 37.076 -29.594 19.452 1.00 22.63  ? 24  ARG   A CB  1 
ATOM   180  C  CG  . ARG   A 1 23  ? 36.069 -30.695 19.777 1.00 26.58  ? 24  ARG   A CG  1 
ATOM   181  C  CD  . ARG   A 1 23  ? 35.874 -31.635 18.596 1.00 28.14  ? 24  ARG   A CD  1 
ATOM   182  N  NE  . ARG   A 1 23  ? 35.026 -32.765 18.972 1.00 35.75  ? 24  ARG   A NE  1 
ATOM   183  C  CZ  . ARG   A 1 23  ? 34.365 -33.532 18.113 1.00 52.42  ? 24  ARG   A CZ  1 
ATOM   184  N  NH1 . ARG   A 1 23  ? 34.402 -33.269 16.811 1.00 40.21  ? 24  ARG   A NH1 1 
ATOM   185  N  NH2 . ARG   A 1 23  ? 33.646 -34.553 18.549 1.00 45.08  ? 24  ARG   A NH2 1 
ATOM   186  N  N   . LEU   A 1 24  ? 38.348 -26.665 19.422 1.00 23.09  ? 25  LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 24  ? 39.500 -25.768 19.258 1.00 23.48  ? 25  LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 24  ? 39.654 -24.911 20.515 1.00 27.55  ? 25  LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 24  ? 40.779 -24.726 21.006 1.00 27.82  ? 25  LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 24  ? 39.321 -24.853 18.051 1.00 23.18  ? 25  LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 24  ? 39.309 -25.533 16.669 1.00 27.95  ? 25  LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 24  ? 39.182 -24.484 15.569 1.00 28.10  ? 25  LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 24  ? 40.550 -26.415 16.473 1.00 29.05  ? 25  LEU   A CD2 1 
ATOM   194  N  N   . ARG   A 1 25  ? 38.515 -24.409 21.058 1.00 24.16  ? 26  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 25  ? 38.569 -23.622 22.291 1.00 24.75  ? 26  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 25  ? 39.188 -24.432 23.465 1.00 29.07  ? 26  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 25  ? 40.071 -23.913 24.164 1.00 29.34  ? 26  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 25  ? 37.175 -23.101 22.670 1.00 24.47  ? 26  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 25  ? 37.272 -22.267 23.952 1.00 27.05  ? 26  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 25  ? 35.985 -21.603 24.312 1.00 32.90  ? 26  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 25  ? 34.968 -22.565 24.707 1.00 30.83  ? 26  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 25  ? 34.351 -22.579 25.883 1.00 40.75  ? 26  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 25  ? 34.708 -21.727 26.841 1.00 33.11  ? 26  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 25  ? 33.396 -23.458 26.122 1.00 31.58  ? 26  ARG   A NH2 1 
ATOM   205  N  N   A SER   A 1 26  ? 38.726 -25.676 23.669 0.39 26.82  ? 27  SER   A N   1 
ATOM   206  N  N   B SER   A 1 26  ? 38.729 -25.687 23.651 0.28 26.46  ? 27  SER   A N   1 
ATOM   207  N  N   C SER   A 1 26  ? 38.726 -25.679 23.666 0.33 26.86  ? 27  SER   A N   1 
ATOM   208  C  CA  A SER   A 1 26  ? 39.196 -26.558 24.745 0.39 28.06  ? 27  SER   A CA  1 
ATOM   209  C  CA  B SER   A 1 26  ? 39.178 -26.624 24.691 0.28 27.57  ? 27  SER   A CA  1 
ATOM   210  C  CA  C SER   A 1 26  ? 39.191 -26.576 24.732 0.33 28.15  ? 27  SER   A CA  1 
ATOM   211  C  C   A SER   A 1 26  ? 40.707 -26.830 24.671 0.39 34.07  ? 27  SER   A C   1 
ATOM   212  C  C   B SER   A 1 26  ? 40.691 -26.837 24.658 0.28 33.65  ? 27  SER   A C   1 
ATOM   213  C  C   C SER   A 1 26  ? 40.704 -26.831 24.666 0.33 33.99  ? 27  SER   A C   1 
ATOM   214  O  O   A SER   A 1 26  ? 41.361 -26.937 25.712 0.39 35.21  ? 27  SER   A O   1 
ATOM   215  O  O   B SER   A 1 26  ? 41.325 -26.934 25.711 0.28 34.66  ? 27  SER   A O   1 
ATOM   216  O  O   C SER   A 1 26  ? 41.351 -26.938 25.711 0.33 35.05  ? 27  SER   A O   1 
ATOM   217  C  CB  A SER   A 1 26  ? 38.410 -27.864 24.753 0.39 31.12  ? 27  SER   A CB  1 
ATOM   218  C  CB  B SER   A 1 26  ? 38.492 -27.975 24.513 0.28 30.35  ? 27  SER   A CB  1 
ATOM   219  C  CB  C SER   A 1 26  ? 38.433 -27.897 24.683 0.33 31.53  ? 27  SER   A CB  1 
ATOM   220  O  OG  A SER   A 1 26  ? 38.730 -28.697 23.651 0.39 37.01  ? 27  SER   A OG  1 
ATOM   221  O  OG  B SER   A 1 26  ? 37.122 -27.935 24.868 0.28 35.43  ? 27  SER   A OG  1 
ATOM   222  O  OG  C SER   A 1 26  ? 38.826 -28.759 25.739 0.33 40.19  ? 27  SER   A OG  1 
ATOM   223  N  N   . ARG   A 1 27  ? 41.260 -26.909 23.444 1.00 30.04  ? 28  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 27  ? 42.689 -27.149 23.219 1.00 31.46  ? 28  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 27  ? 43.475 -25.852 23.021 1.00 33.94  ? 28  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 27  ? 44.681 -25.897 22.754 1.00 34.80  ? 28  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 27  ? 42.851 -28.109 22.035 1.00 33.19  ? 28  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 27  ? 42.145 -29.445 22.263 1.00 39.51  ? 28  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 27  ? 42.100 -30.287 21.009 1.00 45.19  ? 28  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 27  ? 43.449 -30.607 20.542 1.00 58.21  ? 28  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 27  ? 43.759 -30.821 19.270 1.00 72.40  ? 28  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 27  ? 45.011 -31.083 18.922 1.00 60.24  ? 28  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 27  ? 42.828 -30.741 18.333 1.00 57.71  ? 28  ARG   A NH2 1 
ATOM   234  N  N   . ASP   A 1 28  ? 42.797 -24.700 23.171 1.00 28.03  ? 29  ASP   A N   1 
ATOM   235  C  CA  . ASP   A 1 28  ? 43.358 -23.355 23.025 1.00 29.08  ? 29  ASP   A CA  1 
ATOM   236  C  C   . ASP   A 1 28  ? 43.981 -23.118 21.619 1.00 33.56  ? 29  ASP   A C   1 
ATOM   237  O  O   . ASP   A 1 28  ? 45.024 -22.472 21.479 1.00 35.89  ? 29  ASP   A O   1 
ATOM   238  C  CB  . ASP   A 1 28  ? 44.351 -23.043 24.176 1.00 32.58  ? 29  ASP   A CB  1 
ATOM   239  C  CG  . ASP   A 1 28  ? 44.680 -21.572 24.321 1.00 42.06  ? 29  ASP   A CG  1 
ATOM   240  O  OD1 . ASP   A 1 28  ? 43.765 -20.737 24.126 1.00 41.44  ? 29  ASP   A OD1 1 
ATOM   241  O  OD2 . ASP   A 1 28  ? 45.848 -21.253 24.629 1.00 48.08  ? 29  ASP   A OD2 1 
ATOM   242  N  N   . ILE   A 1 29  ? 43.345 -23.673 20.591 1.00 26.36  ? 30  ILE   A N   1 
ATOM   243  C  CA  . ILE   A 1 29  ? 43.821 -23.570 19.210 1.00 26.30  ? 30  ILE   A CA  1 
ATOM   244  C  C   . ILE   A 1 29  ? 43.225 -22.362 18.499 1.00 28.63  ? 30  ILE   A C   1 
ATOM   245  O  O   . ILE   A 1 29  ? 42.000 -22.241 18.394 1.00 25.22  ? 30  ILE   A O   1 
ATOM   246  C  CB  . ILE   A 1 29  ? 43.585 -24.885 18.428 1.00 29.43  ? 30  ILE   A CB  1 
ATOM   247  C  CG1 . ILE   A 1 29  ? 44.377 -26.061 19.067 1.00 31.64  ? 30  ILE   A CG1 1 
ATOM   248  C  CG2 . ILE   A 1 29  ? 43.914 -24.707 16.913 1.00 29.65  ? 30  ILE   A CG2 1 
ATOM   249  C  CD1 . ILE   A 1 29  ? 43.946 -27.442 18.542 1.00 36.13  ? 30  ILE   A CD1 1 
ATOM   250  N  N   . LEU   A 1 30  ? 44.112 -21.469 18.004 1.00 27.59  ? 31  LEU   A N   1 
ATOM   251  C  CA  . LEU   A 1 30  ? 43.758 -20.271 17.231 1.00 28.15  ? 31  LEU   A CA  1 
ATOM   252  C  C   . LEU   A 1 30  ? 42.861 -19.271 17.988 1.00 29.32  ? 31  LEU   A C   1 
ATOM   253  O  O   . LEU   A 1 30  ? 42.268 -18.389 17.370 1.00 26.81  ? 31  LEU   A O   1 
ATOM   254  C  CB  . LEU   A 1 30  ? 43.184 -20.596 15.846 1.00 29.01  ? 31  LEU   A CB  1 
ATOM   255  C  CG  . LEU   A 1 30  ? 44.219 -21.151 14.821 1.00 36.63  ? 31  LEU   A CG  1 
ATOM   256  C  CD1 . LEU   A 1 30  ? 43.588 -21.302 13.476 1.00 37.63  ? 31  LEU   A CD1 1 
ATOM   257  C  CD2 . LEU   A 1 30  ? 45.415 -20.259 14.680 1.00 43.14  ? 31  LEU   A CD2 1 
ATOM   258  N  N   . THR   A 1 31  ? 42.848 -19.346 19.325 1.00 26.26  ? 32  THR   A N   1 
ATOM   259  C  CA  . THR   A 1 31  ? 42.169 -18.341 20.151 1.00 25.49  ? 32  THR   A CA  1 
ATOM   260  C  C   . THR   A 1 31  ? 42.980 -17.054 19.960 1.00 31.33  ? 32  THR   A C   1 
ATOM   261  O  O   . THR   A 1 31  ? 44.209 -17.106 19.804 1.00 31.45  ? 32  THR   A O   1 
ATOM   262  C  CB  . THR   A 1 31  ? 42.087 -18.785 21.616 1.00 29.81  ? 32  THR   A CB  1 
ATOM   263  O  OG1 . THR   A 1 31  ? 43.406 -19.103 22.058 1.00 33.06  ? 32  THR   A OG1 1 
ATOM   264  C  CG2 . THR   A 1 31  ? 41.144 -19.999 21.808 1.00 28.78  ? 32  THR   A CG2 1 
ATOM   265  N  N   . ASP   A 1 32  ? 42.294 -15.925 19.835 1.00 27.34  ? 33  ASP   A N   1 
ATOM   266  C  CA  . ASP   A 1 32  ? 42.977 -14.677 19.500 1.00 27.44  ? 33  ASP   A CA  1 
ATOM   267  C  C   . ASP   A 1 32  ? 42.636 -13.526 20.409 1.00 29.76  ? 33  ASP   A C   1 
ATOM   268  O  O   . ASP   A 1 32  ? 42.991 -12.386 20.103 1.00 29.74  ? 33  ASP   A O   1 
ATOM   269  C  CB  . ASP   A 1 32  ? 42.685 -14.314 18.033 1.00 28.63  ? 33  ASP   A CB  1 
ATOM   270  C  CG  . ASP   A 1 32  ? 41.205 -14.313 17.645 1.00 38.28  ? 33  ASP   A CG  1 
ATOM   271  O  OD1 . ASP   A 1 32  ? 40.344 -14.436 18.551 1.00 33.69  ? 33  ASP   A OD1 1 
ATOM   272  O  OD2 . ASP   A 1 32  ? 40.911 -14.193 16.443 1.00 48.88  ? 33  ASP   A OD2 1 
ATOM   273  N  N   . VAL   A 1 33  ? 41.950 -13.800 21.525 1.00 24.95  ? 34  VAL   A N   1 
ATOM   274  C  CA  . VAL   A 1 33  ? 41.631 -12.748 22.494 1.00 24.61  ? 34  VAL   A CA  1 
ATOM   275  C  C   . VAL   A 1 33  ? 41.473 -13.356 23.883 1.00 28.03  ? 34  VAL   A C   1 
ATOM   276  O  O   . VAL   A 1 33  ? 41.084 -14.533 24.017 1.00 27.26  ? 34  VAL   A O   1 
ATOM   277  C  CB  . VAL   A 1 33  ? 40.354 -11.925 22.058 1.00 26.56  ? 34  VAL   A CB  1 
ATOM   278  C  CG1 . VAL   A 1 33  ? 39.054 -12.734 22.210 1.00 24.42  ? 34  VAL   A CG1 1 
ATOM   279  C  CG2 . VAL   A 1 33  ? 40.244 -10.576 22.798 1.00 27.21  ? 34  VAL   A CG2 1 
ATOM   280  N  N   A VAL   A 1 34  ? 41.775 -12.544 24.905 0.60 25.37  ? 35  VAL   A N   1 
ATOM   281  N  N   B VAL   A 1 34  ? 41.770 -12.565 24.919 0.40 24.54  ? 35  VAL   A N   1 
ATOM   282  C  CA  A VAL   A 1 34  ? 41.563 -12.858 26.312 0.60 25.51  ? 35  VAL   A CA  1 
ATOM   283  C  CA  B VAL   A 1 34  ? 41.519 -12.951 26.300 0.40 24.23  ? 35  VAL   A CA  1 
ATOM   284  C  C   A VAL   A 1 34  ? 40.484 -11.876 26.782 0.60 27.74  ? 35  VAL   A C   1 
ATOM   285  C  C   B VAL   A 1 34  ? 40.559 -11.913 26.897 0.40 27.55  ? 35  VAL   A C   1 
ATOM   286  O  O   A VAL   A 1 34  ? 40.606 -10.668 26.551 0.60 28.09  ? 35  VAL   A O   1 
ATOM   287  O  O   B VAL   A 1 34  ? 40.805 -10.707 26.808 0.40 28.06  ? 35  VAL   A O   1 
ATOM   288  C  CB  A VAL   A 1 34  ? 42.860 -12.721 27.169 0.60 31.03  ? 35  VAL   A CB  1 
ATOM   289  C  CB  B VAL   A 1 34  ? 42.775 -13.275 27.164 0.40 28.88  ? 35  VAL   A CB  1 
ATOM   290  C  CG1 A VAL   A 1 34  ? 42.592 -13.025 28.643 0.60 31.23  ? 35  VAL   A CG1 1 
ATOM   291  C  CG1 B VAL   A 1 34  ? 43.706 -12.079 27.312 0.40 29.22  ? 35  VAL   A CG1 1 
ATOM   292  C  CG2 A VAL   A 1 34  ? 43.968 -13.620 26.641 0.60 31.73  ? 35  VAL   A CG2 1 
ATOM   293  C  CG2 B VAL   A 1 34  ? 42.387 -13.835 28.531 0.40 28.87  ? 35  VAL   A CG2 1 
ATOM   294  N  N   . ILE   A 1 35  ? 39.427 -12.391 27.416 1.00 23.36  ? 36  ILE   A N   1 
ATOM   295  C  CA  . ILE   A 1 35  ? 38.378 -11.569 28.014 1.00 23.28  ? 36  ILE   A CA  1 
ATOM   296  C  C   . ILE   A 1 35  ? 38.665 -11.580 29.507 1.00 28.60  ? 36  ILE   A C   1 
ATOM   297  O  O   . ILE   A 1 35  ? 38.706 -12.662 30.114 1.00 27.95  ? 36  ILE   A O   1 
ATOM   298  C  CB  . ILE   A 1 35  ? 36.935 -12.062 27.702 1.00 24.61  ? 36  ILE   A CB  1 
ATOM   299  C  CG1 . ILE   A 1 35  ? 36.708 -12.228 26.161 1.00 24.32  ? 36  ILE   A CG1 1 
ATOM   300  C  CG2 . ILE   A 1 35  ? 35.910 -11.096 28.326 1.00 26.29  ? 36  ILE   A CG2 1 
ATOM   301  C  CD1 . ILE   A 1 35  ? 36.982 -10.937 25.290 1.00 25.09  ? 36  ILE   A CD1 1 
ATOM   302  N  N   . VAL   A 1 36  ? 38.896 -10.395 30.077 1.00 25.75  ? 37  VAL   A N   1 
ATOM   303  C  CA  . VAL   A 1 36  ? 39.206 -10.255 31.506 1.00 25.92  ? 37  VAL   A CA  1 
ATOM   304  C  C   . VAL   A 1 36  ? 37.949 -9.833  32.262 1.00 31.18  ? 37  VAL   A C   1 
ATOM   305  O  O   . VAL   A 1 36  ? 37.358 -8.788  31.963 1.00 29.47  ? 37  VAL   A O   1 
ATOM   306  C  CB  . VAL   A 1 36  ? 40.418 -9.307  31.760 1.00 30.14  ? 37  VAL   A CB  1 
ATOM   307  C  CG1 . VAL   A 1 36  ? 40.724 -9.191  33.257 1.00 30.65  ? 37  VAL   A CG1 1 
ATOM   308  C  CG2 . VAL   A 1 36  ? 41.660 -9.805  31.017 1.00 30.51  ? 37  VAL   A CG2 1 
ATOM   309  N  N   . VAL   A 1 37  ? 37.557 -10.646 33.260 1.00 28.16  ? 38  VAL   A N   1 
ATOM   310  C  CA  . VAL   A 1 37  ? 36.365 -10.429 34.077 1.00 27.82  ? 38  VAL   A CA  1 
ATOM   311  C  C   . VAL   A 1 37  ? 36.863 -10.468 35.513 1.00 35.41  ? 38  VAL   A C   1 
ATOM   312  O  O   . VAL   A 1 37  ? 37.028 -11.548 36.086 1.00 32.76  ? 38  VAL   A O   1 
ATOM   313  C  CB  . VAL   A 1 37  ? 35.255 -11.467 33.771 1.00 30.75  ? 38  VAL   A CB  1 
ATOM   314  C  CG1 . VAL   A 1 37  ? 33.938 -11.041 34.411 1.00 30.80  ? 38  VAL   A CG1 1 
ATOM   315  C  CG2 . VAL   A 1 37  ? 35.089 -11.650 32.260 1.00 29.67  ? 38  VAL   A CG2 1 
ATOM   316  N  N   A SER   A 1 38  ? 37.244 -9.290  36.039 0.54 36.15  ? 39  SER   A N   1 
ATOM   317  N  N   B SER   A 1 38  ? 37.082 -9.265  36.076 0.46 35.08  ? 39  SER   A N   1 
ATOM   318  C  CA  A SER   A 1 38  ? 37.840 -9.111  37.370 0.54 37.72  ? 39  SER   A CA  1 
ATOM   319  C  CA  B SER   A 1 38  ? 37.610 -9.006  37.415 0.46 36.26  ? 39  SER   A CA  1 
ATOM   320  C  C   A SER   A 1 38  ? 39.195 -9.868  37.441 0.54 39.13  ? 39  SER   A C   1 
ATOM   321  C  C   B SER   A 1 38  ? 38.703 -10.018 37.783 0.46 38.36  ? 39  SER   A C   1 
ATOM   322  O  O   A SER   A 1 38  ? 40.091 -9.563  36.652 0.54 38.35  ? 39  SER   A O   1 
ATOM   323  O  O   B SER   A 1 38  ? 38.516 -10.905 38.623 0.46 38.07  ? 39  SER   A O   1 
ATOM   324  C  CB  A SER   A 1 38  ? 36.870 -9.537  38.477 0.54 43.70  ? 39  SER   A CB  1 
ATOM   325  C  CB  B SER   A 1 38  ? 36.491 -8.905  38.443 0.46 40.92  ? 39  SER   A CB  1 
ATOM   326  O  OG  A SER   A 1 38  ? 35.607 -8.902  38.352 0.54 58.63  ? 39  SER   A OG  1 
ATOM   327  O  OG  B SER   A 1 38  ? 35.836 -7.653  38.302 0.46 48.75  ? 39  SER   A OG  1 
ATOM   328  N  N   A ARG   A 1 39  ? 39.322 -10.866 38.343 0.54 35.05  ? 40  ARG   A N   1 
ATOM   329  N  N   B ARG   A 1 39  ? 39.808 -9.920  37.024 0.46 33.12  ? 40  ARG   A N   1 
ATOM   330  C  CA  A ARG   A 1 39  ? 40.535 -11.668 38.540 0.54 35.24  ? 40  ARG   A CA  1 
ATOM   331  C  CA  B ARG   A 1 39  ? 41.056 -10.687 37.075 0.46 33.38  ? 40  ARG   A CA  1 
ATOM   332  C  C   A ARG   A 1 39  ? 40.633 -12.859 37.579 0.54 37.83  ? 40  ARG   A C   1 
ATOM   333  C  C   B ARG   A 1 39  ? 40.932 -12.108 36.489 0.46 35.39  ? 40  ARG   A C   1 
ATOM   334  O  O   A ARG   A 1 39  ? 41.662 -13.546 37.572 0.54 37.78  ? 40  ARG   A O   1 
ATOM   335  O  O   B ARG   A 1 39  ? 41.953 -12.633 36.038 0.46 35.83  ? 40  ARG   A O   1 
ATOM   336  C  CB  A ARG   A 1 39  ? 40.629 -12.165 39.997 0.54 35.91  ? 40  ARG   A CB  1 
ATOM   337  C  CB  B ARG   A 1 39  ? 41.710 -10.688 38.470 0.46 35.00  ? 40  ARG   A CB  1 
ATOM   338  C  CG  A ARG   A 1 39  ? 41.057 -11.099 40.993 0.54 42.84  ? 40  ARG   A CG  1 
ATOM   339  C  CG  B ARG   A 1 39  ? 42.215 -9.300  38.864 0.46 45.77  ? 40  ARG   A CG  1 
ATOM   340  C  CD  A ARG   A 1 39  ? 41.378 -11.721 42.337 0.54 43.29  ? 40  ARG   A CD  1 
ATOM   341  C  CD  B ARG   A 1 39  ? 43.212 -9.331  40.003 0.46 53.09  ? 40  ARG   A CD  1 
ATOM   342  N  NE  A ARG   A 1 39  ? 41.587 -10.716 43.378 0.54 46.92  ? 40  ARG   A NE  1 
ATOM   343  N  NE  B ARG   A 1 39  ? 43.638 -7.984  40.387 0.46 59.15  ? 40  ARG   A NE  1 
ATOM   344  C  CZ  A ARG   A 1 39  ? 42.762 -10.174 43.686 0.54 60.45  ? 40  ARG   A CZ  1 
ATOM   345  C  CZ  B ARG   A 1 39  ? 43.043 -7.241  41.317 0.46 70.24  ? 40  ARG   A CZ  1 
ATOM   346  N  NH1 A ARG   A 1 39  ? 42.849 -9.276  44.655 0.54 49.66  ? 40  ARG   A NH1 1 
ATOM   347  N  NH1 B ARG   A 1 39  ? 41.981 -7.701  41.967 0.46 53.55  ? 40  ARG   A NH1 1 
ATOM   348  N  NH2 A ARG   A 1 39  ? 43.857 -10.522 43.021 0.54 45.57  ? 40  ARG   A NH2 1 
ATOM   349  N  NH2 B ARG   A 1 39  ? 43.502 -6.029  41.600 0.46 58.78  ? 40  ARG   A NH2 1 
ATOM   350  N  N   A GLU   A 1 40  ? 39.566 -13.119 36.793 0.54 32.47  ? 41  GLU   A N   1 
ATOM   351  N  N   B GLU   A 1 40  ? 39.705 -12.698 36.425 0.46 30.98  ? 41  GLU   A N   1 
ATOM   352  C  CA  A GLU   A 1 40  ? 39.524 -14.249 35.860 0.54 31.42  ? 41  GLU   A CA  1 
ATOM   353  C  CA  B GLU   A 1 40  ? 39.463 -14.021 35.810 0.46 30.36  ? 41  GLU   A CA  1 
ATOM   354  C  C   A GLU   A 1 40  ? 39.798 -13.836 34.418 0.54 33.80  ? 41  GLU   A C   1 
ATOM   355  C  C   B GLU   A 1 40  ? 39.607 -13.874 34.289 0.46 33.28  ? 41  GLU   A C   1 
ATOM   356  O  O   A GLU   A 1 40  ? 39.481 -12.719 34.009 0.54 31.97  ? 41  GLU   A O   1 
ATOM   357  O  O   B GLU   A 1 40  ? 39.031 -12.952 33.709 0.46 31.28  ? 41  GLU   A O   1 
ATOM   358  C  CB  A GLU   A 1 40  ? 38.186 -15.012 35.964 0.54 32.59  ? 41  GLU   A CB  1 
ATOM   359  C  CB  B GLU   A 1 40  ? 38.076 -14.576 36.184 0.46 31.68  ? 41  GLU   A CB  1 
ATOM   360  C  CG  A GLU   A 1 40  ? 37.914 -15.597 37.343 0.54 47.79  ? 41  GLU   A CG  1 
ATOM   361  C  CG  B GLU   A 1 40  ? 37.997 -15.124 37.599 0.46 45.00  ? 41  GLU   A CG  1 
ATOM   362  C  CD  A GLU   A 1 40  ? 38.206 -17.078 37.480 0.54 84.45  ? 41  GLU   A CD  1 
ATOM   363  C  CD  B GLU   A 1 40  ? 38.195 -16.623 37.696 0.46 80.41  ? 41  GLU   A CD  1 
ATOM   364  O  OE1 A GLU   A 1 40  ? 37.442 -17.894 36.912 0.54 84.51  ? 41  GLU   A OE1 1 
ATOM   365  O  OE1 B GLU   A 1 40  ? 39.248 -17.048 38.223 0.46 82.44  ? 41  GLU   A OE1 1 
ATOM   366  O  OE2 A GLU   A 1 40  ? 39.195 -17.426 38.165 0.54 85.32  ? 41  GLU   A OE2 1 
ATOM   367  O  OE2 B GLU   A 1 40  ? 37.300 -17.374 37.243 0.46 81.18  ? 41  GLU   A OE2 1 
ATOM   368  N  N   . GLN   A 1 41  ? 40.381 -14.769 33.648 1.00 29.96  ? 42  GLN   A N   1 
ATOM   369  C  CA  . GLN   A 1 41  ? 40.716 -14.636 32.236 1.00 29.32  ? 42  GLN   A CA  1 
ATOM   370  C  C   . GLN   A 1 41  ? 40.086 -15.762 31.439 1.00 31.35  ? 42  GLN   A C   1 
ATOM   371  O  O   . GLN   A 1 41  ? 40.119 -16.908 31.891 1.00 31.07  ? 42  GLN   A O   1 
ATOM   372  C  CB  . GLN   A 1 41  ? 42.246 -14.649 32.072 1.00 32.06  ? 42  GLN   A CB  1 
ATOM   373  C  CG  . GLN   A 1 41  ? 42.946 -13.415 32.637 1.00 49.92  ? 42  GLN   A CG  1 
ATOM   374  C  CD  . GLN   A 1 41  ? 44.412 -13.316 32.278 1.00 68.56  ? 42  GLN   A CD  1 
ATOM   375  O  OE1 . GLN   A 1 41  ? 44.989 -14.162 31.578 1.00 61.61  ? 42  GLN   A OE1 1 
ATOM   376  N  NE2 . GLN   A 1 41  ? 45.049 -12.263 32.759 1.00 69.90  ? 42  GLN   A NE2 1 
ATOM   377  N  N   . PHE   A 1 42  ? 39.510 -15.441 30.259 1.00 25.67  ? 43  PHE   A N   1 
ATOM   378  C  CA  . PHE   A 1 42  ? 38.844 -16.420 29.390 1.00 25.47  ? 43  PHE   A CA  1 
ATOM   379  C  C   . PHE   A 1 42  ? 39.352 -16.252 27.976 1.00 29.35  ? 43  PHE   A C   1 
ATOM   380  O  O   . PHE   A 1 42  ? 39.201 -15.172 27.401 1.00 30.07  ? 43  PHE   A O   1 
ATOM   381  C  CB  . PHE   A 1 42  ? 37.320 -16.207 29.405 1.00 26.14  ? 43  PHE   A CB  1 
ATOM   382  C  CG  . PHE   A 1 42  ? 36.710 -16.345 30.779 1.00 27.86  ? 43  PHE   A CG  1 
ATOM   383  C  CD1 . PHE   A 1 42  ? 36.574 -15.239 31.613 1.00 29.66  ? 43  PHE   A CD1 1 
ATOM   384  C  CD2 . PHE   A 1 42  ? 36.235 -17.575 31.224 1.00 30.61  ? 43  PHE   A CD2 1 
ATOM   385  C  CE1 . PHE   A 1 42  ? 36.028 -15.369 32.892 1.00 31.27  ? 43  PHE   A CE1 1 
ATOM   386  C  CE2 . PHE   A 1 42  ? 35.681 -17.703 32.503 1.00 33.73  ? 43  PHE   A CE2 1 
ATOM   387  C  CZ  . PHE   A 1 42  ? 35.579 -16.599 33.327 1.00 31.50  ? 43  PHE   A CZ  1 
ATOM   388  N  N   . ARG   A 1 43  ? 39.985 -17.290 27.431 1.00 26.65  ? 44  ARG   A N   1 
ATOM   389  C  CA  . ARG   A 1 43  ? 40.484 -17.248 26.056 1.00 25.45  ? 44  ARG   A CA  1 
ATOM   390  C  C   . ARG   A 1 43  ? 39.342 -17.636 25.099 1.00 28.07  ? 44  ARG   A C   1 
ATOM   391  O  O   . ARG   A 1 43  ? 38.538 -18.538 25.396 1.00 26.60  ? 44  ARG   A O   1 
ATOM   392  C  CB  . ARG   A 1 43  ? 41.708 -18.172 25.879 1.00 27.25  ? 44  ARG   A CB  1 
ATOM   393  C  CG  . ARG   A 1 43  ? 42.935 -17.717 26.719 1.00 33.21  ? 44  ARG   A CG  1 
ATOM   394  C  CD  . ARG   A 1 43  ? 44.258 -18.138 26.083 1.00 40.54  ? 44  ARG   A CD  1 
ATOM   395  N  NE  . ARG   A 1 43  ? 44.290 -17.771 24.661 1.00 51.42  ? 44  ARG   A NE  1 
ATOM   396  C  CZ  . ARG   A 1 43  ? 44.844 -16.670 24.162 1.00 64.35  ? 44  ARG   A CZ  1 
ATOM   397  N  NH1 . ARG   A 1 43  ? 45.521 -15.845 24.947 1.00 58.59  ? 44  ARG   A NH1 1 
ATOM   398  N  NH2 . ARG   A 1 43  ? 44.772 -16.416 22.864 1.00 45.61  ? 44  ARG   A NH2 1 
ATOM   399  N  N   . ALA   A 1 44  ? 39.261 -16.973 23.938 1.00 24.76  ? 45  ALA   A N   1 
ATOM   400  C  CA  . ALA   A 1 44  ? 38.180 -17.281 22.983 1.00 24.25  ? 45  ALA   A CA  1 
ATOM   401  C  C   . ALA   A 1 44  ? 38.561 -16.867 21.576 1.00 25.54  ? 45  ALA   A C   1 
ATOM   402  O  O   . ALA   A 1 44  ? 39.651 -16.308 21.364 1.00 23.84  ? 45  ALA   A O   1 
ATOM   403  C  CB  . ALA   A 1 44  ? 36.876 -16.582 23.401 1.00 25.05  ? 45  ALA   A CB  1 
ATOM   404  N  N   . HIS   A 1 45  ? 37.668 -17.161 20.621 1.00 21.79  ? 46  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 45  ? 37.815 -16.747 19.232 1.00 21.00  ? 46  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 45  ? 36.944 -15.494 19.048 1.00 22.88  ? 46  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 45  ? 35.731 -15.540 19.321 1.00 22.23  ? 46  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 45  ? 37.322 -17.857 18.282 1.00 20.73  ? 46  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 45  ? 38.097 -19.130 18.443 1.00 23.74  ? 46  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 45  ? 37.628 -20.164 19.248 1.00 25.30  ? 46  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 45  ? 39.346 -19.445 18.004 1.00 25.22  ? 46  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 45  ? 38.574 -21.098 19.222 1.00 24.92  ? 46  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 45  ? 39.635 -20.704 18.500 1.00 24.88  ? 46  HIS   A NE2 1 
ATOM   414  N  N   . LYS   A 1 46  ? 37.544 -14.391 18.596 1.00 22.08  ? 47  LYS   A N   1 
ATOM   415  C  CA  . LYS   A 1 46  ? 36.797 -13.138 18.336 1.00 22.13  ? 47  LYS   A CA  1 
ATOM   416  C  C   . LYS   A 1 46  ? 35.557 -13.410 17.460 1.00 24.15  ? 47  LYS   A C   1 
ATOM   417  O  O   . LYS   A 1 46  ? 34.478 -12.903 17.763 1.00 22.01  ? 47  LYS   A O   1 
ATOM   418  C  CB  . LYS   A 1 46  ? 37.695 -12.102 17.619 1.00 24.15  ? 47  LYS   A CB  1 
ATOM   419  C  CG  . LYS   A 1 46  ? 38.723 -11.479 18.550 1.00 27.78  ? 47  LYS   A CG  1 
ATOM   420  C  CD  . LYS   A 1 46  ? 39.664 -10.591 17.751 1.00 27.29  ? 47  LYS   A CD  1 
ATOM   421  C  CE  . LYS   A 1 46  ? 40.751 -10.070 18.646 1.00 30.10  ? 47  LYS   A CE  1 
ATOM   422  N  NZ  . LYS   A 1 46  ? 41.706 -9.238  17.878 1.00 31.02  ? 47  LYS   A NZ  1 
ATOM   423  N  N   . THR   A 1 47  ? 35.699 -14.203 16.382 1.00 21.94  ? 48  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 47  ? 34.568 -14.454 15.476 1.00 22.24  ? 48  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 47  ? 33.388 -15.103 16.175 1.00 22.81  ? 48  THR   A C   1 
ATOM   426  O  O   . THR   A 1 47  ? 32.255 -14.696 15.928 1.00 23.02  ? 48  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 47  ? 35.000 -15.228 14.239 1.00 25.86  ? 48  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 47  ? 35.603 -16.439 14.674 1.00 29.68  ? 48  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 47  ? 35.930 -14.391 13.341 1.00 29.09  ? 48  THR   A CG2 1 
ATOM   430  N  N   . VAL   A 1 48  ? 33.641 -16.081 17.065 1.00 19.18  ? 49  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 48  ? 32.552 -16.748 17.797 1.00 19.05  ? 49  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 48  ? 31.879 -15.757 18.748 1.00 21.76  ? 49  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 48  ? 30.641 -15.711 18.808 1.00 19.88  ? 49  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 48  ? 33.043 -18.016 18.528 1.00 21.08  ? 49  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 48  ? 31.904 -18.625 19.373 1.00 21.48  ? 49  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 48  ? 33.553 -19.040 17.496 1.00 21.44  ? 49  VAL   A CG2 1 
ATOM   437  N  N   . LEU   A 1 49  ? 32.689 -14.948 19.468 1.00 20.09  ? 50  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 49  ? 32.128 -13.942 20.370 1.00 19.84  ? 50  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 49  ? 31.218 -12.957 19.614 1.00 22.71  ? 50  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 49  ? 30.094 -12.688 20.064 1.00 23.04  ? 50  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 49  ? 33.245 -13.173 21.096 1.00 19.45  ? 50  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 49  ? 34.207 -13.977 22.007 1.00 22.63  ? 50  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 49  ? 35.276 -13.024 22.625 1.00 22.62  ? 50  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 49  ? 33.427 -14.718 23.113 1.00 24.60  ? 50  LEU   A CD2 1 
ATOM   445  N  N   . MET   A 1 50  ? 31.660 -12.494 18.426 1.00 20.27  ? 51  MET   A N   1 
ATOM   446  C  CA  . MET   A 1 50  ? 30.866 -11.556 17.611 1.00 21.43  ? 51  MET   A CA  1 
ATOM   447  C  C   . MET   A 1 50  ? 29.581 -12.199 17.123 1.00 24.74  ? 51  MET   A C   1 
ATOM   448  O  O   . MET   A 1 50  ? 28.527 -11.561 17.126 1.00 25.08  ? 51  MET   A O   1 
ATOM   449  C  CB  . MET   A 1 50  ? 31.671 -11.091 16.399 1.00 23.35  ? 51  MET   A CB  1 
ATOM   450  C  CG  . MET   A 1 50  ? 32.903 -10.304 16.782 1.00 26.18  ? 51  MET   A CG  1 
ATOM   451  S  SD  . MET   A 1 50  ? 33.971 -10.196 15.335 1.00 30.21  ? 51  MET   A SD  1 
ATOM   452  C  CE  . MET   A 1 50  ? 33.195 -8.881  14.526 1.00 27.19  ? 51  MET   A CE  1 
ATOM   453  N  N   . ALA   A 1 51  ? 29.658 -13.481 16.723 1.00 21.53  ? 52  ALA   A N   1 
ATOM   454  C  CA  . ALA   A 1 51  ? 28.501 -14.220 16.216 1.00 21.23  ? 52  ALA   A CA  1 
ATOM   455  C  C   . ALA   A 1 51  ? 27.403 -14.421 17.284 1.00 24.88  ? 52  ALA   A C   1 
ATOM   456  O  O   . ALA   A 1 51  ? 26.243 -14.634 16.923 1.00 25.09  ? 52  ALA   A O   1 
ATOM   457  C  CB  . ALA   A 1 51  ? 28.958 -15.583 15.664 1.00 21.76  ? 52  ALA   A CB  1 
ATOM   458  N  N   . CYS   A 1 52  ? 27.784 -14.384 18.585 1.00 20.21  ? 53  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 52  ? 26.867 -14.634 19.708 1.00 21.55  ? 53  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 52  ? 26.407 -13.419 20.497 1.00 24.84  ? 53  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 52  ? 25.467 -13.569 21.282 1.00 23.35  ? 53  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 52  ? 27.518 -15.625 20.663 1.00 21.26  ? 53  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 52  ? 27.870 -17.236 19.931 1.00 23.35  ? 53  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 53  ? 27.155 -12.300 20.438 1.00 21.96  ? 54  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 53  ? 26.946 -11.168 21.340 1.00 21.79  ? 54  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 53  ? 26.956 -9.853  20.586 1.00 25.27  ? 54  SER   A C   1 
ATOM   467  O  O   . SER   A 1 53  ? 27.935 -9.554  19.883 1.00 23.84  ? 54  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 53  ? 28.077 -11.188 22.373 1.00 22.76  ? 54  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 53  ? 28.375 -9.945  22.993 1.00 25.58  ? 54  SER   A OG  1 
ATOM   470  N  N   . GLY   A 1 54  ? 25.906 -9.046  20.785 1.00 23.46  ? 55  GLY   A N   1 
ATOM   471  C  CA  . GLY   A 1 54  ? 25.847 -7.716  20.187 1.00 23.53  ? 55  GLY   A CA  1 
ATOM   472  C  C   . GLY   A 1 54  ? 26.967 -6.823  20.694 1.00 25.98  ? 55  GLY   A C   1 
ATOM   473  O  O   . GLY   A 1 54  ? 27.517 -6.012  19.929 1.00 25.36  ? 55  GLY   A O   1 
ATOM   474  N  N   . LEU   A 1 55  ? 27.367 -7.001  21.984 1.00 23.77  ? 56  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 55  ? 28.488 -6.202  22.524 1.00 23.51  ? 56  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 55  ? 29.829 -6.554  21.834 1.00 26.54  ? 56  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 55  ? 30.537 -5.654  21.371 1.00 23.95  ? 56  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 55  ? 28.599 -6.388  24.057 1.00 23.06  ? 56  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 55  ? 29.672 -5.496  24.729 1.00 28.57  ? 56  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 55  ? 29.260 -4.003  24.732 1.00 30.25  ? 56  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 55  ? 29.955 -5.970  26.126 1.00 28.56  ? 56  LEU   A CD2 1 
ATOM   482  N  N   . PHE   A 1 56  ? 30.156 -7.852  21.723 1.00 22.66  ? 57  PHE   A N   1 
ATOM   483  C  CA  . PHE   A 1 56  ? 31.413 -8.241  21.054 1.00 21.24  ? 57  PHE   A CA  1 
ATOM   484  C  C   . PHE   A 1 56  ? 31.391 -7.897  19.576 1.00 24.51  ? 57  PHE   A C   1 
ATOM   485  O  O   . PHE   A 1 56  ? 32.418 -7.503  19.035 1.00 23.78  ? 57  PHE   A O   1 
ATOM   486  C  CB  . PHE   A 1 56  ? 31.764 -9.711  21.303 1.00 22.13  ? 57  PHE   A CB  1 
ATOM   487  C  CG  . PHE   A 1 56  ? 32.209 -9.942  22.733 1.00 22.34  ? 57  PHE   A CG  1 
ATOM   488  C  CD1 . PHE   A 1 56  ? 33.274 -9.218  23.279 1.00 24.92  ? 57  PHE   A CD1 1 
ATOM   489  C  CD2 . PHE   A 1 56  ? 31.586 -10.901 23.527 1.00 23.47  ? 57  PHE   A CD2 1 
ATOM   490  C  CE1 . PHE   A 1 56  ? 33.652 -9.396  24.624 1.00 24.75  ? 57  PHE   A CE1 1 
ATOM   491  C  CE2 . PHE   A 1 56  ? 32.004 -11.116 24.852 1.00 25.42  ? 57  PHE   A CE2 1 
ATOM   492  C  CZ  . PHE   A 1 56  ? 33.023 -10.355 25.392 1.00 22.93  ? 57  PHE   A CZ  1 
ATOM   493  N  N   . TYR   A 1 57  ? 30.213 -7.976  18.934 1.00 22.92  ? 58  TYR   A N   1 
ATOM   494  C  CA  . TYR   A 1 57  ? 30.094 -7.594  17.515 1.00 23.89  ? 58  TYR   A CA  1 
ATOM   495  C  C   . TYR   A 1 57  ? 30.518 -6.111  17.366 1.00 27.51  ? 58  TYR   A C   1 
ATOM   496  O  O   . TYR   A 1 57  ? 31.311 -5.783  16.478 1.00 26.17  ? 58  TYR   A O   1 
ATOM   497  C  CB  . TYR   A 1 57  ? 28.642 -7.801  17.060 1.00 25.64  ? 58  TYR   A CB  1 
ATOM   498  C  CG  . TYR   A 1 57  ? 28.373 -7.282  15.671 1.00 29.73  ? 58  TYR   A CG  1 
ATOM   499  C  CD1 . TYR   A 1 57  ? 29.022 -7.822  14.566 1.00 31.23  ? 58  TYR   A CD1 1 
ATOM   500  C  CD2 . TYR   A 1 57  ? 27.494 -6.224  15.463 1.00 33.90  ? 58  TYR   A CD2 1 
ATOM   501  C  CE1 . TYR   A 1 57  ? 28.776 -7.341  13.276 1.00 33.59  ? 58  TYR   A CE1 1 
ATOM   502  C  CE2 . TYR   A 1 57  ? 27.239 -5.739  14.185 1.00 37.18  ? 58  TYR   A CE2 1 
ATOM   503  C  CZ  . TYR   A 1 57  ? 27.871 -6.310  13.096 1.00 43.84  ? 58  TYR   A CZ  1 
ATOM   504  O  OH  . TYR   A 1 57  ? 27.598 -5.822  11.851 1.00 49.32  ? 58  TYR   A OH  1 
ATOM   505  N  N   A SER   A 1 58  ? 29.997 -5.233  18.239 0.53 25.51  ? 59  SER   A N   1 
ATOM   506  N  N   B SER   A 1 58  ? 29.996 -5.236  18.244 0.47 25.65  ? 59  SER   A N   1 
ATOM   507  C  CA  A SER   A 1 58  ? 30.323 -3.805  18.228 0.53 26.06  ? 59  SER   A CA  1 
ATOM   508  C  CA  B SER   A 1 58  ? 30.319 -3.807  18.250 0.47 26.37  ? 59  SER   A CA  1 
ATOM   509  C  C   A SER   A 1 58  ? 31.812 -3.557  18.531 0.53 31.41  ? 59  SER   A C   1 
ATOM   510  C  C   B SER   A 1 58  ? 31.816 -3.582  18.513 0.47 31.38  ? 59  SER   A C   1 
ATOM   511  O  O   A SER   A 1 58  ? 32.441 -2.752  17.846 0.53 32.67  ? 59  SER   A O   1 
ATOM   512  O  O   B SER   A 1 58  ? 32.449 -2.812  17.792 0.47 32.42  ? 59  SER   A O   1 
ATOM   513  C  CB  A SER   A 1 58  ? 29.432 -3.050  19.211 0.53 28.12  ? 59  SER   A CB  1 
ATOM   514  C  CB  B SER   A 1 58  ? 29.484 -3.080  19.301 0.47 29.02  ? 59  SER   A CB  1 
ATOM   515  O  OG  A SER   A 1 58  ? 28.087 -3.032  18.761 0.53 30.57  ? 59  SER   A OG  1 
ATOM   516  O  OG  B SER   A 1 58  ? 29.791 -1.695  19.327 0.47 34.81  ? 59  SER   A OG  1 
ATOM   517  N  N   . ILE   A 1 59  ? 32.372 -4.268  19.531 1.00 27.69  ? 60  ILE   A N   1 
ATOM   518  C  CA  . ILE   A 1 59  ? 33.791 -4.152  19.928 1.00 27.15  ? 60  ILE   A CA  1 
ATOM   519  C  C   . ILE   A 1 59  ? 34.737 -4.532  18.785 1.00 30.13  ? 60  ILE   A C   1 
ATOM   520  O  O   . ILE   A 1 59  ? 35.635 -3.756  18.456 1.00 31.49  ? 60  ILE   A O   1 
ATOM   521  C  CB  . ILE   A 1 59  ? 34.122 -4.998  21.216 1.00 29.52  ? 60  ILE   A CB  1 
ATOM   522  C  CG1 . ILE   A 1 59  ? 33.380 -4.461  22.468 1.00 29.49  ? 60  ILE   A CG1 1 
ATOM   523  C  CG2 . ILE   A 1 59  ? 35.655 -5.062  21.471 1.00 28.54  ? 60  ILE   A CG2 1 
ATOM   524  C  CD1 . ILE   A 1 59  ? 33.437 -5.441  23.693 1.00 30.70  ? 60  ILE   A CD1 1 
ATOM   525  N  N   . PHE   A 1 60  ? 34.557 -5.724  18.203 1.00 24.69  ? 61  PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 60  ? 35.528 -6.180  17.227 1.00 24.93  ? 61  PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 60  ? 35.310 -5.641  15.815 1.00 29.21  ? 61  PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 60  ? 36.150 -5.906  14.951 1.00 30.37  ? 61  PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 60  ? 35.661 -7.711  17.266 1.00 25.05  ? 61  PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 60  ? 36.096 -8.185  18.640 1.00 25.39  ? 61  PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 60  ? 37.308 -7.766  19.190 1.00 28.60  ? 61  PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 60  ? 35.312 -9.074  19.368 1.00 26.88  ? 61  PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 60  ? 37.697 -8.185  20.472 1.00 29.75  ? 61  PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 60  ? 35.715 -9.514  20.637 1.00 29.60  ? 61  PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 60  ? 36.904 -9.069  21.179 1.00 27.96  ? 61  PHE   A CZ  1 
ATOM   536  N  N   . THR   A 1 61  ? 34.252 -4.837  15.584 1.00 27.09  ? 62  THR   A N   1 
ATOM   537  C  CA  . THR   A 1 61  ? 34.091 -4.152  14.291 1.00 27.57  ? 62  THR   A CA  1 
ATOM   538  C  C   . THR   A 1 61  ? 34.633 -2.733  14.414 1.00 34.05  ? 62  THR   A C   1 
ATOM   539  O  O   . THR   A 1 61  ? 34.715 -2.011  13.413 1.00 34.23  ? 62  THR   A O   1 
ATOM   540  C  CB  . THR   A 1 61  ? 32.663 -4.186  13.736 1.00 35.02  ? 62  THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 61  ? 31.758 -3.665  14.705 1.00 32.36  ? 62  THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 61  ? 32.244 -5.575  13.245 1.00 31.85  ? 62  THR   A CG2 1 
ATOM   543  N  N   . ASP   A 1 62  ? 35.035 -2.333  15.640 1.00 30.07  ? 63  ASP   A N   1 
ATOM   544  C  CA  . ASP   A 1 62  ? 35.641 -1.013  15.833 1.00 30.92  ? 63  ASP   A CA  1 
ATOM   545  C  C   . ASP   A 1 62  ? 37.062 -1.074  15.283 1.00 37.10  ? 63  ASP   A C   1 
ATOM   546  O  O   . ASP   A 1 62  ? 37.804 -1.983  15.641 1.00 35.07  ? 63  ASP   A O   1 
ATOM   547  C  CB  . ASP   A 1 62  ? 35.640 -0.611  17.316 1.00 32.03  ? 63  ASP   A CB  1 
ATOM   548  C  CG  . ASP   A 1 62  ? 36.388 0.683   17.546 1.00 44.34  ? 63  ASP   A CG  1 
ATOM   549  O  OD1 . ASP   A 1 62  ? 35.786 1.751   17.355 1.00 48.57  ? 63  ASP   A OD1 1 
ATOM   550  O  OD2 . ASP   A 1 62  ? 37.596 0.622   17.855 1.00 46.70  ? 63  ASP   A OD2 1 
ATOM   551  N  N   . GLN   A 1 63  ? 37.451 -0.079  14.454 1.00 38.95  ? 64  GLN   A N   1 
ATOM   552  C  CA  . GLN   A 1 63  ? 38.754 -0.013  13.780 1.00 40.44  ? 64  GLN   A CA  1 
ATOM   553  C  C   . GLN   A 1 63  ? 39.966 -0.048  14.725 1.00 44.17  ? 64  GLN   A C   1 
ATOM   554  O  O   . GLN   A 1 63  ? 41.033 -0.487  14.292 1.00 46.67  ? 64  GLN   A O   1 
ATOM   555  C  CB  . GLN   A 1 63  ? 38.830 1.189   12.825 1.00 44.24  ? 64  GLN   A CB  1 
ATOM   556  C  CG  . GLN   A 1 63  ? 37.992 0.995   11.562 1.00 61.75  ? 64  GLN   A CG  1 
ATOM   557  N  N   . LEU   A 1 64  ? 39.822 0.405   15.992 1.00 36.55  ? 65  LEU   A N   1 
ATOM   558  C  CA  . LEU   A 1 64  ? 40.907 0.319   16.972 1.00 36.27  ? 65  LEU   A CA  1 
ATOM   559  C  C   . LEU   A 1 64  ? 40.804 -0.940  17.834 1.00 39.69  ? 65  LEU   A C   1 
ATOM   560  O  O   . LEU   A 1 64  ? 41.818 -1.588  18.083 1.00 40.84  ? 65  LEU   A O   1 
ATOM   561  C  CB  . LEU   A 1 64  ? 40.925 1.548   17.916 1.00 37.32  ? 65  LEU   A CB  1 
ATOM   562  C  CG  . LEU   A 1 64  ? 41.509 2.844   17.392 1.00 44.48  ? 65  LEU   A CG  1 
ATOM   563  C  CD1 . LEU   A 1 64  ? 41.352 3.945   18.428 1.00 44.88  ? 65  LEU   A CD1 1 
ATOM   564  C  CD2 . LEU   A 1 64  ? 42.988 2.703   17.030 1.00 49.65  ? 65  LEU   A CD2 1 
ATOM   565  N  N   . LYS   A 1 65  ? 39.599 -1.259  18.350 1.00 32.75  ? 66  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 65  ? 39.445 -2.382  19.277 1.00 31.55  ? 66  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 65  ? 39.584 -3.740  18.597 1.00 36.19  ? 66  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 65  ? 39.965 -4.699  19.267 1.00 35.30  ? 66  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 65  ? 38.140 -2.290  20.095 1.00 31.95  ? 66  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 65  ? 38.023 -1.018  20.955 1.00 31.47  ? 66  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 65  ? 36.743 -1.097  21.797 1.00 30.39  ? 66  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 65  ? 36.397 0.215   22.475 1.00 36.75  ? 66  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 65  ? 35.938 1.262   21.531 1.00 37.68  ? 66  LYS   A NZ  1 
ATOM   574  N  N   . CYS   A 1 66  ? 39.332 -3.814  17.268 1.00 35.41  ? 67  CYS   A N   1 
ATOM   575  C  CA  . CYS   A 1 66  ? 39.475 -5.064  16.494 1.00 35.83  ? 67  CYS   A CA  1 
ATOM   576  C  C   . CYS   A 1 66  ? 40.873 -5.682  16.643 1.00 40.08  ? 67  CYS   A C   1 
ATOM   577  O  O   . CYS   A 1 66  ? 41.015 -6.898  16.485 1.00 40.72  ? 67  CYS   A O   1 
ATOM   578  C  CB  . CYS   A 1 66  ? 39.117 -4.853  15.024 1.00 38.12  ? 67  CYS   A CB  1 
ATOM   579  S  SG  . CYS   A 1 66  ? 40.255 -3.760  14.116 1.00 44.55  ? 67  CYS   A SG  1 
ATOM   580  N  N   . ASN   A 1 67  ? 41.901 -4.835  16.920 1.00 35.38  ? 68  ASN   A N   1 
ATOM   581  C  CA  . ASN   A 1 67  ? 43.303 -5.234  17.039 1.00 35.94  ? 68  ASN   A CA  1 
ATOM   582  C  C   . ASN   A 1 67  ? 43.771 -5.542  18.460 1.00 39.28  ? 68  ASN   A C   1 
ATOM   583  O  O   . ASN   A 1 67  ? 44.936 -5.911  18.660 1.00 38.45  ? 68  ASN   A O   1 
ATOM   584  C  CB  . ASN   A 1 67  ? 44.210 -4.178  16.375 1.00 38.69  ? 68  ASN   A CB  1 
ATOM   585  C  CG  . ASN   A 1 67  ? 44.001 -4.132  14.870 1.00 53.63  ? 68  ASN   A CG  1 
ATOM   586  O  OD1 . ASN   A 1 67  ? 43.942 -3.064  14.263 1.00 52.94  ? 68  ASN   A OD1 1 
ATOM   587  N  ND2 . ASN   A 1 67  ? 43.826 -5.290  14.236 1.00 45.05  ? 68  ASN   A ND2 1 
ATOM   588  N  N   . LEU   A 1 68  ? 42.886 -5.381  19.450 1.00 36.67  ? 69  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 68  ? 43.260 -5.647  20.835 1.00 35.87  ? 69  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 68  ? 43.262 -7.146  21.109 1.00 37.48  ? 69  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 68  ? 42.368 -7.859  20.626 1.00 36.00  ? 69  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 68  ? 42.305 -4.930  21.816 1.00 35.99  ? 69  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 68  ? 42.307 -3.389  21.773 1.00 41.02  ? 69  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 68  ? 41.239 -2.827  22.693 1.00 41.15  ? 69  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 68  ? 43.681 -2.810  22.132 1.00 43.30  ? 69  LEU   A CD2 1 
ATOM   596  N  N   A SER   A 1 69  ? 44.252 -7.623  21.883 0.51 34.37  ? 70  SER   A N   1 
ATOM   597  N  N   B SER   A 1 69  ? 44.255 -7.612  21.887 0.49 34.36  ? 70  SER   A N   1 
ATOM   598  C  CA  A SER   A 1 69  ? 44.349 -9.041  22.255 0.51 33.87  ? 70  SER   A CA  1 
ATOM   599  C  CA  B SER   A 1 69  ? 44.399 -9.020  22.279 0.49 33.92  ? 70  SER   A CA  1 
ATOM   600  C  C   A SER   A 1 69  ? 43.740 -9.281  23.649 0.51 34.85  ? 70  SER   A C   1 
ATOM   601  C  C   B SER   A 1 69  ? 43.771 -9.273  23.658 0.49 34.91  ? 70  SER   A C   1 
ATOM   602  O  O   A SER   A 1 69  ? 43.565 -10.429 24.057 0.51 32.66  ? 70  SER   A O   1 
ATOM   603  O  O   B SER   A 1 69  ? 43.611 -10.424 24.064 0.49 32.73  ? 70  SER   A O   1 
ATOM   604  C  CB  A SER   A 1 69  ? 45.800 -9.513  22.210 0.51 38.85  ? 70  SER   A CB  1 
ATOM   605  C  CB  B SER   A 1 69  ? 45.874 -9.415  22.293 0.49 38.88  ? 70  SER   A CB  1 
ATOM   606  O  OG  A SER   A 1 69  ? 46.615 -8.768  23.098 0.51 47.27  ? 70  SER   A OG  1 
ATOM   607  O  OG  B SER   A 1 69  ? 46.391 -9.455  20.974 0.49 47.19  ? 70  SER   A OG  1 
ATOM   608  N  N   . VAL   A 1 70  ? 43.447 -8.186  24.384 1.00 31.57  ? 71  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 70  ? 42.851 -8.223  25.728 1.00 30.83  ? 71  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 70  ? 41.672 -7.248  25.778 1.00 32.04  ? 71  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 70  ? 41.816 -6.076  25.391 1.00 32.18  ? 71  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 70  ? 43.884 -7.905  26.858 1.00 36.24  ? 71  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 70  ? 43.224 -7.911  28.243 1.00 36.59  ? 71  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 70  ? 45.083 -8.862  26.823 1.00 36.74  ? 71  VAL   A CG2 1 
ATOM   615  N  N   . ILE   A 1 71  ? 40.523 -7.734  26.282 1.00 25.24  ? 72  ILE   A N   1 
ATOM   616  C  CA  . ILE   A 1 71  ? 39.315 -6.935  26.485 1.00 25.32  ? 72  ILE   A CA  1 
ATOM   617  C  C   . ILE   A 1 71  ? 38.906 -7.057  27.949 1.00 29.00  ? 72  ILE   A C   1 
ATOM   618  O  O   . ILE   A 1 71  ? 38.650 -8.165  28.425 1.00 27.89  ? 72  ILE   A O   1 
ATOM   619  C  CB  . ILE   A 1 71  ? 38.155 -7.295  25.507 1.00 26.85  ? 72  ILE   A CB  1 
ATOM   620  C  CG1 . ILE   A 1 71  ? 38.570 -7.116  23.996 1.00 28.01  ? 72  ILE   A CG1 1 
ATOM   621  C  CG2 . ILE   A 1 71  ? 36.844 -6.545  25.849 1.00 28.04  ? 72  ILE   A CG2 1 
ATOM   622  C  CD1 . ILE   A 1 71  ? 38.921 -5.668  23.508 1.00 30.64  ? 72  ILE   A CD1 1 
ATOM   623  N  N   . ASN   A 1 72  ? 38.780 -5.914  28.638 1.00 26.93  ? 73  ASN   A N   1 
ATOM   624  C  CA  . ASN   A 1 72  ? 38.386 -5.857  30.037 1.00 27.06  ? 73  ASN   A CA  1 
ATOM   625  C  C   . ASN   A 1 72  ? 36.916 -5.521  30.155 1.00 29.54  ? 73  ASN   A C   1 
ATOM   626  O  O   . ASN   A 1 72  ? 36.490 -4.455  29.705 1.00 28.46  ? 73  ASN   A O   1 
ATOM   627  C  CB  . ASN   A 1 72  ? 39.213 -4.802  30.805 1.00 31.03  ? 73  ASN   A CB  1 
ATOM   628  C  CG  . ASN   A 1 72  ? 40.695 -4.983  30.725 1.00 49.81  ? 73  ASN   A CG  1 
ATOM   629  O  OD1 . ASN   A 1 72  ? 41.235 -6.026  31.077 1.00 39.78  ? 73  ASN   A OD1 1 
ATOM   630  N  ND2 . ASN   A 1 72  ? 41.389 -3.952  30.286 1.00 46.18  ? 73  ASN   A ND2 1 
ATOM   631  N  N   . LEU   A 1 73  ? 36.140 -6.419  30.761 1.00 24.77  ? 74  LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 73  ? 34.721 -6.165  30.955 1.00 23.87  ? 74  LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 73  ? 34.484 -5.277  32.183 1.00 28.57  ? 74  LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 73  ? 35.366 -5.131  33.043 1.00 28.52  ? 74  LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 73  ? 33.920 -7.477  31.083 1.00 23.23  ? 74  LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 73  ? 33.988 -8.488  29.911 1.00 27.23  ? 74  LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 73  ? 32.882 -9.533  30.057 1.00 27.80  ? 74  LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 73  ? 33.923 -7.801  28.532 1.00 26.33  ? 74  LEU   A CD2 1 
ATOM   639  N  N   . ASP   A 1 74  ? 33.290 -4.689  32.257 1.00 26.01  ? 75  ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 74  ? 32.855 -3.831  33.362 1.00 26.83  ? 75  ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 74  ? 33.068 -4.588  34.696 1.00 31.15  ? 75  ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 74  ? 32.738 -5.776  34.761 1.00 30.00  ? 75  ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 74  ? 31.371 -3.487  33.166 1.00 28.56  ? 75  ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 74  ? 30.809 -2.473  34.149 1.00 39.09  ? 75  ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 74  ? 30.689 -2.807  35.347 1.00 39.77  ? 75  ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 74  ? 30.461 -1.361  33.715 1.00 39.81  ? 75  ASP   A OD2 1 
ATOM   647  N  N   . PRO   A 1 75  ? 33.624 -3.938  35.741 1.00 31.41  ? 76  PRO   A N   1 
ATOM   648  C  CA  . PRO   A 1 75  ? 33.865 -4.657  37.018 1.00 32.54  ? 76  PRO   A CA  1 
ATOM   649  C  C   . PRO   A 1 75  ? 32.632 -5.251  37.691 1.00 35.99  ? 76  PRO   A C   1 
ATOM   650  O  O   . PRO   A 1 75  ? 32.784 -6.131  38.539 1.00 36.46  ? 76  PRO   A O   1 
ATOM   651  C  CB  . PRO   A 1 75  ? 34.549 -3.612  37.916 1.00 35.66  ? 76  PRO   A CB  1 
ATOM   652  C  CG  . PRO   A 1 75  ? 34.280 -2.298  37.280 1.00 40.44  ? 76  PRO   A CG  1 
ATOM   653  C  CD  . PRO   A 1 75  ? 34.096 -2.535  35.810 1.00 34.17  ? 76  PRO   A CD  1 
ATOM   654  N  N   . GLU   A 1 76  ? 31.421 -4.815  37.308 1.00 32.89  ? 77  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 76  ? 30.174 -5.349  37.876 1.00 34.65  ? 77  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 76  ? 29.895 -6.766  37.332 1.00 34.29  ? 77  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 76  ? 29.076 -7.492  37.896 1.00 33.11  ? 77  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 76  ? 28.990 -4.426  37.522 1.00 37.51  ? 77  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 76  ? 27.833 -4.466  38.506 1.00 58.16  ? 77  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 76  ? 27.998 -3.560  39.712 1.00 87.54  ? 77  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 76  ? 28.035 -2.321  39.525 1.00 88.79  ? 77  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 76  ? 28.084 -4.087  40.845 1.00 81.01  ? 77  GLU   A OE2 1 
ATOM   663  N  N   . ILE   A 1 77  ? 30.547 -7.149  36.227 1.00 28.73  ? 78  ILE   A N   1 
ATOM   664  C  CA  . ILE   A 1 77  ? 30.289 -8.461  35.625 1.00 27.17  ? 78  ILE   A CA  1 
ATOM   665  C  C   . ILE   A 1 77  ? 30.862 -9.590  36.453 1.00 31.55  ? 78  ILE   A C   1 
ATOM   666  O  O   . ILE   A 1 77  ? 32.037 -9.575  36.820 1.00 31.20  ? 78  ILE   A O   1 
ATOM   667  C  CB  . ILE   A 1 77  ? 30.753 -8.505  34.144 1.00 29.32  ? 78  ILE   A CB  1 
ATOM   668  C  CG1 . ILE   A 1 77  ? 30.076 -7.369  33.328 1.00 30.49  ? 78  ILE   A CG1 1 
ATOM   669  C  CG2 . ILE   A 1 77  ? 30.498 -9.888  33.512 1.00 27.56  ? 78  ILE   A CG2 1 
ATOM   670  C  CD1 . ILE   A 1 77  ? 28.493 -7.341  33.337 1.00 34.92  ? 78  ILE   A CD1 1 
ATOM   671  N  N   . ASN   A 1 78  ? 30.021 -10.578 36.700 1.00 31.72  ? 79  ASN   A N   1 
ATOM   672  C  CA  . ASN   A 1 78  ? 30.338 -11.767 37.476 1.00 32.36  ? 79  ASN   A CA  1 
ATOM   673  C  C   . ASN   A 1 78  ? 31.097 -12.786 36.609 1.00 31.91  ? 79  ASN   A C   1 
ATOM   674  O  O   . ASN   A 1 78  ? 30.583 -13.164 35.556 1.00 29.54  ? 79  ASN   A O   1 
ATOM   675  C  CB  . ASN   A 1 78  ? 29.033 -12.370 38.031 1.00 35.51  ? 79  ASN   A CB  1 
ATOM   676  C  CG  . ASN   A 1 78  ? 29.246 -13.640 38.802 1.00 49.35  ? 79  ASN   A CG  1 
ATOM   677  O  OD1 . ASN   A 1 78  ? 28.940 -14.724 38.317 1.00 39.97  ? 79  ASN   A OD1 1 
ATOM   678  N  ND2 . ASN   A 1 78  ? 29.783 -13.533 40.017 1.00 42.40  ? 79  ASN   A ND2 1 
ATOM   679  N  N   . PRO   A 1 79  ? 32.304 -13.256 37.026 1.00 30.01  ? 80  PRO   A N   1 
ATOM   680  C  CA  . PRO   A 1 79  ? 33.045 -14.236 36.201 1.00 29.34  ? 80  PRO   A CA  1 
ATOM   681  C  C   . PRO   A 1 79  ? 32.302 -15.556 35.946 1.00 32.09  ? 80  PRO   A C   1 
ATOM   682  O  O   . PRO   A 1 79  ? 32.412 -16.103 34.842 1.00 30.40  ? 80  PRO   A O   1 
ATOM   683  C  CB  . PRO   A 1 79  ? 34.344 -14.454 36.986 1.00 32.88  ? 80  PRO   A CB  1 
ATOM   684  C  CG  . PRO   A 1 79  ? 34.465 -13.256 37.888 1.00 37.80  ? 80  PRO   A CG  1 
ATOM   685  C  CD  . PRO   A 1 79  ? 33.063 -12.897 38.244 1.00 33.61  ? 80  PRO   A CD  1 
ATOM   686  N  N   . GLU   A 1 80  ? 31.519 -16.048 36.937 1.00 29.47  ? 81  GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 80  ? 30.755 -17.287 36.757 1.00 28.91  ? 81  GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 80  ? 29.660 -17.100 35.679 1.00 30.60  ? 81  GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 80  ? 29.522 -17.953 34.808 1.00 28.78  ? 81  GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 80  ? 30.167 -17.805 38.082 1.00 31.29  ? 81  GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 80  ? 29.592 -19.206 37.903 1.00 39.74  ? 81  GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 80  ? 28.733 -19.777 39.018 1.00 64.67  ? 81  GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 80  ? 28.714 -21.021 39.156 1.00 60.88  ? 81  GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 80  ? 28.064 -18.998 39.735 1.00 56.81  ? 81  GLU   A OE2 1 
ATOM   695  N  N   . GLY   A 1 81  ? 28.918 -15.986 35.746 1.00 27.87  ? 82  GLY   A N   1 
ATOM   696  C  CA  . GLY   A 1 81  ? 27.905 -15.653 34.747 1.00 27.16  ? 82  GLY   A CA  1 
ATOM   697  C  C   . GLY   A 1 81  ? 28.526 -15.584 33.359 1.00 28.32  ? 82  GLY   A C   1 
ATOM   698  O  O   . GLY   A 1 81  ? 27.968 -16.118 32.387 1.00 26.41  ? 82  GLY   A O   1 
ATOM   699  N  N   . PHE   A 1 82  ? 29.713 -14.946 33.261 1.00 23.80  ? 83  PHE   A N   1 
ATOM   700  C  CA  . PHE   A 1 82  ? 30.410 -14.879 31.967 1.00 22.20  ? 83  PHE   A CA  1 
ATOM   701  C  C   . PHE   A 1 82  ? 30.791 -16.301 31.499 1.00 25.69  ? 83  PHE   A C   1 
ATOM   702  O  O   . PHE   A 1 82  ? 30.569 -16.646 30.338 1.00 24.14  ? 83  PHE   A O   1 
ATOM   703  C  CB  . PHE   A 1 82  ? 31.670 -13.969 32.044 1.00 23.47  ? 83  PHE   A CB  1 
ATOM   704  C  CG  . PHE   A 1 82  ? 32.295 -13.838 30.674 1.00 23.69  ? 83  PHE   A CG  1 
ATOM   705  C  CD1 . PHE   A 1 82  ? 31.719 -13.016 29.705 1.00 26.23  ? 83  PHE   A CD1 1 
ATOM   706  C  CD2 . PHE   A 1 82  ? 33.345 -14.669 30.289 1.00 24.72  ? 83  PHE   A CD2 1 
ATOM   707  C  CE1 . PHE   A 1 82  ? 32.235 -12.963 28.407 1.00 27.00  ? 83  PHE   A CE1 1 
ATOM   708  C  CE2 . PHE   A 1 82  ? 33.865 -14.613 28.992 1.00 26.08  ? 83  PHE   A CE2 1 
ATOM   709  C  CZ  . PHE   A 1 82  ? 33.290 -13.782 28.050 1.00 25.34  ? 83  PHE   A CZ  1 
ATOM   710  N  N   . CYS   A 1 83  ? 31.374 -17.108 32.389 1.00 27.01  ? 84  CYS   A N   1 
ATOM   711  C  CA  . CYS   A 1 83  ? 31.764 -18.485 32.065 1.00 28.43  ? 84  CYS   A CA  1 
ATOM   712  C  C   . CYS   A 1 83  ? 30.588 -19.316 31.495 1.00 29.37  ? 84  CYS   A C   1 
ATOM   713  O  O   . CYS   A 1 83  ? 30.743 -20.008 30.474 1.00 27.39  ? 84  CYS   A O   1 
ATOM   714  C  CB  . CYS   A 1 83  ? 32.381 -19.161 33.284 1.00 31.71  ? 84  CYS   A CB  1 
ATOM   715  S  SG  . CYS   A 1 83  ? 33.098 -20.785 32.921 1.00 37.37  ? 84  CYS   A SG  1 
ATOM   716  N  N   . ILE   A 1 84  ? 29.407 -19.201 32.143 1.00 25.93  ? 85  ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 84  ? 28.180 -19.904 31.745 1.00 24.44  ? 85  ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 84  ? 27.785 -19.455 30.335 1.00 23.99  ? 85  ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 84  ? 27.433 -20.286 29.490 1.00 23.86  ? 85  ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 84  ? 27.061 -19.673 32.794 1.00 27.46  ? 85  ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 84  ? 27.376 -20.476 34.106 1.00 28.28  ? 85  ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 84  ? 25.660 -20.024 32.229 1.00 27.58  ? 85  ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 84  ? 26.620 -19.996 35.314 1.00 35.98  ? 85  ILE   A CD1 1 
ATOM   724  N  N   . LEU   A 1 85  ? 27.845 -18.147 30.096 1.00 20.91  ? 86  LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 85  ? 27.497 -17.608 28.770 1.00 20.64  ? 86  LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 85  ? 28.507 -17.971 27.698 1.00 24.54  ? 86  LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 85  ? 28.100 -18.256 26.565 1.00 22.33  ? 86  LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 85  ? 27.235 -16.110 28.849 1.00 21.09  ? 86  LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 85  ? 25.941 -15.760 29.631 1.00 26.76  ? 86  LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 85  ? 25.836 -14.285 29.772 1.00 28.33  ? 86  LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 85  ? 24.672 -16.306 28.932 1.00 27.46  ? 86  LEU   A CD2 1 
ATOM   732  N  N   . LEU   A 1 86  ? 29.822 -17.989 28.031 1.00 21.23  ? 87  LEU   A N   1 
ATOM   733  C  CA  . LEU   A 1 86  ? 30.858 -18.407 27.074 1.00 21.34  ? 87  LEU   A CA  1 
ATOM   734  C  C   . LEU   A 1 86  ? 30.633 -19.878 26.669 1.00 23.66  ? 87  LEU   A C   1 
ATOM   735  O  O   . LEU   A 1 86  ? 30.655 -20.226 25.477 1.00 21.46  ? 87  LEU   A O   1 
ATOM   736  C  CB  . LEU   A 1 86  ? 32.254 -18.173 27.683 1.00 21.37  ? 87  LEU   A CB  1 
ATOM   737  C  CG  . LEU   A 1 86  ? 33.436 -18.457 26.727 1.00 25.91  ? 87  LEU   A CG  1 
ATOM   738  C  CD1 . LEU   A 1 86  ? 33.389 -17.539 25.482 1.00 25.00  ? 87  LEU   A CD1 1 
ATOM   739  C  CD2 . LEU   A 1 86  ? 34.786 -18.306 27.465 1.00 28.02  ? 87  LEU   A CD2 1 
ATOM   740  N  N   . ASP   A 1 87  ? 30.361 -20.732 27.654 1.00 21.69  ? 88  ASP   A N   1 
ATOM   741  C  CA  . ASP   A 1 87  ? 30.019 -22.123 27.373 1.00 22.23  ? 88  ASP   A CA  1 
ATOM   742  C  C   . ASP   A 1 87  ? 28.785 -22.209 26.449 1.00 24.51  ? 88  ASP   A C   1 
ATOM   743  O  O   . ASP   A 1 87  ? 28.792 -23.001 25.508 1.00 24.10  ? 88  ASP   A O   1 
ATOM   744  C  CB  . ASP   A 1 87  ? 29.740 -22.858 28.678 1.00 25.74  ? 88  ASP   A CB  1 
ATOM   745  C  CG  . ASP   A 1 87  ? 30.977 -23.217 29.482 1.00 39.33  ? 88  ASP   A CG  1 
ATOM   746  O  OD1 . ASP   A 1 87  ? 32.100 -23.152 28.918 1.00 40.11  ? 88  ASP   A OD1 1 
ATOM   747  O  OD2 . ASP   A 1 87  ? 30.826 -23.575 30.671 1.00 39.13  ? 88  ASP   A OD2 1 
ATOM   748  N  N   . PHE   A 1 88  ? 27.726 -21.424 26.724 1.00 21.89  ? 89  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 88  ? 26.529 -21.400 25.858 1.00 20.19  ? 89  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 88  ? 26.904 -21.009 24.414 1.00 21.19  ? 89  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 88  ? 26.409 -21.602 23.452 1.00 20.28  ? 89  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 88  ? 25.459 -20.431 26.399 1.00 20.94  ? 89  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 88  ? 24.356 -20.150 25.405 1.00 20.92  ? 89  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 88  ? 23.385 -21.111 25.124 1.00 23.74  ? 89  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 88  ? 24.331 -18.957 24.685 1.00 24.08  ? 89  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 88  ? 22.401 -20.869 24.168 1.00 23.73  ? 89  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 88  ? 23.344 -18.722 23.716 1.00 26.38  ? 89  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 88  ? 22.386 -19.677 23.469 1.00 24.70  ? 89  PHE   A CZ  1 
ATOM   759  N  N   . MET   A 1 89  ? 27.743 -19.970 24.256 1.00 17.91  ? 90  MET   A N   1 
ATOM   760  C  CA  . MET   A 1 89  ? 28.143 -19.550 22.900 1.00 17.73  ? 90  MET   A CA  1 
ATOM   761  C  C   . MET   A 1 89  ? 28.703 -20.696 22.079 1.00 21.67  ? 90  MET   A C   1 
ATOM   762  O  O   . MET   A 1 89  ? 28.390 -20.804 20.894 1.00 21.17  ? 90  MET   A O   1 
ATOM   763  C  CB  . MET   A 1 89  ? 29.231 -18.461 23.002 1.00 18.66  ? 90  MET   A CB  1 
ATOM   764  C  CG  . MET   A 1 89  ? 28.699 -17.166 23.585 1.00 20.33  ? 90  MET   A CG  1 
ATOM   765  S  SD  . MET   A 1 89  ? 30.048 -15.928 23.495 1.00 24.90  ? 90  MET   A SD  1 
ATOM   766  C  CE  . MET   A 1 89  ? 29.355 -14.610 24.597 1.00 25.08  ? 90  MET   A CE  1 
ATOM   767  N  N   . TYR   A 1 90  ? 29.564 -21.521 22.698 1.00 18.72  ? 91  TYR   A N   1 
ATOM   768  C  CA  . TYR   A 1 90  ? 30.242 -22.612 22.003 1.00 18.96  ? 91  TYR   A CA  1 
ATOM   769  C  C   . TYR   A 1 90  ? 29.500 -23.925 21.995 1.00 23.69  ? 91  TYR   A C   1 
ATOM   770  O  O   . TYR   A 1 90  ? 29.982 -24.881 21.376 1.00 22.16  ? 91  TYR   A O   1 
ATOM   771  C  CB  . TYR   A 1 90  ? 31.631 -22.828 22.618 1.00 20.17  ? 91  TYR   A CB  1 
ATOM   772  C  CG  . TYR   A 1 90  ? 32.677 -21.838 22.142 1.00 21.77  ? 91  TYR   A CG  1 
ATOM   773  C  CD1 . TYR   A 1 90  ? 32.819 -20.590 22.753 1.00 23.51  ? 91  TYR   A CD1 1 
ATOM   774  C  CD2 . TYR   A 1 90  ? 33.512 -22.139 21.062 1.00 22.46  ? 91  TYR   A CD2 1 
ATOM   775  C  CE1 . TYR   A 1 90  ? 33.789 -19.674 22.317 1.00 24.23  ? 91  TYR   A CE1 1 
ATOM   776  C  CE2 . TYR   A 1 90  ? 34.529 -21.260 20.663 1.00 23.67  ? 91  TYR   A CE2 1 
ATOM   777  C  CZ  . TYR   A 1 90  ? 34.635 -20.015 21.264 1.00 26.69  ? 91  TYR   A CZ  1 
ATOM   778  O  OH  . TYR   A 1 90  ? 35.660 -19.181 20.865 1.00 24.00  ? 91  TYR   A OH  1 
ATOM   779  N  N   . THR   A 1 91  ? 28.346 -24.004 22.675 1.00 20.34  ? 92  THR   A N   1 
ATOM   780  C  CA  . THR   A 1 91  ? 27.650 -25.301 22.757 1.00 20.68  ? 92  THR   A CA  1 
ATOM   781  C  C   . THR   A 1 91  ? 26.142 -25.299 22.524 1.00 22.75  ? 92  THR   A C   1 
ATOM   782  O  O   . THR   A 1 91  ? 25.582 -26.386 22.317 1.00 22.70  ? 92  THR   A O   1 
ATOM   783  C  CB  . THR   A 1 91  ? 27.849 -25.970 24.158 1.00 24.56  ? 92  THR   A CB  1 
ATOM   784  O  OG1 . THR   A 1 91  ? 27.164 -25.219 25.166 1.00 24.18  ? 92  THR   A OG1 1 
ATOM   785  C  CG2 . THR   A 1 91  ? 29.324 -26.196 24.550 1.00 24.98  ? 92  THR   A CG2 1 
ATOM   786  N  N   A SER   A 1 92  ? 25.491 -24.131 22.604 0.67 19.60  ? 93  SER   A N   1 
ATOM   787  N  N   B SER   A 1 92  ? 25.491 -24.125 22.635 0.33 19.37  ? 93  SER   A N   1 
ATOM   788  C  CA  A SER   A 1 92  ? 24.017 -23.938 22.567 0.67 19.54  ? 93  SER   A CA  1 
ATOM   789  C  CA  B SER   A 1 92  ? 24.031 -23.913 22.579 0.33 19.33  ? 93  SER   A CA  1 
ATOM   790  C  C   A SER   A 1 92  ? 23.363 -24.336 23.914 0.67 22.34  ? 93  SER   A C   1 
ATOM   791  C  C   B SER   A 1 92  ? 23.340 -24.421 23.869 0.33 23.31  ? 93  SER   A C   1 
ATOM   792  O  O   A SER   A 1 92  ? 22.161 -24.138 24.075 0.67 21.55  ? 93  SER   A O   1 
ATOM   793  O  O   B SER   A 1 92  ? 22.110 -24.441 23.936 0.33 23.33  ? 93  SER   A O   1 
ATOM   794  C  CB  A SER   A 1 92  ? 23.342 -24.727 21.438 0.67 21.73  ? 93  SER   A CB  1 
ATOM   795  C  CB  B SER   A 1 92  ? 23.404 -24.546 21.333 0.33 21.71  ? 93  SER   A CB  1 
ATOM   796  O  OG  A SER   A 1 92  ? 23.978 -24.560 20.184 0.67 19.22  ? 93  SER   A OG  1 
ATOM   797  O  OG  B SER   A 1 92  ? 23.086 -25.916 21.528 0.33 24.09  ? 93  SER   A OG  1 
ATOM   798  N  N   A ARG   A 1 93  ? 24.149 -24.849 24.885 0.67 19.92  ? 94  ARG   A N   1 
ATOM   799  N  N   B ARG   A 1 93  ? 24.138 -24.802 24.893 0.33 20.47  ? 94  ARG   A N   1 
ATOM   800  C  CA  A ARG   A 1 93  ? 23.598 -25.288 26.178 0.67 20.92  ? 94  ARG   A CA  1 
ATOM   801  C  CA  B ARG   A 1 93  ? 23.651 -25.336 26.172 0.33 21.42  ? 94  ARG   A CA  1 
ATOM   802  C  C   A ARG   A 1 93  ? 23.843 -24.258 27.237 0.67 25.08  ? 94  ARG   A C   1 
ATOM   803  C  C   B ARG   A 1 93  ? 23.866 -24.305 27.268 0.33 25.32  ? 94  ARG   A C   1 
ATOM   804  O  O   A ARG   A 1 93  ? 24.972 -23.774 27.403 0.67 23.21  ? 94  ARG   A O   1 
ATOM   805  O  O   B ARG   A 1 93  ? 24.996 -23.845 27.467 0.33 24.05  ? 94  ARG   A O   1 
ATOM   806  C  CB  A ARG   A 1 93  ? 24.163 -26.642 26.631 0.67 23.47  ? 94  ARG   A CB  1 
ATOM   807  C  CB  B ARG   A 1 93  ? 24.361 -26.662 26.532 0.33 23.53  ? 94  ARG   A CB  1 
ATOM   808  C  CG  A ARG   A 1 93  ? 23.880 -27.794 25.662 0.67 29.18  ? 94  ARG   A CG  1 
ATOM   809  C  CG  B ARG   A 1 93  ? 24.249 -27.758 25.464 0.33 31.05  ? 94  ARG   A CG  1 
ATOM   810  C  CD  A ARG   A 1 93  ? 24.876 -28.931 25.881 0.67 37.77  ? 94  ARG   A CD  1 
ATOM   811  C  CD  B ARG   A 1 93  ? 23.103 -28.716 25.727 0.33 37.25  ? 94  ARG   A CD  1 
ATOM   812  N  NE  A ARG   A 1 93  ? 24.813 -29.445 27.251 0.67 47.91  ? 94  ARG   A NE  1 
ATOM   813  N  NE  B ARG   A 1 93  ? 22.970 -29.732 24.677 0.33 38.05  ? 94  ARG   A NE  1 
ATOM   814  C  CZ  A ARG   A 1 93  ? 24.018 -30.437 27.636 0.67 59.49  ? 94  ARG   A CZ  1 
ATOM   815  C  CZ  B ARG   A 1 93  ? 23.248 -31.024 24.835 0.33 50.50  ? 94  ARG   A CZ  1 
ATOM   816  N  NH1 A ARG   A 1 93  ? 23.228 -31.043 26.759 0.67 45.19  ? 94  ARG   A NH1 1 
ATOM   817  N  NH1 B ARG   A 1 93  ? 23.084 -31.871 23.827 0.33 39.73  ? 94  ARG   A NH1 1 
ATOM   818  N  NH2 A ARG   A 1 93  ? 24.011 -30.835 28.900 0.67 45.71  ? 94  ARG   A NH2 1 
ATOM   819  N  NH2 B ARG   A 1 93  ? 23.671 -31.482 26.006 0.33 33.10  ? 94  ARG   A NH2 1 
ATOM   820  N  N   . LEU   A 1 94  ? 22.786 -23.938 27.970 1.00 22.36  ? 95  LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 94  ? 22.835 -22.926 29.029 1.00 22.70  ? 95  LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 94  ? 22.603 -23.555 30.388 1.00 27.57  ? 95  LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 94  ? 21.539 -24.139 30.619 1.00 26.88  ? 95  LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 94  ? 21.792 -21.843 28.728 1.00 23.41  ? 95  LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 94  ? 21.789 -20.625 29.679 1.00 26.48  ? 95  LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 94  ? 23.050 -19.764 29.457 1.00 24.43  ? 95  LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 94  ? 20.519 -19.801 29.512 1.00 29.11  ? 95  LEU   A CD2 1 
ATOM   828  N  N   . ASN   A 1 95  ? 23.596 -23.431 31.289 1.00 26.61  ? 96  ASN   A N   1 
ATOM   829  C  CA  . ASN   A 1 95  ? 23.493 -23.983 32.650 1.00 28.35  ? 96  ASN   A CA  1 
ATOM   830  C  C   . ASN   A 1 95  ? 22.791 -22.973 33.575 1.00 33.37  ? 96  ASN   A C   1 
ATOM   831  O  O   . ASN   A 1 95  ? 23.439 -22.269 34.356 1.00 33.16  ? 96  ASN   A O   1 
ATOM   832  C  CB  . ASN   A 1 95  ? 24.877 -24.400 33.179 1.00 32.73  ? 96  ASN   A CB  1 
ATOM   833  C  CG  . ASN   A 1 95  ? 24.832 -25.041 34.556 1.00 49.50  ? 96  ASN   A CG  1 
ATOM   834  O  OD1 . ASN   A 1 95  ? 23.820 -25.606 34.976 1.00 41.23  ? 96  ASN   A OD1 1 
ATOM   835  N  ND2 . ASN   A 1 95  ? 25.926 -24.959 35.288 1.00 43.91  ? 96  ASN   A ND2 1 
ATOM   836  N  N   . LEU   A 1 96  ? 21.478 -22.853 33.409 1.00 30.18  ? 97  LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 96  ? 20.649 -21.916 34.161 1.00 31.82  ? 97  LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 96  ? 20.125 -22.577 35.433 1.00 35.85  ? 97  LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 96  ? 19.477 -23.635 35.379 1.00 34.79  ? 97  LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 96  ? 19.527 -21.412 33.242 1.00 32.71  ? 97  LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 96  ? 18.810 -20.133 33.602 1.00 38.98  ? 97  LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 96  ? 19.808 -18.950 33.737 1.00 39.10  ? 97  LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 96  ? 17.723 -19.837 32.569 1.00 38.55  ? 97  LEU   A CD2 1 
ATOM   844  N  N   . ARG   A 1 97  ? 20.494 -21.994 36.596 1.00 33.74  ? 98  ARG   A N   1 
ATOM   845  C  CA  . ARG   A 1 97  ? 20.137 -22.511 37.925 1.00 35.49  ? 98  ARG   A CA  1 
ATOM   846  C  C   . ARG   A 1 97  ? 19.606 -21.385 38.808 1.00 36.75  ? 98  ARG   A C   1 
ATOM   847  O  O   . ARG   A 1 97  ? 19.955 -20.214 38.593 1.00 33.69  ? 98  ARG   A O   1 
ATOM   848  C  CB  . ARG   A 1 97  ? 21.362 -23.167 38.601 1.00 37.66  ? 98  ARG   A CB  1 
ATOM   849  C  CG  . ARG   A 1 97  ? 21.977 -24.330 37.816 1.00 44.52  ? 98  ARG   A CG  1 
ATOM   850  C  CD  . ARG   A 1 97  ? 23.220 -24.915 38.477 1.00 60.60  ? 98  ARG   A CD  1 
ATOM   851  N  NE  . ARG   A 1 97  ? 22.932 -25.540 39.774 1.00 80.10  ? 98  ARG   A NE  1 
ATOM   852  C  CZ  . ARG   A 1 97  ? 22.496 -26.788 39.937 1.00 101.49 ? 98  ARG   A CZ  1 
ATOM   853  N  NH1 . ARG   A 1 97  ? 22.256 -27.259 41.154 1.00 89.77  ? 98  ARG   A NH1 1 
ATOM   854  N  NH2 . ARG   A 1 97  ? 22.284 -27.570 38.883 1.00 91.84  ? 98  ARG   A NH2 1 
ATOM   855  N  N   . GLU   A 1 98  ? 18.774 -21.722 39.808 1.00 35.52  ? 99  GLU   A N   1 
ATOM   856  C  CA  . GLU   A 1 98  ? 18.227 -20.708 40.729 1.00 35.37  ? 99  GLU   A CA  1 
ATOM   857  C  C   . GLU   A 1 98  ? 19.338 -19.809 41.308 1.00 39.40  ? 99  GLU   A C   1 
ATOM   858  O  O   . GLU   A 1 98  ? 19.176 -18.588 41.367 1.00 40.05  ? 99  GLU   A O   1 
ATOM   859  C  CB  . GLU   A 1 98  ? 17.425 -21.377 41.873 1.00 38.73  ? 99  GLU   A CB  1 
ATOM   860  C  CG  . GLU   A 1 98  ? 16.750 -20.392 42.812 1.00 49.63  ? 99  GLU   A CG  1 
ATOM   861  C  CD  . GLU   A 1 98  ? 15.996 -21.019 43.972 1.00 80.55  ? 99  GLU   A CD  1 
ATOM   862  O  OE1 . GLU   A 1 98  ? 16.545 -21.934 44.630 1.00 73.54  ? 99  GLU   A OE1 1 
ATOM   863  O  OE2 . GLU   A 1 98  ? 14.851 -20.583 44.228 1.00 82.42  ? 99  GLU   A OE2 1 
ATOM   864  N  N   . GLY   A 1 99  ? 20.461 -20.421 41.673 1.00 36.97  ? 100 GLY   A N   1 
ATOM   865  C  CA  . GLY   A 1 99  ? 21.607 -19.726 42.251 1.00 37.66  ? 100 GLY   A CA  1 
ATOM   866  C  C   . GLY   A 1 99  ? 22.398 -18.836 41.310 1.00 39.03  ? 100 GLY   A C   1 
ATOM   867  O  O   . GLY   A 1 99  ? 23.137 -17.963 41.771 1.00 39.10  ? 100 GLY   A O   1 
ATOM   868  N  N   . ASN   A 1 100 ? 22.253 -19.020 39.982 1.00 33.95  ? 101 ASN   A N   1 
ATOM   869  C  CA  . ASN   A 1 100 ? 23.044 -18.204 39.048 1.00 31.89  ? 101 ASN   A CA  1 
ATOM   870  C  C   . ASN   A 1 100 ? 22.210 -17.344 38.088 1.00 34.47  ? 101 ASN   A C   1 
ATOM   871  O  O   . ASN   A 1 100 ? 22.787 -16.550 37.335 1.00 32.70  ? 101 ASN   A O   1 
ATOM   872  C  CB  . ASN   A 1 100 ? 24.023 -19.115 38.272 1.00 31.32  ? 101 ASN   A CB  1 
ATOM   873  C  CG  . ASN   A 1 100 ? 23.376 -20.056 37.270 1.00 41.12  ? 101 ASN   A CG  1 
ATOM   874  O  OD1 . ASN   A 1 100 ? 22.305 -19.778 36.724 1.00 29.62  ? 101 ASN   A OD1 1 
ATOM   875  N  ND2 . ASN   A 1 100 ? 24.027 -21.182 36.982 1.00 33.28  ? 101 ASN   A ND2 1 
ATOM   876  N  N   . ILE   A 1 101 ? 20.868 -17.536 38.066 1.00 31.81  ? 102 ILE   A N   1 
ATOM   877  C  CA  . ILE   A 1 101 ? 19.992 -16.879 37.081 1.00 31.60  ? 102 ILE   A CA  1 
ATOM   878  C  C   . ILE   A 1 101 ? 20.104 -15.359 37.075 1.00 32.83  ? 102 ILE   A C   1 
ATOM   879  O  O   . ILE   A 1 101 ? 20.127 -14.763 35.989 1.00 30.45  ? 102 ILE   A O   1 
ATOM   880  C  CB  . ILE   A 1 101 ? 18.515 -17.336 37.156 1.00 36.14  ? 102 ILE   A CB  1 
ATOM   881  C  CG1 . ILE   A 1 101 ? 17.692 -16.755 35.966 1.00 36.65  ? 102 ILE   A CG1 1 
ATOM   882  C  CG2 . ILE   A 1 101 ? 17.880 -17.057 38.523 1.00 36.54  ? 102 ILE   A CG2 1 
ATOM   883  C  CD1 . ILE   A 1 101 ? 16.533 -17.610 35.510 1.00 39.61  ? 102 ILE   A CD1 1 
ATOM   884  N  N   . MET   A 1 102 ? 20.199 -14.732 38.250 1.00 31.64  ? 103 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 102 ? 20.322 -13.273 38.280 1.00 32.26  ? 103 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 102 ? 21.618 -12.791 37.625 1.00 34.56  ? 103 MET   A C   1 
ATOM   887  O  O   . MET   A 1 102 ? 21.579 -11.837 36.840 1.00 32.05  ? 103 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 102 ? 20.160 -12.714 39.709 1.00 37.14  ? 103 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 102 ? 18.791 -13.006 40.324 1.00 44.17  ? 103 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 102 ? 17.356 -12.647 39.266 1.00 50.40  ? 103 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 102 ? 17.393 -10.846 39.244 1.00 48.55  ? 103 MET   A CE  1 
ATOM   892  N  N   . ALA   A 1 103 ? 22.757 -13.468 37.916 1.00 31.94  ? 104 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 103 ? 24.069 -13.095 37.358 1.00 30.86  ? 104 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 103 ? 24.103 -13.391 35.867 1.00 31.22  ? 104 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 103 ? 24.625 -12.596 35.092 1.00 29.91  ? 104 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 103 ? 25.189 -13.853 38.062 1.00 32.38  ? 104 ALA   A CB  1 
ATOM   897  N  N   . VAL   A 1 104 ? 23.523 -14.532 35.458 1.00 25.62  ? 105 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 104 ? 23.480 -14.883 34.030 1.00 23.97  ? 105 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 104 ? 22.655 -13.844 33.250 1.00 27.26  ? 105 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 104 ? 23.118 -13.396 32.191 1.00 25.88  ? 105 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 104 ? 22.957 -16.335 33.837 1.00 27.79  ? 105 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 104 ? 22.644 -16.638 32.364 1.00 25.85  ? 105 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 104 ? 23.974 -17.335 34.368 1.00 28.67  ? 105 VAL   A CG2 1 
ATOM   904  N  N   A MET   A 1 105 ? 21.454 -13.477 33.752 0.20 26.26  ? 106 MET   A N   1 
ATOM   905  N  N   B MET   A 1 105 ? 21.453 -13.473 33.749 0.80 26.71  ? 106 MET   A N   1 
ATOM   906  C  CA  A MET   A 1 105 ? 20.593 -12.495 33.087 0.20 27.26  ? 106 MET   A CA  1 
ATOM   907  C  CA  B MET   A 1 105 ? 20.620 -12.495 33.041 0.80 28.30  ? 106 MET   A CA  1 
ATOM   908  C  C   A MET   A 1 105 ? 21.296 -11.148 32.946 0.20 31.58  ? 106 MET   A C   1 
ATOM   909  C  C   B MET   A 1 105 ? 21.319 -11.138 32.935 0.80 31.28  ? 106 MET   A C   1 
ATOM   910  O  O   A MET   A 1 105 ? 21.282 -10.571 31.858 0.20 30.47  ? 106 MET   A O   1 
ATOM   911  O  O   B MET   A 1 105 ? 21.311 -10.537 31.862 0.80 29.09  ? 106 MET   A O   1 
ATOM   912  C  CB  A MET   A 1 105 ? 19.253 -12.324 33.812 0.20 31.06  ? 106 MET   A CB  1 
ATOM   913  C  CB  B MET   A 1 105 ? 19.247 -12.328 33.691 0.80 32.31  ? 106 MET   A CB  1 
ATOM   914  C  CG  A MET   A 1 105 ? 18.290 -11.440 33.051 0.20 35.39  ? 106 MET   A CG  1 
ATOM   915  C  CG  B MET   A 1 105 ? 18.320 -11.417 32.888 0.80 36.71  ? 106 MET   A CG  1 
ATOM   916  S  SD  A MET   A 1 105 ? 16.737 -11.163 33.907 0.20 41.25  ? 106 MET   A SD  1 
ATOM   917  S  SD  B MET   A 1 105 ? 16.630 -11.404 33.526 0.80 42.36  ? 106 MET   A SD  1 
ATOM   918  C  CE  A MET   A 1 105 ? 16.211 -9.696  33.094 0.20 38.62  ? 106 MET   A CE  1 
ATOM   919  C  CE  B MET   A 1 105 ? 16.834 -10.390 35.076 0.80 40.58  ? 106 MET   A CE  1 
ATOM   920  N  N   . ALA   A 1 106 ? 21.919 -10.661 34.037 1.00 29.41  ? 107 ALA   A N   1 
ATOM   921  C  CA  . ALA   A 1 106 ? 22.654 -9.377  34.042 1.00 29.75  ? 107 ALA   A CA  1 
ATOM   922  C  C   . ALA   A 1 106 ? 23.824 -9.406  33.023 1.00 30.92  ? 107 ALA   A C   1 
ATOM   923  O  O   . ALA   A 1 106 ? 24.029 -8.438  32.264 1.00 29.04  ? 107 ALA   A O   1 
ATOM   924  C  CB  . ALA   A 1 106 ? 23.171 -9.077  35.441 1.00 31.25  ? 107 ALA   A CB  1 
ATOM   925  N  N   . THR   A 1 107 ? 24.562 -10.533 32.987 1.00 25.91  ? 108 THR   A N   1 
ATOM   926  C  CA  . THR   A 1 107 ? 25.670 -10.704 32.044 1.00 25.12  ? 108 THR   A CA  1 
ATOM   927  C  C   . THR   A 1 107 ? 25.128 -10.732 30.597 1.00 26.66  ? 108 THR   A C   1 
ATOM   928  O  O   . THR   A 1 107 ? 25.702 -10.069 29.739 1.00 24.73  ? 108 THR   A O   1 
ATOM   929  C  CB  . THR   A 1 107 ? 26.583 -11.905 32.402 1.00 29.31  ? 108 THR   A CB  1 
ATOM   930  O  OG1 . THR   A 1 107 ? 26.898 -11.884 33.798 1.00 29.23  ? 108 THR   A OG1 1 
ATOM   931  C  CG2 . THR   A 1 107 ? 27.892 -11.916 31.594 1.00 29.59  ? 108 THR   A CG2 1 
ATOM   932  N  N   . ALA   A 1 108 ? 24.027 -11.481 30.326 1.00 23.93  ? 109 ALA   A N   1 
ATOM   933  C  CA  . ALA   A 1 108 ? 23.453 -11.547 28.966 1.00 22.84  ? 109 ALA   A CA  1 
ATOM   934  C  C   . ALA   A 1 108 ? 22.924 -10.186 28.499 1.00 26.07  ? 109 ALA   A C   1 
ATOM   935  O  O   . ALA   A 1 108 ? 23.065 -9.842  27.320 1.00 24.98  ? 109 ALA   A O   1 
ATOM   936  C  CB  . ALA   A 1 108 ? 22.362 -12.614 28.893 1.00 23.83  ? 109 ALA   A CB  1 
ATOM   937  N  N   . MET   A 1 109 ? 22.385 -9.372  29.424 1.00 25.40  ? 110 MET   A N   1 
ATOM   938  C  CA  . MET   A 1 109 ? 21.933 -8.030  29.040 1.00 25.47  ? 110 MET   A CA  1 
ATOM   939  C  C   . MET   A 1 109 ? 23.129 -7.162  28.609 1.00 27.88  ? 110 MET   A C   1 
ATOM   940  O  O   . MET   A 1 109 ? 23.093 -6.513  27.560 1.00 28.34  ? 110 MET   A O   1 
ATOM   941  C  CB  . MET   A 1 109 ? 21.153 -7.373  30.194 1.00 28.55  ? 110 MET   A CB  1 
ATOM   942  C  CG  . MET   A 1 109 ? 19.777 -7.997  30.426 1.00 33.13  ? 110 MET   A CG  1 
ATOM   943  S  SD  . MET   A 1 109 ? 19.034 -7.395  31.970 1.00 40.77  ? 110 MET   A SD  1 
ATOM   944  C  CE  . MET   A 1 109 ? 18.744 -5.669  31.526 1.00 38.43  ? 110 MET   A CE  1 
ATOM   945  N  N   . TYR   A 1 110 ? 24.200 -7.200  29.396 1.00 26.25  ? 111 TYR   A N   1 
ATOM   946  C  CA  . TYR   A 1 110 ? 25.444 -6.465  29.122 1.00 25.59  ? 111 TYR   A CA  1 
ATOM   947  C  C   . TYR   A 1 110 ? 26.056 -6.930  27.778 1.00 27.69  ? 111 TYR   A C   1 
ATOM   948  O  O   . TYR   A 1 110 ? 26.455 -6.101  26.956 1.00 26.46  ? 111 TYR   A O   1 
ATOM   949  C  CB  . TYR   A 1 110 ? 26.425 -6.735  30.261 1.00 25.56  ? 111 TYR   A CB  1 
ATOM   950  C  CG  . TYR   A 1 110 ? 27.830 -6.224  30.021 1.00 25.49  ? 111 TYR   A CG  1 
ATOM   951  C  CD1 . TYR   A 1 110 ? 28.125 -4.863  30.112 1.00 28.37  ? 111 TYR   A CD1 1 
ATOM   952  C  CD2 . TYR   A 1 110 ? 28.883 -7.108  29.787 1.00 25.21  ? 111 TYR   A CD2 1 
ATOM   953  C  CE1 . TYR   A 1 110 ? 29.427 -4.389  29.903 1.00 27.80  ? 111 TYR   A CE1 1 
ATOM   954  C  CE2 . TYR   A 1 110 ? 30.187 -6.651  29.615 1.00 25.62  ? 111 TYR   A CE2 1 
ATOM   955  C  CZ  . TYR   A 1 110 ? 30.454 -5.291  29.686 1.00 28.27  ? 111 TYR   A CZ  1 
ATOM   956  O  OH  . TYR   A 1 110 ? 31.744 -4.871  29.546 1.00 28.05  ? 111 TYR   A OH  1 
ATOM   957  N  N   . LEU   A 1 111 ? 26.117 -8.259  27.564 1.00 23.74  ? 112 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 111 ? 26.674 -8.844  26.343 1.00 22.33  ? 112 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 111 ? 25.747 -8.712  25.135 1.00 26.04  ? 112 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 111 ? 26.166 -9.001  24.011 1.00 25.60  ? 112 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 111 ? 27.073 -10.315 26.574 1.00 21.05  ? 112 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 111 ? 28.227 -10.585 27.571 1.00 23.52  ? 112 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 111 ? 28.512 -12.102 27.664 1.00 24.54  ? 112 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 111 ? 29.531 -9.827  27.175 1.00 24.76  ? 112 LEU   A CD2 1 
ATOM   965  N  N   . GLN   A 1 112 ? 24.478 -8.318  25.357 1.00 23.34  ? 113 GLN   A N   1 
ATOM   966  C  CA  . GLN   A 1 112 ? 23.479 -8.193  24.286 1.00 24.32  ? 113 GLN   A CA  1 
ATOM   967  C  C   . GLN   A 1 112 ? 23.228 -9.552  23.602 1.00 26.80  ? 113 GLN   A C   1 
ATOM   968  O  O   . GLN   A 1 112 ? 23.481 -9.735  22.404 1.00 25.83  ? 113 GLN   A O   1 
ATOM   969  C  CB  . GLN   A 1 112 ? 23.857 -7.096  23.273 1.00 25.78  ? 113 GLN   A CB  1 
ATOM   970  C  CG  . GLN   A 1 112 ? 24.006 -5.708  23.913 1.00 27.35  ? 113 GLN   A CG  1 
ATOM   971  C  CD  . GLN   A 1 112 ? 24.716 -4.747  22.989 1.00 37.47  ? 113 GLN   A CD  1 
ATOM   972  O  OE1 . GLN   A 1 112 ? 24.619 -4.844  21.772 1.00 32.05  ? 113 GLN   A OE1 1 
ATOM   973  N  NE2 . GLN   A 1 112 ? 25.469 -3.815  23.541 1.00 37.44  ? 113 GLN   A NE2 1 
ATOM   974  N  N   . MET   A 1 113 ? 22.785 -10.515 24.407 1.00 23.90  ? 114 MET   A N   1 
ATOM   975  C  CA  . MET   A 1 113 ? 22.444 -11.887 23.988 1.00 23.89  ? 114 MET   A CA  1 
ATOM   976  C  C   . MET   A 1 113 ? 20.945 -12.046 24.252 1.00 29.80  ? 114 MET   A C   1 
ATOM   977  O  O   . MET   A 1 113 ? 20.508 -12.507 25.321 1.00 27.39  ? 114 MET   A O   1 
ATOM   978  C  CB  . MET   A 1 113 ? 23.288 -12.893 24.771 1.00 25.30  ? 114 MET   A CB  1 
ATOM   979  C  CG  . MET   A 1 113 ? 24.777 -12.741 24.493 1.00 26.52  ? 114 MET   A CG  1 
ATOM   980  S  SD  . MET   A 1 113 ? 25.822 -13.797 25.505 1.00 28.60  ? 114 MET   A SD  1 
ATOM   981  C  CE  . MET   A 1 113 ? 25.477 -15.474 24.724 1.00 25.70  ? 114 MET   A CE  1 
ATOM   982  N  N   . GLU   A 1 114 ? 20.154 -11.552 23.293 1.00 29.91  ? 115 GLU   A N   1 
ATOM   983  C  CA  . GLU   A 1 114 ? 18.692 -11.414 23.408 1.00 31.42  ? 115 GLU   A CA  1 
ATOM   984  C  C   . GLU   A 1 114 ? 17.922 -12.689 23.759 1.00 32.11  ? 115 GLU   A C   1 
ATOM   985  O  O   . GLU   A 1 114 ? 17.013 -12.612 24.579 1.00 31.28  ? 115 GLU   A O   1 
ATOM   986  C  CB  . GLU   A 1 114 ? 18.094 -10.782 22.138 1.00 34.52  ? 115 GLU   A CB  1 
ATOM   987  C  CG  . GLU   A 1 114 ? 18.614 -9.379  21.876 1.00 47.73  ? 115 GLU   A CG  1 
ATOM   988  N  N   . HIS   A 1 115 ? 18.261 -13.838 23.153 1.00 28.85  ? 116 HIS   A N   1 
ATOM   989  C  CA  . HIS   A 1 115 ? 17.532 -15.079 23.440 1.00 30.32  ? 116 HIS   A CA  1 
ATOM   990  C  C   . HIS   A 1 115 ? 17.764 -15.560 24.875 1.00 31.30  ? 116 HIS   A C   1 
ATOM   991  O  O   . HIS   A 1 115 ? 16.824 -16.032 25.530 1.00 31.90  ? 116 HIS   A O   1 
ATOM   992  C  CB  . HIS   A 1 115 ? 17.861 -16.158 22.408 1.00 32.40  ? 116 HIS   A CB  1 
ATOM   993  C  CG  . HIS   A 1 115 ? 17.414 -15.798 21.027 1.00 37.51  ? 116 HIS   A CG  1 
ATOM   994  N  ND1 . HIS   A 1 115 ? 16.083 -15.536 20.747 1.00 41.28  ? 116 HIS   A ND1 1 
ATOM   995  C  CD2 . HIS   A 1 115 ? 18.129 -15.699 19.883 1.00 39.20  ? 116 HIS   A CD2 1 
ATOM   996  C  CE1 . HIS   A 1 115 ? 16.035 -15.257 19.454 1.00 41.16  ? 116 HIS   A CE1 1 
ATOM   997  N  NE2 . HIS   A 1 115 ? 17.240 -15.352 18.890 1.00 40.14  ? 116 HIS   A NE2 1 
ATOM   998  N  N   . VAL   A 1 116 ? 19.008 -15.406 25.376 1.00 24.96  ? 117 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 116 ? 19.331 -15.755 26.768 1.00 25.41  ? 117 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 116 ? 18.543 -14.841 27.728 1.00 31.11  ? 117 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 116 ? 17.915 -15.343 28.674 1.00 28.58  ? 117 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 116 ? 20.856 -15.742 27.070 1.00 27.89  ? 117 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 116 ? 21.113 -15.963 28.565 1.00 27.62  ? 117 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 116 ? 21.592 -16.784 26.227 1.00 27.38  ? 117 VAL   A CG2 1 
ATOM   1005 N  N   . VAL   A 1 117 ? 18.557 -13.506 27.484 1.00 27.88  ? 118 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 117 ? 17.801 -12.551 28.319 1.00 28.19  ? 118 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 117 ? 16.322 -12.982 28.390 1.00 33.46  ? 118 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 117 ? 15.784 -13.092 29.483 1.00 33.16  ? 118 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 117 ? 17.967 -11.075 27.855 1.00 31.33  ? 118 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 117 ? 17.117 -10.116 28.709 1.00 32.31  ? 118 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 117 ? 19.433 -10.655 27.894 1.00 30.02  ? 118 VAL   A CG2 1 
ATOM   1012 N  N   A ASP   A 1 118 ? 15.726 -13.322 27.234 0.61 31.74  ? 119 ASP   A N   1 
ATOM   1013 N  N   B ASP   A 1 118 ? 15.686 -13.205 27.221 0.39 31.54  ? 119 ASP   A N   1 
ATOM   1014 C  CA  A ASP   A 1 118 ? 14.342 -13.790 27.114 0.61 33.16  ? 119 ASP   A CA  1 
ATOM   1015 C  CA  B ASP   A 1 118 ? 14.282 -13.616 27.080 0.39 32.97  ? 119 ASP   A CA  1 
ATOM   1016 C  C   A ASP   A 1 118 ? 14.027 -15.023 27.982 0.61 36.52  ? 119 ASP   A C   1 
ATOM   1017 C  C   B ASP   A 1 118 ? 13.912 -14.825 27.944 0.39 37.09  ? 119 ASP   A C   1 
ATOM   1018 O  O   A ASP   A 1 118 ? 13.038 -14.985 28.719 0.61 37.23  ? 119 ASP   A O   1 
ATOM   1019 O  O   B ASP   A 1 118 ? 12.895 -14.787 28.639 0.39 38.03  ? 119 ASP   A O   1 
ATOM   1020 C  CB  A ASP   A 1 118 ? 13.988 -14.051 25.640 0.61 35.52  ? 119 ASP   A CB  1 
ATOM   1021 C  CB  B ASP   A 1 118 ? 13.956 -13.915 25.603 0.39 35.07  ? 119 ASP   A CB  1 
ATOM   1022 C  CG  A ASP   A 1 118 ? 12.536 -14.430 25.412 0.61 50.00  ? 119 ASP   A CG  1 
ATOM   1023 C  CG  B ASP   A 1 118 ? 13.714 -12.708 24.714 0.39 47.46  ? 119 ASP   A CG  1 
ATOM   1024 O  OD1 A ASP   A 1 118 ? 11.651 -13.606 25.729 0.61 53.67  ? 119 ASP   A OD1 1 
ATOM   1025 O  OD1 B ASP   A 1 118 ? 13.300 -11.654 25.242 0.39 50.13  ? 119 ASP   A OD1 1 
ATOM   1026 O  OD2 A ASP   A 1 118 ? 12.287 -15.545 24.911 0.61 56.14  ? 119 ASP   A OD2 1 
ATOM   1027 O  OD2 B ASP   A 1 118 ? 13.913 -12.827 23.486 0.39 53.75  ? 119 ASP   A OD2 1 
ATOM   1028 N  N   A THR   A 1 119 ? 14.855 -16.099 27.918 0.61 31.88  ? 120 THR   A N   1 
ATOM   1029 N  N   B THR   A 1 119 ? 14.745 -15.884 27.910 0.39 32.42  ? 120 THR   A N   1 
ATOM   1030 C  CA  A THR   A 1 119 ? 14.582 -17.293 28.742 0.61 32.01  ? 120 THR   A CA  1 
ATOM   1031 C  CA  B THR   A 1 119 ? 14.508 -17.121 28.659 0.39 32.64  ? 120 THR   A CA  1 
ATOM   1032 C  C   A THR   A 1 119 ? 14.773 -17.009 30.227 0.61 34.64  ? 120 THR   A C   1 
ATOM   1033 C  C   B THR   A 1 119 ? 14.700 -16.906 30.168 0.39 35.33  ? 120 THR   A C   1 
ATOM   1034 O  O   A THR   A 1 119 ? 14.071 -17.600 31.043 0.61 34.61  ? 120 THR   A O   1 
ATOM   1035 O  O   B THR   A 1 119 ? 13.906 -17.435 30.945 0.39 35.67  ? 120 THR   A O   1 
ATOM   1036 C  CB  A THR   A 1 119 ? 15.338 -18.556 28.291 0.61 31.83  ? 120 THR   A CB  1 
ATOM   1037 C  CB  B THR   A 1 119 ? 15.324 -18.283 28.083 0.39 37.20  ? 120 THR   A CB  1 
ATOM   1038 O  OG1 A THR   A 1 119 ? 14.710 -19.684 28.910 0.61 33.22  ? 120 THR   A OG1 1 
ATOM   1039 O  OG1 B THR   A 1 119 ? 15.312 -18.197 26.655 0.39 35.85  ? 120 THR   A OG1 1 
ATOM   1040 C  CG2 A THR   A 1 119 ? 16.826 -18.541 28.663 0.61 27.02  ? 120 THR   A CG2 1 
ATOM   1041 C  CG2 B THR   A 1 119 ? 14.767 -19.634 28.494 0.39 37.08  ? 120 THR   A CG2 1 
ATOM   1042 N  N   . CYS   A 1 120 ? 15.724 -16.116 30.579 1.00 30.99  ? 121 CYS   A N   1 
ATOM   1043 C  CA  . CYS   A 1 120 ? 15.957 -15.759 31.997 1.00 31.50  ? 121 CYS   A CA  1 
ATOM   1044 C  C   . CYS   A 1 120 ? 14.736 -15.056 32.551 1.00 37.77  ? 121 CYS   A C   1 
ATOM   1045 O  O   . CYS   A 1 120 ? 14.272 -15.419 33.642 1.00 36.01  ? 121 CYS   A O   1 
ATOM   1046 C  CB  . CYS   A 1 120 ? 17.198 -14.887 32.143 1.00 31.06  ? 121 CYS   A CB  1 
ATOM   1047 S  SG  . CYS   A 1 120 ? 18.741 -15.788 31.917 1.00 33.47  ? 121 CYS   A SG  1 
ATOM   1048 N  N   A ARG   A 1 121 ? 14.195 -14.078 31.783 0.48 35.81  ? 122 ARG   A N   1 
ATOM   1049 N  N   B ARG   A 1 121 ? 14.200 -14.064 31.801 0.52 36.12  ? 122 ARG   A N   1 
ATOM   1050 C  CA  A ARG   A 1 121 ? 12.993 -13.309 32.122 0.48 37.42  ? 122 ARG   A CA  1 
ATOM   1051 C  CA  B ARG   A 1 121 ? 13.000 -13.317 32.182 0.52 37.88  ? 122 ARG   A CA  1 
ATOM   1052 C  C   A ARG   A 1 121 ? 11.808 -14.246 32.381 0.48 41.24  ? 122 ARG   A C   1 
ATOM   1053 C  C   B ARG   A 1 121 ? 11.801 -14.253 32.396 0.52 41.40  ? 122 ARG   A C   1 
ATOM   1054 O  O   A ARG   A 1 121 ? 11.093 -14.074 33.371 0.48 41.43  ? 122 ARG   A O   1 
ATOM   1055 O  O   B ARG   A 1 121 ? 11.073 -14.092 33.377 0.52 41.50  ? 122 ARG   A O   1 
ATOM   1056 C  CB  A ARG   A 1 121 ? 12.636 -12.325 30.992 0.48 38.69  ? 122 ARG   A CB  1 
ATOM   1057 C  CB  B ARG   A 1 121 ? 12.669 -12.237 31.144 0.52 39.86  ? 122 ARG   A CB  1 
ATOM   1058 C  CG  A ARG   A 1 121 ? 13.580 -11.142 30.869 0.48 50.93  ? 122 ARG   A CG  1 
ATOM   1059 C  CG  B ARG   A 1 121 ? 13.425 -10.932 31.361 0.52 54.38  ? 122 ARG   A CG  1 
ATOM   1060 C  CD  A ARG   A 1 121 ? 12.962 -10.003 30.077 0.48 63.61  ? 122 ARG   A CD  1 
ATOM   1061 C  CD  B ARG   A 1 121 ? 12.700 -9.753  30.732 0.52 66.34  ? 122 ARG   A CD  1 
ATOM   1062 N  NE  A ARG   A 1 121 ? 13.960 -8.999  29.699 0.48 68.11  ? 122 ARG   A NE  1 
ATOM   1063 N  NE  B ARG   A 1 121 ? 12.847 -9.725  29.274 0.52 71.82  ? 122 ARG   A NE  1 
ATOM   1064 C  CZ  A ARG   A 1 121 ? 14.315 -7.962  30.451 0.48 78.84  ? 122 ARG   A CZ  1 
ATOM   1065 C  CZ  B ARG   A 1 121 ? 13.631 -8.879  28.612 0.52 81.72  ? 122 ARG   A CZ  1 
ATOM   1066 N  NH1 A ARG   A 1 121 ? 13.751 -7.767  31.637 0.48 70.43  ? 122 ARG   A NH1 1 
ATOM   1067 N  NH1 B ARG   A 1 121 ? 14.343 -7.969  29.268 0.52 65.36  ? 122 ARG   A NH1 1 
ATOM   1068 N  NH2 A ARG   A 1 121 ? 15.236 -7.110  30.022 0.48 59.87  ? 122 ARG   A NH2 1 
ATOM   1069 N  NH2 B ARG   A 1 121 ? 13.704 -8.931  27.289 0.52 66.69  ? 122 ARG   A NH2 1 
ATOM   1070 N  N   . LYS   A 1 122 ? 11.631 -15.254 31.507 1.00 37.11  ? 123 LYS   A N   1 
ATOM   1071 C  CA  . LYS   A 1 122 ? 10.541 -16.245 31.599 1.00 38.98  ? 123 LYS   A CA  1 
ATOM   1072 C  C   . LYS   A 1 122 ? 10.685 -17.165 32.812 1.00 43.01  ? 123 LYS   A C   1 
ATOM   1073 O  O   . LYS   A 1 122 ? 9.694  -17.401 33.503 1.00 43.07  ? 123 LYS   A O   1 
ATOM   1074 C  CB  . LYS   A 1 122 ? 10.400 -17.044 30.295 1.00 40.97  ? 123 LYS   A CB  1 
ATOM   1075 C  CG  . LYS   A 1 122 ? 9.857  -16.187 29.157 1.00 61.36  ? 123 LYS   A CG  1 
ATOM   1076 C  CD  . LYS   A 1 122 ? 9.740  -16.928 27.842 1.00 73.28  ? 123 LYS   A CD  1 
ATOM   1077 C  CE  . LYS   A 1 122 ? 9.304  -15.982 26.747 1.00 87.37  ? 123 LYS   A CE  1 
ATOM   1078 N  NZ  . LYS   A 1 122 ? 8.457  -16.659 25.733 1.00 99.89  ? 123 LYS   A NZ  1 
ATOM   1079 N  N   . PHE   A 1 123 ? 11.919 -17.645 33.096 1.00 38.62  ? 124 PHE   A N   1 
ATOM   1080 C  CA  . PHE   A 1 123 ? 12.189 -18.510 34.254 1.00 38.75  ? 124 PHE   A CA  1 
ATOM   1081 C  C   . PHE   A 1 123 ? 12.001 -17.744 35.561 1.00 43.39  ? 124 PHE   A C   1 
ATOM   1082 O  O   . PHE   A 1 123 ? 11.450 -18.297 36.519 1.00 42.91  ? 124 PHE   A O   1 
ATOM   1083 C  CB  . PHE   A 1 123 ? 13.590 -19.132 34.166 1.00 38.98  ? 124 PHE   A CB  1 
ATOM   1084 C  CG  . PHE   A 1 123 ? 13.714 -20.399 33.336 1.00 40.64  ? 124 PHE   A CG  1 
ATOM   1085 C  CD1 . PHE   A 1 123 ? 13.149 -20.482 32.063 1.00 43.82  ? 124 PHE   A CD1 1 
ATOM   1086 C  CD2 . PHE   A 1 123 ? 14.452 -21.484 33.800 1.00 43.11  ? 124 PHE   A CD2 1 
ATOM   1087 C  CE1 . PHE   A 1 123 ? 13.287 -21.644 31.290 1.00 44.36  ? 124 PHE   A CE1 1 
ATOM   1088 C  CE2 . PHE   A 1 123 ? 14.588 -22.647 33.024 1.00 45.00  ? 124 PHE   A CE2 1 
ATOM   1089 C  CZ  . PHE   A 1 123 ? 14.001 -22.719 31.779 1.00 42.71  ? 124 PHE   A CZ  1 
ATOM   1090 N  N   . ILE   A 1 124 ? 12.399 -16.457 35.586 1.00 38.40  ? 125 ILE   A N   1 
ATOM   1091 C  CA  . ILE   A 1 124 ? 12.198 -15.607 36.775 1.00 39.66  ? 125 ILE   A CA  1 
ATOM   1092 C  C   . ILE   A 1 124 ? 10.699 -15.351 37.025 1.00 47.70  ? 125 ILE   A C   1 
ATOM   1093 O  O   . ILE   A 1 124 ? 10.245 -15.498 38.167 1.00 49.46  ? 125 ILE   A O   1 
ATOM   1094 C  CB  . ILE   A 1 124 ? 13.047 -14.312 36.699 1.00 41.85  ? 125 ILE   A CB  1 
ATOM   1095 C  CG1 . ILE   A 1 124 ? 14.542 -14.672 36.804 1.00 40.64  ? 125 ILE   A CG1 1 
ATOM   1096 C  CG2 . ILE   A 1 124 ? 12.645 -13.295 37.803 1.00 44.76  ? 125 ILE   A CG2 1 
ATOM   1097 C  CD1 . ILE   A 1 124 ? 15.502 -13.612 36.298 1.00 44.96  ? 125 ILE   A CD1 1 
ATOM   1098 N  N   . LYS   A 1 125 ? 9.933  -15.026 35.954 1.00 45.71  ? 126 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 125 ? 8.489  -14.772 36.027 1.00 48.41  ? 126 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 125 ? 7.722  -15.994 36.555 1.00 53.26  ? 126 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 125 ? 6.757  -15.825 37.295 1.00 53.54  ? 126 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 125 ? 7.932  -14.340 34.663 1.00 51.68  ? 126 LYS   A CB  1 
ATOM   1103 N  N   . ALA   A 1 126 ? 8.175  -17.215 36.206 1.00 48.83  ? 127 ALA   A N   1 
ATOM   1104 C  CA  . ALA   A 1 126 ? 7.543  -18.457 36.668 1.00 50.27  ? 127 ALA   A CA  1 
ATOM   1105 C  C   . ALA   A 1 126 ? 7.701  -18.692 38.184 1.00 56.42  ? 127 ALA   A C   1 
ATOM   1106 O  O   . ALA   A 1 126 ? 6.822  -19.289 38.792 1.00 56.96  ? 127 ALA   A O   1 
ATOM   1107 C  CB  . ALA   A 1 126 ? 8.095  -19.646 35.892 1.00 49.53  ? 127 ALA   A CB  1 
ATOM   1108 N  N   . SER   A 1 127 ? 8.821  -18.248 38.779 1.00 55.07  ? 128 SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 127 ? 9.112  -18.450 40.202 1.00 57.89  ? 128 SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 127 ? 8.516  -17.386 41.141 1.00 66.35  ? 128 SER   A C   1 
ATOM   1111 O  O   . SER   A 1 127 ? 8.483  -17.614 42.354 1.00 68.57  ? 128 SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 127 ? 10.616 -18.584 40.427 1.00 61.47  ? 128 SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 127 ? 11.043 -19.920 40.207 1.00 71.79  ? 128 SER   A OG  1 
ATOM   1114 N  N   . GLU   A 1 128 ? 8.023  -16.248 40.598 1.00 63.16  ? 129 GLU   A N   1 
ATOM   1115 C  CA  . GLU   A 1 128 ? 7.438  -15.167 41.406 1.00 83.97  ? 129 GLU   A CA  1 
ATOM   1116 C  C   . GLU   A 1 128 ? 6.003  -15.465 41.875 1.00 125.33 ? 129 GLU   A C   1 
ATOM   1117 O  O   . GLU   A 1 128 ? 5.590  -16.621 41.962 1.00 92.09  ? 129 GLU   A O   1 
ATOM   1118 C  CB  . GLU   A 1 128 ? 7.525  -13.808 40.682 1.00 84.55  ? 129 GLU   A CB  1 
ATOM   1119 C  CG  . GLU   A 1 128 ? 6.486  -13.586 39.591 1.00 94.50  ? 129 GLU   A CG  1 
ATOM   1120 C  CD  . GLU   A 1 128 ? 6.643  -12.349 38.725 1.00 114.50 ? 129 GLU   A CD  1 
ATOM   1121 O  OE1 . GLU   A 1 128 ? 7.775  -11.820 38.618 1.00 105.86 ? 129 GLU   A OE1 1 
ATOM   1122 O  OE2 . GLU   A 1 128 ? 5.626  -11.917 38.135 1.00 108.09 ? 129 GLU   A OE2 1 
HETATM 1123 C  C   . ACE   B 2 1   ? 21.244 -35.167 5.845  1.00 28.72  ? 0   ACE   D C   1 
HETATM 1124 O  O   . ACE   B 2 1   ? 21.327 -34.032 6.339  1.00 29.56  ? 0   ACE   D O   1 
HETATM 1125 C  CH3 . ACE   B 2 1   ? 21.445 -36.399 6.710  1.00 28.24  ? 0   ACE   D CH3 1 
ATOM   1126 N  N   A TRP   B 2 2   ? 20.969 -35.392 4.561  0.66 26.24  ? 1   TRP   D N   1 
ATOM   1127 N  N   B TRP   B 2 2   ? 20.981 -35.391 4.558  0.34 27.61  ? 1   TRP   D N   1 
ATOM   1128 C  CA  A TRP   B 2 2   ? 20.758 -34.328 3.579  0.66 25.29  ? 1   TRP   D CA  1 
ATOM   1129 C  CA  B TRP   B 2 2   ? 20.714 -34.308 3.612  0.34 27.43  ? 1   TRP   D CA  1 
ATOM   1130 C  C   A TRP   B 2 2   ? 19.247 -34.172 3.292  0.66 29.61  ? 1   TRP   D C   1 
ATOM   1131 C  C   B TRP   B 2 2   ? 19.208 -34.147 3.438  0.34 29.77  ? 1   TRP   D C   1 
ATOM   1132 O  O   A TRP   B 2 2   ? 18.527 -35.174 3.234  0.66 29.42  ? 1   TRP   D O   1 
ATOM   1133 O  O   B TRP   B 2 2   ? 18.459 -35.125 3.548  0.34 28.91  ? 1   TRP   D O   1 
ATOM   1134 C  CB  A TRP   B 2 2   ? 21.552 -34.633 2.283  0.66 24.21  ? 1   TRP   D CB  1 
ATOM   1135 C  CB  B TRP   B 2 2   ? 21.399 -34.536 2.241  0.34 26.97  ? 1   TRP   D CB  1 
ATOM   1136 C  CG  A TRP   B 2 2   ? 23.052 -34.615 2.470  0.66 24.27  ? 1   TRP   D CG  1 
ATOM   1137 C  CG  B TRP   B 2 2   ? 20.773 -35.601 1.388  0.34 28.38  ? 1   TRP   D CG  1 
ATOM   1138 C  CD1 A TRP   B 2 2   ? 23.843 -35.651 2.878  0.66 26.49  ? 1   TRP   D CD1 1 
ATOM   1139 C  CD1 B TRP   B 2 2   ? 21.119 -36.917 1.343  0.34 31.53  ? 1   TRP   D CD1 1 
ATOM   1140 C  CD2 A TRP   B 2 2   ? 23.935 -33.503 2.245  0.66 24.16  ? 1   TRP   D CD2 1 
ATOM   1141 C  CD2 B TRP   B 2 2   ? 19.690 -35.437 0.458  0.34 28.39  ? 1   TRP   D CD2 1 
ATOM   1142 N  NE1 A TRP   B 2 2   ? 25.152 -35.233 2.988  0.66 25.26  ? 1   TRP   D NE1 1 
ATOM   1143 N  NE1 B TRP   B 2 2   ? 20.305 -37.592 0.466  0.34 31.22  ? 1   TRP   D NE1 1 
ATOM   1144 C  CE2 A TRP   B 2 2   ? 25.242 -33.930 2.577  0.66 26.51  ? 1   TRP   D CE2 1 
ATOM   1145 C  CE2 B TRP   B 2 2   ? 19.420 -36.708 -0.097 0.34 32.52  ? 1   TRP   D CE2 1 
ATOM   1146 C  CE3 A TRP   B 2 2   ? 23.739 -32.164 1.863  0.66 25.11  ? 1   TRP   D CE3 1 
ATOM   1147 C  CE3 B TRP   B 2 2   ? 18.897 -34.344 0.062  0.34 29.37  ? 1   TRP   D CE3 1 
ATOM   1148 C  CZ2 A TRP   B 2 2   ? 26.360 -33.094 2.446  0.66 26.19  ? 1   TRP   D CZ2 1 
ATOM   1149 C  CZ2 B TRP   B 2 2   ? 18.407 -36.914 -1.041 0.34 31.87  ? 1   TRP   D CZ2 1 
ATOM   1150 C  CZ3 A TRP   B 2 2   ? 24.849 -31.344 1.715  0.66 26.15  ? 1   TRP   D CZ3 1 
ATOM   1151 C  CZ3 B TRP   B 2 2   ? 17.883 -34.554 -0.861 0.34 30.97  ? 1   TRP   D CZ3 1 
ATOM   1152 C  CH2 A TRP   B 2 2   ? 26.135 -31.800 2.032  0.66 26.54  ? 1   TRP   D CH2 1 
ATOM   1153 C  CH2 B TRP   B 2 2   ? 17.648 -35.824 -1.405 0.34 31.57  ? 1   TRP   D CH2 1 
ATOM   1154 N  N   . VAL   B 2 3   ? 18.765 -32.924 3.141  1.00 25.30  ? 2   VAL   D N   1 
ATOM   1155 C  CA  . VAL   B 2 3   ? 17.334 -32.627 2.901  1.00 25.43  ? 2   VAL   D CA  1 
ATOM   1156 C  C   . VAL   B 2 3   ? 17.188 -31.573 1.796  1.00 27.29  ? 2   VAL   D C   1 
ATOM   1157 O  O   . VAL   B 2 3   ? 18.161 -30.886 1.455  1.00 26.59  ? 2   VAL   D O   1 
ATOM   1158 C  CB  . VAL   B 2 3   ? 16.626 -32.120 4.210  1.00 28.64  ? 2   VAL   D CB  1 
ATOM   1159 C  CG1 . VAL   B 2 3   ? 16.655 -33.176 5.324  1.00 28.85  ? 2   VAL   D CG1 1 
ATOM   1160 C  CG2 . VAL   B 2 3   ? 17.224 -30.786 4.706  1.00 27.90  ? 2   VAL   D CG2 1 
ATOM   1161 N  N   . ILE   B 2 4   ? 15.951 -31.385 1.334  1.00 25.63  ? 3   ILE   D N   1 
ATOM   1162 C  CA  . ILE   B 2 4   ? 15.561 -30.304 0.441  1.00 25.51  ? 3   ILE   D CA  1 
ATOM   1163 C  C   . ILE   B 2 4   ? 15.187 -29.162 1.424  1.00 29.81  ? 3   ILE   D C   1 
ATOM   1164 O  O   . ILE   B 2 4   ? 14.169 -29.283 2.125  1.00 29.77  ? 3   ILE   D O   1 
ATOM   1165 C  CB  . ILE   B 2 4   ? 14.351 -30.682 -0.467 1.00 27.39  ? 3   ILE   D CB  1 
ATOM   1166 C  CG1 . ILE   B 2 4   ? 14.647 -31.959 -1.349 1.00 25.21  ? 3   ILE   D CG1 1 
ATOM   1167 C  CG2 . ILE   B 2 4   ? 13.936 -29.451 -1.325 1.00 29.82  ? 3   ILE   D CG2 1 
ATOM   1168 C  CD1 . ILE   B 2 4   ? 15.919 -31.848 -2.326 1.00 30.24  ? 3   ILE   D CD1 1 
ATOM   1169 N  N   . PRO   B 2 5   ? 15.970 -28.062 1.507  1.00 28.83  ? 4   PRO   D N   1 
ATOM   1170 C  CA  . PRO   B 2 5   ? 15.637 -27.002 2.479  1.00 29.53  ? 4   PRO   D CA  1 
ATOM   1171 C  C   . PRO   B 2 5   ? 14.389 -26.200 2.102  1.00 34.04  ? 4   PRO   D C   1 
ATOM   1172 O  O   . PRO   B 2 5   ? 14.097 -26.040 0.918  1.00 32.69  ? 4   PRO   D O   1 
ATOM   1173 C  CB  . PRO   B 2 5   ? 16.902 -26.131 2.495  1.00 31.04  ? 4   PRO   D CB  1 
ATOM   1174 C  CG  . PRO   B 2 5   ? 17.466 -26.296 1.095  1.00 34.85  ? 4   PRO   D CG  1 
ATOM   1175 C  CD  . PRO   B 2 5   ? 17.224 -27.749 0.779  1.00 30.51  ? 4   PRO   D CD  1 
ATOM   1176 N  N   . ALA   B 2 6   ? 13.687 -25.656 3.107  1.00 32.67  ? 5   ALA   D N   1 
HETATM 1177 C  C4  . A1ACA C 3 .   ? 25.512 -10.176 16.510 1.00 26.05  ? 201 A1ACA A C4  1 
HETATM 1178 C  C5  . A1ACA C 3 .   ? 24.917 -8.909  16.545 1.00 25.74  ? 201 A1ACA A C5  1 
HETATM 1179 C  C6  . A1ACA C 3 .   ? 23.897 -8.626  17.445 1.00 28.84  ? 201 A1ACA A C6  1 
HETATM 1180 C  C7  . A1ACA C 3 .   ? 23.456 -9.640  18.292 1.00 29.78  ? 201 A1ACA A C7  1 
HETATM 1181 C  C8  . A1ACA C 3 .   ? 22.283 -10.821 19.856 1.00 32.74  ? 201 A1ACA A C8  1 
HETATM 1182 C  C10 . A1ACA C 3 .   ? 23.994 -10.922 18.227 1.00 28.27  ? 201 A1ACA A C10 1 
HETATM 1183 C  C1  . A1ACA C 3 .   ? 27.300 -10.311 11.951 1.00 28.26  ? 201 A1ACA A C1  1 
HETATM 1184 C  C2  . A1ACA C 3 .   ? 27.446 -10.632 13.289 1.00 26.09  ? 201 A1ACA A C2  1 
HETATM 1185 C  C3  . A1ACA C 3 .   ? 26.416 -10.277 14.186 1.00 27.38  ? 201 A1ACA A C3  1 
HETATM 1186 C  C9  . A1ACA C 3 .   ? 23.277 -11.778 19.232 1.00 30.75  ? 201 A1ACA A C9  1 
HETATM 1187 O  O   . A1ACA C 3 .   ? 21.452 -11.083 20.724 1.00 32.55  ? 201 A1ACA A O   1 
HETATM 1188 N  N2  . A1ACA C 3 .   ? 22.455 -9.607  19.270 1.00 29.74  ? 201 A1ACA A N2  1 
HETATM 1189 C  C11 . A1ACA C 3 .   ? 25.020 -11.198 17.330 1.00 26.04  ? 201 A1ACA A C11 1 
HETATM 1190 N  N1  . A1ACA C 3 .   ? 26.420 -10.581 15.511 1.00 24.18  ? 201 A1ACA A N1  1 
HETATM 1191 N  N3  . A1ACA C 3 .   ? 25.321 -9.667  13.698 1.00 29.77  ? 201 A1ACA A N3  1 
HETATM 1192 C  C   . A1ACA C 3 .   ? 25.304 -9.427  12.398 1.00 31.80  ? 201 A1ACA A C   1 
HETATM 1193 CL CL  . A1ACA C 3 .   ? 23.852 -8.672  11.814 0.51 32.98  ? 201 A1ACA A CL  1 
HETATM 1194 BR BR  . A1ACA C 3 .   ? 29.004 -11.521 13.863 0.70 25.68  ? 201 A1ACA A BR  1 
HETATM 1195 N  N   . A1ACA C 3 .   ? 26.212 -9.692  11.477 1.00 32.02  ? 201 A1ACA A N   1 
HETATM 1196 CL CL  . CL    D 4 .   ? 21.396 -15.376 22.727 1.00 37.89  ? 202 CL    A CL  1 
HETATM 1197 S  S   A DMS   E 5 .   ? 17.505 -35.393 -1.271 0.66 45.96  ? 101 DMS   D S   1 
HETATM 1198 O  O   A DMS   E 5 .   ? 16.220 -35.179 -0.614 0.66 47.40  ? 101 DMS   D O   1 
HETATM 1199 C  C1  A DMS   E 5 .   ? 18.648 -34.507 -0.242 0.66 45.60  ? 101 DMS   D C1  1 
HETATM 1200 C  C2  A DMS   E 5 .   ? 17.938 -37.032 -0.807 0.66 45.84  ? 101 DMS   D C2  1 
HETATM 1201 O  O   . HOH   F 6 .   ? 35.707 -25.826 25.566 1.00 39.13  ? 301 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 6 .   ? 25.875 -3.555  26.563 1.00 35.70  ? 302 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 6 .   ? 22.779 -5.480  19.951 1.00 52.73  ? 303 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 6 .   ? 44.392 -0.900  17.989 1.00 51.50  ? 304 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 6 .   ? 16.466 -27.566 -3.242 1.00 47.65  ? 305 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 6 .   ? 41.175 -21.722 25.227 1.00 42.68  ? 306 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 6 .   ? 38.529 -15.028 15.555 1.00 36.37  ? 307 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 6 .   ? 20.820 -5.929  26.273 1.00 42.00  ? 308 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 6 .   ? 45.063 -11.241 18.846 1.00 60.18  ? 309 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 6 .   ? 29.846 -32.308 9.537  1.00 50.05  ? 310 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 6 .   ? 37.910 2.370   19.869 1.00 38.89  ? 311 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 6 .   ? 37.734 -20.519 27.021 1.00 35.59  ? 312 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 6 .   ? 15.481 -10.100 25.034 1.00 49.27  ? 313 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 6 .   ? 37.263 -12.470 40.413 1.00 60.61  ? 314 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 6 .   ? 26.821 -32.111 16.182 1.00 43.54  ? 315 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 6 .   ? 33.391 -20.899 29.629 1.00 46.63  ? 316 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 6 .   ? 17.914 -29.509 7.693  1.00 34.06  ? 317 HOH   A O   1 
HETATM 1218 O  O   A HOH   F 6 .   ? 19.109 -22.987 4.378  0.67 50.40  ? 318 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 6 .   ? 22.706 -27.801 17.809 1.00 50.65  ? 319 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 6 .   ? 20.431 -13.585 20.619 1.00 49.79  ? 320 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 6 .   ? 43.689 -6.647  32.031 1.00 48.89  ? 321 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 6 .   ? 32.782 -24.581 32.246 1.00 58.55  ? 322 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 6 .   ? 28.366 -8.969  40.051 1.00 47.02  ? 323 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 6 .   ? 21.706 -29.567 -5.247 1.00 37.90  ? 324 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 6 .   ? 23.456 -5.902  33.022 1.00 36.83  ? 325 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 6 .   ? 31.755 -0.939  15.949 1.00 43.64  ? 326 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 6 .   ? 30.356 1.342   33.914 1.00 68.70  ? 327 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 6 .   ? 21.503 -27.213 14.667 0.50 37.91  ? 328 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 6 .   ? 19.871 -9.748  37.137 1.00 40.36  ? 329 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 6 .   ? 22.973 -28.322 12.689 1.00 23.92  ? 330 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 6 .   ? 25.710 -3.007  20.090 1.00 57.69  ? 331 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 6 .   ? 28.924 -21.964 41.700 1.00 73.05  ? 332 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 6 .   ? 41.326 -16.960 15.253 1.00 39.92  ? 333 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 6 .   ? 27.341 -28.283 18.670 1.00 26.81  ? 334 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 6 .   ? 28.332 -23.855 31.738 1.00 40.83  ? 335 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 6 .   ? 41.277 -1.470  11.758 1.00 62.36  ? 336 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 6 .   ? 41.425 -12.831 14.133 1.00 101.91 ? 337 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 6 .   ? 27.229 -10.272 35.980 1.00 37.33  ? 338 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 6 .   ? 36.865 -5.792  12.315 1.00 37.21  ? 339 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 6 .   ? 27.033 -35.412 11.661 1.00 57.49  ? 340 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 6 .   ? 23.329 -17.145 44.374 1.00 67.02  ? 341 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 6 .   ? 26.948 -16.700 38.756 1.00 52.03  ? 342 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 6 .   ? 34.539 -23.874 29.934 1.00 74.63  ? 343 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 6 .   ? 26.168 -21.941 38.739 1.00 38.81  ? 344 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 6 .   ? 21.515 -30.031 14.210 1.00 71.36  ? 345 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 6 .   ? 24.028 -15.911 21.335 1.00 31.03  ? 346 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 6 .   ? 29.428 -27.484 20.686 1.00 25.19  ? 347 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 6 .   ? 12.765 -20.704 42.429 1.00 56.81  ? 348 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 6 .   ? 12.243 -18.115 25.924 1.00 59.12  ? 349 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 6 .   ? 20.262 -16.075 40.988 1.00 36.92  ? 350 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 6 .   ? 24.927 -26.912 19.076 1.00 34.38  ? 351 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 6 .   ? 21.937 -25.067 18.378 1.00 23.69  ? 352 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 6 .   ? 10.792 -11.599 34.583 1.00 50.64  ? 353 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 6 .   ? 43.972 -4.383  25.823 1.00 45.03  ? 354 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 6 .   ? 18.032 -34.585 8.333  1.00 34.20  ? 355 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 6 .   ? 44.436 -12.750 41.458 1.00 53.69  ? 356 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 6 .   ? 29.091 -31.207 7.225  1.00 35.10  ? 357 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 6 .   ? 20.905 -7.368  19.862 1.00 48.34  ? 358 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 6 .   ? 45.998 -14.257 21.593 1.00 58.69  ? 359 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 6 .   ? 42.518 -10.651 15.614 1.00 51.03  ? 360 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 6 .   ? 37.385 -6.510  34.388 1.00 40.02  ? 361 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 6 .   ? 28.999 -0.411  16.979 1.00 75.91  ? 362 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 6 .   ? 46.893 -21.613 18.196 1.00 47.63  ? 363 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 6 .   ? 30.359 -0.671  37.114 1.00 51.32  ? 364 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 6 .   ? 28.523 -24.416 34.406 1.00 54.34  ? 365 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 6 .   ? 30.725 -29.028 22.705 1.00 39.51  ? 366 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 6 .   ? 27.215 -2.465  16.160 1.00 65.04  ? 367 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 6 .   ? 11.586 -15.345 40.625 1.00 78.40  ? 368 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 6 .   ? 46.309 -15.904 27.638 1.00 69.20  ? 369 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 6 .   ? 41.353 -7.821  46.541 1.00 56.46  ? 370 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 6 .   ? 24.116 -28.687 21.628 1.00 53.03  ? 371 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 6 .   ? 39.065 -18.952 33.516 1.00 48.18  ? 372 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 6 .   ? 37.613 3.281   15.854 1.00 43.82  ? 373 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 6 .   ? 26.187 -22.760 30.020 1.00 28.69  ? 374 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 6 .   ? 34.802 -19.040 13.905 0.50 23.42  ? 375 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 6 .   ? 34.167 -8.009  35.754 1.00 35.74  ? 376 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 6 .   ? 26.491 -30.904 18.964 1.00 60.41  ? 377 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 6 .   ? 14.362 -16.934 23.549 1.00 44.38  ? 378 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 6 .   ? 45.317 -12.671 23.669 1.00 48.67  ? 379 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 6 .   ? 43.861 -10.674 35.200 1.00 71.36  ? 380 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 6 .   ? 47.242 -25.303 21.626 1.00 52.05  ? 381 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 6 .   ? 41.275 -7.029  36.050 1.00 44.66  ? 382 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 6 .   ? 45.585 -10.925 30.287 1.00 56.28  ? 383 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 6 .   ? 26.089 -19.284 41.792 1.00 59.51  ? 384 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 6 .   ? 26.237 -8.108  9.081  1.00 42.83  ? 385 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 6 .   ? 38.023 -16.705 13.142 0.50 27.26  ? 386 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 6 .   ? 44.690 -16.374 29.763 1.00 52.36  ? 387 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 6 .   ? 31.935 -31.942 14.568 1.00 38.07  ? 388 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 6 .   ? 46.413 -18.959 19.663 1.00 52.08  ? 389 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 6 .   ? 27.698 -23.141 13.905 0.50 27.77  ? 390 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 6 .   ? 4.328  -20.499 37.934 1.00 61.32  ? 391 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 6 .   ? 16.789 -6.543  27.630 1.00 64.77  ? 392 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 6 .   ? 44.677 -8.718  17.939 1.00 64.83  ? 393 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 6 .   ? 19.867 -25.602 41.313 1.00 80.49  ? 394 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 6 .   ? 23.690 -15.691 17.867 1.00 43.56  ? 395 HOH   A O   1 
HETATM 1296 O  O   A HOH   F 6 .   ? 12.286 -21.064 27.984 0.66 44.87  ? 396 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 6 .   ? 47.426 -6.767  20.361 1.00 67.56  ? 397 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 6 .   ? 46.128 -9.064  44.206 1.00 53.64  ? 398 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 6 .   ? 21.279 -31.329 29.890 1.00 69.43  ? 399 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 6 .   ? 40.470 -19.681 29.086 1.00 35.93  ? 400 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 6 .   ? 34.748 -29.213 26.075 1.00 66.89  ? 401 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 6 .   ? 29.716 -22.702 36.940 1.00 68.04  ? 402 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 6 .   ? 33.139 -29.865 21.544 1.00 42.70  ? 403 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 6 .   ? 25.710 -4.678  17.977 1.00 50.21  ? 404 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 6 .   ? 37.031 -2.282  11.563 1.00 59.87  ? 405 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 6 .   ? 42.112 -5.975  11.873 1.00 68.20  ? 406 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 6 .   ? 45.885 -17.085 17.307 1.00 64.91  ? 407 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 6 .   ? 47.012 -20.263 21.952 1.00 66.35  ? 408 HOH   A O   1 
HETATM 1309 O  O   . HOH   F 6 .   ? 41.329 -17.136 35.251 1.00 44.16  ? 409 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 6 .   ? 30.425 -10.661 40.668 1.00 43.13  ? 410 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 6 .   ? 35.321 1.859   13.551 1.00 54.93  ? 411 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 6 .   ? 35.190 -29.811 23.467 1.00 43.07  ? 412 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 6 .   ? 27.082 -1.714  22.047 1.00 54.18  ? 413 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 6 .   ? 23.043 -15.066 40.493 1.00 34.07  ? 414 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 6 .   ? 21.167 -23.359 42.157 1.00 46.86  ? 415 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 6 .   ? 34.557 -18.745 36.335 1.00 62.98  ? 416 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 6 .   ? 32.206 -15.760 39.911 1.00 36.72  ? 417 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 6 .   ? 34.097 -32.948 21.906 1.00 61.51  ? 418 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 6 .   ? 32.460 -9.074  39.837 1.00 59.29  ? 419 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 6 .   ? 27.382 -25.556 28.425 1.00 57.73  ? 420 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 6 .   ? 42.035 -8.006  13.782 1.00 62.46  ? 421 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 6 .   ? 19.627 -27.358 10.085 1.00 51.57  ? 422 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 6 .   ? 33.584 -33.104 12.109 1.00 48.44  ? 423 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 6 .   ? 10.518 -11.786 40.134 1.00 65.67  ? 424 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 6 .   ? 29.547 -0.809  22.337 1.00 56.08  ? 425 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 6 .   ? 33.577 -0.370  20.185 1.00 45.32  ? 426 HOH   A O   1 
HETATM 1327 O  O   . HOH   F 6 .   ? 25.638 -16.096 41.152 1.00 50.94  ? 427 HOH   A O   1 
HETATM 1328 O  O   . HOH   F 6 .   ? 39.916 -5.577  34.014 1.00 42.58  ? 428 HOH   A O   1 
HETATM 1329 O  O   . HOH   F 6 .   ? 45.895 -5.558  23.800 1.00 48.31  ? 429 HOH   A O   1 
HETATM 1330 O  O   . HOH   F 6 .   ? 31.865 -26.158 27.122 1.00 57.40  ? 430 HOH   A O   1 
HETATM 1331 O  O   . HOH   F 6 .   ? 23.572 -30.627 19.369 1.00 67.95  ? 431 HOH   A O   1 
HETATM 1332 O  O   . HOH   F 6 .   ? 22.314 -10.556 14.654 1.00 47.09  ? 432 HOH   A O   1 
HETATM 1333 O  O   . HOH   F 6 .   ? 37.207 -31.620 23.450 1.00 80.92  ? 433 HOH   A O   1 
HETATM 1334 O  O   . HOH   F 6 .   ? 42.892 -18.294 30.745 1.00 49.79  ? 434 HOH   A O   1 
HETATM 1335 O  O   . HOH   F 6 .   ? 26.459 -29.573 22.730 1.00 56.06  ? 435 HOH   A O   1 
HETATM 1336 O  O   . HOH   F 6 .   ? 31.996 -0.062  13.370 1.00 67.46  ? 436 HOH   A O   1 
HETATM 1337 O  O   . HOH   F 6 .   ? 44.465 -4.271  28.949 1.00 66.19  ? 437 HOH   A O   1 
HETATM 1338 O  O   . HOH   F 6 .   ? 23.134 -3.146  26.863 1.00 63.32  ? 438 HOH   A O   1 
HETATM 1339 O  O   . HOH   F 6 .   ? 26.988 -34.557 18.067 1.00 65.65  ? 439 HOH   A O   1 
HETATM 1340 O  O   . HOH   F 6 .   ? 19.483 -31.818 13.916 1.00 64.58  ? 440 HOH   A O   1 
HETATM 1341 O  O   . HOH   F 6 .   ? 30.604 -34.406 14.960 1.00 60.30  ? 441 HOH   A O   1 
HETATM 1342 O  O   . HOH   F 6 .   ? 28.785 -2.710  12.981 1.00 75.91  ? 442 HOH   A O   1 
HETATM 1343 O  O   . HOH   F 6 .   ? 48.030 -23.484 19.795 1.00 61.87  ? 443 HOH   A O   1 
HETATM 1344 O  O   . HOH   F 6 .   ? 35.430 -4.270  10.674 1.00 49.35  ? 444 HOH   A O   1 
HETATM 1345 O  O   . HOH   F 6 .   ? 36.878 -24.530 27.651 1.00 61.32  ? 445 HOH   A O   1 
HETATM 1346 O  O   . HOH   F 6 .   ? 19.822 -8.189  24.654 1.00 51.24  ? 446 HOH   A O   1 
HETATM 1347 O  O   . HOH   F 6 .   ? 24.510 -21.821 41.132 1.00 57.29  ? 447 HOH   A O   1 
HETATM 1348 O  O   . HOH   F 6 .   ? 46.743 -14.692 18.323 1.00 63.97  ? 448 HOH   A O   1 
HETATM 1349 O  O   . HOH   F 6 .   ? 47.507 -28.489 17.678 1.00 59.27  ? 449 HOH   A O   1 
HETATM 1350 O  O   . HOH   F 6 .   ? 34.190 -17.713 39.561 1.00 65.50  ? 450 HOH   A O   1 
HETATM 1351 O  O   . HOH   F 6 .   ? 32.202 -1.120  22.396 1.00 60.34  ? 451 HOH   A O   1 
HETATM 1352 O  O   . HOH   F 6 .   ? 47.264 -11.910 25.413 1.00 64.00  ? 452 HOH   A O   1 
HETATM 1353 O  O   . HOH   F 6 .   ? 35.923 -21.264 30.593 1.00 60.72  ? 453 HOH   A O   1 
HETATM 1354 O  O   . HOH   F 6 .   ? 11.957 -18.908 22.818 1.00 66.38  ? 454 HOH   A O   1 
HETATM 1355 O  O   . HOH   F 6 .   ? 19.509 -7.751  35.379 1.00 53.69  ? 455 HOH   A O   1 
HETATM 1356 O  O   . HOH   F 6 .   ? 44.024 -13.713 13.904 0.50 86.20  ? 456 HOH   A O   1 
HETATM 1357 O  O   . HOH   F 6 .   ? 47.102 -12.600 28.488 1.00 60.50  ? 457 HOH   A O   1 
HETATM 1358 O  O   . HOH   F 6 .   ? 25.445 -5.771  35.025 1.00 61.04  ? 458 HOH   A O   1 
HETATM 1359 O  O   . HOH   F 6 .   ? 45.623 -8.446  31.351 1.00 68.57  ? 459 HOH   A O   1 
HETATM 1360 O  O   . HOH   F 6 .   ? 20.138 -35.365 10.150 1.00 40.15  ? 460 HOH   A O   1 
HETATM 1361 O  O   . HOH   F 6 .   ? 19.944 -15.040 43.480 1.00 52.68  ? 461 HOH   A O   1 
HETATM 1362 O  O   . HOH   F 6 .   ? 43.233 -3.073  33.963 1.00 59.56  ? 462 HOH   A O   1 
HETATM 1363 O  O   . HOH   F 6 .   ? 17.153 -8.023  25.028 1.00 66.71  ? 463 HOH   A O   1 
HETATM 1364 O  O   . HOH   F 6 .   ? 17.088 -28.186 9.897  1.00 49.06  ? 464 HOH   A O   1 
HETATM 1365 O  O   . HOH   F 6 .   ? 19.127 -28.328 13.860 0.50 68.39  ? 465 HOH   A O   1 
HETATM 1366 O  O   . HOH   F 6 .   ? 33.890 -11.212 41.715 0.50 64.73  ? 466 HOH   A O   1 
HETATM 1367 O  O   . HOH   F 6 .   ? 33.890 -14.052 41.715 0.50 42.68  ? 467 HOH   A O   1 
HETATM 1368 O  O   . HOH   F 6 .   ? 28.417 -29.908 24.604 1.00 68.34  ? 468 HOH   A O   1 
HETATM 1369 O  O   . HOH   F 6 .   ? 32.143 -23.932 35.013 1.00 70.95  ? 469 HOH   A O   1 
HETATM 1370 O  O   . HOH   F 6 .   ? 32.720 -20.654 37.004 1.00 73.82  ? 470 HOH   A O   1 
HETATM 1371 O  O   . HOH   F 6 .   ? 12.553 -18.374 20.025 1.00 63.62  ? 471 HOH   A O   1 
HETATM 1372 O  O   . HOH   F 6 .   ? 16.771 -6.941  34.995 1.00 75.33  ? 472 HOH   A O   1 
HETATM 1373 O  O   . HOH   F 6 .   ? 21.301 -5.772  34.832 1.00 50.70  ? 473 HOH   A O   1 
HETATM 1374 O  O   . HOH   F 6 .   ? 45.198 -12.357 15.966 1.00 73.43  ? 474 HOH   A O   1 
HETATM 1375 O  O   . HOH   F 6 .   ? 39.436 -5.546  11.488 1.00 66.02  ? 475 HOH   A O   1 
HETATM 1376 O  O   . HOH   F 6 .   ? 16.702 -30.174 12.433 1.00 57.14  ? 476 HOH   A O   1 
HETATM 1377 O  O   . HOH   G 6 .   ? 12.230 -24.287 0.007  1.00 51.46  ? 201 HOH   D O   1 
HETATM 1378 O  O   . HOH   G 6 .   ? 14.983 -25.847 -1.768 1.00 44.43  ? 202 HOH   D O   1 
HETATM 1379 O  O   . HOH   G 6 .   ? 22.644 -34.092 8.853  1.00 34.37  ? 203 HOH   D O   1 
HETATM 1380 O  O   . HOH   G 6 .   ? 17.727 -36.345 6.042  1.00 42.81  ? 204 HOH   D O   1 
HETATM 1381 O  O   . HOH   G 6 .   ? 20.886 -38.364 4.020  1.00 50.03  ? 205 HOH   D O   1 
HETATM 1382 O  O   . HOH   G 6 .   ? 11.463 -23.602 3.164  1.00 55.92  ? 206 HOH   D O   1 
HETATM 1383 O  O   . HOH   G 6 .   ? 20.826 -39.560 -2.137 1.00 54.42  ? 207 HOH   D O   1 
HETATM 1384 O  O   . HOH   G 6 .   ? 10.636 -24.733 5.519  1.00 56.42  ? 208 HOH   D O   1 
HETATM 1385 O  O   . HOH   G 6 .   ? 23.622 -36.567 9.995  1.00 50.72  ? 209 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   ? 0.8070 0.9890 0.7137 0.0273  -0.1295 -0.0165 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8004 0.9778 0.6904 0.0111  -0.1206 -0.0196 6   ASP A CA  
3    C C   . ASP A 5   ? 0.7744 0.9809 0.6877 0.0002  -0.1161 -0.0363 6   ASP A C   
4    O O   . ASP A 5   ? 0.7689 0.9998 0.7099 0.0046  -0.1202 -0.0454 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8236 0.9731 0.7053 0.0029  -0.1039 -0.0137 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0199 1.1514 0.8691 -0.0078 -0.0988 -0.0096 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0191 1.1634 0.8671 -0.0192 -0.0952 -0.0190 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1337 1.2380 0.9586 -0.0057 -0.0973 0.0021  6   ASP A OD2 
9    N N   . SER A 6   ? 0.6633 0.8669 0.5654 -0.0144 -0.1068 -0.0413 7   SER A N   
10   C CA  . SER A 6   ? 0.6153 0.8402 0.5354 -0.0264 -0.1002 -0.0568 7   SER A CA  
11   C C   . SER A 6   ? 0.5650 0.7763 0.4968 -0.0360 -0.0819 -0.0599 7   SER A C   
12   O O   . SER A 6   ? 0.5489 0.7657 0.4852 -0.0479 -0.0733 -0.0702 7   SER A O   
13   C CB  . SER A 6   ? 0.6880 0.9206 0.5870 -0.0352 -0.1043 -0.0617 7   SER A CB  
14   O OG  . SER A 6   ? 0.8394 1.0470 0.7106 -0.0417 -0.0969 -0.0543 7   SER A OG  
15   N N   . CYS A 7   ? 0.4627 0.6561 0.3996 -0.0301 -0.0767 -0.0515 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4259 0.6056 0.3727 -0.0368 -0.0619 -0.0532 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4083 0.6023 0.3803 -0.0423 -0.0558 -0.0653 8   CYS A C   
18   O O   . CYS A 7   ? 0.3934 0.6075 0.3804 -0.0391 -0.0620 -0.0713 8   CYS A O   
19   C CB  . CYS A 7   ? 0.4414 0.6013 0.3876 -0.0288 -0.0595 -0.0421 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5270 0.6610 0.4417 -0.0277 -0.0592 -0.0292 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3120 0.4949 0.2884 -0.0506 -0.0435 -0.0695 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2654 0.4511 0.2610 -0.0557 -0.0356 -0.0780 9   ILE A CA  
23   C C   . ILE A 8   ? 0.2900 0.4564 0.2896 -0.0505 -0.0303 -0.0699 9   ILE A C   
24   O O   . ILE A 8   ? 0.2917 0.4430 0.2796 -0.0467 -0.0301 -0.0608 9   ILE A O   
25   C CB  . ILE A 8   ? 0.2993 0.4848 0.2963 -0.0676 -0.0268 -0.0891 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3067 0.4727 0.2921 -0.0704 -0.0198 -0.0860 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3056 0.5138 0.3011 -0.0736 -0.0323 -0.0990 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3883 0.5505 0.3763 -0.0803 -0.0105 -0.0970 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2320 0.3977 0.2463 -0.0519 -0.0251 -0.0738 10  GLN A N   
30   N N   B GLN A 9   ? 0.2377 0.4054 0.2525 -0.0512 -0.0262 -0.0737 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2246 0.3725 0.2411 -0.0476 -0.0206 -0.0667 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2286 0.3799 0.2468 -0.0469 -0.0218 -0.0671 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2669 0.4020 0.2884 -0.0546 -0.0107 -0.0717 10  GLN A C   
34   C C   B GLN A 9   ? 0.2768 0.4150 0.2995 -0.0540 -0.0118 -0.0719 10  GLN A C   
35   O O   A GLN A 9   ? 0.2707 0.4136 0.2997 -0.0616 -0.0071 -0.0811 10  GLN A O   
36   O O   B GLN A 9   ? 0.2767 0.4220 0.3065 -0.0615 -0.0078 -0.0814 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2407 0.3966 0.2669 -0.0398 -0.0255 -0.0637 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2383 0.4005 0.2682 -0.0401 -0.0265 -0.0662 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.3010 0.4418 0.3325 -0.0383 -0.0190 -0.0602 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.2525 0.3983 0.2815 -0.0334 -0.0246 -0.0570 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5759 0.7166 0.6106 -0.0285 -0.0235 -0.0535 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4292 0.5769 0.4723 -0.0345 -0.0196 -0.0613 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4781 0.6286 0.5112 -0.0209 -0.0324 -0.0504 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.2996 0.4667 0.3563 -0.0356 -0.0210 -0.0697 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.5337 0.6615 0.5715 -0.0280 -0.0177 -0.0509 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.3944 0.5227 0.4344 -0.0348 -0.0133 -0.0566 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2489 0.3639 0.2652 -0.0526 -0.0067 -0.0658 11  PHE A N   
48   N N   B PHE A 10  ? 0.2447 0.3628 0.2621 -0.0517 -0.0079 -0.0654 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2313 0.3305 0.2493 -0.0571 0.0009  -0.0689 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2366 0.3380 0.2548 -0.0561 -0.0003 -0.0680 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2584 0.3507 0.2805 -0.0544 0.0025  -0.0651 11  PHE A C   
52   C C   B PHE A 10  ? 0.2673 0.3622 0.2902 -0.0537 0.0016  -0.0648 11  PHE A C   
53   O O   A PHE A 10  ? 0.2433 0.3267 0.2624 -0.0483 0.0009  -0.0571 11  PHE A O   
54   O O   B PHE A 10  ? 0.2592 0.3477 0.2798 -0.0472 -0.0006 -0.0568 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2451 0.3284 0.2562 -0.0560 0.0032  -0.0666 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2578 0.3441 0.2686 -0.0543 0.0014  -0.0645 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2635 0.3291 0.2744 -0.0593 0.0092  -0.0703 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.2839 0.3748 0.2914 -0.0591 0.0027  -0.0710 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3039 0.3691 0.3156 -0.0668 0.0136  -0.0794 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3254 0.4317 0.3283 -0.0600 -0.0017 -0.0719 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.2805 0.3280 0.2887 -0.0548 0.0099  -0.0648 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3316 0.4100 0.3391 -0.0622 0.0081  -0.0763 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3222 0.3660 0.3305 -0.0692 0.0190  -0.0819 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3435 0.4540 0.3418 -0.0657 0.0003  -0.0787 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3123 0.3403 0.3170 -0.0565 0.0138  -0.0671 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3750 0.4579 0.3805 -0.0669 0.0103  -0.0837 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.2984 0.3229 0.3024 -0.0634 0.0184  -0.0752 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3448 0.4442 0.3456 -0.0694 0.0069  -0.0851 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2230 0.3204 0.2520 -0.0602 0.0065  -0.0719 12  THR A N   
70   C CA  . THR A 11  ? 0.2303 0.3236 0.2637 -0.0602 0.0098  -0.0710 12  THR A CA  
71   C C   . THR A 11  ? 0.2794 0.3486 0.3040 -0.0571 0.0123  -0.0631 12  THR A C   
72   O O   . THR A 11  ? 0.2751 0.3436 0.3013 -0.0521 0.0110  -0.0580 12  THR A O   
73   C CB  . THR A 11  ? 0.3274 0.4245 0.3662 -0.0708 0.0172  -0.0817 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3530 0.4765 0.4019 -0.0733 0.0136  -0.0900 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3643 0.4592 0.4078 -0.0727 0.0223  -0.0827 12  THR A CG2 
76   N N   . ARG A 12  ? 0.2541 0.3043 0.2697 -0.0595 0.0152  -0.0627 13  ARG A N   
77   C CA  . ARG A 12  ? 0.2646 0.2924 0.2712 -0.0564 0.0161  -0.0563 13  ARG A CA  
78   C C   . ARG A 12  ? 0.2843 0.3105 0.2891 -0.0481 0.0106  -0.0493 13  ARG A C   
79   O O   . ARG A 12  ? 0.2809 0.2914 0.2796 -0.0450 0.0101  -0.0448 13  ARG A O   
80   C CB  . ARG A 12  ? 0.3322 0.3384 0.3295 -0.0608 0.0203  -0.0590 13  ARG A CB  
81   C CG  . ARG A 12  ? 0.4687 0.4680 0.4628 -0.0712 0.0283  -0.0657 13  ARG A CG  
82   C CD  . ARG A 12  ? 0.7440 0.7343 0.7333 -0.0741 0.0324  -0.0634 13  ARG A CD  
83   N NE  . ARG A 12  ? 0.9162 0.8801 0.8907 -0.0702 0.0311  -0.0559 13  ARG A NE  
84   C CZ  . ARG A 12  ? 1.0579 1.0133 1.0261 -0.0701 0.0325  -0.0517 13  ARG A CZ  
85   N NH1 . ARG A 12  ? 0.9107 0.8426 0.8641 -0.0663 0.0298  -0.0452 13  ARG A NH1 
86   N NH2 . ARG A 12  ? 0.8283 0.7998 0.8058 -0.0732 0.0360  -0.0546 13  ARG A NH2 
87   N N   . HIS A 13  ? 0.2378 0.2793 0.2465 -0.0452 0.0066  -0.0487 14  HIS A N   
88   C CA  . HIS A 13  ? 0.2384 0.2775 0.2442 -0.0399 0.0034  -0.0437 14  HIS A CA  
89   C C   . HIS A 13  ? 0.2708 0.3025 0.2747 -0.0355 0.0025  -0.0370 14  HIS A C   
90   O O   . HIS A 13  ? 0.2527 0.2742 0.2535 -0.0331 0.0020  -0.0349 14  HIS A O   
91   C CB  . HIS A 13  ? 0.2304 0.2844 0.2363 -0.0391 0.0003  -0.0436 14  HIS A CB  
92   C CG  . HIS A 13  ? 0.2563 0.3065 0.2578 -0.0361 -0.0008 -0.0397 14  HIS A CG  
93   N ND1 . HIS A 13  ? 0.2588 0.3042 0.2603 -0.0371 0.0010  -0.0433 14  HIS A ND1 
94   C CD2 . HIS A 13  ? 0.2588 0.3094 0.2563 -0.0327 -0.0026 -0.0336 14  HIS A CD2 
95   C CE1 . HIS A 13  ? 0.2572 0.3024 0.2559 -0.0354 0.0008  -0.0403 14  HIS A CE1 
96   N NE2 . HIS A 13  ? 0.2487 0.2952 0.2434 -0.0333 -0.0010 -0.0340 14  HIS A NE2 
97   N N   . ALA A 14  ? 0.2290 0.2672 0.2360 -0.0340 0.0021  -0.0348 15  ALA A N   
98   C CA  . ALA A 14  ? 0.2350 0.2658 0.2401 -0.0303 0.0022  -0.0293 15  ALA A CA  
99   C C   . ALA A 14  ? 0.2642 0.2787 0.2642 -0.0322 0.0048  -0.0290 15  ALA A C   
100  O O   . ALA A 14  ? 0.2528 0.2588 0.2488 -0.0296 0.0038  -0.0254 15  ALA A O   
101  C CB  . ALA A 14  ? 0.2438 0.2842 0.2549 -0.0280 0.0018  -0.0288 15  ALA A CB  
102  N N   A SER A 15  ? 0.2572 0.2666 0.2558 -0.0372 0.0083  -0.0330 16  SER A N   
103  N N   B SER A 15  ? 0.2493 0.2586 0.2478 -0.0372 0.0083  -0.0330 16  SER A N   
104  N N   C SER A 15  ? 0.2483 0.2574 0.2468 -0.0372 0.0083  -0.0329 16  SER A N   
105  C CA  A SER A 15  ? 0.2655 0.2556 0.2543 -0.0395 0.0105  -0.0320 16  SER A CA  
106  C CA  B SER A 15  ? 0.2575 0.2475 0.2463 -0.0397 0.0106  -0.0322 16  SER A CA  
107  C CA  C SER A 15  ? 0.2560 0.2458 0.2446 -0.0394 0.0105  -0.0319 16  SER A CA  
108  C C   A SER A 15  ? 0.3115 0.2905 0.2948 -0.0361 0.0066  -0.0307 16  SER A C   
109  C C   B SER A 15  ? 0.3116 0.2901 0.2946 -0.0363 0.0067  -0.0308 16  SER A C   
110  C C   C SER A 15  ? 0.3115 0.2899 0.2945 -0.0362 0.0067  -0.0307 16  SER A C   
111  O O   A SER A 15  ? 0.2877 0.2544 0.2639 -0.0337 0.0045  -0.0274 16  SER A O   
112  O O   B SER A 15  ? 0.2969 0.2625 0.2724 -0.0340 0.0048  -0.0276 16  SER A O   
113  O O   C SER A 15  ? 0.2977 0.2628 0.2730 -0.0340 0.0047  -0.0276 16  SER A O   
114  C CB  A SER A 15  ? 0.3236 0.3082 0.3093 -0.0472 0.0162  -0.0371 16  SER A CB  
115  C CB  B SER A 15  ? 0.3071 0.2921 0.2931 -0.0473 0.0163  -0.0373 16  SER A CB  
116  C CB  C SER A 15  ? 0.3067 0.2908 0.2921 -0.0470 0.0164  -0.0366 16  SER A CB  
117  O OG  A SER A 15  ? 0.3725 0.3340 0.3439 -0.0498 0.0183  -0.0351 16  SER A OG  
118  O OG  B SER A 15  ? 0.3284 0.3266 0.3226 -0.0504 0.0201  -0.0406 16  SER A OG  
119  O OG  C SER A 15  ? 0.3370 0.3223 0.3233 -0.0501 0.0171  -0.0413 16  SER A OG  
120  N N   . ASP A 16  ? 0.2745 0.2591 0.2618 -0.0357 0.0053  -0.0341 17  ASP A N   
121  C CA  . ASP A 16  ? 0.2834 0.2607 0.2695 -0.0317 0.0018  -0.0352 17  ASP A CA  
122  C C   . ASP A 16  ? 0.2852 0.2688 0.2750 -0.0268 -0.0018 -0.0327 17  ASP A C   
123  O O   . ASP A 16  ? 0.2874 0.2628 0.2753 -0.0227 -0.0054 -0.0325 17  ASP A O   
124  C CB  . ASP A 16  ? 0.3063 0.2909 0.2976 -0.0333 0.0027  -0.0410 17  ASP A CB  
125  C CG  . ASP A 16  ? 0.4389 0.4130 0.4253 -0.0386 0.0067  -0.0450 17  ASP A CG  
126  O OD1 . ASP A 16  ? 0.4291 0.3877 0.4063 -0.0413 0.0090  -0.0430 17  ASP A OD1 
127  O OD2 . ASP A 16  ? 0.4763 0.4569 0.4668 -0.0413 0.0085  -0.0508 17  ASP A OD2 
128  N N   . VAL A 17  ? 0.2355 0.2330 0.2300 -0.0273 -0.0009 -0.0311 18  VAL A N   
129  C CA  . VAL A 17  ? 0.2221 0.2236 0.2183 -0.0248 -0.0023 -0.0291 18  VAL A CA  
130  C C   . VAL A 17  ? 0.2871 0.2781 0.2786 -0.0232 -0.0035 -0.0257 18  VAL A C   
131  O O   . VAL A 17  ? 0.2628 0.2518 0.2549 -0.0208 -0.0063 -0.0267 18  VAL A O   
132  C CB  . VAL A 17  ? 0.2446 0.2568 0.2418 -0.0257 -0.0008 -0.0266 18  VAL A CB  
133  C CG1 . VAL A 17  ? 0.2430 0.2541 0.2388 -0.0247 -0.0005 -0.0239 18  VAL A CG1 
134  C CG2 . VAL A 17  ? 0.2429 0.2650 0.2418 -0.0277 -0.0004 -0.0302 18  VAL A CG2 
135  N N   . LEU A 18  ? 0.2479 0.2341 0.2353 -0.0251 -0.0012 -0.0231 19  LEU A N   
136  C CA  . LEU A 18  ? 0.2733 0.2496 0.2544 -0.0250 -0.0012 -0.0204 19  LEU A CA  
137  C C   . LEU A 18  ? 0.2840 0.2460 0.2569 -0.0236 -0.0050 -0.0208 19  LEU A C   
138  O O   . LEU A 18  ? 0.2815 0.2392 0.2510 -0.0215 -0.0084 -0.0200 19  LEU A O   
139  C CB  . LEU A 18  ? 0.2839 0.2591 0.2635 -0.0281 0.0034  -0.0192 19  LEU A CB  
140  C CG  . LEU A 18  ? 0.3349 0.3020 0.3086 -0.0288 0.0050  -0.0170 19  LEU A CG  
141  C CD1 . LEU A 18  ? 0.3291 0.3021 0.3070 -0.0263 0.0046  -0.0153 19  LEU A CD1 
142  C CD2 . LEU A 18  ? 0.3794 0.3458 0.3529 -0.0326 0.0108  -0.0181 19  LEU A CD2 
143  N N   . LEU A 19  ? 0.2727 0.2268 0.2418 -0.0245 -0.0051 -0.0225 20  LEU A N   
144  C CA  . LEU A 19  ? 0.2968 0.2336 0.2558 -0.0216 -0.0098 -0.0224 20  LEU A CA  
145  C C   . LEU A 19  ? 0.3237 0.2670 0.2905 -0.0148 -0.0166 -0.0248 20  LEU A C   
146  O O   . LEU A 19  ? 0.3250 0.2599 0.2856 -0.0108 -0.0226 -0.0239 20  LEU A O   
147  C CB  . LEU A 19  ? 0.3292 0.2568 0.2844 -0.0238 -0.0076 -0.0246 20  LEU A CB  
148  C CG  . LEU A 19  ? 0.4472 0.3511 0.3886 -0.0202 -0.0124 -0.0237 20  LEU A CG  
149  C CD1 . LEU A 19  ? 0.4889 0.3726 0.4107 -0.0234 -0.0119 -0.0188 20  LEU A CD1 
150  C CD2 . LEU A 19  ? 0.5051 0.3997 0.4437 -0.0232 -0.0086 -0.0268 20  LEU A CD2 
151  N N   . ASN A 20  ? 0.2739 0.2337 0.2541 -0.0140 -0.0155 -0.0288 21  ASN A N   
152  C CA  . ASN A 20  ? 0.2528 0.2219 0.2430 -0.0090 -0.0202 -0.0335 21  ASN A CA  
153  C C   . ASN A 20  ? 0.2783 0.2546 0.2708 -0.0093 -0.0212 -0.0329 21  ASN A C   
154  O O   . ASN A 20  ? 0.2828 0.2617 0.2795 -0.0048 -0.0271 -0.0365 21  ASN A O   
155  C CB  . ASN A 20  ? 0.2650 0.2484 0.2667 -0.0101 -0.0170 -0.0390 21  ASN A CB  
156  C CG  . ASN A 20  ? 0.3776 0.3535 0.3795 -0.0079 -0.0179 -0.0426 21  ASN A CG  
157  O OD1 . ASN A 20  ? 0.3677 0.3271 0.3627 -0.0031 -0.0227 -0.0418 21  ASN A OD1 
158  N ND2 . ASN A 20  ? 0.3339 0.3198 0.3418 -0.0114 -0.0133 -0.0465 21  ASN A ND2 
159  N N   . LEU A 21  ? 0.2696 0.2494 0.2600 -0.0142 -0.0158 -0.0292 22  LEU A N   
160  C CA  . LEU A 21  ? 0.2589 0.2425 0.2497 -0.0155 -0.0155 -0.0289 22  LEU A CA  
161  C C   . LEU A 21  ? 0.2930 0.2645 0.2742 -0.0135 -0.0206 -0.0272 22  LEU A C   
162  O O   . LEU A 21  ? 0.2841 0.2599 0.2676 -0.0125 -0.0242 -0.0300 22  LEU A O   
163  C CB  . LEU A 21  ? 0.2577 0.2430 0.2464 -0.0199 -0.0088 -0.0247 22  LEU A CB  
164  C CG  . LEU A 21  ? 0.2800 0.2757 0.2743 -0.0218 -0.0048 -0.0253 22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.3003 0.2944 0.2907 -0.0236 -0.0005 -0.0203 22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.3085 0.3138 0.3095 -0.0231 -0.0042 -0.0307 22  LEU A CD2 
167  N N   . ASN A 22  ? 0.2703 0.2266 0.2393 -0.0142 -0.0205 -0.0231 23  ASN A N   
168  C CA  . ASN A 22  ? 0.2959 0.2370 0.2505 -0.0131 -0.0254 -0.0208 23  ASN A CA  
169  C C   . ASN A 22  ? 0.3484 0.2863 0.3031 -0.0054 -0.0360 -0.0238 23  ASN A C   
170  O O   . ASN A 22  ? 0.3549 0.2894 0.3036 -0.0028 -0.0427 -0.0243 23  ASN A O   
171  C CB  . ASN A 22  ? 0.3361 0.2598 0.2756 -0.0173 -0.0214 -0.0166 23  ASN A CB  
172  C CG  . ASN A 22  ? 0.4287 0.3362 0.3499 -0.0190 -0.0239 -0.0138 23  ASN A CG  
173  O OD1 . ASN A 22  ? 0.3959 0.3084 0.3174 -0.0194 -0.0255 -0.0146 23  ASN A OD1 
174  N ND2 . ASN A 22  ? 0.4689 0.3557 0.3724 -0.0209 -0.0238 -0.0109 23  ASN A ND2 
175  N N   . ARG A 23  ? 0.3191 0.2589 0.2813 -0.0011 -0.0378 -0.0267 24  ARG A N   
176  C CA  . ARG A 23  ? 0.3252 0.2641 0.2918 0.0083  -0.0481 -0.0310 24  ARG A CA  
177  C C   . ARG A 23  ? 0.3684 0.3287 0.3513 0.0107  -0.0518 -0.0380 24  ARG A C   
178  O O   . ARG A 23  ? 0.3614 0.3214 0.3442 0.0176  -0.0621 -0.0409 24  ARG A O   
179  C CB  . ARG A 23  ? 0.3154 0.2544 0.2899 0.0113  -0.0470 -0.0343 24  ARG A CB  
180  C CG  . ARG A 23  ? 0.3796 0.2939 0.3364 0.0099  -0.0451 -0.0291 24  ARG A CG  
181  C CD  . ARG A 23  ? 0.3959 0.3121 0.3611 0.0101  -0.0412 -0.0331 24  ARG A CD  
182  N NE  . ARG A 23  ? 0.5068 0.3972 0.4543 0.0082  -0.0392 -0.0293 24  ARG A NE  
183  C CZ  . ARG A 23  ? 0.7181 0.6062 0.6675 0.0042  -0.0327 -0.0317 24  ARG A CZ  
184  N NH1 . ARG A 23  ? 0.5501 0.4605 0.5173 0.0018  -0.0280 -0.0372 24  ARG A NH1 
185  N NH2 . ARG A 23  ? 0.6395 0.5020 0.5712 0.0012  -0.0301 -0.0288 24  ARG A NH2 
186  N N   . LEU A 24  ? 0.3011 0.2793 0.2968 0.0045  -0.0435 -0.0410 25  LEU A N   
187  C CA  . LEU A 24  ? 0.2948 0.2926 0.3049 0.0038  -0.0443 -0.0487 25  LEU A CA  
188  C C   . LEU A 24  ? 0.3504 0.3447 0.3516 0.0019  -0.0474 -0.0468 25  LEU A C   
189  O O   . LEU A 24  ? 0.3478 0.3526 0.3566 0.0053  -0.0547 -0.0535 25  LEU A O   
190  C CB  . LEU A 24  ? 0.2837 0.2946 0.3024 -0.0041 -0.0334 -0.0505 25  LEU A CB  
191  C CG  . LEU A 24  ? 0.3387 0.3567 0.3665 -0.0041 -0.0294 -0.0540 25  LEU A CG  
192  C CD1 . LEU A 24  ? 0.3362 0.3642 0.3671 -0.0126 -0.0194 -0.0549 25  LEU A CD1 
193  C CD2 . LEU A 24  ? 0.3441 0.3726 0.3870 0.0031  -0.0360 -0.0641 25  LEU A CD2 
194  N N   . ARG A 25  ? 0.3171 0.2979 0.3031 -0.0037 -0.0420 -0.0389 26  ARG A N   
195  C CA  . ARG A 25  ? 0.3297 0.3053 0.3053 -0.0065 -0.0438 -0.0375 26  ARG A CA  
196  C C   . ARG A 25  ? 0.3912 0.3571 0.3563 0.0008  -0.0570 -0.0377 26  ARG A C   
197  O O   . ARG A 25  ? 0.3913 0.3652 0.3582 0.0017  -0.0632 -0.0425 26  ARG A O   
198  C CB  . ARG A 25  ? 0.3352 0.2974 0.2972 -0.0130 -0.0353 -0.0301 26  ARG A CB  
199  C CG  . ARG A 25  ? 0.3733 0.3302 0.3243 -0.0168 -0.0362 -0.0299 26  ARG A CG  
200  C CD  . ARG A 25  ? 0.4541 0.4007 0.3953 -0.0233 -0.0266 -0.0250 26  ARG A CD  
201  N NE  . ARG A 25  ? 0.4379 0.3680 0.3654 -0.0234 -0.0260 -0.0198 26  ARG A NE  
202  C CZ  . ARG A 25  ? 0.5748 0.4893 0.4841 -0.0275 -0.0245 -0.0170 26  ARG A CZ  
203  N NH1 . ARG A 25  ? 0.4809 0.3942 0.3831 -0.0308 -0.0252 -0.0189 26  ARG A NH1 
204  N NH2 . ARG A 25  ? 0.4677 0.3672 0.3648 -0.0294 -0.0218 -0.0133 26  ARG A NH2 
205  N N   A SER A 26  ? 0.3726 0.3206 0.3257 0.0058  -0.0613 -0.0327 27  SER A N   
206  N N   B SER A 26  ? 0.3680 0.3160 0.3212 0.0059  -0.0613 -0.0328 27  SER A N   
207  N N   C SER A 26  ? 0.3732 0.3211 0.3262 0.0058  -0.0613 -0.0327 27  SER A N   
208  C CA  A SER A 26  ? 0.3988 0.3310 0.3365 0.0137  -0.0744 -0.0309 27  SER A CA  
209  C CA  B SER A 26  ? 0.3926 0.3245 0.3306 0.0139  -0.0743 -0.0309 27  SER A CA  
210  C CA  C SER A 26  ? 0.3999 0.3319 0.3376 0.0138  -0.0743 -0.0309 27  SER A CA  
211  C C   A SER A 26  ? 0.4639 0.4126 0.4180 0.0240  -0.0870 -0.0397 27  SER A C   
212  C C   B SER A 26  ? 0.4586 0.4072 0.4127 0.0239  -0.0868 -0.0396 27  SER A C   
213  C C   C SER A 26  ? 0.4629 0.4115 0.4169 0.0239  -0.0869 -0.0397 27  SER A C   
214  O O   A SER A 26  ? 0.4829 0.4273 0.4277 0.0296  -0.0992 -0.0405 27  SER A O   
215  O O   B SER A 26  ? 0.4762 0.4201 0.4206 0.0294  -0.0989 -0.0403 27  SER A O   
216  O O   C SER A 26  ? 0.4810 0.4252 0.4256 0.0296  -0.0991 -0.0404 27  SER A O   
217  C CB  A SER A 26  ? 0.4510 0.3585 0.3728 0.0162  -0.0745 -0.0244 27  SER A CB  
218  C CB  B SER A 26  ? 0.4391 0.3492 0.3649 0.0172  -0.0745 -0.0254 27  SER A CB  
219  C CB  C SER A 26  ? 0.4555 0.3638 0.3785 0.0165  -0.0744 -0.0247 27  SER A CB  
220  O OG  A SER A 26  ? 0.5183 0.4324 0.4556 0.0221  -0.0752 -0.0283 27  SER A OG  
221  O OG  B SER A 26  ? 0.5153 0.4078 0.4231 0.0082  -0.0648 -0.0183 27  SER A OG  
222  O OG  C SER A 26  ? 0.5790 0.4661 0.4820 0.0243  -0.0871 -0.0214 27  SER A OG  
223  N N   . ARG A 27  ? 0.3981 0.3669 0.3766 0.0260  -0.0840 -0.0472 28  ARG A N   
224  C CA  . ARG A 27  ? 0.4021 0.3914 0.4017 0.0351  -0.0940 -0.0584 28  ARG A CA  
225  C C   . ARG A 27  ? 0.4183 0.4351 0.4362 0.0284  -0.0900 -0.0680 28  ARG A C   
226  O O   . ARG A 27  ? 0.4145 0.4537 0.4539 0.0337  -0.0960 -0.0799 28  ARG A O   
227  C CB  . ARG A 27  ? 0.4175 0.4113 0.4323 0.0405  -0.0922 -0.0626 28  ARG A CB  
228  C CG  . ARG A 27  ? 0.5135 0.4781 0.5097 0.0468  -0.0961 -0.0543 28  ARG A CG  
229  C CD  . ARG A 27  ? 0.5799 0.5477 0.5896 0.0492  -0.0910 -0.0583 28  ARG A CD  
230  N NE  . ARG A 27  ? 0.7292 0.7184 0.7643 0.0590  -0.0984 -0.0711 28  ARG A NE  
231  C CZ  . ARG A 27  ? 0.8962 0.9022 0.9523 0.0579  -0.0914 -0.0799 28  ARG A CZ  
232  N NH1 . ARG A 27  ? 0.7269 0.7541 0.8078 0.0665  -0.0976 -0.0933 28  ARG A NH1 
233  N NH2 . ARG A 27  ? 0.7121 0.7155 0.7650 0.0479  -0.0780 -0.0763 28  ARG A NH2 
234  N N   . ASP A 28  ? 0.3469 0.3617 0.3565 0.0167  -0.0793 -0.0637 29  ASP A N   
235  C CA  . ASP A 28  ? 0.3495 0.3841 0.3712 0.0079  -0.0727 -0.0713 29  ASP A CA  
236  C C   . ASP A 28  ? 0.3911 0.4475 0.4364 0.0044  -0.0645 -0.0809 29  ASP A C   
237  O O   . ASP A 28  ? 0.4078 0.4860 0.4697 0.0009  -0.0638 -0.0925 29  ASP A O   
238  C CB  . ASP A 28  ? 0.3903 0.4345 0.4130 0.0109  -0.0845 -0.0783 29  ASP A CB  
239  C CG  . ASP A 28  ? 0.5041 0.5619 0.5321 -0.0008 -0.0762 -0.0845 29  ASP A CG  
240  O OD1 . ASP A 28  ? 0.5031 0.5503 0.5213 -0.0105 -0.0633 -0.0780 29  ASP A OD1 
241  O OD2 . ASP A 28  ? 0.5683 0.6475 0.6109 -0.0001 -0.0827 -0.0966 29  ASP A OD2 
242  N N   . ILE A 29  ? 0.3017 0.3522 0.3476 0.0044  -0.0581 -0.0768 30  ILE A N   
243  C CA  . ILE A 29  ? 0.2893 0.3568 0.3530 0.0005  -0.0497 -0.0849 30  ILE A CA  
244  C C   . ILE A 29  ? 0.3211 0.3873 0.3795 -0.0121 -0.0351 -0.0813 30  ILE A C   
245  O O   . ILE A 29  ? 0.2885 0.3380 0.3318 -0.0145 -0.0302 -0.0703 30  ILE A O   
246  C CB  . ILE A 29  ? 0.3292 0.3923 0.3967 0.0075  -0.0514 -0.0842 30  ILE A CB  
247  C CG1 . ILE A 29  ? 0.3544 0.4185 0.4291 0.0216  -0.0665 -0.0894 30  ILE A CG1 
248  C CG2 . ILE A 29  ? 0.3219 0.4007 0.4040 0.0010  -0.0404 -0.0919 30  ILE A CG2 
249  C CD1 . ILE A 29  ? 0.4164 0.4676 0.4889 0.0291  -0.0686 -0.0864 30  ILE A CD1 
250  N N   . LEU A 30  ? 0.2980 0.3815 0.3687 -0.0201 -0.0282 -0.0913 31  LEU A N   
251  C CA  . LEU A 30  ? 0.3082 0.3887 0.3727 -0.0321 -0.0142 -0.0891 31  LEU A CA  
252  C C   . LEU A 30  ? 0.3346 0.3979 0.3814 -0.0365 -0.0108 -0.0792 31  LEU A C   
253  O O   . LEU A 30  ? 0.3089 0.3631 0.3466 -0.0437 -0.0005 -0.0740 31  LEU A O   
254  C CB  . LEU A 30  ? 0.3213 0.3980 0.3832 -0.0343 -0.0067 -0.0854 31  LEU A CB  
255  C CG  . LEU A 30  ? 0.4053 0.5013 0.4853 -0.0354 -0.0041 -0.0983 31  LEU A CG  
256  C CD1 . LEU A 30  ? 0.4220 0.5125 0.4951 -0.0397 0.0043  -0.0942 31  LEU A CD1 
257  C CD2 . LEU A 30  ? 0.4777 0.5913 0.5699 -0.0446 0.0024  -0.1116 31  LEU A CD2 
258  N N   . THR A 31  ? 0.2991 0.3579 0.3408 -0.0323 -0.0193 -0.0776 32  THR A N   
259  C CA  . THR A 31  ? 0.2988 0.3438 0.3260 -0.0372 -0.0154 -0.0712 32  THR A CA  
260  C C   . THR A 31  ? 0.3677 0.4221 0.4006 -0.0479 -0.0067 -0.0799 32  THR A C   
261  O O   . THR A 31  ? 0.3574 0.4317 0.4060 -0.0498 -0.0085 -0.0924 32  THR A O   
262  C CB  . THR A 31  ? 0.3585 0.3970 0.3773 -0.0315 -0.0264 -0.0691 32  THR A CB  
263  O OG1 . THR A 31  ? 0.3893 0.4457 0.4210 -0.0281 -0.0359 -0.0803 32  THR A OG1 
264  C CG2 . THR A 31  ? 0.3539 0.3774 0.3624 -0.0232 -0.0323 -0.0597 32  THR A CG2 
265  N N   . ASP A 32  ? 0.3257 0.3661 0.3470 -0.0551 0.0036  -0.0741 33  ASP A N   
266  C CA  . ASP A 32  ? 0.3251 0.3691 0.3483 -0.0667 0.0142  -0.0814 33  ASP A CA  
267  C C   . ASP A 32  ? 0.3626 0.3937 0.3746 -0.0724 0.0190  -0.0794 33  ASP A C   
268  O O   . ASP A 32  ? 0.3642 0.3919 0.3739 -0.0828 0.0298  -0.0836 33  ASP A O   
269  C CB  . ASP A 32  ? 0.3439 0.3811 0.3629 -0.0717 0.0250  -0.0778 33  ASP A CB  
270  C CG  . ASP A 32  ? 0.4775 0.4948 0.4822 -0.0668 0.0265  -0.0634 33  ASP A CG  
271  O OD1 . ASP A 32  ? 0.4248 0.4325 0.4230 -0.0613 0.0218  -0.0567 33  ASP A OD1 
272  O OD2 . ASP A 32  ? 0.6150 0.6272 0.6149 -0.0687 0.0323  -0.0597 33  ASP A OD2 
273  N N   . VAL A 33  ? 0.3072 0.3297 0.3111 -0.0668 0.0122  -0.0736 34  VAL A N   
274  C CA  . VAL A 33  ? 0.3102 0.3211 0.3038 -0.0724 0.0168  -0.0731 34  VAL A CA  
275  C C   . VAL A 33  ? 0.3554 0.3660 0.3436 -0.0672 0.0060  -0.0723 34  VAL A C   
276  O O   . VAL A 33  ? 0.3465 0.3561 0.3330 -0.0583 -0.0030 -0.0671 34  VAL A O   
277  C CB  . VAL A 33  ? 0.3464 0.3350 0.3277 -0.0735 0.0271  -0.0627 34  VAL A CB  
278  C CG1 . VAL A 33  ? 0.3244 0.3036 0.2997 -0.0642 0.0222  -0.0522 34  VAL A CG1 
279  C CG2 . VAL A 33  ? 0.3615 0.3378 0.3344 -0.0815 0.0356  -0.0649 34  VAL A CG2 
280  N N   A VAL A 34  ? 0.3237 0.3332 0.3069 -0.0737 0.0075  -0.0777 35  VAL A N   
281  N N   B VAL A 34  ? 0.3133 0.3228 0.2964 -0.0735 0.0073  -0.0777 35  VAL A N   
282  C CA  A VAL A 34  ? 0.3306 0.3357 0.3030 -0.0713 -0.0007 -0.0769 35  VAL A CA  
283  C CA  B VAL A 34  ? 0.3144 0.3193 0.2867 -0.0706 -0.0013 -0.0763 35  VAL A CA  
284  C C   A VAL A 34  ? 0.3700 0.3551 0.3291 -0.0765 0.0099  -0.0717 35  VAL A C   
285  C C   B VAL A 34  ? 0.3673 0.3534 0.3262 -0.0765 0.0089  -0.0724 35  VAL A C   
286  O O   A VAL A 34  ? 0.3756 0.3564 0.3354 -0.0847 0.0209  -0.0754 35  VAL A O   
287  O O   B VAL A 34  ? 0.3743 0.3578 0.3340 -0.0853 0.0190  -0.0774 35  VAL A O   
288  C CB  A VAL A 34  ? 0.3928 0.4156 0.3705 -0.0750 -0.0086 -0.0895 35  VAL A CB  
289  C CB  B VAL A 34  ? 0.3657 0.3887 0.3431 -0.0704 -0.0134 -0.0871 35  VAL A CB  
290  C CG1 A VAL A 34  ? 0.4032 0.4184 0.3648 -0.0730 -0.0176 -0.0876 35  VAL A CG1 
291  C CG1 B VAL A 34  ? 0.3638 0.3982 0.3484 -0.0819 -0.0067 -0.0995 35  VAL A CG1 
292  C CG2 A VAL A 34  ? 0.3884 0.4337 0.3836 -0.0690 -0.0189 -0.0968 35  VAL A CG2 
293  C CG2 B VAL A 34  ? 0.3744 0.3878 0.3348 -0.0662 -0.0236 -0.0830 35  VAL A CG2 
294  N N   . ILE A 35  ? 0.3228 0.2948 0.2700 -0.0719 0.0075  -0.0639 36  ILE A N   
295  C CA  . ILE A 35  ? 0.3311 0.2861 0.2673 -0.0760 0.0170  -0.0607 36  ILE A CA  
296  C C   . ILE A 35  ? 0.4030 0.3569 0.3269 -0.0800 0.0116  -0.0654 36  ILE A C   
297  O O   . ILE A 35  ? 0.3973 0.3516 0.3132 -0.0752 0.0006  -0.0630 36  ILE A O   
298  C CB  . ILE A 35  ? 0.3534 0.2962 0.2857 -0.0700 0.0199  -0.0509 36  ILE A CB  
299  C CG1 . ILE A 35  ? 0.3449 0.2908 0.2882 -0.0651 0.0223  -0.0461 36  ILE A CG1 
300  C CG2 . ILE A 35  ? 0.3821 0.3100 0.3068 -0.0741 0.0305  -0.0502 36  ILE A CG2 
301  C CD1 . ILE A 35  ? 0.3540 0.2971 0.3023 -0.0698 0.0324  -0.0481 36  ILE A CD1 
302  N N   . VAL A 36  ? 0.3689 0.3199 0.2896 -0.0891 0.0193  -0.0722 37  VAL A N   
303  C CA  . VAL A 36  ? 0.3756 0.3260 0.2832 -0.0947 0.0151  -0.0780 37  VAL A CA  
304  C C   . VAL A 36  ? 0.4532 0.3845 0.3469 -0.0979 0.0243  -0.0746 37  VAL A C   
305  O O   . VAL A 36  ? 0.4337 0.3553 0.3307 -0.1014 0.0375  -0.0750 37  VAL A O   
306  C CB  . VAL A 36  ? 0.4229 0.3858 0.3364 -0.1040 0.0166  -0.0906 37  VAL A CB  
307  C CG1 . VAL A 36  ? 0.4344 0.3976 0.3328 -0.1098 0.0110  -0.0970 37  VAL A CG1 
308  C CG2 . VAL A 36  ? 0.4147 0.3997 0.3447 -0.1009 0.0078  -0.0960 37  VAL A CG2 
309  N N   . VAL A 37  ? 0.4226 0.3474 0.2999 -0.0967 0.0175  -0.0717 38  VAL A N   
310  C CA  . VAL A 37  ? 0.4287 0.3368 0.2917 -0.1008 0.0261  -0.0697 38  VAL A CA  
311  C C   . VAL A 37  ? 0.5321 0.4382 0.3752 -0.1077 0.0201  -0.0753 38  VAL A C   
312  O O   . VAL A 37  ? 0.5043 0.4080 0.3325 -0.1045 0.0082  -0.0717 38  VAL A O   
313  C CB  . VAL A 37  ? 0.4695 0.3694 0.3296 -0.0941 0.0258  -0.0605 38  VAL A CB  
314  C CG1 . VAL A 37  ? 0.4776 0.3633 0.3294 -0.0991 0.0385  -0.0608 38  VAL A CG1 
315  C CG2 . VAL A 37  ? 0.4471 0.3537 0.3267 -0.0861 0.0267  -0.0554 38  VAL A CG2 
316  N N   A SER A 38  ? 0.5414 0.4486 0.3836 -0.1170 0.0270  -0.0845 39  SER A N   
317  N N   B SER A 38  ? 0.5289 0.4339 0.3701 -0.1173 0.0285  -0.0840 39  SER A N   
318  C CA  A SER A 38  ? 0.5671 0.4749 0.3911 -0.1253 0.0217  -0.0921 39  SER A CA  
319  C CA  B SER A 38  ? 0.5502 0.4547 0.3730 -0.1261 0.0246  -0.0917 39  SER A CA  
320  C C   A SER A 38  ? 0.5789 0.5042 0.4038 -0.1206 0.0026  -0.0944 39  SER A C   
321  C C   B SER A 38  ? 0.5752 0.4916 0.3906 -0.1214 0.0045  -0.0918 39  SER A C   
322  O O   A SER A 38  ? 0.5568 0.4989 0.4016 -0.1191 0.0005  -0.0994 39  SER A O   
323  O O   B SER A 38  ? 0.5820 0.4892 0.3751 -0.1200 -0.0047 -0.0875 39  SER A O   
324  C CB  A SER A 38  ? 0.6570 0.5471 0.4561 -0.1292 0.0242  -0.0889 39  SER A CB  
325  C CB  B SER A 38  ? 0.6220 0.5082 0.4247 -0.1325 0.0336  -0.0912 39  SER A CB  
326  O OG  A SER A 38  ? 0.8490 0.7266 0.6519 -0.1322 0.0415  -0.0884 39  SER A OG  
327  O OG  B SER A 38  ? 0.7205 0.5996 0.5322 -0.1382 0.0512  -0.0961 39  SER A OG  
328  N N   A ARG A 39  ? 0.5360 0.4564 0.3393 -0.1178 -0.0112 -0.0910 40  ARG A N   
329  N N   B ARG A 39  ? 0.4958 0.4318 0.3309 -0.1181 -0.0019 -0.0964 40  ARG A N   
330  C CA  A ARG A 39  ? 0.5340 0.4690 0.3359 -0.1109 -0.0317 -0.0930 40  ARG A CA  
331  C CA  B ARG A 39  ? 0.4916 0.4460 0.3305 -0.1120 -0.0207 -0.0997 40  ARG A CA  
332  C C   A ARG A 39  ? 0.5618 0.5004 0.3750 -0.0972 -0.0412 -0.0846 40  ARG A C   
333  C C   B ARG A 39  ? 0.5170 0.4700 0.3575 -0.0984 -0.0321 -0.0894 40  ARG A C   
334  O O   A ARG A 39  ? 0.5553 0.5076 0.3726 -0.0892 -0.0583 -0.0868 40  ARG A O   
335  O O   B ARG A 39  ? 0.5120 0.4831 0.3664 -0.0912 -0.0445 -0.0927 40  ARG A O   
336  C CB  A ARG A 39  ? 0.5572 0.4812 0.3262 -0.1135 -0.0433 -0.0926 40  ARG A CB  
337  C CB  B ARG A 39  ? 0.5178 0.4754 0.3366 -0.1170 -0.0322 -0.1068 40  ARG A CB  
338  C CG  A ARG A 39  ? 0.6465 0.5754 0.4060 -0.1262 -0.0404 -0.1044 40  ARG A CG  
339  C CG  B ARG A 39  ? 0.6496 0.6162 0.4733 -0.1304 -0.0230 -0.1204 40  ARG A CG  
340  C CD  A ARG A 39  ? 0.6660 0.5867 0.3920 -0.1270 -0.0562 -0.1039 40  ARG A CD  
341  C CD  B ARG A 39  ? 0.7423 0.7217 0.5534 -0.1343 -0.0379 -0.1302 40  ARG A CD  
342  N NE  A ARG A 39  ? 0.7161 0.6382 0.4284 -0.1409 -0.0515 -0.1150 40  ARG A NE  
343  N NE  B ARG A 39  ? 0.8150 0.8023 0.6303 -0.1489 -0.0274 -0.1442 40  ARG A NE  
344  C CZ  A ARG A 39  ? 0.8773 0.8220 0.5976 -0.1444 -0.0605 -0.1276 40  ARG A CZ  
345  C CZ  B ARG A 39  ? 0.9670 0.9388 0.7630 -0.1604 -0.0167 -0.1475 40  ARG A CZ  
346  N NH1 A ARG A 39  ? 0.7456 0.6896 0.4515 -0.1583 -0.0549 -0.1378 40  ARG A NH1 
347  N NH1 B ARG A 39  ? 0.7715 0.7202 0.5429 -0.1597 -0.0145 -0.1381 40  ARG A NH1 
348  N NH2 A ARG A 39  ? 0.6726 0.6422 0.4165 -0.1348 -0.0744 -0.1315 40  ARG A NH2 
349  N NH2 B ARG A 39  ? 0.8177 0.7968 0.6189 -0.1738 -0.0069 -0.1612 40  ARG A NH2 
350  N N   A GLU A 40  ? 0.4960 0.4232 0.3147 -0.0942 -0.0307 -0.0759 41  GLU A N   
351  N N   B GLU A 40  ? 0.4716 0.4048 0.3007 -0.0955 -0.0267 -0.0786 41  GLU A N   
352  C CA  A GLU A 40  ? 0.4791 0.4076 0.3072 -0.0825 -0.0377 -0.0682 41  GLU A CA  
353  C CA  B GLU A 40  ? 0.4648 0.3939 0.2950 -0.0841 -0.0349 -0.0691 41  GLU A CA  
354  C C   A GLU A 40  ? 0.4940 0.4382 0.3520 -0.0798 -0.0312 -0.0703 41  GLU A C   
355  C C   B GLU A 40  ? 0.4878 0.4301 0.3465 -0.0794 -0.0295 -0.0689 41  GLU A C   
356  O O   A GLU A 40  ? 0.4673 0.4122 0.3354 -0.0865 -0.0170 -0.0735 41  GLU A O   
357  O O   B GLU A 40  ? 0.4597 0.4001 0.3286 -0.0843 -0.0147 -0.0695 41  GLU A O   
358  C CB  A GLU A 40  ? 0.5068 0.4128 0.3189 -0.0813 -0.0322 -0.0576 41  GLU A CB  
359  C CB  B GLU A 40  ? 0.4960 0.4012 0.3066 -0.0853 -0.0280 -0.0598 41  GLU A CB  
360  C CG  A GLU A 40  ? 0.7171 0.6037 0.4951 -0.0847 -0.0384 -0.0546 41  GLU A CG  
361  C CG  B GLU A 40  ? 0.6812 0.5699 0.4586 -0.0885 -0.0359 -0.0579 41  GLU A CG  
362  C CD  A GLU A 40  ? 1.1897 1.0665 0.9526 -0.0747 -0.0544 -0.0471 41  GLU A CD  
363  C CD  B GLU A 40  ? 1.1379 1.0166 0.9007 -0.0786 -0.0512 -0.0498 41  GLU A CD  
364  O OE1 A GLU A 40  ? 1.1943 1.0600 0.9569 -0.0708 -0.0508 -0.0394 41  GLU A OE1 
365  O OE1 B GLU A 40  ? 1.1649 1.0486 0.9190 -0.0732 -0.0686 -0.0518 41  GLU A OE1 
366  O OE2 A GLU A 40  ? 1.2037 1.0834 0.9547 -0.0707 -0.0710 -0.0493 41  GLU A OE2 
367  O OE2 B GLU A 40  ? 1.1529 1.0186 0.9131 -0.0759 -0.0461 -0.0420 41  GLU A OE2 
368  N N   . GLN A 41  ? 0.4378 0.3924 0.3082 -0.0697 -0.0416 -0.0684 42  GLN A N   
369  C CA  . GLN A 41  ? 0.4163 0.3853 0.3123 -0.0665 -0.0372 -0.0702 42  GLN A CA  
370  C C   . GLN A 41  ? 0.4437 0.4055 0.3418 -0.0576 -0.0390 -0.0608 42  GLN A C   
371  O O   . GLN A 41  ? 0.4468 0.4010 0.3326 -0.0505 -0.0506 -0.0563 42  GLN A O   
372  C CB  . GLN A 41  ? 0.4372 0.4311 0.3497 -0.0641 -0.0480 -0.0810 42  GLN A CB  
373  C CG  . GLN A 41  ? 0.6587 0.6639 0.5742 -0.0749 -0.0439 -0.0927 42  GLN A CG  
374  C CD  . GLN A 41  ? 0.8780 0.9119 0.8153 -0.0744 -0.0514 -0.1058 42  GLN A CD  
375  O OE1 . GLN A 41  ? 0.7805 0.8276 0.7328 -0.0652 -0.0601 -0.1070 42  GLN A OE1 
376  N NE2 . GLN A 41  ? 0.8901 0.9350 0.8307 -0.0851 -0.0473 -0.1175 42  GLN A NE2 
377  N N   . PHE A 42  ? 0.3672 0.3295 0.2787 -0.0580 -0.0277 -0.0578 43  PHE A N   
378  C CA  . PHE A 42  ? 0.3652 0.3223 0.2801 -0.0509 -0.0278 -0.0500 43  PHE A CA  
379  C C   . PHE A 42  ? 0.4021 0.3744 0.3387 -0.0489 -0.0246 -0.0529 43  PHE A C   
380  O O   . PHE A 42  ? 0.4081 0.3823 0.3520 -0.0548 -0.0135 -0.0547 43  PHE A O   
381  C CB  . PHE A 42  ? 0.3821 0.3227 0.2883 -0.0540 -0.0163 -0.0430 43  PHE A CB  
382  C CG  . PHE A 42  ? 0.4169 0.3412 0.3004 -0.0581 -0.0164 -0.0410 43  PHE A CG  
383  C CD1 . PHE A 42  ? 0.4433 0.3639 0.3197 -0.0666 -0.0093 -0.0454 43  PHE A CD1 
384  C CD2 . PHE A 42  ? 0.4615 0.3723 0.3291 -0.0547 -0.0223 -0.0350 43  PHE A CD2 
385  C CE1 . PHE A 42  ? 0.4763 0.3817 0.3300 -0.0717 -0.0086 -0.0444 43  PHE A CE1 
386  C CE2 . PHE A 42  ? 0.5150 0.4086 0.3581 -0.0603 -0.0213 -0.0334 43  PHE A CE2 
387  C CZ  . PHE A 42  ? 0.4895 0.3813 0.3260 -0.0689 -0.0144 -0.0383 43  PHE A CZ  
388  N N   . ARG A 43  ? 0.3618 0.3433 0.3073 -0.0411 -0.0340 -0.0538 44  ARG A N   
389  C CA  . ARG A 43  ? 0.3353 0.3313 0.3004 -0.0400 -0.0305 -0.0574 44  ARG A CA  
390  C C   . ARG A 43  ? 0.3719 0.3583 0.3364 -0.0379 -0.0236 -0.0488 44  ARG A C   
391  O O   . ARG A 43  ? 0.3609 0.3349 0.3151 -0.0337 -0.0267 -0.0421 44  ARG A O   
392  C CB  . ARG A 43  ? 0.3485 0.3609 0.3261 -0.0324 -0.0431 -0.0643 44  ARG A CB  
393  C CG  . ARG A 43  ? 0.4172 0.4450 0.3997 -0.0343 -0.0508 -0.0752 44  ARG A CG  
394  C CD  . ARG A 43  ? 0.4941 0.5468 0.4996 -0.0296 -0.0578 -0.0866 44  ARG A CD  
395  N NE  . ARG A 43  ? 0.6242 0.6850 0.6444 -0.0344 -0.0455 -0.0890 44  ARG A NE  
396  C CZ  . ARG A 43  ? 0.7806 0.8534 0.8112 -0.0449 -0.0350 -0.0975 44  ARG A CZ  
397  N NH1 . ARG A 43  ? 0.7040 0.7860 0.7361 -0.0516 -0.0355 -0.1063 44  ARG A NH1 
398  N NH2 . ARG A 43  ? 0.5398 0.6149 0.5782 -0.0494 -0.0240 -0.0979 44  ARG A NH2 
399  N N   . ALA A 44  ? 0.3250 0.3165 0.2993 -0.0413 -0.0142 -0.0494 45  ALA A N   
400  C CA  . ALA A 44  ? 0.3210 0.3055 0.2950 -0.0391 -0.0089 -0.0419 45  ALA A CA  
401  C C   . ALA A 44  ? 0.3307 0.3242 0.3155 -0.0414 -0.0028 -0.0443 45  ALA A C   
402  O O   . ALA A 44  ? 0.3028 0.3073 0.2956 -0.0459 -0.0011 -0.0522 45  ALA A O   
403  C CB  . ALA A 44  ? 0.3395 0.3093 0.3031 -0.0420 -0.0012 -0.0358 45  ALA A CB  
404  N N   . HIS A 45  ? 0.2848 0.2739 0.2691 -0.0391 0.0006  -0.0382 46  HIS A N   
405  C CA  . HIS A 45  ? 0.2717 0.2652 0.2609 -0.0417 0.0068  -0.0386 46  HIS A CA  
406  C C   . HIS A 45  ? 0.3025 0.2833 0.2835 -0.0450 0.0154  -0.0331 46  HIS A C   
407  O O   . HIS A 45  ? 0.2990 0.2708 0.2747 -0.0415 0.0157  -0.0269 46  HIS A O   
408  C CB  . HIS A 45  ? 0.2664 0.2626 0.2585 -0.0368 0.0042  -0.0355 46  HIS A CB  
409  C CG  . HIS A 45  ? 0.2990 0.3044 0.2988 -0.0322 -0.0041 -0.0406 46  HIS A CG  
410  N ND1 . HIS A 45  ? 0.3226 0.3210 0.3175 -0.0266 -0.0110 -0.0375 46  HIS A ND1 
411  C CD2 . HIS A 45  ? 0.3089 0.3287 0.3206 -0.0323 -0.0062 -0.0494 46  HIS A CD2 
412  C CE1 . HIS A 45  ? 0.3125 0.3191 0.3154 -0.0221 -0.0182 -0.0433 46  HIS A CE1 
413  N NE2 . HIS A 45  ? 0.3028 0.3244 0.3179 -0.0248 -0.0159 -0.0512 46  HIS A NE2 
414  N N   . LYS A 46  ? 0.2933 0.2726 0.2732 -0.0515 0.0225  -0.0360 47  LYS A N   
415  C CA  . LYS A 46  ? 0.3022 0.2658 0.2727 -0.0536 0.0305  -0.0306 47  LYS A CA  
416  C C   . LYS A 46  ? 0.3309 0.2887 0.2979 -0.0472 0.0298  -0.0221 47  LYS A C   
417  O O   . LYS A 46  ? 0.3088 0.2562 0.2714 -0.0436 0.0313  -0.0170 47  LYS A O   
418  C CB  . LYS A 46  ? 0.3301 0.2904 0.2972 -0.0622 0.0390  -0.0346 47  LYS A CB  
419  C CG  . LYS A 46  ? 0.3738 0.3380 0.3437 -0.0699 0.0418  -0.0436 47  LYS A CG  
420  C CD  . LYS A 46  ? 0.3691 0.3314 0.3363 -0.0804 0.0515  -0.0492 47  LYS A CD  
421  C CE  . LYS A 46  ? 0.4000 0.3707 0.3729 -0.0891 0.0541  -0.0606 47  LYS A CE  
422  N NZ  . LYS A 46  ? 0.4128 0.3825 0.3835 -0.1015 0.0652  -0.0680 47  LYS A NZ  
423  N N   . THR A 47  ? 0.2993 0.2653 0.2691 -0.0457 0.0273  -0.0217 48  THR A N   
424  C CA  . THR A 47  ? 0.3053 0.2680 0.2716 -0.0403 0.0258  -0.0148 48  THR A CA  
425  C C   . THR A 47  ? 0.3112 0.2746 0.2809 -0.0340 0.0213  -0.0118 48  THR A C   
426  O O   . THR A 47  ? 0.3167 0.2743 0.2838 -0.0297 0.0218  -0.0068 48  THR A O   
427  C CB  . THR A 47  ? 0.3474 0.3195 0.3156 -0.0413 0.0244  -0.0163 48  THR A CB  
428  O OG1 . THR A 47  ? 0.3881 0.3730 0.3666 -0.0404 0.0194  -0.0222 48  THR A OG1 
429  C CG2 . THR A 47  ? 0.3920 0.3601 0.3530 -0.0491 0.0315  -0.0186 48  THR A CG2 
430  N N   . VAL A 48  ? 0.2615 0.2312 0.2363 -0.0335 0.0169  -0.0153 49  VAL A N   
431  C CA  . VAL A 48  ? 0.2601 0.2282 0.2354 -0.0299 0.0143  -0.0133 49  VAL A CA  
432  C C   . VAL A 48  ? 0.2988 0.2574 0.2706 -0.0303 0.0185  -0.0120 49  VAL A C   
433  O O   . VAL A 48  ? 0.2752 0.2320 0.2484 -0.0270 0.0197  -0.0097 49  VAL A O   
434  C CB  . VAL A 48  ? 0.2842 0.2560 0.2609 -0.0297 0.0088  -0.0165 49  VAL A CB  
435  C CG1 . VAL A 48  ? 0.2923 0.2585 0.2656 -0.0284 0.0084  -0.0147 49  VAL A CG1 
436  C CG2 . VAL A 48  ? 0.2840 0.2647 0.2659 -0.0282 0.0053  -0.0184 49  VAL A CG2 
437  N N   . LEU A 49  ? 0.2803 0.2342 0.2489 -0.0345 0.0212  -0.0149 50  LEU A N   
438  C CA  . LEU A 49  ? 0.2816 0.2256 0.2466 -0.0357 0.0264  -0.0149 50  LEU A CA  
439  C C   . LEU A 49  ? 0.3204 0.2571 0.2853 -0.0317 0.0307  -0.0107 50  LEU A C   
440  O O   . LEU A 49  ? 0.3251 0.2581 0.2920 -0.0284 0.0328  -0.0099 50  LEU A O   
441  C CB  . LEU A 49  ? 0.2790 0.2198 0.2404 -0.0420 0.0290  -0.0197 50  LEU A CB  
442  C CG  . LEU A 49  ? 0.3170 0.2650 0.2779 -0.0447 0.0230  -0.0247 50  LEU A CG  
443  C CD1 . LEU A 49  ? 0.3178 0.2652 0.2767 -0.0515 0.0259  -0.0308 50  LEU A CD1 
444  C CD2 . LEU A 49  ? 0.3451 0.2890 0.3006 -0.0434 0.0203  -0.0236 50  LEU A CD2 
445  N N   . MET A 50  ? 0.2911 0.2257 0.2533 -0.0317 0.0316  -0.0082 51  MET A N   
446  C CA  . MET A 50  ? 0.3105 0.2349 0.2689 -0.0266 0.0338  -0.0029 51  MET A CA  
447  C C   . MET A 50  ? 0.3478 0.2798 0.3124 -0.0187 0.0289  0.0001  51  MET A C   
448  O O   . MET A 50  ? 0.3532 0.2799 0.3198 -0.0123 0.0295  0.0022  51  MET A O   
449  C CB  . MET A 50  ? 0.3396 0.2583 0.2894 -0.0296 0.0356  -0.0005 51  MET A CB  
450  C CG  . MET A 50  ? 0.3796 0.2910 0.3240 -0.0387 0.0422  -0.0049 51  MET A CG  
451  S SD  . MET A 50  ? 0.4340 0.3442 0.3697 -0.0452 0.0450  -0.0048 51  MET A SD  
452  C CE  . MET A 50  ? 0.4096 0.2946 0.3290 -0.0410 0.0488  0.0040  51  MET A CE  
453  N N   . ALA A 51  ? 0.3014 0.2465 0.2702 -0.0191 0.0240  -0.0008 52  ALA A N   
454  C CA  . ALA A 51  ? 0.2923 0.2470 0.2675 -0.0135 0.0196  0.0003  52  ALA A CA  
455  C C   . ALA A 51  ? 0.3348 0.2926 0.3180 -0.0117 0.0210  -0.0028 52  ALA A C   
456  O O   . ALA A 51  ? 0.3325 0.2980 0.3231 -0.0065 0.0189  -0.0031 52  ALA A O   
457  C CB  . ALA A 51  ? 0.2945 0.2605 0.2716 -0.0160 0.0156  -0.0013 52  ALA A CB  
458  N N   . CYS A 52  ? 0.2780 0.2308 0.2593 -0.0167 0.0247  -0.0061 53  CYS A N   
459  C CA  . CYS A 52  ? 0.2931 0.2471 0.2787 -0.0177 0.0278  -0.0101 53  CYS A CA  
460  C C   . CYS A 52  ? 0.3374 0.2826 0.3239 -0.0167 0.0339  -0.0120 53  CYS A C   
461  O O   . CYS A 52  ? 0.3159 0.2638 0.3077 -0.0173 0.0375  -0.0163 53  CYS A O   
462  C CB  . CYS A 52  ? 0.2917 0.2447 0.2713 -0.0244 0.0272  -0.0126 53  CYS A CB  
463  S SG  . CYS A 52  ? 0.3154 0.2768 0.2951 -0.0248 0.0209  -0.0118 53  CYS A SG  
464  N N   . SER A 53  ? 0.3067 0.2407 0.2871 -0.0172 0.0363  -0.0102 54  SER A N   
465  C CA  . SER A 53  ? 0.3085 0.2316 0.2879 -0.0180 0.0431  -0.0131 54  SER A CA  
466  C C   . SER A 53  ? 0.3574 0.2683 0.3344 -0.0126 0.0449  -0.0093 54  SER A C   
467  O O   . SER A 53  ? 0.3442 0.2489 0.3127 -0.0150 0.0441  -0.0059 54  SER A O   
468  C CB  . SER A 53  ? 0.3254 0.2436 0.2957 -0.0273 0.0455  -0.0162 54  SER A CB  
469  O OG  . SER A 53  ? 0.3667 0.2724 0.3326 -0.0303 0.0521  -0.0187 54  SER A OG  
470  N N   . GLY A 54  ? 0.3339 0.2398 0.3175 -0.0058 0.0481  -0.0108 55  GLY A N   
471  C CA  . GLY A 54  ? 0.3421 0.2310 0.3210 0.0007  0.0498  -0.0069 55  GLY A CA  
472  C C   . GLY A 54  ? 0.3827 0.2548 0.3497 -0.0077 0.0569  -0.0080 55  GLY A C   
473  O O   . GLY A 54  ? 0.3836 0.2401 0.3398 -0.0073 0.0581  -0.0033 55  GLY A O   
474  N N   . LEU A 55  ? 0.3539 0.2286 0.3206 -0.0168 0.0617  -0.0145 56  LEU A N   
475  C CA  . LEU A 55  ? 0.3583 0.2202 0.3146 -0.0262 0.0680  -0.0174 56  LEU A CA  
476  C C   . LEU A 55  ? 0.3983 0.2632 0.3469 -0.0328 0.0650  -0.0151 56  LEU A C   
477  O O   . LEU A 55  ? 0.3731 0.2241 0.3128 -0.0364 0.0695  -0.0140 56  LEU A O   
478  C CB  . LEU A 55  ? 0.3514 0.2172 0.3078 -0.0343 0.0723  -0.0253 56  LEU A CB  
479  C CG  . LEU A 55  ? 0.4280 0.2825 0.3749 -0.0445 0.0790  -0.0302 56  LEU A CG  
480  C CD1 . LEU A 55  ? 0.4570 0.2904 0.4019 -0.0418 0.0879  -0.0312 56  LEU A CD1 
481  C CD2 . LEU A 55  ? 0.4264 0.2882 0.3704 -0.0531 0.0798  -0.0371 56  LEU A CD2 
482  N N   . PHE A 56  ? 0.3422 0.2244 0.2942 -0.0344 0.0581  -0.0150 57  PHE A N   
483  C CA  . PHE A 56  ? 0.3237 0.2115 0.2717 -0.0399 0.0553  -0.0146 57  PHE A CA  
484  C C   . PHE A 56  ? 0.3690 0.2499 0.3123 -0.0359 0.0547  -0.0083 57  PHE A C   
485  O O   . PHE A 56  ? 0.3638 0.2398 0.2999 -0.0424 0.0579  -0.0089 57  PHE A O   
486  C CB  . PHE A 56  ? 0.3274 0.2331 0.2803 -0.0412 0.0479  -0.0165 57  PHE A CB  
487  C CG  . PHE A 56  ? 0.3296 0.2384 0.2809 -0.0473 0.0480  -0.0226 57  PHE A CG  
488  C CD1 . PHE A 56  ? 0.3648 0.2704 0.3118 -0.0554 0.0518  -0.0282 57  PHE A CD1 
489  C CD2 . PHE A 56  ? 0.3416 0.2562 0.2941 -0.0458 0.0444  -0.0232 57  PHE A CD2 
490  C CE1 . PHE A 56  ? 0.3628 0.2712 0.3064 -0.0608 0.0507  -0.0339 57  PHE A CE1 
491  C CE2 . PHE A 56  ? 0.3682 0.2828 0.3147 -0.0516 0.0437  -0.0280 57  PHE A CE2 
492  C CZ  . PHE A 56  ? 0.3389 0.2510 0.2811 -0.0585 0.0461  -0.0332 57  PHE A CZ  
493  N N   . TYR A 57  ? 0.3483 0.2283 0.2945 -0.0258 0.0511  -0.0028 58  TYR A N   
494  C CA  . TYR A 57  ? 0.3663 0.2372 0.3043 -0.0211 0.0493  0.0041  58  TYR A CA  
495  C C   . TYR A 57  ? 0.4252 0.2707 0.3495 -0.0241 0.0573  0.0058  58  TYR A C   
496  O O   . TYR A 57  ? 0.4155 0.2515 0.3274 -0.0294 0.0599  0.0083  58  TYR A O   
497  C CB  . TYR A 57  ? 0.3848 0.2597 0.3297 -0.0085 0.0432  0.0083  58  TYR A CB  
498  C CG  . TYR A 57  ? 0.4444 0.3073 0.3781 -0.0019 0.0398  0.0162  58  TYR A CG  
499  C CD1 . TYR A 57  ? 0.4649 0.3317 0.3901 -0.0057 0.0368  0.0193  58  TYR A CD1 
500  C CD2 . TYR A 57  ? 0.5040 0.3499 0.4341 0.0085  0.0395  0.0204  58  TYR A CD2 
501  C CE1 . TYR A 57  ? 0.5040 0.3576 0.4147 -0.0004 0.0335  0.0270  58  TYR A CE1 
502  C CE2 . TYR A 57  ? 0.5550 0.3868 0.4710 0.0156  0.0348  0.0287  58  TYR A CE2 
503  C CZ  . TYR A 57  ? 0.6417 0.4771 0.5467 0.0106  0.0318  0.0323  58  TYR A CZ  
504  O OH  . TYR A 57  ? 0.7224 0.5419 0.6098 0.0170  0.0271  0.0409  58  TYR A OH  
505  N N   A SER A 58  ? 0.4033 0.2367 0.3292 -0.0216 0.0624  0.0036  59  SER A N   
506  N N   B SER A 58  ? 0.4050 0.2385 0.3310 -0.0217 0.0624  0.0036  59  SER A N   
507  C CA  A SER A 58  ? 0.4237 0.2300 0.3365 -0.0245 0.0710  0.0044  59  SER A CA  
508  C CA  B SER A 58  ? 0.4274 0.2340 0.3405 -0.0246 0.0711  0.0043  59  SER A CA  
509  C C   A SER A 58  ? 0.4946 0.2988 0.4001 -0.0402 0.0785  -0.0016 59  SER A C   
510  C C   B SER A 58  ? 0.4939 0.2986 0.3996 -0.0402 0.0784  -0.0015 59  SER A C   
511  O O   A SER A 58  ? 0.5220 0.3069 0.4124 -0.0458 0.0847  0.0006  59  SER A O   
512  O O   B SER A 58  ? 0.5185 0.3043 0.4090 -0.0457 0.0842  0.0008  59  SER A O   
513  C CB  A SER A 58  ? 0.4509 0.2476 0.3699 -0.0187 0.0751  0.0013  59  SER A CB  
514  C CB  B SER A 58  ? 0.4617 0.2595 0.3813 -0.0196 0.0754  0.0006  59  SER A CB  
515  O OG  A SER A 58  ? 0.4797 0.2763 0.4056 -0.0035 0.0688  0.0060  59  SER A OG  
516  O OG  B SER A 58  ? 0.5490 0.3181 0.4553 -0.0224 0.0845  0.0009  59  SER A OG  
517  N N   . ILE A 59  ? 0.4375 0.2615 0.3531 -0.0474 0.0778  -0.0095 60  ILE A N   
518  C CA  . ILE A 59  ? 0.4299 0.2585 0.3430 -0.0614 0.0829  -0.0174 60  ILE A CA  
519  C C   . ILE A 59  ? 0.4673 0.3016 0.3759 -0.0671 0.0821  -0.0166 60  ILE A C   
520  O O   . ILE A 59  ? 0.4917 0.3144 0.3906 -0.0774 0.0906  -0.0199 60  ILE A O   
521  C CB  . ILE A 59  ? 0.4490 0.2993 0.3733 -0.0653 0.0787  -0.0253 60  ILE A CB  
522  C CG1 . ILE A 59  ? 0.4506 0.2934 0.3763 -0.0639 0.0825  -0.0285 60  ILE A CG1 
523  C CG2 . ILE A 59  ? 0.4328 0.2941 0.3576 -0.0781 0.0807  -0.0343 60  ILE A CG2 
524  C CD1 . ILE A 59  ? 0.4575 0.3189 0.3899 -0.0661 0.0769  -0.0340 60  ILE A CD1 
525  N N   . PHE A 60  ? 0.3903 0.2422 0.3058 -0.0616 0.0733  -0.0136 61  PHE A N   
526  C CA  . PHE A 60  ? 0.3911 0.2516 0.3045 -0.0679 0.0733  -0.0152 61  PHE A CA  
527  C C   . PHE A 60  ? 0.4570 0.2987 0.3543 -0.0667 0.0763  -0.0072 61  PHE A C   
528  O O   . PHE A 60  ? 0.4714 0.3179 0.3644 -0.0740 0.0785  -0.0093 61  PHE A O   
529  C CB  . PHE A 60  ? 0.3792 0.2662 0.3065 -0.0646 0.0637  -0.0174 61  PHE A CB  
530  C CG  . PHE A 60  ? 0.3749 0.2767 0.3130 -0.0672 0.0606  -0.0253 61  PHE A CG  
531  C CD1 . PHE A 60  ? 0.4135 0.3201 0.3532 -0.0778 0.0651  -0.0349 61  PHE A CD1 
532  C CD2 . PHE A 60  ? 0.3885 0.2992 0.3337 -0.0597 0.0531  -0.0236 61  PHE A CD2 
533  C CE1 . PHE A 60  ? 0.4212 0.3407 0.3685 -0.0794 0.0606  -0.0418 61  PHE A CE1 
534  C CE2 . PHE A 60  ? 0.4179 0.3386 0.3682 -0.0622 0.0497  -0.0298 61  PHE A CE2 
535  C CZ  . PHE A 60  ? 0.3955 0.3206 0.3464 -0.0713 0.0525  -0.0385 61  PHE A CZ  
536  N N   . THR A 61  ? 0.4409 0.2604 0.3281 -0.0580 0.0767  0.0012  62  THR A N   
537  C CA  . THR A 61  ? 0.4617 0.2574 0.3283 -0.0567 0.0792  0.0097  62  THR A CA  
538  C C   . THR A 61  ? 0.5592 0.3255 0.4089 -0.0657 0.0916  0.0086  62  THR A C   
539  O O   . THR A 61  ? 0.5778 0.3180 0.4049 -0.0678 0.0962  0.0151  62  THR A O   
540  C CB  . THR A 61  ? 0.5593 0.3480 0.4232 -0.0404 0.0702  0.0199  62  THR A CB  
541  O OG1 . THR A 61  ? 0.5249 0.3076 0.3971 -0.0318 0.0697  0.0198  62  THR A OG1 
542  C CG2 . THR A 61  ? 0.5065 0.3215 0.3822 -0.0345 0.0596  0.0210  62  THR A CG2 
543  N N   . ASP A 62  ? 0.5052 0.2740 0.3634 -0.0720 0.0974  0.0000  63  ASP A N   
544  C CA  . ASP A 62  ? 0.5298 0.2719 0.3730 -0.0829 0.1105  -0.0033 63  ASP A CA  
545  C C   . ASP A 62  ? 0.6082 0.3559 0.4457 -0.1002 0.1185  -0.0106 63  ASP A C   
546  O O   . ASP A 62  ? 0.5664 0.3451 0.4211 -0.1057 0.1154  -0.0197 63  ASP A O   
547  C CB  . ASP A 62  ? 0.5390 0.2845 0.3936 -0.0855 0.1143  -0.0116 63  ASP A CB  
548  C CG  . ASP A 62  ? 0.7080 0.4283 0.5483 -0.0992 0.1288  -0.0172 63  ASP A CG  
549  O OD1 . ASP A 62  ? 0.7781 0.4646 0.6027 -0.0945 0.1342  -0.0109 63  ASP A OD1 
550  O OD2 . ASP A 62  ? 0.7319 0.4659 0.5765 -0.1145 0.1349  -0.0284 63  ASP A OD2 
551  N N   . GLN A 63  ? 0.6503 0.3667 0.4630 -0.1089 0.1294  -0.0075 64  GLN A N   
552  C CA  . GLN A 63  ? 0.6715 0.3894 0.4756 -0.1271 0.1396  -0.0150 64  GLN A CA  
553  C C   . GLN A 63  ? 0.7054 0.4464 0.5266 -0.1423 0.1465  -0.0322 64  GLN A C   
554  O O   . GLN A 63  ? 0.7290 0.4887 0.5556 -0.1545 0.1506  -0.0415 64  GLN A O   
555  C CB  . GLN A 63  ? 0.7459 0.4192 0.5156 -0.1343 0.1515  -0.0079 64  GLN A CB  
556  C CG  . GLN A 63  ? 0.9799 0.6362 0.7302 -0.1224 0.1437  0.0073  64  GLN A CG  
557  N N   . LEU A 64  ? 0.6056 0.3471 0.4360 -0.1419 0.1476  -0.0374 65  LEU A N   
558  C CA  . LEU A 64  ? 0.5881 0.3545 0.4355 -0.1548 0.1515  -0.0540 65  LEU A CA  
559  C C   . LEU A 64  ? 0.6102 0.4146 0.4835 -0.1455 0.1368  -0.0578 65  LEU A C   
560  O O   . LEU A 64  ? 0.6094 0.4438 0.4987 -0.1528 0.1345  -0.0697 65  LEU A O   
561  C CB  . LEU A 64  ? 0.6108 0.3559 0.4514 -0.1621 0.1618  -0.0592 65  LEU A CB  
562  C CG  . LEU A 64  ? 0.7205 0.4316 0.5378 -0.1782 0.1798  -0.0620 65  LEU A CG  
563  C CD1 . LEU A 64  ? 0.7342 0.4246 0.5466 -0.1828 0.1886  -0.0668 65  LEU A CD1 
564  C CD2 . LEU A 64  ? 0.7779 0.5084 0.6001 -0.1984 0.1888  -0.0768 65  LEU A CD2 
565  N N   . LYS A 65  ? 0.5214 0.3241 0.3987 -0.1298 0.1272  -0.0490 66  LYS A N   
566  C CA  . LYS A 65  ? 0.4897 0.3224 0.3868 -0.1222 0.1147  -0.0522 66  LYS A CA  
567  C C   . LYS A 65  ? 0.5369 0.3936 0.4446 -0.1162 0.1044  -0.0502 66  LYS A C   
568  O O   . LYS A 65  ? 0.5115 0.3947 0.4349 -0.1144 0.0957  -0.0564 66  LYS A O   
569  C CB  . LYS A 65  ? 0.4975 0.3211 0.3954 -0.1098 0.1100  -0.0455 66  LYS A CB  
570  C CG  . LYS A 65  ? 0.5009 0.3034 0.3913 -0.1156 0.1201  -0.0497 66  LYS A CG  
571  C CD  . LYS A 65  ? 0.4870 0.2858 0.3817 -0.1034 0.1152  -0.0451 66  LYS A CD  
572  C CE  . LYS A 65  ? 0.5789 0.3522 0.4653 -0.1065 0.1260  -0.0479 66  LYS A CE  
573  N NZ  . LYS A 65  ? 0.6074 0.3464 0.4778 -0.1029 0.1335  -0.0397 66  LYS A NZ  
574  N N   . CYS A 66  ? 0.5340 0.3801 0.4314 -0.1136 0.1054  -0.0421 67  CYS A N   
575  C CA  . CYS A 66  ? 0.5294 0.3965 0.4354 -0.1091 0.0972  -0.0409 67  CYS A CA  
576  C C   . CYS A 66  ? 0.5686 0.4640 0.4901 -0.1189 0.0972  -0.0550 67  CYS A C   
577  O O   . CYS A 66  ? 0.5647 0.4827 0.4996 -0.1131 0.0879  -0.0565 67  CYS A O   
578  C CB  . CYS A 66  ? 0.5702 0.4191 0.4589 -0.1080 0.1003  -0.0315 67  CYS A CB  
579  S SG  . CYS A 66  ? 0.6647 0.4940 0.5341 -0.1270 0.1173  -0.0370 67  CYS A SG  
580  N N   . ASN A 67  ? 0.5099 0.4040 0.4303 -0.1336 0.1078  -0.0662 68  ASN A N   
581  C CA  . ASN A 67  ? 0.5022 0.4244 0.4390 -0.1440 0.1090  -0.0822 68  ASN A CA  
582  C C   . ASN A 67  ? 0.5312 0.4759 0.4852 -0.1433 0.1013  -0.0923 68  ASN A C   
583  O O   . ASN A 67  ? 0.5064 0.4778 0.4769 -0.1499 0.0998  -0.1067 68  ASN A O   
584  C CB  . ASN A 67  ? 0.5446 0.4548 0.4706 -0.1625 0.1259  -0.0904 68  ASN A CB  
585  C CG  . ASN A 67  ? 0.7454 0.6382 0.6541 -0.1645 0.1321  -0.0824 68  ASN A CG  
586  O OD1 . ASN A 67  ? 0.7546 0.6168 0.6402 -0.1736 0.1448  -0.0784 68  ASN A OD1 
587  N ND2 . ASN A 67  ? 0.6285 0.5377 0.5454 -0.1558 0.1231  -0.0790 68  ASN A ND2 
588  N N   . LEU A 68  ? 0.5029 0.4375 0.4529 -0.1354 0.0963  -0.0857 69  LEU A N   
589  C CA  . LEU A 68  ? 0.4830 0.4355 0.4443 -0.1350 0.0887  -0.0942 69  LEU A CA  
590  C C   . LEU A 68  ? 0.4910 0.4670 0.4661 -0.1231 0.0728  -0.0934 69  LEU A C   
591  O O   . LEU A 68  ? 0.4751 0.4454 0.4474 -0.1121 0.0672  -0.0821 69  LEU A O   
592  C CB  . LEU A 68  ? 0.4952 0.4270 0.4454 -0.1323 0.0906  -0.0884 69  LEU A CB  
593  C CG  . LEU A 68  ? 0.5723 0.4779 0.5083 -0.1435 0.1062  -0.0901 69  LEU A CG  
594  C CD1 . LEU A 68  ? 0.5832 0.4695 0.5107 -0.1382 0.1072  -0.0843 69  LEU A CD1 
595  C CD2 . LEU A 68  ? 0.5948 0.5135 0.5369 -0.1603 0.1136  -0.1073 69  LEU A CD2 
596  N N   A SER A 69  ? 0.4383 0.4398 0.4278 -0.1250 0.0650  -0.1057 70  SER A N   
597  N N   B SER A 69  ? 0.4383 0.4397 0.4277 -0.1251 0.0651  -0.1058 70  SER A N   
598  C CA  A SER A 69  ? 0.4217 0.4427 0.4225 -0.1131 0.0489  -0.1055 70  SER A CA  
599  C CA  B SER A 69  ? 0.4220 0.4437 0.4231 -0.1135 0.0490  -0.1061 70  SER A CA  
600  C C   A SER A 69  ? 0.4380 0.4542 0.4319 -0.1067 0.0398  -0.1013 70  SER A C   
601  C C   B SER A 69  ? 0.4385 0.4552 0.4328 -0.1069 0.0398  -0.1017 70  SER A C   
602  O O   A SER A 69  ? 0.4068 0.4306 0.4036 -0.0961 0.0268  -0.0979 70  SER A O   
603  O O   B SER A 69  ? 0.4072 0.4319 0.4045 -0.0964 0.0267  -0.0984 70  SER A O   
604  C CB  A SER A 69  ? 0.4679 0.5198 0.4886 -0.1166 0.0439  -0.1214 70  SER A CB  
605  C CB  B SER A 69  ? 0.4681 0.5205 0.4889 -0.1178 0.0444  -0.1226 70  SER A CB  
606  O OG  A SER A 69  ? 0.5696 0.6320 0.5945 -0.1265 0.0457  -0.1345 70  SER A OG  
607  O OG  B SER A 69  ? 0.5688 0.6275 0.5966 -0.1229 0.0523  -0.1267 70  SER A OG  
608  N N   . VAL A 70  ? 0.4047 0.4066 0.3881 -0.1139 0.0474  -0.1022 71  VAL A N   
609  C CA  . VAL A 70  ? 0.4007 0.3957 0.3749 -0.1108 0.0418  -0.0995 71  VAL A CA  
610  C C   . VAL A 70  ? 0.4300 0.3973 0.3900 -0.1124 0.0532  -0.0911 71  VAL A C   
611  O O   . VAL A 70  ? 0.4371 0.3923 0.3933 -0.1215 0.0661  -0.0941 71  VAL A O   
612  C CB  . VAL A 70  ? 0.4627 0.4737 0.4404 -0.1186 0.0376  -0.1135 71  VAL A CB  
613  C CG1 . VAL A 70  ? 0.4751 0.4763 0.4391 -0.1166 0.0327  -0.1104 71  VAL A CG1 
614  C CG2 . VAL A 70  ? 0.4535 0.4943 0.4480 -0.1150 0.0245  -0.1232 71  VAL A CG2 
615  N N   . ILE A 71  ? 0.3499 0.3067 0.3024 -0.1038 0.0489  -0.0817 72  ILE A N   
616  C CA  . ILE A 71  ? 0.3620 0.2957 0.3043 -0.1031 0.0581  -0.0751 72  ILE A CA  
617  C C   . ILE A 71  ? 0.4121 0.3435 0.3464 -0.1036 0.0545  -0.0769 72  ILE A C   
618  O O   . ILE A 71  ? 0.3965 0.3342 0.3289 -0.0973 0.0442  -0.0735 72  ILE A O   
619  C CB  . ILE A 71  ? 0.3850 0.3082 0.3269 -0.0931 0.0588  -0.0629 72  ILE A CB  
620  C CG1 . ILE A 71  ? 0.3986 0.3216 0.3442 -0.0937 0.0627  -0.0608 72  ILE A CG1 
621  C CG2 . ILE A 71  ? 0.4094 0.3120 0.3439 -0.0904 0.0664  -0.0577 72  ILE A CG2 
622  C CD1 . ILE A 71  ? 0.4394 0.3462 0.3786 -0.1032 0.0762  -0.0638 72  ILE A CD1 
623  N N   . ASN A 72  ? 0.3922 0.3115 0.3196 -0.1116 0.0642  -0.0820 73  ASN A N   
624  C CA  . ASN A 72  ? 0.3985 0.3137 0.3161 -0.1144 0.0633  -0.0851 73  ASN A CA  
625  C C   . ASN A 72  ? 0.4378 0.3341 0.3504 -0.1097 0.0711  -0.0783 73  ASN A C   
626  O O   . ASN A 72  ? 0.4292 0.3100 0.3423 -0.1108 0.0824  -0.0777 73  ASN A O   
627  C CB  . ASN A 72  ? 0.4497 0.3655 0.3637 -0.1273 0.0695  -0.0974 73  ASN A CB  
628  C CG  . ASN A 72  ? 0.6776 0.6153 0.5996 -0.1331 0.0628  -0.1072 73  ASN A CG  
629  O OD1 . ASN A 72  ? 0.5439 0.4992 0.4684 -0.1288 0.0487  -0.1085 73  ASN A OD1 
630  N ND2 . ASN A 72  ? 0.6307 0.5671 0.5568 -0.1432 0.0731  -0.1151 73  ASN A ND2 
631  N N   . LEU A 73  ? 0.3789 0.2756 0.2865 -0.1045 0.0654  -0.0739 74  LEU A N   
632  C CA  . LEU A 73  ? 0.3729 0.2556 0.2784 -0.1007 0.0730  -0.0699 74  LEU A CA  
633  C C   . LEU A 73  ? 0.4390 0.3114 0.3352 -0.1093 0.0819  -0.0779 74  LEU A C   
634  O O   . LEU A 73  ? 0.4392 0.3168 0.3276 -0.1181 0.0794  -0.0855 74  LEU A O   
635  C CB  . LEU A 73  ? 0.3641 0.2506 0.2677 -0.0937 0.0657  -0.0634 74  LEU A CB  
636  C CG  . LEU A 73  ? 0.4088 0.3047 0.3211 -0.0850 0.0573  -0.0558 74  LEU A CG  
637  C CD1 . LEU A 73  ? 0.4170 0.3118 0.3273 -0.0796 0.0546  -0.0505 74  LEU A CD1 
638  C CD2 . LEU A 73  ? 0.3950 0.2879 0.3177 -0.0808 0.0623  -0.0523 74  LEU A CD2 
639  N N   . ASP A 74  ? 0.4104 0.2695 0.3083 -0.1065 0.0919  -0.0770 75  ASP A N   
640  C CA  . ASP A 74  ? 0.4269 0.2749 0.3177 -0.1139 0.1024  -0.0851 75  ASP A CA  
641  C C   . ASP A 74  ? 0.4845 0.3386 0.3603 -0.1212 0.0967  -0.0892 75  ASP A C   
642  O O   . ASP A 74  ? 0.4693 0.3292 0.3415 -0.1168 0.0885  -0.0836 75  ASP A O   
643  C CB  . ASP A 74  ? 0.4498 0.2872 0.3483 -0.1063 0.1112  -0.0829 75  ASP A CB  
644  C CG  . ASP A 74  ? 0.5887 0.4133 0.4834 -0.1125 0.1243  -0.0922 75  ASP A CG  
645  O OD1 . ASP A 74  ? 0.6004 0.4269 0.4838 -0.1205 0.1254  -0.0979 75  ASP A OD1 
646  O OD2 . ASP A 74  ? 0.5999 0.4109 0.5017 -0.1092 0.1336  -0.0937 75  ASP A OD2 
647  N N   . PRO A 75  ? 0.4925 0.3438 0.3573 -0.1325 0.1006  -0.0988 76  PRO A N   
648  C CA  . PRO A 75  ? 0.5116 0.3670 0.3579 -0.1394 0.0938  -0.1022 76  PRO A CA  
649  C C   . PRO A 75  ? 0.5609 0.4086 0.3979 -0.1390 0.0976  -0.1002 76  PRO A C   
650  O O   . PRO A 75  ? 0.5725 0.4213 0.3914 -0.1429 0.0898  -0.0995 76  PRO A O   
651  C CB  . PRO A 75  ? 0.5550 0.4075 0.3925 -0.1522 0.0999  -0.1141 76  PRO A CB  
652  C CG  . PRO A 75  ? 0.6148 0.4563 0.4653 -0.1522 0.1140  -0.1172 76  PRO A CG  
653  C CD  . PRO A 75  ? 0.5296 0.3727 0.3961 -0.1401 0.1112  -0.1073 76  PRO A CD  
654  N N   . GLU A 76  ? 0.5203 0.3602 0.3691 -0.1343 0.1091  -0.0995 77  GLU A N   
655  C CA  . GLU A 76  ? 0.5459 0.3811 0.3896 -0.1347 0.1148  -0.0998 77  GLU A CA  
656  C C   . GLU A 76  ? 0.5389 0.3809 0.3832 -0.1273 0.1045  -0.0899 77  GLU A C   
657  O O   . GLU A 76  ? 0.5282 0.3668 0.3632 -0.1300 0.1071  -0.0898 77  GLU A O   
658  C CB  . GLU A 76  ? 0.5785 0.4069 0.4399 -0.1300 0.1293  -0.1036 77  GLU A CB  
659  C CG  . GLU A 76  ? 0.8435 0.6667 0.6995 -0.1359 0.1408  -0.1110 77  GLU A CG  
660  C CD  . GLU A 76  ? 1.2232 1.0370 1.0661 -0.1486 0.1513  -0.1227 77  GLU A CD  
661  O OE1 . GLU A 76  ? 1.2377 1.0448 1.0913 -0.1477 0.1602  -0.1284 77  GLU A OE1 
662  O OE2 . GLU A 76  ? 1.1489 0.9602 0.9690 -0.1598 0.1510  -0.1263 77  GLU A OE2 
663  N N   . ILE A 77  ? 0.4620 0.3127 0.3168 -0.1189 0.0943  -0.0825 78  ILE A N   
664  C CA  . ILE A 77  ? 0.4398 0.2963 0.2964 -0.1116 0.0852  -0.0739 78  ILE A CA  
665  C C   . ILE A 77  ? 0.5029 0.3583 0.3374 -0.1161 0.0744  -0.0717 78  ILE A C   
666  O O   . ILE A 77  ? 0.5004 0.3592 0.3257 -0.1190 0.0656  -0.0733 78  ILE A O   
667  C CB  . ILE A 77  ? 0.4580 0.3235 0.3326 -0.1016 0.0787  -0.0674 78  ILE A CB  
668  C CG1 . ILE A 77  ? 0.4680 0.3300 0.3604 -0.0962 0.0888  -0.0683 78  ILE A CG1 
669  C CG2 . ILE A 77  ? 0.4330 0.3045 0.3095 -0.0946 0.0698  -0.0594 78  ILE A CG2 
670  C CD1 . ILE A 77  ? 0.5221 0.3813 0.4235 -0.0921 0.0978  -0.0695 78  ILE A CD1 
671  N N   . ASN A 78  ? 0.5095 0.3600 0.3356 -0.1163 0.0750  -0.0683 79  ASN A N   
672  C CA  . ASN A 78  ? 0.5284 0.3717 0.3293 -0.1199 0.0656  -0.0647 79  ASN A CA  
673  C C   . ASN A 78  ? 0.5188 0.3693 0.3244 -0.1103 0.0506  -0.0565 79  ASN A C   
674  O O   . ASN A 78  ? 0.4812 0.3373 0.3037 -0.1030 0.0514  -0.0522 79  ASN A O   
675  C CB  . ASN A 78  ? 0.5756 0.4082 0.3653 -0.1256 0.0752  -0.0653 79  ASN A CB  
676  C CG  . ASN A 78  ? 0.7655 0.5848 0.5249 -0.1299 0.0668  -0.0604 79  ASN A CG  
677  O OD1 . ASN A 78  ? 0.6478 0.4646 0.4062 -0.1256 0.0626  -0.0540 79  ASN A OD1 
678  N ND2 . ASN A 78  ? 0.6900 0.4989 0.4221 -0.1385 0.0639  -0.0632 79  ASN A ND2 
679  N N   . PRO A 79  ? 0.4990 0.3503 0.2908 -0.1096 0.0364  -0.0551 80  PRO A N   
680  C CA  . PRO A 79  ? 0.4859 0.3447 0.2843 -0.0996 0.0224  -0.0488 80  PRO A CA  
681  C C   . PRO A 79  ? 0.5263 0.3756 0.3175 -0.0960 0.0207  -0.0415 80  PRO A C   
682  O O   . PRO A 79  ? 0.4967 0.3542 0.3040 -0.0875 0.0162  -0.0372 80  PRO A O   
683  C CB  . PRO A 79  ? 0.5356 0.3957 0.3179 -0.1001 0.0079  -0.0507 80  PRO A CB  
684  C CG  . PRO A 79  ? 0.6005 0.4599 0.3760 -0.1103 0.0152  -0.0592 80  PRO A CG  
685  C CD  . PRO A 79  ? 0.5531 0.4002 0.3239 -0.1174 0.0319  -0.0604 80  PRO A CD  
686  N N   . GLU A 80  ? 0.5071 0.3387 0.2738 -0.1038 0.0258  -0.0408 81  GLU A N   
687  C CA  . GLU A 80  ? 0.5069 0.3270 0.2646 -0.1029 0.0265  -0.0349 81  GLU A CA  
688  C C   . GLU A 80  ? 0.5158 0.3464 0.3003 -0.1003 0.0379  -0.0358 81  GLU A C   
689  O O   . GLU A 80  ? 0.4890 0.3224 0.2821 -0.0940 0.0339  -0.0311 81  GLU A O   
690  C CB  . GLU A 80  ? 0.5565 0.3533 0.2791 -0.1140 0.0312  -0.0348 81  GLU A CB  
691  C CG  . GLU A 80  ? 0.6729 0.4547 0.3823 -0.1136 0.0303  -0.0284 81  GLU A CG  
692  C CD  . GLU A 80  ? 1.0083 0.7650 0.6840 -0.1267 0.0396  -0.0286 81  GLU A CD  
693  O OE1 . GLU A 80  ? 0.9744 0.7114 0.6275 -0.1267 0.0342  -0.0220 81  GLU A OE1 
694  O OE2 . GLU A 80  ? 0.9107 0.6658 0.5818 -0.1376 0.0531  -0.0359 81  GLU A OE2 
695  N N   . GLY A 81  ? 0.4751 0.3113 0.2725 -0.1046 0.0511  -0.0423 82  GLY A N   
696  C CA  . GLY A 81  ? 0.4534 0.3011 0.2774 -0.1006 0.0603  -0.0440 82  GLY A CA  
697  C C   . GLY A 81  ? 0.4559 0.3181 0.3022 -0.0892 0.0520  -0.0398 82  GLY A C   
698  O O   . GLY A 81  ? 0.4248 0.2937 0.2848 -0.0839 0.0521  -0.0370 82  GLY A O   
699  N N   . PHE A 82  ? 0.3960 0.2634 0.2449 -0.0867 0.0452  -0.0400 83  PHE A N   
700  C CA  . PHE A 82  ? 0.3651 0.2454 0.2328 -0.0778 0.0384  -0.0369 83  PHE A CA  
701  C C   . PHE A 82  ? 0.4105 0.2911 0.2744 -0.0725 0.0276  -0.0312 83  PHE A C   
702  O O   . PHE A 82  ? 0.3831 0.2719 0.2621 -0.0664 0.0266  -0.0283 83  PHE A O   
703  C CB  . PHE A 82  ? 0.3785 0.2644 0.2487 -0.0784 0.0344  -0.0402 83  PHE A CB  
704  C CG  . PHE A 82  ? 0.3710 0.2693 0.2598 -0.0713 0.0303  -0.0381 83  PHE A CG  
705  C CD1 . PHE A 82  ? 0.3967 0.2983 0.3015 -0.0682 0.0380  -0.0376 83  PHE A CD1 
706  C CD2 . PHE A 82  ? 0.3813 0.2869 0.2710 -0.0669 0.0185  -0.0363 83  PHE A CD2 
707  C CE1 . PHE A 82  ? 0.3992 0.3096 0.3171 -0.0628 0.0348  -0.0351 83  PHE A CE1 
708  C CE2 . PHE A 82  ? 0.3891 0.3062 0.2954 -0.0616 0.0162  -0.0353 83  PHE A CE2 
709  C CZ  . PHE A 82  ? 0.3752 0.2938 0.2939 -0.0603 0.0247  -0.0343 83  PHE A CZ  
710  N N   . CYS A 83  ? 0.4377 0.3082 0.2803 -0.0745 0.0192  -0.0296 84  CYS A N   
711  C CA  . CYS A 83  ? 0.4590 0.3258 0.2956 -0.0688 0.0087  -0.0244 84  CYS A CA  
712  C C   . CYS A 83  ? 0.4711 0.3338 0.3109 -0.0687 0.0149  -0.0215 84  CYS A C   
713  O O   . CYS A 83  ? 0.4401 0.3093 0.2913 -0.0621 0.0102  -0.0187 84  CYS A O   
714  C CB  . CYS A 83  ? 0.5150 0.3663 0.3235 -0.0709 -0.0008 -0.0228 84  CYS A CB  
715  S SG  . CYS A 83  ? 0.5915 0.4358 0.3924 -0.0612 -0.0161 -0.0166 84  CYS A SG  
716  N N   . ILE A 84  ? 0.4334 0.2872 0.2647 -0.0769 0.0263  -0.0237 85  ILE A N   
717  C CA  . ILE A 84  ? 0.4140 0.2657 0.2489 -0.0792 0.0341  -0.0236 85  ILE A CA  
718  C C   . ILE A 84  ? 0.3917 0.2633 0.2566 -0.0723 0.0366  -0.0245 85  ILE A C   
719  O O   . ILE A 84  ? 0.3862 0.2618 0.2586 -0.0692 0.0352  -0.0226 85  ILE A O   
720  C CB  . ILE A 84  ? 0.4598 0.3014 0.2822 -0.0906 0.0474  -0.0286 85  ILE A CB  
721  C CG1 . ILE A 84  ? 0.4909 0.3074 0.2763 -0.0983 0.0443  -0.0259 85  ILE A CG1 
722  C CG2 . ILE A 84  ? 0.4544 0.3027 0.2908 -0.0933 0.0581  -0.0322 85  ILE A CG2 
723  C CD1 . ILE A 84  ? 0.5974 0.4032 0.3663 -0.1109 0.0568  -0.0317 85  ILE A CD1 
724  N N   . LEU A 85  ? 0.3443 0.2263 0.2238 -0.0703 0.0401  -0.0274 86  LEU A N   
725  C CA  . LEU A 85  ? 0.3275 0.2250 0.2315 -0.0633 0.0415  -0.0273 86  LEU A CA  
726  C C   . LEU A 85  ? 0.3719 0.2771 0.2833 -0.0560 0.0315  -0.0231 86  LEU A C   
727  O O   . LEU A 85  ? 0.3363 0.2508 0.2611 -0.0513 0.0310  -0.0217 86  LEU A O   
728  C CB  . LEU A 85  ? 0.3286 0.2300 0.2429 -0.0630 0.0485  -0.0312 86  LEU A CB  
729  C CG  . LEU A 85  ? 0.4012 0.2997 0.3159 -0.0687 0.0604  -0.0374 86  LEU A CG  
730  C CD1 . LEU A 85  ? 0.4178 0.3173 0.3414 -0.0675 0.0666  -0.0413 86  LEU A CD1 
731  C CD2 . LEU A 85  ? 0.4020 0.3102 0.3311 -0.0665 0.0643  -0.0392 86  LEU A CD2 
732  N N   . LEU A 86  ? 0.3335 0.2362 0.2368 -0.0553 0.0236  -0.0222 87  LEU A N   
733  C CA  . LEU A 86  ? 0.3294 0.2407 0.2407 -0.0491 0.0147  -0.0201 87  LEU A CA  
734  C C   . LEU A 86  ? 0.3607 0.2691 0.2691 -0.0465 0.0102  -0.0172 87  LEU A C   
735  O O   . LEU A 86  ? 0.3255 0.2434 0.2466 -0.0420 0.0085  -0.0161 87  LEU A O   
736  C CB  . LEU A 86  ? 0.3319 0.2433 0.2367 -0.0493 0.0071  -0.0220 87  LEU A CB  
737  C CG  . LEU A 86  ? 0.3814 0.3050 0.2979 -0.0436 -0.0009 -0.0227 87  LEU A CG  
738  C CD1 . LEU A 86  ? 0.3607 0.2952 0.2940 -0.0425 0.0050  -0.0233 87  LEU A CD1 
739  C CD2 . LEU A 86  ? 0.4088 0.3353 0.3204 -0.0438 -0.0092 -0.0266 87  LEU A CD2 
740  N N   . ASP A 87  ? 0.3470 0.2403 0.2368 -0.0503 0.0093  -0.0161 88  ASP A N   
741  C CA  . ASP A 87  ? 0.3583 0.2441 0.2421 -0.0493 0.0071  -0.0136 88  ASP A CA  
742  C C   . ASP A 87  ? 0.3794 0.2742 0.2777 -0.0504 0.0152  -0.0149 88  ASP A C   
743  O O   . ASP A 87  ? 0.3701 0.2697 0.2757 -0.0468 0.0124  -0.0140 88  ASP A O   
744  C CB  . ASP A 87  ? 0.4192 0.2826 0.2762 -0.0554 0.0076  -0.0121 88  ASP A CB  
745  C CG  . ASP A 87  ? 0.6008 0.4530 0.4404 -0.0521 -0.0044 -0.0098 88  ASP A CG  
746  O OD1 . ASP A 87  ? 0.6028 0.4667 0.4543 -0.0442 -0.0137 -0.0102 88  ASP A OD1 
747  O OD2 . ASP A 87  ? 0.6137 0.4457 0.4273 -0.0574 -0.0046 -0.0081 88  ASP A OD2 
748  N N   . PHE A 88  ? 0.3434 0.2417 0.2467 -0.0549 0.0249  -0.0180 89  PHE A N   
749  C CA  . PHE A 88  ? 0.3123 0.2229 0.2320 -0.0547 0.0313  -0.0207 89  PHE A CA  
750  C C   . PHE A 88  ? 0.3134 0.2401 0.2515 -0.0467 0.0265  -0.0191 89  PHE A C   
751  O O   . PHE A 88  ? 0.2961 0.2312 0.2433 -0.0448 0.0260  -0.0195 89  PHE A O   
752  C CB  . PHE A 88  ? 0.3186 0.2328 0.2442 -0.0587 0.0413  -0.0256 89  PHE A CB  
753  C CG  . PHE A 88  ? 0.3055 0.2368 0.2526 -0.0553 0.0452  -0.0290 89  PHE A CG  
754  C CD1 . PHE A 88  ? 0.3384 0.2742 0.2892 -0.0590 0.0489  -0.0325 89  PHE A CD1 
755  C CD2 . PHE A 88  ? 0.3366 0.2790 0.2992 -0.0480 0.0442  -0.0286 89  PHE A CD2 
756  C CE1 . PHE A 88  ? 0.3251 0.2797 0.2969 -0.0550 0.0505  -0.0365 89  PHE A CE1 
757  C CE2 . PHE A 88  ? 0.3544 0.3124 0.3355 -0.0429 0.0452  -0.0311 89  PHE A CE2 
758  C CZ  . PHE A 88  ? 0.3287 0.2945 0.3154 -0.0462 0.0477  -0.0354 89  PHE A CZ  
759  N N   . MET A 89  ? 0.2694 0.1996 0.2115 -0.0431 0.0239  -0.0179 90  MET A N   
760  C CA  . MET A 89  ? 0.2587 0.2009 0.2140 -0.0371 0.0205  -0.0162 90  MET A CA  
761  C C   . MET A 89  ? 0.3071 0.2527 0.2634 -0.0347 0.0143  -0.0149 90  MET A C   
762  O O   . MET A 89  ? 0.2943 0.2498 0.2603 -0.0317 0.0138  -0.0146 90  MET A O   
763  C CB  . MET A 89  ? 0.2708 0.2124 0.2256 -0.0362 0.0191  -0.0158 90  MET A CB  
764  C CG  . MET A 89  ? 0.2929 0.2310 0.2486 -0.0378 0.0260  -0.0175 90  MET A CG  
765  S SD  . MET A 89  ? 0.3513 0.2882 0.3065 -0.0382 0.0253  -0.0178 90  MET A SD  
766  C CE  . MET A 89  ? 0.3577 0.2854 0.3099 -0.0417 0.0344  -0.0211 90  MET A CE  
767  N N   . TYR A 90  ? 0.2762 0.2130 0.2219 -0.0353 0.0091  -0.0145 91  TYR A N   
768  C CA  . TYR A 90  ? 0.2782 0.2168 0.2254 -0.0319 0.0029  -0.0142 91  TYR A CA  
769  C C   . TYR A 90  ? 0.3424 0.2736 0.2840 -0.0339 0.0040  -0.0143 91  TYR A C   
770  O O   . TYR A 90  ? 0.3224 0.2538 0.2656 -0.0310 -0.0004 -0.0146 91  TYR A O   
771  C CB  . TYR A 90  ? 0.2974 0.2309 0.2380 -0.0295 -0.0048 -0.0146 91  TYR A CB  
772  C CG  . TYR A 90  ? 0.3103 0.2558 0.2610 -0.0276 -0.0065 -0.0168 91  TYR A CG  
773  C CD1 . TYR A 90  ? 0.3329 0.2783 0.2820 -0.0305 -0.0033 -0.0176 91  TYR A CD1 
774  C CD2 . TYR A 90  ? 0.3118 0.2683 0.2733 -0.0241 -0.0099 -0.0191 91  TYR A CD2 
775  C CE1 . TYR A 90  ? 0.3363 0.2911 0.2934 -0.0307 -0.0033 -0.0204 91  TYR A CE1 
776  C CE2 . TYR A 90  ? 0.3210 0.2879 0.2907 -0.0244 -0.0100 -0.0224 91  TYR A CE2 
777  C CZ  . TYR A 90  ? 0.3604 0.3261 0.3276 -0.0281 -0.0064 -0.0229 91  TYR A CZ  
778  O OH  . TYR A 90  ? 0.3209 0.2957 0.2952 -0.0300 -0.0053 -0.0272 91  TYR A OH  
779  N N   . THR A 91  ? 0.3043 0.2288 0.2396 -0.0396 0.0106  -0.0150 92  THR A N   
780  C CA  . THR A 91  ? 0.3144 0.2293 0.2419 -0.0437 0.0132  -0.0160 92  THR A CA  
781  C C   . THR A 91  ? 0.3355 0.2582 0.2706 -0.0493 0.0220  -0.0200 92  THR A C   
782  O O   . THR A 91  ? 0.3376 0.2557 0.2694 -0.0535 0.0248  -0.0221 92  THR A O   
783  C CB  . THR A 91  ? 0.3796 0.2703 0.2831 -0.0480 0.0126  -0.0140 92  THR A CB  
784  O OG1 . THR A 91  ? 0.3785 0.2650 0.2752 -0.0544 0.0197  -0.0154 92  THR A OG1 
785  C CG2 . THR A 91  ? 0.3910 0.2728 0.2853 -0.0416 0.0018  -0.0108 92  THR A CG2 
786  N N   A SER A 92  ? 0.2887 0.2222 0.2338 -0.0495 0.0266  -0.0219 93  SER A N   
787  N N   B SER A 92  ? 0.2860 0.2192 0.2308 -0.0496 0.0267  -0.0219 93  SER A N   
788  C CA  A SER A 92  ? 0.2812 0.2249 0.2364 -0.0538 0.0349  -0.0277 93  SER A CA  
789  C CA  B SER A 92  ? 0.2785 0.2222 0.2337 -0.0537 0.0348  -0.0276 93  SER A CA  
790  C C   A SER A 92  ? 0.3265 0.2553 0.2669 -0.0640 0.0434  -0.0310 93  SER A C   
791  C C   B SER A 92  ? 0.3388 0.2676 0.2793 -0.0641 0.0434  -0.0311 93  SER A C   
792  O O   A SER A 92  ? 0.3105 0.2482 0.2599 -0.0689 0.0518  -0.0376 93  SER A O   
793  O O   B SER A 92  ? 0.3333 0.2707 0.2822 -0.0696 0.0517  -0.0379 93  SER A O   
794  C CB  A SER A 92  ? 0.3008 0.2574 0.2675 -0.0540 0.0349  -0.0311 93  SER A CB  
795  C CB  B SER A 92  ? 0.2993 0.2579 0.2679 -0.0527 0.0341  -0.0306 93  SER A CB  
796  O OG  A SER A 92  ? 0.2624 0.2299 0.2382 -0.0464 0.0275  -0.0281 93  SER A OG  
797  O OG  B SER A 92  ? 0.3360 0.2844 0.2948 -0.0600 0.0375  -0.0332 93  SER A OG  
798  N N   A ARG A 93  ? 0.3109 0.2174 0.2285 -0.0670 0.0413  -0.0269 94  ARG A N   
799  N N   B ARG A 93  ? 0.3177 0.2246 0.2357 -0.0669 0.0414  -0.0270 94  ARG A N   
800  C CA  A ARG A 93  ? 0.3366 0.2242 0.2339 -0.0779 0.0495  -0.0292 94  ARG A CA  
801  C CA  B ARG A 93  ? 0.3436 0.2304 0.2400 -0.0777 0.0490  -0.0288 94  ARG A CA  
802  C C   A ARG A 93  ? 0.3938 0.2759 0.2832 -0.0794 0.0514  -0.0289 94  ARG A C   
803  C C   B ARG A 93  ? 0.3976 0.2786 0.2858 -0.0795 0.0512  -0.0287 94  ARG A C   
804  O O   A ARG A 93  ? 0.3728 0.2516 0.2575 -0.0733 0.0431  -0.0241 94  ARG A O   
805  O O   B ARG A 93  ? 0.3846 0.2617 0.2674 -0.0737 0.0430  -0.0238 94  ARG A O   
806  C CB  A ARG A 93  ? 0.3861 0.2477 0.2578 -0.0811 0.0460  -0.0248 94  ARG A CB  
807  C CB  B ARG A 93  ? 0.3868 0.2485 0.2588 -0.0793 0.0440  -0.0238 94  ARG A CB  
808  C CG  A ARG A 93  ? 0.4561 0.3194 0.3331 -0.0813 0.0458  -0.0261 94  ARG A CG  
809  C CG  B ARG A 93  ? 0.4789 0.3434 0.3576 -0.0778 0.0421  -0.0244 94  ARG A CG  
810  C CD  A ARG A 93  ? 0.5806 0.4187 0.4358 -0.0785 0.0379  -0.0199 94  ARG A CD  
811  C CD  B ARG A 93  ? 0.5638 0.4183 0.4335 -0.0901 0.0533  -0.0298 94  ARG A CD  
812  N NE  A ARG A 93  ? 0.7300 0.5373 0.5531 -0.0868 0.0415  -0.0174 94  ARG A NE  
813  N NE  B ARG A 93  ? 0.5703 0.4284 0.4473 -0.0895 0.0523  -0.0316 94  ARG A NE  
814  C CZ  A ARG A 93  ? 0.8891 0.6766 0.6944 -0.0981 0.0508  -0.0197 94  ARG A CZ  
815  C CZ  B ARG A 93  ? 0.7429 0.5759 0.5998 -0.0928 0.0519  -0.0292 94  ARG A CZ  
816  N NH1 A ARG A 93  ? 0.7001 0.4978 0.5191 -0.1025 0.0572  -0.0254 94  ARG A NH1 
817  N NH1 B ARG A 93  ? 0.6021 0.4401 0.4676 -0.0927 0.0520  -0.0322 94  ARG A NH1 
818  N NH2 A ARG A 93  ? 0.7361 0.4926 0.5081 -0.1061 0.0540  -0.0166 94  ARG A NH2 
819  N NH2 B ARG A 93  ? 0.5434 0.3445 0.3696 -0.0962 0.0513  -0.0240 94  ARG A NH2 
820  N N   . LEU A 94  ? 0.3599 0.2417 0.2481 -0.0883 0.0629  -0.0353 95  LEU A N   
821  C CA  . LEU A 94  ? 0.3682 0.2452 0.2492 -0.0915 0.0673  -0.0371 95  LEU A CA  
822  C C   . LEU A 94  ? 0.4483 0.3003 0.2989 -0.1044 0.0744  -0.0381 95  LEU A C   
823  O O   . LEU A 94  ? 0.4415 0.2907 0.2891 -0.1147 0.0855  -0.0443 95  LEU A O   
824  C CB  . LEU A 94  ? 0.3612 0.2600 0.2684 -0.0903 0.0754  -0.0451 95  LEU A CB  
825  C CG  . LEU A 94  ? 0.4016 0.2980 0.3065 -0.0925 0.0809  -0.0484 95  LEU A CG  
826  C CD1 . LEU A 94  ? 0.3754 0.2718 0.2811 -0.0832 0.0708  -0.0419 95  LEU A CD1 
827  C CD2 . LEU A 94  ? 0.4203 0.3356 0.3502 -0.0922 0.0908  -0.0584 95  LEU A CD2 
828  N N   . ASN A 95  ? 0.4501 0.2840 0.2770 -0.1045 0.0683  -0.0326 96  ASN A N   
829  C CA  . ASN A 95  ? 0.4931 0.2992 0.2848 -0.1165 0.0735  -0.0322 96  ASN A CA  
830  C C   . ASN A 95  ? 0.5559 0.3649 0.3471 -0.1256 0.0860  -0.0401 96  ASN A C   
831  O O   . ASN A 95  ? 0.5596 0.3619 0.3384 -0.1258 0.0830  -0.0388 96  ASN A O   
832  C CB  . ASN A 95  ? 0.5642 0.3498 0.3295 -0.1115 0.0591  -0.0229 96  ASN A CB  
833  C CG  . ASN A 95  ? 0.8015 0.5542 0.5248 -0.1230 0.0623  -0.0207 96  ASN A CG  
834  O OD1 . ASN A 95  ? 0.7058 0.4455 0.4153 -0.1358 0.0752  -0.0246 96  ASN A OD1 
835  N ND2 . ASN A 95  ? 0.7428 0.4814 0.4440 -0.1192 0.0506  -0.0149 96  ASN A ND2 
836  N N   . LEU A 96  ? 0.5056 0.3274 0.3137 -0.1325 0.0999  -0.0498 97  LEU A N   
837  C CA  . LEU A 96  ? 0.5224 0.3507 0.3361 -0.1406 0.1136  -0.0599 97  LEU A CA  
838  C C   . LEU A 96  ? 0.5930 0.3962 0.3730 -0.1587 0.1260  -0.0637 97  LEU A C   
839  O O   . LEU A 96  ? 0.5854 0.3800 0.3564 -0.1677 0.1329  -0.0659 97  LEU A O   
840  C CB  . LEU A 96  ? 0.5103 0.3689 0.3637 -0.1366 0.1208  -0.0696 97  LEU A CB  
841  C CG  . LEU A 96  ? 0.5780 0.4518 0.4512 -0.1373 0.1310  -0.0802 97  LEU A CG  
842  C CD1 . LEU A 96  ? 0.5795 0.4525 0.4535 -0.1281 0.1229  -0.0750 97  LEU A CD1 
843  C CD2 . LEU A 96  ? 0.5495 0.4534 0.4619 -0.1307 0.1347  -0.0889 97  LEU A CD2 
844  N N   . ARG A 97  ? 0.5786 0.3674 0.3361 -0.1650 0.1284  -0.0641 98  ARG A N   
845  C CA  . ARG A 97  ? 0.6231 0.3839 0.3415 -0.1831 0.1396  -0.0668 98  ARG A CA  
846  C C   . ARG A 97  ? 0.6359 0.4028 0.3575 -0.1917 0.1531  -0.0779 98  ARG A C   
847  O O   . ARG A 97  ? 0.5840 0.3683 0.3278 -0.1820 0.1490  -0.0795 98  ARG A O   
848  C CB  . ARG A 97  ? 0.6755 0.4044 0.3511 -0.1824 0.1258  -0.0538 98  ARG A CB  
849  C CG  . ARG A 97  ? 0.7672 0.4867 0.4376 -0.1731 0.1119  -0.0430 98  ARG A CG  
850  C CD  . ARG A 97  ? 0.9939 0.6835 0.6249 -0.1694 0.0962  -0.0309 98  ARG A CD  
851  N NE  . ARG A 97  ? 1.2692 0.9223 0.8519 -0.1858 0.1039  -0.0298 98  ARG A NE  
852  C CZ  . ARG A 97  ? 1.5585 1.1839 1.1139 -0.1949 0.1093  -0.0269 98  ARG A CZ  
853  N NH1 . ARG A 97  ? 1.4379 1.0275 0.9456 -0.2108 0.1171  -0.0256 98  ARG A NH1 
854  N NH2 . ARG A 97  ? 1.4281 1.0598 1.0017 -0.1894 0.1079  -0.0255 98  ARG A NH2 
855  N N   . GLU A 98  ? 0.6334 0.3846 0.3317 -0.2108 0.1702  -0.0862 99  GLU A N   
856  C CA  . GLU A 98  ? 0.6296 0.3852 0.3290 -0.2210 0.1851  -0.0985 99  GLU A CA  
857  C C   . GLU A 98  ? 0.6874 0.4362 0.3734 -0.2153 0.1746  -0.0929 99  GLU A C   
858  O O   . GLU A 98  ? 0.6820 0.4484 0.3913 -0.2119 0.1797  -0.1010 99  GLU A O   
859  C CB  . GLU A 98  ? 0.6921 0.4236 0.3560 -0.2448 0.2038  -0.1061 99  GLU A CB  
860  C CG  . GLU A 98  ? 0.8274 0.5647 0.4936 -0.2571 0.2218  -0.1213 99  GLU A CG  
861  C CD  . GLU A 98  ? 1.2400 0.9523 0.8684 -0.2827 0.2419  -0.1296 99  GLU A CD  
862  O OE1 . GLU A 98  ? 1.1805 0.8558 0.7580 -0.2916 0.2372  -0.1186 99  GLU A OE1 
863  O OE2 . GLU A 98  ? 1.2511 0.9803 0.9001 -0.2938 0.2625  -0.1477 99  GLU A OE2 
864  N N   . GLY A 99  ? 0.6767 0.4010 0.3271 -0.2132 0.1595  -0.0795 100 GLY A N   
865  C CA  . GLY A 99  ? 0.6928 0.4106 0.3275 -0.2087 0.1479  -0.0744 100 GLY A CA  
866  C C   . GLY A 99  ? 0.6902 0.4326 0.3599 -0.1902 0.1346  -0.0712 100 GLY A C   
867  O O   . GLY A 99  ? 0.6922 0.4357 0.3577 -0.1883 0.1296  -0.0717 100 GLY A O   
868  N N   . ASN A 100 ? 0.6082 0.3702 0.3116 -0.1775 0.1295  -0.0687 101 ASN A N   
869  C CA  . ASN A 100 ? 0.5655 0.3478 0.2983 -0.1611 0.1174  -0.0651 101 ASN A CA  
870  C C   . ASN A 100 ? 0.5744 0.3840 0.3514 -0.1537 0.1253  -0.0728 101 ASN A C   
871  O O   . ASN A 100 ? 0.5398 0.3635 0.3390 -0.1415 0.1174  -0.0704 101 ASN A O   
872  C CB  . ASN A 100 ? 0.5604 0.3397 0.2898 -0.1497 0.0992  -0.0529 101 ASN A CB  
873  C CG  . ASN A 100 ? 0.6774 0.4630 0.4219 -0.1462 0.1003  -0.0511 101 ASN A CG  
874  O OD1 . ASN A 100 ? 0.5171 0.3199 0.2884 -0.1468 0.1112  -0.0588 101 ASN A OD1 
875  N ND2 . ASN A 100 ? 0.5875 0.3603 0.3165 -0.1418 0.0883  -0.0417 101 ASN A ND2 
876  N N   . ILE A 101 ? 0.5342 0.3509 0.3236 -0.1607 0.1401  -0.0822 102 ILE A N   
877  C CA  . ILE A 101 ? 0.5084 0.3519 0.3403 -0.1517 0.1454  -0.0895 102 ILE A CA  
878  C C   . ILE A 101 ? 0.5138 0.3679 0.3657 -0.1449 0.1476  -0.0946 102 ILE A C   
879  O O   . ILE A 101 ? 0.4684 0.3392 0.3494 -0.1308 0.1417  -0.0929 102 ILE A O   
880  C CB  . ILE A 101 ? 0.5592 0.4114 0.4026 -0.1612 0.1612  -0.1014 102 ILE A CB  
881  C CG1 . ILE A 101 ? 0.5402 0.4226 0.4295 -0.1483 0.1620  -0.1078 102 ILE A CG1 
882  C CG2 . ILE A 101 ? 0.5737 0.4151 0.3996 -0.1784 0.1787  -0.1131 102 ILE A CG2 
883  C CD1 . ILE A 101 ? 0.5681 0.4642 0.4726 -0.1529 0.1695  -0.1155 102 ILE A CD1 
884  N N   . MET A 102 ? 0.5081 0.3510 0.3429 -0.1548 0.1560  -0.1006 103 MET A N   
885  C CA  . MET A 102 ? 0.5076 0.3578 0.3601 -0.1490 0.1591  -0.1061 103 MET A CA  
886  C C   . MET A 102 ? 0.5358 0.3863 0.3910 -0.1371 0.1436  -0.0957 103 MET A C   
887  O O   . MET A 102 ? 0.4914 0.3534 0.3729 -0.1257 0.1425  -0.0966 103 MET A O   
888  C CB  . MET A 102 ? 0.5802 0.4180 0.4129 -0.1636 0.1723  -0.1161 103 MET A CB  
889  C CG  . MET A 102 ? 0.6679 0.5080 0.5024 -0.1763 0.1909  -0.1295 103 MET A CG  
890  S SD  . MET A 102 ? 0.7198 0.5896 0.6055 -0.1653 0.1990  -0.1406 103 MET A SD  
891  C CE  . MET A 102 ? 0.6858 0.5626 0.5964 -0.1551 0.2029  -0.1481 103 MET A CE  
892  N N   . ALA A 103 ? 0.5161 0.3537 0.3439 -0.1395 0.1315  -0.0861 104 ALA A N   
893  C CA  . ALA A 103 ? 0.5010 0.3406 0.3309 -0.1300 0.1172  -0.0780 104 ALA A CA  
894  C C   . ALA A 103 ? 0.4928 0.3463 0.3469 -0.1165 0.1086  -0.0712 104 ALA A C   
895  O O   . ALA A 103 ? 0.4681 0.3293 0.3388 -0.1072 0.1038  -0.0690 104 ALA A O   
896  C CB  . ALA A 103 ? 0.5361 0.3612 0.3331 -0.1350 0.1058  -0.0711 104 ALA A CB  
897  N N   . VAL A 104 ? 0.4211 0.2765 0.2757 -0.1163 0.1076  -0.0685 105 VAL A N   
898  C CA  . VAL A 104 ? 0.3884 0.2575 0.2649 -0.1045 0.0999  -0.0630 105 VAL A CA  
899  C C   . VAL A 104 ? 0.4143 0.2991 0.3223 -0.0960 0.1058  -0.0683 105 VAL A C   
900  O O   . VAL A 104 ? 0.3894 0.2818 0.3121 -0.0850 0.0981  -0.0632 105 VAL A O   
901  C CB  . VAL A 104 ? 0.4399 0.3069 0.3093 -0.1079 0.0992  -0.0607 105 VAL A CB  
902  C CG1 . VAL A 104 ? 0.4013 0.2851 0.2959 -0.0970 0.0937  -0.0576 105 VAL A CG1 
903  C CG2 . VAL A 104 ? 0.4671 0.3163 0.3060 -0.1117 0.0893  -0.0528 105 VAL A CG2 
904  N N   A MET A 105 ? 0.3970 0.2860 0.3146 -0.1008 0.1192  -0.0789 106 MET A N   
905  N N   B MET A 105 ? 0.4027 0.2917 0.3204 -0.1007 0.1192  -0.0789 106 MET A N   
906  C CA  A MET A 105 ? 0.3948 0.2982 0.3428 -0.0911 0.1241  -0.0850 106 MET A CA  
907  C CA  B MET A 105 ? 0.4078 0.3114 0.3561 -0.0906 0.1235  -0.0846 106 MET A CA  
908  C C   A MET A 105 ? 0.4496 0.3481 0.4021 -0.0843 0.1221  -0.0834 106 MET A C   
909  C C   B MET A 105 ? 0.4459 0.3444 0.3983 -0.0842 0.1218  -0.0831 106 MET A C   
910  O O   A MET A 105 ? 0.4270 0.3327 0.3979 -0.0718 0.1167  -0.0798 106 MET A O   
911  O O   B MET A 105 ? 0.4098 0.3151 0.3804 -0.0717 0.1167  -0.0797 106 MET A O   
912  C CB  A MET A 105 ? 0.4376 0.3469 0.3955 -0.0982 0.1395  -0.0990 106 MET A CB  
913  C CB  B MET A 105 ? 0.4524 0.3629 0.4122 -0.0969 0.1386  -0.0984 106 MET A CB  
914  C CG  A MET A 105 ? 0.4753 0.4018 0.4676 -0.0856 0.1424  -0.1058 106 MET A CG  
915  C CG  B MET A 105 ? 0.4910 0.4185 0.4852 -0.0837 0.1409  -0.1048 106 MET A CG  
916  S SD  A MET A 105 ? 0.5401 0.4777 0.5495 -0.0929 0.1610  -0.1252 106 MET A SD  
917  S SD  B MET A 105 ? 0.5509 0.4934 0.5652 -0.0901 0.1579  -0.1236 106 MET A SD  
918  C CE  A MET A 105 ? 0.4913 0.4407 0.5355 -0.0735 0.1594  -0.1295 106 MET A CE  
919  C CE  B MET A 105 ? 0.5392 0.4648 0.5379 -0.1015 0.1721  -0.1328 106 MET A CE  
920  N N   . ALA A 106 ? 0.4329 0.3180 0.3665 -0.0933 0.1263  -0.0859 107 ALA A N   
921  C CA  . ALA A 106 ? 0.4389 0.3173 0.3739 -0.0898 0.1262  -0.0858 107 ALA A CA  
922  C C   . ALA A 106 ? 0.4539 0.3326 0.3882 -0.0821 0.1128  -0.0747 107 ALA A C   
923  O O   . ALA A 106 ? 0.4261 0.3044 0.3728 -0.0735 0.1117  -0.0729 107 ALA A O   
924  C CB  . ALA A 106 ? 0.4701 0.3354 0.3819 -0.1031 0.1321  -0.0910 107 ALA A CB  
925  N N   . THR A 107 ? 0.3955 0.2739 0.3150 -0.0851 0.1031  -0.0679 108 THR A N   
926  C CA  . THR A 107 ? 0.3845 0.2655 0.3044 -0.0788 0.0911  -0.0592 108 THR A CA  
927  C C   . THR A 107 ? 0.3935 0.2851 0.3345 -0.0669 0.0876  -0.0549 108 THR A C   
928  O O   . THR A 107 ? 0.3668 0.2584 0.3142 -0.0605 0.0838  -0.0508 108 THR A O   
929  C CB  . THR A 107 ? 0.4449 0.3232 0.3454 -0.0835 0.0812  -0.0541 108 THR A CB  
930  O OG1 . THR A 107 ? 0.4548 0.3224 0.3335 -0.0942 0.0840  -0.0583 108 THR A OG1 
931  C CG2 . THR A 107 ? 0.4465 0.3289 0.3487 -0.0782 0.0701  -0.0481 108 THR A CG2 
932  N N   . ALA A 108 ? 0.3529 0.2531 0.3031 -0.0649 0.0893  -0.0562 109 ALA A N   
933  C CA  . ALA A 108 ? 0.3288 0.2408 0.2983 -0.0538 0.0849  -0.0530 109 ALA A CA  
934  C C   . ALA A 108 ? 0.3642 0.2763 0.3500 -0.0447 0.0889  -0.0555 109 ALA A C   
935  O O   . ALA A 108 ? 0.3469 0.2614 0.3409 -0.0349 0.0827  -0.0497 109 ALA A O   
936  C CB  . ALA A 108 ? 0.3355 0.2581 0.3120 -0.0553 0.0868  -0.0562 109 ALA A CB  
937  N N   . MET A 109 ? 0.3566 0.2635 0.3449 -0.0479 0.0993  -0.0640 110 MET A N   
938  C CA  . MET A 109 ? 0.3539 0.2572 0.3566 -0.0382 0.1031  -0.0665 110 MET A CA  
939  C C   . MET A 109 ? 0.3923 0.2816 0.3853 -0.0363 0.0995  -0.0598 110 MET A C   
940  O O   . MET A 109 ? 0.3968 0.2828 0.3971 -0.0256 0.0956  -0.0549 110 MET A O   
941  C CB  . MET A 109 ? 0.3923 0.2926 0.3998 -0.0429 0.1161  -0.0786 110 MET A CB  
942  C CG  . MET A 109 ? 0.4398 0.3560 0.4629 -0.0432 0.1215  -0.0875 110 MET A CG  
943  S SD  . MET A 109 ? 0.5374 0.4498 0.5618 -0.0533 0.1390  -0.1034 110 MET A SD  
944  C CE  . MET A 109 ? 0.5040 0.4090 0.5471 -0.0383 0.1416  -0.1065 110 MET A CE  
945  N N   . TYR A 110 ? 0.3803 0.2615 0.3557 -0.0472 0.1005  -0.0600 111 TYR A N   
946  C CA  . TYR A 110 ? 0.3788 0.2489 0.3446 -0.0488 0.0984  -0.0560 111 TYR A CA  
947  C C   . TYR A 110 ? 0.4035 0.2785 0.3701 -0.0428 0.0880  -0.0464 111 TYR A C   
948  O O   . TYR A 110 ? 0.3908 0.2571 0.3577 -0.0381 0.0875  -0.0425 111 TYR A O   
949  C CB  . TYR A 110 ? 0.3854 0.2522 0.3336 -0.0619 0.0991  -0.0592 111 TYR A CB  
950  C CG  . TYR A 110 ? 0.3894 0.2503 0.3288 -0.0657 0.0960  -0.0569 111 TYR A CG  
951  C CD1 . TYR A 110 ? 0.4305 0.2782 0.3691 -0.0674 0.1036  -0.0606 111 TYR A CD1 
952  C CD2 . TYR A 110 ? 0.3856 0.2543 0.3179 -0.0686 0.0862  -0.0527 111 TYR A CD2 
953  C CE1 . TYR A 110 ? 0.4274 0.2706 0.3583 -0.0731 0.1022  -0.0602 111 TYR A CE1 
954  C CE2 . TYR A 110 ? 0.3932 0.2600 0.3200 -0.0732 0.0841  -0.0532 111 TYR A CE2 
955  C CZ  . TYR A 110 ? 0.4312 0.2858 0.3571 -0.0764 0.0925  -0.0572 111 TYR A CZ  
956  O OH  . TYR A 110 ? 0.4302 0.2844 0.3512 -0.0829 0.0916  -0.0593 111 TYR A OH  
957  N N   . LEU A 111 ? 0.3499 0.2368 0.3152 -0.0438 0.0807  -0.0431 112 LEU A N   
958  C CA  . LEU A 111 ? 0.3297 0.2228 0.2960 -0.0392 0.0715  -0.0355 112 LEU A CA  
959  C C   . LEU A 111 ? 0.3708 0.2686 0.3500 -0.0276 0.0688  -0.0316 112 LEU A C   
960  O O   . LEU A 111 ? 0.3643 0.2652 0.3431 -0.0236 0.0621  -0.0254 112 LEU A O   
961  C CB  . LEU A 111 ? 0.3125 0.2148 0.2725 -0.0438 0.0649  -0.0340 112 LEU A CB  
962  C CG  . LEU A 111 ? 0.3500 0.2485 0.2952 -0.0532 0.0631  -0.0362 112 LEU A CG  
963  C CD1 . LEU A 111 ? 0.3630 0.2677 0.3018 -0.0547 0.0551  -0.0335 112 LEU A CD1 
964  C CD2 . LEU A 111 ? 0.3678 0.2631 0.3100 -0.0549 0.0614  -0.0354 112 LEU A CD2 
965  N N   . GLN A 112 ? 0.3319 0.2317 0.3230 -0.0221 0.0735  -0.0362 113 GLN A N   
966  C CA  . GLN A 112 ? 0.3375 0.2442 0.3426 -0.0096 0.0694  -0.0339 113 GLN A CA  
967  C C   . GLN A 112 ? 0.3618 0.2852 0.3710 -0.0087 0.0618  -0.0312 113 GLN A C   
968  O O   . GLN A 112 ? 0.3490 0.2750 0.3575 -0.0032 0.0543  -0.0246 113 GLN A O   
969  C CB  . GLN A 112 ? 0.3618 0.2545 0.3631 -0.0015 0.0669  -0.0273 113 GLN A CB  
970  C CG  . GLN A 112 ? 0.3894 0.2630 0.3869 -0.0020 0.0756  -0.0306 113 GLN A CG  
971  C CD  . GLN A 112 ? 0.5275 0.3822 0.5139 0.0016  0.0743  -0.0232 113 GLN A CD  
972  O OE1 . GLN A 112 ? 0.4593 0.3141 0.4445 0.0094  0.0669  -0.0159 113 GLN A OE1 
973  N NE2 . GLN A 112 ? 0.5364 0.3735 0.5125 -0.0053 0.0819  -0.0254 113 GLN A NE2 
974  N N   . MET A 113 ? 0.3216 0.2541 0.3324 -0.0157 0.0647  -0.0367 114 MET A N   
975  C CA  . MET A 113 ? 0.3158 0.2623 0.3297 -0.0172 0.0598  -0.0362 114 MET A CA  
976  C C   . MET A 113 ? 0.3805 0.3403 0.4114 -0.0151 0.0646  -0.0449 114 MET A C   
977  O O   . MET A 113 ? 0.3501 0.3111 0.3794 -0.0241 0.0723  -0.0521 114 MET A O   
978  C CB  . MET A 113 ? 0.3405 0.2823 0.3385 -0.0284 0.0598  -0.0355 114 MET A CB  
979  C CG  . MET A 113 ? 0.3630 0.2962 0.3485 -0.0298 0.0546  -0.0292 114 MET A CG  
980  S SD  . MET A 113 ? 0.3973 0.3247 0.3649 -0.0402 0.0523  -0.0290 114 MET A SD  
981  C CE  . MET A 113 ? 0.3562 0.2938 0.3264 -0.0390 0.0461  -0.0265 114 MET A CE  
982  N N   . GLU A 114 ? 0.3735 0.3427 0.4204 -0.0031 0.0604  -0.0450 115 GLU A N   
983  C CA  . GLU A 114 ? 0.3801 0.3650 0.4487 0.0021  0.0639  -0.0549 115 GLU A CA  
984  C C   . GLU A 114 ? 0.3810 0.3824 0.4565 -0.0065 0.0676  -0.0629 115 GLU A C   
985  O O   . GLU A 114 ? 0.3643 0.3731 0.4510 -0.0102 0.0767  -0.0740 115 GLU A O   
986  C CB  . GLU A 114 ? 0.4120 0.4049 0.4948 0.0184  0.0548  -0.0523 115 GLU A CB  
987  C CG  . GLU A 114 ? 0.5882 0.5612 0.6641 0.0272  0.0534  -0.0458 115 GLU A CG  
988  N N   . HIS A 115 ? 0.3404 0.3467 0.4091 -0.0103 0.0618  -0.0583 116 HIS A N   
989  C CA  . HIS A 115 ? 0.3533 0.3723 0.4265 -0.0196 0.0662  -0.0660 116 HIS A CA  
990  C C   . HIS A 115 ? 0.3755 0.3813 0.4325 -0.0345 0.0768  -0.0697 116 HIS A C   
991  O O   . HIS A 115 ? 0.3783 0.3920 0.4417 -0.0428 0.0861  -0.0803 116 HIS A O   
992  C CB  . HIS A 115 ? 0.3791 0.4041 0.4481 -0.0198 0.0577  -0.0603 116 HIS A CB  
993  C CG  . HIS A 115 ? 0.4337 0.4739 0.5178 -0.0067 0.0478  -0.0585 116 HIS A CG  
994  N ND1 . HIS A 115 ? 0.4663 0.5278 0.5744 0.0001  0.0477  -0.0681 116 HIS A ND1 
995  C CD2 . HIS A 115 ? 0.4584 0.4954 0.5356 0.0003  0.0377  -0.0487 116 HIS A CD2 
996  C CE1 . HIS A 115 ? 0.4604 0.5296 0.5737 0.0119  0.0361  -0.0628 116 HIS A CE1 
997  N NE2 . HIS A 115 ? 0.4591 0.5131 0.5530 0.0116  0.0305  -0.0510 116 HIS A NE2 
998  N N   . VAL A 116 ? 0.3091 0.2948 0.3444 -0.0383 0.0755  -0.0619 117 VAL A N   
999  C CA  . VAL A 116 ? 0.3264 0.2969 0.3422 -0.0514 0.0836  -0.0642 117 VAL A CA  
1000 C C   . VAL A 116 ? 0.3956 0.3668 0.4195 -0.0541 0.0951  -0.0745 117 VAL A C   
1001 O O   . VAL A 116 ? 0.3655 0.3356 0.3845 -0.0656 0.1054  -0.0828 117 VAL A O   
1002 C CB  . VAL A 116 ? 0.3716 0.3237 0.3646 -0.0536 0.0778  -0.0547 117 VAL A CB  
1003 C CG1 . VAL A 116 ? 0.3806 0.3168 0.3522 -0.0660 0.0851  -0.0575 117 VAL A CG1 
1004 C CG2 . VAL A 116 ? 0.3674 0.3195 0.3535 -0.0519 0.0680  -0.0468 117 VAL A CG2 
1005 N N   . VAL A 117 ? 0.3509 0.3223 0.3862 -0.0440 0.0942  -0.0744 118 VAL A N   
1006 C CA  . VAL A 117 ? 0.3511 0.3233 0.3969 -0.0447 0.1051  -0.0851 118 VAL A CA  
1007 C C   . VAL A 117 ? 0.4037 0.3965 0.4710 -0.0466 0.1126  -0.0983 118 VAL A C   
1008 O O   . VAL A 117 ? 0.4012 0.3929 0.4660 -0.0580 0.1252  -0.1087 118 VAL A O   
1009 C CB  . VAL A 117 ? 0.3887 0.3568 0.4451 -0.0313 0.1021  -0.0828 118 VAL A CB  
1010 C CG1 . VAL A 117 ? 0.3962 0.3654 0.4659 -0.0311 0.1140  -0.0954 118 VAL A CG1 
1011 C CG2 . VAL A 117 ? 0.3856 0.3341 0.4207 -0.0327 0.0974  -0.0723 118 VAL A CG2 
1012 N N   A ASP A 118 ? 0.3693 0.3811 0.4556 -0.0373 0.1049  -0.0983 119 ASP A N   
1013 N N   B ASP A 118 ? 0.3661 0.3783 0.4541 -0.0362 0.1049  -0.0987 119 ASP A N   
1014 C CA  A ASP A 118 ? 0.3711 0.4073 0.4813 -0.0383 0.1101  -0.1118 119 ASP A CA  
1015 C CA  B ASP A 118 ? 0.3675 0.4046 0.4805 -0.0364 0.1099  -0.1123 119 ASP A CA  
1016 C C   A ASP A 118 ? 0.4184 0.4532 0.5161 -0.0575 0.1212  -0.1188 119 ASP A C   
1017 C C   B ASP A 118 ? 0.4233 0.4604 0.5253 -0.0554 0.1212  -0.1200 119 ASP A C   
1018 O O   A ASP A 118 ? 0.4200 0.4650 0.5297 -0.0651 0.1341  -0.1336 119 ASP A O   
1019 O O   B ASP A 118 ? 0.4269 0.4755 0.5425 -0.0624 0.1338  -0.1350 119 ASP A O   
1020 C CB  A ASP A 118 ? 0.3889 0.4441 0.5165 -0.0256 0.0972  -0.1085 119 ASP A CB  
1021 C CB  B ASP A 118 ? 0.3824 0.4382 0.5119 -0.0240 0.0968  -0.1087 119 ASP A CB  
1022 C CG  A ASP A 118 ? 0.5527 0.6379 0.7093 -0.0250 0.1009  -0.1239 119 ASP A CG  
1023 C CG  B ASP A 118 ? 0.5311 0.5933 0.6788 -0.0041 0.0874  -0.1063 119 ASP A CG  
1024 O OD1 A ASP A 118 ? 0.5872 0.6851 0.7669 -0.0189 0.1063  -0.1358 119 ASP A OD1 
1025 O OD1 B ASP A 118 ? 0.5616 0.6222 0.7208 0.0015  0.0930  -0.1131 119 ASP A OD1 
1026 O OD2 A ASP A 118 ? 0.6263 0.7229 0.7837 -0.0308 0.0986  -0.1252 119 ASP A OD2 
1027 O OD2 B ASP A 118 ? 0.6086 0.6759 0.7578 0.0059  0.0744  -0.0979 119 ASP A OD2 
1028 N N   A THR A 119 ? 0.3725 0.3935 0.4454 -0.0656 0.1169  -0.1089 120 THR A N   
1029 N N   B THR A 119 ? 0.3774 0.4003 0.4543 -0.0639 0.1173  -0.1102 120 THR A N   
1030 C CA  A THR A 119 ? 0.3822 0.3958 0.4381 -0.0839 0.1273  -0.1142 120 THR A CA  
1031 C CA  B THR A 119 ? 0.3879 0.4042 0.4481 -0.0818 0.1268  -0.1149 120 THR A CA  
1032 C C   A THR A 119 ? 0.4290 0.4230 0.4640 -0.0965 0.1393  -0.1178 120 THR A C   
1033 C C   B THR A 119 ? 0.4359 0.4322 0.4743 -0.0952 0.1392  -0.1185 120 THR A C   
1034 O O   A THR A 119 ? 0.4312 0.4239 0.4600 -0.1116 0.1526  -0.1281 120 THR A O   
1035 O O   B THR A 119 ? 0.4408 0.4382 0.4761 -0.1096 0.1529  -0.1299 120 THR A O   
1036 C CB  A THR A 119 ? 0.3907 0.3927 0.4259 -0.0881 0.1195  -0.1035 120 THR A CB  
1037 C CB  B THR A 119 ? 0.4555 0.4613 0.4965 -0.0841 0.1176  -0.1032 120 THR A CB  
1038 O OG1 A THR A 119 ? 0.4131 0.4113 0.4377 -0.1047 0.1308  -0.1113 120 THR A OG1 
1039 O OG1 B THR A 119 ? 0.4266 0.4493 0.4862 -0.0700 0.1052  -0.0987 120 THR A OG1 
1040 C CG2 A THR A 119 ? 0.3484 0.3241 0.3542 -0.0881 0.1124  -0.0895 120 THR A CG2 
1041 C CG2 B THR A 119 ? 0.4584 0.4615 0.4888 -0.1001 0.1268  -0.1097 120 THR A CG2 
1042 N N   . CYS A 120 ? 0.3920 0.3705 0.4148 -0.0916 0.1352  -0.1100 121 CYS A N   
1043 C CA  . CYS A 120 ? 0.4117 0.3719 0.4134 -0.1036 0.1458  -0.1137 121 CYS A CA  
1044 C C   . CYS A 120 ? 0.4792 0.4535 0.5026 -0.1066 0.1604  -0.1307 121 CYS A C   
1045 O O   . CYS A 120 ? 0.4636 0.4308 0.4736 -0.1229 0.1746  -0.1400 121 CYS A O   
1046 C CB  . CYS A 120 ? 0.4157 0.3604 0.4040 -0.0972 0.1380  -0.1036 121 CYS A CB  
1047 S SG  . CYS A 120 ? 0.4624 0.3884 0.4208 -0.0978 0.1237  -0.0868 121 CYS A SG  
1048 N N   A ARG A 121 ? 0.4367 0.4305 0.4932 -0.0907 0.1570  -0.1353 122 ARG A N   
1049 N N   B ARG A 121 ? 0.4409 0.4345 0.4971 -0.0908 0.1571  -0.1353 122 ARG A N   
1050 C CA  A ARG A 121 ? 0.4418 0.4534 0.5267 -0.0889 0.1687  -0.1526 122 ARG A CA  
1051 C CA  B ARG A 121 ? 0.4482 0.4590 0.5319 -0.0897 0.1693  -0.1528 122 ARG A CA  
1052 C C   A ARG A 121 ? 0.4808 0.5097 0.5766 -0.1016 0.1806  -0.1675 122 ARG A C   
1053 C C   B ARG A 121 ? 0.4828 0.5117 0.5784 -0.1019 0.1808  -0.1676 122 ARG A C   
1054 O O   A ARG A 121 ? 0.4813 0.5128 0.5802 -0.1133 0.1971  -0.1825 122 ARG A O   
1055 O O   B ARG A 121 ? 0.4820 0.5137 0.5810 -0.1136 0.1973  -0.1828 122 ARG A O   
1056 C CB  A ARG A 121 ? 0.4410 0.4703 0.5586 -0.0666 0.1584  -0.1525 122 ARG A CB  
1057 C CB  B ARG A 121 ? 0.4572 0.4842 0.5731 -0.0677 0.1599  -0.1530 122 ARG A CB  
1058 C CG  A ARG A 121 ? 0.6044 0.6161 0.7146 -0.0555 0.1514  -0.1421 122 ARG A CG  
1059 C CG  B ARG A 121 ? 0.6490 0.6586 0.7586 -0.0593 0.1576  -0.1471 122 ARG A CG  
1060 C CD  A ARG A 121 ? 0.7501 0.7751 0.8916 -0.0351 0.1461  -0.1460 122 ARG A CD  
1061 C CD  B ARG A 121 ? 0.7848 0.8084 0.9276 -0.0402 0.1547  -0.1534 122 ARG A CD  
1062 N NE  A ARG A 121 ? 0.8174 0.8225 0.9481 -0.0245 0.1378  -0.1334 122 ARG A NE  
1063 N NE  B ARG A 121 ? 0.8481 0.8794 1.0013 -0.0230 0.1377  -0.1425 122 ARG A NE  
1064 C CZ  A ARG A 121 ? 0.9611 0.9493 1.0850 -0.0255 0.1450  -0.1356 122 ARG A CZ  
1065 C CZ  B ARG A 121 ? 0.9805 0.9970 1.1274 -0.0103 0.1274  -0.1300 122 ARG A CZ  
1066 N NH1 A ARG A 121 ? 0.8535 0.8424 0.9801 -0.0363 0.1606  -0.1500 122 ARG A NH1 
1067 N NH1 B ARG A 121 ? 0.7855 0.7798 0.9179 -0.0123 0.1324  -0.1274 122 ARG A NH1 
1068 N NH2 A ARG A 121 ? 0.7305 0.7003 0.8440 -0.0171 0.1378  -0.1244 122 ARG A NH2 
1069 N NH2 B ARG A 121 ? 0.7858 0.8088 0.9394 0.0036  0.1128  -0.1207 122 ARG A NH2 
1070 N N   . LYS A 122 ? 0.4233 0.4633 0.5236 -0.1008 0.1733  -0.1640 123 LYS A N   
1071 C CA  . LYS A 122 ? 0.4376 0.4949 0.5485 -0.1136 0.1841  -0.1782 123 LYS A CA  
1072 C C   . LYS A 122 ? 0.5084 0.5420 0.5836 -0.1378 0.1983  -0.1800 123 LYS A C   
1073 O O   . LYS A 122 ? 0.5038 0.5466 0.5860 -0.1522 0.2155  -0.1972 123 LYS A O   
1074 C CB  . LYS A 122 ? 0.4532 0.5269 0.5766 -0.1063 0.1718  -0.1736 123 LYS A CB  
1075 C CG  . LYS A 122 ? 0.6891 0.7913 0.8512 -0.0844 0.1604  -0.1768 123 LYS A CG  
1076 C CD  . LYS A 122 ? 0.8311 0.9497 1.0037 -0.0773 0.1475  -0.1723 123 LYS A CD  
1077 C CE  . LYS A 122 ? 0.9909 1.1330 1.1958 -0.0543 0.1341  -0.1732 123 LYS A CE  
1078 N NZ  . LYS A 122 ? 1.1309 1.3041 1.3603 -0.0509 0.1280  -0.1814 123 LYS A NZ  
1079 N N   . PHE A 123 ? 0.4761 0.4787 0.5125 -0.1421 0.1913  -0.1631 124 PHE A N   
1080 C CA  . PHE A 123 ? 0.5007 0.4749 0.4967 -0.1632 0.2020  -0.1619 124 PHE A CA  
1081 C C   . PHE A 123 ? 0.5662 0.5305 0.5519 -0.1736 0.2166  -0.1713 124 PHE A C   
1082 O O   . PHE A 123 ? 0.5694 0.5238 0.5371 -0.1937 0.2333  -0.1812 124 PHE A O   
1083 C CB  . PHE A 123 ? 0.5250 0.4708 0.4854 -0.1614 0.1879  -0.1416 124 PHE A CB  
1084 C CG  . PHE A 123 ? 0.5481 0.4926 0.5033 -0.1616 0.1804  -0.1346 124 PHE A CG  
1085 C CD1 . PHE A 123 ? 0.5676 0.5406 0.5567 -0.1507 0.1741  -0.1382 124 PHE A CD1 
1086 C CD2 . PHE A 123 ? 0.6032 0.5166 0.5183 -0.1716 0.1783  -0.1241 124 PHE A CD2 
1087 C CE1 . PHE A 123 ? 0.5767 0.5482 0.5605 -0.1517 0.1677  -0.1325 124 PHE A CE1 
1088 C CE2 . PHE A 123 ? 0.6297 0.5399 0.5401 -0.1714 0.1718  -0.1182 124 PHE A CE2 
1089 C CZ  . PHE A 123 ? 0.5793 0.5190 0.5244 -0.1622 0.1673  -0.1229 124 PHE A CZ  
1090 N N   . ILE A 124 ? 0.4984 0.4651 0.4955 -0.1609 0.2117  -0.1694 125 ILE A N   
1091 C CA  . ILE A 124 ? 0.5190 0.4782 0.5097 -0.1697 0.2258  -0.1798 125 ILE A CA  
1092 C C   . ILE A 124 ? 0.6015 0.5866 0.6245 -0.1758 0.2438  -0.2032 125 ILE A C   
1093 O O   . ILE A 124 ? 0.6321 0.6082 0.6390 -0.1950 0.2620  -0.2150 125 ILE A O   
1094 C CB  . ILE A 124 ? 0.5474 0.5009 0.5416 -0.1550 0.2164  -0.1722 125 ILE A CB  
1095 C CG1 . ILE A 124 ? 0.5536 0.4802 0.5105 -0.1550 0.2026  -0.1527 125 ILE A CG1 
1096 C CG2 . ILE A 124 ? 0.5845 0.5354 0.5807 -0.1623 0.2323  -0.1864 125 ILE A CG2 
1097 C CD1 . ILE A 124 ? 0.6068 0.5311 0.5702 -0.1388 0.1895  -0.1428 125 ILE A CD1 
1098 N N   . LYS A 125 ? 0.5506 0.5681 0.6180 -0.1599 0.2385  -0.2103 126 LYS A N   
1099 C CA  . LYS A 125 ? 0.5617 0.6102 0.6674 -0.1622 0.2528  -0.2339 126 LYS A CA  
1100 C C   . LYS A 125 ? 0.6262 0.6767 0.7209 -0.1861 0.2695  -0.2461 126 LYS A C   
1101 O O   . LYS A 125 ? 0.6213 0.6841 0.7290 -0.1988 0.2890  -0.2670 126 LYS A O   
1102 C CB  . LYS A 125 ? 0.5768 0.6585 0.7283 -0.1389 0.2395  -0.2365 126 LYS A CB  
1103 N N   . ALA A 126 ? 0.5833 0.6195 0.6526 -0.1930 0.2629  -0.2338 127 ALA A N   
1104 C CA  . ALA A 126 ? 0.6085 0.6402 0.6615 -0.2168 0.2785  -0.2433 127 ALA A CA  
1105 C C   . ALA A 126 ? 0.7117 0.7108 0.7210 -0.2411 0.2965  -0.2463 127 ALA A C   
1106 O O   . ALA A 126 ? 0.7192 0.7206 0.7243 -0.2624 0.3166  -0.2625 127 ALA A O   
1107 C CB  . ALA A 126 ? 0.6091 0.6291 0.6436 -0.2163 0.2658  -0.2278 127 ALA A CB  
1108 N N   . SER A 127 ? 0.7158 0.6849 0.6917 -0.2388 0.2893  -0.2311 128 SER A N   
1109 C CA  . SER A 127 ? 0.7784 0.7137 0.7075 -0.2605 0.3031  -0.2314 128 SER A CA  
1110 C C   . SER A 127 ? 0.8788 0.8225 0.8198 -0.2675 0.3207  -0.2497 128 SER A C   
1111 O O   . SER A 127 ? 0.9272 0.8466 0.8314 -0.2893 0.3363  -0.2546 128 SER A O   
1112 C CB  . SER A 127 ? 0.8500 0.7499 0.7357 -0.2557 0.2862  -0.2074 128 SER A CB  
1113 O OG  . SER A 127 ? 0.9984 0.8762 0.8531 -0.2622 0.2796  -0.1945 128 SER A OG  
1114 N N   . GLU A 128 ? 0.8109 0.7873 0.8015 -0.2495 0.3186  -0.2602 129 GLU A N   
1115 C CA  . GLU A 128 ? 1.0657 1.0520 1.0730 -0.2535 0.3349  -0.2789 129 GLU A CA  
1116 C C   . GLU A 128 ? 1.5751 1.5836 1.6035 -0.2718 0.3599  -0.3063 129 GLU A C   
1117 O O   . GLU A 128 ? 1.1603 1.1649 1.1736 -0.2892 0.3687  -0.3098 129 GLU A O   
1118 C CB  . GLU A 128 ? 1.0520 1.0595 1.1010 -0.2261 0.3225  -0.2788 129 GLU A CB  
1119 C CG  . GLU A 128 ? 1.1449 1.1945 1.2512 -0.2094 0.3191  -0.2916 129 GLU A CG  
1120 C CD  . GLU A 128 ? 1.3810 1.4461 1.5232 -0.1802 0.3034  -0.2876 129 GLU A CD  
1121 O OE1 . GLU A 128 ? 1.2859 1.3285 1.4078 -0.1701 0.2899  -0.2692 129 GLU A OE1 
1122 O OE2 . GLU A 128 ? 1.2724 1.3720 1.4627 -0.1673 0.3043  -0.3032 129 GLU A OE2 
1126 N N   A TRP B 2   ? 0.2125 0.4634 0.3211 -0.0441 -0.0040 -0.0847 1   TRP D N   
1127 N N   B TRP B 2   ? 0.2299 0.4808 0.3385 -0.0441 -0.0040 -0.0847 1   TRP D N   
1128 C CA  A TRP B 2   ? 0.2007 0.4509 0.3092 -0.0440 -0.0037 -0.0852 1   TRP D CA  
1129 C CA  B TRP B 2   ? 0.2278 0.4781 0.3365 -0.0440 -0.0037 -0.0852 1   TRP D CA  
1130 C C   A TRP B 2   ? 0.2546 0.5049 0.3658 -0.0446 -0.0047 -0.0840 1   TRP D C   
1131 C C   B TRP B 2   ? 0.2563 0.5069 0.3677 -0.0447 -0.0046 -0.0839 1   TRP D C   
1132 O O   A TRP B 2   ? 0.2521 0.5015 0.3642 -0.0451 -0.0061 -0.0833 1   TRP D O   
1133 O O   B TRP B 2   ? 0.2453 0.4954 0.3578 -0.0453 -0.0059 -0.0831 1   TRP D O   
1134 C CB  A TRP B 2   ? 0.1889 0.4368 0.2942 -0.0436 -0.0052 -0.0865 1   TRP D CB  
1135 C CB  B TRP B 2   ? 0.2237 0.4716 0.3293 -0.0436 -0.0052 -0.0863 1   TRP D CB  
1136 C CG  A TRP B 2   ? 0.1909 0.4386 0.2925 -0.0431 -0.0044 -0.0891 1   TRP D CG  
1137 C CG  B TRP B 2   ? 0.2413 0.4886 0.3484 -0.0436 -0.0079 -0.0859 1   TRP D CG  
1138 C CD1 A TRP B 2   ? 0.2200 0.4672 0.3194 -0.0429 -0.0055 -0.0907 1   TRP D CD1 
1139 C CD1 B TRP B 2   ? 0.2811 0.5282 0.3888 -0.0436 -0.0101 -0.0865 1   TRP D CD1 
1140 C CD2 A TRP B 2   ? 0.1901 0.4381 0.2897 -0.0428 -0.0022 -0.0910 1   TRP D CD2 
1141 C CD2 B TRP B 2   ? 0.2405 0.4884 0.3497 -0.0431 -0.0087 -0.0853 1   TRP D CD2 
1142 N NE1 A TRP B 2   ? 0.2058 0.4530 0.3010 -0.0422 -0.0040 -0.0942 1   TRP D NE1 
1143 N NE1 B TRP B 2   ? 0.2755 0.5236 0.3870 -0.0432 -0.0121 -0.0865 1   TRP D NE1 
1144 C CE2 A TRP B 2   ? 0.2214 0.4692 0.3168 -0.0423 -0.0018 -0.0945 1   TRP D CE2 
1145 C CE2 B TRP B 2   ? 0.2916 0.5404 0.4036 -0.0427 -0.0110 -0.0860 1   TRP D CE2 
1146 C CE3 A TRP B 2   ? 0.2017 0.4498 0.3027 -0.0429 -0.0003 -0.0904 1   TRP D CE3 
1147 C CE3 B TRP B 2   ? 0.2529 0.5007 0.3623 -0.0427 -0.0077 -0.0847 1   TRP D CE3 
1148 C CZ2 A TRP B 2   ? 0.2183 0.4662 0.3107 -0.0420 0.0005  -0.0978 1   TRP D CZ2 
1149 C CZ2 B TRP B 2   ? 0.2817 0.5323 0.3969 -0.0415 -0.0117 -0.0865 1   TRP D CZ2 
1150 C CZ3 A TRP B 2   ? 0.2156 0.4637 0.3144 -0.0427 0.0019  -0.0928 1   TRP D CZ3 
1151 C CZ3 B TRP B 2   ? 0.2723 0.5210 0.3834 -0.0415 -0.0087 -0.0850 1   TRP D CZ3 
1152 C CH2 A TRP B 2   ? 0.2220 0.4701 0.3165 -0.0423 0.0026  -0.0967 1   TRP D CH2 
1153 C CH2 B TRP B 2   ? 0.2783 0.5288 0.3923 -0.0408 -0.0103 -0.0861 1   TRP D CH2 
1154 N N   . VAL B 3   ? 0.1992 0.4504 0.3117 -0.0446 -0.0040 -0.0842 2   VAL D N   
1155 C CA  . VAL B 3   ? 0.2003 0.4516 0.3144 -0.0450 -0.0051 -0.0842 2   VAL D CA  
1156 C C   . VAL B 3   ? 0.2248 0.4743 0.3380 -0.0440 -0.0052 -0.0843 2   VAL D C   
1157 O O   . VAL B 3   ? 0.2165 0.4653 0.3287 -0.0436 -0.0040 -0.0841 2   VAL D O   
1158 C CB  . VAL B 3   ? 0.2382 0.4940 0.3560 -0.0463 -0.0050 -0.0847 2   VAL D CB  
1159 C CG1 . VAL B 3   ? 0.2396 0.4982 0.3583 -0.0472 -0.0049 -0.0838 2   VAL D CG1 
1160 C CG2 . VAL B 3   ? 0.2265 0.4859 0.3476 -0.0459 -0.0036 -0.0856 2   VAL D CG2 
1161 N N   . ILE B 4   ? 0.2039 0.4527 0.3172 -0.0437 -0.0063 -0.0850 3   ILE D N   
1162 C CA  . ILE B 4   ? 0.2031 0.4504 0.3156 -0.0426 -0.0066 -0.0850 3   ILE D CA  
1163 C C   . ILE B 4   ? 0.2556 0.5052 0.3717 -0.0437 -0.0068 -0.0860 3   ILE D C   
1164 O O   . ILE B 4   ? 0.2539 0.5057 0.3715 -0.0448 -0.0082 -0.0878 3   ILE D O   
1165 C CB  . ILE B 4   ? 0.2278 0.4742 0.3388 -0.0411 -0.0077 -0.0863 3   ILE D CB  
1166 C CG1 . ILE B 4   ? 0.2001 0.4471 0.3106 -0.0397 -0.0077 -0.0863 3   ILE D CG1 
1167 C CG2 . ILE B 4   ? 0.2594 0.5043 0.3693 -0.0395 -0.0080 -0.0862 3   ILE D CG2 
1168 C CD1 . ILE B 4   ? 0.2640 0.5117 0.3733 -0.0388 -0.0075 -0.0846 3   ILE D CD1 
1169 N N   . PRO B 5   ? 0.2424 0.4923 0.3608 -0.0436 -0.0057 -0.0853 4   PRO D N   
1170 C CA  . PRO B 5   ? 0.2478 0.5019 0.3722 -0.0445 -0.0063 -0.0869 4   PRO D CA  
1171 C C   . PRO B 5   ? 0.3050 0.5582 0.4301 -0.0444 -0.0089 -0.0883 4   PRO D C   
1172 O O   . PRO B 5   ? 0.2909 0.5393 0.4119 -0.0430 -0.0092 -0.0872 4   PRO D O   
1173 C CB  . PRO B 5   ? 0.2659 0.5204 0.3932 -0.0441 -0.0039 -0.0861 4   PRO D CB  
1174 C CG  . PRO B 5   ? 0.3181 0.5668 0.4394 -0.0431 -0.0031 -0.0837 4   PRO D CG  
1175 C CD  . PRO B 5   ? 0.2650 0.5127 0.3816 -0.0429 -0.0039 -0.0836 4   PRO D CD  
1176 N N   . ALA B 6   ? 0.2839 0.5426 0.4146 -0.0457 -0.0109 -0.0911 5   ALA D N   
# 
