data_7GUS
# 
_entry.id   7GUS 
# 
_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   7GUS         pdb_00007gus 10.2210/pdb7gus/pdb 
WWPDB D_1001406663 ?            ?                   
# 
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                        7GUS 
_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 7   HOH   HOH A . 
F 6 HOH   2   302 178 HOH   HOH A . 
F 6 HOH   3   303 45  HOH   HOH A . 
F 6 HOH   4   304 173 HOH   HOH A . 
F 6 HOH   5   305 202 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  310 247 HOH   HOH A . 
F 6 HOH   11  311 139 HOH   HOH A . 
F 6 HOH   12  312 166 HOH   HOH A . 
F 6 HOH   13  313 99  HOH   HOH A . 
F 6 HOH   14  314 106 HOH   HOH A . 
F 6 HOH   15  315 90  HOH   HOH A . 
F 6 HOH   16  316 40  HOH   HOH A . 
F 6 HOH   17  317 179 HOH   HOH A . 
F 6 HOH   18  318 17  HOH   HOH A . 
F 6 HOH   19  319 37  HOH   HOH A . 
F 6 HOH   20  320 75  HOH   HOH A . 
F 6 HOH   21  321 83  HOH   HOH A . 
F 6 HOH   22  322 29  HOH   HOH A . 
F 6 HOH   23  323 142 HOH   HOH A . 
F 6 HOH   24  324 87  HOH   HOH A . 
F 6 HOH   25  325 193 HOH   HOH A . 
F 6 HOH   26  326 237 HOH   HOH A . 
F 6 HOH   27  327 6   HOH   HOH A . 
F 6 HOH   28  328 101 HOH   HOH A . 
F 6 HOH   29  329 84  HOH   HOH A . 
F 6 HOH   30  330 239 HOH   HOH A . 
F 6 HOH   31  331 117 HOH   HOH A . 
F 6 HOH   32  332 151 HOH   HOH A . 
F 6 HOH   33  333 119 HOH   HOH A . 
F 6 HOH   34  334 47  HOH   HOH A . 
F 6 HOH   35  335 132 HOH   HOH A . 
F 6 HOH   36  336 5   HOH   HOH A . 
F 6 HOH   37  337 91  HOH   HOH A . 
F 6 HOH   38  338 144 HOH   HOH A . 
F 6 HOH   39  339 27  HOH   HOH A . 
F 6 HOH   40  340 34  HOH   HOH A . 
F 6 HOH   41  341 14  HOH   HOH A . 
F 6 HOH   42  342 122 HOH   HOH A . 
F 6 HOH   43  343 243 HOH   HOH A . 
F 6 HOH   44  344 4   HOH   HOH A . 
F 6 HOH   45  345 28  HOH   HOH A . 
F 6 HOH   46  346 196 HOH   HOH A . 
F 6 HOH   47  347 12  HOH   HOH A . 
F 6 HOH   48  348 24  HOH   HOH A . 
F 6 HOH   49  349 242 HOH   HOH A . 
F 6 HOH   50  350 20  HOH   HOH A . 
F 6 HOH   51  351 244 HOH   HOH A . 
F 6 HOH   52  352 86  HOH   HOH A . 
F 6 HOH   53  353 85  HOH   HOH A . 
F 6 HOH   54  354 44  HOH   HOH A . 
F 6 HOH   55  355 50  HOH   HOH A . 
F 6 HOH   56  356 133 HOH   HOH A . 
F 6 HOH   57  357 145 HOH   HOH A . 
F 6 HOH   58  358 96  HOH   HOH A . 
F 6 HOH   59  359 93  HOH   HOH A . 
F 6 HOH   60  360 141 HOH   HOH A . 
F 6 HOH   61  361 186 HOH   HOH A . 
F 6 HOH   62  362 42  HOH   HOH A . 
F 6 HOH   63  363 74  HOH   HOH A . 
F 6 HOH   64  364 51  HOH   HOH A . 
F 6 HOH   65  365 89  HOH   HOH A . 
F 6 HOH   66  366 97  HOH   HOH A . 
F 6 HOH   67  367 175 HOH   HOH A . 
F 6 HOH   68  368 30  HOH   HOH A . 
F 6 HOH   69  369 245 HOH   HOH A . 
F 6 HOH   70  370 124 HOH   HOH A . 
F 6 HOH   71  371 177 HOH   HOH A . 
F 6 HOH   72  372 207 HOH   HOH A . 
F 6 HOH   73  373 25  HOH   HOH A . 
F 6 HOH   74  374 103 HOH   HOH A . 
F 6 HOH   75  375 169 HOH   HOH A . 
F 6 HOH   76  376 229 HOH   HOH A . 
F 6 HOH   77  377 191 HOH   HOH A . 
F 6 HOH   78  378 194 HOH   HOH A . 
F 6 HOH   79  379 105 HOH   HOH A . 
F 6 HOH   80  380 170 HOH   HOH A . 
F 6 HOH   81  381 21  HOH   HOH A . 
F 6 HOH   82  382 131 HOH   HOH A . 
F 6 HOH   83  383 15  HOH   HOH A . 
F 6 HOH   84  384 192 HOH   HOH A . 
F 6 HOH   85  385 174 HOH   HOH A . 
F 6 HOH   86  386 39  HOH   HOH A . 
F 6 HOH   87  387 157 HOH   HOH A . 
F 6 HOH   88  388 76  HOH   HOH A . 
F 6 HOH   89  389 167 HOH   HOH A . 
F 6 HOH   90  390 32  HOH   HOH A . 
F 6 HOH   91  391 61  HOH   HOH A . 
F 6 HOH   92  392 70  HOH   HOH A . 
F 6 HOH   93  393 69  HOH   HOH A . 
F 6 HOH   94  394 241 HOH   HOH A . 
F 6 HOH   95  395 165 HOH   HOH A . 
F 6 HOH   96  396 55  HOH   HOH A . 
F 6 HOH   97  397 205 HOH   HOH A . 
F 6 HOH   98  398 64  HOH   HOH A . 
F 6 HOH   99  399 180 HOH   HOH A . 
F 6 HOH   100 400 22  HOH   HOH A . 
F 6 HOH   101 401 185 HOH   HOH A . 
F 6 HOH   102 402 92  HOH   HOH A . 
F 6 HOH   103 403 67  HOH   HOH A . 
F 6 HOH   104 404 35  HOH   HOH A . 
F 6 HOH   105 405 120 HOH   HOH A . 
F 6 HOH   106 406 26  HOH   HOH A . 
F 6 HOH   107 407 190 HOH   HOH A . 
F 6 HOH   108 408 43  HOH   HOH A . 
F 6 HOH   109 409 212 HOH   HOH A . 
F 6 HOH   110 410 60  HOH   HOH A . 
F 6 HOH   111 411 129 HOH   HOH A . 
F 6 HOH   112 412 223 HOH   HOH A . 
F 6 HOH   113 413 82  HOH   HOH A . 
F 6 HOH   114 414 236 HOH   HOH A . 
F 6 HOH   115 415 176 HOH   HOH A . 
F 6 HOH   116 416 16  HOH   HOH A . 
F 6 HOH   117 417 108 HOH   HOH A . 
F 6 HOH   118 418 88  HOH   HOH A . 
F 6 HOH   119 419 36  HOH   HOH A . 
F 6 HOH   120 420 56  HOH   HOH A . 
F 6 HOH   121 421 46  HOH   HOH A . 
F 6 HOH   122 422 68  HOH   HOH A . 
F 6 HOH   123 423 215 HOH   HOH A . 
F 6 HOH   124 424 65  HOH   HOH A . 
F 6 HOH   125 425 57  HOH   HOH A . 
F 6 HOH   126 426 110 HOH   HOH A . 
F 6 HOH   127 427 204 HOH   HOH A . 
F 6 HOH   128 428 95  HOH   HOH A . 
F 6 HOH   129 429 168 HOH   HOH A . 
F 6 HOH   130 430 41  HOH   HOH A . 
F 6 HOH   131 431 135 HOH   HOH A . 
F 6 HOH   132 432 116 HOH   HOH A . 
F 6 HOH   133 433 147 HOH   HOH A . 
F 6 HOH   134 434 227 HOH   HOH A . 
F 6 HOH   135 435 187 HOH   HOH A . 
F 6 HOH   136 436 231 HOH   HOH A . 
F 6 HOH   137 437 123 HOH   HOH A . 
F 6 HOH   138 438 214 HOH   HOH A . 
F 6 HOH   139 439 200 HOH   HOH A . 
F 6 HOH   140 440 228 HOH   HOH A . 
F 6 HOH   141 441 248 HOH   HOH A . 
F 6 HOH   142 442 71  HOH   HOH A . 
F 6 HOH   143 443 121 HOH   HOH A . 
F 6 HOH   144 444 63  HOH   HOH A . 
F 6 HOH   145 445 171 HOH   HOH A . 
F 6 HOH   146 446 203 HOH   HOH A . 
F 6 HOH   147 447 225 HOH   HOH A . 
F 6 HOH   148 448 238 HOH   HOH A . 
F 6 HOH   149 449 220 HOH   HOH A . 
F 6 HOH   150 450 234 HOH   HOH A . 
F 6 HOH   151 451 125 HOH   HOH A . 
F 6 HOH   152 452 158 HOH   HOH A . 
F 6 HOH   153 453 181 HOH   HOH A . 
F 6 HOH   154 454 114 HOH   HOH A . 
F 6 HOH   155 455 79  HOH   HOH A . 
F 6 HOH   156 456 217 HOH   HOH A . 
F 6 HOH   157 457 246 HOH   HOH A . 
F 6 HOH   158 458 81  HOH   HOH A . 
F 6 HOH   159 459 107 HOH   HOH A . 
F 6 HOH   160 460 221 HOH   HOH A . 
F 6 HOH   161 461 115 HOH   HOH A . 
F 6 HOH   162 462 235 HOH   HOH A . 
F 6 HOH   163 463 113 HOH   HOH A . 
F 6 HOH   164 464 230 HOH   HOH A . 
F 6 HOH   165 465 216 HOH   HOH A . 
F 6 HOH   166 466 182 HOH   HOH A . 
F 6 HOH   167 467 188 HOH   HOH A . 
F 6 HOH   168 468 201 HOH   HOH A . 
F 6 HOH   169 469 148 HOH   HOH A . 
F 6 HOH   170 470 213 HOH   HOH A . 
F 6 HOH   171 471 206 HOH   HOH A . 
F 6 HOH   172 472 48  HOH   HOH A . 
F 6 HOH   173 473 183 HOH   HOH A . 
F 6 HOH   174 474 172 HOH   HOH A . 
F 6 HOH   175 475 211 HOH   HOH A . 
G 6 HOH   1   201 62  HOH   HOH D . 
G 6 HOH   2   202 78  HOH   HOH D . 
G 6 HOH   3   203 23  HOH   HOH D . 
G 6 HOH   4   204 38  HOH   HOH D . 
G 6 HOH   5   205 53  HOH   HOH D . 
G 6 HOH   6   206 73  HOH   HOH D . 
G 6 HOH   7   207 240 HOH   HOH D . 
G 6 HOH   8   208 49  HOH   HOH D . 
G 6 HOH   9   209 58  HOH   HOH D . 
G 6 HOH   10  210 195 HOH   HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 64  ? CD  ? A GLN 63  CD  
2  1 Y 1 A GLN 64  ? OE1 ? A GLN 63  OE1 
3  1 Y 1 A GLN 64  ? NE2 ? A GLN 63  NE2 
4  1 Y 1 A GLU 115 ? CD  ? A GLU 114 CD  
5  1 Y 1 A GLU 115 ? OE1 ? A GLU 114 OE1 
6  1 Y 1 A GLU 115 ? OE2 ? A GLU 114 OE2 
7  1 Y 1 A LYS 126 ? CG  ? A LYS 125 CG  
8  1 Y 1 A LYS 126 ? CD  ? A LYS 125 CD  
9  1 Y 1 A LYS 126 ? CE  ? A LYS 125 CE  
10 1 Y 1 A LYS 126 ? NZ  ? A LYS 125 NZ  
11 1 Y 1 D ALA 5   ? CA  ? B ALA 6   CA  
12 1 Y 1 D ALA 5   ? C   ? B ALA 6   C   
13 1 Y 1 D ALA 5   ? O   ? B ALA 6   O   
14 1 Y 1 D ALA 5   ? CB  ? B ALA 6   CB  
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      2.10.3 ?                                         program 'Gerard Bricogne' buster-develop@GlobalPhasing.com 
refinement        http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.5.32 29/03/17                                  program 'Phil Evans'      ?                                
'data scaling'    http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 Aimless     0.5.32 29/03/17                                  program 'Phil Evans'      ?                                
'data reduction'  http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
4 PHASER      2.7.17 'Tue Jun 20 23:45:36 2017 (svn exported)' program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk      phasing 
http://www-structmed.cimr.cam.ac.uk/phaser/         ?   ? 
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           7GUS 
_cell.length_a           67.737 
_cell.length_b           67.737 
_cell.length_c           166.681 
_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                         7GUS 
_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          7GUS 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.64 
_exptl_crystal.density_percent_sol   66.24 
_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                     7GUS 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.970 
_reflns.d_resolution_high            1.750 
_reflns.number_obs                   23750 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.073 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.400 
_reflns.B_iso_Wilson_estimate        27.110 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.078 
_reflns.pdbx_Rpim_I_all              0.026 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     215288 
_reflns.pdbx_scaling_rejects         1327 
_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  ? 11903 1284 ? 0.585 ? ? ? 9.300 ? 3.400  ? ? ? ? ? ? 100.000 0.619 0.200 0.943 ? 
1 2 9.090 33.970 ? 1511  234  ? 0.050 ? ? ? 6.500 ? 26.800 ? ? ? ? ? ? 98.800  0.054 0.021 0.998 ? 
# 
_refine.entry_id                                 7GUS 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.7500 
_refine.ls_d_res_low                             33.9700 
_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                     23684 
_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                          0.1860 
_refine.ls_R_factor_R_work                       0.1850 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2150 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1400 
_refine.ls_number_reflns_R_free                  1218 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               31.2200 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.2213 
_refine.aniso_B[2][2]                            0.2213 
_refine.aniso_B[3][3]                            -0.4426 
_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               0.9560 
_refine.correlation_coeff_Fo_to_Fc_free          0.9390 
_refine.overall_SU_R_Cruickshank_DPI             0.0890 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0900 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1020 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.0990 
_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          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                113.030 
_refine.B_iso_min                                14.810 
_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                        7GUS 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.230 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.7500 
_refine_hist.d_res_low                        33.9700 
_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           25.69 
_refine_hist.pdbx_B_iso_mean_solvent          45.89 
_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      1650 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1233 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1689 0.870  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.400  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    14.690 ? ?      ?            
# 
_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               99.9300 
_refine_ls_shell.number_reflns_R_work             2693 
_refine_ls_shell.R_factor_all                     0.3183 
_refine_ls_shell.R_factor_R_work                  0.3166 
_refine_ls_shell.R_factor_R_free                  0.3564 
_refine_ls_shell.percent_reflns_R_free            4.6100 
_refine_ls_shell.number_reflns_R_free             130 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2823 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUS 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 at 1.25 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUS 
_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 7GUS       7GUS   ? 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 7GUS A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUS D 1 ? 6   ? 7GUS   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 7GUS GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUS PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUS 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)' 7400  ? 
1 MORE         -64   ? 
1 'SSA (A^2)'  12990 ? 
# 
_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 33.8685000000 0.8660254038 
-0.5000000000 0.0000000000 -58.6619627761 0.0000000000 0.0000000000 -1.0000000000 27.7801666667 
# 
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 ? ? ? ? ? ? ? 1.333 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
# 
_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                   7GUS 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 39 ? A 61.33 -118.88 
2 1 SER A 39 ? B 39.44 64.74   
3 1 ARG A 40 ? B 74.61 -20.85  
4 1 SER A 93 ? A 76.80 -5.25   
# 
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 380 ? F HOH . 
3 1 A HOH 462 ? F HOH . 
4 1 A HOH 464 ? F HOH . 
5 1 A HOH 468 ? F HOH . 
6 1 A HOH 473 ? 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 0.0164  -0.0493 -0.0798 -0.0397 0.0299  -0.0215 0.9727 1.7692  1.9569 
0.3975  -0.2929 1.1296 0.1326 -0.0729 -0.0597 -0.0473 0.0968 0.0795 0.2575  -0.0005 0.0040  
'X-RAY DIFFRACTION' 2 ? refined 18.9076 -32.4261 1.8469  -0.1108 0.1403  -0.0507 -0.0267 -0.0200 -0.0974 0.6324 -0.2993 0.0000 
-0.0766 0.0970  0.0755 0.0135 -0.0070 -0.0065 -0.0074 0.0071 0.0172 -0.0085 0.0156  -0.0064 
# 
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}'   ? ? ? ? ? 
# 
_pdbx_phasing_MR.entry_id                     7GUS 
_pdbx_phasing_MR.method_rotation              ? 
_pdbx_phasing_MR.method_translation           ? 
_pdbx_phasing_MR.model_details                'Phaser MODE: MR_AUTO' 
_pdbx_phasing_MR.R_factor                     ? 
_pdbx_phasing_MR.R_rigid_body                 ? 
_pdbx_phasing_MR.correlation_coeff_Fo_to_Fc   ? 
_pdbx_phasing_MR.correlation_coeff_Io_to_Ic   ? 
_pdbx_phasing_MR.d_res_high_rotation          5.560 
_pdbx_phasing_MR.d_res_low_rotation           33.970 
_pdbx_phasing_MR.d_res_high_translation       5.560 
_pdbx_phasing_MR.d_res_low_translation        33.970 
_pdbx_phasing_MR.packing                      ? 
_pdbx_phasing_MR.reflns_percent_rotation      ? 
_pdbx_phasing_MR.reflns_percent_translation   ? 
_pdbx_phasing_MR.sigma_F_rotation             ? 
_pdbx_phasing_MR.sigma_F_translation          ? 
_pdbx_phasing_MR.sigma_I_rotation             ? 
_pdbx_phasing_MR.sigma_I_translation          ? 
# 
_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                    7GUS 
_atom_sites.fract_transf_matrix[1][1]   0.014763 
_atom_sites.fract_transf_matrix[1][2]   0.008523 
_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]   0.017047 
_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]   0.005999 
_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   ? 17.284 -21.256 -4.844 1.00 60.24  ? 6   ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 5   ? 18.214 -22.144 -5.541 1.00 59.08  ? 6   ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 5   ? 17.769 -23.622 -5.453 1.00 58.56  ? 6   ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 5   ? 16.737 -23.933 -4.845 1.00 59.45  ? 6   ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 5   ? 19.644 -21.968 -4.972 1.00 60.00  ? 6   ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 5   ? 20.743 -22.037 -6.022 1.00 73.87  ? 6   ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 5   ? 20.904 -23.113 -6.651 1.00 73.79  ? 6   ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 5   ? 21.451 -21.020 -6.207 1.00 81.55  ? 6   ASP   A OD2 1 
ATOM   9    N  N   . SER   A 1 6   ? 18.544 -24.522 -6.075 1.00 49.60  ? 7   SER   A N   1 
ATOM   10   C  CA  . SER   A 1 6   ? 18.302 -25.961 -6.060 1.00 46.89  ? 7   SER   A CA  1 
ATOM   11   C  C   . SER   A 1 6   ? 19.288 -26.676 -5.088 1.00 42.76  ? 7   SER   A C   1 
ATOM   12   O  O   . SER   A 1 6   ? 19.567 -27.862 -5.260 1.00 41.98  ? 7   SER   A O   1 
ATOM   13   C  CB  . SER   A 1 6   ? 18.416 -26.525 -7.472 1.00 52.50  ? 7   SER   A CB  1 
ATOM   14   O  OG  . SER   A 1 6   ? 19.695 -26.268 -8.029 1.00 63.39  ? 7   SER   A OG  1 
ATOM   15   N  N   . CYS   A 1 7   ? 19.780 -25.965 -4.056 1.00 34.09  ? 8   CYS   A N   1 
ATOM   16   C  CA  . CYS   A 1 7   ? 20.716 -26.538 -3.085 1.00 30.42  ? 8   CYS   A CA  1 
ATOM   17   C  C   . CYS   A 1 7   ? 20.080 -27.689 -2.282 1.00 32.02  ? 8   CYS   A C   1 
ATOM   18   O  O   . CYS   A 1 7   ? 18.862 -27.716 -2.095 1.00 31.87  ? 8   CYS   A O   1 
ATOM   19   C  CB  . CYS   A 1 7   ? 21.226 -25.454 -2.130 1.00 30.73  ? 8   CYS   A CB  1 
ATOM   20   S  SG  . CYS   A 1 7   ? 22.401 -24.274 -2.859 1.00 35.32  ? 8   CYS   A SG  1 
ATOM   21   N  N   . ILE   A 1 8   ? 20.909 -28.612 -1.783 1.00 24.58  ? 9   ILE   A N   1 
ATOM   22   C  CA  . ILE   A 1 8   ? 20.530 -29.597 -0.770 1.00 22.34  ? 9   ILE   A CA  1 
ATOM   23   C  C   . ILE   A 1 8   ? 21.157 -29.062 0.523  1.00 24.38  ? 9   ILE   A C   1 
ATOM   24   O  O   . ILE   A 1 8   ? 22.113 -28.280 0.464  1.00 23.41  ? 9   ILE   A O   1 
ATOM   25   C  CB  . ILE   A 1 8   ? 20.883 -31.080 -1.065 1.00 25.24  ? 9   ILE   A CB  1 
ATOM   26   C  CG1 . ILE   A 1 8   ? 22.404 -31.269 -1.315 1.00 24.51  ? 9   ILE   A CG1 1 
ATOM   27   C  CG2 . ILE   A 1 8   ? 20.063 -31.608 -2.232 1.00 24.59  ? 9   ILE   A CG2 1 
ATOM   28   C  CD1 . ILE   A 1 8   ? 22.900 -32.725 -1.488 1.00 28.86  ? 9   ILE   A CD1 1 
ATOM   29   N  N   A GLN   A 1 9   ? 20.682 -29.495 1.698  0.66 19.88  ? 10  GLN   A N   1 
ATOM   30   N  N   B GLN   A 1 9   ? 20.558 -29.410 1.662  0.34 20.08  ? 10  GLN   A N   1 
ATOM   31   C  CA  A GLN   A 1 9   ? 21.238 -29.016 2.967  0.66 19.18  ? 10  GLN   A CA  1 
ATOM   32   C  CA  B GLN   A 1 9   ? 20.987 -28.927 2.960  0.34 18.98  ? 10  GLN   A CA  1 
ATOM   33   C  C   A GLN   A 1 9   ? 21.591 -30.168 3.900  0.66 22.30  ? 10  GLN   A C   1 
ATOM   34   C  C   B GLN   A 1 9   ? 21.387 -30.068 3.876  0.34 23.12  ? 10  GLN   A C   1 
ATOM   35   O  O   A GLN   A 1 9   ? 20.817 -31.113 4.012  0.66 22.81  ? 10  GLN   A O   1 
ATOM   36   O  O   B GLN   A 1 9   ? 20.696 -31.082 3.939  0.34 23.52  ? 10  GLN   A O   1 
ATOM   37   C  CB  A GLN   A 1 9   ? 20.251 -28.041 3.655  0.66 20.92  ? 10  GLN   A CB  1 
ATOM   38   C  CB  B GLN   A 1 9   ? 19.872 -28.090 3.591  0.34 20.05  ? 10  GLN   A CB  1 
ATOM   39   C  CG  A GLN   A 1 9   ? 20.569 -27.749 5.147  0.66 25.14  ? 10  GLN   A CG  1 
ATOM   40   C  CG  B GLN   A 1 9   ? 20.385 -27.096 4.633  0.34 19.21  ? 10  GLN   A CG  1 
ATOM   41   C  CD  A GLN   A 1 9   ? 20.127 -26.398 5.637  0.66 43.40  ? 10  GLN   A CD  1 
ATOM   42   C  CD  B GLN   A 1 9   ? 19.677 -27.226 5.958  0.34 33.38  ? 10  GLN   A CD  1 
ATOM   43   O  OE1 A GLN   A 1 9   ? 19.703 -25.531 4.867  0.66 35.02  ? 10  GLN   A OE1 1 
ATOM   44   O  OE1 B GLN   A 1 9   ? 18.460 -27.437 6.029  0.34 27.78  ? 10  GLN   A OE1 1 
ATOM   45   N  NE2 A GLN   A 1 9   ? 20.256 -26.173 6.941  0.66 37.88  ? 10  GLN   A NE2 1 
ATOM   46   N  NE2 B GLN   A 1 9   ? 20.427 -27.077 7.041  0.34 27.47  ? 10  GLN   A NE2 1 
ATOM   47   N  N   A PHE   A 1 10  ? 22.735 -30.073 4.592  0.66 19.49  ? 11  PHE   A N   1 
ATOM   48   N  N   B PHE   A 1 10  ? 22.497 -29.890 4.591  0.34 19.97  ? 11  PHE   A N   1 
ATOM   49   C  CA  A PHE   A 1 10  ? 23.112 -31.081 5.580  0.66 18.83  ? 11  PHE   A CA  1 
ATOM   50   C  CA  B PHE   A 1 10  ? 23.023 -30.866 5.540  0.34 19.63  ? 11  PHE   A CA  1 
ATOM   51   C  C   A PHE   A 1 10  ? 22.648 -30.572 6.944  0.66 21.19  ? 11  PHE   A C   1 
ATOM   52   C  C   B PHE   A 1 10  ? 22.543 -30.430 6.906  0.34 22.14  ? 11  PHE   A C   1 
ATOM   53   O  O   A PHE   A 1 10  ? 23.238 -29.625 7.499  0.66 20.20  ? 11  PHE   A O   1 
ATOM   54   O  O   B PHE   A 1 10  ? 22.998 -29.395 7.425  0.34 21.43  ? 11  PHE   A O   1 
ATOM   55   C  CB  A PHE   A 1 10  ? 24.625 -31.387 5.538  0.66 19.69  ? 11  PHE   A CB  1 
ATOM   56   C  CB  B PHE   A 1 10  ? 24.557 -30.940 5.426  0.34 20.98  ? 11  PHE   A CB  1 
ATOM   57   C  CG  A PHE   A 1 10  ? 25.009 -32.589 6.369  0.66 20.07  ? 11  PHE   A CG  1 
ATOM   58   C  CG  B PHE   A 1 10  ? 25.019 -31.734 4.221  0.34 23.17  ? 11  PHE   A CG  1 
ATOM   59   C  CD1 A PHE   A 1 10  ? 24.643 -33.875 5.978  0.66 22.72  ? 11  PHE   A CD1 1 
ATOM   60   C  CD1 B PHE   A 1 10  ? 24.753 -31.291 2.927  0.34 26.70  ? 11  PHE   A CD1 1 
ATOM   61   C  CD2 A PHE   A 1 10  ? 25.761 -32.440 7.529  0.66 21.20  ? 11  PHE   A CD2 1 
ATOM   62   C  CD2 B PHE   A 1 10  ? 25.722 -32.920 4.379  0.34 26.13  ? 11  PHE   A CD2 1 
ATOM   63   C  CE1 A PHE   A 1 10  ? 24.987 -34.986 6.762  0.66 23.74  ? 11  PHE   A CE1 1 
ATOM   64   C  CE1 B PHE   A 1 10  ? 25.179 -32.023 1.816  0.34 27.65  ? 11  PHE   A CE1 1 
ATOM   65   C  CE2 A PHE   A 1 10  ? 26.092 -33.545 8.317  0.66 23.48  ? 11  PHE   A CE2 1 
ATOM   66   C  CE2 B PHE   A 1 10  ? 26.136 -33.661 3.262  0.34 29.55  ? 11  PHE   A CE2 1 
ATOM   67   C  CZ  A PHE   A 1 10  ? 25.715 -34.811 7.926  0.66 21.72  ? 11  PHE   A CZ  1 
ATOM   68   C  CZ  B PHE   A 1 10  ? 25.865 -33.203 1.991  0.34 27.43  ? 11  PHE   A CZ  1 
ATOM   69   N  N   . THR   A 1 11  ? 21.559 -31.175 7.455  1.00 19.00  ? 12  THR   A N   1 
ATOM   70   C  CA  . THR   A 1 11  ? 20.891 -30.809 8.722  1.00 19.35  ? 12  THR   A CA  1 
ATOM   71   C  C   . THR   A 1 11  ? 21.864 -30.559 9.890  1.00 20.67  ? 12  THR   A C   1 
ATOM   72   O  O   . THR   A 1 11  ? 21.741 -29.545 10.591 1.00 20.95  ? 12  THR   A O   1 
ATOM   73   C  CB  . THR   A 1 11  ? 19.826 -31.848 9.085  1.00 25.29  ? 12  THR   A CB  1 
ATOM   74   O  OG1 . THR   A 1 11  ? 18.927 -32.000 7.971  1.00 24.56  ? 12  THR   A OG1 1 
ATOM   75   C  CG2 . THR   A 1 11  ? 19.018 -31.462 10.344 1.00 28.93  ? 12  THR   A CG2 1 
ATOM   76   N  N   . ARG   A 1 12  ? 22.791 -31.491 10.100 1.00 18.50  ? 13  ARG   A N   1 
ATOM   77   C  CA  . ARG   A 1 12  ? 23.717 -31.393 11.246 1.00 18.61  ? 13  ARG   A CA  1 
ATOM   78   C  C   . ARG   A 1 12  ? 24.951 -30.492 11.033 1.00 20.51  ? 13  ARG   A C   1 
ATOM   79   O  O   . ARG   A 1 12  ? 25.787 -30.421 11.947 1.00 18.83  ? 13  ARG   A O   1 
ATOM   80   C  CB  . ARG   A 1 12  ? 24.201 -32.808 11.647 1.00 23.87  ? 13  ARG   A CB  1 
ATOM   81   C  CG  . ARG   A 1 12  ? 23.119 -33.761 12.185 1.00 34.83  ? 13  ARG   A CG  1 
ATOM   82   C  CD  . ARG   A 1 12  ? 22.522 -33.308 13.503 1.00 54.47  ? 13  ARG   A CD  1 
ATOM   83   N  NE  . ARG   A 1 12  ? 23.481 -33.368 14.608 1.00 66.74  ? 13  ARG   A NE  1 
ATOM   84   C  CZ  . ARG   A 1 12  ? 23.297 -32.792 15.792 1.00 78.46  ? 13  ARG   A CZ  1 
ATOM   85   N  NH1 . ARG   A 1 12  ? 24.215 -32.906 16.741 1.00 65.84  ? 13  ARG   A NH1 1 
ATOM   86   N  NH2 . ARG   A 1 12  ? 22.199 -32.083 16.031 1.00 63.57  ? 13  ARG   A NH2 1 
ATOM   87   N  N   . HIS   A 1 13  ? 25.104 -29.846 9.861  1.00 16.97  ? 14  HIS   A N   1 
ATOM   88   C  CA  . HIS   A 1 13  ? 26.345 -29.113 9.573  1.00 16.98  ? 14  HIS   A CA  1 
ATOM   89   C  C   . HIS   A 1 13  ? 26.656 -28.017 10.591 1.00 18.99  ? 14  HIS   A C   1 
ATOM   90   O  O   . HIS   A 1 13  ? 27.796 -27.961 11.097 1.00 18.70  ? 14  HIS   A O   1 
ATOM   91   C  CB  . HIS   A 1 13  ? 26.336 -28.531 8.141  1.00 17.22  ? 14  HIS   A CB  1 
ATOM   92   C  CG  . HIS   A 1 13  ? 27.595 -27.781 7.824  1.00 19.22  ? 14  HIS   A CG  1 
ATOM   93   N  ND1 . HIS   A 1 13  ? 28.781 -28.450 7.592  1.00 19.94  ? 14  HIS   A ND1 1 
ATOM   94   C  CD2 . HIS   A 1 13  ? 27.814 -26.450 7.701  1.00 19.77  ? 14  HIS   A CD2 1 
ATOM   95   C  CE1 . HIS   A 1 13  ? 29.684 -27.517 7.345  1.00 19.66  ? 14  HIS   A CE1 1 
ATOM   96   N  NE2 . HIS   A 1 13  ? 29.148 -26.296 7.388  1.00 19.08  ? 14  HIS   A NE2 1 
ATOM   97   N  N   . ALA   A 1 14  ? 25.666 -27.140 10.874 1.00 16.35  ? 15  ALA   A N   1 
ATOM   98   C  CA  . ALA   A 1 14  ? 25.889 -26.019 11.810 1.00 16.45  ? 15  ALA   A CA  1 
ATOM   99   C  C   . ALA   A 1 14  ? 26.308 -26.520 13.198 1.00 18.78  ? 15  ALA   A C   1 
ATOM   100  O  O   . ALA   A 1 14  ? 27.226 -25.948 13.802 1.00 16.40  ? 15  ALA   A O   1 
ATOM   101  C  CB  . ALA   A 1 14  ? 24.652 -25.120 11.901 1.00 18.02  ? 15  ALA   A CB  1 
ATOM   102  N  N   A SER   A 1 15  ? 25.656 -27.579 13.687 0.42 17.45  ? 16  SER   A N   1 
ATOM   103  N  N   B SER   A 1 15  ? 25.652 -27.585 13.692 0.30 17.26  ? 16  SER   A N   1 
ATOM   104  N  N   C SER   A 1 15  ? 25.653 -27.581 13.703 0.28 16.79  ? 16  SER   A N   1 
ATOM   105  C  CA  A SER   A 1 15  ? 25.949 -28.175 14.990 0.42 17.24  ? 16  SER   A CA  1 
ATOM   106  C  CA  B SER   A 1 15  ? 25.942 -28.189 14.995 0.30 17.22  ? 16  SER   A CA  1 
ATOM   107  C  CA  C SER   A 1 15  ? 25.971 -28.149 15.017 0.28 16.50  ? 16  SER   A CA  1 
ATOM   108  C  C   A SER   A 1 15  ? 27.361 -28.758 15.016 0.42 20.49  ? 16  SER   A C   1 
ATOM   109  C  C   B SER   A 1 15  ? 27.348 -28.783 15.028 0.30 20.89  ? 16  SER   A C   1 
ATOM   110  C  C   C SER   A 1 15  ? 27.359 -28.790 15.040 0.28 20.62  ? 16  SER   A C   1 
ATOM   111  O  O   A SER   A 1 15  ? 28.091 -28.548 15.989 0.42 17.83  ? 16  SER   A O   1 
ATOM   112  O  O   B SER   A 1 15  ? 28.059 -28.613 16.023 0.30 19.07  ? 16  SER   A O   1 
ATOM   113  O  O   C SER   A 1 15  ? 28.072 -28.651 16.037 0.28 18.85  ? 16  SER   A O   1 
ATOM   114  C  CB  A SER   A 1 15  ? 24.910 -29.243 15.327 0.42 20.16  ? 16  SER   A CB  1 
ATOM   115  C  CB  B SER   A 1 15  ? 24.908 -29.261 15.332 0.30 20.49  ? 16  SER   A CB  1 
ATOM   116  C  CB  C SER   A 1 15  ? 24.894 -29.131 15.470 0.28 18.93  ? 16  SER   A CB  1 
ATOM   117  O  OG  A SER   A 1 15  ? 25.116 -29.800 16.614 0.42 21.11  ? 16  SER   A OG  1 
ATOM   118  O  OG  B SER   A 1 15  ? 23.598 -28.723 15.407 0.30 23.62  ? 16  SER   A OG  1 
ATOM   119  O  OG  C SER   A 1 15  ? 24.818 -30.269 14.627 0.28 19.36  ? 16  SER   A OG  1 
ATOM   120  N  N   . ASP   A 1 16  ? 27.754 -29.464 13.936 1.00 18.32  ? 17  ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 16  ? 29.080 -30.084 13.822 1.00 18.82  ? 17  ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 16  ? 30.153 -28.986 13.783 1.00 19.37  ? 17  ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 16  ? 31.213 -29.142 14.380 1.00 18.90  ? 17  ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 16  ? 29.150 -30.954 12.569 1.00 20.72  ? 17  ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 16  ? 28.362 -32.259 12.666 1.00 25.94  ? 17  ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 16  ? 27.845 -32.569 13.768 1.00 24.05  ? 17  ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 16  ? 28.250 -32.953 11.644 1.00 27.56  ? 17  ASP   A OD2 1 
ATOM   128  N  N   . VAL   A 1 17  ? 29.869 -27.872 13.078 1.00 16.02  ? 18  VAL   A N   1 
ATOM   129  C  CA  . VAL   A 1 17  ? 30.802 -26.742 13.029 1.00 15.59  ? 18  VAL   A CA  1 
ATOM   130  C  C   . VAL   A 1 17  ? 31.013 -26.203 14.449 1.00 19.29  ? 18  VAL   A C   1 
ATOM   131  O  O   . VAL   A 1 17  ? 32.150 -26.038 14.886 1.00 17.53  ? 18  VAL   A O   1 
ATOM   132  C  CB  . VAL   A 1 17  ? 30.300 -25.633 12.056 1.00 17.16  ? 18  VAL   A CB  1 
ATOM   133  C  CG1 . VAL   A 1 17  ? 31.042 -24.308 12.280 1.00 17.20  ? 18  VAL   A CG1 1 
ATOM   134  C  CG2 . VAL   A 1 17  ? 30.401 -26.085 10.592 1.00 16.95  ? 18  VAL   A CG2 1 
ATOM   135  N  N   . LEU   A 1 18  ? 29.921 -25.981 15.178 1.00 16.24  ? 19  LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 18  ? 30.034 -25.416 16.524 1.00 16.39  ? 19  LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 18  ? 30.786 -26.368 17.469 1.00 17.70  ? 19  LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 18  ? 31.627 -25.913 18.269 1.00 16.90  ? 19  LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 18  ? 28.655 -25.037 17.075 1.00 16.48  ? 19  LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 18  ? 28.703 -24.100 18.318 1.00 18.83  ? 19  LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 18  ? 29.284 -22.705 17.961 1.00 19.28  ? 19  LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 18  ? 27.322 -23.932 18.906 1.00 23.88  ? 19  LEU   A CD2 1 
ATOM   143  N  N   . LEU   A 1 19  ? 30.504 -27.672 17.353 1.00 16.40  ? 20  LEU   A N   1 
ATOM   144  C  CA  . LEU   A 1 19  ? 31.181 -28.694 18.155 1.00 17.19  ? 20  LEU   A CA  1 
ATOM   145  C  C   . LEU   A 1 19  ? 32.699 -28.600 17.903 1.00 19.65  ? 20  LEU   A C   1 
ATOM   146  O  O   . LEU   A 1 19  ? 33.485 -28.584 18.867 1.00 18.99  ? 20  LEU   A O   1 
ATOM   147  C  CB  . LEU   A 1 19  ? 30.648 -30.084 17.776 1.00 18.86  ? 20  LEU   A CB  1 
ATOM   148  C  CG  . LEU   A 1 19  ? 31.248 -31.263 18.523 1.00 26.67  ? 20  LEU   A CG  1 
ATOM   149  C  CD1 . LEU   A 1 19  ? 30.865 -31.203 20.008 1.00 29.21  ? 20  LEU   A CD1 1 
ATOM   150  C  CD2 . LEU   A 1 19  ? 30.727 -32.575 17.926 1.00 30.55  ? 20  LEU   A CD2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 33.108 -28.471 16.618 1.00 17.56  ? 21  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 34.531 -28.353 16.280 1.00 16.83  ? 21  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 35.155 -27.060 16.800 1.00 18.66  ? 21  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 36.288 -27.066 17.263 1.00 18.70  ? 21  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 34.745 -28.542 14.799 1.00 19.13  ? 21  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.703 -30.015 14.420 1.00 25.73  ? 21  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.974 -30.910 15.244 1.00 22.94  ? 21  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.368 -30.309 13.165 1.00 20.04  ? 21  ASN   A ND2 1 
ATOM   159  N  N   . LEU   A 1 21  ? 34.407 -25.948 16.728 1.00 16.07  ? 22  LEU   A N   1 
ATOM   160  C  CA  . LEU   A 1 21  ? 34.870 -24.666 17.278 1.00 16.11  ? 22  LEU   A CA  1 
ATOM   161  C  C   . LEU   A 1 21  ? 35.076 -24.818 18.789 1.00 19.00  ? 22  LEU   A C   1 
ATOM   162  O  O   . LEU   A 1 21  ? 36.062 -24.301 19.326 1.00 18.61  ? 22  LEU   A O   1 
ATOM   163  C  CB  . LEU   A 1 21  ? 33.883 -23.521 16.965 1.00 16.37  ? 22  LEU   A CB  1 
ATOM   164  C  CG  . LEU   A 1 21  ? 33.783 -23.138 15.469 1.00 19.68  ? 22  LEU   A CG  1 
ATOM   165  C  CD1 . LEU   A 1 21  ? 32.644 -22.140 15.229 1.00 19.93  ? 22  LEU   A CD1 1 
ATOM   166  C  CD2 . LEU   A 1 21  ? 35.118 -22.592 14.917 1.00 19.96  ? 22  LEU   A CD2 1 
ATOM   167  N  N   . ASN   A 1 22  ? 34.154 -25.538 19.483 1.00 17.42  ? 23  ASN   A N   1 
ATOM   168  C  CA  . ASN   A 1 22  ? 34.330 -25.758 20.925 1.00 17.98  ? 23  ASN   A CA  1 
ATOM   169  C  C   . ASN   A 1 22  ? 35.564 -26.634 21.224 1.00 21.46  ? 23  ASN   A C   1 
ATOM   170  O  O   . ASN   A 1 22  ? 36.259 -26.387 22.209 1.00 22.22  ? 23  ASN   A O   1 
ATOM   171  C  CB  . ASN   A 1 22  ? 33.085 -26.364 21.554 1.00 18.29  ? 23  ASN   A CB  1 
ATOM   172  C  CG  . ASN   A 1 22  ? 33.107 -26.215 23.063 1.00 26.78  ? 23  ASN   A CG  1 
ATOM   173  O  OD1 . ASN   A 1 22  ? 33.639 -25.244 23.619 1.00 23.49  ? 23  ASN   A OD1 1 
ATOM   174  N  ND2 . ASN   A 1 22  ? 32.528 -27.174 23.747 1.00 26.35  ? 23  ASN   A ND2 1 
ATOM   175  N  N   . ARG   A 1 23  ? 35.856 -27.634 20.355 1.00 19.38  ? 24  ARG   A N   1 
ATOM   176  C  CA  . ARG   A 1 23  ? 37.050 -28.485 20.494 1.00 20.43  ? 24  ARG   A CA  1 
ATOM   177  C  C   . ARG   A 1 23  ? 38.301 -27.627 20.357 1.00 23.44  ? 24  ARG   A C   1 
ATOM   178  O  O   . ARG   A 1 23  ? 39.254 -27.813 21.113 1.00 23.23  ? 24  ARG   A O   1 
ATOM   179  C  CB  . ARG   A 1 23  ? 37.056 -29.589 19.437 1.00 20.15  ? 24  ARG   A CB  1 
ATOM   180  C  CG  . ARG   A 1 23  ? 36.034 -30.668 19.752 1.00 21.73  ? 24  ARG   A CG  1 
ATOM   181  C  CD  . ARG   A 1 23  ? 35.812 -31.582 18.554 1.00 27.10  ? 24  ARG   A CD  1 
ATOM   182  N  NE  . ARG   A 1 23  ? 35.005 -32.740 18.931 1.00 32.29  ? 24  ARG   A NE  1 
ATOM   183  C  CZ  . ARG   A 1 23  ? 34.346 -33.517 18.077 1.00 44.70  ? 24  ARG   A CZ  1 
ATOM   184  N  NH1 . ARG   A 1 23  ? 34.349 -33.241 16.777 1.00 32.42  ? 24  ARG   A NH1 1 
ATOM   185  N  NH2 . ARG   A 1 23  ? 33.663 -34.561 18.517 1.00 37.35  ? 24  ARG   A NH2 1 
ATOM   186  N  N   . LEU   A 1 24  ? 38.292 -26.657 19.414 1.00 19.88  ? 25  LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 24  ? 39.425 -25.748 19.267 1.00 19.80  ? 25  LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 24  ? 39.572 -24.893 20.528 1.00 22.94  ? 25  LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 24  ? 40.693 -24.723 21.020 1.00 23.64  ? 25  LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 24  ? 39.241 -24.830 18.067 1.00 19.50  ? 25  LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 24  ? 39.277 -25.499 16.695 1.00 23.23  ? 25  LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 24  ? 39.172 -24.448 15.599 1.00 23.41  ? 25  LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 24  ? 40.568 -26.344 16.521 1.00 23.87  ? 25  LEU   A CD2 1 
ATOM   194  N  N   . ARG   A 1 25  ? 38.440 -24.390 21.069 1.00 19.28  ? 26  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 25  ? 38.492 -23.613 22.313 1.00 19.94  ? 26  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 25  ? 39.126 -24.450 23.473 1.00 25.19  ? 26  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 25  ? 40.018 -23.937 24.183 1.00 25.41  ? 26  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 25  ? 37.091 -23.124 22.717 1.00 20.13  ? 26  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 25  ? 37.209 -22.205 23.944 1.00 24.71  ? 26  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 25  ? 35.902 -21.600 24.346 1.00 26.36  ? 26  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 25  ? 34.900 -22.595 24.707 1.00 24.98  ? 26  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 25  ? 34.260 -22.633 25.872 1.00 34.14  ? 26  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 25  ? 34.586 -21.790 26.848 1.00 30.61  ? 26  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 25  ? 33.319 -23.536 26.085 1.00 25.42  ? 26  ARG   A NH2 1 
ATOM   205  N  N   A SER   A 1 26  ? 38.658 -25.696 23.664 0.39 23.08  ? 27  SER   A N   1 
ATOM   206  N  N   B SER   A 1 26  ? 38.663 -25.708 23.645 0.28 23.02  ? 27  SER   A N   1 
ATOM   207  N  N   C SER   A 1 26  ? 38.659 -25.699 23.661 0.33 23.05  ? 27  SER   A N   1 
ATOM   208  C  CA  A SER   A 1 26  ? 39.140 -26.594 24.722 0.39 24.07  ? 27  SER   A CA  1 
ATOM   209  C  CA  B SER   A 1 26  ? 39.126 -26.660 24.667 0.28 24.11  ? 27  SER   A CA  1 
ATOM   210  C  CA  C SER   A 1 26  ? 39.136 -26.616 24.707 0.33 24.10  ? 27  SER   A CA  1 
ATOM   211  C  C   A SER   A 1 26  ? 40.655 -26.839 24.649 0.39 29.53  ? 27  SER   A C   1 
ATOM   212  C  C   B SER   A 1 26  ? 40.641 -26.845 24.636 0.28 29.49  ? 27  SER   A C   1 
ATOM   213  C  C   C SER   A 1 26  ? 40.652 -26.845 24.643 0.33 29.52  ? 27  SER   A C   1 
ATOM   214  O  O   A SER   A 1 26  ? 41.308 -26.927 25.692 0.39 30.29  ? 27  SER   A O   1 
ATOM   215  O  O   B SER   A 1 26  ? 41.275 -26.922 25.691 0.28 30.22  ? 27  SER   A O   1 
ATOM   216  O  O   C SER   A 1 26  ? 41.298 -26.940 25.689 0.33 30.28  ? 27  SER   A O   1 
ATOM   217  C  CB  A SER   A 1 26  ? 38.372 -27.912 24.707 0.39 26.95  ? 27  SER   A CB  1 
ATOM   218  C  CB  B SER   A 1 26  ? 38.466 -28.021 24.463 0.28 27.46  ? 27  SER   A CB  1 
ATOM   219  C  CB  C SER   A 1 26  ? 38.397 -27.950 24.629 0.33 27.21  ? 27  SER   A CB  1 
ATOM   220  O  OG  A SER   A 1 26  ? 38.755 -28.749 23.629 0.39 31.53  ? 27  SER   A OG  1 
ATOM   221  O  OG  B SER   A 1 26  ? 37.092 -28.017 24.803 0.28 33.71  ? 27  SER   A OG  1 
ATOM   222  O  OG  C SER   A 1 26  ? 38.875 -28.869 25.598 0.33 34.17  ? 27  SER   A OG  1 
ATOM   223  N  N   . ARG   A 1 27  ? 41.212 -26.916 23.422 1.00 26.04  ? 28  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 27  ? 42.649 -27.140 23.198 1.00 27.26  ? 28  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 27  ? 43.442 -25.845 23.005 1.00 28.69  ? 28  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 27  ? 44.652 -25.892 22.732 1.00 28.94  ? 28  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 27  ? 42.835 -28.108 22.021 1.00 29.07  ? 28  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 27  ? 42.104 -29.434 22.219 1.00 35.76  ? 28  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 27  ? 42.056 -30.252 20.950 1.00 38.66  ? 28  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 27  ? 43.401 -30.646 20.530 1.00 50.36  ? 28  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 27  ? 43.752 -30.866 19.270 1.00 63.91  ? 28  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 27  ? 45.000 -31.201 18.971 1.00 54.13  ? 28  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 27  ? 42.867 -30.727 18.295 1.00 47.83  ? 28  ARG   A NH2 1 
ATOM   234  N  N   . ASP   A 1 28  ? 42.762 -24.690 23.167 1.00 22.94  ? 29  ASP   A N   1 
ATOM   235  C  CA  . ASP   A 1 28  ? 43.329 -23.350 23.024 1.00 23.55  ? 29  ASP   A CA  1 
ATOM   236  C  C   . ASP   A 1 28  ? 43.944 -23.142 21.620 1.00 26.95  ? 29  ASP   A C   1 
ATOM   237  O  O   . ASP   A 1 28  ? 45.005 -22.533 21.473 1.00 27.99  ? 29  ASP   A O   1 
ATOM   238  C  CB  . ASP   A 1 28  ? 44.335 -23.047 24.169 1.00 26.53  ? 29  ASP   A CB  1 
ATOM   239  C  CG  . ASP   A 1 28  ? 44.654 -21.574 24.315 1.00 33.05  ? 29  ASP   A CG  1 
ATOM   240  O  OD1 . ASP   A 1 28  ? 43.743 -20.743 24.095 1.00 32.06  ? 29  ASP   A OD1 1 
ATOM   241  O  OD2 . ASP   A 1 28  ? 45.808 -21.251 24.649 1.00 35.53  ? 29  ASP   A OD2 1 
ATOM   242  N  N   . ILE   A 1 29  ? 43.273 -23.670 20.588 1.00 22.46  ? 30  ILE   A N   1 
ATOM   243  C  CA  . ILE   A 1 29  ? 43.782 -23.581 19.218 1.00 22.62  ? 30  ILE   A CA  1 
ATOM   244  C  C   . ILE   A 1 29  ? 43.185 -22.386 18.497 1.00 25.23  ? 30  ILE   A C   1 
ATOM   245  O  O   . ILE   A 1 29  ? 41.957 -22.262 18.398 1.00 22.29  ? 30  ILE   A O   1 
ATOM   246  C  CB  . ILE   A 1 29  ? 43.568 -24.893 18.420 1.00 25.25  ? 30  ILE   A CB  1 
ATOM   247  C  CG1 . ILE   A 1 29  ? 44.348 -26.077 19.066 1.00 26.69  ? 30  ILE   A CG1 1 
ATOM   248  C  CG2 . ILE   A 1 29  ? 43.952 -24.697 16.920 1.00 24.67  ? 30  ILE   A CG2 1 
ATOM   249  C  CD1 . ILE   A 1 29  ? 43.929 -27.452 18.548 1.00 30.58  ? 30  ILE   A CD1 1 
ATOM   250  N  N   . LEU   A 1 30  ? 44.075 -21.495 18.007 1.00 23.89  ? 31  LEU   A N   1 
ATOM   251  C  CA  . LEU   A 1 30  ? 43.713 -20.305 17.234 1.00 23.79  ? 31  LEU   A CA  1 
ATOM   252  C  C   . LEU   A 1 30  ? 42.808 -19.306 17.981 1.00 24.55  ? 31  LEU   A C   1 
ATOM   253  O  O   . LEU   A 1 30  ? 42.236 -18.418 17.356 1.00 22.75  ? 31  LEU   A O   1 
ATOM   254  C  CB  . LEU   A 1 30  ? 43.136 -20.650 15.857 1.00 24.22  ? 31  LEU   A CB  1 
ATOM   255  C  CG  . LEU   A 1 30  ? 44.190 -21.183 14.837 1.00 31.51  ? 31  LEU   A CG  1 
ATOM   256  C  CD1 . LEU   A 1 30  ? 43.615 -21.232 13.482 1.00 31.57  ? 31  LEU   A CD1 1 
ATOM   257  C  CD2 . LEU   A 1 30  ? 45.414 -20.308 14.779 1.00 37.85  ? 31  LEU   A CD2 1 
ATOM   258  N  N   . THR   A 1 31  ? 42.761 -19.395 19.315 1.00 21.37  ? 32  THR   A N   1 
ATOM   259  C  CA  . THR   A 1 31  ? 42.106 -18.384 20.145 1.00 20.44  ? 32  THR   A CA  1 
ATOM   260  C  C   . THR   A 1 31  ? 42.941 -17.093 19.938 1.00 26.43  ? 32  THR   A C   1 
ATOM   261  O  O   . THR   A 1 31  ? 44.170 -17.156 19.795 1.00 26.35  ? 32  THR   A O   1 
ATOM   262  C  CB  . THR   A 1 31  ? 42.044 -18.829 21.600 1.00 25.27  ? 32  THR   A CB  1 
ATOM   263  O  OG1 . THR   A 1 31  ? 43.369 -19.155 22.017 1.00 28.23  ? 32  THR   A OG1 1 
ATOM   264  C  CG2 . THR   A 1 31  ? 41.084 -20.043 21.805 1.00 22.73  ? 32  THR   A CG2 1 
ATOM   265  N  N   . ASP   A 1 32  ? 42.273 -15.950 19.830 1.00 22.67  ? 33  ASP   A N   1 
ATOM   266  C  CA  . ASP   A 1 32  ? 42.913 -14.688 19.469 1.00 23.25  ? 33  ASP   A CA  1 
ATOM   267  C  C   . ASP   A 1 32  ? 42.568 -13.530 20.365 1.00 25.10  ? 33  ASP   A C   1 
ATOM   268  O  O   . ASP   A 1 32  ? 42.882 -12.379 20.040 1.00 25.38  ? 33  ASP   A O   1 
ATOM   269  C  CB  . ASP   A 1 32  ? 42.569 -14.358 18.005 1.00 24.24  ? 33  ASP   A CB  1 
ATOM   270  C  CG  . ASP   A 1 32  ? 41.083 -14.396 17.672 1.00 29.06  ? 33  ASP   A CG  1 
ATOM   271  O  OD1 . ASP   A 1 32  ? 40.253 -14.454 18.618 1.00 23.23  ? 33  ASP   A OD1 1 
ATOM   272  O  OD2 . ASP   A 1 32  ? 40.750 -14.400 16.480 1.00 34.06  ? 33  ASP   A OD2 1 
ATOM   273  N  N   . VAL   A 1 33  ? 41.910 -13.812 21.492 1.00 20.41  ? 34  VAL   A N   1 
ATOM   274  C  CA  . VAL   A 1 33  ? 41.596 -12.761 22.460 1.00 20.41  ? 34  VAL   A CA  1 
ATOM   275  C  C   . VAL   A 1 33  ? 41.438 -13.357 23.852 1.00 23.95  ? 34  VAL   A C   1 
ATOM   276  O  O   . VAL   A 1 33  ? 41.050 -14.529 23.988 1.00 22.74  ? 34  VAL   A O   1 
ATOM   277  C  CB  . VAL   A 1 33  ? 40.331 -11.927 22.023 1.00 23.19  ? 34  VAL   A CB  1 
ATOM   278  C  CG1 . VAL   A 1 33  ? 39.023 -12.717 22.177 1.00 21.83  ? 34  VAL   A CG1 1 
ATOM   279  C  CG2 . VAL   A 1 33  ? 40.241 -10.575 22.756 1.00 23.50  ? 34  VAL   A CG2 1 
ATOM   280  N  N   A VAL   A 1 34  ? 41.733 -12.541 24.879 0.60 20.90  ? 35  VAL   A N   1 
ATOM   281  N  N   B VAL   A 1 34  ? 41.733 -12.558 24.883 0.40 20.75  ? 35  VAL   A N   1 
ATOM   282  C  CA  A VAL   A 1 34  ? 41.512 -12.870 26.282 0.60 20.98  ? 35  VAL   A CA  1 
ATOM   283  C  CA  B VAL   A 1 34  ? 41.474 -12.941 26.260 0.40 20.65  ? 35  VAL   A CA  1 
ATOM   284  C  C   A VAL   A 1 34  ? 40.445 -11.885 26.764 0.60 23.98  ? 35  VAL   A C   1 
ATOM   285  C  C   B VAL   A 1 34  ? 40.497 -11.911 26.848 0.40 24.15  ? 35  VAL   A C   1 
ATOM   286  O  O   A VAL   A 1 34  ? 40.589 -10.674 26.547 0.60 23.76  ? 35  VAL   A O   1 
ATOM   287  O  O   B VAL   A 1 34  ? 40.714 -10.702 26.716 0.40 24.26  ? 35  VAL   A O   1 
ATOM   288  C  CB  A VAL   A 1 34  ? 42.800 -12.759 27.148 0.60 25.87  ? 35  VAL   A CB  1 
ATOM   289  C  CB  B VAL   A 1 34  ? 42.728 -13.246 27.131 0.40 25.38  ? 35  VAL   A CB  1 
ATOM   290  C  CG1 A VAL   A 1 34  ? 42.530 -13.121 28.612 0.60 26.21  ? 35  VAL   A CG1 1 
ATOM   291  C  CG1 B VAL   A 1 34  ? 43.590 -12.010 27.362 0.40 25.93  ? 35  VAL   A CG1 1 
ATOM   292  C  CG2 A VAL   A 1 34  ? 43.914 -13.624 26.587 0.60 26.22  ? 35  VAL   A CG2 1 
ATOM   293  C  CG2 B VAL   A 1 34  ? 42.337 -13.893 28.457 0.40 25.51  ? 35  VAL   A CG2 1 
ATOM   294  N  N   . ILE   A 1 35  ? 39.379 -12.402 27.395 1.00 19.92  ? 36  ILE   A N   1 
ATOM   295  C  CA  . ILE   A 1 35  ? 38.323 -11.586 28.001 1.00 20.59  ? 36  ILE   A CA  1 
ATOM   296  C  C   . ILE   A 1 35  ? 38.606 -11.619 29.490 1.00 25.17  ? 36  ILE   A C   1 
ATOM   297  O  O   . ILE   A 1 35  ? 38.588 -12.704 30.102 1.00 24.04  ? 36  ILE   A O   1 
ATOM   298  C  CB  . ILE   A 1 35  ? 36.883 -12.082 27.683 1.00 22.14  ? 36  ILE   A CB  1 
ATOM   299  C  CG1 . ILE   A 1 35  ? 36.627 -12.249 26.153 1.00 21.44  ? 36  ILE   A CG1 1 
ATOM   300  C  CG2 . ILE   A 1 35  ? 35.832 -11.173 28.342 1.00 22.72  ? 36  ILE   A CG2 1 
ATOM   301  C  CD1 . ILE   A 1 35  ? 36.935 -10.973 25.267 1.00 21.41  ? 36  ILE   A CD1 1 
ATOM   302  N  N   . VAL   A 1 36  ? 38.850 -10.436 30.065 1.00 22.55  ? 37  VAL   A N   1 
ATOM   303  C  CA  . VAL   A 1 36  ? 39.156 -10.294 31.487 1.00 23.16  ? 37  VAL   A CA  1 
ATOM   304  C  C   . VAL   A 1 36  ? 37.905 -9.882  32.236 1.00 27.30  ? 37  VAL   A C   1 
ATOM   305  O  O   . VAL   A 1 36  ? 37.291 -8.864  31.906 1.00 26.55  ? 37  VAL   A O   1 
ATOM   306  C  CB  . VAL   A 1 36  ? 40.346 -9.324  31.745 1.00 27.76  ? 37  VAL   A CB  1 
ATOM   307  C  CG1 . VAL   A 1 36  ? 40.650 -9.202  33.243 1.00 28.54  ? 37  VAL   A CG1 1 
ATOM   308  C  CG2 . VAL   A 1 36  ? 41.602 -9.769  30.991 1.00 28.67  ? 37  VAL   A CG2 1 
ATOM   309  N  N   . VAL   A 1 37  ? 37.520 -10.686 33.246 1.00 24.38  ? 38  VAL   A N   1 
ATOM   310  C  CA  . VAL   A 1 37  ? 36.326 -10.449 34.051 1.00 24.50  ? 38  VAL   A CA  1 
ATOM   311  C  C   . VAL   A 1 37  ? 36.825 -10.462 35.479 1.00 31.41  ? 38  VAL   A C   1 
ATOM   312  O  O   . VAL   A 1 37  ? 36.974 -11.534 36.077 1.00 28.43  ? 38  VAL   A O   1 
ATOM   313  C  CB  . VAL   A 1 37  ? 35.212 -11.498 33.770 1.00 27.36  ? 38  VAL   A CB  1 
ATOM   314  C  CG1 . VAL   A 1 37  ? 33.892 -11.067 34.397 1.00 27.85  ? 38  VAL   A CG1 1 
ATOM   315  C  CG2 . VAL   A 1 37  ? 35.033 -11.727 32.264 1.00 26.17  ? 38  VAL   A CG2 1 
ATOM   316  N  N   A SER   A 1 38  ? 37.237 -9.278  35.973 0.54 31.53  ? 39  SER   A N   1 
ATOM   317  N  N   B SER   A 1 38  ? 37.040 -9.250  36.028 0.46 31.14  ? 39  SER   A N   1 
ATOM   318  C  CA  A SER   A 1 38  ? 37.845 -9.088  37.293 0.54 32.97  ? 39  SER   A CA  1 
ATOM   319  C  CA  B SER   A 1 38  ? 37.561 -8.990  37.370 0.46 32.61  ? 39  SER   A CA  1 
ATOM   320  C  C   A SER   A 1 38  ? 39.165 -9.898  37.387 0.54 34.28  ? 39  SER   A C   1 
ATOM   321  C  C   B SER   A 1 38  ? 38.676 -9.981  37.734 0.46 35.09  ? 39  SER   A C   1 
ATOM   322  O  O   A SER   A 1 38  ? 40.059 -9.657  36.579 0.54 33.69  ? 39  SER   A O   1 
ATOM   323  O  O   B SER   A 1 38  ? 38.508 -10.863 38.580 0.46 34.78  ? 39  SER   A O   1 
ATOM   324  C  CB  A SER   A 1 38  ? 36.859 -9.427  38.413 0.54 38.88  ? 39  SER   A CB  1 
ATOM   325  C  CB  B SER   A 1 38  ? 36.436 -8.931  38.397 0.46 37.66  ? 39  SER   A CB  1 
ATOM   326  O  OG  A SER   A 1 38  ? 35.654 -8.691  38.282 0.54 53.52  ? 39  SER   A OG  1 
ATOM   327  O  OG  B SER   A 1 38  ? 35.739 -7.702  38.270 0.46 46.83  ? 39  SER   A OG  1 
ATOM   328  N  N   A ARG   A 1 39  ? 39.268 -10.869 38.323 0.54 30.03  ? 40  ARG   A N   1 
ATOM   329  N  N   B ARG   A 1 39  ? 39.779 -9.878  36.973 0.46 29.73  ? 40  ARG   A N   1 
ATOM   330  C  CA  A ARG   A 1 39  ? 40.473 -11.687 38.518 0.54 30.17  ? 40  ARG   A CA  1 
ATOM   331  C  CA  B ARG   A 1 39  ? 41.027 -10.647 37.041 0.46 30.02  ? 40  ARG   A CA  1 
ATOM   332  C  C   A ARG   A 1 39  ? 40.572 -12.873 37.553 0.54 32.23  ? 40  ARG   A C   1 
ATOM   333  C  C   B ARG   A 1 39  ? 40.907 -12.082 36.489 0.46 32.38  ? 40  ARG   A C   1 
ATOM   334  O  O   A ARG   A 1 39  ? 41.610 -13.543 37.522 0.54 32.09  ? 40  ARG   A O   1 
ATOM   335  O  O   B ARG   A 1 39  ? 41.936 -12.629 36.087 0.46 33.08  ? 40  ARG   A O   1 
ATOM   336  C  CB  A ARG   A 1 39  ? 40.586 -12.171 39.979 0.54 30.81  ? 40  ARG   A CB  1 
ATOM   337  C  CB  B ARG   A 1 39  ? 41.680 -10.628 38.438 0.46 30.96  ? 40  ARG   A CB  1 
ATOM   338  C  CG  A ARG   A 1 39  ? 41.029 -11.094 40.959 0.54 35.17  ? 40  ARG   A CG  1 
ATOM   339  C  CG  B ARG   A 1 39  ? 42.218 -9.248  38.809 0.46 42.39  ? 40  ARG   A CG  1 
ATOM   340  C  CD  A ARG   A 1 39  ? 41.407 -11.706 42.293 0.54 37.92  ? 40  ARG   A CD  1 
ATOM   341  C  CD  B ARG   A 1 39  ? 43.229 -9.299  39.934 0.46 49.22  ? 40  ARG   A CD  1 
ATOM   342  N  NE  A ARG   A 1 39  ? 41.576 -10.696 43.336 0.54 39.42  ? 40  ARG   A NE  1 
ATOM   343  N  NE  B ARG   A 1 39  ? 43.643 -7.960  40.360 0.46 55.04  ? 40  ARG   A NE  1 
ATOM   344  C  CZ  A ARG   A 1 39  ? 42.740 -10.171 43.707 0.54 54.56  ? 40  ARG   A CZ  1 
ATOM   345  C  CZ  B ARG   A 1 39  ? 43.028 -7.244  41.297 0.46 64.55  ? 40  ARG   A CZ  1 
ATOM   346  N  NH1 A ARG   A 1 39  ? 42.787 -9.268  44.674 0.54 45.33  ? 40  ARG   A NH1 1 
ATOM   347  N  NH1 B ARG   A 1 39  ? 41.953 -7.722  41.911 0.46 46.80  ? 40  ARG   A NH1 1 
ATOM   348  N  NH2 A ARG   A 1 39  ? 43.867 -10.541 43.109 0.54 41.19  ? 40  ARG   A NH2 1 
ATOM   349  N  NH2 B ARG   A 1 39  ? 43.479 -6.039  41.621 0.46 51.90  ? 40  ARG   A NH2 1 
ATOM   350  N  N   A GLU   A 1 40  ? 39.497 -13.142 36.779 0.54 26.85  ? 41  GLU   A N   1 
ATOM   351  N  N   B GLU   A 1 40  ? 39.677 -12.665 36.402 0.46 27.81  ? 41  GLU   A N   1 
ATOM   352  C  CA  A GLU   A 1 40  ? 39.463 -14.271 35.848 0.54 25.98  ? 41  GLU   A CA  1 
ATOM   353  C  CA  B GLU   A 1 40  ? 39.461 -13.999 35.805 0.46 27.13  ? 41  GLU   A CA  1 
ATOM   354  C  C   A GLU   A 1 40  ? 39.718 -13.861 34.402 0.54 29.59  ? 41  GLU   A C   1 
ATOM   355  C  C   B GLU   A 1 40  ? 39.610 -13.854 34.288 0.46 30.06  ? 41  GLU   A C   1 
ATOM   356  O  O   A GLU   A 1 40  ? 39.345 -12.764 33.985 0.54 28.09  ? 41  GLU   A O   1 
ATOM   357  O  O   B GLU   A 1 40  ? 39.071 -12.907 33.715 0.46 28.35  ? 41  GLU   A O   1 
ATOM   358  C  CB  A GLU   A 1 40  ? 38.137 -15.053 35.965 0.54 26.93  ? 41  GLU   A CB  1 
ATOM   359  C  CB  B GLU   A 1 40  ? 38.077 -14.572 36.168 0.46 28.36  ? 41  GLU   A CB  1 
ATOM   360  C  CG  A GLU   A 1 40  ? 37.860 -15.586 37.365 0.54 40.93  ? 41  GLU   A CG  1 
ATOM   361  C  CG  B GLU   A 1 40  ? 37.996 -15.131 37.579 0.46 40.39  ? 41  GLU   A CG  1 
ATOM   362  C  CD  A GLU   A 1 40  ? 38.152 -17.061 37.551 0.54 75.92  ? 41  GLU   A CD  1 
ATOM   363  C  CD  B GLU   A 1 40  ? 38.174 -16.633 37.663 0.46 72.10  ? 41  GLU   A CD  1 
ATOM   364  O  OE1 A GLU   A 1 40  ? 37.362 -17.894 37.049 0.54 75.56  ? 41  GLU   A OE1 1 
ATOM   365  O  OE1 B GLU   A 1 40  ? 39.226 -17.077 38.176 0.46 73.46  ? 41  GLU   A OE1 1 
ATOM   366  O  OE2 A GLU   A 1 40  ? 39.169 -17.385 38.207 0.54 77.16  ? 41  GLU   A OE2 1 
ATOM   367  O  OE2 B GLU   A 1 40  ? 37.265 -17.368 37.212 0.46 70.61  ? 41  GLU   A OE2 1 
ATOM   368  N  N   . GLN   A 1 41  ? 40.343 -14.774 33.639 1.00 26.19  ? 42  GLN   A N   1 
ATOM   369  C  CA  . GLN   A 1 41  ? 40.656 -14.648 32.219 1.00 25.01  ? 42  GLN   A CA  1 
ATOM   370  C  C   . GLN   A 1 41  ? 40.024 -15.766 31.429 1.00 26.28  ? 42  GLN   A C   1 
ATOM   371  O  O   . GLN   A 1 41  ? 40.096 -16.918 31.859 1.00 26.14  ? 42  GLN   A O   1 
ATOM   372  C  CB  . GLN   A 1 41  ? 42.177 -14.696 32.020 1.00 27.84  ? 42  GLN   A CB  1 
ATOM   373  C  CG  . GLN   A 1 41  ? 42.904 -13.502 32.629 1.00 41.19  ? 42  GLN   A CG  1 
ATOM   374  C  CD  . GLN   A 1 41  ? 44.347 -13.364 32.198 1.00 59.24  ? 42  GLN   A CD  1 
ATOM   375  O  OE1 . GLN   A 1 41  ? 44.908 -14.187 31.458 1.00 52.05  ? 42  GLN   A OE1 1 
ATOM   376  N  NE2 . GLN   A 1 41  ? 44.983 -12.307 32.666 1.00 60.62  ? 42  GLN   A NE2 1 
ATOM   377  N  N   . PHE   A 1 42  ? 39.454 -15.442 30.254 1.00 21.08  ? 43  PHE   A N   1 
ATOM   378  C  CA  . PHE   A 1 42  ? 38.805 -16.439 29.375 1.00 21.08  ? 43  PHE   A CA  1 
ATOM   379  C  C   . PHE   A 1 42  ? 39.320 -16.263 27.968 1.00 25.62  ? 43  PHE   A C   1 
ATOM   380  O  O   . PHE   A 1 42  ? 39.159 -15.178 27.395 1.00 25.99  ? 43  PHE   A O   1 
ATOM   381  C  CB  . PHE   A 1 42  ? 37.270 -16.265 29.389 1.00 21.91  ? 43  PHE   A CB  1 
ATOM   382  C  CG  . PHE   A 1 42  ? 36.650 -16.388 30.761 1.00 23.67  ? 43  PHE   A CG  1 
ATOM   383  C  CD1 . PHE   A 1 42  ? 36.555 -15.278 31.604 1.00 26.42  ? 43  PHE   A CD1 1 
ATOM   384  C  CD2 . PHE   A 1 42  ? 36.197 -17.616 31.228 1.00 27.01  ? 43  PHE   A CD2 1 
ATOM   385  C  CE1 . PHE   A 1 42  ? 36.005 -15.396 32.880 1.00 28.34  ? 43  PHE   A CE1 1 
ATOM   386  C  CE2 . PHE   A 1 42  ? 35.644 -17.730 32.508 1.00 30.49  ? 43  PHE   A CE2 1 
ATOM   387  C  CZ  . PHE   A 1 42  ? 35.560 -16.621 33.327 1.00 28.66  ? 43  PHE   A CZ  1 
ATOM   388  N  N   . ARG   A 1 43  ? 39.929 -17.321 27.397 1.00 22.43  ? 44  ARG   A N   1 
ATOM   389  C  CA  . ARG   A 1 43  ? 40.445 -17.268 26.032 1.00 20.79  ? 44  ARG   A CA  1 
ATOM   390  C  C   . ARG   A 1 43  ? 39.325 -17.675 25.080 1.00 23.01  ? 44  ARG   A C   1 
ATOM   391  O  O   . ARG   A 1 43  ? 38.530 -18.569 25.399 1.00 22.05  ? 44  ARG   A O   1 
ATOM   392  C  CB  . ARG   A 1 43  ? 41.665 -18.190 25.855 1.00 22.68  ? 44  ARG   A CB  1 
ATOM   393  C  CG  . ARG   A 1 43  ? 42.887 -17.737 26.710 1.00 27.64  ? 44  ARG   A CG  1 
ATOM   394  C  CD  . ARG   A 1 43  ? 44.217 -18.172 26.097 1.00 36.52  ? 44  ARG   A CD  1 
ATOM   395  N  NE  . ARG   A 1 43  ? 44.263 -17.837 24.668 1.00 47.60  ? 44  ARG   A NE  1 
ATOM   396  C  CZ  . ARG   A 1 43  ? 44.798 -16.733 24.155 1.00 59.48  ? 44  ARG   A CZ  1 
ATOM   397  N  NH1 . ARG   A 1 43  ? 45.435 -15.871 24.934 1.00 50.18  ? 44  ARG   A NH1 1 
ATOM   398  N  NH2 . ARG   A 1 43  ? 44.743 -16.509 22.849 1.00 42.60  ? 44  ARG   A NH2 1 
ATOM   399  N  N   . ALA   A 1 44  ? 39.246 -17.022 23.917 1.00 20.05  ? 45  ALA   A N   1 
ATOM   400  C  CA  . ALA   A 1 44  ? 38.169 -17.327 22.953 1.00 20.36  ? 45  ALA   A CA  1 
ATOM   401  C  C   . ALA   A 1 44  ? 38.555 -16.895 21.553 1.00 21.73  ? 45  ALA   A C   1 
ATOM   402  O  O   . ALA   A 1 44  ? 39.663 -16.405 21.340 1.00 19.99  ? 45  ALA   A O   1 
ATOM   403  C  CB  . ALA   A 1 44  ? 36.867 -16.632 23.371 1.00 21.53  ? 45  ALA   A CB  1 
ATOM   404  N  N   . HIS   A 1 45  ? 37.650 -17.144 20.591 1.00 18.65  ? 46  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 45  ? 37.807 -16.727 19.205 1.00 17.29  ? 46  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 45  ? 36.911 -15.502 19.019 1.00 20.34  ? 46  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 45  ? 35.696 -15.569 19.286 1.00 18.46  ? 46  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 45  ? 37.359 -17.853 18.243 1.00 16.47  ? 46  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 45  ? 38.114 -19.131 18.454 1.00 19.36  ? 46  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 45  ? 37.629 -20.132 19.296 1.00 20.37  ? 46  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 45  ? 39.333 -19.502 17.987 1.00 20.53  ? 46  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 45  ? 38.550 -21.086 19.287 1.00 20.21  ? 46  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 45  ? 39.601 -20.746 18.519 1.00 20.28  ? 46  HIS   A NE2 1 
ATOM   414  N  N   . LYS   A 1 46  ? 37.502 -14.388 18.570 1.00 19.53  ? 47  LYS   A N   1 
ATOM   415  C  CA  . LYS   A 1 46  ? 36.738 -13.146 18.331 1.00 18.42  ? 47  LYS   A CA  1 
ATOM   416  C  C   . LYS   A 1 46  ? 35.500 -13.415 17.455 1.00 20.01  ? 47  LYS   A C   1 
ATOM   417  O  O   . LYS   A 1 46  ? 34.435 -12.906 17.781 1.00 18.04  ? 47  LYS   A O   1 
ATOM   418  C  CB  . LYS   A 1 46  ? 37.619 -12.091 17.631 1.00 20.05  ? 47  LYS   A CB  1 
ATOM   419  C  CG  . LYS   A 1 46  ? 38.627 -11.465 18.581 1.00 20.88  ? 47  LYS   A CG  1 
ATOM   420  C  CD  . LYS   A 1 46  ? 39.595 -10.609 17.763 1.00 19.21  ? 47  LYS   A CD  1 
ATOM   421  C  CE  . LYS   A 1 46  ? 40.654 -10.045 18.661 1.00 25.52  ? 47  LYS   A CE  1 
ATOM   422  N  NZ  . LYS   A 1 46  ? 41.655 -9.313  17.860 1.00 24.68  ? 47  LYS   A NZ  1 
ATOM   423  N  N   . THR   A 1 47  ? 35.628 -14.225 16.384 1.00 17.75  ? 48  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 47  ? 34.498 -14.444 15.481 1.00 17.40  ? 48  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 47  ? 33.338 -15.115 16.172 1.00 18.25  ? 48  THR   A C   1 
ATOM   426  O  O   . THR   A 1 47  ? 32.192 -14.787 15.894 1.00 19.18  ? 48  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 47  ? 34.910 -15.158 14.206 1.00 23.48  ? 48  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 47  ? 35.591 -16.355 14.572 1.00 25.38  ? 48  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 47  ? 35.755 -14.250 13.296 1.00 24.18  ? 48  THR   A CG2 1 
ATOM   430  N  N   . VAL   A 1 48  ? 33.627 -16.052 17.061 1.00 14.81  ? 49  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 48  ? 32.559 -16.757 17.784 1.00 15.40  ? 49  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 48  ? 31.869 -15.794 18.751 1.00 17.49  ? 49  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 48  ? 30.621 -15.770 18.829 1.00 16.22  ? 49  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 48  ? 33.058 -18.054 18.477 1.00 16.87  ? 49  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 48  ? 31.936 -18.680 19.324 1.00 17.37  ? 49  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 48  ? 33.531 -19.074 17.423 1.00 16.90  ? 49  VAL   A CG2 1 
ATOM   437  N  N   . LEU   A 1 49  ? 32.665 -15.002 19.490 1.00 16.14  ? 50  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 49  ? 32.086 -13.999 20.394 1.00 15.74  ? 50  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 49  ? 31.165 -13.031 19.632 1.00 18.87  ? 50  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 49  ? 30.055 -12.737 20.092 1.00 18.61  ? 50  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 49  ? 33.202 -13.203 21.109 1.00 15.39  ? 50  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 49  ? 34.189 -13.986 22.008 1.00 18.20  ? 50  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 49  ? 35.230 -13.020 22.630 1.00 18.30  ? 50  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 49  ? 33.445 -14.774 23.112 1.00 19.44  ? 50  LEU   A CD2 1 
ATOM   445  N  N   . MET   A 1 50  ? 31.629 -12.542 18.463 1.00 16.58  ? 51  MET   A N   1 
ATOM   446  C  CA  . MET   A 1 50  ? 30.846 -11.630 17.646 1.00 17.09  ? 51  MET   A CA  1 
ATOM   447  C  C   . MET   A 1 50  ? 29.551 -12.283 17.167 1.00 21.28  ? 51  MET   A C   1 
ATOM   448  O  O   . MET   A 1 50  ? 28.502 -11.641 17.199 1.00 20.69  ? 51  MET   A O   1 
ATOM   449  C  CB  . MET   A 1 50  ? 31.646 -11.151 16.438 1.00 17.76  ? 51  MET   A CB  1 
ATOM   450  C  CG  . MET   A 1 50  ? 32.864 -10.311 16.811 1.00 19.08  ? 51  MET   A CG  1 
ATOM   451  S  SD  . MET   A 1 50  ? 33.931 -10.266 15.365 1.00 22.85  ? 51  MET   A SD  1 
ATOM   452  C  CE  . MET   A 1 50  ? 33.167 -8.923  14.481 1.00 20.53  ? 51  MET   A CE  1 
ATOM   453  N  N   . ALA   A 1 51  ? 29.619 -13.571 16.768 1.00 18.68  ? 52  ALA   A N   1 
ATOM   454  C  CA  . ALA   A 1 51  ? 28.459 -14.306 16.254 1.00 17.73  ? 52  ALA   A CA  1 
ATOM   455  C  C   . ALA   A 1 51  ? 27.357 -14.520 17.334 1.00 19.29  ? 52  ALA   A C   1 
ATOM   456  O  O   . ALA   A 1 51  ? 26.195 -14.773 16.992 1.00 20.56  ? 52  ALA   A O   1 
ATOM   457  C  CB  . ALA   A 1 51  ? 28.908 -15.657 15.667 1.00 18.18  ? 52  ALA   A CB  1 
ATOM   458  N  N   . CYS   A 1 52  ? 27.734 -14.428 18.632 1.00 16.03  ? 53  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 52  ? 26.826 -14.686 19.750 1.00 15.97  ? 53  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 52  ? 26.373 -13.468 20.533 1.00 20.35  ? 53  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 52  ? 25.422 -13.595 21.303 1.00 18.48  ? 53  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 52  ? 27.483 -15.686 20.700 1.00 15.93  ? 53  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 52  ? 27.842 -17.288 19.957 1.00 18.95  ? 53  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 53  ? 27.103 -12.351 20.435 1.00 17.33  ? 54  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 53  ? 26.913 -11.198 21.318 1.00 16.57  ? 54  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 53  ? 26.930 -9.883  20.569 1.00 21.29  ? 54  SER   A C   1 
ATOM   467  O  O   . SER   A 1 53  ? 27.905 -9.595  19.859 1.00 18.90  ? 54  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 53  ? 28.036 -11.231 22.356 1.00 18.43  ? 54  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 53  ? 28.381 -9.987  22.946 1.00 20.61  ? 54  SER   A OG  1 
ATOM   470  N  N   . GLY   A 1 54  ? 25.890 -9.066  20.777 1.00 19.71  ? 55  GLY   A N   1 
ATOM   471  C  CA  . GLY   A 1 54  ? 25.823 -7.731  20.179 1.00 19.70  ? 55  GLY   A CA  1 
ATOM   472  C  C   . GLY   A 1 54  ? 26.955 -6.845  20.665 1.00 22.58  ? 55  GLY   A C   1 
ATOM   473  O  O   . GLY   A 1 54  ? 27.511 -6.050  19.886 1.00 21.69  ? 55  GLY   A O   1 
ATOM   474  N  N   . LEU   A 1 55  ? 27.355 -7.025  21.949 1.00 20.74  ? 56  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 55  ? 28.470 -6.254  22.513 1.00 21.34  ? 56  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 55  ? 29.812 -6.604  21.833 1.00 22.59  ? 56  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 55  ? 30.507 -5.689  21.379 1.00 21.15  ? 56  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 55  ? 28.552 -6.395  24.049 1.00 21.29  ? 56  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 55  ? 29.613 -5.520  24.733 1.00 26.03  ? 56  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 55  ? 29.177 -4.032  24.791 1.00 27.31  ? 56  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 55  ? 29.927 -6.044  26.125 1.00 23.54  ? 56  LEU   A CD2 1 
ATOM   482  N  N   . PHE   A 1 56  ? 30.139 -7.918  21.702 1.00 18.33  ? 57  PHE   A N   1 
ATOM   483  C  CA  . PHE   A 1 56  ? 31.392 -8.305  21.038 1.00 17.90  ? 57  PHE   A CA  1 
ATOM   484  C  C   . PHE   A 1 56  ? 31.376 -7.960  19.566 1.00 21.72  ? 57  PHE   A C   1 
ATOM   485  O  O   . PHE   A 1 56  ? 32.408 -7.567  19.030 1.00 20.04  ? 57  PHE   A O   1 
ATOM   486  C  CB  . PHE   A 1 56  ? 31.760 -9.771  21.296 1.00 18.63  ? 57  PHE   A CB  1 
ATOM   487  C  CG  . PHE   A 1 56  ? 32.171 -10.004 22.733 1.00 19.08  ? 57  PHE   A CG  1 
ATOM   488  C  CD1 . PHE   A 1 56  ? 33.216 -9.276  23.309 1.00 21.00  ? 57  PHE   A CD1 1 
ATOM   489  C  CD2 . PHE   A 1 56  ? 31.518 -10.956 23.514 1.00 19.71  ? 57  PHE   A CD2 1 
ATOM   490  C  CE1 . PHE   A 1 56  ? 33.576 -9.470  24.656 1.00 21.51  ? 57  PHE   A CE1 1 
ATOM   491  C  CE2 . PHE   A 1 56  ? 31.922 -11.197 24.836 1.00 22.71  ? 57  PHE   A CE2 1 
ATOM   492  C  CZ  . PHE   A 1 56  ? 32.926 -10.437 25.408 1.00 21.17  ? 57  PHE   A CZ  1 
ATOM   493  N  N   . TYR   A 1 57  ? 30.189 -8.032  18.920 1.00 19.29  ? 58  TYR   A N   1 
ATOM   494  C  CA  . TYR   A 1 57  ? 30.073 -7.634  17.504 1.00 20.59  ? 58  TYR   A CA  1 
ATOM   495  C  C   . TYR   A 1 57  ? 30.493 -6.166  17.347 1.00 24.37  ? 58  TYR   A C   1 
ATOM   496  O  O   . TYR   A 1 57  ? 31.302 -5.849  16.469 1.00 22.17  ? 58  TYR   A O   1 
ATOM   497  C  CB  . TYR   A 1 57  ? 28.632 -7.873  17.022 1.00 22.43  ? 58  TYR   A CB  1 
ATOM   498  C  CG  . TYR   A 1 57  ? 28.344 -7.335  15.640 1.00 25.46  ? 58  TYR   A CG  1 
ATOM   499  C  CD1 . TYR   A 1 57  ? 28.987 -7.854  14.521 1.00 27.46  ? 58  TYR   A CD1 1 
ATOM   500  C  CD2 . TYR   A 1 57  ? 27.425 -6.308  15.453 1.00 29.70  ? 58  TYR   A CD2 1 
ATOM   501  C  CE1 . TYR   A 1 57  ? 28.718 -7.361  13.239 1.00 29.24  ? 58  TYR   A CE1 1 
ATOM   502  C  CE2 . TYR   A 1 57  ? 27.152 -5.807  14.183 1.00 32.69  ? 58  TYR   A CE2 1 
ATOM   503  C  CZ  . TYR   A 1 57  ? 27.784 -6.354  13.080 1.00 38.38  ? 58  TYR   A CZ  1 
ATOM   504  O  OH  . TYR   A 1 57  ? 27.491 -5.860  11.839 1.00 42.64  ? 58  TYR   A OH  1 
ATOM   505  N  N   A SER   A 1 58  ? 29.956 -5.281  18.207 0.53 21.85  ? 59  SER   A N   1 
ATOM   506  N  N   B SER   A 1 58  ? 29.955 -5.283  18.213 0.47 21.62  ? 59  SER   A N   1 
ATOM   507  C  CA  A SER   A 1 58  ? 30.280 -3.850  18.197 0.53 22.57  ? 59  SER   A CA  1 
ATOM   508  C  CA  B SER   A 1 58  ? 30.274 -3.851  18.219 0.47 22.27  ? 59  SER   A CA  1 
ATOM   509  C  C   A SER   A 1 58  ? 31.772 -3.606  18.499 0.53 27.01  ? 59  SER   A C   1 
ATOM   510  C  C   B SER   A 1 58  ? 31.771 -3.625  18.487 0.47 26.81  ? 59  SER   A C   1 
ATOM   511  O  O   A SER   A 1 58  ? 32.412 -2.830  17.793 0.53 28.27  ? 59  SER   A O   1 
ATOM   512  O  O   B SER   A 1 58  ? 32.412 -2.876  17.753 0.47 27.91  ? 59  SER   A O   1 
ATOM   513  C  CB  A SER   A 1 58  ? 29.391 -3.106  19.187 0.53 25.04  ? 59  SER   A CB  1 
ATOM   514  C  CB  B SER   A 1 58  ? 29.435 -3.132  19.272 0.47 24.45  ? 59  SER   A CB  1 
ATOM   515  O  OG  A SER   A 1 58  ? 28.056 -3.064  18.709 0.53 28.94  ? 59  SER   A OG  1 
ATOM   516  O  OG  B SER   A 1 58  ? 29.735 -1.746  19.297 0.47 28.57  ? 59  SER   A OG  1 
ATOM   517  N  N   . ILE   A 1 59  ? 32.322 -4.284  19.525 1.00 23.24  ? 60  ILE   A N   1 
ATOM   518  C  CA  . ILE   A 1 59  ? 33.739 -4.153  19.917 1.00 22.46  ? 60  ILE   A CA  1 
ATOM   519  C  C   . ILE   A 1 59  ? 34.689 -4.527  18.782 1.00 25.14  ? 60  ILE   A C   1 
ATOM   520  O  O   . ILE   A 1 59  ? 35.538 -3.713  18.397 1.00 25.95  ? 60  ILE   A O   1 
ATOM   521  C  CB  . ILE   A 1 59  ? 34.065 -4.992  21.210 1.00 24.03  ? 60  ILE   A CB  1 
ATOM   522  C  CG1 . ILE   A 1 59  ? 33.331 -4.416  22.446 1.00 23.98  ? 60  ILE   A CG1 1 
ATOM   523  C  CG2 . ILE   A 1 59  ? 35.602 -5.042  21.463 1.00 23.24  ? 60  ILE   A CG2 1 
ATOM   524  C  CD1 . ILE   A 1 59  ? 33.376 -5.378  23.676 1.00 26.04  ? 60  ILE   A CD1 1 
ATOM   525  N  N   . PHE   A 1 60  ? 34.524 -5.730  18.219 1.00 20.56  ? 61  PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 60  ? 35.492 -6.189  17.240 1.00 21.25  ? 61  PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 60  ? 35.279 -5.654  15.821 1.00 24.79  ? 61  PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 60  ? 36.134 -5.906  14.971 1.00 25.83  ? 61  PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 60  ? 35.646 -7.708  17.276 1.00 21.13  ? 61  PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 60  ? 36.062 -8.204  18.652 1.00 21.50  ? 61  PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 60  ? 37.273 -7.810  19.219 1.00 24.54  ? 61  PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 60  ? 35.238 -9.055  19.382 1.00 21.01  ? 61  PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 60  ? 37.654 -8.268  20.490 1.00 24.80  ? 61  PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 60  ? 35.628 -9.528  20.640 1.00 23.33  ? 61  PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 60  ? 36.830 -9.123  21.192 1.00 22.64  ? 61  PHE   A CZ  1 
ATOM   536  N  N   . THR   A 1 61  ? 34.200 -4.892  15.568 1.00 22.56  ? 62  THR   A N   1 
ATOM   537  C  CA  . THR   A 1 61  ? 34.034 -4.210  14.268 1.00 23.19  ? 62  THR   A CA  1 
ATOM   538  C  C   . THR   A 1 61  ? 34.573 -2.785  14.406 1.00 29.57  ? 62  THR   A C   1 
ATOM   539  O  O   . THR   A 1 61  ? 34.641 -2.044  13.413 1.00 29.53  ? 62  THR   A O   1 
ATOM   540  C  CB  . THR   A 1 61  ? 32.602 -4.233  13.723 1.00 29.51  ? 62  THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 61  ? 31.705 -3.720  14.706 1.00 26.51  ? 62  THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 61  ? 32.170 -5.622  13.228 1.00 25.76  ? 62  THR   A CG2 1 
ATOM   543  N  N   . ASP   A 1 62  ? 34.981 -2.392  15.637 1.00 26.55  ? 63  ASP   A N   1 
ATOM   544  C  CA  . ASP   A 1 62  ? 35.585 -1.073  15.839 1.00 27.56  ? 63  ASP   A CA  1 
ATOM   545  C  C   . ASP   A 1 62  ? 36.999 -1.110  15.265 1.00 32.46  ? 63  ASP   A C   1 
ATOM   546  O  O   . ASP   A 1 62  ? 37.769 -2.003  15.609 1.00 29.53  ? 63  ASP   A O   1 
ATOM   547  C  CB  . ASP   A 1 62  ? 35.603 -0.679  17.326 1.00 28.98  ? 63  ASP   A CB  1 
ATOM   548  C  CG  . ASP   A 1 62  ? 36.319 0.630   17.553 1.00 37.34  ? 63  ASP   A CG  1 
ATOM   549  O  OD1 . ASP   A 1 62  ? 35.682 1.684   17.395 1.00 41.69  ? 63  ASP   A OD1 1 
ATOM   550  O  OD2 . ASP   A 1 62  ? 37.534 0.599   17.830 1.00 35.86  ? 63  ASP   A OD2 1 
ATOM   551  N  N   . GLN   A 1 63  ? 37.345 -0.118  14.418 1.00 34.35  ? 64  GLN   A N   1 
ATOM   552  C  CA  . GLN   A 1 63  ? 38.636 -0.029  13.733 1.00 36.04  ? 64  GLN   A CA  1 
ATOM   553  C  C   . GLN   A 1 63  ? 39.859 -0.051  14.662 1.00 39.22  ? 64  GLN   A C   1 
ATOM   554  O  O   . GLN   A 1 63  ? 40.933 -0.439  14.200 1.00 40.49  ? 64  GLN   A O   1 
ATOM   555  C  CB  . GLN   A 1 63  ? 38.684 1.181   12.790 1.00 39.51  ? 64  GLN   A CB  1 
ATOM   556  C  CG  . GLN   A 1 63  ? 37.868 0.982   11.514 1.00 56.45  ? 64  GLN   A CG  1 
ATOM   557  N  N   . LEU   A 1 64  ? 39.720 0.363   15.946 1.00 32.32  ? 65  LEU   A N   1 
ATOM   558  C  CA  . LEU   A 1 64  ? 40.829 0.277   16.900 1.00 31.17  ? 65  LEU   A CA  1 
ATOM   559  C  C   . LEU   A 1 64  ? 40.731 -0.974  17.751 1.00 34.98  ? 65  LEU   A C   1 
ATOM   560  O  O   . LEU   A 1 64  ? 41.730 -1.651  17.966 1.00 36.87  ? 65  LEU   A O   1 
ATOM   561  C  CB  . LEU   A 1 64  ? 40.870 1.486   17.856 1.00 31.89  ? 65  LEU   A CB  1 
ATOM   562  C  CG  . LEU   A 1 64  ? 41.461 2.766   17.299 1.00 37.83  ? 65  LEU   A CG  1 
ATOM   563  C  CD1 . LEU   A 1 64  ? 41.418 3.867   18.346 1.00 39.30  ? 65  LEU   A CD1 1 
ATOM   564  C  CD2 . LEU   A 1 64  ? 42.899 2.573   16.805 1.00 42.73  ? 65  LEU   A CD2 1 
ATOM   565  N  N   . LYS   A 1 65  ? 39.545 -1.249  18.306 1.00 28.70  ? 66  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 65  ? 39.379 -2.370  19.225 1.00 25.98  ? 66  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 65  ? 39.520 -3.734  18.557 1.00 30.97  ? 66  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 65  ? 39.913 -4.681  19.228 1.00 29.92  ? 66  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 65  ? 38.064 -2.281  20.018 1.00 25.57  ? 66  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 65  ? 37.952 -1.048  20.913 1.00 26.50  ? 66  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 65  ? 36.673 -1.126  21.747 1.00 23.81  ? 66  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 65  ? 36.348 0.191   22.433 1.00 26.35  ? 66  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 65  ? 35.826 1.215   21.492 1.00 29.48  ? 66  LYS   A NZ  1 
ATOM   574  N  N   . CYS   A 1 66  ? 39.261 -3.815  17.239 1.00 29.97  ? 67  CYS   A N   1 
ATOM   575  C  CA  . CYS   A 1 66  ? 39.395 -5.060  16.467 1.00 29.59  ? 67  CYS   A CA  1 
ATOM   576  C  C   . CYS   A 1 66  ? 40.793 -5.682  16.613 1.00 34.65  ? 67  CYS   A C   1 
ATOM   577  O  O   . CYS   A 1 66  ? 40.928 -6.898  16.444 1.00 35.09  ? 67  CYS   A O   1 
ATOM   578  C  CB  . CYS   A 1 66  ? 39.042 -4.834  14.999 1.00 31.12  ? 67  CYS   A CB  1 
ATOM   579  S  SG  . CYS   A 1 66  ? 40.200 -3.755  14.106 1.00 37.17  ? 67  CYS   A SG  1 
ATOM   580  N  N   . ASN   A 1 67  ? 41.825 -4.841  16.893 1.00 31.31  ? 68  ASN   A N   1 
ATOM   581  C  CA  . ASN   A 1 67  ? 43.224 -5.255  16.999 1.00 32.25  ? 68  ASN   A CA  1 
ATOM   582  C  C   . ASN   A 1 67  ? 43.701 -5.539  18.421 1.00 35.40  ? 68  ASN   A C   1 
ATOM   583  O  O   . ASN   A 1 67  ? 44.867 -5.902  18.625 1.00 34.30  ? 68  ASN   A O   1 
ATOM   584  C  CB  . ASN   A 1 67  ? 44.140 -4.235  16.295 1.00 33.09  ? 68  ASN   A CB  1 
ATOM   585  C  CG  . ASN   A 1 67  ? 43.869 -4.172  14.799 1.00 45.95  ? 68  ASN   A CG  1 
ATOM   586  O  OD1 . ASN   A 1 67  ? 43.788 -3.094  14.209 1.00 46.30  ? 68  ASN   A OD1 1 
ATOM   587  N  ND2 . ASN   A 1 67  ? 43.665 -5.323  14.158 1.00 36.91  ? 68  ASN   A ND2 1 
ATOM   588  N  N   . LEU   A 1 68  ? 42.808 -5.386  19.410 1.00 32.53  ? 69  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 68  ? 43.190 -5.653  20.788 1.00 31.00  ? 69  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 68  ? 43.186 -7.144  21.057 1.00 33.41  ? 69  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 68  ? 42.313 -7.857  20.545 1.00 31.58  ? 69  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 68  ? 42.251 -4.932  21.779 1.00 30.73  ? 69  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 68  ? 42.250 -3.392  21.712 1.00 35.06  ? 69  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 68  ? 41.157 -2.827  22.598 1.00 34.62  ? 69  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 68  ? 43.620 -2.798  22.096 1.00 36.90  ? 69  LEU   A CD2 1 
ATOM   596  N  N   A SER   A 1 69  ? 44.154 -7.620  21.855 0.51 30.75  ? 70  SER   A N   1 
ATOM   597  N  N   B SER   A 1 69  ? 44.160 -7.608  21.857 0.49 30.43  ? 70  SER   A N   1 
ATOM   598  C  CA  A SER   A 1 69  ? 44.246 -9.036  22.225 0.51 29.80  ? 70  SER   A CA  1 
ATOM   599  C  CA  B SER   A 1 69  ? 44.304 -9.013  22.249 0.49 29.39  ? 70  SER   A CA  1 
ATOM   600  C  C   A SER   A 1 69  ? 43.651 -9.264  23.623 0.51 30.18  ? 70  SER   A C   1 
ATOM   601  C  C   B SER   A 1 69  ? 43.682 -9.256  23.630 0.49 30.05  ? 70  SER   A C   1 
ATOM   602  O  O   A SER   A 1 69  ? 43.448 -10.410 24.028 0.51 27.95  ? 70  SER   A O   1 
ATOM   603  O  O   B SER   A 1 69  ? 43.487 -10.406 24.027 0.49 27.88  ? 70  SER   A O   1 
ATOM   604  C  CB  A SER   A 1 69  ? 45.691 -9.521  22.160 0.51 34.89  ? 70  SER   A CB  1 
ATOM   605  C  CB  B SER   A 1 69  ? 45.778 -9.410  22.255 0.49 33.79  ? 70  SER   A CB  1 
ATOM   606  O  OG  A SER   A 1 69  ? 46.517 -8.788  23.048 0.51 43.05  ? 70  SER   A OG  1 
ATOM   607  O  OG  B SER   A 1 69  ? 46.301 -9.397  20.937 0.49 38.60  ? 70  SER   A OG  1 
ATOM   608  N  N   . VAL   A 1 70  ? 43.383 -8.163  24.362 1.00 27.11  ? 71  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 70  ? 42.789 -8.204  25.704 1.00 26.90  ? 71  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 70  ? 41.609 -7.227  25.746 1.00 28.54  ? 71  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 70  ? 41.766 -6.054  25.358 1.00 27.42  ? 71  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 70  ? 43.828 -7.857  26.822 1.00 31.89  ? 71  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 70  ? 43.173 -7.817  28.208 1.00 31.96  ? 71  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 70  ? 45.013 -8.827  26.817 1.00 32.77  ? 71  VAL   A CG2 1 
ATOM   615  N  N   . ILE   A 1 71  ? 40.453 -7.708  26.242 1.00 22.61  ? 72  ILE   A N   1 
ATOM   616  C  CA  . ILE   A 1 71  ? 39.240 -6.908  26.450 1.00 21.69  ? 72  ILE   A CA  1 
ATOM   617  C  C   . ILE   A 1 71  ? 38.842 -7.032  27.915 1.00 25.01  ? 72  ILE   A C   1 
ATOM   618  O  O   . ILE   A 1 71  ? 38.636 -8.148  28.408 1.00 25.42  ? 72  ILE   A O   1 
ATOM   619  C  CB  . ILE   A 1 71  ? 38.073 -7.276  25.484 1.00 23.63  ? 72  ILE   A CB  1 
ATOM   620  C  CG1 . ILE   A 1 71  ? 38.466 -7.077  23.976 1.00 24.50  ? 72  ILE   A CG1 1 
ATOM   621  C  CG2 . ILE   A 1 71  ? 36.753 -6.545  25.855 1.00 25.37  ? 72  ILE   A CG2 1 
ATOM   622  C  CD1 . ILE   A 1 71  ? 38.800 -5.625  23.506 1.00 28.64  ? 72  ILE   A CD1 1 
ATOM   623  N  N   . ASN   A 1 72  ? 38.723 -5.879  28.612 1.00 23.57  ? 73  ASN   A N   1 
ATOM   624  C  CA  . ASN   A 1 72  ? 38.332 -5.863  30.010 1.00 23.92  ? 73  ASN   A CA  1 
ATOM   625  C  C   . ASN   A 1 72  ? 36.856 -5.543  30.136 1.00 26.26  ? 73  ASN   A C   1 
ATOM   626  O  O   . ASN   A 1 72  ? 36.425 -4.462  29.724 1.00 24.05  ? 73  ASN   A O   1 
ATOM   627  C  CB  . ASN   A 1 72  ? 39.146 -4.821  30.794 1.00 26.58  ? 73  ASN   A CB  1 
ATOM   628  C  CG  . ASN   A 1 72  ? 40.623 -5.006  30.712 1.00 45.01  ? 73  ASN   A CG  1 
ATOM   629  O  OD1 . ASN   A 1 72  ? 41.155 -6.049  31.074 1.00 33.84  ? 73  ASN   A OD1 1 
ATOM   630  N  ND2 . ASN   A 1 72  ? 41.320 -3.979  30.264 1.00 40.83  ? 73  ASN   A ND2 1 
ATOM   631  N  N   . LEU   A 1 73  ? 36.089 -6.451  30.741 1.00 21.31  ? 74  LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 73  ? 34.665 -6.197  30.943 1.00 20.59  ? 74  LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 73  ? 34.437 -5.299  32.153 1.00 24.55  ? 74  LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 73  ? 35.315 -5.155  33.025 1.00 24.86  ? 74  LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 73  ? 33.836 -7.496  31.076 1.00 19.96  ? 74  LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 73  ? 33.903 -8.529  29.912 1.00 22.46  ? 74  LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 73  ? 32.793 -9.590  30.070 1.00 22.91  ? 74  LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 73  ? 33.820 -7.864  28.532 1.00 23.00  ? 74  LEU   A CD2 1 
ATOM   639  N  N   . ASP   A 1 74  ? 33.243 -4.717  32.217 1.00 21.51  ? 75  ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 74  ? 32.804 -3.851  33.320 1.00 22.80  ? 75  ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 74  ? 33.013 -4.606  34.656 1.00 26.84  ? 75  ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 74  ? 32.697 -5.796  34.728 1.00 26.41  ? 75  ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 74  ? 31.329 -3.474  33.129 1.00 24.61  ? 75  ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 74  ? 30.801 -2.437  34.110 1.00 31.03  ? 75  ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 74  ? 30.733 -2.739  35.320 1.00 32.04  ? 75  ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 74  ? 30.438 -1.337  33.666 1.00 32.16  ? 75  ASP   A OD2 1 
ATOM   647  N  N   . PRO   A 1 75  ? 33.587 -3.956  35.692 1.00 27.76  ? 76  PRO   A N   1 
ATOM   648  C  CA  . PRO   A 1 75  ? 33.835 -4.680  36.964 1.00 27.97  ? 76  PRO   A CA  1 
ATOM   649  C  C   . PRO   A 1 75  ? 32.613 -5.265  37.653 1.00 30.89  ? 76  PRO   A C   1 
ATOM   650  O  O   . PRO   A 1 75  ? 32.782 -6.104  38.530 1.00 31.42  ? 76  PRO   A O   1 
ATOM   651  C  CB  . PRO   A 1 75  ? 34.531 -3.643  37.860 1.00 30.73  ? 76  PRO   A CB  1 
ATOM   652  C  CG  . PRO   A 1 75  ? 34.292 -2.330  37.222 1.00 36.29  ? 76  PRO   A CG  1 
ATOM   653  C  CD  . PRO   A 1 75  ? 34.051 -2.554  35.764 1.00 30.38  ? 76  PRO   A CD  1 
ATOM   654  N  N   . GLU   A 1 76  ? 31.399 -4.843  37.270 1.00 28.34  ? 77  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 76  ? 30.153 -5.357  37.858 1.00 29.99  ? 77  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 76  ? 29.852 -6.772  37.301 1.00 29.35  ? 77  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 76  ? 29.021 -7.490  37.857 1.00 28.68  ? 77  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 76  ? 28.983 -4.405  37.516 1.00 32.62  ? 77  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 76  ? 27.808 -4.464  38.472 1.00 51.50  ? 77  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 76  ? 27.972 -3.568  39.683 1.00 76.85  ? 77  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 76  ? 27.950 -2.327  39.512 1.00 77.00  ? 77  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 76  ? 28.129 -4.106  40.803 1.00 69.37  ? 77  GLU   A OE2 1 
ATOM   663  N  N   . ILE   A 1 77  ? 30.503 -7.157  36.195 1.00 25.21  ? 78  ILE   A N   1 
ATOM   664  C  CA  . ILE   A 1 77  ? 30.255 -8.454  35.574 1.00 24.44  ? 78  ILE   A CA  1 
ATOM   665  C  C   . ILE   A 1 77  ? 30.842 -9.585  36.394 1.00 28.31  ? 78  ILE   A C   1 
ATOM   666  O  O   . ILE   A 1 77  ? 32.008 -9.542  36.790 1.00 27.84  ? 78  ILE   A O   1 
ATOM   667  C  CB  . ILE   A 1 77  ? 30.701 -8.485  34.090 1.00 25.93  ? 78  ILE   A CB  1 
ATOM   668  C  CG1 . ILE   A 1 77  ? 29.992 -7.363  33.283 1.00 25.87  ? 78  ILE   A CG1 1 
ATOM   669  C  CG2 . ILE   A 1 77  ? 30.454 -9.875  33.469 1.00 23.55  ? 78  ILE   A CG2 1 
ATOM   670  C  CD1 . ILE   A 1 77  ? 28.385 -7.362  33.320 1.00 30.98  ? 78  ILE   A CD1 1 
ATOM   671  N  N   . ASN   A 1 78  ? 30.007 -10.575 36.648 1.00 27.77  ? 79  ASN   A N   1 
ATOM   672  C  CA  . ASN   A 1 78  ? 30.317 -11.764 37.428 1.00 28.42  ? 79  ASN   A CA  1 
ATOM   673  C  C   . ASN   A 1 78  ? 31.062 -12.807 36.575 1.00 27.83  ? 79  ASN   A C   1 
ATOM   674  O  O   . ASN   A 1 78  ? 30.536 -13.210 35.541 1.00 26.51  ? 79  ASN   A O   1 
ATOM   675  C  CB  . ASN   A 1 78  ? 29.015 -12.343 37.998 1.00 30.82  ? 79  ASN   A CB  1 
ATOM   676  C  CG  . ASN   A 1 78  ? 29.210 -13.618 38.768 1.00 42.20  ? 79  ASN   A CG  1 
ATOM   677  O  OD1 . ASN   A 1 78  ? 28.887 -14.698 38.283 1.00 32.65  ? 79  ASN   A OD1 1 
ATOM   678  N  ND2 . ASN   A 1 78  ? 29.749 -13.516 39.983 1.00 36.09  ? 79  ASN   A ND2 1 
ATOM   679  N  N   . PRO   A 1 79  ? 32.277 -13.259 36.992 1.00 25.20  ? 80  PRO   A N   1 
ATOM   680  C  CA  . PRO   A 1 79  ? 33.023 -14.257 36.194 1.00 24.36  ? 80  PRO   A CA  1 
ATOM   681  C  C   . PRO   A 1 79  ? 32.262 -15.564 35.937 1.00 27.19  ? 80  PRO   A C   1 
ATOM   682  O  O   . PRO   A 1 79  ? 32.345 -16.098 34.828 1.00 26.67  ? 80  PRO   A O   1 
ATOM   683  C  CB  . PRO   A 1 79  ? 34.285 -14.505 37.029 1.00 27.96  ? 80  PRO   A CB  1 
ATOM   684  C  CG  . PRO   A 1 79  ? 34.447 -13.266 37.844 1.00 32.82  ? 80  PRO   A CG  1 
ATOM   685  C  CD  . PRO   A 1 79  ? 33.055 -12.839 38.178 1.00 28.36  ? 80  PRO   A CD  1 
ATOM   686  N  N   . GLU   A 1 80  ? 31.505 -16.071 36.942 1.00 24.67  ? 81  GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 80  ? 30.748 -17.311 36.731 1.00 24.25  ? 81  GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 80  ? 29.661 -17.117 35.660 1.00 25.82  ? 81  GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 80  ? 29.533 -17.961 34.779 1.00 23.60  ? 81  GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 80  ? 30.158 -17.860 38.042 1.00 26.62  ? 81  GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 80  ? 29.500 -19.211 37.801 1.00 32.54  ? 81  GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 80  ? 28.715 -19.839 38.937 1.00 52.43  ? 81  GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 80  ? 28.729 -21.086 39.028 1.00 50.45  ? 81  GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 80  ? 28.070 -19.102 39.715 1.00 44.17  ? 81  GLU   A OE2 1 
ATOM   695  N  N   . GLY   A 1 81  ? 28.918 -16.002 35.734 1.00 24.81  ? 82  GLY   A N   1 
ATOM   696  C  CA  . GLY   A 1 81  ? 27.895 -15.668 34.743 1.00 24.50  ? 82  GLY   A CA  1 
ATOM   697  C  C   . GLY   A 1 81  ? 28.493 -15.597 33.346 1.00 25.61  ? 82  GLY   A C   1 
ATOM   698  O  O   . GLY   A 1 81  ? 27.930 -16.144 32.378 1.00 22.55  ? 82  GLY   A O   1 
ATOM   699  N  N   . PHE   A 1 82  ? 29.681 -14.979 33.245 1.00 21.59  ? 83  PHE   A N   1 
ATOM   700  C  CA  . PHE   A 1 82  ? 30.374 -14.911 31.950 1.00 20.12  ? 83  PHE   A CA  1 
ATOM   701  C  C   . PHE   A 1 82  ? 30.765 -16.321 31.482 1.00 21.49  ? 83  PHE   A C   1 
ATOM   702  O  O   . PHE   A 1 82  ? 30.565 -16.660 30.312 1.00 21.45  ? 83  PHE   A O   1 
ATOM   703  C  CB  . PHE   A 1 82  ? 31.623 -14.000 32.000 1.00 21.54  ? 83  PHE   A CB  1 
ATOM   704  C  CG  . PHE   A 1 82  ? 32.234 -13.882 30.623 1.00 21.13  ? 83  PHE   A CG  1 
ATOM   705  C  CD1 . PHE   A 1 82  ? 31.661 -13.053 29.659 1.00 24.01  ? 83  PHE   A CD1 1 
ATOM   706  C  CD2 . PHE   A 1 82  ? 33.289 -14.702 30.240 1.00 22.19  ? 83  PHE   A CD2 1 
ATOM   707  C  CE1 . PHE   A 1 82  ? 32.172 -13.003 28.362 1.00 24.55  ? 83  PHE   A CE1 1 
ATOM   708  C  CE2 . PHE   A 1 82  ? 33.794 -14.661 28.938 1.00 23.71  ? 83  PHE   A CE2 1 
ATOM   709  C  CZ  . PHE   A 1 82  ? 33.215 -13.831 27.999 1.00 22.44  ? 83  PHE   A CZ  1 
ATOM   710  N  N   . CYS   A 1 83  ? 31.350 -17.129 32.378 1.00 21.50  ? 84  CYS   A N   1 
ATOM   711  C  CA  . CYS   A 1 83  ? 31.754 -18.506 32.047 1.00 23.34  ? 84  CYS   A CA  1 
ATOM   712  C  C   . CYS   A 1 83  ? 30.573 -19.329 31.481 1.00 24.56  ? 84  CYS   A C   1 
ATOM   713  O  O   . CYS   A 1 83  ? 30.718 -20.007 30.451 1.00 22.53  ? 84  CYS   A O   1 
ATOM   714  C  CB  . CYS   A 1 83  ? 32.371 -19.190 33.264 1.00 26.34  ? 84  CYS   A CB  1 
ATOM   715  S  SG  . CYS   A 1 83  ? 33.051 -20.832 32.904 1.00 31.64  ? 84  CYS   A SG  1 
ATOM   716  N  N   . ILE   A 1 84  ? 29.400 -19.257 32.159 1.00 22.09  ? 85  ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 84  ? 28.183 -19.971 31.747 1.00 20.51  ? 85  ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 84  ? 27.774 -19.525 30.348 1.00 21.82  ? 85  ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 84  ? 27.436 -20.368 29.497 1.00 19.31  ? 85  ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 84  ? 27.059 -19.734 32.793 1.00 23.49  ? 85  ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 84  ? 27.366 -20.536 34.100 1.00 23.58  ? 85  ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 84  ? 25.657 -20.067 32.215 1.00 23.56  ? 85  ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 84  ? 26.612 -20.074 35.309 1.00 28.57  ? 85  ILE   A CD1 1 
ATOM   724  N  N   . LEU   A 1 85  ? 27.859 -18.221 30.093 1.00 18.97  ? 86  LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 85  ? 27.501 -17.671 28.775 1.00 18.46  ? 86  LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 85  ? 28.498 -18.021 27.694 1.00 20.66  ? 86  LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 85  ? 28.086 -18.343 26.577 1.00 19.82  ? 86  LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 85  ? 27.250 -16.172 28.851 1.00 19.18  ? 86  LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 85  ? 25.942 -15.804 29.603 1.00 23.90  ? 86  LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 85  ? 25.852 -14.321 29.779 1.00 24.50  ? 86  LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 85  ? 24.683 -16.304 28.856 1.00 25.34  ? 86  LEU   A CD2 1 
ATOM   732  N  N   . LEU   A 1 86  ? 29.799 -18.012 28.020 1.00 18.79  ? 87  LEU   A N   1 
ATOM   733  C  CA  . LEU   A 1 86  ? 30.832 -18.415 27.055 1.00 18.28  ? 87  LEU   A CA  1 
ATOM   734  C  C   . LEU   A 1 86  ? 30.612 -19.895 26.657 1.00 21.52  ? 87  LEU   A C   1 
ATOM   735  O  O   . LEU   A 1 86  ? 30.670 -20.240 25.473 1.00 19.33  ? 87  LEU   A O   1 
ATOM   736  C  CB  . LEU   A 1 86  ? 32.231 -18.190 27.655 1.00 18.42  ? 87  LEU   A CB  1 
ATOM   737  C  CG  . LEU   A 1 86  ? 33.401 -18.503 26.696 1.00 21.69  ? 87  LEU   A CG  1 
ATOM   738  C  CD1 . LEU   A 1 86  ? 33.359 -17.611 25.443 1.00 20.88  ? 87  LEU   A CD1 1 
ATOM   739  C  CD2 . LEU   A 1 86  ? 34.761 -18.369 27.430 1.00 24.54  ? 87  LEU   A CD2 1 
ATOM   740  N  N   . ASP   A 1 87  ? 30.320 -20.763 27.638 1.00 18.38  ? 88  ASP   A N   1 
ATOM   741  C  CA  . ASP   A 1 87  ? 30.005 -22.165 27.352 1.00 18.15  ? 88  ASP   A CA  1 
ATOM   742  C  C   . ASP   A 1 87  ? 28.790 -22.267 26.431 1.00 20.25  ? 88  ASP   A C   1 
ATOM   743  O  O   . ASP   A 1 87  ? 28.818 -23.048 25.481 1.00 20.16  ? 88  ASP   A O   1 
ATOM   744  C  CB  . ASP   A 1 87  ? 29.720 -22.904 28.659 1.00 20.68  ? 88  ASP   A CB  1 
ATOM   745  C  CG  . ASP   A 1 87  ? 30.957 -23.241 29.470 1.00 31.93  ? 88  ASP   A CG  1 
ATOM   746  O  OD1 . ASP   A 1 87  ? 32.079 -23.164 28.911 1.00 32.11  ? 88  ASP   A OD1 1 
ATOM   747  O  OD2 . ASP   A 1 87  ? 30.804 -23.599 30.653 1.00 30.95  ? 88  ASP   A OD2 1 
ATOM   748  N  N   . PHE   A 1 88  ? 27.730 -21.483 26.709 1.00 18.74  ? 89  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 88  ? 26.526 -21.441 25.859 1.00 17.23  ? 89  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 88  ? 26.898 -21.043 24.421 1.00 19.22  ? 89  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 88  ? 26.432 -21.671 23.454 1.00 17.31  ? 89  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 88  ? 25.476 -20.465 26.439 1.00 17.77  ? 89  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 88  ? 24.365 -20.190 25.446 1.00 18.10  ? 89  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 88  ? 23.407 -21.161 25.163 1.00 21.15  ? 89  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 88  ? 24.342 -19.004 24.711 1.00 20.38  ? 89  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 88  ? 22.416 -20.930 24.211 1.00 20.33  ? 89  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 88  ? 23.353 -18.782 23.740 1.00 22.89  ? 89  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 88  ? 22.404 -19.755 23.491 1.00 21.09  ? 89  PHE   A CZ  1 
ATOM   759  N  N   . MET   A 1 89  ? 27.723 -19.999 24.275 1.00 15.78  ? 90  MET   A N   1 
ATOM   760  C  CA  . MET   A 1 89  ? 28.126 -19.558 22.925 1.00 15.09  ? 90  MET   A CA  1 
ATOM   761  C  C   . MET   A 1 89  ? 28.680 -20.708 22.088 1.00 19.52  ? 90  MET   A C   1 
ATOM   762  O  O   . MET   A 1 89  ? 28.331 -20.842 20.917 1.00 18.65  ? 90  MET   A O   1 
ATOM   763  C  CB  . MET   A 1 89  ? 29.212 -18.464 23.009 1.00 15.93  ? 90  MET   A CB  1 
ATOM   764  C  CG  . MET   A 1 89  ? 28.699 -17.182 23.623 1.00 17.03  ? 90  MET   A CG  1 
ATOM   765  S  SD  . MET   A 1 89  ? 30.038 -15.955 23.521 1.00 19.81  ? 90  MET   A SD  1 
ATOM   766  C  CE  . MET   A 1 89  ? 29.368 -14.712 24.696 1.00 20.06  ? 90  MET   A CE  1 
ATOM   767  N  N   . TYR   A 1 90  ? 29.552 -21.530 22.697 1.00 16.33  ? 91  TYR   A N   1 
ATOM   768  C  CA  . TYR   A 1 90  ? 30.235 -22.621 22.000 1.00 16.03  ? 91  TYR   A CA  1 
ATOM   769  C  C   . TYR   A 1 90  ? 29.492 -23.954 21.990 1.00 19.68  ? 91  TYR   A C   1 
ATOM   770  O  O   . TYR   A 1 90  ? 29.972 -24.905 21.356 1.00 19.11  ? 91  TYR   A O   1 
ATOM   771  C  CB  . TYR   A 1 90  ? 31.632 -22.824 22.618 1.00 16.36  ? 91  TYR   A CB  1 
ATOM   772  C  CG  . TYR   A 1 90  ? 32.672 -21.832 22.125 1.00 17.35  ? 91  TYR   A CG  1 
ATOM   773  C  CD1 . TYR   A 1 90  ? 32.822 -20.590 22.735 1.00 19.18  ? 91  TYR   A CD1 1 
ATOM   774  C  CD2 . TYR   A 1 90  ? 33.542 -22.163 21.081 1.00 18.63  ? 91  TYR   A CD2 1 
ATOM   775  C  CE1 . TYR   A 1 90  ? 33.789 -19.675 22.291 1.00 18.26  ? 91  TYR   A CE1 1 
ATOM   776  C  CE2 . TYR   A 1 90  ? 34.542 -21.275 20.657 1.00 19.13  ? 91  TYR   A CE2 1 
ATOM   777  C  CZ  . TYR   A 1 90  ? 34.649 -20.031 21.258 1.00 20.40  ? 91  TYR   A CZ  1 
ATOM   778  O  OH  . TYR   A 1 90  ? 35.665 -19.196 20.860 1.00 18.42  ? 91  TYR   A OH  1 
ATOM   779  N  N   . THR   A 1 91  ? 28.325 -24.050 22.673 1.00 16.79  ? 92  THR   A N   1 
ATOM   780  C  CA  . THR   A 1 91  ? 27.623 -25.358 22.729 1.00 17.21  ? 92  THR   A CA  1 
ATOM   781  C  C   . THR   A 1 91  ? 26.106 -25.354 22.491 1.00 20.11  ? 92  THR   A C   1 
ATOM   782  O  O   . THR   A 1 91  ? 25.541 -26.454 22.288 1.00 19.15  ? 92  THR   A O   1 
ATOM   783  C  CB  . THR   A 1 91  ? 27.802 -26.015 24.131 1.00 19.95  ? 92  THR   A CB  1 
ATOM   784  O  OG1 . THR   A 1 91  ? 27.140 -25.217 25.131 1.00 20.65  ? 92  THR   A OG1 1 
ATOM   785  C  CG2 . THR   A 1 91  ? 29.268 -26.261 24.511 1.00 21.09  ? 92  THR   A CG2 1 
ATOM   786  N  N   A SER   A 1 92  ? 25.450 -24.168 22.572 0.67 16.67  ? 93  SER   A N   1 
ATOM   787  N  N   B SER   A 1 92  ? 25.454 -24.171 22.610 0.33 17.20  ? 93  SER   A N   1 
ATOM   788  C  CA  A SER   A 1 92  ? 23.978 -23.963 22.521 0.67 16.78  ? 93  SER   A CA  1 
ATOM   789  C  CA  B SER   A 1 92  ? 23.994 -23.943 22.564 0.33 17.59  ? 93  SER   A CA  1 
ATOM   790  C  C   A SER   A 1 92  ? 23.324 -24.346 23.870 0.67 18.99  ? 93  SER   A C   1 
ATOM   791  C  C   B SER   A 1 92  ? 23.319 -24.462 23.856 0.33 21.21  ? 93  SER   A C   1 
ATOM   792  O  O   A SER   A 1 92  ? 22.135 -24.105 24.049 0.67 18.57  ? 93  SER   A O   1 
ATOM   793  O  O   B SER   A 1 92  ? 22.092 -24.522 23.923 0.33 21.25  ? 93  SER   A O   1 
ATOM   794  C  CB  A SER   A 1 92  ? 23.316 -24.759 21.390 0.67 17.35  ? 93  SER   A CB  1 
ATOM   795  C  CB  B SER   A 1 92  ? 23.351 -24.550 21.313 0.33 20.17  ? 93  SER   A CB  1 
ATOM   796  O  OG  A SER   A 1 92  ? 23.944 -24.554 20.137 0.67 15.89  ? 93  SER   A OG  1 
ATOM   797  O  OG  B SER   A 1 92  ? 23.049 -25.929 21.458 0.33 25.34  ? 93  SER   A OG  1 
ATOM   798  N  N   A ARG   A 1 93  ? 24.108 -24.894 24.830 0.67 17.36  ? 94  ARG   A N   1 
ATOM   799  N  N   B ARG   A 1 93  ? 24.131 -24.813 24.882 0.33 18.61  ? 94  ARG   A N   1 
ATOM   800  C  CA  A ARG   A 1 93  ? 23.581 -25.312 26.141 0.67 17.59  ? 94  ARG   A CA  1 
ATOM   801  C  CA  B ARG   A 1 93  ? 23.667 -25.342 26.171 0.33 19.08  ? 94  ARG   A CA  1 
ATOM   802  C  C   A ARG   A 1 93  ? 23.823 -24.253 27.203 0.67 21.55  ? 94  ARG   A C   1 
ATOM   803  C  C   B ARG   A 1 93  ? 23.858 -24.295 27.263 0.33 22.62  ? 94  ARG   A C   1 
ATOM   804  O  O   A ARG   A 1 93  ? 24.952 -23.788 27.385 0.67 20.04  ? 94  ARG   A O   1 
ATOM   805  O  O   B ARG   A 1 93  ? 24.983 -23.840 27.493 0.33 21.46  ? 94  ARG   A O   1 
ATOM   806  C  CB  A ARG   A 1 93  ? 24.189 -26.652 26.586 0.67 21.28  ? 94  ARG   A CB  1 
ATOM   807  C  CB  B ARG   A 1 93  ? 24.416 -26.648 26.535 0.33 21.20  ? 94  ARG   A CB  1 
ATOM   808  C  CG  A ARG   A 1 93  ? 23.909 -27.810 25.617 0.67 24.81  ? 94  ARG   A CG  1 
ATOM   809  C  CG  B ARG   A 1 93  ? 24.314 -27.758 25.479 0.33 29.74  ? 94  ARG   A CG  1 
ATOM   810  C  CD  A ARG   A 1 93  ? 24.895 -28.953 25.855 0.67 29.38  ? 94  ARG   A CD  1 
ATOM   811  C  CD  B ARG   A 1 93  ? 23.094 -28.633 25.681 0.33 35.25  ? 94  ARG   A CD  1 
ATOM   812  N  NE  A ARG   A 1 93  ? 24.801 -29.468 27.225 0.67 37.46  ? 94  ARG   A NE  1 
ATOM   813  N  NE  B ARG   A 1 93  ? 22.960 -29.656 24.641 0.33 38.37  ? 94  ARG   A NE  1 
ATOM   814  C  CZ  A ARG   A 1 93  ? 23.986 -30.449 27.595 0.67 50.92  ? 94  ARG   A CZ  1 
ATOM   815  C  CZ  B ARG   A 1 93  ? 23.233 -30.945 24.817 0.33 50.84  ? 94  ARG   A CZ  1 
ATOM   816  N  NH1 A ARG   A 1 93  ? 23.205 -31.044 26.703 0.67 41.07  ? 94  ARG   A NH1 1 
ATOM   817  N  NH1 B ARG   A 1 93  ? 23.065 -31.806 23.822 0.33 41.53  ? 94  ARG   A NH1 1 
ATOM   818  N  NH2 A ARG   A 1 93  ? 23.952 -30.849 28.857 0.67 38.70  ? 94  ARG   A NH2 1 
ATOM   819  N  NH2 B ARG   A 1 93  ? 23.660 -31.386 25.992 0.33 32.91  ? 94  ARG   A NH2 1 
ATOM   820  N  N   . LEU   A 1 94  ? 22.763 -23.924 27.945 1.00 19.93  ? 95  LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 94  ? 22.810 -22.913 28.999 1.00 19.35  ? 95  LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 94  ? 22.580 -23.547 30.353 1.00 24.50  ? 95  LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 94  ? 21.517 -24.141 30.590 1.00 23.77  ? 95  LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 94  ? 21.755 -21.840 28.712 1.00 19.77  ? 95  LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 94  ? 21.810 -20.619 29.652 1.00 22.79  ? 95  LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 94  ? 23.096 -19.778 29.390 1.00 22.23  ? 95  LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 94  ? 20.541 -19.774 29.513 1.00 25.66  ? 95  LEU   A CD2 1 
ATOM   828  N  N   . ASN   A 1 95  ? 23.577 -23.425 31.254 1.00 23.18  ? 96  ASN   A N   1 
ATOM   829  C  CA  . ASN   A 1 95  ? 23.474 -23.995 32.604 1.00 24.42  ? 96  ASN   A CA  1 
ATOM   830  C  C   . ASN   A 1 95  ? 22.757 -22.991 33.524 1.00 29.18  ? 96  ASN   A C   1 
ATOM   831  O  O   . ASN   A 1 95  ? 23.390 -22.300 34.317 1.00 28.91  ? 96  ASN   A O   1 
ATOM   832  C  CB  . ASN   A 1 95  ? 24.869 -24.388 33.143 1.00 28.74  ? 96  ASN   A CB  1 
ATOM   833  C  CG  . ASN   A 1 95  ? 24.835 -25.015 34.532 1.00 45.69  ? 96  ASN   A CG  1 
ATOM   834  O  OD1 . ASN   A 1 95  ? 23.833 -25.579 34.956 1.00 36.52  ? 96  ASN   A OD1 1 
ATOM   835  N  ND2 . ASN   A 1 95  ? 25.923 -24.907 35.280 1.00 38.90  ? 96  ASN   A ND2 1 
ATOM   836  N  N   . LEU   A 1 96  ? 21.440 -22.884 33.364 1.00 26.87  ? 97  LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 96  ? 20.620 -21.940 34.110 1.00 28.05  ? 97  LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 96  ? 20.103 -22.598 35.382 1.00 31.84  ? 97  LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 96  ? 19.454 -23.652 35.325 1.00 31.29  ? 97  LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 96  ? 19.496 -21.457 33.180 1.00 28.98  ? 97  LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 96  ? 18.744 -20.195 33.540 1.00 35.56  ? 97  LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 96  ? 19.711 -18.983 33.653 1.00 35.99  ? 97  LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 96  ? 17.643 -19.936 32.507 1.00 35.63  ? 97  LEU   A CD2 1 
ATOM   844  N  N   . ARG   A 1 97  ? 20.475 -22.021 36.542 1.00 29.81  ? 98  ARG   A N   1 
ATOM   845  C  CA  . ARG   A 1 97  ? 20.119 -22.550 37.867 1.00 31.44  ? 98  ARG   A CA  1 
ATOM   846  C  C   . ARG   A 1 97  ? 19.580 -21.428 38.750 1.00 32.69  ? 98  ARG   A C   1 
ATOM   847  O  O   . ARG   A 1 97  ? 19.868 -20.248 38.507 1.00 30.68  ? 98  ARG   A O   1 
ATOM   848  C  CB  . ARG   A 1 97  ? 21.352 -23.192 38.546 1.00 32.75  ? 98  ARG   A CB  1 
ATOM   849  C  CG  . ARG   A 1 97  ? 21.978 -24.349 37.757 1.00 38.41  ? 98  ARG   A CG  1 
ATOM   850  C  CD  . ARG   A 1 97  ? 23.201 -24.957 38.435 1.00 56.83  ? 98  ARG   A CD  1 
ATOM   851  N  NE  . ARG   A 1 97  ? 22.892 -25.559 39.738 1.00 74.16  ? 98  ARG   A NE  1 
ATOM   852  C  CZ  . ARG   A 1 97  ? 22.442 -26.799 39.917 1.00 94.86  ? 98  ARG   A CZ  1 
ATOM   853  N  NH1 . ARG   A 1 97  ? 22.183 -27.248 41.139 1.00 82.49  ? 98  ARG   A NH1 1 
ATOM   854  N  NH2 . ARG   A 1 97  ? 22.229 -27.594 38.873 1.00 85.30  ? 98  ARG   A NH2 1 
ATOM   855  N  N   . GLU   A 1 98  ? 18.787 -21.782 39.772 1.00 30.82  ? 99  GLU   A N   1 
ATOM   856  C  CA  . GLU   A 1 98  ? 18.252 -20.771 40.690 1.00 30.94  ? 99  GLU   A CA  1 
ATOM   857  C  C   . GLU   A 1 98  ? 19.366 -19.867 41.260 1.00 35.47  ? 99  GLU   A C   1 
ATOM   858  O  O   . GLU   A 1 98  ? 19.194 -18.648 41.325 1.00 34.95  ? 99  GLU   A O   1 
ATOM   859  C  CB  . GLU   A 1 98  ? 17.484 -21.450 41.843 1.00 33.73  ? 99  GLU   A CB  1 
ATOM   860  C  CG  . GLU   A 1 98  ? 16.747 -20.473 42.742 1.00 42.62  ? 99  GLU   A CG  1 
ATOM   861  C  CD  . GLU   A 1 98  ? 16.018 -21.096 43.919 1.00 69.32  ? 99  GLU   A CD  1 
ATOM   862  O  OE1 . GLU   A 1 98  ? 16.590 -21.992 44.584 1.00 59.84  ? 99  GLU   A OE1 1 
ATOM   863  O  OE2 . GLU   A 1 98  ? 14.870 -20.674 44.184 1.00 67.85  ? 99  GLU   A OE2 1 
ATOM   864  N  N   . GLY   A 1 99  ? 20.496 -20.473 41.623 1.00 33.84  ? 100 GLY   A N   1 
ATOM   865  C  CA  . GLY   A 1 99  ? 21.632 -19.765 42.213 1.00 34.02  ? 100 GLY   A CA  1 
ATOM   866  C  C   . GLY   A 1 99  ? 22.409 -18.855 41.276 1.00 34.72  ? 100 GLY   A C   1 
ATOM   867  O  O   . GLY   A 1 99  ? 23.126 -17.964 41.736 1.00 34.98  ? 100 GLY   A O   1 
ATOM   868  N  N   . ASN   A 1 100 ? 22.266 -19.045 39.956 1.00 30.45  ? 101 ASN   A N   1 
ATOM   869  C  CA  . ASN   A 1 100 ? 23.022 -18.234 39.004 1.00 27.71  ? 101 ASN   A CA  1 
ATOM   870  C  C   . ASN   A 1 100 ? 22.164 -17.383 38.053 1.00 31.65  ? 101 ASN   A C   1 
ATOM   871  O  O   . ASN   A 1 100 ? 22.732 -16.576 37.309 1.00 30.77  ? 101 ASN   A O   1 
ATOM   872  C  CB  . ASN   A 1 100 ? 23.995 -19.134 38.216 1.00 26.78  ? 101 ASN   A CB  1 
ATOM   873  C  CG  . ASN   A 1 100 ? 23.342 -20.073 37.216 1.00 36.00  ? 101 ASN   A CG  1 
ATOM   874  O  OD1 . ASN   A 1 100 ? 22.283 -19.787 36.659 1.00 26.86  ? 101 ASN   A OD1 1 
ATOM   875  N  ND2 . ASN   A 1 100 ? 23.985 -21.199 36.930 1.00 28.40  ? 101 ASN   A ND2 1 
ATOM   876  N  N   . ILE   A 1 101 ? 20.819 -17.589 38.027 1.00 29.33  ? 102 ILE   A N   1 
ATOM   877  C  CA  . ILE   A 1 101 ? 19.945 -16.926 37.039 1.00 28.92  ? 102 ILE   A CA  1 
ATOM   878  C  C   . ILE   A 1 101 ? 20.075 -15.392 37.030 1.00 29.00  ? 102 ILE   A C   1 
ATOM   879  O  O   . ILE   A 1 101 ? 20.094 -14.800 35.940 1.00 27.18  ? 102 ILE   A O   1 
ATOM   880  C  CB  . ILE   A 1 101 ? 18.461 -17.367 37.104 1.00 33.21  ? 102 ILE   A CB  1 
ATOM   881  C  CG1 . ILE   A 1 101 ? 17.651 -16.778 35.912 1.00 33.27  ? 102 ILE   A CG1 1 
ATOM   882  C  CG2 . ILE   A 1 101 ? 17.819 -17.066 38.470 1.00 33.57  ? 102 ILE   A CG2 1 
ATOM   883  C  CD1 . ILE   A 1 101 ? 16.512 -17.627 35.425 1.00 35.63  ? 102 ILE   A CD1 1 
ATOM   884  N  N   . MET   A 1 102 ? 20.177 -14.755 38.207 1.00 27.97  ? 103 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 102 ? 20.320 -13.299 38.248 1.00 27.68  ? 103 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 102 ? 21.632 -12.827 37.610 1.00 30.13  ? 103 MET   A C   1 
ATOM   887  O  O   . MET   A 1 102 ? 21.607 -11.891 36.803 1.00 27.49  ? 103 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 102 ? 20.135 -12.737 39.673 1.00 31.64  ? 103 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 102 ? 18.757 -13.039 40.274 1.00 38.24  ? 103 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 102 ? 17.326 -12.595 39.240 1.00 43.82  ? 103 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 102 ? 17.343 -10.825 39.390 1.00 42.23  ? 103 MET   A CE  1 
ATOM   892  N  N   . ALA   A 1 103 ? 22.768 -13.506 37.922 1.00 28.13  ? 104 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 103 ? 24.077 -13.151 37.339 1.00 27.83  ? 104 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 103 ? 24.097 -13.444 35.842 1.00 28.87  ? 104 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 103 ? 24.635 -12.648 35.064 1.00 27.12  ? 104 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 103 ? 25.199 -13.912 38.035 1.00 29.59  ? 104 ALA   A CB  1 
ATOM   897  N  N   . VAL   A 1 104 ? 23.503 -14.566 35.431 1.00 24.62  ? 105 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 104 ? 23.449 -14.917 34.001 1.00 21.53  ? 105 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 104 ? 22.642 -13.880 33.209 1.00 24.66  ? 105 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 104 ? 23.130 -13.421 32.169 1.00 23.71  ? 105 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 104 ? 22.957 -16.374 33.776 1.00 24.48  ? 105 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 104 ? 22.686 -16.659 32.292 1.00 22.82  ? 105 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 104 ? 23.979 -17.365 34.315 1.00 24.55  ? 105 VAL   A CG2 1 
ATOM   904  N  N   A MET   A 1 105 ? 21.438 -13.504 33.698 0.20 23.21  ? 106 MET   A N   1 
ATOM   905  N  N   B MET   A 1 105 ? 21.426 -13.507 33.691 0.80 23.56  ? 106 MET   A N   1 
ATOM   906  C  CA  A MET   A 1 105 ? 20.579 -12.514 33.039 0.20 23.89  ? 106 MET   A CA  1 
ATOM   907  C  CA  B MET   A 1 105 ? 20.602 -12.509 32.988 0.80 24.62  ? 106 MET   A CA  1 
ATOM   908  C  C   A MET   A 1 105 ? 21.277 -11.159 32.900 0.20 28.09  ? 106 MET   A C   1 
ATOM   909  C  C   B MET   A 1 105 ? 21.309 -11.149 32.881 0.80 27.76  ? 106 MET   A C   1 
ATOM   910  O  O   A MET   A 1 105 ? 21.249 -10.572 31.817 0.20 27.15  ? 106 MET   A O   1 
ATOM   911  O  O   B MET   A 1 105 ? 21.305 -10.536 31.808 0.80 26.02  ? 106 MET   A O   1 
ATOM   912  C  CB  A MET   A 1 105 ? 19.246 -12.356 33.779 0.20 27.36  ? 106 MET   A CB  1 
ATOM   913  C  CB  B MET   A 1 105 ? 19.228 -12.341 33.645 0.80 27.64  ? 106 MET   A CB  1 
ATOM   914  C  CG  A MET   A 1 105 ? 18.267 -11.478 33.040 0.20 31.28  ? 106 MET   A CG  1 
ATOM   915  C  CG  B MET   A 1 105 ? 18.303 -11.419 32.852 0.80 30.73  ? 106 MET   A CG  1 
ATOM   916  S  SD  A MET   A 1 105 ? 16.775 -11.172 33.990 0.20 36.65  ? 106 MET   A SD  1 
ATOM   917  S  SD  B MET   A 1 105 ? 16.609 -11.397 33.483 0.80 34.72  ? 106 MET   A SD  1 
ATOM   918  C  CE  A MET   A 1 105 ? 16.136 -9.799  33.104 0.20 33.98  ? 106 MET   A CE  1 
ATOM   919  C  CE  B MET   A 1 105 ? 16.805 -10.430 35.043 0.80 32.84  ? 106 MET   A CE  1 
ATOM   920  N  N   . ALA   A 1 106 ? 21.901 -10.672 33.992 1.00 25.71  ? 107 ALA   A N   1 
ATOM   921  C  CA  . ALA   A 1 106 ? 22.628 -9.385  34.001 1.00 25.75  ? 107 ALA   A CA  1 
ATOM   922  C  C   . ALA   A 1 106 ? 23.799 -9.415  32.999 1.00 26.58  ? 107 ALA   A C   1 
ATOM   923  O  O   . ALA   A 1 106 ? 23.967 -8.463  32.220 1.00 24.98  ? 107 ALA   A O   1 
ATOM   924  C  CB  . ALA   A 1 106 ? 23.127 -9.072  35.406 1.00 27.02  ? 107 ALA   A CB  1 
ATOM   925  N  N   . THR   A 1 107 ? 24.538 -10.545 32.949 1.00 22.26  ? 108 THR   A N   1 
ATOM   926  C  CA  . THR   A 1 107 ? 25.647 -10.699 32.006 1.00 21.51  ? 108 THR   A CA  1 
ATOM   927  C  C   . THR   A 1 107 ? 25.123 -10.739 30.551 1.00 24.42  ? 108 THR   A C   1 
ATOM   928  O  O   . THR   A 1 107 ? 25.708 -10.079 29.684 1.00 22.03  ? 108 THR   A O   1 
ATOM   929  C  CB  . THR   A 1 107 ? 26.578 -11.882 32.378 1.00 25.25  ? 108 THR   A CB  1 
ATOM   930  O  OG1 . THR   A 1 107 ? 26.878 -11.856 33.784 1.00 24.78  ? 108 THR   A OG1 1 
ATOM   931  C  CG2 . THR   A 1 107 ? 27.887 -11.874 31.573 1.00 25.31  ? 108 THR   A CG2 1 
ATOM   932  N  N   . ALA   A 1 108 ? 24.022 -11.496 30.289 1.00 21.81  ? 109 ALA   A N   1 
ATOM   933  C  CA  . ALA   A 1 108 ? 23.435 -11.588 28.944 1.00 20.69  ? 109 ALA   A CA  1 
ATOM   934  C  C   . ALA   A 1 108 ? 22.902 -10.231 28.468 1.00 23.26  ? 109 ALA   A C   1 
ATOM   935  O  O   . ALA   A 1 108 ? 23.078 -9.887  27.295 1.00 22.35  ? 109 ALA   A O   1 
ATOM   936  C  CB  . ALA   A 1 108 ? 22.347 -12.657 28.902 1.00 21.30  ? 109 ALA   A CB  1 
ATOM   937  N  N   . MET   A 1 109 ? 22.334 -9.411  29.388 1.00 21.79  ? 110 MET   A N   1 
ATOM   938  C  CA  . MET   A 1 109 ? 21.897 -8.056  29.015 1.00 21.50  ? 110 MET   A CA  1 
ATOM   939  C  C   . MET   A 1 109 ? 23.109 -7.179  28.581 1.00 24.65  ? 110 MET   A C   1 
ATOM   940  O  O   . MET   A 1 109 ? 23.077 -6.522  27.540 1.00 24.63  ? 110 MET   A O   1 
ATOM   941  C  CB  . MET   A 1 109 ? 21.135 -7.419  30.189 1.00 24.49  ? 110 MET   A CB  1 
ATOM   942  C  CG  . MET   A 1 109 ? 19.760 -8.025  30.395 1.00 28.75  ? 110 MET   A CG  1 
ATOM   943  S  SD  . MET   A 1 109 ? 19.030 -7.445  31.950 1.00 35.73  ? 110 MET   A SD  1 
ATOM   944  C  CE  . MET   A 1 109 ? 18.754 -5.694  31.521 1.00 33.92  ? 110 MET   A CE  1 
ATOM   945  N  N   . TYR   A 1 110 ? 24.182 -7.212  29.365 1.00 21.90  ? 111 TYR   A N   1 
ATOM   946  C  CA  . TYR   A 1 110 ? 25.425 -6.477  29.074 1.00 21.37  ? 111 TYR   A CA  1 
ATOM   947  C  C   . TYR   A 1 110 ? 26.031 -6.950  27.741 1.00 23.94  ? 111 TYR   A C   1 
ATOM   948  O  O   . TYR   A 1 110 ? 26.408 -6.124  26.893 1.00 21.36  ? 111 TYR   A O   1 
ATOM   949  C  CB  . TYR   A 1 110 ? 26.411 -6.726  30.218 1.00 21.44  ? 111 TYR   A CB  1 
ATOM   950  C  CG  . TYR   A 1 110 ? 27.818 -6.217  29.976 1.00 21.13  ? 111 TYR   A CG  1 
ATOM   951  C  CD1 . TYR   A 1 110 ? 28.116 -4.858  30.076 1.00 24.45  ? 111 TYR   A CD1 1 
ATOM   952  C  CD2 . TYR   A 1 110 ? 28.868 -7.103  29.744 1.00 20.72  ? 111 TYR   A CD2 1 
ATOM   953  C  CE1 . TYR   A 1 110 ? 29.421 -4.387  29.872 1.00 22.00  ? 111 TYR   A CE1 1 
ATOM   954  C  CE2 . TYR   A 1 110 ? 30.177 -6.651  29.582 1.00 20.54  ? 111 TYR   A CE2 1 
ATOM   955  C  CZ  . TYR   A 1 110 ? 30.447 -5.294  29.654 1.00 24.22  ? 111 TYR   A CZ  1 
ATOM   956  O  OH  . TYR   A 1 110 ? 31.746 -4.896  29.526 1.00 22.62  ? 111 TYR   A OH  1 
ATOM   957  N  N   . LEU   A 1 111 ? 26.081 -8.276  27.541 1.00 21.64  ? 112 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 111 ? 26.647 -8.864  26.319 1.00 19.74  ? 112 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 111 ? 25.712 -8.760  25.114 1.00 22.80  ? 112 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 111 ? 26.140 -9.026  23.990 1.00 21.65  ? 112 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 111 ? 27.052 -10.331 26.553 1.00 18.63  ? 112 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 111 ? 28.188 -10.602 27.555 1.00 20.75  ? 112 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 111 ? 28.493 -12.121 27.632 1.00 20.54  ? 112 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 111 ? 29.484 -9.844  27.172 1.00 21.63  ? 112 LEU   A CD2 1 
ATOM   965  N  N   . GLN   A 1 112 ? 24.441 -8.373  25.335 1.00 20.33  ? 113 GLN   A N   1 
ATOM   966  C  CA  . GLN   A 1 112 ? 23.449 -8.256  24.256 1.00 20.14  ? 113 GLN   A CA  1 
ATOM   967  C  C   . GLN   A 1 112 ? 23.207 -9.619  23.586 1.00 22.92  ? 113 GLN   A C   1 
ATOM   968  O  O   . GLN   A 1 112 ? 23.447 -9.809  22.396 1.00 21.95  ? 113 GLN   A O   1 
ATOM   969  C  CB  . GLN   A 1 112 ? 23.812 -7.148  23.246 1.00 20.95  ? 113 GLN   A CB  1 
ATOM   970  C  CG  . GLN   A 1 112 ? 23.978 -5.759  23.907 1.00 24.11  ? 113 GLN   A CG  1 
ATOM   971  C  CD  . GLN   A 1 112 ? 24.688 -4.798  22.988 1.00 33.76  ? 113 GLN   A CD  1 
ATOM   972  O  OE1 . GLN   A 1 112 ? 24.582 -4.882  21.773 1.00 27.95  ? 113 GLN   A OE1 1 
ATOM   973  N  NE2 . GLN   A 1 112 ? 25.440 -3.866  23.549 1.00 32.34  ? 113 GLN   A NE2 1 
ATOM   974  N  N   . MET   A 1 113 ? 22.759 -10.571 24.402 1.00 20.02  ? 114 MET   A N   1 
ATOM   975  C  CA  . MET   A 1 113 ? 22.426 -11.944 23.988 1.00 19.47  ? 114 MET   A CA  1 
ATOM   976  C  C   . MET   A 1 113 ? 20.924 -12.102 24.254 1.00 25.92  ? 114 MET   A C   1 
ATOM   977  O  O   . MET   A 1 113 ? 20.499 -12.585 25.312 1.00 24.53  ? 114 MET   A O   1 
ATOM   978  C  CB  . MET   A 1 113 ? 23.294 -12.913 24.790 1.00 20.02  ? 114 MET   A CB  1 
ATOM   979  C  CG  . MET   A 1 113 ? 24.769 -12.772 24.456 1.00 20.93  ? 114 MET   A CG  1 
ATOM   980  S  SD  . MET   A 1 113 ? 25.801 -13.806 25.499 1.00 23.90  ? 114 MET   A SD  1 
ATOM   981  C  CE  . MET   A 1 113 ? 25.446 -15.463 24.752 1.00 21.23  ? 114 MET   A CE  1 
ATOM   982  N  N   . GLU   A 1 114 ? 20.121 -11.593 23.302 1.00 25.13  ? 115 GLU   A N   1 
ATOM   983  C  CA  . GLU   A 1 114 ? 18.658 -11.462 23.413 1.00 26.77  ? 115 GLU   A CA  1 
ATOM   984  C  C   . GLU   A 1 114 ? 17.911 -12.736 23.769 1.00 27.44  ? 115 GLU   A C   1 
ATOM   985  O  O   . GLU   A 1 114 ? 17.019 -12.673 24.614 1.00 27.26  ? 115 GLU   A O   1 
ATOM   986  C  CB  . GLU   A 1 114 ? 18.049 -10.837 22.147 1.00 29.60  ? 115 GLU   A CB  1 
ATOM   987  C  CG  . GLU   A 1 114 ? 18.586 -9.443  21.866 1.00 41.69  ? 115 GLU   A CG  1 
ATOM   988  N  N   . HIS   A 1 115 ? 18.243 -13.875 23.138 1.00 24.84  ? 116 HIS   A N   1 
ATOM   989  C  CA  . HIS   A 1 115 ? 17.513 -15.115 23.443 1.00 26.18  ? 116 HIS   A CA  1 
ATOM   990  C  C   . HIS   A 1 115 ? 17.755 -15.593 24.880 1.00 27.54  ? 116 HIS   A C   1 
ATOM   991  O  O   . HIS   A 1 115 ? 16.817 -16.066 25.535 1.00 27.66  ? 116 HIS   A O   1 
ATOM   992  C  CB  . HIS   A 1 115 ? 17.819 -16.206 22.410 1.00 28.09  ? 116 HIS   A CB  1 
ATOM   993  C  CG  . HIS   A 1 115 ? 17.377 -15.846 21.026 1.00 33.07  ? 116 HIS   A CG  1 
ATOM   994  N  ND1 . HIS   A 1 115 ? 16.044 -15.625 20.732 1.00 36.93  ? 116 HIS   A ND1 1 
ATOM   995  C  CD2 . HIS   A 1 115 ? 18.099 -15.741 19.886 1.00 34.85  ? 116 HIS   A CD2 1 
ATOM   996  C  CE1 . HIS   A 1 115 ? 16.001 -15.348 19.438 1.00 36.58  ? 116 HIS   A CE1 1 
ATOM   997  N  NE2 . HIS   A 1 115 ? 17.210 -15.409 18.887 1.00 35.75  ? 116 HIS   A NE2 1 
ATOM   998  N  N   . VAL   A 1 116 ? 19.002 -15.431 25.386 1.00 21.87  ? 117 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 116 ? 19.337 -15.795 26.772 1.00 21.71  ? 117 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 116 ? 18.551 -14.885 27.729 1.00 27.70  ? 117 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 116 ? 17.942 -15.379 28.683 1.00 26.92  ? 117 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 116 ? 20.862 -15.779 27.070 1.00 24.91  ? 117 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 116 ? 21.127 -16.024 28.559 1.00 25.09  ? 117 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 116 ? 21.583 -16.825 26.221 1.00 24.14  ? 117 VAL   A CG2 1 
ATOM   1005 N  N   . VAL   A 1 117 ? 18.546 -13.563 27.457 1.00 23.70  ? 118 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 117 ? 17.789 -12.600 28.285 1.00 24.50  ? 118 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 117 ? 16.298 -13.030 28.366 1.00 29.75  ? 118 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 117 ? 15.750 -13.118 29.464 1.00 28.50  ? 118 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 117 ? 17.969 -11.122 27.825 1.00 27.17  ? 118 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 117 ? 17.129 -10.170 28.694 1.00 27.76  ? 118 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 117 ? 19.438 -10.706 27.865 1.00 26.03  ? 118 VAL   A CG2 1 
ATOM   1012 N  N   A ASP   A 1 118 ? 15.700 -13.386 27.213 0.61 27.80  ? 119 ASP   A N   1 
ATOM   1013 N  N   B ASP   A 1 118 ? 15.665 -13.280 27.202 0.39 27.61  ? 119 ASP   A N   1 
ATOM   1014 C  CA  A ASP   A 1 118 ? 14.314 -13.845 27.102 0.61 28.98  ? 119 ASP   A CA  1 
ATOM   1015 C  CA  B ASP   A 1 118 ? 14.259 -13.683 27.077 0.39 28.81  ? 119 ASP   A CA  1 
ATOM   1016 C  C   A ASP   A 1 118 ? 14.017 -15.071 27.975 0.61 31.66  ? 119 ASP   A C   1 
ATOM   1017 C  C   B ASP   A 1 118 ? 13.891 -14.889 27.941 0.39 32.60  ? 119 ASP   A C   1 
ATOM   1018 O  O   A ASP   A 1 118 ? 13.040 -15.032 28.728 0.61 32.37  ? 119 ASP   A O   1 
ATOM   1019 O  O   B ASP   A 1 118 ? 12.877 -14.844 28.638 0.39 33.43  ? 119 ASP   A O   1 
ATOM   1020 C  CB  A ASP   A 1 118 ? 13.949 -14.118 25.630 0.61 31.21  ? 119 ASP   A CB  1 
ATOM   1021 C  CB  B ASP   A 1 118 ? 13.904 -13.958 25.600 0.39 30.75  ? 119 ASP   A CB  1 
ATOM   1022 C  CG  A ASP   A 1 118 ? 12.490 -14.479 25.412 0.61 43.58  ? 119 ASP   A CG  1 
ATOM   1023 C  CG  B ASP   A 1 118 ? 13.707 -12.726 24.734 0.39 40.35  ? 119 ASP   A CG  1 
ATOM   1024 O  OD1 A ASP   A 1 118 ? 11.618 -13.649 25.742 0.61 46.00  ? 119 ASP   A OD1 1 
ATOM   1025 O  OD1 B ASP   A 1 118 ? 13.329 -11.669 25.280 0.39 42.72  ? 119 ASP   A OD1 1 
ATOM   1026 O  OD2 A ASP   A 1 118 ? 12.225 -15.586 24.902 0.61 48.98  ? 119 ASP   A OD2 1 
ATOM   1027 O  OD2 B ASP   A 1 118 ? 13.905 -12.828 23.505 0.39 46.15  ? 119 ASP   A OD2 1 
ATOM   1028 N  N   A THR   A 1 119 ? 14.844 -16.150 27.894 0.61 26.86  ? 120 THR   A N   1 
ATOM   1029 N  N   B THR   A 1 119 ? 14.718 -15.953 27.909 0.39 28.21  ? 120 THR   A N   1 
ATOM   1030 C  CA  A THR   A 1 119 ? 14.575 -17.344 28.720 0.61 27.07  ? 120 THR   A CA  1 
ATOM   1031 C  CA  B THR   A 1 119 ? 14.463 -17.181 28.672 0.39 28.45  ? 120 THR   A CA  1 
ATOM   1032 C  C   A THR   A 1 119 ? 14.774 -17.069 30.213 0.61 30.32  ? 120 THR   A C   1 
ATOM   1033 C  C   B THR   A 1 119 ? 14.682 -16.961 30.176 0.39 31.44  ? 120 THR   A C   1 
ATOM   1034 O  O   A THR   A 1 119 ? 14.094 -17.688 31.033 0.61 29.65  ? 120 THR   A O   1 
ATOM   1035 O  O   B THR   A 1 119 ? 13.913 -17.502 30.973 0.39 31.48  ? 120 THR   A O   1 
ATOM   1036 C  CB  A THR   A 1 119 ? 15.332 -18.601 28.254 0.61 27.64  ? 120 THR   A CB  1 
ATOM   1037 C  CB  B THR   A 1 119 ? 15.244 -18.362 28.094 0.39 34.36  ? 120 THR   A CB  1 
ATOM   1038 O  OG1 A THR   A 1 119 ? 14.744 -19.727 28.914 0.61 29.08  ? 120 THR   A OG1 1 
ATOM   1039 O  OG1 B THR   A 1 119 ? 15.216 -18.272 26.669 0.39 33.12  ? 120 THR   A OG1 1 
ATOM   1040 C  CG2 A THR   A 1 119 ? 16.831 -18.556 28.565 0.61 21.84  ? 120 THR   A CG2 1 
ATOM   1041 C  CG2 B THR   A 1 119 ? 14.655 -19.698 28.511 0.39 34.36  ? 120 THR   A CG2 1 
ATOM   1042 N  N   . CYS   A 1 120 ? 15.702 -16.154 30.560 1.00 27.31  ? 121 CYS   A N   1 
ATOM   1043 C  CA  . CYS   A 1 120 ? 15.961 -15.788 31.970 1.00 27.67  ? 121 CYS   A CA  1 
ATOM   1044 C  C   . CYS   A 1 120 ? 14.738 -15.076 32.516 1.00 33.49  ? 121 CYS   A C   1 
ATOM   1045 O  O   . CYS   A 1 120 ? 14.280 -15.424 33.619 1.00 33.14  ? 121 CYS   A O   1 
ATOM   1046 C  CB  . CYS   A 1 120 ? 17.199 -14.910 32.094 1.00 27.07  ? 121 CYS   A CB  1 
ATOM   1047 S  SG  . CYS   A 1 120 ? 18.757 -15.802 31.898 1.00 29.08  ? 121 CYS   A SG  1 
ATOM   1048 N  N   A ARG   A 1 121 ? 14.188 -14.111 31.734 0.48 31.07  ? 122 ARG   A N   1 
ATOM   1049 N  N   B ARG   A 1 121 ? 14.190 -14.098 31.753 0.52 31.33  ? 122 ARG   A N   1 
ATOM   1050 C  CA  A ARG   A 1 121 ? 12.988 -13.337 32.087 0.48 32.88  ? 122 ARG   A CA  1 
ATOM   1051 C  CA  B ARG   A 1 121 ? 12.993 -13.349 32.157 0.52 33.22  ? 122 ARG   A CA  1 
ATOM   1052 C  C   A ARG   A 1 121 ? 11.806 -14.277 32.355 0.48 37.42  ? 122 ARG   A C   1 
ATOM   1053 C  C   B ARG   A 1 121 ? 11.790 -14.280 32.365 0.52 37.53  ? 122 ARG   A C   1 
ATOM   1054 O  O   A ARG   A 1 121 ? 11.078 -14.093 33.335 0.48 37.95  ? 122 ARG   A O   1 
ATOM   1055 O  O   B ARG   A 1 121 ? 11.033 -14.097 33.323 0.52 37.99  ? 122 ARG   A O   1 
ATOM   1056 C  CB  A ARG   A 1 121 ? 12.612 -12.349 30.963 0.48 34.07  ? 122 ARG   A CB  1 
ATOM   1057 C  CB  B ARG   A 1 121 ? 12.659 -12.241 31.148 0.52 35.00  ? 122 ARG   A CB  1 
ATOM   1058 C  CG  A ARG   A 1 121 ? 13.564 -11.171 30.800 0.48 45.66  ? 122 ARG   A CG  1 
ATOM   1059 C  CG  B ARG   A 1 121 ? 13.434 -10.947 31.378 0.52 49.07  ? 122 ARG   A CG  1 
ATOM   1060 C  CD  A ARG   A 1 121 ? 12.904 -9.996  30.097 0.48 58.89  ? 122 ARG   A CD  1 
ATOM   1061 C  CD  B ARG   A 1 121 ? 12.729 -9.745  30.765 0.52 60.05  ? 122 ARG   A CD  1 
ATOM   1062 N  NE  A ARG   A 1 121 ? 13.884 -8.992  29.677 0.48 63.69  ? 122 ARG   A NE  1 
ATOM   1063 N  NE  B ARG   A 1 121 ? 12.863 -9.706  29.306 0.52 64.60  ? 122 ARG   A NE  1 
ATOM   1064 C  CZ  A ARG   A 1 121 ? 14.281 -7.962  30.419 0.48 74.38  ? 122 ARG   A CZ  1 
ATOM   1065 C  CZ  B ARG   A 1 121 ? 13.652 -8.865  28.643 0.52 73.52  ? 122 ARG   A CZ  1 
ATOM   1066 N  NH1 A ARG   A 1 121 ? 13.779 -7.776  31.633 0.48 66.07  ? 122 ARG   A NH1 1 
ATOM   1067 N  NH1 B ARG   A 1 121 ? 14.383 -7.971  29.300 0.52 56.63  ? 122 ARG   A NH1 1 
ATOM   1068 N  NH2 A ARG   A 1 121 ? 15.181 -7.108  29.951 0.48 54.59  ? 122 ARG   A NH2 1 
ATOM   1069 N  NH2 B ARG   A 1 121 ? 13.710 -8.906  27.319 0.52 58.54  ? 122 ARG   A NH2 1 
ATOM   1070 N  N   . LYS   A 1 122 ? 11.642 -15.296 31.494 1.00 33.88  ? 123 LYS   A N   1 
ATOM   1071 C  CA  . LYS   A 1 122 ? 10.559 -16.287 31.588 1.00 35.26  ? 123 LYS   A CA  1 
ATOM   1072 C  C   . LYS   A 1 122 ? 10.708 -17.203 32.801 1.00 39.01  ? 123 LYS   A C   1 
ATOM   1073 O  O   . LYS   A 1 122 ? 9.723  -17.413 33.516 1.00 38.77  ? 123 LYS   A O   1 
ATOM   1074 C  CB  . LYS   A 1 122 ? 10.417 -17.082 30.282 1.00 37.08  ? 123 LYS   A CB  1 
ATOM   1075 C  CG  . LYS   A 1 122 ? 9.881  -16.214 29.146 1.00 55.88  ? 123 LYS   A CG  1 
ATOM   1076 C  CD  . LYS   A 1 122 ? 9.756  -16.939 27.822 1.00 67.28  ? 123 LYS   A CD  1 
ATOM   1077 C  CE  . LYS   A 1 122 ? 9.328  -15.973 26.741 1.00 79.33  ? 123 LYS   A CE  1 
ATOM   1078 N  NZ  . LYS   A 1 122 ? 8.420  -16.607 25.752 1.00 91.10  ? 123 LYS   A NZ  1 
ATOM   1079 N  N   . PHE   A 1 123 ? 11.936 -17.713 33.061 1.00 34.07  ? 124 PHE   A N   1 
ATOM   1080 C  CA  . PHE   A 1 123 ? 12.202 -18.585 34.217 1.00 34.02  ? 124 PHE   A CA  1 
ATOM   1081 C  C   . PHE   A 1 123 ? 12.001 -17.837 35.532 1.00 38.79  ? 124 PHE   A C   1 
ATOM   1082 O  O   . PHE   A 1 123 ? 11.458 -18.409 36.482 1.00 36.96  ? 124 PHE   A O   1 
ATOM   1083 C  CB  . PHE   A 1 123 ? 13.606 -19.202 34.131 1.00 34.00  ? 124 PHE   A CB  1 
ATOM   1084 C  CG  . PHE   A 1 123 ? 13.722 -20.473 33.308 1.00 34.36  ? 124 PHE   A CG  1 
ATOM   1085 C  CD1 . PHE   A 1 123 ? 13.118 -20.575 32.056 1.00 36.73  ? 124 PHE   A CD1 1 
ATOM   1086 C  CD2 . PHE   A 1 123 ? 14.506 -21.536 33.748 1.00 36.14  ? 124 PHE   A CD2 1 
ATOM   1087 C  CE1 . PHE   A 1 123 ? 13.237 -21.749 31.293 1.00 37.17  ? 124 PHE   A CE1 1 
ATOM   1088 C  CE2 . PHE   A 1 123 ? 14.639 -22.703 32.975 1.00 37.16  ? 124 PHE   A CE2 1 
ATOM   1089 C  CZ  . PHE   A 1 123 ? 14.015 -22.794 31.750 1.00 34.80  ? 124 PHE   A CZ  1 
ATOM   1090 N  N   . ILE   A 1 124 ? 12.380 -16.542 35.569 1.00 35.03  ? 125 ILE   A N   1 
ATOM   1091 C  CA  . ILE   A 1 124 ? 12.179 -15.693 36.757 1.00 36.58  ? 125 ILE   A CA  1 
ATOM   1092 C  C   . ILE   A 1 124 ? 10.681 -15.448 37.001 1.00 43.44  ? 125 ILE   A C   1 
ATOM   1093 O  O   . ILE   A 1 124 ? 10.220 -15.595 38.141 1.00 44.28  ? 125 ILE   A O   1 
ATOM   1094 C  CB  . ILE   A 1 124 ? 13.018 -14.384 36.689 1.00 38.48  ? 125 ILE   A CB  1 
ATOM   1095 C  CG1 . ILE   A 1 124 ? 14.524 -14.707 36.807 1.00 37.49  ? 125 ILE   A CG1 1 
ATOM   1096 C  CG2 . ILE   A 1 124 ? 12.595 -13.374 37.797 1.00 40.88  ? 125 ILE   A CG2 1 
ATOM   1097 C  CD1 . ILE   A 1 124 ? 15.444 -13.642 36.283 1.00 42.15  ? 125 ILE   A CD1 1 
ATOM   1098 N  N   . LYS   A 1 125 ? 9.921  -15.120 35.926 1.00 41.62  ? 126 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 125 ? 8.474  -14.871 35.996 1.00 44.07  ? 126 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 125 ? 7.703  -16.088 36.526 1.00 48.46  ? 126 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 125 ? 6.737  -15.915 37.263 1.00 48.50  ? 126 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 125 ? 7.918  -14.439 34.632 1.00 47.43  ? 126 LYS   A CB  1 
ATOM   1103 N  N   . ALA   A 1 126 ? 8.148  -17.310 36.177 1.00 44.23  ? 127 ALA   A N   1 
ATOM   1104 C  CA  . ALA   A 1 126 ? 7.511  -18.550 36.638 1.00 45.70  ? 127 ALA   A CA  1 
ATOM   1105 C  C   . ALA   A 1 126 ? 7.669  -18.791 38.152 1.00 51.82  ? 127 ALA   A C   1 
ATOM   1106 O  O   . ALA   A 1 126 ? 6.809  -19.427 38.751 1.00 52.92  ? 127 ALA   A O   1 
ATOM   1107 C  CB  . ALA   A 1 126 ? 8.065  -19.738 35.859 1.00 44.96  ? 127 ALA   A CB  1 
ATOM   1108 N  N   . SER   A 1 127 ? 8.768  -18.311 38.755 1.00 49.59  ? 128 SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 127 ? 9.066  -18.513 40.176 1.00 51.99  ? 128 SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 127 ? 8.517  -17.423 41.112 1.00 59.70  ? 128 SER   A C   1 
ATOM   1111 O  O   . SER   A 1 127 ? 8.556  -17.609 42.332 1.00 61.70  ? 128 SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 127 ? 10.567 -18.692 40.386 1.00 55.22  ? 128 SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 127 ? 10.941 -20.055 40.253 1.00 65.81  ? 128 SER   A OG  1 
ATOM   1114 N  N   . GLU   A 1 128 ? 7.989  -16.307 40.559 1.00 56.36  ? 129 GLU   A N   1 
ATOM   1115 C  CA  . GLU   A 1 128 ? 7.442  -15.206 41.369 1.00 75.04  ? 129 GLU   A CA  1 
ATOM   1116 C  C   . GLU   A 1 128 ? 6.015  -15.475 41.868 1.00 113.03 ? 129 GLU   A C   1 
ATOM   1117 O  O   . GLU   A 1 128 ? 5.566  -16.619 41.903 1.00 78.47  ? 129 GLU   A O   1 
ATOM   1118 C  CB  . GLU   A 1 128 ? 7.543  -13.853 40.634 1.00 75.54  ? 129 GLU   A CB  1 
ATOM   1119 C  CG  . GLU   A 1 128 ? 6.495  -13.621 39.554 1.00 86.01  ? 129 GLU   A CG  1 
ATOM   1120 C  CD  . GLU   A 1 128 ? 6.656  -12.380 38.692 1.00 106.72 ? 129 GLU   A CD  1 
ATOM   1121 O  OE1 . GLU   A 1 128 ? 7.793  -11.864 38.575 1.00 97.68  ? 129 GLU   A OE1 1 
ATOM   1122 O  OE2 . GLU   A 1 128 ? 5.638  -11.935 38.116 1.00 101.16 ? 129 GLU   A OE2 1 
HETATM 1123 C  C   . ACE   B 2 1   ? 21.241 -35.125 5.847  1.00 25.16  ? 0   ACE   D C   1 
HETATM 1124 O  O   . ACE   B 2 1   ? 21.311 -33.984 6.337  1.00 25.59  ? 0   ACE   D O   1 
HETATM 1125 C  CH3 . ACE   B 2 1   ? 21.456 -36.351 6.713  1.00 25.53  ? 0   ACE   D CH3 1 
ATOM   1126 N  N   A TRP   B 2 2   ? 20.953 -35.364 4.568  0.66 23.24  ? 1   TRP   D N   1 
ATOM   1127 N  N   B TRP   B 2 2   ? 20.972 -35.361 4.561  0.34 24.29  ? 1   TRP   D N   1 
ATOM   1128 C  CA  A TRP   B 2 2   ? 20.737 -34.313 3.581  0.66 22.49  ? 1   TRP   D CA  1 
ATOM   1129 C  CA  B TRP   B 2 2   ? 20.683 -34.288 3.611  0.34 24.00  ? 1   TRP   D CA  1 
ATOM   1130 C  C   A TRP   B 2 2   ? 19.225 -34.178 3.269  0.66 26.86  ? 1   TRP   D C   1 
ATOM   1131 C  C   B TRP   B 2 2   ? 19.176 -34.151 3.441  0.34 27.07  ? 1   TRP   D C   1 
ATOM   1132 O  O   A TRP   B 2 2   ? 18.527 -35.195 3.154  0.66 26.76  ? 1   TRP   D O   1 
ATOM   1133 O  O   B TRP   B 2 2   ? 18.437 -35.138 3.542  0.34 26.54  ? 1   TRP   D O   1 
ATOM   1134 C  CB  A TRP   B 2 2   ? 21.541 -34.637 2.304  0.66 21.73  ? 1   TRP   D CB  1 
ATOM   1135 C  CB  B TRP   B 2 2   ? 21.360 -34.507 2.235  0.34 23.36  ? 1   TRP   D CB  1 
ATOM   1136 C  CG  A TRP   B 2 2   ? 23.035 -34.630 2.495  0.66 21.89  ? 1   TRP   D CG  1 
ATOM   1137 C  CG  B TRP   B 2 2   ? 20.744 -35.585 1.386  0.34 24.43  ? 1   TRP   D CG  1 
ATOM   1138 C  CD1 A TRP   B 2 2   ? 23.824 -35.668 2.903  0.66 24.46  ? 1   TRP   D CD1 1 
ATOM   1139 C  CD1 B TRP   B 2 2   ? 21.136 -36.888 1.315  0.34 27.50  ? 1   TRP   D CD1 1 
ATOM   1140 C  CD2 A TRP   B 2 2   ? 23.914 -33.522 2.271  0.66 21.40  ? 1   TRP   D CD2 1 
ATOM   1141 C  CD2 B TRP   B 2 2   ? 19.651 -35.444 0.461  0.34 24.51  ? 1   TRP   D CD2 1 
ATOM   1142 N  NE1 A TRP   B 2 2   ? 25.139 -35.264 2.977  0.66 23.72  ? 1   TRP   D NE1 1 
ATOM   1143 N  NE1 B TRP   B 2 2   ? 20.327 -37.581 0.447  0.34 27.15  ? 1   TRP   D NE1 1 
ATOM   1144 C  CE2 A TRP   B 2 2   ? 25.224 -33.952 2.589  0.66 24.73  ? 1   TRP   D CE2 1 
ATOM   1145 C  CE2 B TRP   B 2 2   ? 19.412 -36.718 -0.101 0.34 28.44  ? 1   TRP   D CE2 1 
ATOM   1146 C  CE3 A TRP   B 2 2   ? 23.718 -32.182 1.889  0.66 22.30  ? 1   TRP   D CE3 1 
ATOM   1147 C  CE3 B TRP   B 2 2   ? 18.820 -34.373 0.083  0.34 25.34  ? 1   TRP   D CE3 1 
ATOM   1148 C  CZ2 A TRP   B 2 2   ? 26.337 -33.112 2.470  0.66 24.52  ? 1   TRP   D CZ2 1 
ATOM   1149 C  CZ2 B TRP   B 2 2   ? 18.392 -36.947 -1.031 0.34 27.72  ? 1   TRP   D CZ2 1 
ATOM   1150 C  CZ3 A TRP   B 2 2   ? 24.825 -31.359 1.755  0.66 23.21  ? 1   TRP   D CZ3 1 
ATOM   1151 C  CZ3 B TRP   B 2 2   ? 17.810 -34.602 -0.839 0.34 27.00  ? 1   TRP   D CZ3 1 
ATOM   1152 C  CH2 A TRP   B 2 2   ? 26.113 -31.822 2.051  0.66 23.97  ? 1   TRP   D CH2 1 
ATOM   1153 C  CH2 B TRP   B 2 2   ? 17.607 -35.875 -1.388 0.34 27.50  ? 1   TRP   D CH2 1 
ATOM   1154 N  N   . VAL   B 2 3   ? 18.725 -32.931 3.150  1.00 23.01  ? 2   VAL   D N   1 
ATOM   1155 C  CA  . VAL   B 2 3   ? 17.306 -32.623 2.904  1.00 22.75  ? 2   VAL   D CA  1 
ATOM   1156 C  C   . VAL   B 2 3   ? 17.166 -31.565 1.801  1.00 24.88  ? 2   VAL   D C   1 
ATOM   1157 O  O   . VAL   B 2 3   ? 18.144 -30.903 1.435  1.00 23.23  ? 2   VAL   D O   1 
ATOM   1158 C  CB  . VAL   B 2 3   ? 16.587 -32.121 4.206  1.00 25.56  ? 2   VAL   D CB  1 
ATOM   1159 C  CG1 . VAL   B 2 3   ? 16.656 -33.156 5.337  1.00 25.13  ? 2   VAL   D CG1 1 
ATOM   1160 C  CG2 . VAL   B 2 3   ? 17.136 -30.760 4.673  1.00 25.51  ? 2   VAL   D CG2 1 
ATOM   1161 N  N   . ILE   B 2 4   ? 15.927 -31.374 1.338  1.00 22.13  ? 3   ILE   D N   1 
ATOM   1162 C  CA  . ILE   B 2 4   ? 15.543 -30.285 0.448  1.00 21.17  ? 3   ILE   D CA  1 
ATOM   1163 C  C   . ILE   B 2 4   ? 15.155 -29.150 1.431  1.00 24.99  ? 3   ILE   D C   1 
ATOM   1164 O  O   . ILE   B 2 4   ? 14.119 -29.276 2.108  1.00 24.49  ? 3   ILE   D O   1 
ATOM   1165 C  CB  . ILE   B 2 4   ? 14.350 -30.663 -0.469 1.00 22.97  ? 3   ILE   D CB  1 
ATOM   1166 C  CG1 . ILE   B 2 4   ? 14.657 -31.914 -1.368 1.00 21.56  ? 3   ILE   D CG1 1 
ATOM   1167 C  CG2 . ILE   B 2 4   ? 13.906 -29.425 -1.313 1.00 24.72  ? 3   ILE   D CG2 1 
ATOM   1168 C  CD1 . ILE   B 2 4   ? 16.010 -31.794 -2.282 1.00 25.18  ? 3   ILE   D CD1 1 
ATOM   1169 N  N   . PRO   B 2 5   ? 15.956 -28.064 1.547  1.00 25.24  ? 4   PRO   D N   1 
ATOM   1170 C  CA  . PRO   B 2 5   ? 15.614 -27.002 2.514  1.00 25.87  ? 4   PRO   D CA  1 
ATOM   1171 C  C   . PRO   B 2 5   ? 14.377 -26.194 2.125  1.00 28.77  ? 4   PRO   D C   1 
ATOM   1172 O  O   . PRO   B 2 5   ? 14.084 -26.030 0.938  1.00 28.09  ? 4   PRO   D O   1 
ATOM   1173 C  CB  . PRO   B 2 5   ? 16.873 -26.127 2.545  1.00 27.46  ? 4   PRO   D CB  1 
ATOM   1174 C  CG  . PRO   B 2 5   ? 17.480 -26.305 1.166  1.00 31.61  ? 4   PRO   D CG  1 
ATOM   1175 C  CD  . PRO   B 2 5   ? 17.211 -27.756 0.826  1.00 27.29  ? 4   PRO   D CD  1 
ATOM   1176 N  N   . ALA   B 2 6   ? 13.670 -25.666 3.132  1.00 27.31  ? 5   ALA   D N   1 
HETATM 1177 C  C4  . A1ACA C 3 .   ? 25.493 -10.257 16.507 1.00 21.10  ? 201 A1ACA A C4  1 
HETATM 1178 C  C5  . A1ACA C 3 .   ? 24.895 -8.993  16.547 1.00 20.55  ? 201 A1ACA A C5  1 
HETATM 1179 C  C6  . A1ACA C 3 .   ? 23.884 -8.714  17.457 1.00 21.62  ? 201 A1ACA A C6  1 
HETATM 1180 C  C7  . A1ACA C 3 .   ? 23.455 -9.729  18.307 1.00 22.20  ? 201 A1ACA A C7  1 
HETATM 1181 C  C8  . A1ACA C 3 .   ? 22.292 -10.919 19.872 1.00 25.98  ? 201 A1ACA A C8  1 
HETATM 1182 C  C10 . A1ACA C 3 .   ? 23.999 -11.008 18.240 1.00 21.08  ? 201 A1ACA A C10 1 
HETATM 1183 C  C1  . A1ACA C 3 .   ? 27.266 -10.348 11.948 1.00 25.98  ? 201 A1ACA A C1  1 
HETATM 1184 C  C2  . A1ACA C 3 .   ? 27.421 -10.676 13.287 1.00 24.80  ? 201 A1ACA A C2  1 
HETATM 1185 C  C3  . A1ACA C 3 .   ? 26.381 -10.322 14.180 1.00 22.55  ? 201 A1ACA A C3  1 
HETATM 1186 C  C9  . A1ACA C 3 .   ? 23.293 -11.868 19.246 1.00 24.01  ? 201 A1ACA A C9  1 
HETATM 1187 O  O   . A1ACA C 3 .   ? 21.469 -11.186 20.741 1.00 27.41  ? 201 A1ACA A O   1 
HETATM 1188 N  N2  . A1ACA C 3 .   ? 22.458 -9.702  19.289 1.00 24.65  ? 201 A1ACA A N2  1 
HETATM 1189 C  C11 . A1ACA C 3 .   ? 25.022 -11.279 17.336 1.00 20.68  ? 201 A1ACA A C11 1 
HETATM 1190 N  N1  . A1ACA C 3 .   ? 26.391 -10.646 15.499 1.00 21.02  ? 201 A1ACA A N1  1 
HETATM 1191 N  N3  . A1ACA C 3 .   ? 25.280 -9.716  13.699 1.00 25.37  ? 201 A1ACA A N3  1 
HETATM 1192 C  C   . A1ACA C 3 .   ? 25.260 -9.469  12.403 1.00 27.81  ? 201 A1ACA A C   1 
HETATM 1193 CL CL  . A1ACA C 3 .   ? 23.808 -8.703  11.825 0.81 29.15  ? 201 A1ACA A CL  1 
HETATM 1194 BR BR  . A1ACA C 3 .   ? 28.993 -11.565 13.869 0.96 23.78  ? 201 A1ACA A BR  1 
HETATM 1195 N  N   . A1ACA C 3 .   ? 26.169 -9.731  11.479 1.00 26.65  ? 201 A1ACA A N   1 
HETATM 1196 CL CL  . CL    D 4 .   ? 21.363 -15.481 22.707 1.00 32.61  ? 202 CL    A CL  1 
HETATM 1197 S  S   A DMS   E 5 .   ? 17.572 -35.398 -1.296 0.66 36.48  ? 101 DMS   D S   1 
HETATM 1198 O  O   A DMS   E 5 .   ? 16.268 -35.233 -0.654 0.66 37.49  ? 101 DMS   D O   1 
HETATM 1199 C  C1  A DMS   E 5 .   ? 18.649 -34.458 -0.237 0.66 35.49  ? 101 DMS   D C1  1 
HETATM 1200 C  C2  A DMS   E 5 .   ? 18.048 -37.005 -0.777 0.66 35.45  ? 101 DMS   D C2  1 
HETATM 1201 O  O   . HOH   F 6 .   ? 25.828 -3.571  26.538 1.00 29.75  ? 301 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 6 .   ? 35.639 -25.924 25.526 1.00 34.75  ? 302 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 6 .   ? 26.816 -32.111 16.168 1.00 36.24  ? 303 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 6 .   ? 44.273 -0.900  17.878 1.00 41.92  ? 304 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 6 .   ? 37.203 -12.412 40.307 1.00 53.83  ? 305 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 6 .   ? 41.092 -21.726 25.216 1.00 34.90  ? 306 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 6 .   ? 38.341 -15.049 15.526 1.00 29.71  ? 307 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 6 .   ? 20.826 -5.932  26.222 1.00 36.15  ? 308 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 6 .   ? 45.033 -11.425 18.764 1.00 55.52  ? 309 HOH   A O   1 
HETATM 1210 O  O   A HOH   F 6 .   ? 19.043 -22.985 4.363  0.67 41.65  ? 310 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 6 .   ? 23.425 -5.949  32.972 1.00 33.02  ? 311 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 6 .   ? 22.803 -5.529  19.875 1.00 46.98  ? 312 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 6 .   ? 15.438 -10.042 24.956 1.00 45.70  ? 313 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 6 .   ? 16.438 -27.474 -3.223 1.00 42.08  ? 314 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 6 .   ? 29.733 -32.271 9.510  1.00 40.06  ? 315 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 6 .   ? 17.890 -29.535 7.689  1.00 28.69  ? 316 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 6 .   ? 33.314 -20.863 29.590 1.00 38.70  ? 317 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 6 .   ? 41.329 -17.039 15.218 1.00 28.88  ? 318 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 6 .   ? 28.402 -9.029  39.990 1.00 42.51  ? 319 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 6 .   ? 20.292 -13.618 20.702 1.00 39.38  ? 320 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 6 .   ? 21.687 -29.538 -5.226 1.00 31.23  ? 321 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 6 .   ? 37.870 2.327   19.882 1.00 31.74  ? 322 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 6 .   ? 43.607 -6.662  32.035 1.00 44.56  ? 323 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 6 .   ? 31.673 -1.002  15.940 1.00 36.78  ? 324 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 6 .   ? 32.807 -24.601 32.176 1.00 51.99  ? 325 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 6 .   ? 28.860 -21.967 41.591 1.00 59.88  ? 326 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 6 .   ? 22.986 -28.307 12.660 1.00 21.12  ? 327 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 6 .   ? 22.693 -27.756 17.776 1.00 43.53  ? 328 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 6 .   ? 19.973 -9.749  37.143 1.00 34.45  ? 329 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 6 .   ? 41.476 -12.873 14.354 1.00 63.74  ? 330 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 6 .   ? 23.300 -17.094 44.305 1.00 55.54  ? 331 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 6 .   ? 41.194 -1.418  11.677 1.00 50.67  ? 332 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 6 .   ? 21.419 -27.242 14.731 0.50 28.92  ? 333 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 6 .   ? 37.658 -20.544 27.054 1.00 31.41  ? 334 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 6 .   ? 30.411 1.364   34.010 1.00 61.34  ? 335 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 6 .   ? 29.347 -27.458 20.637 1.00 20.68  ? 336 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 6 .   ? 25.724 -3.034  20.123 1.00 51.95  ? 337 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 6 .   ? 12.269 -18.102 25.956 1.00 49.86  ? 338 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 6 .   ? 27.300 -10.220 35.927 1.00 33.12  ? 339 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 6 .   ? 30.466 -0.700  37.115 1.00 37.59  ? 340 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 6 .   ? 27.368 -28.300 18.652 1.00 22.13  ? 341 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 6 .   ? 43.881 -4.393  25.835 1.00 37.83  ? 342 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 6 .   ? 34.494 -23.805 30.018 1.00 56.83  ? 343 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 6 .   ? 21.942 -25.116 18.362 1.00 21.26  ? 344 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 6 .   ? 37.926 -16.555 13.160 0.50 21.87  ? 345 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 6 .   ? 26.959 -35.367 11.613 1.00 47.05  ? 346 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 6 .   ? 26.141 -22.723 30.031 1.00 23.93  ? 347 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 6 .   ? 18.059 -34.577 8.313  1.00 29.85  ? 348 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 6 .   ? 21.528 -30.070 14.207 1.00 67.62  ? 349 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 6 .   ? 36.832 -5.782  12.317 1.00 32.44  ? 350 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 6 .   ? 26.957 -16.790 38.729 1.00 44.90  ? 351 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 6 .   ? 24.960 -26.851 19.017 1.00 29.46  ? 352 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 6 .   ? 28.975 -31.170 7.219  1.00 29.31  ? 353 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 6 .   ? 24.019 -15.968 21.328 1.00 25.33  ? 354 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 6 .   ? 26.150 -22.026 38.704 1.00 31.85  ? 355 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 6 .   ? 12.740 -20.675 42.416 1.00 49.10  ? 356 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 6 .   ? 28.914 -0.593  16.917 1.00 60.72  ? 357 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 6 .   ? 20.950 -7.465  19.920 1.00 39.64  ? 358 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 6 .   ? 42.385 -10.471 15.447 1.00 42.08  ? 359 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 6 .   ? 28.491 -24.324 34.404 1.00 47.70  ? 360 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 6 .   ? 24.113 -28.737 21.605 1.00 46.96  ? 361 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 6 .   ? 28.250 -23.841 31.730 1.00 34.30  ? 362 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 6 .   ? 44.619 -16.391 29.784 1.00 46.78  ? 363 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 6 .   ? 46.839 -21.525 18.362 1.00 43.25  ? 364 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 6 .   ? 10.784 -11.633 34.621 1.00 41.45  ? 365 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 6 .   ? 30.726 -29.017 22.652 1.00 35.94  ? 366 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 6 .   ? 45.864 -14.297 21.544 1.00 46.89  ? 367 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 6 .   ? 37.341 -6.505  34.413 1.00 34.36  ? 368 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 6 .   ? 11.678 -15.520 40.535 1.00 66.13  ? 369 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 6 .   ? 44.445 -12.758 41.491 1.00 46.12  ? 370 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 6 .   ? 47.156 -25.312 21.608 1.00 44.26  ? 371 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 6 .   ? 46.156 -15.794 27.647 1.00 55.25  ? 372 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 6 .   ? 34.157 -8.063  35.750 1.00 29.81  ? 373 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 6 .   ? 41.321 -7.782  46.555 1.00 49.92  ? 374 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 6 .   ? 27.617 -23.163 13.890 0.50 22.96  ? 375 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 6 .   ? 45.495 -10.915 30.273 1.00 51.58  ? 376 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 6 .   ? 19.854 -25.670 41.306 1.00 67.92  ? 377 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 6 .   ? 34.797 -29.118 26.020 1.00 52.99  ? 378 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 6 .   ? 26.084 -19.313 41.714 1.00 50.89  ? 379 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 6 .   ? 34.837 -18.995 13.890 0.50 16.74  ? 380 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 6 .   ? 38.940 -18.878 33.542 1.00 38.91  ? 381 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 6 .   ? 27.138 -2.495  16.087 1.00 57.79  ? 382 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 6 .   ? 20.279 -16.052 40.947 1.00 32.44  ? 383 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 6 .   ? 17.969 -24.505 39.727 1.00 36.03  ? 384 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 6 .   ? 47.279 -6.766  20.364 1.00 64.22  ? 385 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 6 .   ? 45.183 -12.675 23.585 1.00 42.65  ? 386 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 6 .   ? 29.632 -22.770 36.890 1.00 57.01  ? 387 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 6 .   ? 43.821 -10.657 35.200 1.00 63.92  ? 388 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 6 .   ? 26.141 -8.180  9.058  1.00 36.62  ? 389 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 6 .   ? 23.672 -15.794 17.930 1.00 33.48  ? 390 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 6 .   ? 27.181 -25.452 28.420 1.00 48.22  ? 391 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 6 .   ? 46.333 -19.075 19.710 1.00 43.68  ? 392 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 6 .   ? 4.300  -20.578 37.867 1.00 57.26  ? 393 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 6 .   ? 17.351 -24.583 -2.088 1.00 60.59  ? 394 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 6 .   ? 16.849 -6.563  27.643 1.00 58.05  ? 395 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 6 .   ? 41.264 -7.076  36.010 1.00 39.21  ? 396 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 6 .   ? 42.075 -6.019  11.822 1.00 57.91  ? 397 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 6 .   ? 46.144 -9.028  44.111 1.00 45.31  ? 398 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 6 .   ? 14.344 -17.038 23.507 1.00 37.48  ? 399 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 6 .   ? 40.382 -19.697 29.054 1.00 30.01  ? 400 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 6 .   ? 36.915 -2.272  11.564 1.00 52.90  ? 401 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 6 .   ? 33.197 -29.917 21.486 1.00 41.31  ? 402 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 6 .   ? 21.038 -23.347 42.111 1.00 42.36  ? 403 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 6 .   ? 30.453 -10.713 40.648 1.00 36.90  ? 404 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 6 .   ? 45.714 -17.061 17.258 1.00 57.04  ? 405 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 6 .   ? 22.995 -15.076 40.435 1.00 29.12  ? 406 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 6 .   ? 35.234 1.797   13.555 1.00 52.39  ? 407 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 6 .   ? 41.292 -17.119 35.215 1.00 38.51  ? 408 HOH   A O   1 
HETATM 1309 O  O   A HOH   F 6 .   ? 12.227 -21.038 27.988 0.66 37.72  ? 409 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 6 .   ? 35.129 -29.791 23.421 1.00 39.55  ? 410 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 6 .   ? 44.606 -8.842  18.025 1.00 55.28  ? 411 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 6 .   ? 10.435 -11.712 40.011 1.00 57.99  ? 412 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 6 .   ? 25.622 -4.678  17.970 1.00 45.53  ? 413 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 6 .   ? 33.519 -32.987 12.065 1.00 39.23  ? 414 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 6 .   ? 47.021 -20.342 21.984 1.00 58.09  ? 415 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 6 .   ? 31.851 -32.093 14.496 1.00 32.90  ? 416 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 6 .   ? 26.602 -30.891 19.012 1.00 50.75  ? 417 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 6 .   ? 32.421 -9.055  39.751 1.00 51.39  ? 418 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 6 .   ? 32.276 -15.811 39.876 1.00 29.29  ? 419 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 6 .   ? 33.558 -0.373  20.213 1.00 36.43  ? 420 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 6 .   ? 26.947 -1.624  22.112 1.00 49.46  ? 421 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 6 .   ? 29.495 -0.943  22.243 1.00 49.02  ? 422 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 6 .   ? 19.638 -27.369 10.022 1.00 53.16  ? 423 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 6 .   ? 34.630 -19.011 36.132 1.00 61.03  ? 424 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 6 .   ? 25.545 -16.143 41.092 1.00 44.70  ? 425 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 6 .   ? 33.921 -32.903 21.869 1.00 56.04  ? 426 HOH   A O   1 
HETATM 1327 O  O   . HOH   F 6 .   ? 42.030 -8.017  13.685 1.00 50.76  ? 427 HOH   A O   1 
HETATM 1328 O  O   . HOH   F 6 .   ? 39.921 -5.588  33.999 1.00 38.85  ? 428 HOH   A O   1 
HETATM 1329 O  O   . HOH   F 6 .   ? 22.305 -10.469 14.664 1.00 37.87  ? 429 HOH   A O   1 
HETATM 1330 O  O   . HOH   F 6 .   ? 45.818 -5.559  23.735 1.00 42.48  ? 430 HOH   A O   1 
HETATM 1331 O  O   . HOH   F 6 .   ? 31.910 -26.269 27.100 1.00 45.72  ? 431 HOH   A O   1 
HETATM 1332 O  O   . HOH   F 6 .   ? 42.821 -18.340 30.804 1.00 43.92  ? 432 HOH   A O   1 
HETATM 1333 O  O   . HOH   F 6 .   ? 23.572 -30.673 19.368 1.00 58.51  ? 433 HOH   A O   1 
HETATM 1334 O  O   . HOH   F 6 .   ? 31.981 -0.096  13.384 1.00 56.81  ? 434 HOH   A O   1 
HETATM 1335 O  O   . HOH   F 6 .   ? 26.426 -29.630 22.712 1.00 52.28  ? 435 HOH   A O   1 
HETATM 1336 O  O   . HOH   F 6 .   ? 19.510 -31.900 14.004 1.00 58.16  ? 436 HOH   A O   1 
HETATM 1337 O  O   . HOH   F 6 .   ? 23.026 -3.193  26.877 1.00 59.28  ? 437 HOH   A O   1 
HETATM 1338 O  O   . HOH   F 6 .   ? 37.036 -31.695 23.416 1.00 65.20  ? 438 HOH   A O   1 
HETATM 1339 O  O   . HOH   F 6 .   ? 44.464 -4.323  28.848 1.00 64.29  ? 439 HOH   A O   1 
HETATM 1340 O  O   . HOH   F 6 .   ? 28.765 -2.807  13.010 1.00 67.24  ? 440 HOH   A O   1 
HETATM 1341 O  O   . HOH   F 6 .   ? 27.054 -34.548 18.014 1.00 60.55  ? 441 HOH   A O   1 
HETATM 1342 O  O   . HOH   F 6 .   ? 36.600 -24.578 27.659 1.00 46.61  ? 442 HOH   A O   1 
HETATM 1343 O  O   . HOH   F 6 .   ? 30.651 -34.523 14.850 1.00 52.84  ? 443 HOH   A O   1 
HETATM 1344 O  O   . HOH   F 6 .   ? 47.977 -23.576 19.734 1.00 52.40  ? 444 HOH   A O   1 
HETATM 1345 O  O   . HOH   F 6 .   ? 35.373 -4.284  10.618 1.00 40.30  ? 445 HOH   A O   1 
HETATM 1346 O  O   . HOH   F 6 .   ? 24.489 -21.745 41.082 1.00 49.43  ? 446 HOH   A O   1 
HETATM 1347 O  O   . HOH   F 6 .   ? 19.932 -8.085  24.528 1.00 50.17  ? 447 HOH   A O   1 
HETATM 1348 O  O   . HOH   F 6 .   ? 34.204 -17.716 39.412 1.00 55.27  ? 448 HOH   A O   1 
HETATM 1349 O  O   . HOH   F 6 .   ? 47.396 -28.516 17.642 1.00 55.41  ? 449 HOH   A O   1 
HETATM 1350 O  O   . HOH   F 6 .   ? 46.707 -14.717 18.227 1.00 60.72  ? 450 HOH   A O   1 
HETATM 1351 O  O   . HOH   F 6 .   ? 47.241 -11.979 25.241 1.00 59.39  ? 451 HOH   A O   1 
HETATM 1352 O  O   . HOH   F 6 .   ? 11.953 -18.846 22.659 1.00 59.34  ? 452 HOH   A O   1 
HETATM 1353 O  O   . HOH   F 6 .   ? 32.159 -1.151  22.400 1.00 50.63  ? 453 HOH   A O   1 
HETATM 1354 O  O   . HOH   F 6 .   ? 35.935 -21.314 30.587 1.00 52.25  ? 454 HOH   A O   1 
HETATM 1355 O  O   . HOH   F 6 .   ? 19.451 -7.802  35.373 1.00 48.57  ? 455 HOH   A O   1 
HETATM 1356 O  O   . HOH   F 6 .   ? 47.050 -12.594 28.374 1.00 55.03  ? 456 HOH   A O   1 
HETATM 1357 O  O   . HOH   F 6 .   ? 45.567 -8.441  31.340 1.00 57.34  ? 457 HOH   A O   1 
HETATM 1358 O  O   . HOH   F 6 .   ? 25.391 -5.749  35.010 1.00 54.35  ? 458 HOH   A O   1 
HETATM 1359 O  O   . HOH   F 6 .   ? 19.831 -15.043 43.410 1.00 45.41  ? 459 HOH   A O   1 
HETATM 1360 O  O   . HOH   F 6 .   ? 17.333 -8.190  25.177 1.00 58.46  ? 460 HOH   A O   1 
HETATM 1361 O  O   . HOH   F 6 .   ? 17.105 -28.306 9.987  1.00 43.17  ? 461 HOH   A O   1 
HETATM 1362 O  O   . HOH   F 6 .   ? 44.129 -13.625 13.889 0.50 58.41  ? 462 HOH   A O   1 
HETATM 1363 O  O   . HOH   F 6 .   ? 32.000 -23.816 34.818 1.00 63.18  ? 463 HOH   A O   1 
HETATM 1364 O  O   . HOH   F 6 .   ? 19.089 -28.313 13.812 0.50 59.21  ? 464 HOH   A O   1 
HETATM 1365 O  O   . HOH   F 6 .   ? 43.224 -3.097  34.133 1.00 58.47  ? 465 HOH   A O   1 
HETATM 1366 O  O   . HOH   F 6 .   ? 32.577 -20.612 36.920 1.00 59.50  ? 466 HOH   A O   1 
HETATM 1367 O  O   . HOH   F 6 .   ? 28.389 -29.880 24.589 1.00 60.72  ? 467 HOH   A O   1 
HETATM 1368 O  O   . HOH   F 6 .   ? 33.868 -14.112 41.670 0.50 35.36  ? 468 HOH   A O   1 
HETATM 1369 O  O   . HOH   F 6 .   ? 16.814 -6.952  34.881 1.00 63.16  ? 469 HOH   A O   1 
HETATM 1370 O  O   . HOH   F 6 .   ? 12.453 -18.323 19.991 1.00 57.08  ? 470 HOH   A O   1 
HETATM 1371 O  O   . HOH   F 6 .   ? 45.147 -12.287 16.039 1.00 59.10  ? 471 HOH   A O   1 
HETATM 1372 O  O   . HOH   F 6 .   ? 21.255 -5.821  34.837 1.00 43.57  ? 472 HOH   A O   1 
HETATM 1373 O  O   . HOH   F 6 .   ? 33.869 -11.254 41.670 0.50 59.46  ? 473 HOH   A O   1 
HETATM 1374 O  O   . HOH   F 6 .   ? 48.549 -21.670 16.333 1.00 47.04  ? 474 HOH   A O   1 
HETATM 1375 O  O   . HOH   F 6 .   ? 16.697 -29.903 12.309 1.00 51.87  ? 475 HOH   A O   1 
HETATM 1376 O  O   . HOH   G 6 .   ? 12.180 -24.265 0.068  1.00 44.02  ? 201 HOH   D O   1 
HETATM 1377 O  O   . HOH   G 6 .   ? 14.925 -25.777 -1.730 1.00 39.64  ? 202 HOH   D O   1 
HETATM 1378 O  O   . HOH   G 6 .   ? 22.589 -34.090 8.851  1.00 31.24  ? 203 HOH   D O   1 
HETATM 1379 O  O   . HOH   G 6 .   ? 17.761 -36.281 6.033  1.00 38.26  ? 204 HOH   D O   1 
HETATM 1380 O  O   . HOH   G 6 .   ? 20.890 -38.331 4.013  1.00 44.26  ? 205 HOH   D O   1 
HETATM 1381 O  O   . HOH   G 6 .   ? 11.417 -23.652 3.206  1.00 46.07  ? 206 HOH   D O   1 
HETATM 1382 O  O   . HOH   G 6 .   ? 20.757 -39.440 -2.136 1.00 48.72  ? 207 HOH   D O   1 
HETATM 1383 O  O   . HOH   G 6 .   ? 10.608 -24.785 5.558  1.00 50.52  ? 208 HOH   D O   1 
HETATM 1384 O  O   . HOH   G 6 .   ? 20.166 -35.375 10.106 1.00 33.67  ? 209 HOH   D O   1 
HETATM 1385 O  O   . HOH   G 6 .   ? 23.646 -36.601 10.019 1.00 46.62  ? 210 HOH   D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP A 5   ? 0.7507 0.9187 0.6194 0.0364  -0.1250 -0.0230 6   ASP A N   
2    C CA  . ASP A 5   ? 0.7434 0.9056 0.5955 0.0212  -0.1161 -0.0253 6   ASP A CA  
3    C C   . ASP A 5   ? 0.7197 0.9098 0.5955 0.0104  -0.1120 -0.0411 6   ASP A C   
4    O O   . ASP A 5   ? 0.7135 0.9275 0.6179 0.0136  -0.1154 -0.0502 6   ASP A O   
5    C CB  . ASP A 5   ? 0.7670 0.9026 0.6102 0.0130  -0.0995 -0.0185 6   ASP A CB  
6    C CG  . ASP A 5   ? 0.9596 1.0766 0.7706 0.0034  -0.0942 -0.0143 6   ASP A CG  
7    O OD1 . ASP A 5   ? 0.9551 1.0836 0.7650 -0.0070 -0.0911 -0.0231 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.0738 1.1641 0.8606 0.0054  -0.0919 -0.0031 6   ASP A OD2 
9    N N   . SER A 6   ? 0.6115 0.7979 0.4751 -0.0030 -0.1038 -0.0451 7   SER A N   
10   C CA  . SER A 6   ? 0.5646 0.7710 0.4458 -0.0148 -0.0978 -0.0596 7   SER A CA  
11   C C   . SER A 6   ? 0.5125 0.7069 0.4051 -0.0246 -0.0798 -0.0616 7   SER A C   
12   O O   . SER A 6   ? 0.4996 0.6988 0.3965 -0.0359 -0.0720 -0.0710 7   SER A O   
13   C CB  . SER A 6   ? 0.6414 0.8524 0.5010 -0.0222 -0.1020 -0.0642 7   SER A CB  
14   O OG  . SER A 6   ? 0.7970 0.9827 0.6287 -0.0276 -0.0944 -0.0563 7   SER A OG  
15   N N   . CYS A 7   ? 0.4064 0.5849 0.3040 -0.0197 -0.0741 -0.0533 8   CYS A N   
16   C CA  . CYS A 7   ? 0.3607 0.5273 0.2678 -0.0269 -0.0594 -0.0543 8   CYS A CA  
17   C C   . CYS A 7   ? 0.3679 0.5490 0.2999 -0.0329 -0.0541 -0.0658 8   CYS A C   
18   O O   . CYS A 7   ? 0.3543 0.5547 0.3017 -0.0298 -0.0605 -0.0717 8   CYS A O   
19   C CB  . CYS A 7   ? 0.3705 0.5195 0.2777 -0.0199 -0.0563 -0.0438 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.4474 0.5710 0.3237 -0.0180 -0.0556 -0.0312 8   CYS A SG  
21   N N   . ILE A 8   ? 0.2758 0.4467 0.2114 -0.0413 -0.0423 -0.0694 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2401 0.4145 0.1944 -0.0470 -0.0349 -0.0774 9   ILE A CA  
23   C C   . ILE A 8   ? 0.2702 0.4275 0.2285 -0.0429 -0.0291 -0.0696 9   ILE A C   
24   O O   . ILE A 8   ? 0.2665 0.4097 0.2134 -0.0388 -0.0285 -0.0607 9   ILE A O   
25   C CB  . ILE A 8   ? 0.2772 0.4500 0.2316 -0.0583 -0.0270 -0.0875 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.2786 0.4325 0.2203 -0.0602 -0.0202 -0.0839 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.2630 0.4557 0.2157 -0.0633 -0.0329 -0.0971 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3352 0.4835 0.2779 -0.0694 -0.0116 -0.0937 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2085 0.3657 0.1813 -0.0452 -0.0238 -0.0733 10  GLN A N   
30   N N   B GLN A 9   ? 0.2101 0.3692 0.1836 -0.0446 -0.0248 -0.0733 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2044 0.3452 0.1793 -0.0418 -0.0187 -0.0664 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2000 0.3442 0.1768 -0.0412 -0.0199 -0.0669 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2468 0.3752 0.2253 -0.0491 -0.0092 -0.0709 10  GLN A C   
34   C C   B GLN A 9   ? 0.2557 0.3870 0.2356 -0.0487 -0.0102 -0.0712 10  GLN A C   
35   O O   A GLN A 9   ? 0.2487 0.3839 0.2343 -0.0563 -0.0060 -0.0799 10  GLN A O   
36   O O   B GLN A 9   ? 0.2566 0.3942 0.2429 -0.0562 -0.0067 -0.0804 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2199 0.3693 0.2057 -0.0351 -0.0227 -0.0642 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2057 0.3611 0.1949 -0.0352 -0.0239 -0.0664 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2770 0.4115 0.2668 -0.0341 -0.0160 -0.0600 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.2006 0.3408 0.1886 -0.0291 -0.0215 -0.0573 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5061 0.6425 0.5005 -0.0251 -0.0199 -0.0543 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.3751 0.5164 0.3766 -0.0313 -0.0159 -0.0613 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.3975 0.5428 0.3904 -0.0174 -0.0284 -0.0515 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.2936 0.4529 0.3089 -0.0330 -0.0168 -0.0696 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.4385 0.5641 0.4367 -0.0254 -0.0138 -0.0523 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.3079 0.4306 0.3053 -0.0317 -0.0098 -0.0561 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2194 0.3288 0.1923 -0.0472 -0.0050 -0.0649 11  PHE A N   
48   N N   B PHE A 10  ? 0.2241 0.3365 0.1984 -0.0465 -0.0061 -0.0647 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2163 0.3098 0.1895 -0.0518 0.0022  -0.0675 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2255 0.3212 0.1992 -0.0509 0.0012  -0.0668 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2464 0.3344 0.2243 -0.0502 0.0043  -0.0641 11  PHE A C   
52   C C   B PHE A 10  ? 0.2575 0.3476 0.2362 -0.0496 0.0037  -0.0639 11  PHE A C   
53   O O   A PHE A 10  ? 0.2373 0.3178 0.2127 -0.0442 0.0030  -0.0565 11  PHE A O   
54   O O   B PHE A 10  ? 0.2509 0.3354 0.2279 -0.0434 0.0020  -0.0563 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2349 0.3129 0.2004 -0.0501 0.0043  -0.0648 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2500 0.3315 0.2157 -0.0483 0.0026  -0.0629 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2463 0.3065 0.2099 -0.0534 0.0098  -0.0681 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.2780 0.3628 0.2394 -0.0521 0.0033  -0.0688 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.2807 0.3389 0.2436 -0.0605 0.0135  -0.0766 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3193 0.4185 0.2767 -0.0524 -0.0012 -0.0696 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.2672 0.3106 0.2278 -0.0493 0.0108  -0.0628 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3203 0.3923 0.2801 -0.0550 0.0081  -0.0737 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3025 0.3391 0.2603 -0.0629 0.0185  -0.0788 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3322 0.4341 0.2842 -0.0570 0.0003  -0.0759 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3044 0.3279 0.2597 -0.0511 0.0144  -0.0649 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3636 0.4388 0.3204 -0.0587 0.0097  -0.0805 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.2845 0.3031 0.2376 -0.0575 0.0183  -0.0724 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3328 0.4236 0.2858 -0.0603 0.0063  -0.0818 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2151 0.3074 0.1995 -0.0566 0.0084  -0.0710 12  THR A N   
70   C CA  . THR A 11  ? 0.2189 0.3081 0.2083 -0.0576 0.0122  -0.0705 12  THR A CA  
71   C C   . THR A 11  ? 0.2463 0.3126 0.2264 -0.0546 0.0148  -0.0627 12  THR A C   
72   O O   . THR A 11  ? 0.2491 0.3153 0.2316 -0.0502 0.0142  -0.0581 12  THR A O   
73   C CB  . THR A 11  ? 0.2915 0.3836 0.2857 -0.0686 0.0194  -0.0808 12  THR A CB  
74   O OG1 . THR A 11  ? 0.2705 0.3877 0.2752 -0.0711 0.0157  -0.0892 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3361 0.4272 0.3358 -0.0715 0.0250  -0.0823 12  THR A CG2 
76   N N   . ARG A 12  ? 0.2286 0.2759 0.1984 -0.0565 0.0172  -0.0620 13  ARG A N   
77   C CA  . ARG A 12  ? 0.2403 0.2661 0.2006 -0.0533 0.0182  -0.0557 13  ARG A CA  
78   C C   . ARG A 12  ? 0.2649 0.2902 0.2240 -0.0447 0.0128  -0.0488 13  ARG A C   
79   O O   . ARG A 12  ? 0.2510 0.2609 0.2035 -0.0418 0.0125  -0.0447 13  ARG A O   
80   C CB  . ARG A 12  ? 0.3182 0.3215 0.2672 -0.0574 0.0219  -0.0581 13  ARG A CB  
81   C CG  . ARG A 12  ? 0.4613 0.4561 0.4061 -0.0681 0.0297  -0.0643 13  ARG A CG  
82   C CD  . ARG A 12  ? 0.7139 0.7009 0.6547 -0.0713 0.0342  -0.0622 13  ARG A CD  
83   N NE  . ARG A 12  ? 0.8832 0.8443 0.8084 -0.0674 0.0331  -0.0551 13  ARG A NE  
84   C CZ  . ARG A 12  ? 1.0367 0.9890 0.9555 -0.0683 0.0354  -0.0515 13  ARG A CZ  
85   N NH1 . ARG A 12  ? 0.8899 0.8187 0.7928 -0.0644 0.0328  -0.0454 13  ARG A NH1 
86   N NH2 . ARG A 12  ? 0.8396 0.8074 0.7683 -0.0727 0.0399  -0.0548 13  ARG A NH2 
87   N N   . HIS A 13  ? 0.2135 0.2541 0.1773 -0.0414 0.0088  -0.0482 14  HIS A N   
88   C CA  . HIS A 13  ? 0.2150 0.2538 0.1762 -0.0358 0.0058  -0.0433 14  HIS A CA  
89   C C   . HIS A 13  ? 0.2429 0.2755 0.2031 -0.0319 0.0053  -0.0372 14  HIS A C   
90   O O   . HIS A 13  ? 0.2435 0.2665 0.2003 -0.0294 0.0047  -0.0352 14  HIS A O   
91   C CB  . HIS A 13  ? 0.2130 0.2664 0.1751 -0.0345 0.0027  -0.0432 14  HIS A CB  
92   C CG  . HIS A 13  ? 0.2404 0.2911 0.1988 -0.0312 0.0018  -0.0395 14  HIS A CG  
93   N ND1 . HIS A 13  ? 0.2513 0.2973 0.2088 -0.0316 0.0032  -0.0428 14  HIS A ND1 
94   C CD2 . HIS A 13  ? 0.2480 0.2996 0.2036 -0.0281 0.0005  -0.0338 14  HIS A CD2 
95   C CE1 . HIS A 13  ? 0.2482 0.2949 0.2038 -0.0299 0.0033  -0.0400 14  HIS A CE1 
96   N NE2 . HIS A 13  ? 0.2412 0.2896 0.1940 -0.0283 0.0020  -0.0341 14  HIS A NE2 
97   N N   . ALA A 14  ? 0.2060 0.2451 0.1701 -0.0311 0.0054  -0.0354 15  ALA A N   
98   C CA  . ALA A 14  ? 0.2097 0.2426 0.1726 -0.0278 0.0057  -0.0303 15  ALA A CA  
99   C C   . ALA A 14  ? 0.2466 0.2635 0.2036 -0.0298 0.0083  -0.0299 15  ALA A C   
100  O O   . ALA A 14  ? 0.2202 0.2295 0.1734 -0.0272 0.0072  -0.0266 15  ALA A O   
101  C CB  . ALA A 14  ? 0.2242 0.2667 0.1938 -0.0260 0.0058  -0.0300 15  ALA A CB  
102  N N   A SER A 15  ? 0.2325 0.2434 0.1870 -0.0349 0.0116  -0.0337 16  SER A N   
103  N N   B SER A 15  ? 0.2302 0.2410 0.1847 -0.0349 0.0116  -0.0337 16  SER A N   
104  N N   C SER A 15  ? 0.2243 0.2350 0.1788 -0.0349 0.0116  -0.0337 16  SER A N   
105  C CA  A SER A 15  ? 0.2400 0.2314 0.1838 -0.0373 0.0138  -0.0329 16  SER A CA  
106  C CA  B SER A 15  ? 0.2397 0.2310 0.1834 -0.0374 0.0139  -0.0330 16  SER A CA  
107  C CA  C SER A 15  ? 0.2307 0.2219 0.1744 -0.0372 0.0138  -0.0328 16  SER A CA  
108  C C   A SER A 15  ? 0.2870 0.2671 0.2243 -0.0334 0.0096  -0.0316 16  SER A C   
109  C C   B SER A 15  ? 0.2922 0.2721 0.2294 -0.0335 0.0096  -0.0316 16  SER A C   
110  C C   C SER A 15  ? 0.2889 0.2686 0.2259 -0.0334 0.0096  -0.0316 16  SER A C   
111  O O   A SER A 15  ? 0.2597 0.2280 0.1897 -0.0308 0.0075  -0.0286 16  SER A O   
112  O O   B SER A 15  ? 0.2759 0.2433 0.2053 -0.0311 0.0076  -0.0287 16  SER A O   
113  O O   C SER A 15  ? 0.2734 0.2404 0.2026 -0.0311 0.0076  -0.0287 16  SER A O   
114  C CB  A SER A 15  ? 0.2802 0.2655 0.2204 -0.0451 0.0195  -0.0378 16  SER A CB  
115  C CB  B SER A 15  ? 0.2844 0.2695 0.2244 -0.0452 0.0196  -0.0378 16  SER A CB  
116  C CB  C SER A 15  ? 0.2649 0.2495 0.2047 -0.0451 0.0197  -0.0374 16  SER A CB  
117  O OG  A SER A 15  ? 0.3050 0.2673 0.2299 -0.0482 0.0221  -0.0362 16  SER A OG  
118  O OG  B SER A 15  ? 0.3166 0.3150 0.2657 -0.0489 0.0238  -0.0412 16  SER A OG  
119  O OG  C SER A 15  ? 0.2701 0.2555 0.2101 -0.0479 0.0201  -0.0418 16  SER A OG  
120  N N   . ASP A 16  ? 0.2566 0.2420 0.1975 -0.0325 0.0079  -0.0347 17  ASP A N   
121  C CA  . ASP A 16  ? 0.2662 0.2441 0.2047 -0.0278 0.0040  -0.0356 17  ASP A CA  
122  C C   . ASP A 16  ? 0.2690 0.2546 0.2125 -0.0228 0.0005  -0.0333 17  ASP A C   
123  O O   . ASP A 16  ? 0.2662 0.2444 0.2075 -0.0184 -0.0033 -0.0333 17  ASP A O   
124  C CB  . ASP A 16  ? 0.2866 0.2711 0.2296 -0.0289 0.0046  -0.0409 17  ASP A CB  
125  C CG  . ASP A 16  ? 0.3588 0.3315 0.2954 -0.0343 0.0083  -0.0446 17  ASP A CG  
126  O OD1 . ASP A 16  ? 0.3434 0.3002 0.2701 -0.0374 0.0107  -0.0428 17  ASP A OD1 
127  O OD2 . ASP A 16  ? 0.3761 0.3547 0.3162 -0.0366 0.0097  -0.0498 17  ASP A OD2 
128  N N   . VAL A 17  ? 0.2197 0.2197 0.1693 -0.0235 0.0018  -0.0318 18  VAL A N   
129  C CA  . VAL A 17  ? 0.2115 0.2169 0.1640 -0.0210 0.0005  -0.0299 18  VAL A CA  
130  C C   . VAL A 17  ? 0.2632 0.2588 0.2111 -0.0198 -0.0005 -0.0269 18  VAL A C   
131  O O   . VAL A 17  ? 0.2412 0.2351 0.1897 -0.0172 -0.0035 -0.0280 18  VAL A O   
132  C CB  . VAL A 17  ? 0.2268 0.2434 0.1818 -0.0222 0.0023  -0.0276 18  VAL A CB  
133  C CG1 . VAL A 17  ? 0.2274 0.2441 0.1820 -0.0213 0.0028  -0.0249 18  VAL A CG1 
134  C CG2 . VAL A 17  ? 0.2204 0.2464 0.1772 -0.0236 0.0025  -0.0309 18  VAL A CG2 
135  N N   . LEU A 18  ? 0.2277 0.2179 0.1715 -0.0223 0.0020  -0.0245 19  LEU A N   
136  C CA  . LEU A 18  ? 0.2349 0.2153 0.1724 -0.0223 0.0020  -0.0221 19  LEU A CA  
137  C C   . LEU A 18  ? 0.2595 0.2253 0.1876 -0.0205 -0.0021 -0.0227 19  LEU A C   
138  O O   . LEU A 18  ? 0.2520 0.2137 0.1767 -0.0183 -0.0056 -0.0221 19  LEU A O   
139  C CB  . LEU A 18  ? 0.2373 0.2159 0.1731 -0.0260 0.0070  -0.0210 19  LEU A CB  
140  C CG  . LEU A 18  ? 0.2713 0.2424 0.2017 -0.0267 0.0085  -0.0189 19  LEU A CG  
141  C CD1 . LEU A 18  ? 0.2726 0.2513 0.2088 -0.0243 0.0081  -0.0174 19  LEU A CD1 
142  C CD2 . LEU A 18  ? 0.3361 0.3056 0.2658 -0.0309 0.0146  -0.0199 19  LEU A CD2 
143  N N   . LEU A 19  ? 0.2476 0.2048 0.1707 -0.0211 -0.0023 -0.0243 20  LEU A N   
144  C CA  . LEU A 19  ? 0.2676 0.2067 0.1790 -0.0179 -0.0073 -0.0243 20  LEU A CA  
145  C C   . LEU A 19  ? 0.2937 0.2400 0.2129 -0.0105 -0.0145 -0.0268 20  LEU A C   
146  O O   . LEU A 19  ? 0.2903 0.2283 0.2029 -0.0063 -0.0206 -0.0262 20  LEU A O   
147  C CB  . LEU A 19  ? 0.2941 0.2226 0.2000 -0.0200 -0.0052 -0.0262 20  LEU A CB  
148  C CG  . LEU A 19  ? 0.4061 0.3106 0.2967 -0.0158 -0.0104 -0.0256 20  LEU A CG  
149  C CD1 . LEU A 19  ? 0.4521 0.3353 0.3223 -0.0189 -0.0099 -0.0212 20  LEU A CD1 
150  C CD2 . LEU A 19  ? 0.4600 0.3543 0.3465 -0.0186 -0.0068 -0.0285 20  LEU A CD2 
151  N N   . ASN A 20  ? 0.2568 0.2202 0.1901 -0.0096 -0.0135 -0.0305 21  ASN A N   
152  C CA  . ASN A 20  ? 0.2406 0.2145 0.1843 -0.0042 -0.0183 -0.0353 21  ASN A CA  
153  C C   . ASN A 20  ? 0.2598 0.2418 0.2072 -0.0046 -0.0194 -0.0350 21  ASN A C   
154  O O   . ASN A 20  ? 0.2581 0.2429 0.2094 0.0002  -0.0255 -0.0387 21  ASN A O   
155  C CB  . ASN A 20  ? 0.2610 0.2495 0.2163 -0.0052 -0.0151 -0.0400 21  ASN A CB  
156  C CG  . ASN A 20  ? 0.3479 0.3280 0.3015 -0.0024 -0.0163 -0.0434 21  ASN A CG  
157  O OD1 . ASN A 20  ? 0.3208 0.2843 0.2665 0.0028  -0.0216 -0.0432 21  ASN A OD1 
158  N ND2 . ASN A 20  ? 0.2711 0.2602 0.2301 -0.0059 -0.0117 -0.0465 21  ASN A ND2 
159  N N   . LEU A 21  ? 0.2262 0.2119 0.1727 -0.0100 -0.0136 -0.0312 22  LEU A N   
160  C CA  . LEU A 21  ? 0.2248 0.2148 0.1725 -0.0117 -0.0131 -0.0308 22  LEU A CA  
161  C C   . LEU A 21  ? 0.2692 0.2464 0.2064 -0.0096 -0.0184 -0.0295 22  LEU A C   
162  O O   . LEU A 21  ? 0.2616 0.2436 0.2017 -0.0082 -0.0224 -0.0327 22  LEU A O   
163  C CB  . LEU A 21  ? 0.2278 0.2197 0.1745 -0.0166 -0.0061 -0.0266 22  LEU A CB  
164  C CG  . LEU A 21  ? 0.2638 0.2667 0.2171 -0.0185 -0.0020 -0.0271 22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.2685 0.2701 0.2188 -0.0207 0.0027  -0.0221 22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.2616 0.2747 0.2221 -0.0197 -0.0012 -0.0320 22  LEU A CD2 
167  N N   . ASN A 22  ? 0.2590 0.2198 0.1829 -0.0103 -0.0182 -0.0256 23  ASN A N   
168  C CA  . ASN A 22  ? 0.2766 0.2214 0.1853 -0.0090 -0.0233 -0.0238 23  ASN A CA  
169  C C   . ASN A 22  ? 0.3221 0.2635 0.2297 -0.0006 -0.0342 -0.0271 23  ASN A C   
170  O O   . ASN A 22  ? 0.3351 0.2728 0.2365 0.0022  -0.0411 -0.0278 23  ASN A O   
171  C CB  . ASN A 22  ? 0.2921 0.2182 0.1845 -0.0133 -0.0190 -0.0196 23  ASN A CB  
172  C CG  . ASN A 22  ? 0.4115 0.3208 0.2852 -0.0147 -0.0216 -0.0172 23  ASN A CG  
173  O OD1 . ASN A 22  ? 0.3677 0.2825 0.2425 -0.0150 -0.0235 -0.0182 23  ASN A OD1 
174  N ND2 . ASN A 22  ? 0.4198 0.3071 0.2741 -0.0167 -0.0211 -0.0144 23  ASN A ND2 
175  N N   . ARG A 23  ? 0.2927 0.2364 0.2074 0.0040  -0.0362 -0.0299 24  ARG A N   
176  C CA  . ARG A 23  ? 0.3055 0.2479 0.2230 0.0139  -0.0469 -0.0344 24  ARG A CA  
177  C C   . ARG A 23  ? 0.3301 0.2952 0.2653 0.0164  -0.0508 -0.0414 24  ARG A C   
178  O O   . ARG A 23  ? 0.3277 0.2925 0.2623 0.0237  -0.0614 -0.0447 24  ARG A O   
179  C CB  . ARG A 23  ? 0.2996 0.2421 0.2241 0.0173  -0.0459 -0.0374 24  ARG A CB  
180  C CG  . ARG A 23  ? 0.3346 0.2513 0.2398 0.0156  -0.0437 -0.0321 24  ARG A CG  
181  C CD  . ARG A 23  ? 0.3993 0.3181 0.3122 0.0157  -0.0397 -0.0356 24  ARG A CD  
182  N NE  . ARG A 23  ? 0.4807 0.3722 0.3741 0.0141  -0.0381 -0.0319 24  ARG A NE  
183  C CZ  . ARG A 23  ? 0.6385 0.5270 0.5330 0.0101  -0.0317 -0.0338 24  ARG A CZ  
184  N NH1 . ARG A 23  ? 0.4691 0.3806 0.3822 0.0075  -0.0269 -0.0387 24  ARG A NH1 
185  N NH2 . ARG A 23  ? 0.5609 0.4222 0.4360 0.0074  -0.0295 -0.0311 24  ARG A NH2 
186  N N   . LEU A 24  ? 0.2739 0.2580 0.2236 0.0099  -0.0423 -0.0439 25  LEU A N   
187  C CA  . LEU A 24  ? 0.2608 0.2655 0.2260 0.0092  -0.0433 -0.0514 25  LEU A CA  
188  C C   . LEU A 24  ? 0.3047 0.3056 0.2615 0.0072  -0.0465 -0.0499 25  LEU A C   
189  O O   . LEU A 24  ? 0.3073 0.3189 0.2718 0.0110  -0.0542 -0.0569 25  LEU A O   
190  C CB  . LEU A 24  ? 0.2489 0.2677 0.2243 0.0010  -0.0322 -0.0527 25  LEU A CB  
191  C CG  . LEU A 24  ? 0.2904 0.3170 0.2752 0.0014  -0.0283 -0.0561 25  LEU A CG  
192  C CD1 . LEU A 24  ? 0.2873 0.3250 0.2772 -0.0073 -0.0180 -0.0567 25  LEU A CD1 
193  C CD2 . LEU A 24  ? 0.2899 0.3279 0.2893 0.0093  -0.0354 -0.0664 25  LEU A CD2 
194  N N   . ARG A 25  ? 0.2680 0.2548 0.2097 0.0012  -0.0409 -0.0421 26  ARG A N   
195  C CA  . ARG A 25  ? 0.2817 0.2627 0.2131 -0.0015 -0.0430 -0.0410 26  ARG A CA  
196  C C   . ARG A 25  ? 0.3558 0.3260 0.2754 0.0066  -0.0566 -0.0418 26  ARG A C   
197  O O   . ARG A 25  ? 0.3552 0.3335 0.2769 0.0078  -0.0633 -0.0469 26  ARG A O   
198  C CB  . ARG A 25  ? 0.2937 0.2601 0.2110 -0.0084 -0.0343 -0.0334 26  ARG A CB  
199  C CG  . ARG A 25  ? 0.3565 0.3182 0.2641 -0.0123 -0.0350 -0.0337 26  ARG A CG  
200  C CD  . ARG A 25  ? 0.3848 0.3349 0.2818 -0.0190 -0.0255 -0.0284 26  ARG A CD  
201  N NE  . ARG A 25  ? 0.3782 0.3107 0.2603 -0.0189 -0.0245 -0.0233 26  ARG A NE  
202  C CZ  . ARG A 25  ? 0.5063 0.4217 0.3693 -0.0228 -0.0229 -0.0205 26  ARG A CZ  
203  N NH1 . ARG A 25  ? 0.4648 0.3780 0.3204 -0.0259 -0.0237 -0.0223 26  ARG A NH1 
204  N NH2 . ARG A 25  ? 0.4055 0.3050 0.2554 -0.0246 -0.0198 -0.0168 26  ARG A NH2 
205  N N   A SER A 26  ? 0.3401 0.2912 0.2458 0.0117  -0.0606 -0.0370 27  SER A N   
206  N N   B SER A 26  ? 0.3392 0.2904 0.2451 0.0118  -0.0606 -0.0371 27  SER A N   
207  N N   C SER A 26  ? 0.3397 0.2908 0.2455 0.0117  -0.0606 -0.0370 27  SER A N   
208  C CA  A SER A 26  ? 0.3639 0.2979 0.2527 0.0204  -0.0739 -0.0359 27  SER A CA  
209  C CA  B SER A 26  ? 0.3644 0.2982 0.2535 0.0206  -0.0738 -0.0358 27  SER A CA  
210  C CA  C SER A 26  ? 0.3643 0.2982 0.2532 0.0205  -0.0739 -0.0358 27  SER A CA  
211  C C   A SER A 26  ? 0.4217 0.3732 0.3270 0.0310  -0.0869 -0.0450 27  SER A C   
212  C C   B SER A 26  ? 0.4212 0.3726 0.3265 0.0310  -0.0867 -0.0450 27  SER A C   
213  C C   C SER A 26  ? 0.4217 0.3731 0.3270 0.0310  -0.0868 -0.0450 27  SER A C   
214  O O   A SER A 26  ? 0.4363 0.3829 0.3317 0.0371  -0.0993 -0.0464 27  SER A O   
215  O O   B SER A 26  ? 0.4356 0.3818 0.3307 0.0368  -0.0989 -0.0462 27  SER A O   
216  O O   C SER A 26  ? 0.4363 0.3826 0.3316 0.0371  -0.0992 -0.0464 27  SER A O   
217  C CB  A SER A 26  ? 0.4146 0.3232 0.2861 0.0230  -0.0738 -0.0296 27  SER A CB  
218  C CB  B SER A 26  ? 0.4188 0.3302 0.2944 0.0241  -0.0738 -0.0306 27  SER A CB  
219  C CB  C SER A 26  ? 0.4173 0.3267 0.2900 0.0234  -0.0738 -0.0298 27  SER A CB  
220  O OG  A SER A 26  ? 0.4652 0.3811 0.3518 0.0295  -0.0751 -0.0335 27  SER A OG  
221  O OG  B SER A 26  ? 0.5103 0.4030 0.3676 0.0149  -0.0638 -0.0232 27  SER A OG  
222  O OG  C SER A 26  ? 0.5192 0.4072 0.3720 0.0327  -0.0871 -0.0278 27  SER A OG  
223  N N   . ARG A 27  ? 0.3619 0.3350 0.2924 0.0330  -0.0840 -0.0522 28  ARG A N   
224  C CA  . ARG A 27  ? 0.3630 0.3578 0.3149 0.0425  -0.0943 -0.0637 28  ARG A CA  
225  C C   . ARG A 27  ? 0.3646 0.3884 0.3372 0.0357  -0.0906 -0.0731 28  ARG A C   
226  O O   . ARG A 27  ? 0.3525 0.3998 0.3472 0.0413  -0.0969 -0.0852 28  ARG A O   
227  C CB  . ARG A 27  ? 0.3793 0.3793 0.3458 0.0483  -0.0928 -0.0677 28  ARG A CB  
228  C CG  . ARG A 27  ? 0.4813 0.4506 0.4267 0.0544  -0.0960 -0.0594 28  ARG A CG  
229  C CD  . ARG A 27  ? 0.5123 0.4857 0.4708 0.0566  -0.0907 -0.0630 28  ARG A CD  
230  N NE  . ARG A 27  ? 0.6456 0.6398 0.6282 0.0676  -0.0991 -0.0755 28  ARG A NE  
231  C CZ  . ARG A 27  ? 0.8039 0.8162 0.8082 0.0671  -0.0925 -0.0839 28  ARG A CZ  
232  N NH1 . ARG A 27  ? 0.6653 0.6982 0.6933 0.0771  -0.0998 -0.0970 28  ARG A NH1 
233  N NH2 . ARG A 27  ? 0.6009 0.6124 0.6039 0.0564  -0.0786 -0.0802 28  ARG A NH2 
234  N N   . ASP A 28  ? 0.2948 0.3165 0.2602 0.0235  -0.0799 -0.0686 29  ASP A N   
235  C CA  . ASP A 28  ? 0.2908 0.3335 0.2705 0.0144  -0.0735 -0.0760 29  ASP A CA  
236  C C   . ASP A 28  ? 0.3178 0.3838 0.3223 0.0110  -0.0654 -0.0850 29  ASP A C   
237  O O   . ASP A 28  ? 0.3171 0.4063 0.3400 0.0080  -0.0652 -0.0967 29  ASP A O   
238  C CB  . ASP A 28  ? 0.3249 0.3772 0.3060 0.0180  -0.0860 -0.0837 29  ASP A CB  
239  C CG  . ASP A 28  ? 0.4004 0.4670 0.3886 0.0059  -0.0780 -0.0896 29  ASP A CG  
240  O OD1 . ASP A 28  ? 0.3942 0.4504 0.3736 -0.0043 -0.0648 -0.0827 29  ASP A OD1 
241  O OD2 . ASP A 28  ? 0.4196 0.5076 0.4226 0.0069  -0.0850 -0.1017 29  ASP A OD2 
242  N N   . ILE A 29  ? 0.2631 0.3229 0.2673 0.0106  -0.0582 -0.0802 30  ILE A N   
243  C CA  . ILE A 29  ? 0.2525 0.3311 0.2760 0.0069  -0.0500 -0.0881 30  ILE A CA  
244  C C   . ILE A 29  ? 0.2870 0.3649 0.3069 -0.0063 -0.0351 -0.0841 30  ILE A C   
245  O O   . ILE A 29  ? 0.2607 0.3212 0.2652 -0.0091 -0.0299 -0.0730 30  ILE A O   
246  C CB  . ILE A 29  ? 0.2864 0.3606 0.3125 0.0142  -0.0515 -0.0873 30  ILE A CB  
247  C CG1 . ILE A 29  ? 0.3029 0.3771 0.3340 0.0291  -0.0671 -0.0928 30  ILE A CG1 
248  C CG2 . ILE A 29  ? 0.2676 0.3595 0.3101 0.0078  -0.0405 -0.0949 30  ILE A CG2 
249  C CD1 . ILE A 29  ? 0.3580 0.4187 0.3851 0.0369  -0.0691 -0.0897 30  ILE A CD1 
250  N N   . LEU A 30  ? 0.2590 0.3558 0.2931 -0.0142 -0.0284 -0.0940 31  LEU A N   
251  C CA  . LEU A 30  ? 0.2600 0.3545 0.2895 -0.0268 -0.0141 -0.0913 31  LEU A CA  
252  C C   . LEU A 30  ? 0.2814 0.3581 0.2933 -0.0317 -0.0106 -0.0815 31  LEU A C   
253  O O   . LEU A 30  ? 0.2641 0.3324 0.2680 -0.0395 0.0000  -0.0764 31  LEU A O   
254  C CB  . LEU A 30  ? 0.2676 0.3583 0.2944 -0.0288 -0.0062 -0.0872 31  LEU A CB  
255  C CG  . LEU A 30  ? 0.3469 0.4581 0.3924 -0.0294 -0.0036 -0.1000 31  LEU A CG  
256  C CD1 . LEU A 30  ? 0.3516 0.4577 0.3903 -0.0345 0.0060  -0.0958 31  LEU A CD1 
257  C CD2 . LEU A 30  ? 0.4160 0.5465 0.4758 -0.0382 0.0020  -0.1133 31  LEU A CD2 
258  N N   . THR A 31  ? 0.2452 0.3160 0.2509 -0.0273 -0.0195 -0.0800 32  THR A N   
259  C CA  . THR A 31  ? 0.2427 0.2996 0.2342 -0.0327 -0.0158 -0.0740 32  THR A CA  
260  C C   . THR A 31  ? 0.3123 0.3803 0.3117 -0.0437 -0.0073 -0.0827 32  THR A C   
261  O O   . THR A 31  ? 0.2989 0.3876 0.3149 -0.0452 -0.0094 -0.0952 32  THR A O   
262  C CB  . THR A 31  ? 0.3096 0.3589 0.2917 -0.0266 -0.0271 -0.0724 32  THR A CB  
263  O OG1 . THR A 31  ? 0.3364 0.4041 0.3319 -0.0226 -0.0370 -0.0839 32  THR A OG1 
264  C CG2 . THR A 31  ? 0.2870 0.3197 0.2567 -0.0182 -0.0327 -0.0629 32  THR A CG2 
265  N N   . ASP A 32  ? 0.2729 0.3271 0.2612 -0.0515 0.0030  -0.0770 33  ASP A N   
266  C CA  . ASP A 32  ? 0.2779 0.3361 0.2693 -0.0635 0.0138  -0.0837 33  ASP A CA  
267  C C   . ASP A 32  ? 0.3095 0.3545 0.2898 -0.0696 0.0182  -0.0817 33  ASP A C   
268  O O   . ASP A 32  ? 0.3149 0.3562 0.2932 -0.0802 0.0291  -0.0853 33  ASP A O   
269  C CB  . ASP A 32  ? 0.2938 0.3456 0.2814 -0.0683 0.0248  -0.0794 33  ASP A CB  
270  C CG  . ASP A 32  ? 0.3668 0.3982 0.3393 -0.0633 0.0263  -0.0651 33  ASP A CG  
271  O OD1 . ASP A 32  ? 0.2990 0.3197 0.2639 -0.0584 0.0218  -0.0588 33  ASP A OD1 
272  O OD2 . ASP A 32  ? 0.4328 0.4601 0.4014 -0.0645 0.0317  -0.0610 33  ASP A OD2 
273  N N   . VAL A 33  ? 0.2563 0.2917 0.2274 -0.0637 0.0110  -0.0763 34  VAL A N   
274  C CA  . VAL A 33  ? 0.2638 0.2871 0.2245 -0.0694 0.0151  -0.0758 34  VAL A CA  
275  C C   . VAL A 33  ? 0.3116 0.3329 0.2655 -0.0637 0.0040  -0.0753 34  VAL A C   
276  O O   . VAL A 33  ? 0.2978 0.3174 0.2490 -0.0545 -0.0046 -0.0702 34  VAL A O   
277  C CB  . VAL A 33  ? 0.3109 0.3117 0.2587 -0.0712 0.0258  -0.0653 34  VAL A CB  
278  C CG1 . VAL A 33  ? 0.2996 0.2898 0.2399 -0.0619 0.0215  -0.0548 34  VAL A CG1 
279  C CG2 . VAL A 33  ? 0.3216 0.3101 0.2611 -0.0793 0.0336  -0.0675 34  VAL A CG2 
280  N N   A VAL A 34  ? 0.2754 0.2948 0.2241 -0.0700 0.0049  -0.0806 35  VAL A N   
281  N N   B VAL A 34  ? 0.2734 0.2929 0.2222 -0.0698 0.0047  -0.0806 35  VAL A N   
282  C CA  A VAL A 34  ? 0.2824 0.2957 0.2192 -0.0669 -0.0039 -0.0799 35  VAL A CA  
283  C CA  B VAL A 34  ? 0.2783 0.2913 0.2150 -0.0663 -0.0042 -0.0794 35  VAL A CA  
284  C C   A VAL A 34  ? 0.3319 0.3245 0.2546 -0.0722 0.0065  -0.0744 35  VAL A C   
285  C C   B VAL A 34  ? 0.3339 0.3271 0.2564 -0.0722 0.0058  -0.0749 35  VAL A C   
286  O O   A VAL A 34  ? 0.3298 0.3190 0.2539 -0.0809 0.0171  -0.0781 35  VAL A O   
287  O O   B VAL A 34  ? 0.3357 0.3264 0.2596 -0.0811 0.0157  -0.0793 35  VAL A O   
288  C CB  A VAL A 34  ? 0.3366 0.3671 0.2791 -0.0697 -0.0129 -0.0925 35  VAL A CB  
289  C CB  B VAL A 34  ? 0.3306 0.3612 0.2726 -0.0655 -0.0168 -0.0905 35  VAL A CB  
290  C CG1 A VAL A 34  ? 0.3500 0.3708 0.2749 -0.0665 -0.0228 -0.0907 35  VAL A CG1 
291  C CG1 B VAL A 34  ? 0.3318 0.3728 0.2807 -0.0774 -0.0107 -0.1024 35  VAL A CG1 
292  C CG2 A VAL A 34  ? 0.3270 0.3811 0.2881 -0.0638 -0.0225 -0.1002 35  VAL A CG2 
293  C CG2 B VAL A 34  ? 0.3421 0.3613 0.2660 -0.0599 -0.0277 -0.0864 35  VAL A CG2 
294  N N   . ILE A 35  ? 0.2899 0.2679 0.1991 -0.0674 0.0045  -0.0665 36  ILE A N   
295  C CA  . ILE A 35  ? 0.3084 0.2684 0.2056 -0.0714 0.0137  -0.0629 36  ILE A CA  
296  C C   . ILE A 35  ? 0.3718 0.3289 0.2557 -0.0744 0.0076  -0.0676 36  ILE A C   
297  O O   . ILE A 35  ? 0.3610 0.3167 0.2357 -0.0689 -0.0029 -0.0652 36  ILE A O   
298  C CB  . ILE A 35  ? 0.3337 0.2813 0.2260 -0.0656 0.0174  -0.0530 36  ILE A CB  
299  C CG1 . ILE A 35  ? 0.3196 0.2716 0.2236 -0.0614 0.0206  -0.0482 36  ILE A CG1 
300  C CG2 . ILE A 35  ? 0.3494 0.2812 0.2327 -0.0695 0.0275  -0.0518 36  ILE A CG2 
301  C CD1 . ILE A 35  ? 0.3174 0.2684 0.2277 -0.0667 0.0303  -0.0501 36  ILE A CD1 
302  N N   . VAL A 36  ? 0.3406 0.2947 0.2215 -0.0832 0.0142  -0.0741 37  VAL A N   
303  C CA  . VAL A 36  ? 0.3539 0.3053 0.2208 -0.0878 0.0093  -0.0799 37  VAL A CA  
304  C C   . VAL A 36  ? 0.4183 0.3494 0.2697 -0.0907 0.0183  -0.0759 37  VAL A C   
305  O O   . VAL A 36  ? 0.4107 0.3326 0.2654 -0.0944 0.0313  -0.0756 37  VAL A O   
306  C CB  . VAL A 36  ? 0.4058 0.3695 0.2794 -0.0971 0.0101  -0.0923 37  VAL A CB  
307  C CG1 . VAL A 36  ? 0.4217 0.3835 0.2793 -0.1019 0.0037  -0.0987 37  VAL A CG1 
308  C CG2 . VAL A 36  ? 0.4032 0.3907 0.2953 -0.0947 0.0018  -0.0984 37  VAL A CG2 
309  N N   . VAL A 37  ? 0.3900 0.3127 0.2236 -0.0888 0.0117  -0.0733 38  VAL A N   
310  C CA  . VAL A 37  ? 0.4029 0.3073 0.2209 -0.0925 0.0207  -0.0709 38  VAL A CA  
311  C C   . VAL A 37  ? 0.4986 0.3988 0.2960 -0.0982 0.0141  -0.0766 38  VAL A C   
312  O O   . VAL A 37  ? 0.4674 0.3637 0.2490 -0.0946 0.0026  -0.0736 38  VAL A O   
313  C CB  . VAL A 37  ? 0.4432 0.3392 0.2572 -0.0861 0.0214  -0.0618 38  VAL A CB  
314  C CG1 . VAL A 37  ? 0.4577 0.3384 0.2620 -0.0908 0.0342  -0.0615 38  VAL A CG1 
315  C CG2 . VAL A 37  ? 0.4183 0.3232 0.2527 -0.0791 0.0229  -0.0566 38  VAL A CG2 
316  N N   A SER A 38  ? 0.5000 0.4011 0.2970 -0.1071 0.0198  -0.0855 39  SER A N   
317  N N   B SER A 38  ? 0.4964 0.3948 0.2919 -0.1075 0.0216  -0.0849 39  SER A N   
318  C CA  A SER A 38  ? 0.5249 0.4246 0.3034 -0.1141 0.0135  -0.0931 39  SER A CA  
319  C CA  B SER A 38  ? 0.5224 0.4180 0.2988 -0.1150 0.0167  -0.0925 39  SER A CA  
320  C C   A SER A 38  ? 0.5354 0.4520 0.3150 -0.1089 -0.0060 -0.0959 39  SER A C   
321  C C   B SER A 38  ? 0.5521 0.4592 0.3219 -0.1099 -0.0034 -0.0936 39  SER A C   
322  O O   A SER A 38  ? 0.5146 0.4499 0.3157 -0.1076 -0.0088 -0.1006 39  SER A O   
323  O O   B SER A 38  ? 0.5595 0.4559 0.3061 -0.1075 -0.0124 -0.0898 39  SER A O   
324  C CB  A SER A 38  ? 0.6153 0.4947 0.3672 -0.1174 0.0171  -0.0901 39  SER A CB  
325  C CB  B SER A 38  ? 0.6007 0.4757 0.3547 -0.1203 0.0255  -0.0911 39  SER A CB  
326  O OG  A SER A 38  ? 0.8034 0.6710 0.5590 -0.1211 0.0349  -0.0894 39  SER A OG  
327  O OG  B SER A 38  ? 0.7165 0.5844 0.4786 -0.1261 0.0428  -0.0950 39  SER A OG  
328  N N   A ARG A 39  ? 0.4918 0.4010 0.2482 -0.1054 -0.0193 -0.0932 40  ARG A N   
329  N N   B ARG A 39  ? 0.4700 0.3984 0.2612 -0.1073 -0.0099 -0.0986 40  ARG A N   
330  C CA  A ARG A 39  ? 0.4890 0.4125 0.2447 -0.0980 -0.0400 -0.0959 40  ARG A CA  
331  C CA  B ARG A 39  ? 0.4660 0.4129 0.2616 -0.1009 -0.0290 -0.1027 40  ARG A CA  
332  C C   A ARG A 39  ? 0.5094 0.4381 0.2770 -0.0851 -0.0484 -0.0881 40  ARG A C   
333  C C   B ARG A 39  ? 0.4959 0.4419 0.2924 -0.0877 -0.0395 -0.0931 40  ARG A C   
334  O O   A ARG A 39  ? 0.5012 0.4442 0.2741 -0.0769 -0.0653 -0.0912 40  ARG A O   
335  O O   B ARG A 39  ? 0.4939 0.4587 0.3043 -0.0806 -0.0525 -0.0969 40  ARG A O   
336  C CB  A ARG A 39  ? 0.5132 0.4228 0.2345 -0.0991 -0.0521 -0.0961 40  ARG A CB  
337  C CB  B ARG A 39  ? 0.4846 0.4322 0.2596 -0.1047 -0.0412 -0.1102 40  ARG A CB  
338  C CG  A ARG A 39  ? 0.5704 0.4835 0.2825 -0.1108 -0.0503 -0.1076 40  ARG A CG  
339  C CG  B ARG A 39  ? 0.6244 0.5811 0.4053 -0.1178 -0.0335 -0.1234 40  ARG A CG  
340  C CD  A ARG A 39  ? 0.6197 0.5229 0.2981 -0.1098 -0.0671 -0.1082 40  ARG A CD  
341  C CD  B ARG A 39  ? 0.7113 0.6791 0.4797 -0.1201 -0.0497 -0.1336 40  ARG A CD  
342  N NE  A ARG A 39  ? 0.6442 0.5458 0.3079 -0.1228 -0.0632 -0.1185 40  ARG A NE  
343  N NE  B ARG A 39  ? 0.7815 0.7562 0.5535 -0.1345 -0.0407 -0.1470 40  ARG A NE  
344  C CZ  A ARG A 39  ? 0.8265 0.7495 0.4972 -0.1260 -0.0737 -0.1313 40  ARG A CZ  
345  C CZ  B ARG A 39  ? 0.9151 0.8718 0.6659 -0.1450 -0.0309 -0.1493 40  ARG A CZ  
346  N NH1 A ARG A 39  ? 0.7159 0.6352 0.3711 -0.1390 -0.0688 -0.1407 40  ARG A NH1 
347  N NH1 B ARG A 39  ? 0.7072 0.6388 0.4320 -0.1433 -0.0280 -0.1394 40  ARG A NH1 
348  N NH2 A ARG A 39  ? 0.6403 0.5898 0.3348 -0.1169 -0.0888 -0.1361 40  ARG A NH2 
349  N NH2 B ARG A 39  ? 0.7511 0.7144 0.5065 -0.1582 -0.0226 -0.1624 40  ARG A NH2 
350  N N   A GLU A 40  ? 0.4431 0.3613 0.2157 -0.0829 -0.0370 -0.0791 41  GLU A N   
351  N N   B GLU A 40  ? 0.4487 0.3746 0.2331 -0.0848 -0.0330 -0.0821 41  GLU A N   
352  C CA  A GLU A 40  ? 0.4278 0.3489 0.2102 -0.0719 -0.0431 -0.0718 41  GLU A CA  
353  C CA  B GLU A 40  ? 0.4410 0.3637 0.2262 -0.0737 -0.0406 -0.0731 41  GLU A CA  
354  C C   A GLU A 40  ? 0.4571 0.3963 0.2709 -0.0703 -0.0363 -0.0736 41  GLU A C   
355  C C   B GLU A 40  ? 0.4629 0.4015 0.2779 -0.0703 -0.0348 -0.0729 41  GLU A C   
356  O O   A GLU A 40  ? 0.4344 0.3745 0.2585 -0.0775 -0.0220 -0.0758 41  GLU A O   
357  O O   B GLU A 40  ? 0.4377 0.3759 0.2636 -0.0760 -0.0201 -0.0731 41  GLU A O   
358  C CB  A GLU A 40  ? 0.4536 0.3512 0.2183 -0.0706 -0.0369 -0.0612 41  GLU A CB  
359  C CB  B GLU A 40  ? 0.4720 0.3696 0.2361 -0.0745 -0.0331 -0.0635 41  GLU A CB  
360  C CG  A GLU A 40  ? 0.6503 0.5257 0.3791 -0.0731 -0.0428 -0.0586 41  GLU A CG  
361  C CG  B GLU A 40  ? 0.6424 0.5206 0.3716 -0.0764 -0.0413 -0.0618 41  GLU A CG  
362  C CD  A GLU A 40  ? 1.1027 0.9672 0.8146 -0.0631 -0.0584 -0.0520 41  GLU A CD  
363  C CD  B GLU A 40  ? 1.0527 0.9201 0.7666 -0.0662 -0.0557 -0.0545 41  GLU A CD  
364  O OE1 A GLU A 40  ? 1.1030 0.9556 0.8125 -0.0599 -0.0540 -0.0442 41  GLU A OE1 
365  O OE1 B GLU A 40  ? 1.0716 0.9429 0.7767 -0.0599 -0.0736 -0.0571 41  GLU A OE1 
366  O OE2 A GLU A 40  ? 1.1214 0.9884 0.8221 -0.0581 -0.0756 -0.0551 41  GLU A OE2 
367  O OE2 B GLU A 40  ? 1.0391 0.8938 0.7499 -0.0641 -0.0494 -0.0466 41  GLU A OE2 
368  N N   . GLN A 41  ? 0.4055 0.3569 0.2326 -0.0607 -0.0464 -0.0726 42  GLN A N   
369  C CA  . GLN A 41  ? 0.3760 0.3440 0.2302 -0.0584 -0.0416 -0.0740 42  GLN A CA  
370  C C   . GLN A 41  ? 0.3939 0.3552 0.2496 -0.0500 -0.0424 -0.0648 42  GLN A C   
371  O O   . GLN A 41  ? 0.3989 0.3523 0.2420 -0.0423 -0.0540 -0.0610 42  GLN A O   
372  C CB  . GLN A 41  ? 0.3973 0.3909 0.2694 -0.0556 -0.0529 -0.0849 42  GLN A CB  
373  C CG  . GLN A 41  ? 0.5616 0.5665 0.4370 -0.0658 -0.0508 -0.0965 42  GLN A CG  
374  C CD  . GLN A 41  ? 0.7721 0.8069 0.6718 -0.0656 -0.0579 -0.1098 42  GLN A CD  
375  O OE1 . GLN A 41  ? 0.6710 0.7201 0.5866 -0.0568 -0.0654 -0.1112 42  GLN A OE1 
376  N NE2 . GLN A 41  ? 0.7846 0.8303 0.6885 -0.0761 -0.0547 -0.1212 42  GLN A NE2 
377  N N   . PHE A 42  ? 0.3224 0.2860 0.1924 -0.0513 -0.0306 -0.0615 43  PHE A N   
378  C CA  . PHE A 42  ? 0.3229 0.2820 0.1961 -0.0445 -0.0301 -0.0538 43  PHE A CA  
379  C C   . PHE A 42  ? 0.3669 0.3434 0.2632 -0.0433 -0.0267 -0.0566 43  PHE A C   
380  O O   . PHE A 42  ? 0.3679 0.3472 0.2724 -0.0497 -0.0156 -0.0580 43  PHE A O   
381  C CB  . PHE A 42  ? 0.3424 0.2843 0.2059 -0.0478 -0.0183 -0.0462 43  PHE A CB  
382  C CG  . PHE A 42  ? 0.3789 0.3024 0.2182 -0.0513 -0.0183 -0.0442 43  PHE A CG  
383  C CD1 . PHE A 42  ? 0.4175 0.3368 0.2496 -0.0594 -0.0122 -0.0484 43  PHE A CD1 
384  C CD2 . PHE A 42  ? 0.4319 0.3405 0.2537 -0.0476 -0.0239 -0.0386 43  PHE A CD2 
385  C CE1 . PHE A 42  ? 0.4556 0.3576 0.2636 -0.0637 -0.0114 -0.0474 43  PHE A CE1 
386  C CE2 . PHE A 42  ? 0.4910 0.3804 0.2870 -0.0525 -0.0228 -0.0370 43  PHE A CE2 
387  C CZ  . PHE A 42  ? 0.4708 0.3579 0.2602 -0.0606 -0.0166 -0.0416 43  PHE A CZ  
388  N N   . ARG A 43  ? 0.3203 0.3063 0.2256 -0.0353 -0.0358 -0.0576 44  ARG A N   
389  C CA  . ARG A 43  ? 0.2871 0.2896 0.2133 -0.0347 -0.0321 -0.0612 44  ARG A CA  
390  C C   . ARG A 43  ? 0.3185 0.3120 0.2440 -0.0330 -0.0248 -0.0525 44  ARG A C   
391  O O   . ARG A 43  ? 0.3148 0.2946 0.2283 -0.0287 -0.0276 -0.0459 44  ARG A O   
392  C CB  . ARG A 43  ? 0.3013 0.3205 0.2400 -0.0267 -0.0448 -0.0685 44  ARG A CB  
393  C CG  . ARG A 43  ? 0.3573 0.3916 0.3013 -0.0281 -0.0534 -0.0796 44  ARG A CG  
394  C CD  . ARG A 43  ? 0.4531 0.5136 0.4209 -0.0231 -0.0608 -0.0912 44  ARG A CD  
395  N NE  . ARG A 43  ? 0.5847 0.6553 0.5688 -0.0282 -0.0484 -0.0932 44  ARG A NE  
396  C CZ  . ARG A 43  ? 0.7267 0.8103 0.7228 -0.0391 -0.0380 -0.1012 44  ARG A CZ  
397  N NH1 . ARG A 43  ? 0.6055 0.6977 0.6034 -0.0460 -0.0387 -0.1099 44  ARG A NH1 
398  N NH2 . ARG A 43  ? 0.5085 0.5963 0.5137 -0.0439 -0.0267 -0.1014 44  ARG A NH2 
399  N N   . ALA A 44  ? 0.2751 0.2750 0.2115 -0.0370 -0.0152 -0.0528 45  ALA A N   
400  C CA  . ALA A 44  ? 0.2815 0.2747 0.2174 -0.0352 -0.0092 -0.0451 45  ALA A CA  
401  C C   . ALA A 44  ? 0.2913 0.2950 0.2393 -0.0380 -0.0028 -0.0474 45  ALA A C   
402  O O   . ALA A 44  ? 0.2619 0.2781 0.2194 -0.0421 -0.0019 -0.0554 45  ALA A O   
403  C CB  . ALA A 44  ? 0.3051 0.2829 0.2300 -0.0384 -0.0014 -0.0388 45  ALA A CB  
404  N N   . HIS A 45  ? 0.2540 0.2532 0.2012 -0.0362 0.0015  -0.0411 46  HIS A N   
405  C CA  . HIS A 45  ? 0.2330 0.2377 0.1862 -0.0392 0.0081  -0.0414 46  HIS A CA  
406  C C   . HIS A 45  ? 0.2785 0.2705 0.2236 -0.0427 0.0166  -0.0357 46  HIS A C   
407  O O   . HIS A 45  ? 0.2601 0.2424 0.1991 -0.0394 0.0171  -0.0294 46  HIS A O   
408  C CB  . HIS A 45  ? 0.2207 0.2283 0.1766 -0.0341 0.0058  -0.0384 46  HIS A CB  
409  C CG  . HIS A 45  ? 0.2521 0.2685 0.2149 -0.0288 -0.0029 -0.0435 46  HIS A CG  
410  N ND1 . HIS A 45  ? 0.2701 0.2779 0.2261 -0.0231 -0.0099 -0.0404 46  HIS A ND1 
411  C CD2 . HIS A 45  ? 0.2579 0.2893 0.2330 -0.0283 -0.0053 -0.0521 46  HIS A CD2 
412  C CE1 . HIS A 45  ? 0.2629 0.2787 0.2262 -0.0179 -0.0174 -0.0461 46  HIS A CE1 
413  N NE2 . HIS A 45  ? 0.2538 0.2859 0.2308 -0.0204 -0.0152 -0.0539 46  HIS A NE2 
414  N N   . LYS A 46  ? 0.2686 0.2599 0.2136 -0.0495 0.0237  -0.0385 47  LYS A N   
415  C CA  . LYS A 46  ? 0.2629 0.2385 0.1985 -0.0519 0.0317  -0.0330 47  LYS A CA  
416  C C   . LYS A 46  ? 0.2864 0.2559 0.2180 -0.0458 0.0316  -0.0246 47  LYS A C   
417  O O   . LYS A 46  ? 0.2668 0.2254 0.1934 -0.0425 0.0332  -0.0197 47  LYS A O   
418  C CB  . LYS A 46  ? 0.2851 0.2582 0.2185 -0.0608 0.0401  -0.0369 47  LYS A CB  
419  C CG  . LYS A 46  ? 0.2932 0.2703 0.2298 -0.0683 0.0422  -0.0458 47  LYS A CG  
420  C CD  . LYS A 46  ? 0.2725 0.2494 0.2080 -0.0790 0.0517  -0.0514 47  LYS A CD  
421  C CE  . LYS A 46  ? 0.3478 0.3326 0.2891 -0.0877 0.0537  -0.0625 47  LYS A CE  
422  N NZ  . LYS A 46  ? 0.3365 0.3231 0.2782 -0.1000 0.0642  -0.0700 47  LYS A NZ  
423  N N   . THR A 47  ? 0.2538 0.2317 0.1887 -0.0440 0.0293  -0.0242 48  THR A N   
424  C CA  . THR A 47  ? 0.2520 0.2260 0.1830 -0.0388 0.0285  -0.0172 48  THR A CA  
425  C C   . THR A 47  ? 0.2620 0.2360 0.1953 -0.0326 0.0240  -0.0144 48  THR A C   
426  O O   . THR A 47  ? 0.2765 0.2451 0.2072 -0.0285 0.0246  -0.0095 48  THR A O   
427  C CB  . THR A 47  ? 0.3255 0.3084 0.2581 -0.0396 0.0277  -0.0184 48  THR A CB  
428  O OG1 . THR A 47  ? 0.3418 0.3378 0.2846 -0.0387 0.0228  -0.0245 48  THR A OG1 
429  C CG2 . THR A 47  ? 0.3383 0.3166 0.2639 -0.0471 0.0350  -0.0200 48  THR A CG2 
430  N N   . VAL A 48  ? 0.2151 0.1947 0.1528 -0.0320 0.0196  -0.0179 49  VAL A N   
431  C CA  . VAL A 48  ? 0.2235 0.2008 0.1608 -0.0284 0.0170  -0.0159 49  VAL A CA  
432  C C   . VAL A 48  ? 0.2546 0.2222 0.1879 -0.0290 0.0210  -0.0147 49  VAL A C   
433  O O   . VAL A 48  ? 0.2389 0.2043 0.1730 -0.0260 0.0224  -0.0124 49  VAL A O   
434  C CB  . VAL A 48  ? 0.2407 0.2214 0.1789 -0.0277 0.0112  -0.0191 49  VAL A CB  
435  C CG1 . VAL A 48  ? 0.2507 0.2248 0.1843 -0.0264 0.0107  -0.0173 49  VAL A CG1 
436  C CG2 . VAL A 48  ? 0.2363 0.2261 0.1798 -0.0259 0.0079  -0.0208 49  VAL A CG2 
437  N N   . LEU A 49  ? 0.2398 0.2031 0.1702 -0.0331 0.0231  -0.0176 50  LEU A N   
438  C CA  . LEU A 49  ? 0.2397 0.1927 0.1659 -0.0344 0.0280  -0.0175 50  LEU A CA  
439  C C   . LEU A 49  ? 0.2815 0.2278 0.2078 -0.0309 0.0326  -0.0133 50  LEU A C   
440  O O   . LEU A 49  ? 0.2793 0.2213 0.2067 -0.0278 0.0349  -0.0125 50  LEU A O   
441  C CB  . LEU A 49  ? 0.2373 0.1873 0.1602 -0.0405 0.0301  -0.0222 50  LEU A CB  
442  C CG  . LEU A 49  ? 0.2708 0.2274 0.1931 -0.0428 0.0238  -0.0272 50  LEU A CG  
443  C CD1 . LEU A 49  ? 0.2729 0.2290 0.1936 -0.0494 0.0261  -0.0333 50  LEU A CD1 
444  C CD2 . LEU A 49  ? 0.2905 0.2420 0.2063 -0.0411 0.0208  -0.0262 50  LEU A CD2 
445  N N   . MET A 50  ? 0.2535 0.1984 0.1779 -0.0311 0.0337  -0.0111 51  MET A N   
446  C CA  . MET A 50  ? 0.2644 0.1998 0.1852 -0.0265 0.0362  -0.0061 51  MET A CA  
447  C C   . MET A 50  ? 0.3132 0.2556 0.2396 -0.0188 0.0319  -0.0032 51  MET A C   
448  O O   . MET A 50  ? 0.3070 0.2441 0.2350 -0.0128 0.0328  -0.0014 51  MET A O   
449  C CB  . MET A 50  ? 0.2770 0.2076 0.1903 -0.0295 0.0382  -0.0039 51  MET A CB  
450  C CG  . MET A 50  ? 0.2978 0.2211 0.2060 -0.0385 0.0444  -0.0081 51  MET A CG  
451  S SD  . MET A 50  ? 0.3477 0.2715 0.2491 -0.0449 0.0472  -0.0081 51  MET A SD  
452  C CE  . MET A 50  ? 0.3325 0.2308 0.2167 -0.0412 0.0514  0.0004  51  MET A CE  
453  N N   . ALA A 51  ? 0.2745 0.2298 0.2055 -0.0189 0.0272  -0.0041 52  ALA A N   
454  C CA  . ALA A 51  ? 0.2574 0.2217 0.1945 -0.0134 0.0233  -0.0030 52  ALA A CA  
455  C C   . ALA A 51  ? 0.2741 0.2407 0.2181 -0.0118 0.0248  -0.0060 52  ALA A C   
456  O O   . ALA A 51  ? 0.2852 0.2594 0.2364 -0.0070 0.0230  -0.0065 52  ALA A O   
457  C CB  . ALA A 51  ? 0.2588 0.2341 0.1980 -0.0155 0.0193  -0.0044 52  ALA A CB  
458  N N   . CYS A 52  ? 0.2355 0.1965 0.1769 -0.0165 0.0282  -0.0090 53  CYS A N   
459  C CA  . CYS A 52  ? 0.2335 0.1949 0.1782 -0.0176 0.0314  -0.0127 53  CYS A CA  
460  C C   . CYS A 52  ? 0.2919 0.2445 0.2368 -0.0167 0.0372  -0.0145 53  CYS A C   
461  O O   . CYS A 52  ? 0.2661 0.2206 0.2155 -0.0172 0.0410  -0.0186 53  CYS A O   
462  C CB  . CYS A 52  ? 0.2358 0.1955 0.1739 -0.0238 0.0305  -0.0150 53  CYS A CB  
463  S SG  . CYS A 52  ? 0.2712 0.2390 0.2098 -0.0241 0.0244  -0.0142 53  CYS A SG  
464  N N   . SER A 53  ? 0.2590 0.2013 0.1982 -0.0170 0.0391  -0.0127 54  SER A N   
465  C CA  . SER A 53  ? 0.2538 0.1847 0.1909 -0.0178 0.0455  -0.0152 54  SER A CA  
466  C C   . SER A 53  ? 0.3183 0.2377 0.2529 -0.0127 0.0472  -0.0118 54  SER A C   
467  O O   . SER A 53  ? 0.2923 0.2063 0.2195 -0.0151 0.0461  -0.0085 54  SER A O   
468  C CB  . SER A 53  ? 0.2821 0.2079 0.2103 -0.0266 0.0472  -0.0182 54  SER A CB  
469  O OG  . SER A 53  ? 0.3156 0.2288 0.2387 -0.0295 0.0531  -0.0204 54  SER A OG  
470  N N   . GLY A 54  ? 0.2982 0.2123 0.2384 -0.0061 0.0504  -0.0132 55  GLY A N   
471  C CA  . GLY A 54  ? 0.3052 0.2029 0.2403 0.0000  0.0521  -0.0096 55  GLY A CA  
472  C C   . GLY A 54  ? 0.3513 0.2324 0.2743 -0.0082 0.0583  -0.0104 55  GLY A C   
473  O O   . GLY A 54  ? 0.3484 0.2147 0.2611 -0.0081 0.0593  -0.0060 55  GLY A O   
474  N N   . LEU A 55  ? 0.3275 0.2106 0.2500 -0.0168 0.0625  -0.0165 56  LEU A N   
475  C CA  . LEU A 55  ? 0.3425 0.2134 0.2550 -0.0261 0.0680  -0.0192 56  LEU A CA  
476  C C   . LEU A 55  ? 0.3591 0.2337 0.2654 -0.0328 0.0650  -0.0172 56  LEU A C   
477  O O   . LEU A 55  ? 0.3481 0.2093 0.2461 -0.0366 0.0693  -0.0163 56  LEU A O   
478  C CB  . LEU A 55  ? 0.3413 0.2144 0.2531 -0.0335 0.0720  -0.0266 56  LEU A CB  
479  C CG  . LEU A 55  ? 0.4084 0.2702 0.3106 -0.0433 0.0776  -0.0312 56  LEU A CG  
480  C CD1 . LEU A 55  ? 0.4326 0.2735 0.3317 -0.0408 0.0862  -0.0324 56  LEU A CD1 
481  C CD2 . LEU A 55  ? 0.3757 0.2440 0.2746 -0.0513 0.0777  -0.0377 56  LEU A CD2 
482  N N   . PHE A 56  ? 0.2980 0.1899 0.2087 -0.0341 0.0583  -0.0171 57  PHE A N   
483  C CA  . PHE A 56  ? 0.2912 0.1895 0.1994 -0.0396 0.0556  -0.0170 57  PHE A CA  
484  C C   . PHE A 56  ? 0.3429 0.2352 0.2471 -0.0361 0.0555  -0.0110 57  PHE A C   
485  O O   . PHE A 56  ? 0.3250 0.2132 0.2231 -0.0428 0.0585  -0.0119 57  PHE A O   
486  C CB  . PHE A 56  ? 0.2929 0.2087 0.2064 -0.0407 0.0484  -0.0188 57  PHE A CB  
487  C CG  . PHE A 56  ? 0.2985 0.2164 0.2100 -0.0461 0.0479  -0.0246 57  PHE A CG  
488  C CD1 . PHE A 56  ? 0.3253 0.2399 0.2326 -0.0539 0.0509  -0.0301 57  PHE A CD1 
489  C CD2 . PHE A 56  ? 0.3049 0.2272 0.2167 -0.0441 0.0446  -0.0250 57  PHE A CD2 
490  C CE1 . PHE A 56  ? 0.3326 0.2489 0.2359 -0.0586 0.0492  -0.0356 57  PHE A CE1 
491  C CE2 . PHE A 56  ? 0.3454 0.2668 0.2506 -0.0492 0.0433  -0.0296 57  PHE A CE2 
492  C CZ  . PHE A 56  ? 0.3281 0.2469 0.2291 -0.0558 0.0450  -0.0347 57  PHE A CZ  
493  N N   . TYR A 57  ? 0.3118 0.2029 0.2184 -0.0262 0.0525  -0.0058 58  TYR A N   
494  C CA  . TYR A 57  ? 0.3338 0.2161 0.2325 -0.0218 0.0513  0.0007  58  TYR A CA  
495  C C   . TYR A 57  ? 0.3944 0.2521 0.2794 -0.0250 0.0588  0.0023  58  TYR A C   
496  O O   . TYR A 57  ? 0.3732 0.2223 0.2467 -0.0306 0.0615  0.0045  58  TYR A O   
497  C CB  . TYR A 57  ? 0.3537 0.2401 0.2586 -0.0095 0.0455  0.0047  58  TYR A CB  
498  C CG  . TYR A 57  ? 0.3997 0.2741 0.2936 -0.0029 0.0427  0.0121  58  TYR A CG  
499  C CD1 . TYR A 57  ? 0.4262 0.3044 0.3126 -0.0065 0.0401  0.0150  58  TYR A CD1 
500  C CD2 . TYR A 57  ? 0.4601 0.3184 0.3500 0.0074  0.0422  0.0158  58  TYR A CD2 
501  C CE1 . TYR A 57  ? 0.4581 0.3228 0.3300 -0.0011 0.0373  0.0223  58  TYR A CE1 
502  C CE2 . TYR A 57  ? 0.5073 0.3514 0.3832 0.0146  0.0380  0.0234  58  TYR A CE2 
503  C CZ  . TYR A 57  ? 0.5818 0.4290 0.4476 0.0098  0.0354  0.0270  58  TYR A CZ  
504  O OH  . TYR A 57  ? 0.6469 0.4781 0.4952 0.0165  0.0310  0.0350  58  TYR A OH  
505  N N   A SER A 58  ? 0.3667 0.2118 0.2519 -0.0225 0.0634  0.0004  59  SER A N   
506  N N   B SER A 58  ? 0.3637 0.2089 0.2490 -0.0225 0.0634  0.0004  59  SER A N   
507  C CA  A SER A 58  ? 0.3893 0.2076 0.2608 -0.0255 0.0715  0.0012  59  SER A CA  
508  C CA  B SER A 58  ? 0.3854 0.2038 0.2570 -0.0256 0.0715  0.0011  59  SER A CA  
509  C C   A SER A 58  ? 0.4481 0.2648 0.3135 -0.0411 0.0784  -0.0046 59  SER A C   
510  C C   B SER A 58  ? 0.4454 0.2624 0.3109 -0.0411 0.0783  -0.0045 59  SER A C   
511  O O   A SER A 58  ? 0.4749 0.2734 0.3257 -0.0470 0.0843  -0.0026 59  SER A O   
512  O O   B SER A 58  ? 0.4702 0.2694 0.3211 -0.0469 0.0840  -0.0024 59  SER A O   
513  C CB  A SER A 58  ? 0.4223 0.2307 0.2983 -0.0198 0.0751  -0.0017 59  SER A CB  
514  C CB  B SER A 58  ? 0.4144 0.2236 0.2909 -0.0205 0.0754  -0.0023 59  SER A CB  
515  O OG  A SER A 58  ? 0.4703 0.2776 0.3516 -0.0047 0.0694  0.0028  59  SER A OG  
516  O OG  B SER A 58  ? 0.4807 0.2615 0.3433 -0.0234 0.0838  -0.0020 59  SER A OG  
517  N N   . ILE A 59  ? 0.3905 0.2261 0.2662 -0.0479 0.0775  -0.0121 60  ILE A N   
518  C CA  . ILE A 59  ? 0.3796 0.2199 0.2538 -0.0619 0.0820  -0.0198 60  ILE A CA  
519  C C   . ILE A 59  ? 0.4123 0.2591 0.2836 -0.0677 0.0818  -0.0193 60  ILE A C   
520  O O   . ILE A 59  ? 0.4299 0.2644 0.2915 -0.0778 0.0901  -0.0219 60  ILE A O   
521  C CB  . ILE A 59  ? 0.3889 0.2500 0.2742 -0.0652 0.0775  -0.0273 60  ILE A CB  
522  C CG1 . ILE A 59  ? 0.3915 0.2435 0.2763 -0.0637 0.0810  -0.0302 60  ILE A CG1 
523  C CG2 . ILE A 59  ? 0.3745 0.2469 0.2616 -0.0779 0.0791  -0.0362 60  ILE A CG2 
524  C CD1 . ILE A 59  ? 0.4096 0.2789 0.3008 -0.0652 0.0753  -0.0354 60  ILE A CD1 
525  N N   . PHE A 60  ? 0.3458 0.2107 0.2248 -0.0622 0.0736  -0.0166 61  PHE A N   
526  C CA  . PHE A 60  ? 0.3516 0.2259 0.2300 -0.0685 0.0739  -0.0182 61  PHE A CA  
527  C C   . PHE A 60  ? 0.4077 0.2638 0.2703 -0.0675 0.0775  -0.0106 61  PHE A C   
528  O O   . PHE A 60  ? 0.4201 0.2814 0.2797 -0.0749 0.0802  -0.0128 61  PHE A O   
529  C CB  . PHE A 60  ? 0.3365 0.2371 0.2292 -0.0649 0.0647  -0.0205 61  PHE A CB  
530  C CG  . PHE A 60  ? 0.3329 0.2479 0.2362 -0.0669 0.0608  -0.0280 61  PHE A CG  
531  C CD1 . PHE A 60  ? 0.3686 0.2893 0.2746 -0.0773 0.0644  -0.0375 61  PHE A CD1 
532  C CD2 . PHE A 60  ? 0.3223 0.2446 0.2315 -0.0590 0.0536  -0.0260 61  PHE A CD2 
533  C CE1 . PHE A 60  ? 0.3652 0.2984 0.2786 -0.0782 0.0590  -0.0441 61  PHE A CE1 
534  C CE2 . PHE A 60  ? 0.3468 0.2786 0.2609 -0.0610 0.0495  -0.0319 61  PHE A CE2 
535  C CZ  . PHE A 60  ? 0.3358 0.2729 0.2514 -0.0698 0.0513  -0.0405 61  PHE A CZ  
536  N N   . THR A 61  ? 0.3904 0.2245 0.2421 -0.0588 0.0777  -0.0023 62  THR A N   
537  C CA  . THR A 61  ? 0.4132 0.2237 0.2442 -0.0577 0.0807  0.0057  62  THR A CA  
538  C C   . THR A 61  ? 0.5093 0.2909 0.3233 -0.0670 0.0926  0.0045  62  THR A C   
539  O O   . THR A 61  ? 0.5250 0.2804 0.3166 -0.0691 0.0976  0.0107  62  THR A O   
540  C CB  . THR A 61  ? 0.4970 0.2998 0.3243 -0.0415 0.0724  0.0154  62  THR A CB  
541  O OG1 . THR A 61  ? 0.4589 0.2554 0.2930 -0.0331 0.0715  0.0153  62  THR A OG1 
542  C CG2 . THR A 61  ? 0.4370 0.2655 0.2764 -0.0351 0.0623  0.0166  62  THR A CG2 
543  N N   . ASP A 62  ? 0.4674 0.2517 0.2899 -0.0734 0.0975  -0.0037 63  ASP A N   
544  C CA  . ASP A 62  ? 0.4939 0.2519 0.3013 -0.0846 0.1100  -0.0069 63  ASP A CA  
545  C C   . ASP A 62  ? 0.5556 0.3192 0.3585 -0.1017 0.1182  -0.0139 63  ASP A C   
546  O O   . ASP A 62  ? 0.5020 0.2967 0.3231 -0.1074 0.1152  -0.0228 63  ASP A O   
547  C CB  . ASP A 62  ? 0.5073 0.2685 0.3252 -0.0873 0.1128  -0.0149 63  ASP A CB  
548  C CG  . ASP A 62  ? 0.6265 0.3623 0.4298 -0.1008 0.1265  -0.0201 63  ASP A CG  
549  O OD1 . ASP A 62  ? 0.6983 0.4006 0.4851 -0.0960 0.1315  -0.0140 63  ASP A OD1 
550  O OD2 . ASP A 62  ? 0.6017 0.3507 0.4100 -0.1163 0.1324  -0.0308 63  ASP A OD2 
551  N N   . GLN A 63  ? 0.5982 0.3306 0.3763 -0.1102 0.1289  -0.0107 64  GLN A N   
552  C CA  . GLN A 63  ? 0.6216 0.3555 0.3924 -0.1284 0.1394  -0.0178 64  GLN A CA  
553  C C   . GLN A 63  ? 0.6481 0.4052 0.4369 -0.1438 0.1457  -0.0343 64  GLN A C   
554  O O   . GLN A 63  ? 0.6563 0.4312 0.4509 -0.1564 0.1506  -0.0433 64  GLN A O   
555  C CB  . GLN A 63  ? 0.6921 0.3812 0.4281 -0.1356 0.1513  -0.0109 64  GLN A CB  
556  C CG  . GLN A 63  ? 0.9189 0.5908 0.6350 -0.1239 0.1447  0.0036  64  GLN A CG  
557  N N   . LEU A 64  ? 0.5573 0.3155 0.3551 -0.1432 0.1456  -0.0394 65  LEU A N   
558  C CA  . LEU A 64  ? 0.5284 0.3118 0.3441 -0.1564 0.1487  -0.0556 65  LEU A CA  
559  C C   . LEU A 64  ? 0.5555 0.3763 0.3971 -0.1466 0.1341  -0.0593 65  LEU A C   
560  O O   . LEU A 64  ? 0.5635 0.4148 0.4225 -0.1534 0.1315  -0.0706 65  LEU A O   
561  C CB  . LEU A 64  ? 0.5469 0.3094 0.3552 -0.1640 0.1579  -0.0608 65  LEU A CB  
562  C CG  . LEU A 64  ? 0.6410 0.3703 0.4262 -0.1807 0.1756  -0.0636 65  LEU A CG  
563  C CD1 . LEU A 64  ? 0.6679 0.3778 0.4476 -0.1870 0.1837  -0.0693 65  LEU A CD1 
564  C CD2 . LEU A 64  ? 0.6942 0.4436 0.4859 -0.2001 0.1842  -0.0770 65  LEU A CD2 
565  N N   . LYS A 65  ? 0.4763 0.2939 0.3202 -0.1311 0.1249  -0.0509 66  LYS A N   
566  C CA  . LYS A 65  ? 0.4256 0.2725 0.2891 -0.1230 0.1123  -0.0539 66  LYS A CA  
567  C C   . LYS A 65  ? 0.4767 0.3482 0.3518 -0.1167 0.1027  -0.0521 66  LYS A C   
568  O O   . LYS A 65  ? 0.4493 0.3470 0.3404 -0.1147 0.0940  -0.0582 66  LYS A O   
569  C CB  . LYS A 65  ? 0.4243 0.2607 0.2864 -0.1103 0.1074  -0.0469 66  LYS A CB  
570  C CG  . LYS A 65  ? 0.4457 0.2614 0.2996 -0.1160 0.1162  -0.0510 66  LYS A CG  
571  C CD  . LYS A 65  ? 0.4125 0.2233 0.2688 -0.1035 0.1112  -0.0462 66  LYS A CD  
572  C CE  . LYS A 65  ? 0.4568 0.2415 0.3030 -0.1069 0.1211  -0.0488 66  LYS A CE  
573  N NZ  . LYS A 65  ? 0.5132 0.2642 0.3430 -0.1030 0.1285  -0.0405 66  LYS A NZ  
574  N N   . CYS A 66  ? 0.4707 0.3323 0.3360 -0.1143 0.1045  -0.0443 67  CYS A N   
575  C CA  . CYS A 66  ? 0.4557 0.3383 0.3303 -0.1094 0.0970  -0.0430 67  CYS A CA  
576  C C   . CYS A 66  ? 0.5045 0.4161 0.3961 -0.1189 0.0967  -0.0569 67  CYS A C   
577  O O   . CYS A 66  ? 0.4980 0.4321 0.4030 -0.1127 0.0878  -0.0583 67  CYS A O   
578  C CB  . CYS A 66  ? 0.4869 0.3514 0.3442 -0.1085 0.1010  -0.0340 67  CYS A CB  
579  S SG  . CYS A 66  ? 0.5753 0.4219 0.4151 -0.1280 0.1180  -0.0397 67  CYS A SG  
580  N N   . ASN A 67  ? 0.4623 0.3734 0.3538 -0.1338 0.1067  -0.0679 68  ASN A N   
581  C CA  . ASN A 67  ? 0.4585 0.3987 0.3681 -0.1439 0.1075  -0.0836 68  ASN A CA  
582  C C   . ASN A 67  ? 0.4856 0.4474 0.4120 -0.1431 0.0993  -0.0937 68  ASN A C   
583  O O   . ASN A 67  ? 0.4567 0.4457 0.4008 -0.1496 0.0976  -0.1080 68  ASN A O   
584  C CB  . ASN A 67  ? 0.4758 0.4054 0.3759 -0.1626 0.1243  -0.0917 68  ASN A CB  
585  C CG  . ASN A 67  ? 0.6506 0.5622 0.5332 -0.1642 0.1312  -0.0830 68  ASN A CG  
586  O OD1 . ASN A 67  ? 0.6731 0.5539 0.5323 -0.1734 0.1439  -0.0789 68  ASN A OD1 
587  N ND2 . ASN A 67  ? 0.5282 0.4556 0.4186 -0.1548 0.1228  -0.0794 68  ASN A ND2 
588  N N   . LEU A 68  ? 0.4548 0.4053 0.3757 -0.1350 0.0938  -0.0871 69  LEU A N   
589  C CA  . LEU A 68  ? 0.4260 0.3937 0.3580 -0.1342 0.0855  -0.0955 69  LEU A CA  
590  C C   . LEU A 68  ? 0.4444 0.4350 0.3899 -0.1218 0.0699  -0.0949 69  LEU A C   
591  O O   . LEU A 68  ? 0.4243 0.4093 0.3663 -0.1110 0.0652  -0.0838 69  LEU A O   
592  C CB  . LEU A 68  ? 0.4340 0.3801 0.3534 -0.1316 0.0868  -0.0898 69  LEU A CB  
593  C CG  . LEU A 68  ? 0.5024 0.4223 0.4074 -0.1433 0.1020  -0.0912 69  LEU A CG  
594  C CD1 . LEU A 68  ? 0.5075 0.4061 0.4017 -0.1376 0.1025  -0.0848 69  LEU A CD1 
595  C CD2 . LEU A 68  ? 0.5188 0.4520 0.4311 -0.1601 0.1085  -0.1082 69  LEU A CD2 
596  N N   A SER A 69  ? 0.3976 0.4132 0.3577 -0.1231 0.0616  -0.1070 70  SER A N   
597  N N   B SER A 69  ? 0.3935 0.4091 0.3535 -0.1233 0.0617  -0.1071 70  SER A N   
598  C CA  A SER A 69  ? 0.3756 0.4102 0.3465 -0.1107 0.0457  -0.1069 70  SER A CA  
599  C CA  B SER A 69  ? 0.3699 0.4053 0.3413 -0.1112 0.0458  -0.1077 70  SER A CA  
600  C C   A SER A 69  ? 0.3853 0.4136 0.3480 -0.1040 0.0363  -0.1031 70  SER A C   
601  C C   B SER A 69  ? 0.3834 0.4121 0.3464 -0.1042 0.0363  -0.1034 70  SER A C   
602  O O   A SER A 69  ? 0.3543 0.3890 0.3188 -0.0929 0.0236  -0.0997 70  SER A O   
603  O O   B SER A 69  ? 0.3530 0.3885 0.3180 -0.0931 0.0236  -0.1001 70  SER A O   
604  C CB  A SER A 69  ? 0.4225 0.4887 0.4146 -0.1138 0.0405  -0.1228 70  SER A CB  
605  C CB  B SER A 69  ? 0.4082 0.4752 0.4006 -0.1152 0.0409  -0.1242 70  SER A CB  
606  O OG  A SER A 69  ? 0.5207 0.5974 0.5178 -0.1235 0.0412  -0.1358 70  SER A OG  
607  O OG  B SER A 69  ? 0.4639 0.5382 0.4643 -0.1211 0.0498  -0.1283 70  SER A OG  
608  N N   . VAL A 70  ? 0.3549 0.3685 0.3068 -0.1115 0.0432  -0.1041 71  VAL A N   
609  C CA  . VAL A 70  ? 0.3586 0.3636 0.2998 -0.1078 0.0371  -0.1014 71  VAL A CA  
610  C C   . VAL A 70  ? 0.3938 0.3706 0.3200 -0.1097 0.0486  -0.0927 71  VAL A C   
611  O O   . VAL A 70  ? 0.3846 0.3500 0.3073 -0.1193 0.0611  -0.0955 71  VAL A O   
612  C CB  . VAL A 70  ? 0.4155 0.4355 0.3607 -0.1153 0.0322  -0.1155 71  VAL A CB  
613  C CG1 . VAL A 70  ? 0.4255 0.4335 0.3554 -0.1131 0.0273  -0.1126 71  VAL A CG1 
614  C CG2 . VAL A 70  ? 0.4107 0.4609 0.3734 -0.1112 0.0189  -0.1254 71  VAL A CG2 
615  N N   . ILE A 71  ? 0.3256 0.2906 0.2427 -0.1008 0.0446  -0.0832 72  ILE A N   
616  C CA  . ILE A 71  ? 0.3259 0.2671 0.2313 -0.1003 0.0537  -0.0763 72  ILE A CA  
617  C C   . ILE A 71  ? 0.3722 0.3095 0.2684 -0.1000 0.0496  -0.0780 72  ILE A C   
618  O O   . ILE A 71  ? 0.3761 0.3195 0.2701 -0.0933 0.0393  -0.0752 72  ILE A O   
619  C CB  . ILE A 71  ? 0.3540 0.2853 0.2585 -0.0906 0.0553  -0.0642 72  ILE A CB  
620  C CG1 . ILE A 71  ? 0.3630 0.2953 0.2725 -0.0919 0.0600  -0.0621 72  ILE A CG1 
621  C CG2 . ILE A 71  ? 0.3860 0.2961 0.2816 -0.0878 0.0628  -0.0587 72  ILE A CG2 
622  C CD1 . ILE A 71  ? 0.4228 0.3393 0.3260 -0.1017 0.0731  -0.0649 72  ILE A CD1 
623  N N   . ASN A 72  ? 0.3609 0.2853 0.2494 -0.1079 0.0585  -0.0828 73  ASN A N   
624  C CA  . ASN A 72  ? 0.3710 0.2897 0.2483 -0.1095 0.0566  -0.0855 73  ASN A CA  
625  C C   . ASN A 72  ? 0.4093 0.3086 0.2799 -0.1049 0.0646  -0.0784 73  ASN A C   
626  O O   . ASN A 72  ? 0.3863 0.2706 0.2568 -0.1067 0.0759  -0.0777 73  ASN A O   
627  C CB  . ASN A 72  ? 0.4060 0.3245 0.2796 -0.1220 0.0614  -0.0975 73  ASN A CB  
628  C CG  . ASN A 72  ? 0.6286 0.5696 0.5119 -0.1277 0.0543  -0.1074 73  ASN A CG  
629  O OD1 . ASN A 72  ? 0.4806 0.4387 0.3667 -0.1229 0.0403  -0.1091 73  ASN A OD1 
630  N ND2 . ASN A 72  ? 0.5740 0.5148 0.4625 -0.1382 0.0640  -0.1151 73  ASN A ND2 
631  N N   . LEU A 73  ? 0.3488 0.2475 0.2134 -0.0992 0.0593  -0.0741 74  LEU A N   
632  C CA  . LEU A 73  ? 0.3459 0.2298 0.2068 -0.0954 0.0673  -0.0697 74  LEU A CA  
633  C C   . LEU A 73  ? 0.4034 0.2755 0.2537 -0.1032 0.0752  -0.0770 74  LEU A C   
634  O O   . LEU A 73  ? 0.4087 0.2848 0.2511 -0.1113 0.0719  -0.0846 74  LEU A O   
635  C CB  . LEU A 73  ? 0.3376 0.2246 0.1962 -0.0882 0.0612  -0.0634 74  LEU A CB  
636  C CG  . LEU A 73  ? 0.3624 0.2603 0.2308 -0.0801 0.0536  -0.0563 74  LEU A CG  
637  C CD1 . LEU A 73  ? 0.3697 0.2658 0.2350 -0.0746 0.0517  -0.0510 74  LEU A CD1 
638  C CD2 . LEU A 73  ? 0.3658 0.2626 0.2455 -0.0767 0.0587  -0.0528 74  LEU A CD2 
639  N N   . ASP A 74  ? 0.3693 0.2280 0.2200 -0.1004 0.0853  -0.0757 75  ASP A N   
640  C CA  . ASP A 74  ? 0.3929 0.2386 0.2346 -0.1069 0.0950  -0.0830 75  ASP A CA  
641  C C   . ASP A 74  ? 0.4481 0.2977 0.2742 -0.1130 0.0891  -0.0871 75  ASP A C   
642  O O   . ASP A 74  ? 0.4418 0.2971 0.2646 -0.1087 0.0817  -0.0819 75  ASP A O   
643  C CB  . ASP A 74  ? 0.4174 0.2524 0.2654 -0.0998 0.1045  -0.0807 75  ASP A CB  
644  C CG  . ASP A 74  ? 0.5055 0.3260 0.3474 -0.1054 0.1167  -0.0892 75  ASP A CG  
645  O OD1 . ASP A 74  ? 0.5225 0.3430 0.3520 -0.1126 0.1175  -0.0948 75  ASP A OD1 
646  O OD2 . ASP A 74  ? 0.5220 0.3296 0.3702 -0.1023 0.1256  -0.0903 75  ASP A OD2 
647  N N   . PRO A 75  ? 0.4649 0.3103 0.2795 -0.1234 0.0917  -0.0963 76  PRO A N   
648  C CA  . PRO A 75  ? 0.4734 0.3206 0.2689 -0.1291 0.0845  -0.0996 76  PRO A CA  
649  C C   . PRO A 75  ? 0.5170 0.3551 0.3015 -0.1282 0.0890  -0.0974 76  PRO A C   
650  O O   . PRO A 75  ? 0.5301 0.3675 0.2960 -0.1315 0.0816  -0.0973 76  PRO A O   
651  C CB  . PRO A 75  ? 0.5128 0.3559 0.2989 -0.1409 0.0889  -0.1110 76  PRO A CB  
652  C CG  . PRO A 75  ? 0.5823 0.4158 0.3808 -0.1418 0.1024  -0.1137 76  PRO A CG  
653  C CD  . PRO A 75  ? 0.5004 0.3376 0.3163 -0.1311 0.1012  -0.1042 76  PRO A CD  
654  N N   . GLU A 76  ? 0.4835 0.3146 0.2788 -0.1238 0.1009  -0.0962 77  GLU A N   
655  C CA  . GLU A 76  ? 0.5086 0.3336 0.2973 -0.1239 0.1075  -0.0962 77  GLU A CA  
656  C C   . GLU A 76  ? 0.4973 0.3299 0.2879 -0.1169 0.0987  -0.0871 77  GLU A C   
657  O O   . GLU A 76  ? 0.4936 0.3218 0.2745 -0.1191 0.1020  -0.0868 77  GLU A O   
658  C CB  . GLU A 76  ? 0.5385 0.3574 0.3435 -0.1198 0.1222  -0.0996 77  GLU A CB  
659  C CG  . GLU A 76  ? 0.7823 0.5942 0.5803 -0.1244 0.1337  -0.1060 77  GLU A CG  
660  C CD  . GLU A 76  ? 1.1121 0.9126 0.8952 -0.1358 0.1430  -0.1169 77  GLU A CD  
661  O OE1 . GLU A 76  ? 1.1129 0.9068 0.9060 -0.1350 0.1514  -0.1223 77  GLU A OE1 
662  O OE2 . GLU A 76  ? 1.0268 0.8228 0.7861 -0.1457 0.1418  -0.1200 77  GLU A OE2 
663  N N   . ILE A 77  ? 0.4373 0.2805 0.2401 -0.1095 0.0887  -0.0803 78  ILE A N   
664  C CA  . ILE A 77  ? 0.4243 0.2742 0.2301 -0.1027 0.0808  -0.0723 78  ILE A CA  
665  C C   . ILE A 77  ? 0.4814 0.3289 0.2652 -0.1063 0.0701  -0.0705 78  ILE A C   
666  O O   . ILE A 77  ? 0.4777 0.3277 0.2526 -0.1090 0.0608  -0.0726 78  ILE A O   
667  C CB  . ILE A 77  ? 0.4329 0.2940 0.2584 -0.0938 0.0749  -0.0664 78  ILE A CB  
668  C CG1 . ILE A 77  ? 0.4270 0.2859 0.2701 -0.0892 0.0851  -0.0669 78  ILE A CG1 
669  C CG2 . ILE A 77  ? 0.3997 0.2675 0.2277 -0.0875 0.0670  -0.0589 78  ILE A CG2 
670  C CD1 . ILE A 77  ? 0.4901 0.3461 0.3408 -0.0853 0.0948  -0.0678 78  ILE A CD1 
671  N N   . ASN A 78  ? 0.4795 0.3213 0.2542 -0.1063 0.0714  -0.0672 79  ASN A N   
672  C CA  . ASN A 78  ? 0.4992 0.3322 0.2484 -0.1092 0.0624  -0.0640 79  ASN A CA  
673  C C   . ASN A 78  ? 0.4871 0.3283 0.2418 -0.1003 0.0479  -0.0566 79  ASN A C   
674  O O   . ASN A 78  ? 0.4624 0.3105 0.2342 -0.0941 0.0494  -0.0523 79  ASN A O   
675  C CB  . ASN A 78  ? 0.5378 0.3588 0.2745 -0.1146 0.0729  -0.0644 79  ASN A CB  
676  C CG  . ASN A 78  ? 0.6971 0.5032 0.4031 -0.1181 0.0651  -0.0600 79  ASN A CG  
677  O OD1 . ASN A 78  ? 0.5770 0.3811 0.2825 -0.1144 0.0620  -0.0541 79  ASN A OD1 
678  N ND2 . ASN A 78  ? 0.6333 0.4267 0.3111 -0.1254 0.0615  -0.0628 79  ASN A ND2 
679  N N   . PRO A 79  ? 0.4582 0.2996 0.1995 -0.0991 0.0333  -0.0559 80  PRO A N   
680  C CA  . PRO A 79  ? 0.4425 0.2922 0.1909 -0.0897 0.0195  -0.0503 80  PRO A CA  
681  C C   . PRO A 79  ? 0.4841 0.3242 0.2249 -0.0865 0.0191  -0.0433 80  PRO A C   
682  O O   . PRO A 79  ? 0.4684 0.3184 0.2265 -0.0789 0.0154  -0.0393 80  PRO A O   
683  C CB  . PRO A 79  ? 0.4942 0.3430 0.2251 -0.0895 0.0044  -0.0526 80  PRO A CB  
684  C CG  . PRO A 79  ? 0.5576 0.4060 0.2834 -0.0986 0.0107  -0.0607 80  PRO A CG  
685  C CD  . PRO A 79  ? 0.5069 0.3428 0.2279 -0.1056 0.0281  -0.0614 80  PRO A CD  
686  N N   . GLU A 80  ? 0.4675 0.2878 0.1819 -0.0934 0.0242  -0.0424 81  GLU A N   
687  C CA  . GLU A 80  ? 0.4689 0.2779 0.1745 -0.0926 0.0258  -0.0367 81  GLU A CA  
688  C C   . GLU A 80  ? 0.4757 0.2968 0.2085 -0.0912 0.0378  -0.0371 81  GLU A C   
689  O O   . GLU A 80  ? 0.4431 0.2683 0.1853 -0.0855 0.0343  -0.0327 81  GLU A O   
690  C CB  . GLU A 80  ? 0.5200 0.3029 0.1887 -0.1025 0.0306  -0.0363 81  GLU A CB  
691  C CG  . GLU A 80  ? 0.6033 0.3722 0.2608 -0.1025 0.0320  -0.0306 81  GLU A CG  
692  C CD  . GLU A 80  ? 0.8769 0.6175 0.4977 -0.1144 0.0406  -0.0302 81  GLU A CD  
693  O OE1 . GLU A 80  ? 0.8657 0.5867 0.4644 -0.1136 0.0352  -0.0240 81  GLU A OE1 
694  O OE2 . GLU A 80  ? 0.7761 0.5127 0.3893 -0.1250 0.0536  -0.0365 81  GLU A OE2 
695  N N   . GLY A 81  ? 0.4567 0.2838 0.2022 -0.0957 0.0509  -0.0429 82  GLY A N   
696  C CA  . GLY A 81  ? 0.4394 0.2794 0.2119 -0.0928 0.0607  -0.0443 82  GLY A CA  
697  C C   . GLY A 81  ? 0.4399 0.2967 0.2365 -0.0824 0.0526  -0.0404 82  GLY A C   
698  O O   . GLY A 81  ? 0.3938 0.2584 0.2046 -0.0779 0.0533  -0.0378 82  GLY A O   
699  N N   . PHE A 82  ? 0.3861 0.2485 0.1858 -0.0797 0.0449  -0.0408 83  PHE A N   
700  C CA  . PHE A 82  ? 0.3557 0.2330 0.1757 -0.0716 0.0381  -0.0380 83  PHE A CA  
701  C C   . PHE A 82  ? 0.3741 0.2519 0.1906 -0.0664 0.0278  -0.0329 83  PHE A C   
702  O O   . PHE A 82  ? 0.3649 0.2525 0.1975 -0.0610 0.0271  -0.0302 83  PHE A O   
703  C CB  . PHE A 82  ? 0.3704 0.2539 0.1940 -0.0719 0.0333  -0.0414 83  PHE A CB  
704  C CG  . PHE A 82  ? 0.3538 0.2516 0.1975 -0.0655 0.0292  -0.0395 83  PHE A CG  
705  C CD1 . PHE A 82  ? 0.3832 0.2857 0.2433 -0.0633 0.0371  -0.0388 83  PHE A CD1 
706  C CD2 . PHE A 82  ? 0.3641 0.2696 0.2093 -0.0612 0.0175  -0.0382 83  PHE A CD2 
707  C CE1 . PHE A 82  ? 0.3818 0.2948 0.2563 -0.0585 0.0341  -0.0365 83  PHE A CE1 
708  C CE2 . PHE A 82  ? 0.3730 0.2918 0.2361 -0.0565 0.0153  -0.0372 83  PHE A CE2 
709  C CZ  . PHE A 82  ? 0.3517 0.2733 0.2278 -0.0559 0.0240  -0.0360 83  PHE A CZ  
710  N N   . CYS A 83  ? 0.3854 0.2516 0.1798 -0.0677 0.0193  -0.0317 84  CYS A N   
711  C CA  . CYS A 83  ? 0.4119 0.2745 0.2003 -0.0619 0.0090  -0.0270 84  CYS A CA  
712  C C   . CYS A 83  ? 0.4278 0.2865 0.2191 -0.0624 0.0160  -0.0240 84  CYS A C   
713  O O   . CYS A 83  ? 0.3954 0.2617 0.1988 -0.0563 0.0117  -0.0214 84  CYS A O   
714  C CB  . CYS A 83  ? 0.4656 0.3106 0.2247 -0.0629 -0.0008 -0.0258 84  CYS A CB  
715  S SG  . CYS A 83  ? 0.5381 0.3755 0.2887 -0.0533 -0.0156 -0.0204 84  CYS A SG  
716  N N   . ILE A 84  ? 0.4034 0.2514 0.1843 -0.0705 0.0276  -0.0257 85  ILE A N   
717  C CA  . ILE A 84  ? 0.3830 0.2291 0.1674 -0.0733 0.0361  -0.0253 85  ILE A CA  
718  C C   . ILE A 84  ? 0.3819 0.2497 0.1974 -0.0675 0.0389  -0.0261 85  ILE A C   
719  O O   . ILE A 84  ? 0.3461 0.2183 0.1692 -0.0649 0.0378  -0.0242 85  ILE A O   
720  C CB  . ILE A 84  ? 0.4291 0.2636 0.1999 -0.0843 0.0497  -0.0298 85  ILE A CB  
721  C CG1 . ILE A 84  ? 0.4521 0.2593 0.1846 -0.0910 0.0467  -0.0274 85  ILE A CG1 
722  C CG2 . ILE A 84  ? 0.4226 0.2646 0.2080 -0.0876 0.0612  -0.0330 85  ILE A CG2 
723  C CD1 . ILE A 84  ? 0.5254 0.3200 0.2402 -0.1029 0.0592  -0.0326 85  ILE A CD1 
724  N N   . LEU A 85  ? 0.3368 0.2161 0.1677 -0.0656 0.0418  -0.0287 86  LEU A N   
725  C CA  . LEU A 85  ? 0.3161 0.2127 0.1727 -0.0595 0.0435  -0.0286 86  LEU A CA  
726  C C   . LEU A 85  ? 0.3381 0.2437 0.2033 -0.0525 0.0336  -0.0248 86  LEU A C   
727  O O   . LEU A 85  ? 0.3195 0.2351 0.1984 -0.0484 0.0333  -0.0234 86  LEU A O   
728  C CB  . LEU A 85  ? 0.3202 0.2213 0.1872 -0.0593 0.0501  -0.0321 86  LEU A CB  
729  C CG  . LEU A 85  ? 0.3812 0.2788 0.2481 -0.0647 0.0623  -0.0377 86  LEU A CG  
730  C CD1 . LEU A 85  ? 0.3857 0.2844 0.2608 -0.0637 0.0680  -0.0414 86  LEU A CD1 
731  C CD2 . LEU A 85  ? 0.3907 0.2991 0.2731 -0.0627 0.0668  -0.0394 86  LEU A CD2 
732  N N   . LEU A 86  ? 0.3177 0.2209 0.1754 -0.0513 0.0253  -0.0242 87  LEU A N   
733  C CA  . LEU A 86  ? 0.3050 0.2180 0.1717 -0.0453 0.0163  -0.0225 87  LEU A CA  
734  C C   . LEU A 86  ? 0.3483 0.2580 0.2114 -0.0427 0.0122  -0.0198 87  LEU A C   
735  O O   . LEU A 86  ? 0.3128 0.2328 0.1890 -0.0385 0.0105  -0.0187 87  LEU A O   
736  C CB  . LEU A 86  ? 0.3089 0.2218 0.1693 -0.0449 0.0081  -0.0247 87  LEU A CB  
737  C CG  . LEU A 86  ? 0.3417 0.2679 0.2146 -0.0392 -0.0001 -0.0255 87  LEU A CG  
738  C CD1 . LEU A 86  ? 0.3212 0.2600 0.2122 -0.0387 0.0056  -0.0259 87  LEU A CD1 
739  C CD2 . LEU A 86  ? 0.3785 0.3073 0.2466 -0.0387 -0.0093 -0.0298 87  LEU A CD2 
740  N N   . ASP A 87  ? 0.3208 0.2137 0.1640 -0.0461 0.0116  -0.0187 88  ASP A N   
741  C CA  . ASP A 87  ? 0.3228 0.2077 0.1593 -0.0451 0.0096  -0.0164 88  ASP A CA  
742  C C   . ASP A 87  ? 0.3412 0.2357 0.1925 -0.0468 0.0180  -0.0173 88  ASP A C   
743  O O   . ASP A 87  ? 0.3359 0.2355 0.1946 -0.0434 0.0152  -0.0164 88  ASP A O   
744  C CB  . ASP A 87  ? 0.3723 0.2329 0.1805 -0.0506 0.0102  -0.0150 88  ASP A CB  
745  C CG  . ASP A 87  ? 0.5248 0.3734 0.3149 -0.0465 -0.0021 -0.0132 88  ASP A CG  
746  O OD1 . ASP A 87  ? 0.5187 0.3799 0.3213 -0.0386 -0.0118 -0.0139 88  ASP A OD1 
747  O OD2 . ASP A 87  ? 0.5287 0.3555 0.2917 -0.0513 -0.0022 -0.0117 88  ASP A OD2 
748  N N   . PHE A 88  ? 0.3194 0.2171 0.1755 -0.0516 0.0279  -0.0200 89  PHE A N   
749  C CA  . PHE A 88  ? 0.2903 0.2010 0.1634 -0.0521 0.0349  -0.0224 89  PHE A CA  
750  C C   . PHE A 88  ? 0.3032 0.2313 0.1958 -0.0445 0.0301  -0.0210 89  PHE A C   
751  O O   . PHE A 88  ? 0.2731 0.2098 0.1749 -0.0430 0.0297  -0.0213 89  PHE A O   
752  C CB  . PHE A 88  ? 0.2945 0.2081 0.1727 -0.0564 0.0451  -0.0270 89  PHE A CB  
753  C CG  . PHE A 88  ? 0.2853 0.2169 0.1857 -0.0538 0.0495  -0.0302 89  PHE A CG  
754  C CD1 . PHE A 88  ? 0.3215 0.2570 0.2253 -0.0578 0.0535  -0.0336 89  PHE A CD1 
755  C CD2 . PHE A 88  ? 0.3045 0.2485 0.2214 -0.0468 0.0483  -0.0299 89  PHE A CD2 
756  C CE1 . PHE A 88  ? 0.2973 0.2523 0.2227 -0.0545 0.0556  -0.0375 89  PHE A CE1 
757  C CE2 . PHE A 88  ? 0.3246 0.2848 0.2604 -0.0423 0.0497  -0.0324 89  PHE A CE2 
758  C CZ  . PHE A 88  ? 0.2976 0.2650 0.2387 -0.0459 0.0526  -0.0365 89  PHE A CZ  
759  N N   . MET A 89  ? 0.2566 0.1891 0.1539 -0.0410 0.0271  -0.0199 90  MET A N   
760  C CA  . MET A 89  ? 0.2387 0.1844 0.1503 -0.0353 0.0238  -0.0184 90  MET A CA  
761  C C   . MET A 89  ? 0.2931 0.2424 0.2060 -0.0327 0.0176  -0.0172 90  MET A C   
762  O O   . MET A 89  ? 0.2753 0.2350 0.1984 -0.0302 0.0174  -0.0168 90  MET A O   
763  C CB  . MET A 89  ? 0.2491 0.1951 0.1611 -0.0342 0.0219  -0.0181 90  MET A CB  
764  C CG  . MET A 89  ? 0.2641 0.2064 0.1765 -0.0361 0.0286  -0.0196 90  MET A CG  
765  S SD  . MET A 89  ? 0.2992 0.2414 0.2121 -0.0363 0.0272  -0.0201 90  MET A SD  
766  C CE  . MET A 89  ? 0.3072 0.2394 0.2155 -0.0401 0.0358  -0.0231 90  MET A CE  
767  N N   . TYR A 90  ? 0.2596 0.1997 0.1613 -0.0328 0.0121  -0.0169 91  TYR A N   
768  C CA  . TYR A 90  ? 0.2547 0.1966 0.1577 -0.0293 0.0058  -0.0167 91  TYR A CA  
769  C C   . TYR A 90  ? 0.3060 0.2395 0.2023 -0.0312 0.0071  -0.0167 91  TYR A C   
770  O O   . TYR A 90  ? 0.2983 0.2320 0.1959 -0.0281 0.0026  -0.0170 91  TYR A O   
771  C CB  . TYR A 90  ? 0.2628 0.1998 0.1590 -0.0262 -0.0023 -0.0174 91  TYR A CB  
772  C CG  . TYR A 90  ? 0.2670 0.2173 0.1747 -0.0244 -0.0043 -0.0196 91  TYR A CG  
773  C CD1 . TYR A 90  ? 0.2905 0.2410 0.1972 -0.0274 -0.0014 -0.0204 91  TYR A CD1 
774  C CD2 . TYR A 90  ? 0.2757 0.2376 0.1945 -0.0207 -0.0081 -0.0220 91  TYR A CD2 
775  C CE1 . TYR A 90  ? 0.2722 0.2333 0.1882 -0.0276 -0.0017 -0.0233 91  TYR A CE1 
776  C CE2 . TYR A 90  ? 0.2750 0.2486 0.2033 -0.0210 -0.0083 -0.0254 91  TYR A CE2 
777  C CZ  . TYR A 90  ? 0.2920 0.2647 0.2185 -0.0249 -0.0049 -0.0259 91  TYR A CZ  
778  O OH  . TYR A 90  ? 0.2606 0.2436 0.1955 -0.0269 -0.0040 -0.0302 91  TYR A OH  
779  N N   . THR A 91  ? 0.2743 0.2001 0.1636 -0.0372 0.0141  -0.0173 92  THR A N   
780  C CA  . THR A 91  ? 0.2859 0.2013 0.1666 -0.0414 0.0170  -0.0182 92  THR A CA  
781  C C   . THR A 91  ? 0.3175 0.2406 0.2061 -0.0475 0.0263  -0.0219 92  THR A C   
782  O O   . THR A 91  ? 0.3085 0.2262 0.1930 -0.0519 0.0293  -0.0240 92  THR A O   
783  C CB  . THR A 91  ? 0.3377 0.2275 0.1929 -0.0453 0.0165  -0.0165 92  THR A CB  
784  O OG1 . THR A 91  ? 0.3499 0.2357 0.1989 -0.0514 0.0237  -0.0177 92  THR A OG1 
785  C CG2 . THR A 91  ? 0.3583 0.2391 0.2039 -0.0383 0.0053  -0.0137 92  THR A CG2 
786  N N   A SER A 92  ? 0.2664 0.2011 0.1659 -0.0479 0.0310  -0.0238 93  SER A N   
787  N N   B SER A 92  ? 0.2734 0.2076 0.1724 -0.0480 0.0311  -0.0238 93  SER A N   
788  C CA  A SER A 92  ? 0.2608 0.2059 0.1710 -0.0526 0.0397  -0.0292 93  SER A CA  
789  C CA  B SER A 92  ? 0.2713 0.2159 0.1810 -0.0527 0.0397  -0.0292 93  SER A CA  
790  C C   A SER A 92  ? 0.2992 0.2284 0.1938 -0.0626 0.0485  -0.0324 93  SER A C   
791  C C   B SER A 92  ? 0.3280 0.2563 0.2217 -0.0629 0.0485  -0.0324 93  SER A C   
792  O O   A SER A 92  ? 0.2880 0.2260 0.1917 -0.0677 0.0571  -0.0388 93  SER A O   
793  O O   B SER A 92  ? 0.3230 0.2594 0.2249 -0.0690 0.0571  -0.0390 93  SER A O   
794  C CB  A SER A 92  ? 0.2599 0.2177 0.1816 -0.0532 0.0398  -0.0325 93  SER A CB  
795  C CB  B SER A 92  ? 0.2942 0.2542 0.2180 -0.0520 0.0392  -0.0322 93  SER A CB  
796  O OG  A SER A 92  ? 0.2341 0.2039 0.1659 -0.0454 0.0321  -0.0297 93  SER A OG  
797  O OG  B SER A 92  ? 0.3666 0.3160 0.2803 -0.0590 0.0424  -0.0346 93  SER A OG  
798  N N   A ARG A 93  ? 0.2944 0.2001 0.1650 -0.0652 0.0462  -0.0286 94  ARG A N   
799  N N   B ARG A 93  ? 0.3103 0.2160 0.1807 -0.0650 0.0462  -0.0285 94  ARG A N   
800  C CA  A ARG A 93  ? 0.3113 0.1967 0.1604 -0.0756 0.0546  -0.0306 94  ARG A CA  
801  C CA  B ARG A 93  ? 0.3310 0.2151 0.1787 -0.0754 0.0539  -0.0301 94  ARG A CA  
802  C C   A ARG A 93  ? 0.3659 0.2458 0.2072 -0.0766 0.0563  -0.0303 94  ARG A C   
803  C C   B ARG A 93  ? 0.3805 0.2589 0.2201 -0.0769 0.0562  -0.0301 94  ARG A C   
804  O O   A ARG A 93  ? 0.3496 0.2260 0.1858 -0.0703 0.0476  -0.0257 94  ARG A O   
805  O O   B ARG A 93  ? 0.3692 0.2433 0.2028 -0.0709 0.0477  -0.0255 94  ARG A O   
806  C CB  A ARG A 93  ? 0.3761 0.2343 0.1983 -0.0781 0.0506  -0.0263 94  ARG A CB  
807  C CB  B ARG A 93  ? 0.3752 0.2331 0.1971 -0.0763 0.0485  -0.0252 94  ARG A CB  
808  C CG  A ARG A 93  ? 0.4186 0.2784 0.2458 -0.0787 0.0505  -0.0275 94  ARG A CG  
809  C CG  B ARG A 93  ? 0.4805 0.3409 0.3085 -0.0751 0.0465  -0.0258 94  ARG A CG  
810  C CD  A ARG A 93  ? 0.4930 0.3266 0.2968 -0.0756 0.0425  -0.0218 94  ARG A CD  
811  C CD  B ARG A 93  ? 0.5555 0.4075 0.3763 -0.0876 0.0585  -0.0313 94  ARG A CD  
812  N NE  A ARG A 93  ? 0.6172 0.4185 0.3875 -0.0836 0.0465  -0.0196 94  ARG A NE  
813  N NE  B ARG A 93  ? 0.5917 0.4471 0.4193 -0.0874 0.0574  -0.0330 94  ARG A NE  
814  C CZ  A ARG A 93  ? 0.8005 0.5815 0.5527 -0.0951 0.0564  -0.0219 94  ARG A CZ  
815  C CZ  B ARG A 93  ? 0.7656 0.5948 0.5714 -0.0906 0.0570  -0.0308 94  ARG A CZ  
816  N NH1 A ARG A 93  ? 0.6673 0.4592 0.4339 -0.0999 0.0628  -0.0274 94  ARG A NH1 
817  N NH1 B ARG A 93  ? 0.6434 0.4771 0.4573 -0.0909 0.0569  -0.0335 94  ARG A NH1 
818  N NH2 A ARG A 93  ? 0.6681 0.4167 0.3858 -0.1028 0.0601  -0.0192 94  ARG A NH2 
819  N NH2 B ARG A 93  ? 0.5601 0.3564 0.3340 -0.0934 0.0565  -0.0259 94  ARG A NH2 
820  N N   . LEU A 94  ? 0.3461 0.2253 0.1860 -0.0856 0.0683  -0.0364 95  LEU A N   
821  C CA  . LEU A 94  ? 0.3429 0.2168 0.1755 -0.0883 0.0725  -0.0380 95  LEU A CA  
822  C C   . LEU A 94  ? 0.4275 0.2747 0.2284 -0.1005 0.0799  -0.0390 95  LEU A C   
823  O O   . LEU A 94  ? 0.4207 0.2643 0.2181 -0.1110 0.0915  -0.0448 95  LEU A O   
824  C CB  . LEU A 94  ? 0.3318 0.2282 0.1910 -0.0876 0.0810  -0.0457 95  LEU A CB  
825  C CG  . LEU A 94  ? 0.3722 0.2655 0.2283 -0.0890 0.0856  -0.0483 95  LEU A CG  
826  C CD1 . LEU A 94  ? 0.3643 0.2584 0.2218 -0.0793 0.0745  -0.0419 95  LEU A CD1 
827  C CD2 . LEU A 94  ? 0.3938 0.3063 0.2748 -0.0892 0.0960  -0.0579 95  LEU A CD2 
828  N N   . ASN A 95  ? 0.4254 0.2535 0.2019 -0.0998 0.0733  -0.0338 96  ASN A N   
829  C CA  . ASN A 95  ? 0.4633 0.2615 0.2031 -0.1110 0.0787  -0.0333 96  ASN A CA  
830  C C   . ASN A 95  ? 0.5230 0.3235 0.2623 -0.1197 0.0915  -0.0408 96  ASN A C   
831  O O   . ASN A 95  ? 0.5264 0.3192 0.2526 -0.1194 0.0882  -0.0395 96  ASN A O   
832  C CB  . ASN A 95  ? 0.5342 0.3110 0.2469 -0.1052 0.0639  -0.0247 96  ASN A CB  
833  C CG  . ASN A 95  ? 0.7750 0.5167 0.4442 -0.1156 0.0672  -0.0226 96  ASN A CG  
834  O OD1 . ASN A 95  ? 0.6684 0.3961 0.3231 -0.1284 0.0806  -0.0262 96  ASN A OD1 
835  N ND2 . ASN A 95  ? 0.7016 0.4283 0.3480 -0.1112 0.0551  -0.0175 96  ASN A ND2 
836  N N   . LEU A 96  ? 0.4837 0.2973 0.2399 -0.1271 0.1059  -0.0498 97  LEU A N   
837  C CA  . LEU A 96  ? 0.4947 0.3145 0.2565 -0.1348 0.1196  -0.0593 97  LEU A CA  
838  C C   . LEU A 96  ? 0.5635 0.3561 0.2903 -0.1521 0.1323  -0.0628 97  LEU A C   
839  O O   . LEU A 96  ? 0.5625 0.3462 0.2803 -0.1613 0.1399  -0.0651 97  LEU A O   
840  C CB  . LEU A 96  ? 0.4823 0.3340 0.2847 -0.1316 0.1269  -0.0685 97  LEU A CB  
841  C CG  . LEU A 96  ? 0.5537 0.4213 0.3760 -0.1324 0.1374  -0.0787 97  LEU A CG  
842  C CD1 . LEU A 96  ? 0.5584 0.4263 0.3827 -0.1225 0.1287  -0.0739 97  LEU A CD1 
843  C CD2 . LEU A 96  ? 0.5308 0.4299 0.3930 -0.1270 0.1415  -0.0873 97  LEU A CD2 
844  N N   . ARG A 97  ? 0.5509 0.3275 0.2541 -0.1572 0.1344  -0.0629 98  ARG A N   
845  C CA  . ARG A 97  ? 0.5951 0.3414 0.2580 -0.1743 0.1460  -0.0654 98  ARG A CA  
846  C C   . ARG A 97  ? 0.6083 0.3599 0.2737 -0.1822 0.1594  -0.0757 98  ARG A C   
847  O O   . ARG A 97  ? 0.5684 0.3394 0.2580 -0.1726 0.1552  -0.0776 98  ARG A O   
848  C CB  . ARG A 97  ? 0.6374 0.3502 0.2566 -0.1726 0.1317  -0.0531 98  ARG A CB  
849  C CG  . ARG A 97  ? 0.7138 0.4178 0.3280 -0.1638 0.1179  -0.0432 98  ARG A CG  
850  C CD  . ARG A 97  ? 0.9714 0.6433 0.5446 -0.1595 0.1021  -0.0319 98  ARG A CD  
851  N NE  . ARG A 97  ? 1.2202 0.8535 0.7439 -0.1751 0.1107  -0.0312 98  ARG A NE  
852  C CZ  . ARG A 97  ? 1.5016 1.1060 0.9968 -0.1846 0.1171  -0.0286 98  ARG A CZ  
853  N NH1 . ARG A 97  ? 1.3737 0.9403 0.8202 -0.1997 0.1256  -0.0277 98  ARG A NH1 
854  N NH2 . ARG A 97  ? 1.3721 0.9836 0.8853 -0.1803 0.1158  -0.0273 98  ARG A NH2 
855  N N   . GLU A 98  ? 0.5994 0.3326 0.2392 -0.2005 0.1766  -0.0831 99  GLU A N   
856  C CA  . GLU A 98  ? 0.5997 0.3362 0.2395 -0.2097 0.1911  -0.0943 99  GLU A CA  
857  C C   . GLU A 98  ? 0.6642 0.3932 0.2903 -0.2028 0.1796  -0.0888 99  GLU A C   
858  O O   . GLU A 98  ? 0.6438 0.3910 0.2932 -0.1995 0.1843  -0.0965 99  GLU A O   
859  C CB  . GLU A 98  ? 0.6567 0.3661 0.2588 -0.2325 0.2102  -0.1011 99  GLU A CB  
860  C CG  . GLU A 98  ? 0.7661 0.4817 0.3718 -0.2439 0.2288  -0.1158 99  GLU A CG  
861  C CD  . GLU A 98  ? 1.1268 0.8145 0.6926 -0.2684 0.2494  -0.1234 99  GLU A CD  
862  O OE1 . GLU A 98  ? 1.0370 0.6856 0.5511 -0.2763 0.2446  -0.1129 99  GLU A OE1 
863  O OE2 . GLU A 98  ? 1.0960 0.8004 0.6817 -0.2796 0.2705  -0.1405 99  GLU A OE2 
864  N N   . GLY A 99  ? 0.6640 0.3674 0.2543 -0.2001 0.1641  -0.0763 100 GLY A N   
865  C CA  . GLY A 99  ? 0.6742 0.3700 0.2483 -0.1947 0.1516  -0.0716 100 GLY A CA  
866  C C   . GLY A 99  ? 0.6619 0.3847 0.2726 -0.1771 0.1379  -0.0689 100 GLY A C   
867  O O   . GLY A 99  ? 0.6663 0.3899 0.2729 -0.1746 0.1324  -0.0695 100 GLY A O   
868  N N   . ASN A 100 ? 0.5890 0.3337 0.2344 -0.1659 0.1331  -0.0666 101 ASN A N   
869  C CA  . ASN A 100 ? 0.5362 0.3037 0.2130 -0.1503 0.1207  -0.0635 101 ASN A CA  
870  C C   . ASN A 100 ? 0.5615 0.3581 0.2831 -0.1441 0.1289  -0.0708 101 ASN A C   
871  O O   . ASN A 100 ? 0.5374 0.3497 0.2821 -0.1325 0.1206  -0.0686 101 ASN A O   
872  C CB  . ASN A 100 ? 0.5258 0.2913 0.2004 -0.1394 0.1025  -0.0522 101 ASN A CB  
873  C CG  . ASN A 100 ? 0.6347 0.4079 0.3252 -0.1371 0.1044  -0.0507 101 ASN A CG  
874  O OD1 . ASN A 100 ? 0.5036 0.2953 0.2215 -0.1382 0.1155  -0.0578 101 ASN A OD1 
875  N ND2 . ASN A 100 ? 0.5479 0.3081 0.2229 -0.1329 0.0927  -0.0421 101 ASN A ND2 
876  N N   . ILE A 101 ? 0.5256 0.3296 0.2594 -0.1515 0.1445  -0.0796 102 ILE A N   
877  C CA  . ILE A 101 ? 0.4962 0.3291 0.2734 -0.1435 0.1498  -0.0866 102 ILE A CA  
878  C C   . ILE A 101 ? 0.4869 0.3311 0.2839 -0.1362 0.1510  -0.0912 102 ILE A C   
879  O O   . ILE A 101 ? 0.4477 0.3104 0.2746 -0.1230 0.1449  -0.0896 102 ILE A O   
880  C CB  . ILE A 101 ? 0.5436 0.3856 0.3327 -0.1531 0.1666  -0.0981 102 ILE A CB  
881  C CG1 . ILE A 101 ? 0.5179 0.3924 0.3538 -0.1411 0.1673  -0.1042 102 ILE A CG1 
882  C CG2 . ILE A 101 ? 0.5582 0.3880 0.3292 -0.1690 0.1844  -0.1092 102 ILE A CG2 
883  C CD1 . ILE A 101 ? 0.5376 0.4265 0.3896 -0.1461 0.1752  -0.1116 102 ILE A CD1 
884  N N   . MET A 102 ? 0.4844 0.3155 0.2629 -0.1449 0.1588  -0.0966 103 MET A N   
885  C CA  . MET A 102 ? 0.4727 0.3112 0.2678 -0.1390 0.1610  -0.1015 103 MET A CA  
886  C C   . MET A 102 ? 0.5025 0.3420 0.3004 -0.1277 0.1446  -0.0916 103 MET A C   
887  O O   . MET A 102 ? 0.4558 0.3084 0.2804 -0.1168 0.1428  -0.0923 103 MET A O   
888  C CB  . MET A 102 ? 0.5348 0.3588 0.3086 -0.1521 0.1740  -0.1108 103 MET A CB  
889  C CG  . MET A 102 ? 0.6172 0.4431 0.3925 -0.1643 0.1933  -0.1235 103 MET A CG  
890  S SD  . MET A 102 ? 0.6597 0.5178 0.4873 -0.1544 0.2023  -0.1346 103 MET A SD  
891  C CE  . MET A 102 ? 0.6311 0.4946 0.4789 -0.1460 0.2067  -0.1424 103 MET A CE  
892  N N   . ALA A 103 ? 0.4910 0.3164 0.2616 -0.1298 0.1324  -0.0827 104 ALA A N   
893  C CA  . ALA A 103 ? 0.4849 0.3136 0.2589 -0.1205 0.1172  -0.0751 104 ALA A CA  
894  C C   . ALA A 103 ? 0.4839 0.3289 0.2839 -0.1082 0.1092  -0.0689 104 ALA A C   
895  O O   . ALA A 103 ? 0.4531 0.3072 0.2702 -0.0995 0.1037  -0.0667 104 ALA A O   
896  C CB  . ALA A 103 ? 0.5235 0.3361 0.2646 -0.1246 0.1055  -0.0687 104 ALA A CB  
897  N N   . VAL A 104 ? 0.4289 0.2763 0.2302 -0.1086 0.1093  -0.0666 105 VAL A N   
898  C CA  . VAL A 104 ? 0.3768 0.2400 0.2014 -0.0979 0.1020  -0.0616 105 VAL A CA  
899  C C   . VAL A 104 ? 0.4001 0.2805 0.2564 -0.0901 0.1078  -0.0665 105 VAL A C   
900  O O   . VAL A 104 ? 0.3801 0.2692 0.2515 -0.0799 0.0998  -0.0617 105 VAL A O   
901  C CB  . VAL A 104 ? 0.4171 0.2780 0.2350 -0.1014 0.1017  -0.0592 105 VAL A CB  
902  C CG1 . VAL A 104 ? 0.3811 0.2606 0.2253 -0.0914 0.0964  -0.0563 105 VAL A CG1 
903  C CG2 . VAL A 104 ? 0.4346 0.2765 0.2217 -0.1046 0.0918  -0.0519 105 VAL A CG2 
904  N N   A MET A 105 ? 0.3775 0.2618 0.2428 -0.0945 0.1214  -0.0764 106 MET A N   
905  N N   B MET A 105 ? 0.3817 0.2661 0.2472 -0.0944 0.1214  -0.0764 106 MET A N   
906  C CA  A MET A 105 ? 0.3708 0.2707 0.2663 -0.0854 0.1263  -0.0822 106 MET A CA  
907  C CA  B MET A 105 ? 0.3797 0.2799 0.2758 -0.0849 0.1258  -0.0819 106 MET A CA  
908  C C   A MET A 105 ? 0.4240 0.3195 0.3238 -0.0785 0.1235  -0.0806 106 MET A C   
909  C C   B MET A 105 ? 0.4198 0.3153 0.3195 -0.0783 0.1231  -0.0803 106 MET A C   
910  O O   A MET A 105 ? 0.4029 0.3070 0.3217 -0.0668 0.1183  -0.0775 106 MET A O   
911  O O   B MET A 105 ? 0.3889 0.2926 0.3073 -0.0666 0.1179  -0.0772 106 MET A O   
912  C CB  A MET A 105 ? 0.4103 0.3152 0.3142 -0.0922 0.1421  -0.0954 106 MET A CB  
913  C CB  B MET A 105 ? 0.4125 0.3190 0.3189 -0.0909 0.1413  -0.0950 106 MET A CB  
914  C CG  A MET A 105 ? 0.4424 0.3658 0.3803 -0.0806 0.1453  -0.1023 106 MET A CG  
915  C CG  B MET A 105 ? 0.4340 0.3588 0.3747 -0.0784 0.1437  -0.1013 106 MET A CG  
916  S SD  A MET A 105 ? 0.5031 0.4350 0.4545 -0.0883 0.1648  -0.1207 106 MET A SD  
917  S SD  B MET A 105 ? 0.4733 0.4128 0.4333 -0.0844 0.1613  -0.1193 106 MET A SD  
918  C CE  A MET A 105 ? 0.4518 0.3995 0.4398 -0.0692 0.1629  -0.1255 106 MET A CE  
919  C CE  B MET A 105 ? 0.4618 0.3824 0.4035 -0.0948 0.1748  -0.1275 106 MET A CE  
920  N N   . ALA A 106 ? 0.4054 0.2860 0.2854 -0.0866 0.1270  -0.0828 107 ALA A N   
921  C CA  . ALA A 106 ? 0.4078 0.2819 0.2888 -0.0830 0.1260  -0.0826 107 ALA A CA  
922  C C   . ALA A 106 ? 0.4176 0.2932 0.2992 -0.0761 0.1124  -0.0724 107 ALA A C   
923  O O   . ALA A 106 ? 0.3926 0.2693 0.2872 -0.0679 0.1110  -0.0707 107 ALA A O   
924  C CB  . ALA A 106 ? 0.4369 0.2960 0.2938 -0.0950 0.1314  -0.0876 107 ALA A CB  
925  N N   . THR A 107 ? 0.3677 0.2428 0.2355 -0.0790 0.1029  -0.0659 108 THR A N   
926  C CA  . THR A 107 ? 0.3562 0.2352 0.2260 -0.0732 0.0909  -0.0579 108 THR A CA  
927  C C   . THR A 107 ? 0.3817 0.2730 0.2732 -0.0624 0.0878  -0.0538 108 THR A C   
928  O O   . THR A 107 ? 0.3486 0.2411 0.2473 -0.0565 0.0836  -0.0500 108 THR A O   
929  C CB  . THR A 107 ? 0.4111 0.2864 0.2617 -0.0776 0.0811  -0.0534 108 THR A CB  
930  O OG1 . THR A 107 ? 0.4169 0.2797 0.2449 -0.0873 0.0836  -0.0575 108 THR A OG1 
931  C CG2 . THR A 107 ? 0.4092 0.2897 0.2629 -0.0728 0.0698  -0.0480 108 THR A CG2 
932  N N   . ALA A 108 ? 0.3427 0.2426 0.2433 -0.0608 0.0903  -0.0552 109 ALA A N   
933  C CA  . ALA A 108 ? 0.3175 0.2307 0.2381 -0.0508 0.0866  -0.0523 109 ALA A CA  
934  C C   . ALA A 108 ? 0.3443 0.2586 0.2808 -0.0420 0.0903  -0.0547 109 ALA A C   
935  O O   . ALA A 108 ? 0.3288 0.2465 0.2738 -0.0330 0.0841  -0.0493 109 ALA A O   
936  C CB  . ALA A 108 ? 0.3197 0.2429 0.2467 -0.0527 0.0894  -0.0557 109 ALA A CB  
937  N N   . MET A 109 ? 0.3271 0.2357 0.2651 -0.0446 0.1005  -0.0627 110 MET A N   
938  C CA  . MET A 109 ? 0.3201 0.2255 0.2713 -0.0352 0.1039  -0.0652 110 MET A CA  
939  C C   . MET A 109 ? 0.3676 0.2594 0.3094 -0.0335 0.0996  -0.0587 110 MET A C   
940  O O   . MET A 109 ? 0.3658 0.2552 0.3150 -0.0235 0.0958  -0.0541 110 MET A O   
941  C CB  . MET A 109 ? 0.3586 0.2598 0.3123 -0.0395 0.1166  -0.0764 110 MET A CB  
942  C CG  . MET A 109 ? 0.4021 0.3190 0.3713 -0.0395 0.1227  -0.0849 110 MET A CG  
943  S SD  . MET A 109 ? 0.4928 0.4041 0.4607 -0.0488 0.1397  -0.0997 110 MET A SD  
944  C CE  . MET A 109 ? 0.4664 0.3709 0.4513 -0.0341 0.1418  -0.1026 110 MET A CE  
945  N N   . TYR A 110 ? 0.3416 0.2244 0.2659 -0.0438 0.0999  -0.0586 111 TYR A N   
946  C CA  . TYR A 110 ? 0.3414 0.2137 0.2568 -0.0454 0.0971  -0.0548 111 TYR A CA  
947  C C   . TYR A 110 ? 0.3710 0.2496 0.2889 -0.0402 0.0872  -0.0460 111 TYR A C   
948  O O   . TYR A 110 ? 0.3406 0.2116 0.2593 -0.0357 0.0863  -0.0422 111 TYR A O   
949  C CB  . TYR A 110 ? 0.3498 0.2173 0.2475 -0.0577 0.0972  -0.0579 111 TYR A CB  
950  C CG  . TYR A 110 ? 0.3503 0.2124 0.2402 -0.0616 0.0934  -0.0558 111 TYR A CG  
951  C CD1 . TYR A 110 ? 0.3973 0.2463 0.2855 -0.0634 0.1002  -0.0592 111 TYR A CD1 
952  C CD2 . TYR A 110 ? 0.3442 0.2145 0.2284 -0.0645 0.0838  -0.0521 111 TYR A CD2 
953  C CE1 . TYR A 110 ? 0.3698 0.2148 0.2512 -0.0692 0.0981  -0.0591 111 TYR A CE1 
954  C CE2 . TYR A 110 ? 0.3440 0.2129 0.2236 -0.0693 0.0809  -0.0527 111 TYR A CE2 
955  C CZ  . TYR A 110 ? 0.3951 0.2519 0.2733 -0.0725 0.0886  -0.0565 111 TYR A CZ  
956  O OH  . TYR A 110 ? 0.3760 0.2332 0.2502 -0.0792 0.0869  -0.0588 111 TYR A OH  
957  N N   . LEU A 111 ? 0.3380 0.2285 0.2556 -0.0412 0.0806  -0.0431 112 LEU A N   
958  C CA  . LEU A 111 ? 0.3107 0.2085 0.2306 -0.0372 0.0718  -0.0360 112 LEU A CA  
959  C C   . LEU A 111 ? 0.3432 0.2469 0.2763 -0.0263 0.0696  -0.0325 112 LEU A C   
960  O O   . LEU A 111 ? 0.3272 0.2346 0.2609 -0.0228 0.0633  -0.0267 112 LEU A O   
961  C CB  . LEU A 111 ? 0.2957 0.2021 0.2099 -0.0417 0.0655  -0.0347 112 LEU A CB  
962  C CG  . LEU A 111 ? 0.3290 0.2308 0.2286 -0.0503 0.0632  -0.0368 112 LEU A CG  
963  C CD1 . LEU A 111 ? 0.3263 0.2340 0.2200 -0.0516 0.0555  -0.0344 112 LEU A CD1 
964  C CD2 . LEU A 111 ? 0.3417 0.2410 0.2391 -0.0522 0.0610  -0.0363 112 LEU A CD2 
965  N N   . GLN A 112 ? 0.3078 0.2132 0.2516 -0.0209 0.0746  -0.0368 113 GLN A N   
966  C CA  . GLN A 112 ? 0.2980 0.2113 0.2559 -0.0091 0.0710  -0.0348 113 GLN A CA  
967  C C   . GLN A 112 ? 0.3260 0.2560 0.2889 -0.0086 0.0641  -0.0324 113 GLN A C   
968  O O   . GLN A 112 ? 0.3125 0.2459 0.2758 -0.0035 0.0570  -0.0264 113 GLN A O   
969  C CB  . GLN A 112 ? 0.3137 0.2140 0.2681 -0.0013 0.0683  -0.0287 113 GLN A CB  
970  C CG  . GLN A 112 ? 0.3621 0.2429 0.3111 -0.0019 0.0763  -0.0317 113 GLN A CG  
971  C CD  . GLN A 112 ? 0.4939 0.3567 0.4323 0.0014  0.0748  -0.0249 113 GLN A CD  
972  O OE1 . GLN A 112 ? 0.4202 0.2836 0.3581 0.0088  0.0680  -0.0182 113 GLN A OE1 
973  N NE2 . GLN A 112 ? 0.4854 0.3304 0.4129 -0.0054 0.0817  -0.0268 113 GLN A NE2 
974  N N   . MET A 113 ? 0.2862 0.2242 0.2504 -0.0153 0.0673  -0.0377 114 MET A N   
975  C CA  . MET A 113 ? 0.2733 0.2251 0.2413 -0.0170 0.0631  -0.0373 114 MET A CA  
976  C C   . MET A 113 ? 0.3453 0.3100 0.3295 -0.0151 0.0684  -0.0458 114 MET A C   
977  O O   . MET A 113 ? 0.3284 0.2934 0.3102 -0.0237 0.0760  -0.0523 114 MET A O   
978  C CB  . MET A 113 ? 0.2876 0.2334 0.2395 -0.0277 0.0630  -0.0364 114 MET A CB  
979  C CG  . MET A 113 ? 0.3055 0.2437 0.2462 -0.0287 0.0571  -0.0302 114 MET A CG  
980  S SD  . MET A 113 ? 0.3514 0.2826 0.2741 -0.0385 0.0548  -0.0301 114 MET A SD  
981  C CE  . MET A 113 ? 0.3133 0.2544 0.2390 -0.0377 0.0494  -0.0280 114 MET A CE  
982  N N   . GLU A 114 ? 0.3265 0.3013 0.3270 -0.0035 0.0646  -0.0463 115 GLU A N   
983  C CA  . GLU A 114 ? 0.3350 0.3256 0.3566 0.0016  0.0685  -0.0560 115 GLU A CA  
984  C C   . GLU A 114 ? 0.3360 0.3422 0.3643 -0.0071 0.0727  -0.0636 115 GLU A C   
985  O O   . GLU A 114 ? 0.3282 0.3410 0.3664 -0.0111 0.0822  -0.0742 115 GLU A O   
986  C CB  . GLU A 114 ? 0.3630 0.3627 0.3992 0.0174  0.0597  -0.0540 115 GLU A CB  
987  C CG  . GLU A 114 ? 0.5251 0.5054 0.5536 0.0261  0.0576  -0.0477 115 GLU A CG  
988  N N   . HIS A 115 ? 0.3032 0.3144 0.3260 -0.0108 0.0669  -0.0592 116 HIS A N   
989  C CA  . HIS A 115 ? 0.3147 0.3378 0.3421 -0.0203 0.0719  -0.0666 116 HIS A CA  
990  C C   . HIS A 115 ? 0.3425 0.3512 0.3528 -0.0346 0.0824  -0.0698 116 HIS A C   
991  O O   . HIS A 115 ? 0.3396 0.3556 0.3558 -0.0429 0.0921  -0.0800 116 HIS A O   
992  C CB  . HIS A 115 ? 0.3377 0.3673 0.3623 -0.0208 0.0637  -0.0616 116 HIS A CB  
993  C CG  . HIS A 115 ? 0.3902 0.4357 0.4305 -0.0081 0.0539  -0.0601 116 HIS A CG  
994  N ND1 . HIS A 115 ? 0.4239 0.4912 0.4881 -0.0019 0.0541  -0.0699 116 HIS A ND1 
995  C CD2 . HIS A 115 ? 0.4159 0.4583 0.4498 -0.0012 0.0437  -0.0508 116 HIS A CD2 
996  C CE1 . HIS A 115 ? 0.4148 0.4904 0.4848 0.0097  0.0426  -0.0651 116 HIS A CE1 
997  N NE2 . HIS A 115 ? 0.4158 0.4758 0.4668 0.0097  0.0367  -0.0534 116 HIS A NE2 
998  N N   . VAL A 116 ? 0.2848 0.2731 0.2732 -0.0380 0.0807  -0.0620 117 VAL A N   
999  C CA  . VAL A 116 ? 0.2951 0.2668 0.2630 -0.0505 0.0885  -0.0638 117 VAL A CA  
1000 C C   . VAL A 116 ? 0.3686 0.3406 0.3434 -0.0528 0.0999  -0.0735 117 VAL A C   
1001 O O   . VAL A 116 ? 0.3614 0.3310 0.3303 -0.0640 0.1105  -0.0812 117 VAL A O   
1002 C CB  . VAL A 116 ? 0.3493 0.3025 0.2946 -0.0521 0.0821  -0.0545 117 VAL A CB  
1003 C CG1 . VAL A 116 ? 0.3650 0.3007 0.2876 -0.0638 0.0891  -0.0569 117 VAL A CG1 
1004 C CG2 . VAL A 116 ? 0.3413 0.2950 0.2808 -0.0507 0.0724  -0.0472 117 VAL A CG2 
1005 N N   . VAL A 117 ? 0.3135 0.2870 0.2999 -0.0426 0.0985  -0.0735 118 VAL A N   
1006 C CA  . VAL A 117 ? 0.3204 0.2944 0.3162 -0.0429 0.1093  -0.0836 118 VAL A CA  
1007 C C   . VAL A 117 ? 0.3729 0.3675 0.3901 -0.0451 0.1175  -0.0966 118 VAL A C   
1008 O O   . VAL A 117 ? 0.3587 0.3514 0.3728 -0.0558 0.1304  -0.1065 118 VAL A O   
1009 C CB  . VAL A 117 ? 0.3521 0.3226 0.3576 -0.0297 0.1057  -0.0813 118 VAL A CB  
1010 C CG1 . VAL A 117 ? 0.3557 0.3267 0.3726 -0.0294 0.1175  -0.0932 118 VAL A CG1 
1011 C CG2 . VAL A 117 ? 0.3512 0.3021 0.3356 -0.0310 0.1003  -0.0710 118 VAL A CG2 
1012 N N   A ASP A 118 ? 0.3349 0.3495 0.3720 -0.0366 0.1103  -0.0971 119 ASP A N   
1013 N N   B ASP A 118 ? 0.3319 0.3469 0.3704 -0.0357 0.1103  -0.0974 119 ASP A N   
1014 C CA  A ASP A 118 ? 0.3337 0.3728 0.3948 -0.0381 0.1163  -0.1104 119 ASP A CA  
1015 C CA  B ASP A 118 ? 0.3304 0.3704 0.3940 -0.0364 0.1161  -0.1109 119 ASP A CA  
1016 C C   A ASP A 118 ? 0.3729 0.4091 0.4210 -0.0570 0.1277  -0.1168 119 ASP A C   
1017 C C   B ASP A 118 ? 0.3824 0.4212 0.4349 -0.0551 0.1279  -0.1181 119 ASP A C   
1018 O O   A ASP A 118 ? 0.3751 0.4206 0.4342 -0.0646 0.1411  -0.1309 119 ASP A O   
1019 O O   B ASP A 118 ? 0.3851 0.4348 0.4504 -0.0620 0.1409  -0.1326 119 ASP A O   
1020 C CB  A ASP A 118 ? 0.3489 0.4083 0.4287 -0.0263 0.1038  -0.1080 119 ASP A CB  
1021 C CB  B ASP A 118 ? 0.3422 0.4023 0.4241 -0.0245 0.1035  -0.1083 119 ASP A CB  
1022 C CG  A ASP A 118 ? 0.4857 0.5752 0.5949 -0.0261 0.1082  -0.1234 119 ASP A CG  
1023 C CG  B ASP A 118 ? 0.4560 0.5223 0.5549 -0.0050 0.0938  -0.1060 119 ASP A CG  
1024 O OD1 A ASP A 118 ? 0.5048 0.6070 0.6359 -0.0199 0.1138  -0.1349 119 ASP A OD1 
1025 O OD1 B ASP A 118 ? 0.4836 0.5477 0.5920 0.0006  0.0994  -0.1121 119 ASP A OD1 
1026 O OD2 A ASP A 118 ? 0.5493 0.6507 0.6609 -0.0320 0.1063  -0.1250 119 ASP A OD2 
1027 O OD2 B ASP A 118 ? 0.5266 0.5987 0.6282 0.0048  0.0809  -0.0982 119 ASP A OD2 
1028 N N   A THR A 119 ? 0.3249 0.3468 0.3490 -0.0649 0.1233  -0.1071 120 THR A N   
1029 N N   B THR A 119 ? 0.3399 0.3640 0.3679 -0.0636 0.1240  -0.1086 120 THR A N   
1030 C CA  A THR A 119 ? 0.3361 0.3494 0.3430 -0.0829 0.1341  -0.1121 120 THR A CA  
1031 C CA  B THR A 119 ? 0.3511 0.3675 0.3624 -0.0813 0.1343  -0.1132 120 THR A CA  
1032 C C   A THR A 119 ? 0.3918 0.3840 0.3762 -0.0948 0.1460  -0.1150 120 THR A C   
1033 C C   B THR A 119 ? 0.4040 0.3987 0.3919 -0.0937 0.1463  -0.1160 120 THR A C   
1034 O O   A THR A 119 ? 0.3869 0.3762 0.3637 -0.1098 0.1598  -0.1245 120 THR A O   
1035 O O   B THR A 119 ? 0.4062 0.4004 0.3897 -0.1081 0.1605  -0.1267 120 THR A O   
1036 C CB  A THR A 119 ? 0.3538 0.3555 0.3410 -0.0872 0.1264  -0.1018 120 THR A CB  
1037 C CB  B THR A 119 ? 0.4353 0.4415 0.4287 -0.0840 0.1253  -0.1024 120 THR A CB  
1038 O OG1 A THR A 119 ? 0.3780 0.3737 0.3531 -0.1040 0.1382  -0.1090 120 THR A OG1 
1039 O OG1 B THR A 119 ? 0.4067 0.4314 0.4201 -0.0707 0.1129  -0.0986 120 THR A OG1 
1040 C CG2 A THR A 119 ? 0.2986 0.2742 0.2571 -0.0858 0.1181  -0.0878 120 THR A CG2 
1041 C CG2 B THR A 119 ? 0.4398 0.4427 0.4230 -0.1003 0.1353  -0.1090 120 THR A CG2 
1042 N N   . CYS A 120 ? 0.3627 0.3398 0.3351 -0.0892 0.1414  -0.1076 121 CYS A N   
1043 C CA  . CYS A 120 ? 0.3815 0.3386 0.3313 -0.0999 0.1514  -0.1104 121 CYS A CA  
1044 C C   . CYS A 120 ? 0.4435 0.4148 0.4144 -0.1025 0.1661  -0.1267 121 CYS A C   
1045 O O   . CYS A 120 ? 0.4466 0.4093 0.4032 -0.1181 0.1807  -0.1354 121 CYS A O   
1046 C CB  . CYS A 120 ? 0.3833 0.3252 0.3199 -0.0929 0.1426  -0.1005 121 CYS A CB  
1047 S SG  . CYS A 120 ? 0.4252 0.3477 0.3321 -0.0936 0.1281  -0.0844 121 CYS A SG  
1048 N N   A ARG A 121 ? 0.3947 0.3871 0.3989 -0.0872 0.1625  -0.1313 122 ARG A N   
1049 N N   B ARG A 121 ? 0.3981 0.3903 0.4021 -0.0873 0.1627  -0.1313 122 ARG A N   
1050 C CA  A ARG A 121 ? 0.4026 0.4127 0.4339 -0.0853 0.1745  -0.1480 122 ARG A CA  
1051 C CA  B ARG A 121 ? 0.4077 0.4169 0.4378 -0.0862 0.1752  -0.1482 122 ARG A CA  
1052 C C   A ARG A 121 ? 0.4508 0.4779 0.4933 -0.0983 0.1873  -0.1625 122 ARG A C   
1053 C C   B ARG A 121 ? 0.4521 0.4793 0.4947 -0.0984 0.1876  -0.1627 122 ARG A C   
1054 O O   A ARG A 121 ? 0.4559 0.4851 0.5010 -0.1091 0.2040  -0.1769 122 ARG A O   
1055 O O   B ARG A 121 ? 0.4556 0.4859 0.5020 -0.1091 0.2042  -0.1774 122 ARG A O   
1056 C CB  A ARG A 121 ? 0.4001 0.4298 0.4647 -0.0638 0.1643  -0.1485 122 ARG A CB  
1057 C CB  B ARG A 121 ? 0.4136 0.4404 0.4758 -0.0649 0.1659  -0.1490 122 ARG A CB  
1058 C CG  A ARG A 121 ? 0.5554 0.5678 0.6119 -0.0521 0.1559  -0.1380 122 ARG A CG  
1059 C CG  B ARG A 121 ? 0.6005 0.6092 0.6546 -0.0564 0.1628  -0.1428 122 ARG A CG  
1060 C CD  A ARG A 121 ? 0.7078 0.7345 0.7952 -0.0328 0.1516  -0.1431 122 ARG A CD  
1061 C CD  B ARG A 121 ? 0.7241 0.7474 0.8102 -0.0376 0.1598  -0.1491 122 ARG A CD  
1062 N NE  A ARG A 121 ? 0.7784 0.7862 0.8555 -0.0216 0.1421  -0.1307 122 ARG A NE  
1063 N NE  B ARG A 121 ? 0.7746 0.8072 0.8727 -0.0213 0.1430  -0.1393 122 ARG A NE  
1064 C CZ  A ARG A 121 ? 0.9229 0.9125 0.9907 -0.0221 0.1484  -0.1320 122 ARG A CZ  
1065 C CZ  B ARG A 121 ? 0.8945 0.9128 0.9860 -0.0088 0.1321  -0.1273 122 ARG A CZ  
1066 N NH1 A ARG A 121 ? 0.8182 0.8064 0.8859 -0.0326 0.1638  -0.1450 122 ARG A NH1 
1067 N NH1 B ARG A 121 ? 0.6936 0.6890 0.7690 -0.0106 0.1362  -0.1242 122 ARG A NH1 
1068 N NH2 A ARG A 121 ? 0.6814 0.6535 0.7393 -0.0133 0.1402  -0.1211 122 ARG A NH2 
1069 N NH2 B ARG A 121 ? 0.6995 0.7256 0.7992 0.0044  0.1178  -0.1189 122 ARG A NH2 
1070 N N   . LYS A 122 ? 0.4005 0.4388 0.4482 -0.0985 0.1806  -0.1594 123 LYS A N   
1071 C CA  . LYS A 122 ? 0.4086 0.4638 0.4673 -0.1117 0.1922  -0.1732 123 LYS A CA  
1072 C C   . LYS A 122 ? 0.4767 0.5064 0.4991 -0.1350 0.2067  -0.1745 123 LYS A C   
1073 O O   . LYS A 122 ? 0.4688 0.5067 0.4975 -0.1492 0.2246  -0.1911 123 LYS A O   
1074 C CB  . LYS A 122 ? 0.4211 0.4938 0.4940 -0.1053 0.1802  -0.1692 123 LYS A CB  
1075 C CG  . LYS A 122 ? 0.6363 0.7387 0.7481 -0.0839 0.1685  -0.1727 123 LYS A CG  
1076 C CD  . LYS A 122 ? 0.7706 0.8907 0.8949 -0.0774 0.1558  -0.1690 123 LYS A CD  
1077 C CE  . LYS A 122 ? 0.9044 1.0488 1.0611 -0.0548 0.1423  -0.1704 123 LYS A CE  
1078 N NZ  . LYS A 122 ? 1.0335 1.2106 1.2173 -0.0518 0.1370  -0.1797 123 LYS A NZ  
1079 N N   . PHE A 123 ? 0.4376 0.4357 0.4213 -0.1389 0.1991  -0.1579 124 PHE A N   
1080 C CA  . PHE A 123 ? 0.4608 0.4286 0.4033 -0.1593 0.2101  -0.1565 124 PHE A CA  
1081 C C   . PHE A 123 ? 0.5289 0.4854 0.4594 -0.1688 0.2247  -0.1652 124 PHE A C   
1082 O O   . PHE A 123 ? 0.5159 0.4609 0.4275 -0.1884 0.2418  -0.1743 124 PHE A O   
1083 C CB  . PHE A 123 ? 0.4820 0.4207 0.3891 -0.1572 0.1956  -0.1369 124 PHE A CB  
1084 C CG  . PHE A 123 ? 0.4883 0.4260 0.3911 -0.1584 0.1885  -0.1306 124 PHE A CG  
1085 C CD1 . PHE A 123 ? 0.4965 0.4646 0.4346 -0.1491 0.1831  -0.1349 124 PHE A CD1 
1086 C CD2 . PHE A 123 ? 0.5352 0.4404 0.3976 -0.1672 0.1857  -0.1199 124 PHE A CD2 
1087 C CE1 . PHE A 123 ? 0.5041 0.4708 0.4375 -0.1510 0.1772  -0.1300 124 PHE A CE1 
1088 C CE2 . PHE A 123 ? 0.5505 0.4528 0.4088 -0.1677 0.1795  -0.1145 124 PHE A CE2 
1089 C CZ  . PHE A 123 ? 0.4983 0.4316 0.3923 -0.1601 0.1757  -0.1197 124 PHE A CZ  
1090 N N   . ILE A 124 ? 0.4766 0.4363 0.4183 -0.1559 0.2194  -0.1635 125 ILE A N   
1091 C CA  . ILE A 124 ? 0.5018 0.4527 0.4355 -0.1636 0.2332  -0.1731 125 ILE A CA  
1092 C C   . ILE A 124 ? 0.5692 0.5464 0.5348 -0.1697 0.2517  -0.1956 125 ILE A C   
1093 O O   . ILE A 124 ? 0.5891 0.5558 0.5377 -0.1881 0.2703  -0.2067 125 ILE A O   
1094 C CB  . ILE A 124 ? 0.5265 0.4723 0.4633 -0.1485 0.2229  -0.1657 125 ILE A CB  
1095 C CG1 . ILE A 124 ? 0.5356 0.4534 0.4354 -0.1481 0.2086  -0.1469 125 ILE A CG1 
1096 C CG2 . ILE A 124 ? 0.5578 0.5002 0.4951 -0.1549 0.2387  -0.1792 125 ILE A CG2 
1097 C CD1 . ILE A 124 ? 0.5922 0.5095 0.4998 -0.1318 0.1948  -0.1377 125 ILE A CD1 
1098 N N   . LYS A 125 ? 0.5197 0.5312 0.5304 -0.1549 0.2465  -0.2028 126 LYS A N   
1099 C CA  . LYS A 125 ? 0.5274 0.5707 0.5763 -0.1574 0.2615  -0.2258 126 LYS A CA  
1100 C C   . LYS A 125 ? 0.5861 0.6305 0.6246 -0.1812 0.2791  -0.2377 126 LYS A C   
1101 O O   . LYS A 125 ? 0.5784 0.6348 0.6295 -0.1933 0.2990  -0.2577 126 LYS A O   
1102 C CB  . LYS A 125 ? 0.5426 0.6213 0.6383 -0.1353 0.2481  -0.2289 126 LYS A CB  
1103 N N   . ALA A 126 ? 0.5454 0.5754 0.5597 -0.1888 0.2730  -0.2261 127 ALA A N   
1104 C CA  . ALA A 126 ? 0.5710 0.5957 0.5696 -0.2126 0.2895  -0.2354 127 ALA A CA  
1105 C C   . ALA A 126 ? 0.6753 0.6650 0.6288 -0.2355 0.3077  -0.2376 127 ALA A C   
1106 O O   . ALA A 126 ? 0.6909 0.6811 0.6387 -0.2570 0.3283  -0.2528 127 ALA A O   
1107 C CB  . ALA A 126 ? 0.5713 0.5844 0.5525 -0.2128 0.2769  -0.2207 127 ALA A CB  
1108 N N   . SER A 127 ? 0.6683 0.6275 0.5883 -0.2321 0.3001  -0.2231 128 SER A N   
1109 C CA  . SER A 127 ? 0.7270 0.6497 0.5986 -0.2523 0.3139  -0.2227 128 SER A CA  
1110 C C   . SER A 127 ? 0.8190 0.7488 0.7006 -0.2575 0.3306  -0.2393 128 SER A C   
1111 O O   . SER A 127 ? 0.8664 0.7687 0.7091 -0.2773 0.3455  -0.2427 128 SER A O   
1112 C CB  . SER A 127 ? 0.7948 0.6807 0.6224 -0.2471 0.2962  -0.1993 128 SER A CB  
1113 O OG  . SER A 127 ? 0.9476 0.8098 0.7430 -0.2557 0.2917  -0.1881 128 SER A OG  
1114 N N   . GLU A 128 ? 0.7483 0.7130 0.6800 -0.2402 0.3284  -0.2500 129 GLU A N   
1115 C CA  . GLU A 128 ? 0.9772 0.9506 0.9234 -0.2427 0.3440  -0.2670 129 GLU A CA  
1116 C C   . GLU A 128 ? 1.4443 1.4394 1.4110 -0.2609 0.3702  -0.2935 129 GLU A C   
1117 O O   . GLU A 128 ? 1.0113 1.0040 0.9661 -0.2781 0.3797  -0.2975 129 GLU A O   
1118 C CB  . GLU A 128 ? 0.9624 0.9584 0.9496 -0.2156 0.3305  -0.2667 129 GLU A CB  
1119 C CG  . GLU A 128 ? 1.0606 1.1012 1.1062 -0.2003 0.3277  -0.2798 129 GLU A CG  
1120 C CD  . GLU A 128 ? 1.3055 1.3630 1.3863 -0.1717 0.3113  -0.2761 129 GLU A CD  
1121 O OE1 . GLU A 128 ? 1.2056 1.2403 1.2656 -0.1614 0.2969  -0.2581 129 GLU A OE1 
1122 O OE2 . GLU A 128 ? 1.2070 1.3005 1.3360 -0.1595 0.3126  -0.2917 129 GLU A OE2 
1126 N N   A TRP B 2   ? 0.1908 0.4427 0.2494 -0.0274 -0.0196 -0.0962 1   TRP D N   
1127 N N   B TRP B 2   ? 0.2041 0.4560 0.2626 -0.0274 -0.0196 -0.0962 1   TRP D N   
1128 C CA  A TRP B 2   ? 0.1817 0.4328 0.2400 -0.0270 -0.0196 -0.0969 1   TRP D CA  
1129 C CA  B TRP B 2   ? 0.2008 0.4520 0.2592 -0.0270 -0.0196 -0.0969 1   TRP D CA  
1130 C C   A TRP B 2   ? 0.2366 0.4879 0.2961 -0.0273 -0.0201 -0.0969 1   TRP D C   
1131 C C   B TRP B 2   ? 0.2392 0.4907 0.2988 -0.0274 -0.0200 -0.0968 1   TRP D C   
1132 O O   A TRP B 2   ? 0.2353 0.4861 0.2953 -0.0277 -0.0208 -0.0964 1   TRP D O   
1133 O O   B TRP B 2   ? 0.2323 0.4836 0.2925 -0.0278 -0.0206 -0.0963 1   TRP D O   
1134 C CB  A TRP B 2   ? 0.1731 0.4226 0.2300 -0.0264 -0.0203 -0.0973 1   TRP D CB  
1135 C CB  B TRP B 2   ? 0.1936 0.4432 0.2506 -0.0264 -0.0203 -0.0973 1   TRP D CB  
1136 C CG  A TRP B 2   ? 0.1759 0.4251 0.2308 -0.0260 -0.0200 -0.0976 1   TRP D CG  
1137 C CG  B TRP B 2   ? 0.2072 0.4561 0.2649 -0.0264 -0.0215 -0.0974 1   TRP D CG  
1138 C CD1 A TRP B 2   ? 0.2090 0.4577 0.2628 -0.0260 -0.0202 -0.0975 1   TRP D CD1 
1139 C CD1 B TRP B 2   ? 0.2463 0.4944 0.3043 -0.0263 -0.0223 -0.0975 1   TRP D CD1 
1140 C CD2 A TRP B 2   ? 0.1699 0.4194 0.2239 -0.0256 -0.0194 -0.0979 1   TRP D CD2 
1141 C CD2 B TRP B 2   ? 0.2077 0.4571 0.2665 -0.0262 -0.0218 -0.0977 1   TRP D CD2 
1142 N NE1 A TRP B 2   ? 0.2003 0.4489 0.2519 -0.0256 -0.0196 -0.0980 1   TRP D NE1 
1143 N NE1 B TRP B 2   ? 0.2412 0.4894 0.3010 -0.0262 -0.0233 -0.0981 1   TRP D NE1 
1144 C CE2 A TRP B 2   ? 0.2130 0.4621 0.2646 -0.0253 -0.0192 -0.0983 1   TRP D CE2 
1145 C CE2 B TRP B 2   ? 0.2572 0.5063 0.3171 -0.0260 -0.0228 -0.0982 1   TRP D CE2 
1146 C CE3 A TRP B 2   ? 0.1807 0.4308 0.2360 -0.0254 -0.0191 -0.0979 1   TRP D CE3 
1147 C CE3 B TRP B 2   ? 0.2179 0.4680 0.2771 -0.0261 -0.0214 -0.0976 1   TRP D CE3 
1148 C CZ2 A TRP B 2   ? 0.2108 0.4601 0.2609 -0.0249 -0.0186 -0.0987 1   TRP D CZ2 
1149 C CZ2 B TRP B 2   ? 0.2473 0.4974 0.3086 -0.0257 -0.0232 -0.0989 1   TRP D CZ2 
1150 C CZ3 A TRP B 2   ? 0.1923 0.4427 0.2469 -0.0249 -0.0187 -0.0980 1   TRP D CZ3 
1151 C CZ3 B TRP B 2   ? 0.2383 0.4891 0.2983 -0.0259 -0.0216 -0.0979 1   TRP D CZ3 
1152 C CH2 A TRP B 2   ? 0.2030 0.4528 0.2548 -0.0247 -0.0184 -0.0985 1   TRP D CH2 
1153 C CH2 B TRP B 2   ? 0.2443 0.4953 0.3053 -0.0256 -0.0225 -0.0987 1   TRP D CH2 
1154 N N   . VAL B 3   ? 0.1873 0.4393 0.2476 -0.0273 -0.0198 -0.0973 2   VAL D N   
1155 C CA  . VAL B 3   ? 0.1837 0.4360 0.2447 -0.0276 -0.0201 -0.0974 2   VAL D CA  
1156 C C   . VAL B 3   ? 0.2107 0.4626 0.2722 -0.0271 -0.0200 -0.0976 2   VAL D C   
1157 O O   . VAL B 3   ? 0.1896 0.4415 0.2516 -0.0266 -0.0197 -0.0974 2   VAL D O   
1158 C CB  . VAL B 3   ? 0.2180 0.4730 0.2804 -0.0281 -0.0200 -0.0979 2   VAL D CB  
1159 C CG1 . VAL B 3   ? 0.2118 0.4688 0.2744 -0.0286 -0.0201 -0.0971 2   VAL D CG1 
1160 C CG2 . VAL B 3   ? 0.2161 0.4728 0.2804 -0.0278 -0.0195 -0.0989 2   VAL D CG2 
1161 N N   . ILE B 4   ? 0.1756 0.4277 0.2374 -0.0272 -0.0201 -0.0977 3   ILE D N   
1162 C CA  . ILE B 4   ? 0.1630 0.4154 0.2259 -0.0268 -0.0199 -0.0975 3   ILE D CA  
1163 C C   . ILE B 4   ? 0.2105 0.4639 0.2754 -0.0272 -0.0199 -0.0982 3   ILE D C   
1164 O O   . ILE B 4   ? 0.2039 0.4581 0.2686 -0.0277 -0.0203 -0.0989 3   ILE D O   
1165 C CB  . ILE B 4   ? 0.1861 0.4386 0.2482 -0.0267 -0.0199 -0.0975 3   ILE D CB  
1166 C CG1 . ILE B 4   ? 0.1684 0.4210 0.2296 -0.0261 -0.0201 -0.0975 3   ILE D CG1 
1167 C CG2 . ILE B 4   ? 0.2073 0.4609 0.2710 -0.0263 -0.0196 -0.0970 3   ILE D CG2 
1168 C CD1 . ILE B 4   ? 0.2138 0.4676 0.2755 -0.0253 -0.0203 -0.0970 3   ILE D CD1 
1169 N N   . PRO B 5   ? 0.2126 0.4665 0.2800 -0.0269 -0.0197 -0.0983 4   PRO D N   
1170 C CA  . PRO B 5   ? 0.2189 0.4745 0.2895 -0.0272 -0.0199 -0.0996 4   PRO D CA  
1171 C C   . PRO B 5   ? 0.2550 0.5109 0.3272 -0.0273 -0.0203 -0.0998 4   PRO D C   
1172 O O   . PRO B 5   ? 0.2469 0.5018 0.3188 -0.0270 -0.0201 -0.0985 4   PRO D O   
1173 C CB  . PRO B 5   ? 0.2380 0.4939 0.3114 -0.0267 -0.0196 -0.0996 4   PRO D CB  
1174 C CG  . PRO B 5   ? 0.2916 0.5459 0.3636 -0.0262 -0.0194 -0.0976 4   PRO D CG  
1175 C CD  . PRO B 5   ? 0.2386 0.4920 0.3065 -0.0263 -0.0194 -0.0973 4   PRO D CD  
1176 N N   . ALA B 6   ? 0.2352 0.4931 0.3093 -0.0277 -0.0210 -0.1016 5   ALA D N   
# 
