data_7GUU
# 
_entry.id   7GUU 
# 
_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   7GUU         pdb_00007guu 10.2210/pdb7guu/pdb 
WWPDB D_1001406665 ?            ?                   
# 
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                        7GUU 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-09 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              Rob.vanMontfort@icr.ac.uk 
_pdbx_contact_author.name_first         Rob 
_pdbx_contact_author.name_last          'van Montfort' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rodrigues, M.J.'      1 0000-0003-1243-903X 
'Le Bihan, Y.V.'       2 0000-0002-6850-9706 
'van Montfort, R.L.M.' 3 0000-0002-5688-3450 
# 
_citation.id                        primary 
_citation.title                     
'Specific radiation damage to halogenated inhibitors and ligands in protein-ligand crystal structures.' 
_citation.journal_abbrev            J.Appl.Crystallogr. 
_citation.journal_volume            57 
_citation.page_first                1951 
_citation.page_last                 1965 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39628887 
_citation.pdbx_database_id_DOI      10.1107/S1600576724010549 
_citation.journal_id_ASTM           JACGAR 
_citation.country                   DK 
_citation.journal_id_ISSN           0021-8898 
_citation.journal_id_CSD            0228 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rodrigues, M.J.'      1 0000-0003-1243-903X 
primary 'Cabry, M.'            2 0000-0002-9070-5498 
primary 'Collie, G.'           3 0000-0002-0406-922X 
primary 'Carter, M.'           4 ?                   
primary 'McAndrew, C.'         5 0000-0002-1366-088X 
primary 'Owen, R.L.'           6 0000-0002-2104-7057 
primary 'Bellenie, B.R.'       7 0000-0001-9987-3079 
primary 'Le Bihan, Y.V.'       8 0000-0002-6850-9706 
primary 'van Montfort, R.L.M.' 9 0000-0002-5688-3450 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'B-cell lymphoma 6 protein'                                            14536.915 1   ? ? ? ? 
2 polymer     syn 'WVIP tetrapeptide'                                                    610.744   1   ? ? ? ? 
3 non-polymer syn '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' 339.575   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                         35.453    1   ? ? ? ? 
5 non-polymer nat 'DIMETHYL SULFOXIDE'                                                   78.133    1   ? ? ? ? 
6 water       nat water                                                                  18.015    185 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'BCL-6,B-cell lymphoma 5 protein,BCL-5,Protein LAZ-3,Zinc finger and BTB domain-containing protein 27,Zinc finger protein 51' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
A ? 
2 'polypeptide(L)' no yes '(ACE)WVIPA' XWVIPA D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' A1ACA 
4 'CHLORIDE ION'                                                         CL    
5 'DIMETHYL SULFOXIDE'                                                   DMS   
6 water                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   ALA n 
1 5   ASP n 
1 6   SER n 
1 7   CYS n 
1 8   ILE n 
1 9   GLN n 
1 10  PHE n 
1 11  THR n 
1 12  ARG n 
1 13  HIS n 
1 14  ALA n 
1 15  SER n 
1 16  ASP n 
1 17  VAL n 
1 18  LEU n 
1 19  LEU n 
1 20  ASN n 
1 21  LEU n 
1 22  ASN n 
1 23  ARG n 
1 24  LEU n 
1 25  ARG n 
1 26  SER n 
1 27  ARG n 
1 28  ASP n 
1 29  ILE n 
1 30  LEU n 
1 31  THR n 
1 32  ASP n 
1 33  VAL n 
1 34  VAL n 
1 35  ILE n 
1 36  VAL n 
1 37  VAL n 
1 38  SER n 
1 39  ARG n 
1 40  GLU n 
1 41  GLN n 
1 42  PHE n 
1 43  ARG n 
1 44  ALA n 
1 45  HIS n 
1 46  LYS n 
1 47  THR n 
1 48  VAL n 
1 49  LEU n 
1 50  MET n 
1 51  ALA n 
1 52  CYS n 
1 53  SER n 
1 54  GLY n 
1 55  LEU n 
1 56  PHE n 
1 57  TYR n 
1 58  SER n 
1 59  ILE n 
1 60  PHE n 
1 61  THR n 
1 62  ASP n 
1 63  GLN n 
1 64  LEU n 
1 65  LYS n 
1 66  CYS n 
1 67  ASN n 
1 68  LEU n 
1 69  SER n 
1 70  VAL n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ASP n 
1 75  PRO n 
1 76  GLU n 
1 77  ILE n 
1 78  ASN n 
1 79  PRO n 
1 80  GLU n 
1 81  GLY n 
1 82  PHE n 
1 83  CYS n 
1 84  ILE n 
1 85  LEU n 
1 86  LEU n 
1 87  ASP n 
1 88  PHE n 
1 89  MET n 
1 90  TYR n 
1 91  THR n 
1 92  SER n 
1 93  ARG n 
1 94  LEU n 
1 95  ASN n 
1 96  LEU n 
1 97  ARG n 
1 98  GLU n 
1 99  GLY n 
1 100 ASN n 
1 101 ILE n 
1 102 MET n 
1 103 ALA n 
1 104 VAL n 
1 105 MET n 
1 106 ALA n 
1 107 THR n 
1 108 ALA n 
1 109 MET n 
1 110 TYR n 
1 111 LEU n 
1 112 GLN n 
1 113 MET n 
1 114 GLU n 
1 115 HIS n 
1 116 VAL n 
1 117 VAL n 
1 118 ASP n 
1 119 THR n 
1 120 CYS n 
1 121 ARG n 
1 122 LYS n 
1 123 PHE n 
1 124 ILE n 
1 125 LYS n 
1 126 ALA n 
1 127 SER n 
1 128 GLU n 
2 1   ACE n 
2 2   TRP n 
2 3   VAL n 
2 4   ILE n 
2 5   PRO n 
2 6   ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   128 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'BCL6, BCL5, LAZ3, ZBTB27, ZNF51' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               BL21-AI 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               pET48b 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1 6 'synthetic construct' ? 32630 ? 
3 2 sample ? ? 'synthetic construct' ? 32630 ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ACA non-polymer         . '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' ? 'C12 H8 Br Cl N4 O' 339.575 
ACE   non-polymer         . 'ACETYL GROUP'                                                         ? 'C2 H4 O'           44.053  
ALA   'L-peptide linking' y ALANINE                                                                ? 'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE                                                               ? 'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                             ? 'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                        ? 'C4 H7 N O4'        133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                         ? 'Cl -1'             35.453  
CYS   'L-peptide linking' y CYSTEINE                                                               ? 'C3 H7 N O2 S'      121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                   ? 'C2 H6 O S'         78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                              ? 'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                        ? 'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE                                                                ? 'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE                                                              ? 'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER                                                                  ? 'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                             ? 'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE                                                                ? 'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE                                                                 ? 'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE                                                             ? 'C5 H11 N O2 S'     149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                          ? 'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE                                                                ? 'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE                                                                 ? 'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE                                                              ? 'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                             ? 'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE                                                               ? 'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE                                                                 ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   2   ?   ?   ?   A . n 
A 1 2   PRO 2   3   ?   ?   ?   A . n 
A 1 3   GLY 3   4   ?   ?   ?   A . n 
A 1 4   ALA 4   5   ?   ?   ?   A . n 
A 1 5   ASP 5   6   6   ASP ASP A . n 
A 1 6   SER 6   7   7   SER SER A . n 
A 1 7   CYS 7   8   8   CYS CYS A . n 
A 1 8   ILE 8   9   9   ILE ILE A . n 
A 1 9   GLN 9   10  10  GLN GLN A . n 
A 1 10  PHE 10  11  11  PHE PHE A . n 
A 1 11  THR 11  12  12  THR THR A . n 
A 1 12  ARG 12  13  13  ARG ARG A . n 
A 1 13  HIS 13  14  14  HIS HIS A . n 
A 1 14  ALA 14  15  15  ALA ALA A . n 
A 1 15  SER 15  16  16  SER SER A . n 
A 1 16  ASP 16  17  17  ASP ASP A . n 
A 1 17  VAL 17  18  18  VAL VAL A . n 
A 1 18  LEU 18  19  19  LEU LEU A . n 
A 1 19  LEU 19  20  20  LEU LEU A . n 
A 1 20  ASN 20  21  21  ASN ASN A . n 
A 1 21  LEU 21  22  22  LEU LEU A . n 
A 1 22  ASN 22  23  23  ASN ASN A . n 
A 1 23  ARG 23  24  24  ARG ARG A . n 
A 1 24  LEU 24  25  25  LEU LEU A . n 
A 1 25  ARG 25  26  26  ARG ARG A . n 
A 1 26  SER 26  27  27  SER SER A . n 
A 1 27  ARG 27  28  28  ARG ARG A . n 
A 1 28  ASP 28  29  29  ASP ASP A . n 
A 1 29  ILE 29  30  30  ILE ILE A . n 
A 1 30  LEU 30  31  31  LEU LEU A . n 
A 1 31  THR 31  32  32  THR THR A . n 
A 1 32  ASP 32  33  33  ASP ASP A . n 
A 1 33  VAL 33  34  34  VAL VAL A . n 
A 1 34  VAL 34  35  35  VAL VAL A . n 
A 1 35  ILE 35  36  36  ILE ILE A . n 
A 1 36  VAL 36  37  37  VAL VAL A . n 
A 1 37  VAL 37  38  38  VAL VAL A . n 
A 1 38  SER 38  39  39  SER SER A . n 
A 1 39  ARG 39  40  40  ARG ARG A . n 
A 1 40  GLU 40  41  41  GLU GLU A . n 
A 1 41  GLN 41  42  42  GLN GLN A . n 
A 1 42  PHE 42  43  43  PHE PHE A . n 
A 1 43  ARG 43  44  44  ARG ARG A . n 
A 1 44  ALA 44  45  45  ALA ALA A . n 
A 1 45  HIS 45  46  46  HIS HIS A . n 
A 1 46  LYS 46  47  47  LYS LYS A . n 
A 1 47  THR 47  48  48  THR THR A . n 
A 1 48  VAL 48  49  49  VAL VAL A . n 
A 1 49  LEU 49  50  50  LEU LEU A . n 
A 1 50  MET 50  51  51  MET MET A . n 
A 1 51  ALA 51  52  52  ALA ALA A . n 
A 1 52  CYS 52  53  53  CYS CYS A . n 
A 1 53  SER 53  54  54  SER SER A . n 
A 1 54  GLY 54  55  55  GLY GLY A . n 
A 1 55  LEU 55  56  56  LEU LEU A . n 
A 1 56  PHE 56  57  57  PHE PHE A . n 
A 1 57  TYR 57  58  58  TYR TYR A . n 
A 1 58  SER 58  59  59  SER SER A . n 
A 1 59  ILE 59  60  60  ILE ILE A . n 
A 1 60  PHE 60  61  61  PHE PHE A . n 
A 1 61  THR 61  62  62  THR THR A . n 
A 1 62  ASP 62  63  63  ASP ASP A . n 
A 1 63  GLN 63  64  64  GLN GLN A . n 
A 1 64  LEU 64  65  65  LEU LEU A . n 
A 1 65  LYS 65  66  66  LYS LYS A . n 
A 1 66  CYS 66  67  67  CYS CYS A . n 
A 1 67  ASN 67  68  68  ASN ASN A . n 
A 1 68  LEU 68  69  69  LEU LEU A . n 
A 1 69  SER 69  70  70  SER SER A . n 
A 1 70  VAL 70  71  71  VAL VAL A . n 
A 1 71  ILE 71  72  72  ILE ILE A . n 
A 1 72  ASN 72  73  73  ASN ASN A . n 
A 1 73  LEU 73  74  74  LEU LEU A . n 
A 1 74  ASP 74  75  75  ASP ASP A . n 
A 1 75  PRO 75  76  76  PRO PRO A . n 
A 1 76  GLU 76  77  77  GLU GLU A . n 
A 1 77  ILE 77  78  78  ILE ILE A . n 
A 1 78  ASN 78  79  79  ASN ASN A . n 
A 1 79  PRO 79  80  80  PRO PRO A . n 
A 1 80  GLU 80  81  81  GLU GLU A . n 
A 1 81  GLY 81  82  82  GLY GLY A . n 
A 1 82  PHE 82  83  83  PHE PHE A . n 
A 1 83  CYS 83  84  84  CYS CYS A . n 
A 1 84  ILE 84  85  85  ILE ILE A . n 
A 1 85  LEU 85  86  86  LEU LEU A . n 
A 1 86  LEU 86  87  87  LEU LEU A . n 
A 1 87  ASP 87  88  88  ASP ASP A . n 
A 1 88  PHE 88  89  89  PHE PHE A . n 
A 1 89  MET 89  90  90  MET MET A . n 
A 1 90  TYR 90  91  91  TYR TYR A . n 
A 1 91  THR 91  92  92  THR THR A . n 
A 1 92  SER 92  93  93  SER SER A . n 
A 1 93  ARG 93  94  94  ARG ARG A . n 
A 1 94  LEU 94  95  95  LEU LEU A . n 
A 1 95  ASN 95  96  96  ASN ASN A . n 
A 1 96  LEU 96  97  97  LEU LEU A . n 
A 1 97  ARG 97  98  98  ARG ARG A . n 
A 1 98  GLU 98  99  99  GLU GLU A . n 
A 1 99  GLY 99  100 100 GLY GLY A . n 
A 1 100 ASN 100 101 101 ASN ASN A . n 
A 1 101 ILE 101 102 102 ILE ILE A . n 
A 1 102 MET 102 103 103 MET MET A . n 
A 1 103 ALA 103 104 104 ALA ALA A . n 
A 1 104 VAL 104 105 105 VAL VAL A . n 
A 1 105 MET 105 106 106 MET MET A . n 
A 1 106 ALA 106 107 107 ALA ALA A . n 
A 1 107 THR 107 108 108 THR THR A . n 
A 1 108 ALA 108 109 109 ALA ALA A . n 
A 1 109 MET 109 110 110 MET MET A . n 
A 1 110 TYR 110 111 111 TYR TYR A . n 
A 1 111 LEU 111 112 112 LEU LEU A . n 
A 1 112 GLN 112 113 113 GLN GLN A . n 
A 1 113 MET 113 114 114 MET MET A . n 
A 1 114 GLU 114 115 115 GLU GLU A . n 
A 1 115 HIS 115 116 116 HIS HIS A . n 
A 1 116 VAL 116 117 117 VAL VAL A . n 
A 1 117 VAL 117 118 118 VAL VAL A . n 
A 1 118 ASP 118 119 119 ASP ASP A . n 
A 1 119 THR 119 120 120 THR THR A . n 
A 1 120 CYS 120 121 121 CYS CYS A . n 
A 1 121 ARG 121 122 122 ARG ARG A . n 
A 1 122 LYS 122 123 123 LYS LYS A . n 
A 1 123 PHE 123 124 124 PHE PHE A . n 
A 1 124 ILE 124 125 125 ILE ILE A . n 
A 1 125 LYS 125 126 126 LYS LYS A . n 
A 1 126 ALA 126 127 127 ALA ALA A . n 
A 1 127 SER 127 128 128 SER SER A . n 
A 1 128 GLU 128 129 129 GLU GLU A . n 
B 2 1   ACE 1   0   0   ACE ACE D . n 
B 2 2   TRP 2   1   1   TRP TRP D . n 
B 2 3   VAL 3   2   2   VAL VAL D . n 
B 2 4   ILE 4   3   3   ILE ILE D . n 
B 2 5   PRO 5   4   4   PRO PRO D . n 
B 2 6   ALA 6   5   5   ALA ALA D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 A1ACA 1   201 1   A1ACA 763 A . 
D 4 CL    1   202 1   CL    CL  A . 
E 5 DMS   1   101 1   DMS   DMS D . 
F 6 HOH   1   301 178 HOH   HOH A . 
F 6 HOH   2   302 7   HOH   HOH A . 
F 6 HOH   3   303 94  HOH   HOH A . 
F 6 HOH   4   304 140 HOH   HOH A . 
F 6 HOH   5   305 19  HOH   HOH A . 
F 6 HOH   6   306 173 HOH   HOH A . 
F 6 HOH   7   307 106 HOH   HOH A . 
F 6 HOH   8   308 202 HOH   HOH A . 
F 6 HOH   9   309 166 HOH   HOH A . 
F 6 HOH   10  310 29  HOH   HOH A . 
F 6 HOH   11  311 100 HOH   HOH A . 
F 6 HOH   12  312 99  HOH   HOH A . 
F 6 HOH   13  313 247 HOH   HOH A . 
F 6 HOH   14  314 179 HOH   HOH A . 
F 6 HOH   15  315 90  HOH   HOH A . 
F 6 HOH   16  316 45  HOH   HOH A . 
F 6 HOH   17  317 139 HOH   HOH A . 
F 6 HOH   18  318 47  HOH   HOH A . 
F 6 HOH   19  319 83  HOH   HOH A . 
F 6 HOH   20  320 84  HOH   HOH A . 
F 6 HOH   21  321 75  HOH   HOH A . 
F 6 HOH   22  322 40  HOH   HOH A . 
F 6 HOH   23  323 91  HOH   HOH A . 
F 6 HOH   24  324 119 HOH   HOH A . 
F 6 HOH   25  325 101 HOH   HOH A . 
F 6 HOH   26  326 193 HOH   HOH A . 
F 6 HOH   27  327 142 HOH   HOH A . 
F 6 HOH   28  328 87  HOH   HOH A . 
F 6 HOH   29  329 237 HOH   HOH A . 
F 6 HOH   30  330 37  HOH   HOH A . 
F 6 HOH   31  331 17  HOH   HOH A . 
F 6 HOH   32  332 132 HOH   HOH A . 
F 6 HOH   33  333 239 HOH   HOH A . 
F 6 HOH   34  334 14  HOH   HOH A . 
F 6 HOH   35  335 6   HOH   HOH A . 
F 6 HOH   36  336 151 HOH   HOH A . 
F 6 HOH   37  337 20  HOH   HOH A . 
F 6 HOH   38  338 27  HOH   HOH A . 
F 6 HOH   39  339 242 HOH   HOH A . 
F 6 HOH   40  340 243 HOH   HOH A . 
F 6 HOH   41  341 4   HOH   HOH A . 
F 6 HOH   42  342 117 HOH   HOH A . 
F 6 HOH   43  343 42  HOH   HOH A . 
F 6 HOH   44  344 144 HOH   HOH A . 
F 6 HOH   45  345 50  HOH   HOH A . 
F 6 HOH   46  346 145 HOH   HOH A . 
F 6 HOH   47  347 196 HOH   HOH A . 
F 6 HOH   48  348 5   HOH   HOH A . 
F 6 HOH   49  349 44  HOH   HOH A . 
F 6 HOH   50  350 244 HOH   HOH A . 
F 6 HOH   51  351 133 HOH   HOH A . 
F 6 HOH   52  352 24  HOH   HOH A . 
F 6 HOH   53  353 85  HOH   HOH A . 
F 6 HOH   54  354 93  HOH   HOH A . 
F 6 HOH   55  355 175 HOH   HOH A . 
F 6 HOH   56  356 15  HOH   HOH A . 
F 6 HOH   57  357 122 HOH   HOH A . 
F 6 HOH   58  358 34  HOH   HOH A . 
F 6 HOH   59  359 89  HOH   HOH A . 
F 6 HOH   60  360 97  HOH   HOH A . 
F 6 HOH   61  361 141 HOH   HOH A . 
F 6 HOH   62  362 124 HOH   HOH A . 
F 6 HOH   63  363 96  HOH   HOH A . 
F 6 HOH   64  364 12  HOH   HOH A . 
F 6 HOH   65  365 86  HOH   HOH A . 
F 6 HOH   66  366 51  HOH   HOH A . 
F 6 HOH   67  367 30  HOH   HOH A . 
F 6 HOH   68  368 192 HOH   HOH A . 
F 6 HOH   69  369 21  HOH   HOH A . 
F 6 HOH   70  370 103 HOH   HOH A . 
F 6 HOH   71  371 245 HOH   HOH A . 
F 6 HOH   72  372 186 HOH   HOH A . 
F 6 HOH   73  373 207 HOH   HOH A . 
F 6 HOH   74  374 74  HOH   HOH A . 
F 6 HOH   75  375 170 HOH   HOH A . 
F 6 HOH   76  376 39  HOH   HOH A . 
F 6 HOH   77  377 131 HOH   HOH A . 
F 6 HOH   78  378 28  HOH   HOH A . 
F 6 HOH   79  379 229 HOH   HOH A . 
F 6 HOH   80  380 25  HOH   HOH A . 
F 6 HOH   81  381 177 HOH   HOH A . 
F 6 HOH   82  382 180 HOH   HOH A . 
F 6 HOH   83  383 167 HOH   HOH A . 
F 6 HOH   84  384 165 HOH   HOH A . 
F 6 HOH   85  385 105 HOH   HOH A . 
F 6 HOH   86  386 55  HOH   HOH A . 
F 6 HOH   87  387 70  HOH   HOH A . 
F 6 HOH   88  388 191 HOH   HOH A . 
F 6 HOH   89  389 76  HOH   HOH A . 
F 6 HOH   90  390 169 HOH   HOH A . 
F 6 HOH   91  391 69  HOH   HOH A . 
F 6 HOH   92  392 108 HOH   HOH A . 
F 6 HOH   93  393 157 HOH   HOH A . 
F 6 HOH   94  394 194 HOH   HOH A . 
F 6 HOH   95  395 241 HOH   HOH A . 
F 6 HOH   96  396 16  HOH   HOH A . 
F 6 HOH   97  397 174 HOH   HOH A . 
F 6 HOH   98  398 212 HOH   HOH A . 
F 6 HOH   99  399 32  HOH   HOH A . 
F 6 HOH   100 400 92  HOH   HOH A . 
F 6 HOH   101 401 22  HOH   HOH A . 
F 6 HOH   102 402 129 HOH   HOH A . 
F 6 HOH   103 403 61  HOH   HOH A . 
F 6 HOH   104 404 64  HOH   HOH A . 
F 6 HOH   105 405 43  HOH   HOH A . 
F 6 HOH   106 406 190 HOH   HOH A . 
F 6 HOH   107 407 120 HOH   HOH A . 
F 6 HOH   108 408 205 HOH   HOH A . 
F 6 HOH   109 409 82  HOH   HOH A . 
F 6 HOH   110 410 176 HOH   HOH A . 
F 6 HOH   111 411 60  HOH   HOH A . 
F 6 HOH   112 412 35  HOH   HOH A . 
F 6 HOH   113 413 46  HOH   HOH A . 
F 6 HOH   114 414 67  HOH   HOH A . 
F 6 HOH   115 415 185 HOH   HOH A . 
F 6 HOH   116 416 26  HOH   HOH A . 
F 6 HOH   117 417 223 HOH   HOH A . 
F 6 HOH   118 418 36  HOH   HOH A . 
F 6 HOH   119 419 110 HOH   HOH A . 
F 6 HOH   120 420 215 HOH   HOH A . 
F 6 HOH   121 421 65  HOH   HOH A . 
F 6 HOH   122 422 88  HOH   HOH A . 
F 6 HOH   123 423 236 HOH   HOH A . 
F 6 HOH   124 424 204 HOH   HOH A . 
F 6 HOH   125 425 68  HOH   HOH A . 
F 6 HOH   126 426 56  HOH   HOH A . 
F 6 HOH   127 427 57  HOH   HOH A . 
F 6 HOH   128 428 135 HOH   HOH A . 
F 6 HOH   129 429 95  HOH   HOH A . 
F 6 HOH   130 430 41  HOH   HOH A . 
F 6 HOH   131 431 227 HOH   HOH A . 
F 6 HOH   132 432 116 HOH   HOH A . 
F 6 HOH   133 433 187 HOH   HOH A . 
F 6 HOH   134 434 168 HOH   HOH A . 
F 6 HOH   135 435 147 HOH   HOH A . 
F 6 HOH   136 436 200 HOH   HOH A . 
F 6 HOH   137 437 214 HOH   HOH A . 
F 6 HOH   138 438 231 HOH   HOH A . 
F 6 HOH   139 439 123 HOH   HOH A . 
F 6 HOH   140 440 248 HOH   HOH A . 
F 6 HOH   141 441 228 HOH   HOH A . 
F 6 HOH   142 442 121 HOH   HOH A . 
F 6 HOH   143 443 63  HOH   HOH A . 
F 6 HOH   144 444 71  HOH   HOH A . 
F 6 HOH   145 445 225 HOH   HOH A . 
F 6 HOH   146 446 171 HOH   HOH A . 
F 6 HOH   147 447 203 HOH   HOH A . 
F 6 HOH   148 448 238 HOH   HOH A . 
F 6 HOH   149 449 220 HOH   HOH A . 
F 6 HOH   150 450 234 HOH   HOH A . 
F 6 HOH   151 451 158 HOH   HOH A . 
F 6 HOH   152 452 114 HOH   HOH A . 
F 6 HOH   153 453 125 HOH   HOH A . 
F 6 HOH   154 454 181 HOH   HOH A . 
F 6 HOH   155 455 79  HOH   HOH A . 
F 6 HOH   156 456 246 HOH   HOH A . 
F 6 HOH   157 457 81  HOH   HOH A . 
F 6 HOH   158 458 217 HOH   HOH A . 
F 6 HOH   159 459 221 HOH   HOH A . 
F 6 HOH   160 460 235 HOH   HOH A . 
F 6 HOH   161 461 107 HOH   HOH A . 
F 6 HOH   162 462 115 HOH   HOH A . 
F 6 HOH   163 463 216 HOH   HOH A . 
F 6 HOH   164 464 230 HOH   HOH A . 
F 6 HOH   165 465 113 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   169 469 183 HOH   HOH A . 
F 6 HOH   170 470 48  HOH   HOH A . 
F 6 HOH   171 471 148 HOH   HOH A . 
F 6 HOH   172 472 213 HOH   HOH A . 
F 6 HOH   173 473 206 HOH   HOH A . 
F 6 HOH   174 474 172 HOH   HOH A . 
F 6 HOH   175 475 211 HOH   HOH A . 
G 6 HOH   1   201 62  HOH   HOH D . 
G 6 HOH   2   202 23  HOH   HOH D . 
G 6 HOH   3   203 78  HOH   HOH D . 
G 6 HOH   4   204 38  HOH   HOH D . 
G 6 HOH   5   205 53  HOH   HOH D . 
G 6 HOH   6   206 73  HOH   HOH D . 
G 6 HOH   7   207 240 HOH   HOH D . 
G 6 HOH   8   208 49  HOH   HOH D . 
G 6 HOH   9   209 58  HOH   HOH D . 
G 6 HOH   10  210 195 HOH   HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 64  ? CD  ? A GLN 63  CD  
2  1 Y 1 A GLN 64  ? OE1 ? A GLN 63  OE1 
3  1 Y 1 A GLN 64  ? NE2 ? A GLN 63  NE2 
4  1 Y 1 A GLU 115 ? CD  ? A GLU 114 CD  
5  1 Y 1 A GLU 115 ? OE1 ? A GLU 114 OE1 
6  1 Y 1 A GLU 115 ? OE2 ? A GLU 114 OE2 
7  1 Y 1 A LYS 126 ? CG  ? A LYS 125 CG  
8  1 Y 1 A LYS 126 ? CD  ? A LYS 125 CD  
9  1 Y 1 A LYS 126 ? CE  ? A LYS 125 CE  
10 1 Y 1 A LYS 126 ? NZ  ? A LYS 125 NZ  
11 1 Y 1 D ALA 5   ? CA  ? B ALA 6   CA  
12 1 Y 1 D ALA 5   ? C   ? B ALA 6   C   
13 1 Y 1 D ALA 5   ? O   ? B ALA 6   O   
14 1 Y 1 D ALA 5   ? CB  ? B ALA 6   CB  
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
4 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com phasing           
http://www.globalphasing.com/buster/                ?   ? 
5 PDB_EXTRACT 3.24   'Sep. 1, 2017' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.entry_id           7GUU 
_cell.length_a           67.750 
_cell.length_b           67.750 
_cell.length_c           166.780 
_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                         7GUU 
_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          7GUU 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.65 
_exptl_crystal.density_percent_sol   66.28 
_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                     7GUU 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.990 
_reflns.d_resolution_high            1.750 
_reflns.number_obs                   23773 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.075 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.500 
_reflns.B_iso_Wilson_estimate        28.860 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.080 
_reflns.pdbx_Rpim_I_all              0.027 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     215658 
_reflns.pdbx_scaling_rejects         1198 
_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  ? 12042 1295 ? 0.936 ? ? ? 9.300 ? 2.400  ? ? ? ? ? ? 100.000 0.990 0.319 0.843 ? 
1 2 9.090 33.990 ? 1507  236  ? 0.057 ? ? ? 6.400 ? 26.800 ? ? ? ? ? ? 98.800  0.061 0.023 0.995 ? 
# 
_refine.entry_id                                 7GUU 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.7500 
_refine.ls_d_res_low                             33.9900 
_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                     23703 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1810 
_refine.ls_R_factor_R_work                       0.1800 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2030 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1500 
_refine.ls_number_reflns_R_free                  1220 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               32.6800 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.4420 
_refine.aniso_B[2][2]                            -0.4420 
_refine.aniso_B[3][3]                            0.8840 
_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               0.9590 
_refine.correlation_coeff_Fo_to_Fc_free          0.9450 
_refine.overall_SU_R_Cruickshank_DPI             0.0860 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0850 
_refine.pdbx_overall_SU_R_Blow_DPI               0.0990 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.0940 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                116.630 
_refine.B_iso_min                                14.970 
_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                        7GUU 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.220 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.7500 
_refine_hist.d_res_low                        33.9900 
_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           27.78 
_refine_hist.pdbx_B_iso_mean_solvent          48.60 
_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      1627 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1233 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1689 0.880  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.330  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    14.600 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       1.7500 
_refine_ls_shell.d_res_low                        1.8300 
_refine_ls_shell.pdbx_total_number_of_bins_used   12 
_refine_ls_shell.percent_reflns_obs               99.8200 
_refine_ls_shell.number_reflns_R_work             2691 
_refine_ls_shell.R_factor_all                     0.3031 
_refine_ls_shell.R_factor_R_work                  0.3016 
_refine_ls_shell.R_factor_R_free                  0.3347 
_refine_ls_shell.percent_reflns_R_free            4.6400 
_refine_ls_shell.number_reflns_R_free             131 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2822 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUU 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 at 3.75 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUU 
_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 7GUU       7GUU   ? 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 7GUU A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUU D 1 ? 6   ? 7GUU   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 7GUU GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUU PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUU GLY A 3 ? UNP P41182 ? ? 'expression tag' 4 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7390  ? 
1 MORE         -64   ? 
1 'SSA (A^2)'  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 33.8750000000 0.8660254038 
-0.5000000000 0.0000000000 -58.6732211064 0.0000000000 0.0000000000 -1.0000000000 27.7966666667 
# 
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 ? ? ? ? ? ? ? 1.331 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
# 
_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                   7GUU 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 39  ? A 62.98 -117.28 
2 1 SER A 39  ? B 38.77 65.97   
3 1 ARG A 40  ? B 75.16 -23.22  
4 1 SER A 93  ? A 75.98 -3.46   
5 1 GLN A 113 ? ? 61.66 60.29   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 375 ? F HOH . 
2 1 A HOH 390 ? F HOH . 
3 1 A HOH 460 ? F HOH . 
4 1 A HOH 464 ? F HOH . 
5 1 A HOH 468 ? F HOH . 
6 1 A HOH 469 ? 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 0.0014  -0.0678 -0.0452 -0.0422 0.0271  -0.0181 1.0078 1.6786  1.8885 
0.4333  -0.3251 1.0885 0.1460 -0.0815 -0.0644 -0.0492 0.0968 0.0842 0.2377  -0.0152 0.0028  
'X-RAY DIFFRACTION' 2 ? refined 18.9076 -32.4261 1.8469  -0.1357 0.1229  -0.0276 -0.0430 -0.0044 -0.0781 0.7960 -0.4565 0.0000 
-0.1655 -0.0122 0.6306 0.0269 -0.0060 -0.0209 -0.0060 0.0116 0.0448 -0.0383 0.0128  -0.0021 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 6 A 129 '{A|6 - 129}' ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 D 1 D 5   '{D|1 - 5}'   ? ? ? ? ? 
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY 2 ? A GLY 1 
2 1 Y 1 A PRO 3 ? A PRO 2 
3 1 Y 1 A GLY 4 ? A GLY 3 
4 1 Y 1 A ALA 5 ? A ALA 4 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1ACA C4   C  Y N 1   
A1ACA C5   C  Y N 2   
A1ACA C6   C  Y N 3   
A1ACA C7   C  Y N 4   
A1ACA C8   C  N N 5   
A1ACA C10  C  Y N 6   
A1ACA C1   C  Y N 7   
A1ACA C2   C  Y N 8   
A1ACA C3   C  Y N 9   
A1ACA C9   C  N N 10  
A1ACA O    O  N N 11  
A1ACA N2   N  N N 12  
A1ACA C11  C  Y N 13  
A1ACA N1   N  N N 14  
A1ACA N3   N  Y N 15  
A1ACA C    C  Y N 16  
A1ACA CL   CL N N 17  
A1ACA BR   BR N N 18  
A1ACA N    N  Y N 19  
A1ACA H1   H  N N 20  
A1ACA H2   H  N N 21  
A1ACA H3   H  N N 22  
A1ACA H4   H  N N 23  
A1ACA H5   H  N N 24  
A1ACA H6   H  N N 25  
A1ACA H7   H  N N 26  
A1ACA H8   H  N N 27  
ACE   C    C  N N 28  
ACE   O    O  N N 29  
ACE   CH3  C  N N 30  
ACE   H    H  N N 31  
ACE   H1   H  N N 32  
ACE   H2   H  N N 33  
ACE   H3   H  N N 34  
ALA   N    N  N N 35  
ALA   CA   C  N S 36  
ALA   C    C  N N 37  
ALA   O    O  N N 38  
ALA   CB   C  N N 39  
ALA   OXT  O  N N 40  
ALA   H    H  N N 41  
ALA   H2   H  N N 42  
ALA   HA   H  N N 43  
ALA   HB1  H  N N 44  
ALA   HB2  H  N N 45  
ALA   HB3  H  N N 46  
ALA   HXT  H  N N 47  
ARG   N    N  N N 48  
ARG   CA   C  N S 49  
ARG   C    C  N N 50  
ARG   O    O  N N 51  
ARG   CB   C  N N 52  
ARG   CG   C  N N 53  
ARG   CD   C  N N 54  
ARG   NE   N  N N 55  
ARG   CZ   C  N N 56  
ARG   NH1  N  N N 57  
ARG   NH2  N  N N 58  
ARG   OXT  O  N N 59  
ARG   H    H  N N 60  
ARG   H2   H  N N 61  
ARG   HA   H  N N 62  
ARG   HB2  H  N N 63  
ARG   HB3  H  N N 64  
ARG   HG2  H  N N 65  
ARG   HG3  H  N N 66  
ARG   HD2  H  N N 67  
ARG   HD3  H  N N 68  
ARG   HE   H  N N 69  
ARG   HH11 H  N N 70  
ARG   HH12 H  N N 71  
ARG   HH21 H  N N 72  
ARG   HH22 H  N N 73  
ARG   HXT  H  N N 74  
ASN   N    N  N N 75  
ASN   CA   C  N S 76  
ASN   C    C  N N 77  
ASN   O    O  N N 78  
ASN   CB   C  N N 79  
ASN   CG   C  N N 80  
ASN   OD1  O  N N 81  
ASN   ND2  N  N N 82  
ASN   OXT  O  N N 83  
ASN   H    H  N N 84  
ASN   H2   H  N N 85  
ASN   HA   H  N N 86  
ASN   HB2  H  N N 87  
ASN   HB3  H  N N 88  
ASN   HD21 H  N N 89  
ASN   HD22 H  N N 90  
ASN   HXT  H  N N 91  
ASP   N    N  N N 92  
ASP   CA   C  N S 93  
ASP   C    C  N N 94  
ASP   O    O  N N 95  
ASP   CB   C  N N 96  
ASP   CG   C  N N 97  
ASP   OD1  O  N N 98  
ASP   OD2  O  N N 99  
ASP   OXT  O  N N 100 
ASP   H    H  N N 101 
ASP   H2   H  N N 102 
ASP   HA   H  N N 103 
ASP   HB2  H  N N 104 
ASP   HB3  H  N N 105 
ASP   HD2  H  N N 106 
ASP   HXT  H  N N 107 
CL    CL   CL N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
DMS   S    S  N N 123 
DMS   O    O  N N 124 
DMS   C1   C  N N 125 
DMS   C2   C  N N 126 
DMS   H11  H  N N 127 
DMS   H12  H  N N 128 
DMS   H13  H  N N 129 
DMS   H21  H  N N 130 
DMS   H22  H  N N 131 
DMS   H23  H  N N 132 
GLN   N    N  N N 133 
GLN   CA   C  N S 134 
GLN   C    C  N N 135 
GLN   O    O  N N 136 
GLN   CB   C  N N 137 
GLN   CG   C  N N 138 
GLN   CD   C  N N 139 
GLN   OE1  O  N N 140 
GLN   NE2  N  N N 141 
GLN   OXT  O  N N 142 
GLN   H    H  N N 143 
GLN   H2   H  N N 144 
GLN   HA   H  N N 145 
GLN   HB2  H  N N 146 
GLN   HB3  H  N N 147 
GLN   HG2  H  N N 148 
GLN   HG3  H  N N 149 
GLN   HE21 H  N N 150 
GLN   HE22 H  N N 151 
GLN   HXT  H  N N 152 
GLU   N    N  N N 153 
GLU   CA   C  N S 154 
GLU   C    C  N N 155 
GLU   O    O  N N 156 
GLU   CB   C  N N 157 
GLU   CG   C  N N 158 
GLU   CD   C  N N 159 
GLU   OE1  O  N N 160 
GLU   OE2  O  N N 161 
GLU   OXT  O  N N 162 
GLU   H    H  N N 163 
GLU   H2   H  N N 164 
GLU   HA   H  N N 165 
GLU   HB2  H  N N 166 
GLU   HB3  H  N N 167 
GLU   HG2  H  N N 168 
GLU   HG3  H  N N 169 
GLU   HE2  H  N N 170 
GLU   HXT  H  N N 171 
GLY   N    N  N N 172 
GLY   CA   C  N N 173 
GLY   C    C  N N 174 
GLY   O    O  N N 175 
GLY   OXT  O  N N 176 
GLY   H    H  N N 177 
GLY   H2   H  N N 178 
GLY   HA2  H  N N 179 
GLY   HA3  H  N N 180 
GLY   HXT  H  N N 181 
HIS   N    N  N N 182 
HIS   CA   C  N S 183 
HIS   C    C  N N 184 
HIS   O    O  N N 185 
HIS   CB   C  N N 186 
HIS   CG   C  Y N 187 
HIS   ND1  N  Y N 188 
HIS   CD2  C  Y N 189 
HIS   CE1  C  Y N 190 
HIS   NE2  N  Y N 191 
HIS   OXT  O  N N 192 
HIS   H    H  N N 193 
HIS   H2   H  N N 194 
HIS   HA   H  N N 195 
HIS   HB2  H  N N 196 
HIS   HB3  H  N N 197 
HIS   HD1  H  N N 198 
HIS   HD2  H  N N 199 
HIS   HE1  H  N N 200 
HIS   HE2  H  N N 201 
HIS   HXT  H  N N 202 
HOH   O    O  N N 203 
HOH   H1   H  N N 204 
HOH   H2   H  N N 205 
ILE   N    N  N N 206 
ILE   CA   C  N S 207 
ILE   C    C  N N 208 
ILE   O    O  N N 209 
ILE   CB   C  N S 210 
ILE   CG1  C  N N 211 
ILE   CG2  C  N N 212 
ILE   CD1  C  N N 213 
ILE   OXT  O  N N 214 
ILE   H    H  N N 215 
ILE   H2   H  N N 216 
ILE   HA   H  N N 217 
ILE   HB   H  N N 218 
ILE   HG12 H  N N 219 
ILE   HG13 H  N N 220 
ILE   HG21 H  N N 221 
ILE   HG22 H  N N 222 
ILE   HG23 H  N N 223 
ILE   HD11 H  N N 224 
ILE   HD12 H  N N 225 
ILE   HD13 H  N N 226 
ILE   HXT  H  N N 227 
LEU   N    N  N N 228 
LEU   CA   C  N S 229 
LEU   C    C  N N 230 
LEU   O    O  N N 231 
LEU   CB   C  N N 232 
LEU   CG   C  N N 233 
LEU   CD1  C  N N 234 
LEU   CD2  C  N N 235 
LEU   OXT  O  N N 236 
LEU   H    H  N N 237 
LEU   H2   H  N N 238 
LEU   HA   H  N N 239 
LEU   HB2  H  N N 240 
LEU   HB3  H  N N 241 
LEU   HG   H  N N 242 
LEU   HD11 H  N N 243 
LEU   HD12 H  N N 244 
LEU   HD13 H  N N 245 
LEU   HD21 H  N N 246 
LEU   HD22 H  N N 247 
LEU   HD23 H  N N 248 
LEU   HXT  H  N N 249 
LYS   N    N  N N 250 
LYS   CA   C  N S 251 
LYS   C    C  N N 252 
LYS   O    O  N N 253 
LYS   CB   C  N N 254 
LYS   CG   C  N N 255 
LYS   CD   C  N N 256 
LYS   CE   C  N N 257 
LYS   NZ   N  N N 258 
LYS   OXT  O  N N 259 
LYS   H    H  N N 260 
LYS   H2   H  N N 261 
LYS   HA   H  N N 262 
LYS   HB2  H  N N 263 
LYS   HB3  H  N N 264 
LYS   HG2  H  N N 265 
LYS   HG3  H  N N 266 
LYS   HD2  H  N N 267 
LYS   HD3  H  N N 268 
LYS   HE2  H  N N 269 
LYS   HE3  H  N N 270 
LYS   HZ1  H  N N 271 
LYS   HZ2  H  N N 272 
LYS   HZ3  H  N N 273 
LYS   HXT  H  N N 274 
MET   N    N  N N 275 
MET   CA   C  N S 276 
MET   C    C  N N 277 
MET   O    O  N N 278 
MET   CB   C  N N 279 
MET   CG   C  N N 280 
MET   SD   S  N N 281 
MET   CE   C  N N 282 
MET   OXT  O  N N 283 
MET   H    H  N N 284 
MET   H2   H  N N 285 
MET   HA   H  N N 286 
MET   HB2  H  N N 287 
MET   HB3  H  N N 288 
MET   HG2  H  N N 289 
MET   HG3  H  N N 290 
MET   HE1  H  N N 291 
MET   HE2  H  N N 292 
MET   HE3  H  N N 293 
MET   HXT  H  N N 294 
PHE   N    N  N N 295 
PHE   CA   C  N S 296 
PHE   C    C  N N 297 
PHE   O    O  N N 298 
PHE   CB   C  N N 299 
PHE   CG   C  Y N 300 
PHE   CD1  C  Y N 301 
PHE   CD2  C  Y N 302 
PHE   CE1  C  Y N 303 
PHE   CE2  C  Y N 304 
PHE   CZ   C  Y N 305 
PHE   OXT  O  N N 306 
PHE   H    H  N N 307 
PHE   H2   H  N N 308 
PHE   HA   H  N N 309 
PHE   HB2  H  N N 310 
PHE   HB3  H  N N 311 
PHE   HD1  H  N N 312 
PHE   HD2  H  N N 313 
PHE   HE1  H  N N 314 
PHE   HE2  H  N N 315 
PHE   HZ   H  N N 316 
PHE   HXT  H  N N 317 
PRO   N    N  N N 318 
PRO   CA   C  N S 319 
PRO   C    C  N N 320 
PRO   O    O  N N 321 
PRO   CB   C  N N 322 
PRO   CG   C  N N 323 
PRO   CD   C  N N 324 
PRO   OXT  O  N N 325 
PRO   H    H  N N 326 
PRO   HA   H  N N 327 
PRO   HB2  H  N N 328 
PRO   HB3  H  N N 329 
PRO   HG2  H  N N 330 
PRO   HG3  H  N N 331 
PRO   HD2  H  N N 332 
PRO   HD3  H  N N 333 
PRO   HXT  H  N N 334 
SER   N    N  N N 335 
SER   CA   C  N S 336 
SER   C    C  N N 337 
SER   O    O  N N 338 
SER   CB   C  N N 339 
SER   OG   O  N N 340 
SER   OXT  O  N N 341 
SER   H    H  N N 342 
SER   H2   H  N N 343 
SER   HA   H  N N 344 
SER   HB2  H  N N 345 
SER   HB3  H  N N 346 
SER   HG   H  N N 347 
SER   HXT  H  N N 348 
THR   N    N  N N 349 
THR   CA   C  N S 350 
THR   C    C  N N 351 
THR   O    O  N N 352 
THR   CB   C  N R 353 
THR   OG1  O  N N 354 
THR   CG2  C  N N 355 
THR   OXT  O  N N 356 
THR   H    H  N N 357 
THR   H2   H  N N 358 
THR   HA   H  N N 359 
THR   HB   H  N N 360 
THR   HG1  H  N N 361 
THR   HG21 H  N N 362 
THR   HG22 H  N N 363 
THR   HG23 H  N N 364 
THR   HXT  H  N N 365 
TRP   N    N  N N 366 
TRP   CA   C  N S 367 
TRP   C    C  N N 368 
TRP   O    O  N N 369 
TRP   CB   C  N N 370 
TRP   CG   C  Y N 371 
TRP   CD1  C  Y N 372 
TRP   CD2  C  Y N 373 
TRP   NE1  N  Y N 374 
TRP   CE2  C  Y N 375 
TRP   CE3  C  Y N 376 
TRP   CZ2  C  Y N 377 
TRP   CZ3  C  Y N 378 
TRP   CH2  C  Y N 379 
TRP   OXT  O  N N 380 
TRP   H    H  N N 381 
TRP   H2   H  N N 382 
TRP   HA   H  N N 383 
TRP   HB2  H  N N 384 
TRP   HB3  H  N N 385 
TRP   HD1  H  N N 386 
TRP   HE1  H  N N 387 
TRP   HE3  H  N N 388 
TRP   HZ2  H  N N 389 
TRP   HZ3  H  N N 390 
TRP   HH2  H  N N 391 
TRP   HXT  H  N N 392 
TYR   N    N  N N 393 
TYR   CA   C  N S 394 
TYR   C    C  N N 395 
TYR   O    O  N N 396 
TYR   CB   C  N N 397 
TYR   CG   C  Y N 398 
TYR   CD1  C  Y N 399 
TYR   CD2  C  Y N 400 
TYR   CE1  C  Y N 401 
TYR   CE2  C  Y N 402 
TYR   CZ   C  Y N 403 
TYR   OH   O  N N 404 
TYR   OXT  O  N N 405 
TYR   H    H  N N 406 
TYR   H2   H  N N 407 
TYR   HA   H  N N 408 
TYR   HB2  H  N N 409 
TYR   HB3  H  N N 410 
TYR   HD1  H  N N 411 
TYR   HD2  H  N N 412 
TYR   HE1  H  N N 413 
TYR   HE2  H  N N 414 
TYR   HH   H  N N 415 
TYR   HXT  H  N N 416 
VAL   N    N  N N 417 
VAL   CA   C  N S 418 
VAL   C    C  N N 419 
VAL   O    O  N N 420 
VAL   CB   C  N N 421 
VAL   CG1  C  N N 422 
VAL   CG2  C  N N 423 
VAL   OXT  O  N N 424 
VAL   H    H  N N 425 
VAL   H2   H  N N 426 
VAL   HA   H  N N 427 
VAL   HB   H  N N 428 
VAL   HG11 H  N N 429 
VAL   HG12 H  N N 430 
VAL   HG13 H  N N 431 
VAL   HG21 H  N N 432 
VAL   HG22 H  N N 433 
VAL   HG23 H  N N 434 
VAL   HXT  H  N N 435 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1ACA N   C1   doub Y N 1   
A1ACA N   C    sing Y N 2   
A1ACA CL  C    sing N N 3   
A1ACA C1  C2   sing Y N 4   
A1ACA C   N3   doub Y N 5   
A1ACA C2  BR   sing N N 6   
A1ACA C2  C3   doub Y N 7   
A1ACA N3  C3   sing Y N 8   
A1ACA C3  N1   sing N N 9   
A1ACA N1  C4   sing N N 10  
A1ACA C4  C5   doub Y N 11  
A1ACA C4  C11  sing Y N 12  
A1ACA C5  C6   sing Y N 13  
A1ACA C11 C10  doub Y N 14  
A1ACA C6  C7   doub Y N 15  
A1ACA C10 C7   sing Y N 16  
A1ACA C10 C9   sing N N 17  
A1ACA C7  N2   sing N N 18  
A1ACA C9  C8   sing N N 19  
A1ACA N2  C8   sing N N 20  
A1ACA C8  O    doub N N 21  
A1ACA C5  H1   sing N N 22  
A1ACA C6  H2   sing N N 23  
A1ACA C1  H3   sing N N 24  
A1ACA C9  H4   sing N N 25  
A1ACA C9  H5   sing N N 26  
A1ACA N2  H6   sing N N 27  
A1ACA C11 H7   sing N N 28  
A1ACA N1  H8   sing N N 29  
ACE   C   O    doub N N 30  
ACE   C   CH3  sing N N 31  
ACE   C   H    sing N N 32  
ACE   CH3 H1   sing N N 33  
ACE   CH3 H2   sing N N 34  
ACE   CH3 H3   sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
DMS   S   O    doub N N 118 
DMS   S   C1   sing N N 119 
DMS   S   C2   sing N N 120 
DMS   C1  H11  sing N N 121 
DMS   C1  H12  sing N N 122 
DMS   C1  H13  sing N N 123 
DMS   C2  H21  sing N N 124 
DMS   C2  H22  sing N N 125 
DMS   C2  H23  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
HIS   N   CA   sing N N 173 
HIS   N   H    sing N N 174 
HIS   N   H2   sing N N 175 
HIS   CA  C    sing N N 176 
HIS   CA  CB   sing N N 177 
HIS   CA  HA   sing N N 178 
HIS   C   O    doub N N 179 
HIS   C   OXT  sing N N 180 
HIS   CB  CG   sing N N 181 
HIS   CB  HB2  sing N N 182 
HIS   CB  HB3  sing N N 183 
HIS   CG  ND1  sing Y N 184 
HIS   CG  CD2  doub Y N 185 
HIS   ND1 CE1  doub Y N 186 
HIS   ND1 HD1  sing N N 187 
HIS   CD2 NE2  sing Y N 188 
HIS   CD2 HD2  sing N N 189 
HIS   CE1 NE2  sing Y N 190 
HIS   CE1 HE1  sing N N 191 
HIS   NE2 HE2  sing N N 192 
HIS   OXT HXT  sing N N 193 
HOH   O   H1   sing N N 194 
HOH   O   H2   sing N N 195 
ILE   N   CA   sing N N 196 
ILE   N   H    sing N N 197 
ILE   N   H2   sing N N 198 
ILE   CA  C    sing N N 199 
ILE   CA  CB   sing N N 200 
ILE   CA  HA   sing N N 201 
ILE   C   O    doub N N 202 
ILE   C   OXT  sing N N 203 
ILE   CB  CG1  sing N N 204 
ILE   CB  CG2  sing N N 205 
ILE   CB  HB   sing N N 206 
ILE   CG1 CD1  sing N N 207 
ILE   CG1 HG12 sing N N 208 
ILE   CG1 HG13 sing N N 209 
ILE   CG2 HG21 sing N N 210 
ILE   CG2 HG22 sing N N 211 
ILE   CG2 HG23 sing N N 212 
ILE   CD1 HD11 sing N N 213 
ILE   CD1 HD12 sing N N 214 
ILE   CD1 HD13 sing N N 215 
ILE   OXT HXT  sing N N 216 
LEU   N   CA   sing N N 217 
LEU   N   H    sing N N 218 
LEU   N   H2   sing N N 219 
LEU   CA  C    sing N N 220 
LEU   CA  CB   sing N N 221 
LEU   CA  HA   sing N N 222 
LEU   C   O    doub N N 223 
LEU   C   OXT  sing N N 224 
LEU   CB  CG   sing N N 225 
LEU   CB  HB2  sing N N 226 
LEU   CB  HB3  sing N N 227 
LEU   CG  CD1  sing N N 228 
LEU   CG  CD2  sing N N 229 
LEU   CG  HG   sing N N 230 
LEU   CD1 HD11 sing N N 231 
LEU   CD1 HD12 sing N N 232 
LEU   CD1 HD13 sing N N 233 
LEU   CD2 HD21 sing N N 234 
LEU   CD2 HD22 sing N N 235 
LEU   CD2 HD23 sing N N 236 
LEU   OXT HXT  sing N N 237 
LYS   N   CA   sing N N 238 
LYS   N   H    sing N N 239 
LYS   N   H2   sing N N 240 
LYS   CA  C    sing N N 241 
LYS   CA  CB   sing N N 242 
LYS   CA  HA   sing N N 243 
LYS   C   O    doub N N 244 
LYS   C   OXT  sing N N 245 
LYS   CB  CG   sing N N 246 
LYS   CB  HB2  sing N N 247 
LYS   CB  HB3  sing N N 248 
LYS   CG  CD   sing N N 249 
LYS   CG  HG2  sing N N 250 
LYS   CG  HG3  sing N N 251 
LYS   CD  CE   sing N N 252 
LYS   CD  HD2  sing N N 253 
LYS   CD  HD3  sing N N 254 
LYS   CE  NZ   sing N N 255 
LYS   CE  HE2  sing N N 256 
LYS   CE  HE3  sing N N 257 
LYS   NZ  HZ1  sing N N 258 
LYS   NZ  HZ2  sing N N 259 
LYS   NZ  HZ3  sing N N 260 
LYS   OXT HXT  sing N N 261 
MET   N   CA   sing N N 262 
MET   N   H    sing N N 263 
MET   N   H2   sing N N 264 
MET   CA  C    sing N N 265 
MET   CA  CB   sing N N 266 
MET   CA  HA   sing N N 267 
MET   C   O    doub N N 268 
MET   C   OXT  sing N N 269 
MET   CB  CG   sing N N 270 
MET   CB  HB2  sing N N 271 
MET   CB  HB3  sing N N 272 
MET   CG  SD   sing N N 273 
MET   CG  HG2  sing N N 274 
MET   CG  HG3  sing N N 275 
MET   SD  CE   sing N N 276 
MET   CE  HE1  sing N N 277 
MET   CE  HE2  sing N N 278 
MET   CE  HE3  sing N N 279 
MET   OXT HXT  sing N N 280 
PHE   N   CA   sing N N 281 
PHE   N   H    sing N N 282 
PHE   N   H2   sing N N 283 
PHE   CA  C    sing N N 284 
PHE   CA  CB   sing N N 285 
PHE   CA  HA   sing N N 286 
PHE   C   O    doub N N 287 
PHE   C   OXT  sing N N 288 
PHE   CB  CG   sing N N 289 
PHE   CB  HB2  sing N N 290 
PHE   CB  HB3  sing N N 291 
PHE   CG  CD1  doub Y N 292 
PHE   CG  CD2  sing Y N 293 
PHE   CD1 CE1  sing Y N 294 
PHE   CD1 HD1  sing N N 295 
PHE   CD2 CE2  doub Y N 296 
PHE   CD2 HD2  sing N N 297 
PHE   CE1 CZ   doub Y N 298 
PHE   CE1 HE1  sing N N 299 
PHE   CE2 CZ   sing Y N 300 
PHE   CE2 HE2  sing N N 301 
PHE   CZ  HZ   sing N N 302 
PHE   OXT HXT  sing N N 303 
PRO   N   CA   sing N N 304 
PRO   N   CD   sing N N 305 
PRO   N   H    sing N N 306 
PRO   CA  C    sing N N 307 
PRO   CA  CB   sing N N 308 
PRO   CA  HA   sing N N 309 
PRO   C   O    doub N N 310 
PRO   C   OXT  sing N N 311 
PRO   CB  CG   sing N N 312 
PRO   CB  HB2  sing N N 313 
PRO   CB  HB3  sing N N 314 
PRO   CG  CD   sing N N 315 
PRO   CG  HG2  sing N N 316 
PRO   CG  HG3  sing N N 317 
PRO   CD  HD2  sing N N 318 
PRO   CD  HD3  sing N N 319 
PRO   OXT HXT  sing N N 320 
SER   N   CA   sing N N 321 
SER   N   H    sing N N 322 
SER   N   H2   sing N N 323 
SER   CA  C    sing N N 324 
SER   CA  CB   sing N N 325 
SER   CA  HA   sing N N 326 
SER   C   O    doub N N 327 
SER   C   OXT  sing N N 328 
SER   CB  OG   sing N N 329 
SER   CB  HB2  sing N N 330 
SER   CB  HB3  sing N N 331 
SER   OG  HG   sing N N 332 
SER   OXT HXT  sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TRP   N   CA   sing N N 350 
TRP   N   H    sing N N 351 
TRP   N   H2   sing N N 352 
TRP   CA  C    sing N N 353 
TRP   CA  CB   sing N N 354 
TRP   CA  HA   sing N N 355 
TRP   C   O    doub N N 356 
TRP   C   OXT  sing N N 357 
TRP   CB  CG   sing N N 358 
TRP   CB  HB2  sing N N 359 
TRP   CB  HB3  sing N N 360 
TRP   CG  CD1  doub Y N 361 
TRP   CG  CD2  sing Y N 362 
TRP   CD1 NE1  sing Y N 363 
TRP   CD1 HD1  sing N N 364 
TRP   CD2 CE2  doub Y N 365 
TRP   CD2 CE3  sing Y N 366 
TRP   NE1 CE2  sing Y N 367 
TRP   NE1 HE1  sing N N 368 
TRP   CE2 CZ2  sing Y N 369 
TRP   CE3 CZ3  doub Y N 370 
TRP   CE3 HE3  sing N N 371 
TRP   CZ2 CH2  doub Y N 372 
TRP   CZ2 HZ2  sing N N 373 
TRP   CZ3 CH2  sing Y N 374 
TRP   CZ3 HZ3  sing N N 375 
TRP   CH2 HH2  sing N N 376 
TRP   OXT HXT  sing N N 377 
TYR   N   CA   sing N N 378 
TYR   N   H    sing N N 379 
TYR   N   H2   sing N N 380 
TYR   CA  C    sing N N 381 
TYR   CA  CB   sing N N 382 
TYR   CA  HA   sing N N 383 
TYR   C   O    doub N N 384 
TYR   C   OXT  sing N N 385 
TYR   CB  CG   sing N N 386 
TYR   CB  HB2  sing N N 387 
TYR   CB  HB3  sing N N 388 
TYR   CG  CD1  doub Y N 389 
TYR   CG  CD2  sing Y N 390 
TYR   CD1 CE1  sing Y N 391 
TYR   CD1 HD1  sing N N 392 
TYR   CD2 CE2  doub Y N 393 
TYR   CD2 HD2  sing N N 394 
TYR   CE1 CZ   doub Y N 395 
TYR   CE1 HE1  sing N N 396 
TYR   CE2 CZ   sing Y N 397 
TYR   CE2 HE2  sing N N 398 
TYR   CZ  OH   sing N N 399 
TYR   OH  HH   sing N N 400 
TYR   OXT HXT  sing N N 401 
VAL   N   CA   sing N N 402 
VAL   N   H    sing N N 403 
VAL   N   H2   sing N N 404 
VAL   CA  C    sing N N 405 
VAL   CA  CB   sing N N 406 
VAL   CA  HA   sing N N 407 
VAL   C   O    doub N N 408 
VAL   C   OXT  sing N N 409 
VAL   CB  CG1  sing N N 410 
VAL   CB  CG2  sing N N 411 
VAL   CB  HB   sing N N 412 
VAL   CG1 HG11 sing N N 413 
VAL   CG1 HG12 sing N N 414 
VAL   CG1 HG13 sing N N 415 
VAL   CG2 HG21 sing N N 416 
VAL   CG2 HG22 sing N N 417 
VAL   CG2 HG23 sing N N 418 
VAL   OXT HXT  sing N N 419 
# 
_pdbx_deposit_group.group_id            G_1002065 
_pdbx_deposit_group.group_title         'X-ray dose series of B-cell lymphoma 6 protein BTB domain in complex with ligand 2' 
_pdbx_deposit_group.group_description   
;Crystal structures of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 solved at increasing X-ray dose using Many Structures One Crystal (MSOX) crystallography.
;
_pdbx_deposit_group.group_type          undefined 
# 
_atom_sites.entry_id                    7GUU 
_atom_sites.fract_transf_matrix[1][1]   0.014760 
_atom_sites.fract_transf_matrix[1][2]   0.008522 
_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]   0.017044 
_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]   0.005996 
_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   ? 17.312 -21.241 -4.820 1.00 62.08  ? 6   ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 5   ? 18.229 -22.134 -5.528 1.00 60.98  ? 6   ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 5   ? 17.767 -23.608 -5.458 1.00 60.53  ? 6   ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 5   ? 16.718 -23.910 -4.877 1.00 61.51  ? 6   ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 5   ? 19.661 -21.982 -4.960 1.00 61.84  ? 6   ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 5   ? 20.754 -22.039 -6.015 1.00 75.54  ? 6   ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 5   ? 20.914 -23.111 -6.653 1.00 75.66  ? 6   ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 5   ? 21.457 -21.019 -6.198 1.00 82.73  ? 6   ASP   A OD2 1 
ATOM   9    N  N   . SER   A 1 6   ? 18.549 -24.513 -6.067 1.00 51.51  ? 7   SER   A N   1 
ATOM   10   C  CA  . SER   A 1 6   ? 18.294 -25.949 -6.063 1.00 48.78  ? 7   SER   A CA  1 
ATOM   11   C  C   . SER   A 1 6   ? 19.290 -26.670 -5.105 1.00 44.55  ? 7   SER   A C   1 
ATOM   12   O  O   . SER   A 1 6   ? 19.594 -27.845 -5.297 1.00 43.72  ? 7   SER   A O   1 
ATOM   13   C  CB  . SER   A 1 6   ? 18.388 -26.502 -7.482 1.00 54.37  ? 7   SER   A CB  1 
ATOM   14   O  OG  . SER   A 1 6   ? 19.664 -26.264 -8.052 1.00 65.43  ? 7   SER   A OG  1 
ATOM   15   N  N   . CYS   A 1 7   ? 19.770 -25.968 -4.062 1.00 35.87  ? 8   CYS   A N   1 
ATOM   16   C  CA  . CYS   A 1 7   ? 20.713 -26.536 -3.097 1.00 32.78  ? 8   CYS   A CA  1 
ATOM   17   C  C   . CYS   A 1 7   ? 20.092 -27.697 -2.288 1.00 33.29  ? 8   CYS   A C   1 
ATOM   18   O  O   . CYS   A 1 7   ? 18.869 -27.763 -2.128 1.00 32.88  ? 8   CYS   A O   1 
ATOM   19   C  CB  . CYS   A 1 7   ? 21.221 -25.445 -2.152 1.00 33.31  ? 8   CYS   A CB  1 
ATOM   20   S  SG  . CYS   A 1 7   ? 22.415 -24.287 -2.884 1.00 38.44  ? 8   CYS   A SG  1 
ATOM   21   N  N   . ILE   A 1 8   ? 20.935 -28.603 -1.786 1.00 26.06  ? 9   ILE   A N   1 
ATOM   22   C  CA  . ILE   A 1 8   ? 20.578 -29.604 -0.781 1.00 23.48  ? 9   ILE   A CA  1 
ATOM   23   C  C   . ILE   A 1 8   ? 21.196 -29.068 0.518  1.00 24.92  ? 9   ILE   A C   1 
ATOM   24   O  O   . ILE   A 1 8   ? 22.147 -28.272 0.470  1.00 24.46  ? 9   ILE   A O   1 
ATOM   25   C  CB  . ILE   A 1 8   ? 20.932 -31.082 -1.092 1.00 26.54  ? 9   ILE   A CB  1 
ATOM   26   C  CG1 . ILE   A 1 8   ? 22.465 -31.270 -1.318 1.00 26.25  ? 9   ILE   A CG1 1 
ATOM   27   C  CG2 . ILE   A 1 8   ? 20.086 -31.618 -2.267 1.00 27.98  ? 9   ILE   A CG2 1 
ATOM   28   C  CD1 . ILE   A 1 8   ? 22.933 -32.715 -1.542 1.00 30.35  ? 9   ILE   A CD1 1 
ATOM   29   N  N   A GLN   A 1 9   ? 20.725 -29.521 1.681  0.66 20.74  ? 10  GLN   A N   1 
ATOM   30   N  N   B GLN   A 1 9   ? 20.599 -29.435 1.652  0.34 21.38  ? 10  GLN   A N   1 
ATOM   31   C  CA  A GLN   A 1 9   ? 21.266 -29.028 2.955  0.66 19.91  ? 10  GLN   A CA  1 
ATOM   32   C  CA  B GLN   A 1 9   ? 21.014 -28.940 2.953  0.34 20.47  ? 10  GLN   A CA  1 
ATOM   33   C  C   A GLN   A 1 9   ? 21.583 -30.176 3.904  0.66 22.93  ? 10  GLN   A C   1 
ATOM   34   C  C   B GLN   A 1 9   ? 21.400 -30.070 3.886  0.34 23.97  ? 10  GLN   A C   1 
ATOM   35   O  O   A GLN   A 1 9   ? 20.799 -31.120 4.005  0.66 23.81  ? 10  GLN   A O   1 
ATOM   36   O  O   B GLN   A 1 9   ? 20.697 -31.076 3.969  0.34 24.42  ? 10  GLN   A O   1 
ATOM   37   C  CB  A GLN   A 1 9   ? 20.268 -28.032 3.603  0.66 21.47  ? 10  GLN   A CB  1 
ATOM   38   C  CB  B GLN   A 1 9   ? 19.881 -28.109 3.563  0.34 21.61  ? 10  GLN   A CB  1 
ATOM   39   C  CG  A GLN   A 1 9   ? 20.464 -27.806 5.121  0.66 25.79  ? 10  GLN   A CG  1 
ATOM   40   C  CG  B GLN   A 1 9   ? 20.356 -27.127 4.631  0.34 22.39  ? 10  GLN   A CG  1 
ATOM   41   C  CD  A GLN   A 1 9   ? 20.096 -26.434 5.613  0.66 47.13  ? 10  GLN   A CD  1 
ATOM   42   C  CD  B GLN   A 1 9   ? 19.596 -27.252 5.927  0.34 36.37  ? 10  GLN   A CD  1 
ATOM   43   O  OE1 A GLN   A 1 9   ? 19.660 -25.563 4.858  0.66 40.10  ? 10  GLN   A OE1 1 
ATOM   44   O  OE1 B GLN   A 1 9   ? 18.371 -27.439 5.954  0.34 27.89  ? 10  GLN   A OE1 1 
ATOM   45   N  NE2 A GLN   A 1 9   ? 20.289 -26.204 6.906  0.66 43.16  ? 10  GLN   A NE2 1 
ATOM   46   N  NE2 B GLN   A 1 9   ? 20.311 -27.125 7.037  0.34 31.90  ? 10  GLN   A NE2 1 
ATOM   47   N  N   A PHE   A 1 10  ? 22.719 -30.088 4.607  0.66 20.67  ? 11  PHE   A N   1 
ATOM   48   N  N   B PHE   A 1 10  ? 22.513 -29.893 4.595  0.34 20.85  ? 11  PHE   A N   1 
ATOM   49   C  CA  A PHE   A 1 10  ? 23.088 -31.101 5.587  0.66 19.04  ? 11  PHE   A CA  1 
ATOM   50   C  CA  B PHE   A 1 10  ? 23.005 -30.874 5.551  0.34 19.88  ? 11  PHE   A CA  1 
ATOM   51   C  C   A PHE   A 1 10  ? 22.638 -30.595 6.947  0.66 21.50  ? 11  PHE   A C   1 
ATOM   52   C  C   B PHE   A 1 10  ? 22.516 -30.428 6.903  0.34 22.42  ? 11  PHE   A C   1 
ATOM   53   O  O   A PHE   A 1 10  ? 23.236 -29.662 7.504  0.66 19.90  ? 11  PHE   A O   1 
ATOM   54   O  O   B PHE   A 1 10  ? 22.941 -29.377 7.403  0.34 21.39  ? 11  PHE   A O   1 
ATOM   55   C  CB  A PHE   A 1 10  ? 24.602 -31.415 5.529  0.66 19.54  ? 11  PHE   A CB  1 
ATOM   56   C  CB  B PHE   A 1 10  ? 24.538 -30.985 5.462  0.34 21.02  ? 11  PHE   A CB  1 
ATOM   57   C  CG  A PHE   A 1 10  ? 24.996 -32.611 6.363  0.66 20.47  ? 11  PHE   A CG  1 
ATOM   58   C  CG  B PHE   A 1 10  ? 25.004 -31.760 4.249  0.34 23.17  ? 11  PHE   A CG  1 
ATOM   59   C  CD1 A PHE   A 1 10  ? 24.618 -33.899 5.991  0.66 23.13  ? 11  PHE   A CD1 1 
ATOM   60   C  CD1 B PHE   A 1 10  ? 24.748 -31.296 2.961  0.34 26.78  ? 11  PHE   A CD1 1 
ATOM   61   C  CD2 A PHE   A 1 10  ? 25.790 -32.459 7.498  0.66 20.94  ? 11  PHE   A CD2 1 
ATOM   62   C  CD2 B PHE   A 1 10  ? 25.728 -32.937 4.391  0.34 26.51  ? 11  PHE   A CD2 1 
ATOM   63   C  CE1 A PHE   A 1 10  ? 24.977 -35.005 6.773  0.66 23.99  ? 11  PHE   A CE1 1 
ATOM   64   C  CE1 B PHE   A 1 10  ? 25.184 -32.006 1.841  0.34 28.12  ? 11  PHE   A CE1 1 
ATOM   65   C  CE2 A PHE   A 1 10  ? 26.122 -33.559 8.292  0.66 22.60  ? 11  PHE   A CE2 1 
ATOM   66   C  CE2 B PHE   A 1 10  ? 26.162 -33.651 3.265  0.34 30.03  ? 11  PHE   A CE2 1 
ATOM   67   C  CZ  A PHE   A 1 10  ? 25.717 -34.825 7.924  0.66 21.26  ? 11  PHE   A CZ  1 
ATOM   68   C  CZ  B PHE   A 1 10  ? 25.892 -33.175 2.000  0.34 28.01  ? 11  PHE   A CZ  1 
ATOM   69   N  N   . THR   A 1 11  ? 21.550 -31.179 7.455  1.00 19.45  ? 12  THR   A N   1 
ATOM   70   C  CA  . THR   A 1 11  ? 20.897 -30.811 8.723  1.00 19.70  ? 12  THR   A CA  1 
ATOM   71   C  C   . THR   A 1 11  ? 21.859 -30.572 9.907  1.00 22.22  ? 12  THR   A C   1 
ATOM   72   O  O   . THR   A 1 11  ? 21.747 -29.546 10.596 1.00 21.93  ? 12  THR   A O   1 
ATOM   73   C  CB  . THR   A 1 11  ? 19.831 -31.853 9.086  1.00 27.19  ? 12  THR   A CB  1 
ATOM   74   O  OG1 . THR   A 1 11  ? 18.927 -31.988 7.974  1.00 29.15  ? 12  THR   A OG1 1 
ATOM   75   C  CG2 . THR   A 1 11  ? 19.046 -31.472 10.358 1.00 30.39  ? 12  THR   A CG2 1 
ATOM   76   N  N   . ARG   A 1 12  ? 22.802 -31.503 10.114 1.00 19.61  ? 13  ARG   A N   1 
ATOM   77   C  CA  . ARG   A 1 12  ? 23.706 -31.418 11.271 1.00 19.17  ? 13  ARG   A CA  1 
ATOM   78   C  C   . ARG   A 1 12  ? 24.934 -30.512 11.062 1.00 20.76  ? 13  ARG   A C   1 
ATOM   79   O  O   . ARG   A 1 12  ? 25.757 -30.422 11.979 1.00 19.78  ? 13  ARG   A O   1 
ATOM   80   C  CB  . ARG   A 1 12  ? 24.190 -32.828 11.672 1.00 23.82  ? 13  ARG   A CB  1 
ATOM   81   C  CG  . ARG   A 1 12  ? 23.101 -33.799 12.179 1.00 33.81  ? 13  ARG   A CG  1 
ATOM   82   C  CD  . ARG   A 1 12  ? 22.505 -33.386 13.517 1.00 55.41  ? 13  ARG   A CD  1 
ATOM   83   N  NE  . ARG   A 1 12  ? 23.477 -33.423 14.616 1.00 67.83  ? 13  ARG   A NE  1 
ATOM   84   C  CZ  . ARG   A 1 12  ? 23.311 -32.810 15.785 1.00 78.93  ? 13  ARG   A CZ  1 
ATOM   85   N  NH1 . ARG   A 1 12  ? 24.240 -32.904 16.726 1.00 66.65  ? 13  ARG   A NH1 1 
ATOM   86   N  NH2 . ARG   A 1 12  ? 22.222 -32.085 16.016 1.00 62.70  ? 13  ARG   A NH2 1 
ATOM   87   N  N   . HIS   A 1 13  ? 25.092 -29.894 9.873  1.00 17.42  ? 14  HIS   A N   1 
ATOM   88   C  CA  . HIS   A 1 13  ? 26.319 -29.135 9.589  1.00 17.78  ? 14  HIS   A CA  1 
ATOM   89   C  C   . HIS   A 1 13  ? 26.619 -28.029 10.614 1.00 19.80  ? 14  HIS   A C   1 
ATOM   90   O  O   . HIS   A 1 13  ? 27.758 -27.947 11.114 1.00 18.00  ? 14  HIS   A O   1 
ATOM   91   C  CB  . HIS   A 1 13  ? 26.305 -28.560 8.153  1.00 17.76  ? 14  HIS   A CB  1 
ATOM   92   C  CG  . HIS   A 1 13  ? 27.565 -27.807 7.855  1.00 19.54  ? 14  HIS   A CG  1 
ATOM   93   N  ND1 . HIS   A 1 13  ? 28.744 -28.478 7.634  1.00 19.67  ? 14  HIS   A ND1 1 
ATOM   94   C  CD2 . HIS   A 1 13  ? 27.776 -26.479 7.701  1.00 19.85  ? 14  HIS   A CD2 1 
ATOM   95   C  CE1 . HIS   A 1 13  ? 29.653 -27.547 7.372  1.00 19.39  ? 14  HIS   A CE1 1 
ATOM   96   N  NE2 . HIS   A 1 13  ? 29.123 -26.323 7.415  1.00 18.69  ? 14  HIS   A NE2 1 
ATOM   97   N  N   . ALA   A 1 14  ? 25.632 -27.152 10.889 1.00 17.13  ? 15  ALA   A N   1 
ATOM   98   C  CA  . ALA   A 1 14  ? 25.867 -26.034 11.832 1.00 17.11  ? 15  ALA   A CA  1 
ATOM   99   C  C   . ALA   A 1 14  ? 26.287 -26.537 13.232 1.00 19.05  ? 15  ALA   A C   1 
ATOM   100  O  O   . ALA   A 1 14  ? 27.220 -25.983 13.839 1.00 18.10  ? 15  ALA   A O   1 
ATOM   101  C  CB  . ALA   A 1 14  ? 24.628 -25.137 11.903 1.00 18.14  ? 15  ALA   A CB  1 
ATOM   102  N  N   A SER   A 1 15  ? 25.625 -27.590 13.721 0.42 18.15  ? 16  SER   A N   1 
ATOM   103  N  N   B SER   A 1 15  ? 25.625 -27.597 13.720 0.30 17.48  ? 16  SER   A N   1 
ATOM   104  N  N   C SER   A 1 15  ? 25.621 -27.588 13.738 0.28 17.58  ? 16  SER   A N   1 
ATOM   105  C  CA  A SER   A 1 15  ? 25.928 -28.171 15.026 0.42 17.61  ? 16  SER   A CA  1 
ATOM   106  C  CA  B SER   A 1 15  ? 25.912 -28.203 15.021 0.30 16.98  ? 16  SER   A CA  1 
ATOM   107  C  CA  C SER   A 1 15  ? 25.943 -28.148 15.053 0.28 17.17  ? 16  SER   A CA  1 
ATOM   108  C  C   A SER   A 1 15  ? 27.344 -28.747 15.033 0.42 20.93  ? 16  SER   A C   1 
ATOM   109  C  C   B SER   A 1 15  ? 27.321 -28.787 15.046 0.30 20.93  ? 16  SER   A C   1 
ATOM   110  C  C   C SER   A 1 15  ? 27.334 -28.790 15.060 0.28 21.05  ? 16  SER   A C   1 
ATOM   111  O  O   A SER   A 1 15  ? 28.081 -28.546 16.005 0.42 18.94  ? 16  SER   A O   1 
ATOM   112  O  O   B SER   A 1 15  ? 28.034 -28.628 16.042 0.30 19.46  ? 16  SER   A O   1 
ATOM   113  O  O   C SER   A 1 15  ? 28.053 -28.664 16.055 0.28 19.62  ? 16  SER   A O   1 
ATOM   114  C  CB  A SER   A 1 15  ? 24.920 -29.262 15.373 0.42 21.56  ? 16  SER   A CB  1 
ATOM   115  C  CB  B SER   A 1 15  ? 24.894 -29.296 15.330 0.30 20.22  ? 16  SER   A CB  1 
ATOM   116  C  CB  C SER   A 1 15  ? 24.875 -29.141 15.504 0.28 20.88  ? 16  SER   A CB  1 
ATOM   117  O  OG  A SER   A 1 15  ? 25.215 -29.812 16.646 0.42 24.57  ? 16  SER   A OG  1 
ATOM   118  O  OG  B SER   A 1 15  ? 23.595 -28.744 15.452 0.30 22.20  ? 16  SER   A OG  1 
ATOM   119  O  OG  C SER   A 1 15  ? 24.800 -30.260 14.639 0.28 23.77  ? 16  SER   A OG  1 
ATOM   120  N  N   . ASP   A 1 16  ? 27.725 -29.446 13.944 1.00 18.46  ? 17  ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 16  ? 29.059 -30.075 13.810 1.00 18.63  ? 17  ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 16  ? 30.130 -28.990 13.779 1.00 19.52  ? 17  ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 16  ? 31.173 -29.162 14.405 1.00 19.40  ? 17  ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 16  ? 29.145 -30.943 12.547 1.00 20.58  ? 17  ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 16  ? 28.378 -32.260 12.641 1.00 28.26  ? 17  ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 16  ? 27.864 -32.579 13.746 1.00 27.11  ? 17  ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 16  ? 28.276 -32.962 11.609 1.00 31.26  ? 17  ASP   A OD2 1 
ATOM   128  N  N   . VAL   A 1 17  ? 29.863 -27.871 13.074 1.00 15.79  ? 18  VAL   A N   1 
ATOM   129  C  CA  . VAL   A 1 17  ? 30.822 -26.745 13.036 1.00 14.97  ? 18  VAL   A CA  1 
ATOM   130  C  C   . VAL   A 1 17  ? 31.049 -26.218 14.462 1.00 19.66  ? 18  VAL   A C   1 
ATOM   131  O  O   . VAL   A 1 17  ? 32.187 -26.036 14.899 1.00 17.79  ? 18  VAL   A O   1 
ATOM   132  C  CB  . VAL   A 1 17  ? 30.356 -25.614 12.073 1.00 17.27  ? 18  VAL   A CB  1 
ATOM   133  C  CG1 . VAL   A 1 17  ? 31.146 -24.316 12.303 1.00 17.27  ? 18  VAL   A CG1 1 
ATOM   134  C  CG2 . VAL   A 1 17  ? 30.454 -26.058 10.600 1.00 17.51  ? 18  VAL   A CG2 1 
ATOM   135  N  N   . LEU   A 1 18  ? 29.963 -25.966 15.171 1.00 16.87  ? 19  LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 18  ? 30.069 -25.407 16.529 1.00 18.09  ? 19  LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 18  ? 30.797 -26.358 17.492 1.00 18.58  ? 19  LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 18  ? 31.649 -25.905 18.272 1.00 17.91  ? 19  LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 18  ? 28.687 -25.020 17.055 1.00 18.78  ? 19  LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 18  ? 28.702 -24.133 18.318 1.00 22.21  ? 19  LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 18  ? 29.282 -22.752 18.027 1.00 22.24  ? 19  LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 18  ? 27.288 -23.975 18.879 1.00 25.10  ? 19  LEU   A CD2 1 
ATOM   143  N  N   . LEU   A 1 19  ? 30.502 -27.659 17.384 1.00 17.15  ? 20  LEU   A N   1 
ATOM   144  C  CA  . LEU   A 1 19  ? 31.169 -28.696 18.169 1.00 18.10  ? 20  LEU   A CA  1 
ATOM   145  C  C   . LEU   A 1 19  ? 32.689 -28.609 17.910 1.00 20.69  ? 20  LEU   A C   1 
ATOM   146  O  O   . LEU   A 1 19  ? 33.471 -28.605 18.870 1.00 20.21  ? 20  LEU   A O   1 
ATOM   147  C  CB  . LEU   A 1 19  ? 30.638 -30.064 17.774 1.00 20.36  ? 20  LEU   A CB  1 
ATOM   148  C  CG  . LEU   A 1 19  ? 31.238 -31.256 18.511 1.00 28.29  ? 20  LEU   A CG  1 
ATOM   149  C  CD1 . LEU   A 1 19  ? 30.887 -31.191 20.003 1.00 30.53  ? 20  LEU   A CD1 1 
ATOM   150  C  CD2 . LEU   A 1 19  ? 30.666 -32.557 17.953 1.00 31.55  ? 20  LEU   A CD2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 33.093 -28.464 16.629 1.00 17.79  ? 21  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 34.521 -28.351 16.306 1.00 16.15  ? 21  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 35.139 -27.055 16.817 1.00 18.91  ? 21  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 36.279 -27.053 17.276 1.00 19.40  ? 21  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 34.761 -28.554 14.816 1.00 17.64  ? 21  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.715 -30.020 14.431 1.00 26.69  ? 21  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.924 -30.915 15.265 1.00 24.36  ? 21  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.443 -30.296 13.157 1.00 22.98  ? 21  ASN   A ND2 1 
ATOM   159  N  N   . LEU   A 1 21  ? 34.400 -25.953 16.756 1.00 17.99  ? 22  LEU   A N   1 
ATOM   160  C  CA  . LEU   A 1 21  ? 34.928 -24.687 17.281 1.00 17.08  ? 22  LEU   A CA  1 
ATOM   161  C  C   . LEU   A 1 21  ? 35.135 -24.825 18.794 1.00 19.20  ? 22  LEU   A C   1 
ATOM   162  O  O   . LEU   A 1 21  ? 36.101 -24.269 19.333 1.00 19.03  ? 22  LEU   A O   1 
ATOM   163  C  CB  . LEU   A 1 21  ? 33.977 -23.528 16.965 1.00 16.91  ? 22  LEU   A CB  1 
ATOM   164  C  CG  . LEU   A 1 21  ? 33.839 -23.193 15.467 1.00 18.76  ? 22  LEU   A CG  1 
ATOM   165  C  CD1 . LEU   A 1 21  ? 32.728 -22.154 15.251 1.00 20.12  ? 22  LEU   A CD1 1 
ATOM   166  C  CD2 . LEU   A 1 21  ? 35.183 -22.735 14.850 1.00 21.44  ? 22  LEU   A CD2 1 
ATOM   167  N  N   . ASN   A 1 22  ? 34.215 -25.534 19.485 1.00 16.80  ? 23  ASN   A N   1 
ATOM   168  C  CA  . ASN   A 1 22  ? 34.369 -25.751 20.941 1.00 17.89  ? 23  ASN   A CA  1 
ATOM   169  C  C   . ASN   A 1 22  ? 35.602 -26.632 21.244 1.00 21.94  ? 23  ASN   A C   1 
ATOM   170  O  O   . ASN   A 1 22  ? 36.315 -26.378 22.221 1.00 22.53  ? 23  ASN   A O   1 
ATOM   171  C  CB  . ASN   A 1 22  ? 33.116 -26.359 21.558 1.00 20.26  ? 23  ASN   A CB  1 
ATOM   172  C  CG  . ASN   A 1 22  ? 33.118 -26.236 23.073 1.00 27.46  ? 23  ASN   A CG  1 
ATOM   173  O  OD1 . ASN   A 1 22  ? 33.638 -25.270 23.647 1.00 24.59  ? 23  ASN   A OD1 1 
ATOM   174  N  ND2 . ASN   A 1 22  ? 32.550 -27.216 23.735 1.00 28.48  ? 23  ASN   A ND2 1 
ATOM   175  N  N   . ARG   A 1 23  ? 35.877 -27.629 20.384 1.00 19.45  ? 24  ARG   A N   1 
ATOM   176  C  CA  . ARG   A 1 23  ? 37.065 -28.487 20.506 1.00 20.30  ? 24  ARG   A CA  1 
ATOM   177  C  C   . ARG   A 1 23  ? 38.323 -27.629 20.364 1.00 24.41  ? 24  ARG   A C   1 
ATOM   178  O  O   . ARG   A 1 23  ? 39.277 -27.799 21.130 1.00 23.94  ? 24  ARG   A O   1 
ATOM   179  C  CB  . ARG   A 1 23  ? 37.051 -29.597 19.441 1.00 20.76  ? 24  ARG   A CB  1 
ATOM   180  C  CG  . ARG   A 1 23  ? 36.045 -30.699 19.768 1.00 24.49  ? 24  ARG   A CG  1 
ATOM   181  C  CD  . ARG   A 1 23  ? 35.831 -31.620 18.573 1.00 24.12  ? 24  ARG   A CD  1 
ATOM   182  N  NE  . ARG   A 1 23  ? 35.012 -32.775 18.936 1.00 33.18  ? 24  ARG   A NE  1 
ATOM   183  C  CZ  . ARG   A 1 23  ? 34.343 -33.528 18.071 1.00 48.08  ? 24  ARG   A CZ  1 
ATOM   184  N  NH1 . ARG   A 1 23  ? 34.345 -33.229 16.776 1.00 35.85  ? 24  ARG   A NH1 1 
ATOM   185  N  NH2 . ARG   A 1 23  ? 33.651 -34.574 18.495 1.00 40.78  ? 24  ARG   A NH2 1 
ATOM   186  N  N   . LEU   A 1 24  ? 38.316 -26.672 19.412 1.00 20.56  ? 25  LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 24  ? 39.463 -25.769 19.248 1.00 20.79  ? 25  LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 24  ? 39.622 -24.919 20.513 1.00 24.67  ? 25  LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 24  ? 40.750 -24.737 20.996 1.00 25.27  ? 25  LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 24  ? 39.272 -24.846 18.051 1.00 20.34  ? 25  LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 24  ? 39.284 -25.516 16.671 1.00 24.60  ? 25  LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 24  ? 39.182 -24.459 15.577 1.00 24.83  ? 25  LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 24  ? 40.524 -26.407 16.497 1.00 24.52  ? 25  LEU   A CD2 1 
ATOM   194  N  N   . ARG   A 1 25  ? 38.486 -24.410 21.059 1.00 21.09  ? 26  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 25  ? 38.533 -23.622 22.295 1.00 21.93  ? 26  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 25  ? 39.157 -24.434 23.463 1.00 26.54  ? 26  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 25  ? 40.045 -23.919 24.161 1.00 26.94  ? 26  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 25  ? 37.138 -23.109 22.677 1.00 22.22  ? 26  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 25  ? 37.227 -22.268 23.959 1.00 25.09  ? 26  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 25  ? 35.927 -21.623 24.328 1.00 29.72  ? 26  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 25  ? 34.912 -22.594 24.714 1.00 27.69  ? 26  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 25  ? 34.287 -22.614 25.887 1.00 35.67  ? 26  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 25  ? 34.636 -21.765 26.851 1.00 30.03  ? 26  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 25  ? 33.332 -23.498 26.117 1.00 29.12  ? 26  ARG   A NH2 1 
ATOM   205  N  N   A SER   A 1 26  ? 38.692 -25.679 23.664 0.39 24.12  ? 27  SER   A N   1 
ATOM   206  N  N   B SER   A 1 26  ? 38.694 -25.688 23.649 0.28 23.74  ? 27  SER   A N   1 
ATOM   207  N  N   C SER   A 1 26  ? 38.690 -25.679 23.663 0.33 24.03  ? 27  SER   A N   1 
ATOM   208  C  CA  A SER   A 1 26  ? 39.160 -26.574 24.728 0.39 25.42  ? 27  SER   A CA  1 
ATOM   209  C  CA  B SER   A 1 26  ? 39.148 -26.627 24.683 0.28 24.85  ? 27  SER   A CA  1 
ATOM   210  C  CA  C SER   A 1 26  ? 39.154 -26.587 24.719 0.33 25.28  ? 27  SER   A CA  1 
ATOM   211  C  C   A SER   A 1 26  ? 40.670 -26.842 24.657 0.39 30.97  ? 27  SER   A C   1 
ATOM   212  C  C   B SER   A 1 26  ? 40.660 -26.841 24.646 0.28 30.54  ? 27  SER   A C   1 
ATOM   213  C  C   C SER   A 1 26  ? 40.667 -26.844 24.653 0.33 30.82  ? 27  SER   A C   1 
ATOM   214  O  O   A SER   A 1 26  ? 41.317 -26.960 25.699 0.39 31.97  ? 27  SER   A O   1 
ATOM   215  O  O   B SER   A 1 26  ? 41.293 -26.942 25.698 0.28 31.41  ? 27  SER   A O   1 
ATOM   216  O  O   C SER   A 1 26  ? 41.310 -26.962 25.698 0.33 31.77  ? 27  SER   A O   1 
ATOM   217  C  CB  A SER   A 1 26  ? 38.378 -27.883 24.710 0.39 28.38  ? 27  SER   A CB  1 
ATOM   218  C  CB  B SER   A 1 26  ? 38.464 -27.978 24.504 0.28 27.51  ? 27  SER   A CB  1 
ATOM   219  C  CB  C SER   A 1 26  ? 38.393 -27.906 24.654 0.33 28.26  ? 27  SER   A CB  1 
ATOM   220  O  OG  A SER   A 1 26  ? 38.745 -28.726 23.629 0.39 34.95  ? 27  SER   A OG  1 
ATOM   221  O  OG  B SER   A 1 26  ? 37.088 -27.934 24.837 0.28 32.09  ? 27  SER   A OG  1 
ATOM   222  O  OG  C SER   A 1 26  ? 38.831 -28.816 25.651 0.33 36.09  ? 27  SER   A OG  1 
ATOM   223  N  N   . ARG   A 1 27  ? 41.226 -26.909 23.431 1.00 26.89  ? 28  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 27  ? 42.656 -27.149 23.205 1.00 28.24  ? 28  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 27  ? 43.443 -25.855 23.013 1.00 30.20  ? 28  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 27  ? 44.647 -25.902 22.738 1.00 30.79  ? 28  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 27  ? 42.816 -28.101 22.015 1.00 29.90  ? 28  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 27  ? 42.106 -29.434 22.232 1.00 35.48  ? 28  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 27  ? 42.062 -30.270 20.975 1.00 40.29  ? 28  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 27  ? 43.413 -30.614 20.532 1.00 51.97  ? 28  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 27  ? 43.741 -30.842 19.268 1.00 65.87  ? 28  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 27  ? 44.995 -31.126 18.943 1.00 55.22  ? 28  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 27  ? 42.828 -30.755 18.316 1.00 50.59  ? 28  ARG   A NH2 1 
ATOM   234  N  N   . ASP   A 1 28  ? 42.764 -24.701 23.167 1.00 24.52  ? 29  ASP   A N   1 
ATOM   235  C  CA  . ASP   A 1 28  ? 43.325 -23.357 23.024 1.00 25.29  ? 29  ASP   A CA  1 
ATOM   236  C  C   . ASP   A 1 28  ? 43.961 -23.131 21.624 1.00 30.11  ? 29  ASP   A C   1 
ATOM   237  O  O   . ASP   A 1 28  ? 45.012 -22.497 21.491 1.00 31.54  ? 29  ASP   A O   1 
ATOM   238  C  CB  . ASP   A 1 28  ? 44.316 -23.041 24.176 1.00 28.45  ? 29  ASP   A CB  1 
ATOM   239  C  CG  . ASP   A 1 28  ? 44.636 -21.567 24.315 1.00 36.02  ? 29  ASP   A CG  1 
ATOM   240  O  OD1 . ASP   A 1 28  ? 43.724 -20.740 24.101 1.00 36.33  ? 29  ASP   A OD1 1 
ATOM   241  O  OD2 . ASP   A 1 28  ? 45.794 -21.241 24.639 1.00 40.05  ? 29  ASP   A OD2 1 
ATOM   242  N  N   . ILE   A 1 29  ? 43.324 -23.683 20.595 1.00 23.49  ? 30  ILE   A N   1 
ATOM   243  C  CA  . ILE   A 1 29  ? 43.799 -23.592 19.212 1.00 23.43  ? 30  ILE   A CA  1 
ATOM   244  C  C   . ILE   A 1 29  ? 43.198 -22.386 18.497 1.00 25.47  ? 30  ILE   A C   1 
ATOM   245  O  O   . ILE   A 1 29  ? 41.968 -22.261 18.395 1.00 21.48  ? 30  ILE   A O   1 
ATOM   246  C  CB  . ILE   A 1 29  ? 43.549 -24.904 18.432 1.00 26.32  ? 30  ILE   A CB  1 
ATOM   247  C  CG1 . ILE   A 1 29  ? 44.343 -26.091 19.055 1.00 28.26  ? 30  ILE   A CG1 1 
ATOM   248  C  CG2 . ILE   A 1 29  ? 43.879 -24.716 16.923 1.00 26.25  ? 30  ILE   A CG2 1 
ATOM   249  C  CD1 . ILE   A 1 29  ? 43.871 -27.462 18.543 1.00 32.38  ? 30  ILE   A CD1 1 
ATOM   250  N  N   . LEU   A 1 30  ? 44.084 -21.493 18.006 1.00 24.88  ? 31  LEU   A N   1 
ATOM   251  C  CA  . LEU   A 1 30  ? 43.730 -20.291 17.240 1.00 25.63  ? 31  LEU   A CA  1 
ATOM   252  C  C   . LEU   A 1 30  ? 42.824 -19.292 17.993 1.00 25.79  ? 31  LEU   A C   1 
ATOM   253  O  O   . LEU   A 1 30  ? 42.245 -18.404 17.369 1.00 23.20  ? 31  LEU   A O   1 
ATOM   254  C  CB  . LEU   A 1 30  ? 43.166 -20.610 15.852 1.00 26.44  ? 31  LEU   A CB  1 
ATOM   255  C  CG  . LEU   A 1 30  ? 44.212 -21.166 14.832 1.00 34.12  ? 31  LEU   A CG  1 
ATOM   256  C  CD1 . LEU   A 1 30  ? 43.611 -21.252 13.473 1.00 35.20  ? 31  LEU   A CD1 1 
ATOM   257  C  CD2 . LEU   A 1 30  ? 45.441 -20.303 14.752 1.00 41.13  ? 31  LEU   A CD2 1 
ATOM   258  N  N   . THR   A 1 31  ? 42.798 -19.367 19.328 1.00 23.14  ? 32  THR   A N   1 
ATOM   259  C  CA  . THR   A 1 31  ? 42.128 -18.356 20.155 1.00 22.28  ? 32  THR   A CA  1 
ATOM   260  C  C   . THR   A 1 31  ? 42.950 -17.065 19.948 1.00 27.28  ? 32  THR   A C   1 
ATOM   261  O  O   . THR   A 1 31  ? 44.174 -17.124 19.768 1.00 27.48  ? 32  THR   A O   1 
ATOM   262  C  CB  . THR   A 1 31  ? 42.082 -18.796 21.624 1.00 25.60  ? 32  THR   A CB  1 
ATOM   263  O  OG1 . THR   A 1 31  ? 43.411 -19.124 22.035 1.00 30.16  ? 32  THR   A OG1 1 
ATOM   264  C  CG2 . THR   A 1 31  ? 41.139 -20.006 21.841 1.00 25.49  ? 32  THR   A CG2 1 
ATOM   265  N  N   . ASP   A 1 32  ? 42.274 -15.930 19.838 1.00 23.33  ? 33  ASP   A N   1 
ATOM   266  C  CA  . ASP   A 1 32  ? 42.940 -14.678 19.494 1.00 23.21  ? 33  ASP   A CA  1 
ATOM   267  C  C   . ASP   A 1 32  ? 42.598 -13.525 20.398 1.00 26.00  ? 33  ASP   A C   1 
ATOM   268  O  O   . ASP   A 1 32  ? 42.937 -12.383 20.080 1.00 26.13  ? 33  ASP   A O   1 
ATOM   269  C  CB  . ASP   A 1 32  ? 42.624 -14.316 18.028 1.00 23.93  ? 33  ASP   A CB  1 
ATOM   270  C  CG  . ASP   A 1 32  ? 41.139 -14.332 17.666 1.00 32.52  ? 33  ASP   A CG  1 
ATOM   271  O  OD1 . ASP   A 1 32  ? 40.294 -14.416 18.590 1.00 28.12  ? 33  ASP   A OD1 1 
ATOM   272  O  OD2 . ASP   A 1 32  ? 40.828 -14.271 16.470 1.00 40.25  ? 33  ASP   A OD2 1 
ATOM   273  N  N   . VAL   A 1 33  ? 41.921 -13.800 21.519 1.00 21.88  ? 34  VAL   A N   1 
ATOM   274  C  CA  . VAL   A 1 33  ? 41.597 -12.749 22.489 1.00 21.49  ? 34  VAL   A CA  1 
ATOM   275  C  C   . VAL   A 1 33  ? 41.437 -13.356 23.876 1.00 25.81  ? 34  VAL   A C   1 
ATOM   276  O  O   . VAL   A 1 33  ? 41.051 -14.535 24.005 1.00 25.10  ? 34  VAL   A O   1 
ATOM   277  C  CB  . VAL   A 1 33  ? 40.314 -11.934 22.054 1.00 23.39  ? 34  VAL   A CB  1 
ATOM   278  C  CG1 . VAL   A 1 33  ? 39.015 -12.738 22.228 1.00 21.25  ? 34  VAL   A CG1 1 
ATOM   279  C  CG2 . VAL   A 1 33  ? 40.211 -10.578 22.783 1.00 23.90  ? 34  VAL   A CG2 1 
ATOM   280  N  N   A VAL   A 1 34  ? 41.732 -12.542 24.903 0.60 23.07  ? 35  VAL   A N   1 
ATOM   281  N  N   B VAL   A 1 34  ? 41.727 -12.561 24.910 0.40 22.52  ? 35  VAL   A N   1 
ATOM   282  C  CA  A VAL   A 1 34  ? 41.524 -12.853 26.312 0.60 23.14  ? 35  VAL   A CA  1 
ATOM   283  C  CA  B VAL   A 1 34  ? 41.472 -12.936 26.292 0.40 22.26  ? 35  VAL   A CA  1 
ATOM   284  C  C   A VAL   A 1 34  ? 40.453 -11.864 26.786 0.60 25.69  ? 35  VAL   A C   1 
ATOM   285  C  C   B VAL   A 1 34  ? 40.511 -11.897 26.879 0.40 25.52  ? 35  VAL   A C   1 
ATOM   286  O  O   A VAL   A 1 34  ? 40.586 -10.656 26.559 0.60 25.81  ? 35  VAL   A O   1 
ATOM   287  O  O   B VAL   A 1 34  ? 40.743 -10.691 26.762 0.40 25.76  ? 35  VAL   A O   1 
ATOM   288  C  CB  A VAL   A 1 34  ? 42.820 -12.721 27.170 0.60 28.49  ? 35  VAL   A CB  1 
ATOM   289  C  CB  B VAL   A 1 34  ? 42.724 -13.253 27.163 0.40 27.05  ? 35  VAL   A CB  1 
ATOM   290  C  CG1 A VAL   A 1 34  ? 42.551 -13.031 28.644 0.60 28.71  ? 35  VAL   A CG1 1 
ATOM   291  C  CG1 B VAL   A 1 34  ? 43.628 -12.039 27.344 0.40 27.44  ? 35  VAL   A CG1 1 
ATOM   292  C  CG2 A VAL   A 1 34  ? 43.930 -13.616 26.640 0.60 28.91  ? 35  VAL   A CG2 1 
ATOM   293  C  CG2 B VAL   A 1 34  ? 42.328 -13.842 28.516 0.40 27.15  ? 35  VAL   A CG2 1 
ATOM   294  N  N   . ILE   A 1 35  ? 39.390 -12.378 27.414 1.00 21.23  ? 36  ILE   A N   1 
ATOM   295  C  CA  . ILE   A 1 35  ? 38.339 -11.561 28.009 1.00 21.19  ? 36  ILE   A CA  1 
ATOM   296  C  C   . ILE   A 1 35  ? 38.620 -11.568 29.500 1.00 25.75  ? 36  ILE   A C   1 
ATOM   297  O  O   . ILE   A 1 35  ? 38.637 -12.643 30.118 1.00 25.39  ? 36  ILE   A O   1 
ATOM   298  C  CB  . ILE   A 1 35  ? 36.901 -12.067 27.695 1.00 22.34  ? 36  ILE   A CB  1 
ATOM   299  C  CG1 . ILE   A 1 35  ? 36.667 -12.235 26.157 1.00 22.18  ? 36  ILE   A CG1 1 
ATOM   300  C  CG2 . ILE   A 1 35  ? 35.868 -11.110 28.314 1.00 23.31  ? 36  ILE   A CG2 1 
ATOM   301  C  CD1 . ILE   A 1 35  ? 36.949 -10.968 25.276 1.00 22.49  ? 36  ILE   A CD1 1 
ATOM   302  N  N   . VAL   A 1 36  ? 38.865 -10.382 30.061 1.00 23.12  ? 37  VAL   A N   1 
ATOM   303  C  CA  . VAL   A 1 36  ? 39.171 -10.253 31.488 1.00 23.15  ? 37  VAL   A CA  1 
ATOM   304  C  C   . VAL   A 1 36  ? 37.912 -9.840  32.249 1.00 28.45  ? 37  VAL   A C   1 
ATOM   305  O  O   . VAL   A 1 36  ? 37.306 -8.805  31.947 1.00 26.70  ? 37  VAL   A O   1 
ATOM   306  C  CB  . VAL   A 1 36  ? 40.385 -9.313  31.755 1.00 27.66  ? 37  VAL   A CB  1 
ATOM   307  C  CG1 . VAL   A 1 36  ? 40.680 -9.203  33.256 1.00 28.24  ? 37  VAL   A CG1 1 
ATOM   308  C  CG2 . VAL   A 1 36  ? 41.630 -9.809  31.017 1.00 28.14  ? 37  VAL   A CG2 1 
ATOM   309  N  N   . VAL   A 1 37  ? 37.534 -10.652 33.248 1.00 25.81  ? 38  VAL   A N   1 
ATOM   310  C  CA  . VAL   A 1 37  ? 36.343 -10.442 34.065 1.00 25.31  ? 38  VAL   A CA  1 
ATOM   311  C  C   . VAL   A 1 37  ? 36.839 -10.466 35.498 1.00 32.67  ? 38  VAL   A C   1 
ATOM   312  O  O   . VAL   A 1 37  ? 36.986 -11.539 36.089 1.00 29.79  ? 38  VAL   A O   1 
ATOM   313  C  CB  . VAL   A 1 37  ? 35.244 -11.492 33.766 1.00 27.94  ? 38  VAL   A CB  1 
ATOM   314  C  CG1 . VAL   A 1 37  ? 33.915 -11.068 34.385 1.00 28.22  ? 38  VAL   A CG1 1 
ATOM   315  C  CG2 . VAL   A 1 37  ? 35.093 -11.704 32.257 1.00 26.48  ? 38  VAL   A CG2 1 
ATOM   316  N  N   A SER   A 1 38  ? 37.255 -9.286  35.998 0.54 32.82  ? 39  SER   A N   1 
ATOM   317  N  N   B SER   A 1 38  ? 37.070 -9.258  36.043 0.46 32.12  ? 39  SER   A N   1 
ATOM   318  C  CA  A SER   A 1 38  ? 37.857 -9.093  37.324 0.54 34.16  ? 39  SER   A CA  1 
ATOM   319  C  CA  B SER   A 1 38  ? 37.597 -8.991  37.381 0.46 33.23  ? 39  SER   A CA  1 
ATOM   320  C  C   A SER   A 1 38  ? 39.194 -9.873  37.417 0.54 35.61  ? 39  SER   A C   1 
ATOM   321  C  C   B SER   A 1 38  ? 38.688 -9.998  37.753 0.46 35.20  ? 39  SER   A C   1 
ATOM   322  O  O   A SER   A 1 38  ? 40.104 -9.584  36.640 0.54 35.20  ? 39  SER   A O   1 
ATOM   323  O  O   B SER   A 1 38  ? 38.498 -10.885 38.589 0.46 35.07  ? 39  SER   A O   1 
ATOM   324  C  CB  A SER   A 1 38  ? 36.879 -9.470  38.440 0.54 39.66  ? 39  SER   A CB  1 
ATOM   325  C  CB  B SER   A 1 38  ? 36.476 -8.890  38.407 0.46 37.73  ? 39  SER   A CB  1 
ATOM   326  O  OG  A SER   A 1 38  ? 35.637 -8.796  38.304 0.54 54.64  ? 39  SER   A OG  1 
ATOM   327  O  OG  B SER   A 1 38  ? 35.827 -7.636  38.265 0.46 45.46  ? 39  SER   A OG  1 
ATOM   328  N  N   A ARG   A 1 39  ? 39.294 -10.868 38.327 0.54 31.57  ? 40  ARG   A N   1 
ATOM   329  N  N   B ARG   A 1 39  ? 39.794 -9.900  37.000 0.46 29.83  ? 40  ARG   A N   1 
ATOM   330  C  CA  A ARG   A 1 39  ? 40.497 -11.683 38.537 0.54 31.65  ? 40  ARG   A CA  1 
ATOM   331  C  CA  B ARG   A 1 39  ? 41.040 -10.670 37.058 0.46 30.15  ? 40  ARG   A CA  1 
ATOM   332  C  C   A ARG   A 1 39  ? 40.597 -12.872 37.574 0.54 34.03  ? 40  ARG   A C   1 
ATOM   333  C  C   B ARG   A 1 39  ? 40.912 -12.093 36.478 0.46 32.26  ? 40  ARG   A C   1 
ATOM   334  O  O   A ARG   A 1 39  ? 41.627 -13.558 37.561 0.54 33.70  ? 40  ARG   A O   1 
ATOM   335  O  O   B ARG   A 1 39  ? 41.930 -12.615 36.017 0.46 32.86  ? 40  ARG   A O   1 
ATOM   336  C  CB  A ARG   A 1 39  ? 40.580 -12.176 39.996 0.54 32.55  ? 40  ARG   A CB  1 
ATOM   337  C  CB  B ARG   A 1 39  ? 41.692 -10.668 38.454 0.46 31.58  ? 40  ARG   A CB  1 
ATOM   338  C  CG  A ARG   A 1 39  ? 41.022 -11.110 40.986 0.54 38.24  ? 40  ARG   A CG  1 
ATOM   339  C  CG  B ARG   A 1 39  ? 42.208 -9.282  38.843 0.46 42.16  ? 40  ARG   A CG  1 
ATOM   340  C  CD  A ARG   A 1 39  ? 41.372 -11.727 42.326 0.54 40.27  ? 40  ARG   A CD  1 
ATOM   341  C  CD  B ARG   A 1 39  ? 43.221 -9.320  39.969 0.46 49.54  ? 40  ARG   A CD  1 
ATOM   342  N  NE  A ARG   A 1 39  ? 41.566 -10.718 43.364 0.54 42.05  ? 40  ARG   A NE  1 
ATOM   343  N  NE  B ARG   A 1 39  ? 43.638 -7.974  40.372 0.46 54.88  ? 40  ARG   A NE  1 
ATOM   344  C  CZ  A ARG   A 1 39  ? 42.739 -10.186 43.699 0.54 56.38  ? 40  ARG   A CZ  1 
ATOM   345  C  CZ  B ARG   A 1 39  ? 43.034 -7.246  41.308 0.46 65.74  ? 40  ARG   A CZ  1 
ATOM   346  N  NH1 A ARG   A 1 39  ? 42.810 -9.280  44.662 0.54 46.28  ? 40  ARG   A NH1 1 
ATOM   347  N  NH1 B ARG   A 1 39  ? 41.967 -7.718  41.942 0.46 49.38  ? 40  ARG   A NH1 1 
ATOM   348  N  NH2 A ARG   A 1 39  ? 43.847 -10.552 43.068 0.54 41.86  ? 40  ARG   A NH2 1 
ATOM   349  N  NH2 B ARG   A 1 39  ? 43.486 -6.037  41.610 0.46 53.56  ? 40  ARG   A NH2 1 
ATOM   350  N  N   A GLU   A 1 40  ? 39.530 -13.130 36.787 0.54 28.46  ? 41  GLU   A N   1 
ATOM   351  N  N   B GLU   A 1 40  ? 39.685 -12.689 36.422 0.46 27.78  ? 41  GLU   A N   1 
ATOM   352  C  CA  A GLU   A 1 40  ? 39.490 -14.258 35.855 0.54 27.20  ? 41  GLU   A CA  1 
ATOM   353  C  CA  B GLU   A 1 40  ? 39.449 -14.014 35.811 0.46 27.10  ? 41  GLU   A CA  1 
ATOM   354  C  C   A GLU   A 1 40  ? 39.762 -13.843 34.416 0.54 30.36  ? 41  GLU   A C   1 
ATOM   355  C  C   B GLU   A 1 40  ? 39.594 -13.866 34.293 0.46 30.33  ? 41  GLU   A C   1 
ATOM   356  O  O   A GLU   A 1 40  ? 39.441 -12.726 34.009 0.54 28.71  ? 41  GLU   A O   1 
ATOM   357  O  O   B GLU   A 1 40  ? 39.036 -12.930 33.719 0.46 28.68  ? 41  GLU   A O   1 
ATOM   358  C  CB  A GLU   A 1 40  ? 38.152 -15.023 35.959 0.54 28.13  ? 41  GLU   A CB  1 
ATOM   359  C  CB  B GLU   A 1 40  ? 38.059 -14.574 36.178 0.46 28.36  ? 41  GLU   A CB  1 
ATOM   360  C  CG  A GLU   A 1 40  ? 37.873 -15.586 37.346 0.54 42.29  ? 41  GLU   A CG  1 
ATOM   361  C  CG  B GLU   A 1 40  ? 37.976 -15.128 37.591 0.46 40.66  ? 41  GLU   A CG  1 
ATOM   362  C  CD  A GLU   A 1 40  ? 38.172 -17.064 37.505 0.54 78.54  ? 41  GLU   A CD  1 
ATOM   363  C  CD  B GLU   A 1 40  ? 38.175 -16.627 37.679 0.46 75.12  ? 41  GLU   A CD  1 
ATOM   364  O  OE1 A GLU   A 1 40  ? 37.399 -17.891 36.968 0.54 78.57  ? 41  GLU   A OE1 1 
ATOM   365  O  OE1 B GLU   A 1 40  ? 39.235 -17.053 38.193 0.46 76.92  ? 41  GLU   A OE1 1 
ATOM   366  O  OE2 A GLU   A 1 40  ? 39.178 -17.395 38.174 0.54 79.32  ? 41  GLU   A OE2 1 
ATOM   367  O  OE2 B GLU   A 1 40  ? 37.276 -17.375 37.231 0.46 75.58  ? 41  GLU   A OE2 1 
ATOM   368  N  N   . GLN   A 1 41  ? 40.348 -14.773 33.647 1.00 26.48  ? 42  GLN   A N   1 
ATOM   369  C  CA  . GLN   A 1 41  ? 40.681 -14.643 32.231 1.00 25.64  ? 42  GLN   A CA  1 
ATOM   370  C  C   . GLN   A 1 41  ? 40.053 -15.764 31.433 1.00 28.10  ? 42  GLN   A C   1 
ATOM   371  O  O   . GLN   A 1 41  ? 40.101 -16.916 31.874 1.00 28.01  ? 42  GLN   A O   1 
ATOM   372  C  CB  . GLN   A 1 41  ? 42.210 -14.658 32.060 1.00 28.27  ? 42  GLN   A CB  1 
ATOM   373  C  CG  . GLN   A 1 41  ? 42.915 -13.425 32.631 1.00 45.25  ? 42  GLN   A CG  1 
ATOM   374  C  CD  . GLN   A 1 41  ? 44.376 -13.322 32.254 1.00 63.38  ? 42  GLN   A CD  1 
ATOM   375  O  OE1 . GLN   A 1 41  ? 44.951 -14.172 31.557 1.00 56.40  ? 42  GLN   A OE1 1 
ATOM   376  N  NE2 . GLN   A 1 41  ? 45.012 -12.260 32.717 1.00 64.54  ? 42  GLN   A NE2 1 
ATOM   377  N  N   . PHE   A 1 42  ? 39.479 -15.438 30.255 1.00 22.88  ? 43  PHE   A N   1 
ATOM   378  C  CA  . PHE   A 1 42  ? 38.814 -16.416 29.378 1.00 22.63  ? 43  PHE   A CA  1 
ATOM   379  C  C   . PHE   A 1 42  ? 39.322 -16.247 27.963 1.00 27.01  ? 43  PHE   A C   1 
ATOM   380  O  O   . PHE   A 1 42  ? 39.165 -15.169 27.383 1.00 27.68  ? 43  PHE   A O   1 
ATOM   381  C  CB  . PHE   A 1 42  ? 37.287 -16.215 29.393 1.00 23.36  ? 43  PHE   A CB  1 
ATOM   382  C  CG  . PHE   A 1 42  ? 36.681 -16.358 30.768 1.00 25.03  ? 43  PHE   A CG  1 
ATOM   383  C  CD1 . PHE   A 1 42  ? 36.538 -15.254 31.602 1.00 26.75  ? 43  PHE   A CD1 1 
ATOM   384  C  CD2 . PHE   A 1 42  ? 36.230 -17.594 31.220 1.00 27.53  ? 43  PHE   A CD2 1 
ATOM   385  C  CE1 . PHE   A 1 42  ? 36.003 -15.392 32.888 1.00 28.30  ? 43  PHE   A CE1 1 
ATOM   386  C  CE2 . PHE   A 1 42  ? 35.685 -17.731 32.501 1.00 30.66  ? 43  PHE   A CE2 1 
ATOM   387  C  CZ  . PHE   A 1 42  ? 35.563 -16.627 33.322 1.00 28.53  ? 43  PHE   A CZ  1 
ATOM   388  N  N   . ARG   A 1 43  ? 39.967 -17.280 27.425 1.00 23.94  ? 44  ARG   A N   1 
ATOM   389  C  CA  . ARG   A 1 43  ? 40.469 -17.245 26.052 1.00 22.77  ? 44  ARG   A CA  1 
ATOM   390  C  C   . ARG   A 1 43  ? 39.331 -17.635 25.094 1.00 25.27  ? 44  ARG   A C   1 
ATOM   391  O  O   . ARG   A 1 43  ? 38.534 -18.547 25.385 1.00 23.93  ? 44  ARG   A O   1 
ATOM   392  C  CB  . ARG   A 1 43  ? 41.690 -18.173 25.882 1.00 24.24  ? 44  ARG   A CB  1 
ATOM   393  C  CG  . ARG   A 1 43  ? 42.919 -17.709 26.712 1.00 29.94  ? 44  ARG   A CG  1 
ATOM   394  C  CD  . ARG   A 1 43  ? 44.236 -18.160 26.086 1.00 36.15  ? 44  ARG   A CD  1 
ATOM   395  N  NE  . ARG   A 1 43  ? 44.271 -17.820 24.658 1.00 46.07  ? 44  ARG   A NE  1 
ATOM   396  C  CZ  . ARG   A 1 43  ? 44.788 -16.707 24.146 1.00 59.78  ? 44  ARG   A CZ  1 
ATOM   397  N  NH1 . ARG   A 1 43  ? 45.422 -15.843 24.924 1.00 52.61  ? 44  ARG   A NH1 1 
ATOM   398  N  NH2 . ARG   A 1 43  ? 44.722 -16.478 22.843 1.00 43.55  ? 44  ARG   A NH2 1 
ATOM   399  N  N   . ALA   A 1 44  ? 39.248 -16.967 23.935 1.00 22.13  ? 45  ALA   A N   1 
ATOM   400  C  CA  . ALA   A 1 44  ? 38.170 -17.276 22.975 1.00 21.75  ? 45  ALA   A CA  1 
ATOM   401  C  C   . ALA   A 1 44  ? 38.551 -16.866 21.570 1.00 23.11  ? 45  ALA   A C   1 
ATOM   402  O  O   . ALA   A 1 44  ? 39.648 -16.325 21.364 1.00 21.64  ? 45  ALA   A O   1 
ATOM   403  C  CB  . ALA   A 1 44  ? 36.865 -16.583 23.387 1.00 22.40  ? 45  ALA   A CB  1 
ATOM   404  N  N   . HIS   A 1 45  ? 37.655 -17.157 20.610 1.00 19.46  ? 46  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 45  ? 37.787 -16.749 19.219 1.00 18.38  ? 46  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 45  ? 36.908 -15.503 19.037 1.00 19.95  ? 46  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 45  ? 35.697 -15.563 19.310 1.00 19.54  ? 46  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 45  ? 37.310 -17.863 18.269 1.00 18.10  ? 46  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 45  ? 38.087 -19.131 18.438 1.00 20.71  ? 46  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 45  ? 37.621 -20.157 19.253 1.00 21.88  ? 46  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 45  ? 39.334 -19.450 17.999 1.00 22.42  ? 46  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 45  ? 38.566 -21.087 19.237 1.00 21.73  ? 46  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 45  ? 39.620 -20.705 18.500 1.00 21.80  ? 46  HIS   A NE2 1 
ATOM   414  N  N   . LYS   A 1 46  ? 37.505 -14.383 18.605 1.00 19.64  ? 47  LYS   A N   1 
ATOM   415  C  CA  . LYS   A 1 46  ? 36.754 -13.131 18.346 1.00 19.60  ? 47  LYS   A CA  1 
ATOM   416  C  C   . LYS   A 1 46  ? 35.517 -13.413 17.467 1.00 21.84  ? 47  LYS   A C   1 
ATOM   417  O  O   . LYS   A 1 46  ? 34.432 -12.921 17.770 1.00 19.47  ? 47  LYS   A O   1 
ATOM   418  C  CB  . LYS   A 1 46  ? 37.648 -12.103 17.620 1.00 21.87  ? 47  LYS   A CB  1 
ATOM   419  C  CG  . LYS   A 1 46  ? 38.678 -11.471 18.551 1.00 26.21  ? 47  LYS   A CG  1 
ATOM   420  C  CD  . LYS   A 1 46  ? 39.620 -10.599 17.750 1.00 25.25  ? 47  LYS   A CD  1 
ATOM   421  C  CE  . LYS   A 1 46  ? 40.716 -10.072 18.636 1.00 27.24  ? 47  LYS   A CE  1 
ATOM   422  N  NZ  . LYS   A 1 46  ? 41.672 -9.253  17.857 1.00 27.55  ? 47  LYS   A NZ  1 
ATOM   423  N  N   . THR   A 1 47  ? 35.673 -14.189 16.381 1.00 20.08  ? 48  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 47  ? 34.540 -14.440 15.484 1.00 19.70  ? 48  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 47  ? 33.365 -15.108 16.180 1.00 20.65  ? 48  THR   A C   1 
ATOM   426  O  O   . THR   A 1 47  ? 32.233 -14.716 15.922 1.00 19.91  ? 48  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 47  ? 34.964 -15.192 14.233 1.00 23.05  ? 48  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 47  ? 35.578 -16.410 14.634 1.00 25.57  ? 48  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 47  ? 35.873 -14.331 13.329 1.00 25.97  ? 48  THR   A CG2 1 
ATOM   430  N  N   . VAL   A 1 48  ? 33.618 -16.084 17.069 1.00 16.17  ? 49  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 48  ? 32.529 -16.761 17.802 1.00 16.29  ? 49  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 48  ? 31.862 -15.776 18.764 1.00 18.90  ? 49  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 48  ? 30.626 -15.717 18.819 1.00 17.49  ? 49  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 48  ? 33.036 -18.026 18.526 1.00 18.07  ? 49  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 48  ? 31.905 -18.644 19.378 1.00 18.34  ? 49  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 48  ? 33.537 -19.047 17.488 1.00 18.79  ? 49  VAL   A CG2 1 
ATOM   437  N  N   . LEU   A 1 49  ? 32.675 -14.959 19.474 1.00 18.15  ? 50  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 49  ? 32.109 -13.954 20.373 1.00 17.66  ? 50  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 49  ? 31.187 -12.982 19.621 1.00 20.64  ? 50  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 49  ? 30.062 -12.723 20.073 1.00 20.58  ? 50  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 49  ? 33.224 -13.173 21.094 1.00 17.15  ? 50  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 49  ? 34.204 -13.972 22.001 1.00 19.73  ? 50  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 49  ? 35.252 -13.016 22.618 1.00 20.02  ? 50  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 49  ? 33.445 -14.744 23.105 1.00 21.25  ? 50  LEU   A CD2 1 
ATOM   445  N  N   . MET   A 1 50  ? 31.626 -12.508 18.439 1.00 17.74  ? 51  MET   A N   1 
ATOM   446  C  CA  . MET   A 1 50  ? 30.830 -11.570 17.627 1.00 18.59  ? 51  MET   A CA  1 
ATOM   447  C  C   . MET   A 1 50  ? 29.544 -12.223 17.139 1.00 21.73  ? 51  MET   A C   1 
ATOM   448  O  O   . MET   A 1 50  ? 28.482 -11.599 17.171 1.00 21.72  ? 51  MET   A O   1 
ATOM   449  C  CB  . MET   A 1 50  ? 31.630 -11.109 16.412 1.00 20.42  ? 51  MET   A CB  1 
ATOM   450  C  CG  . MET   A 1 50  ? 32.874 -10.336 16.787 1.00 22.76  ? 51  MET   A CG  1 
ATOM   451  S  SD  . MET   A 1 50  ? 33.957 -10.236 15.344 1.00 26.03  ? 51  MET   A SD  1 
ATOM   452  C  CE  . MET   A 1 50  ? 33.207 -8.882  14.523 1.00 23.20  ? 51  MET   A CE  1 
ATOM   453  N  N   . ALA   A 1 51  ? 29.627 -13.504 16.737 1.00 18.62  ? 52  ALA   A N   1 
ATOM   454  C  CA  . ALA   A 1 51  ? 28.469 -14.245 16.229 1.00 18.59  ? 52  ALA   A CA  1 
ATOM   455  C  C   . ALA   A 1 51  ? 27.384 -14.452 17.311 1.00 21.91  ? 52  ALA   A C   1 
ATOM   456  O  O   . ALA   A 1 51  ? 26.224 -14.675 16.962 1.00 22.05  ? 52  ALA   A O   1 
ATOM   457  C  CB  . ALA   A 1 51  ? 28.925 -15.606 15.672 1.00 18.86  ? 52  ALA   A CB  1 
ATOM   458  N  N   . CYS   A 1 52  ? 27.775 -14.406 18.608 1.00 17.33  ? 53  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 52  ? 26.860 -14.660 19.730 1.00 18.82  ? 53  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 52  ? 26.395 -13.444 20.517 1.00 22.13  ? 53  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 52  ? 25.448 -13.588 21.293 1.00 20.48  ? 53  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 52  ? 27.513 -15.648 20.684 1.00 18.26  ? 53  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 52  ? 27.872 -17.258 19.950 1.00 20.07  ? 53  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 53  ? 27.137 -12.325 20.449 1.00 19.32  ? 54  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 53  ? 26.930 -11.184 21.340 1.00 19.00  ? 54  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 53  ? 26.939 -9.869  20.584 1.00 22.86  ? 54  SER   A C   1 
ATOM   467  O  O   . SER   A 1 53  ? 27.912 -9.568  19.880 1.00 21.38  ? 54  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 53  ? 28.070 -11.199 22.362 1.00 19.97  ? 54  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 53  ? 28.370 -9.954  22.974 1.00 23.00  ? 54  SER   A OG  1 
ATOM   470  N  N   . GLY   A 1 54  ? 25.893 -9.061  20.785 1.00 20.79  ? 55  GLY   A N   1 
ATOM   471  C  CA  . GLY   A 1 54  ? 25.834 -7.728  20.187 1.00 20.67  ? 55  GLY   A CA  1 
ATOM   472  C  C   . GLY   A 1 54  ? 26.960 -6.840  20.684 1.00 23.35  ? 55  GLY   A C   1 
ATOM   473  O  O   . GLY   A 1 54  ? 27.519 -6.033  19.916 1.00 22.69  ? 55  GLY   A O   1 
ATOM   474  N  N   . LEU   A 1 55  ? 27.347 -7.011  21.976 1.00 21.33  ? 56  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 55  ? 28.468 -6.210  22.515 1.00 21.10  ? 56  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 55  ? 29.812 -6.576  21.827 1.00 24.06  ? 56  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 55  ? 30.524 -5.679  21.371 1.00 21.54  ? 56  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 55  ? 28.565 -6.386  24.050 1.00 20.70  ? 56  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 55  ? 29.634 -5.493  24.721 1.00 26.48  ? 56  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 55  ? 29.208 -4.014  24.724 1.00 28.09  ? 56  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 55  ? 29.910 -5.965  26.123 1.00 26.06  ? 56  LEU   A CD2 1 
ATOM   482  N  N   . PHE   A 1 56  ? 30.134 -7.877  21.715 1.00 19.98  ? 57  PHE   A N   1 
ATOM   483  C  CA  . PHE   A 1 56  ? 31.393 -8.269  21.050 1.00 18.56  ? 57  PHE   A CA  1 
ATOM   484  C  C   . PHE   A 1 56  ? 31.377 -7.924  19.572 1.00 21.75  ? 57  PHE   A C   1 
ATOM   485  O  O   . PHE   A 1 56  ? 32.408 -7.527  19.036 1.00 20.79  ? 57  PHE   A O   1 
ATOM   486  C  CB  . PHE   A 1 56  ? 31.748 -9.740  21.296 1.00 19.60  ? 57  PHE   A CB  1 
ATOM   487  C  CG  . PHE   A 1 56  ? 32.186 -9.970  22.727 1.00 19.82  ? 57  PHE   A CG  1 
ATOM   488  C  CD1 . PHE   A 1 56  ? 33.249 -9.247  23.278 1.00 21.90  ? 57  PHE   A CD1 1 
ATOM   489  C  CD2 . PHE   A 1 56  ? 31.556 -10.926 23.518 1.00 20.54  ? 57  PHE   A CD2 1 
ATOM   490  C  CE1 . PHE   A 1 56  ? 33.621 -9.424  24.627 1.00 21.97  ? 57  PHE   A CE1 1 
ATOM   491  C  CE2 . PHE   A 1 56  ? 31.968 -11.144 24.846 1.00 22.92  ? 57  PHE   A CE2 1 
ATOM   492  C  CZ  . PHE   A 1 56  ? 32.997 -10.397 25.388 1.00 20.48  ? 57  PHE   A CZ  1 
ATOM   493  N  N   . TYR   A 1 57  ? 30.200 -8.000  18.928 1.00 20.08  ? 58  TYR   A N   1 
ATOM   494  C  CA  . TYR   A 1 57  ? 30.087 -7.617  17.505 1.00 20.94  ? 58  TYR   A CA  1 
ATOM   495  C  C   . TYR   A 1 57  ? 30.498 -6.132  17.361 1.00 24.44  ? 58  TYR   A C   1 
ATOM   496  O  O   . TYR   A 1 57  ? 31.286 -5.793  16.472 1.00 22.53  ? 58  TYR   A O   1 
ATOM   497  C  CB  . TYR   A 1 57  ? 28.641 -7.844  17.039 1.00 23.12  ? 58  TYR   A CB  1 
ATOM   498  C  CG  . TYR   A 1 57  ? 28.359 -7.321  15.654 1.00 27.30  ? 58  TYR   A CG  1 
ATOM   499  C  CD1 . TYR   A 1 57  ? 29.015 -7.842  14.544 1.00 28.60  ? 58  TYR   A CD1 1 
ATOM   500  C  CD2 . TYR   A 1 57  ? 27.433 -6.303  15.452 1.00 31.66  ? 58  TYR   A CD2 1 
ATOM   501  C  CE1 . TYR   A 1 57  ? 28.748 -7.366  13.257 1.00 29.99  ? 58  TYR   A CE1 1 
ATOM   502  C  CE2 . TYR   A 1 57  ? 27.163 -5.817  14.178 1.00 34.86  ? 58  TYR   A CE2 1 
ATOM   503  C  CZ  . TYR   A 1 57  ? 27.812 -6.361  13.084 1.00 41.47  ? 58  TYR   A CZ  1 
ATOM   504  O  OH  . TYR   A 1 57  ? 27.517 -5.879  11.842 1.00 46.70  ? 58  TYR   A OH  1 
ATOM   505  N  N   A SER   A 1 58  ? 29.964 -5.261  18.231 0.53 22.54  ? 59  SER   A N   1 
ATOM   506  N  N   B SER   A 1 58  ? 29.964 -5.263  18.236 0.47 22.51  ? 59  SER   A N   1 
ATOM   507  C  CA  A SER   A 1 58  ? 30.286 -3.829  18.220 0.53 23.13  ? 59  SER   A CA  1 
ATOM   508  C  CA  B SER   A 1 58  ? 30.283 -3.832  18.236 0.47 23.18  ? 59  SER   A CA  1 
ATOM   509  C  C   A SER   A 1 58  ? 31.777 -3.583  18.518 0.53 28.29  ? 59  SER   A C   1 
ATOM   510  C  C   B SER   A 1 58  ? 31.781 -3.606  18.499 0.47 28.19  ? 59  SER   A C   1 
ATOM   511  O  O   A SER   A 1 58  ? 32.412 -2.789  17.823 0.53 29.66  ? 59  SER   A O   1 
ATOM   512  O  O   B SER   A 1 58  ? 32.420 -2.846  17.770 0.47 29.38  ? 59  SER   A O   1 
ATOM   513  C  CB  A SER   A 1 58  ? 29.401 -3.080  19.212 0.53 25.60  ? 59  SER   A CB  1 
ATOM   514  C  CB  B SER   A 1 58  ? 29.449 -3.102  19.286 0.47 25.88  ? 59  SER   A CB  1 
ATOM   515  O  OG  A SER   A 1 58  ? 28.061 -3.045  18.747 0.53 28.45  ? 59  SER   A OG  1 
ATOM   516  O  OG  B SER   A 1 58  ? 29.763 -1.719  19.303 0.47 30.89  ? 59  SER   A OG  1 
ATOM   517  N  N   . ILE   A 1 59  ? 32.335 -4.285  19.524 1.00 24.58  ? 60  ILE   A N   1 
ATOM   518  C  CA  . ILE   A 1 59  ? 33.752 -4.165  19.919 1.00 23.81  ? 60  ILE   A CA  1 
ATOM   519  C  C   . ILE   A 1 59  ? 34.695 -4.546  18.780 1.00 26.74  ? 60  ILE   A C   1 
ATOM   520  O  O   . ILE   A 1 59  ? 35.576 -3.757  18.436 1.00 28.53  ? 60  ILE   A O   1 
ATOM   521  C  CB  . ILE   A 1 59  ? 34.089 -5.005  21.210 1.00 26.18  ? 60  ILE   A CB  1 
ATOM   522  C  CG1 . ILE   A 1 59  ? 33.337 -4.477  22.455 1.00 26.19  ? 60  ILE   A CG1 1 
ATOM   523  C  CG2 . ILE   A 1 59  ? 35.627 -5.052  21.468 1.00 25.11  ? 60  ILE   A CG2 1 
ATOM   524  C  CD1 . ILE   A 1 59  ? 33.429 -5.428  23.684 1.00 28.24  ? 60  ILE   A CD1 1 
ATOM   525  N  N   . PHE   A 1 60  ? 34.521 -5.745  18.204 1.00 22.35  ? 61  PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 60  ? 35.502 -6.188  17.231 1.00 22.18  ? 61  PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 60  ? 35.292 -5.647  15.823 1.00 26.52  ? 61  PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 60  ? 36.126 -5.930  14.958 1.00 28.07  ? 61  PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 60  ? 35.652 -7.717  17.255 1.00 22.04  ? 61  PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 60  ? 36.075 -8.198  18.634 1.00 22.62  ? 61  PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 60  ? 37.284 -7.788  19.194 1.00 25.63  ? 61  PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 60  ? 35.279 -9.081  19.355 1.00 23.00  ? 61  PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 60  ? 37.660 -8.212  20.483 1.00 26.47  ? 61  PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 60  ? 35.669 -9.527  20.629 1.00 25.91  ? 61  PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 60  ? 36.859 -9.095  21.180 1.00 25.02  ? 61  PHE   A CZ  1 
ATOM   536  N  N   . THR   A 1 61  ? 34.229 -4.850  15.586 1.00 24.49  ? 62  THR   A N   1 
ATOM   537  C  CA  . THR   A 1 61  ? 34.063 -4.165  14.291 1.00 24.78  ? 62  THR   A CA  1 
ATOM   538  C  C   . THR   A 1 61  ? 34.603 -2.741  14.416 1.00 30.66  ? 62  THR   A C   1 
ATOM   539  O  O   . THR   A 1 61  ? 34.668 -2.010  13.421 1.00 30.30  ? 62  THR   A O   1 
ATOM   540  C  CB  . THR   A 1 61  ? 32.630 -4.197  13.748 1.00 32.43  ? 62  THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 61  ? 31.729 -3.693  14.734 1.00 30.01  ? 62  THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 61  ? 32.210 -5.581  13.243 1.00 29.16  ? 62  THR   A CG2 1 
ATOM   543  N  N   . ASP   A 1 62  ? 35.016 -2.345  15.640 1.00 27.07  ? 63  ASP   A N   1 
ATOM   544  C  CA  . ASP   A 1 62  ? 35.618 -1.025  15.831 1.00 28.02  ? 63  ASP   A CA  1 
ATOM   545  C  C   . ASP   A 1 62  ? 37.032 -1.075  15.263 1.00 34.21  ? 63  ASP   A C   1 
ATOM   546  O  O   . ASP   A 1 62  ? 37.781 -1.982  15.609 1.00 32.48  ? 63  ASP   A O   1 
ATOM   547  C  CB  . ASP   A 1 62  ? 35.630 -0.632  17.318 1.00 28.96  ? 63  ASP   A CB  1 
ATOM   548  C  CG  . ASP   A 1 62  ? 36.354 0.672   17.546 1.00 39.52  ? 63  ASP   A CG  1 
ATOM   549  O  OD1 . ASP   A 1 62  ? 35.735 1.729   17.350 1.00 43.62  ? 63  ASP   A OD1 1 
ATOM   550  O  OD2 . ASP   A 1 62  ? 37.561 0.631   17.856 1.00 40.92  ? 63  ASP   A OD2 1 
ATOM   551  N  N   . GLN   A 1 63  ? 37.405 -0.071  14.434 1.00 36.02  ? 64  GLN   A N   1 
ATOM   552  C  CA  . GLN   A 1 63  ? 38.698 0.008   13.748 1.00 37.28  ? 64  GLN   A CA  1 
ATOM   553  C  C   . GLN   A 1 63  ? 39.916 -0.024  14.684 1.00 40.04  ? 64  GLN   A C   1 
ATOM   554  O  O   . GLN   A 1 63  ? 40.991 -0.421  14.227 1.00 41.76  ? 64  GLN   A O   1 
ATOM   555  C  CB  . GLN   A 1 63  ? 38.757 1.216   12.797 1.00 41.22  ? 64  GLN   A CB  1 
ATOM   556  C  CG  . GLN   A 1 63  ? 37.917 1.022   11.535 1.00 58.72  ? 64  GLN   A CG  1 
ATOM   557  N  N   . LEU   A 1 64  ? 39.769 0.389   15.971 1.00 32.37  ? 65  LEU   A N   1 
ATOM   558  C  CA  . LEU   A 1 64  ? 40.859 0.298   16.946 1.00 32.15  ? 65  LEU   A CA  1 
ATOM   559  C  C   . LEU   A 1 64  ? 40.756 -0.960  17.809 1.00 35.86  ? 65  LEU   A C   1 
ATOM   560  O  O   . LEU   A 1 64  ? 41.764 -1.628  18.029 1.00 37.23  ? 65  LEU   A O   1 
ATOM   561  C  CB  . LEU   A 1 64  ? 40.909 1.534   17.884 1.00 33.29  ? 65  LEU   A CB  1 
ATOM   562  C  CG  . LEU   A 1 64  ? 41.501 2.816   17.331 1.00 40.09  ? 65  LEU   A CG  1 
ATOM   563  C  CD1 . LEU   A 1 64  ? 41.404 3.927   18.363 1.00 40.40  ? 65  LEU   A CD1 1 
ATOM   564  C  CD2 . LEU   A 1 64  ? 42.964 2.644   16.905 1.00 45.31  ? 65  LEU   A CD2 1 
ATOM   565  N  N   . LYS   A 1 65  ? 39.559 -1.262  18.351 1.00 28.84  ? 66  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 65  ? 39.407 -2.389  19.269 1.00 27.89  ? 66  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 65  ? 39.533 -3.745  18.574 1.00 32.93  ? 66  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 65  ? 39.904 -4.714  19.234 1.00 32.38  ? 66  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 65  ? 38.109 -2.294  20.098 1.00 28.18  ? 66  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 65  ? 37.995 -1.018  20.952 1.00 29.08  ? 66  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 65  ? 36.710 -1.102  21.788 1.00 27.03  ? 66  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 65  ? 36.359 0.205   22.466 1.00 34.03  ? 66  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 65  ? 35.890 1.247   21.523 1.00 33.46  ? 66  LYS   A NZ  1 
ATOM   574  N  N   . CYS   A 1 66  ? 39.289 -3.805  17.240 1.00 31.93  ? 67  CYS   A N   1 
ATOM   575  C  CA  . CYS   A 1 66  ? 39.420 -5.058  16.462 1.00 31.51  ? 67  CYS   A CA  1 
ATOM   576  C  C   . CYS   A 1 66  ? 40.809 -5.686  16.624 1.00 36.19  ? 67  CYS   A C   1 
ATOM   577  O  O   . CYS   A 1 66  ? 40.943 -6.905  16.475 1.00 36.59  ? 67  CYS   A O   1 
ATOM   578  C  CB  . CYS   A 1 66  ? 39.082 -4.841  14.986 1.00 33.48  ? 67  CYS   A CB  1 
ATOM   579  S  SG  . CYS   A 1 66  ? 40.229 -3.744  14.097 1.00 39.52  ? 67  CYS   A SG  1 
ATOM   580  N  N   . ASN   A 1 67  ? 41.838 -4.842  16.901 1.00 31.95  ? 68  ASN   A N   1 
ATOM   581  C  CA  . ASN   A 1 67  ? 43.239 -5.239  17.021 1.00 32.57  ? 68  ASN   A CA  1 
ATOM   582  C  C   . ASN   A 1 67  ? 43.717 -5.531  18.445 1.00 35.80  ? 68  ASN   A C   1 
ATOM   583  O  O   . ASN   A 1 67  ? 44.884 -5.894  18.638 1.00 35.03  ? 68  ASN   A O   1 
ATOM   584  C  CB  . ASN   A 1 67  ? 44.140 -4.189  16.338 1.00 35.10  ? 68  ASN   A CB  1 
ATOM   585  C  CG  . ASN   A 1 67  ? 43.912 -4.155  14.834 1.00 48.92  ? 68  ASN   A CG  1 
ATOM   586  O  OD1 . ASN   A 1 67  ? 43.856 -3.091  14.219 1.00 48.71  ? 68  ASN   A OD1 1 
ATOM   587  N  ND2 . ASN   A 1 67  ? 43.716 -5.317  14.211 1.00 40.36  ? 68  ASN   A ND2 1 
ATOM   588  N  N   . LEU   A 1 68  ? 42.830 -5.389  19.443 1.00 33.16  ? 69  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 68  ? 43.220 -5.648  20.824 1.00 32.07  ? 69  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 68  ? 43.225 -7.143  21.092 1.00 34.44  ? 69  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 68  ? 42.342 -7.855  20.592 1.00 32.91  ? 69  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 68  ? 42.270 -4.937  21.810 1.00 32.11  ? 69  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 68  ? 42.257 -3.398  21.752 1.00 36.81  ? 69  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 68  ? 41.165 -2.840  22.655 1.00 36.98  ? 69  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 68  ? 43.621 -2.808  22.138 1.00 39.00  ? 69  LEU   A CD2 1 
ATOM   596  N  N   A SER   A 1 69  ? 44.206 -7.621  21.876 0.51 31.61  ? 70  SER   A N   1 
ATOM   597  N  N   B SER   A 1 69  ? 44.208 -7.612  21.881 0.49 31.57  ? 70  SER   A N   1 
ATOM   598  C  CA  A SER   A 1 69  ? 44.299 -9.041  22.241 0.51 31.16  ? 70  SER   A CA  1 
ATOM   599  C  CA  B SER   A 1 69  ? 44.341 -9.024  22.262 0.49 31.16  ? 70  SER   A CA  1 
ATOM   600  C  C   A SER   A 1 69  ? 43.696 -9.285  23.636 0.51 31.95  ? 70  SER   A C   1 
ATOM   601  C  C   B SER   A 1 69  ? 43.721 -9.279  23.645 0.49 31.99  ? 70  SER   A C   1 
ATOM   602  O  O   A SER   A 1 69  ? 43.527 -10.433 24.043 0.51 29.90  ? 70  SER   A O   1 
ATOM   603  O  O   B SER   A 1 69  ? 43.567 -10.430 24.052 0.49 29.95  ? 70  SER   A O   1 
ATOM   604  C  CB  A SER   A 1 69  ? 45.749 -9.517  22.190 0.51 36.05  ? 70  SER   A CB  1 
ATOM   605  C  CB  B SER   A 1 69  ? 45.809 -9.437  22.259 0.49 35.97  ? 70  SER   A CB  1 
ATOM   606  O  OG  A SER   A 1 69  ? 46.573 -8.754  23.055 0.51 44.71  ? 70  SER   A OG  1 
ATOM   607  O  OG  B SER   A 1 69  ? 46.323 -9.423  20.938 0.49 43.85  ? 70  SER   A OG  1 
ATOM   608  N  N   . VAL   A 1 70  ? 43.400 -8.193  24.373 1.00 28.67  ? 71  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 70  ? 42.808 -8.231  25.720 1.00 27.90  ? 71  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 70  ? 41.625 -7.257  25.770 1.00 29.14  ? 71  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 70  ? 41.769 -6.086  25.379 1.00 29.09  ? 71  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 70  ? 43.848 -7.900  26.841 1.00 33.03  ? 71  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 70  ? 43.197 -7.884  28.234 1.00 33.44  ? 71  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 70  ? 45.045 -8.859  26.812 1.00 33.57  ? 71  VAL   A CG2 1 
ATOM   615  N  N   . ILE   A 1 71  ? 40.476 -7.741  26.269 1.00 22.33  ? 72  ILE   A N   1 
ATOM   616  C  CA  . ILE   A 1 71  ? 39.275 -6.932  26.472 1.00 22.45  ? 72  ILE   A CA  1 
ATOM   617  C  C   . ILE   A 1 71  ? 38.871 -7.054  27.937 1.00 26.31  ? 72  ILE   A C   1 
ATOM   618  O  O   . ILE   A 1 71  ? 38.618 -8.167  28.409 1.00 25.61  ? 72  ILE   A O   1 
ATOM   619  C  CB  . ILE   A 1 71  ? 38.108 -7.292  25.503 1.00 23.88  ? 72  ILE   A CB  1 
ATOM   620  C  CG1 . ILE   A 1 71  ? 38.511 -7.101  23.988 1.00 25.43  ? 72  ILE   A CG1 1 
ATOM   621  C  CG2 . ILE   A 1 71  ? 36.797 -6.550  25.856 1.00 25.10  ? 72  ILE   A CG2 1 
ATOM   622  C  CD1 . ILE   A 1 71  ? 38.867 -5.651  23.526 1.00 29.48  ? 72  ILE   A CD1 1 
ATOM   623  N  N   . ASN   A 1 72  ? 38.742 -5.912  28.628 1.00 24.29  ? 73  ASN   A N   1 
ATOM   624  C  CA  . ASN   A 1 72  ? 38.352 -5.862  30.025 1.00 24.60  ? 73  ASN   A CA  1 
ATOM   625  C  C   . ASN   A 1 72  ? 36.879 -5.537  30.147 1.00 26.98  ? 73  ASN   A C   1 
ATOM   626  O  O   . ASN   A 1 72  ? 36.445 -4.468  29.711 1.00 25.68  ? 73  ASN   A O   1 
ATOM   627  C  CB  . ASN   A 1 72  ? 39.172 -4.807  30.796 1.00 28.79  ? 73  ASN   A CB  1 
ATOM   628  C  CG  . ASN   A 1 72  ? 40.651 -4.992  30.712 1.00 45.60  ? 73  ASN   A CG  1 
ATOM   629  O  OD1 . ASN   A 1 72  ? 41.187 -6.036  31.066 1.00 35.52  ? 73  ASN   A OD1 1 
ATOM   630  N  ND2 . ASN   A 1 72  ? 41.348 -3.965  30.265 1.00 41.45  ? 73  ASN   A ND2 1 
ATOM   631  N  N   . LEU   A 1 73  ? 36.108 -6.443  30.750 1.00 22.49  ? 74  LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 73  ? 34.690 -6.181  30.944 1.00 21.41  ? 74  LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 73  ? 34.450 -5.286  32.163 1.00 26.31  ? 74  LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 73  ? 35.322 -5.140  33.034 1.00 26.16  ? 74  LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 73  ? 33.885 -7.486  31.081 1.00 20.47  ? 74  LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 73  ? 33.952 -8.497  29.915 1.00 24.09  ? 74  LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 73  ? 32.857 -9.542  30.073 1.00 24.33  ? 74  LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 73  ? 33.874 -7.814  28.532 1.00 22.83  ? 74  LEU   A CD2 1 
ATOM   639  N  N   . ASP   A 1 74  ? 33.252 -4.707  32.231 1.00 23.47  ? 75  ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 74  ? 32.829 -3.844  33.337 1.00 24.41  ? 75  ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 74  ? 33.060 -4.591  34.671 1.00 28.42  ? 75  ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 74  ? 32.742 -5.784  34.740 1.00 27.69  ? 75  ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 74  ? 31.346 -3.506  33.153 1.00 26.11  ? 75  ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 74  ? 30.803 -2.480  34.130 1.00 35.22  ? 75  ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 74  ? 30.683 -2.807  35.330 1.00 35.99  ? 75  ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 74  ? 30.479 -1.361  33.694 1.00 34.97  ? 75  ASP   A OD2 1 
ATOM   647  N  N   . PRO   A 1 75  ? 33.609 -3.931  35.717 1.00 28.77  ? 76  PRO   A N   1 
ATOM   648  C  CA  . PRO   A 1 75  ? 33.855 -4.647  36.995 1.00 29.89  ? 76  PRO   A CA  1 
ATOM   649  C  C   . PRO   A 1 75  ? 32.622 -5.242  37.669 1.00 33.16  ? 76  PRO   A C   1 
ATOM   650  O  O   . PRO   A 1 75  ? 32.771 -6.111  38.529 1.00 33.59  ? 76  PRO   A O   1 
ATOM   651  C  CB  . PRO   A 1 75  ? 34.543 -3.603  37.889 1.00 32.87  ? 76  PRO   A CB  1 
ATOM   652  C  CG  . PRO   A 1 75  ? 34.285 -2.286  37.245 1.00 37.75  ? 76  PRO   A CG  1 
ATOM   653  C  CD  . PRO   A 1 75  ? 34.072 -2.524  35.780 1.00 31.47  ? 76  PRO   A CD  1 
ATOM   654  N  N   . GLU   A 1 76  ? 31.411 -4.808  37.282 1.00 29.88  ? 77  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 76  ? 30.167 -5.336  37.855 1.00 31.70  ? 77  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 76  ? 29.885 -6.752  37.315 1.00 31.39  ? 77  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 76  ? 29.069 -7.473  37.887 1.00 30.39  ? 77  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 76  ? 28.980 -4.406  37.510 1.00 34.41  ? 77  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 76  ? 27.820 -4.455  38.488 1.00 54.55  ? 77  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 76  ? 27.989 -3.559  39.701 1.00 82.43  ? 77  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 76  ? 28.006 -2.319  39.527 1.00 82.98  ? 77  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 76  ? 28.104 -4.098  40.827 1.00 75.98  ? 77  GLU   A OE2 1 
ATOM   663  N  N   . ILE   A 1 77  ? 30.536 -7.143  36.211 1.00 26.08  ? 78  ILE   A N   1 
ATOM   664  C  CA  . ILE   A 1 77  ? 30.269 -8.457  35.612 1.00 24.33  ? 78  ILE   A CA  1 
ATOM   665  C  C   . ILE   A 1 77  ? 30.843 -9.593  36.433 1.00 28.23  ? 78  ILE   A C   1 
ATOM   666  O  O   . ILE   A 1 77  ? 32.019 -9.585  36.797 1.00 28.13  ? 78  ILE   A O   1 
ATOM   667  C  CB  . ILE   A 1 77  ? 30.728 -8.494  34.131 1.00 26.51  ? 78  ILE   A CB  1 
ATOM   668  C  CG1 . ILE   A 1 77  ? 30.046 -7.356  33.324 1.00 27.55  ? 78  ILE   A CG1 1 
ATOM   669  C  CG2 . ILE   A 1 77  ? 30.487 -9.877  33.495 1.00 25.08  ? 78  ILE   A CG2 1 
ATOM   670  C  CD1 . ILE   A 1 77  ? 28.464 -7.327  33.332 1.00 31.66  ? 78  ILE   A CD1 1 
ATOM   671  N  N   . ASN   A 1 78  ? 29.996 -10.579 36.682 1.00 28.38  ? 79  ASN   A N   1 
ATOM   672  C  CA  . ASN   A 1 78  ? 30.307 -11.773 37.457 1.00 29.14  ? 79  ASN   A CA  1 
ATOM   673  C  C   . ASN   A 1 78  ? 31.069 -12.800 36.597 1.00 29.43  ? 79  ASN   A C   1 
ATOM   674  O  O   . ASN   A 1 78  ? 30.559 -13.182 35.546 1.00 27.19  ? 79  ASN   A O   1 
ATOM   675  C  CB  . ASN   A 1 78  ? 29.000 -12.372 38.005 1.00 31.77  ? 79  ASN   A CB  1 
ATOM   676  C  CG  . ASN   A 1 78  ? 29.205 -13.645 38.772 1.00 44.11  ? 79  ASN   A CG  1 
ATOM   677  O  OD1 . ASN   A 1 78  ? 28.897 -14.726 38.283 1.00 35.56  ? 79  ASN   A OD1 1 
ATOM   678  N  ND2 . ASN   A 1 78  ? 29.732 -13.544 39.992 1.00 37.74  ? 79  ASN   A ND2 1 
ATOM   679  N  N   . PRO   A 1 79  ? 32.281 -13.259 37.015 1.00 27.72  ? 80  PRO   A N   1 
ATOM   680  C  CA  . PRO   A 1 79  ? 33.029 -14.239 36.197 1.00 26.83  ? 80  PRO   A CA  1 
ATOM   681  C  C   . PRO   A 1 79  ? 32.281 -15.557 35.946 1.00 29.24  ? 80  PRO   A C   1 
ATOM   682  O  O   . PRO   A 1 79  ? 32.381 -16.109 34.844 1.00 27.63  ? 80  PRO   A O   1 
ATOM   683  C  CB  . PRO   A 1 79  ? 34.318 -14.459 36.997 1.00 30.22  ? 80  PRO   A CB  1 
ATOM   684  C  CG  . PRO   A 1 79  ? 34.446 -13.235 37.871 1.00 35.10  ? 80  PRO   A CG  1 
ATOM   685  C  CD  . PRO   A 1 79  ? 33.044 -12.879 38.224 1.00 30.93  ? 80  PRO   A CD  1 
ATOM   686  N  N   . GLU   A 1 80  ? 31.514 -16.051 36.944 1.00 26.35  ? 81  GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 80  ? 30.752 -17.291 36.752 1.00 25.83  ? 81  GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 80  ? 29.657 -17.102 35.674 1.00 27.70  ? 81  GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 80  ? 29.529 -17.948 34.797 1.00 25.90  ? 81  GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 80  ? 30.171 -17.825 38.070 1.00 28.09  ? 81  GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 80  ? 29.556 -19.202 37.858 1.00 34.83  ? 81  GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 80  ? 28.724 -19.801 38.976 1.00 56.79  ? 81  GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 80  ? 28.720 -21.047 39.088 1.00 53.74  ? 81  GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 80  ? 28.061 -19.044 39.719 1.00 49.39  ? 81  GLU   A OE2 1 
ATOM   695  N  N   . GLY   A 1 81  ? 28.910 -15.991 35.741 1.00 25.18  ? 82  GLY   A N   1 
ATOM   696  C  CA  . GLY   A 1 81  ? 27.900 -15.667 34.734 1.00 24.57  ? 82  GLY   A CA  1 
ATOM   697  C  C   . GLY   A 1 81  ? 28.516 -15.593 33.344 1.00 25.77  ? 82  GLY   A C   1 
ATOM   698  O  O   . GLY   A 1 81  ? 27.951 -16.114 32.367 1.00 24.00  ? 82  GLY   A O   1 
ATOM   699  N  N   . PHE   A 1 82  ? 29.706 -14.967 33.250 1.00 21.72  ? 83  PHE   A N   1 
ATOM   700  C  CA  . PHE   A 1 82  ? 30.403 -14.896 31.954 1.00 19.81  ? 83  PHE   A CA  1 
ATOM   701  C  C   . PHE   A 1 82  ? 30.777 -16.312 31.482 1.00 23.09  ? 83  PHE   A C   1 
ATOM   702  O  O   . PHE   A 1 82  ? 30.531 -16.659 30.323 1.00 21.29  ? 83  PHE   A O   1 
ATOM   703  C  CB  . PHE   A 1 82  ? 31.663 -13.977 32.027 1.00 21.15  ? 83  PHE   A CB  1 
ATOM   704  C  CG  . PHE   A 1 82  ? 32.273 -13.839 30.651 1.00 21.18  ? 83  PHE   A CG  1 
ATOM   705  C  CD1 . PHE   A 1 82  ? 31.688 -13.009 29.694 1.00 23.57  ? 83  PHE   A CD1 1 
ATOM   706  C  CD2 . PHE   A 1 82  ? 33.322 -14.665 30.252 1.00 22.31  ? 83  PHE   A CD2 1 
ATOM   707  C  CE1 . PHE   A 1 82  ? 32.187 -12.958 28.387 1.00 24.20  ? 83  PHE   A CE1 1 
ATOM   708  C  CE2 . PHE   A 1 82  ? 33.825 -14.609 28.950 1.00 23.73  ? 83  PHE   A CE2 1 
ATOM   709  C  CZ  . PHE   A 1 82  ? 33.244 -13.772 28.018 1.00 22.74  ? 83  PHE   A CZ  1 
ATOM   710  N  N   . CYS   A 1 83  ? 31.362 -17.122 32.371 1.00 23.81  ? 84  CYS   A N   1 
ATOM   711  C  CA  . CYS   A 1 83  ? 31.750 -18.500 32.052 1.00 24.89  ? 84  CYS   A CA  1 
ATOM   712  C  C   . CYS   A 1 83  ? 30.569 -19.333 31.490 1.00 26.05  ? 84  CYS   A C   1 
ATOM   713  O  O   . CYS   A 1 83  ? 30.721 -20.026 30.467 1.00 23.93  ? 84  CYS   A O   1 
ATOM   714  C  CB  . CYS   A 1 83  ? 32.374 -19.170 33.271 1.00 27.81  ? 84  CYS   A CB  1 
ATOM   715  S  SG  . CYS   A 1 83  ? 33.090 -20.796 32.912 1.00 33.15  ? 84  CYS   A SG  1 
ATOM   716  N  N   . ILE   A 1 84  ? 29.388 -19.222 32.142 1.00 22.85  ? 85  ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 84  ? 28.165 -19.929 31.742 1.00 21.52  ? 85  ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 84  ? 27.774 -19.482 30.335 1.00 21.71  ? 85  ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 84  ? 27.421 -20.312 29.481 1.00 21.62  ? 85  ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 84  ? 27.041 -19.676 32.780 1.00 24.80  ? 85  ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 84  ? 27.356 -20.471 34.093 1.00 25.61  ? 85  ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 84  ? 25.645 -20.036 32.203 1.00 25.31  ? 85  ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 84  ? 26.545 -20.039 35.307 1.00 32.58  ? 85  ILE   A CD1 1 
ATOM   724  N  N   . LEU   A 1 85  ? 27.836 -18.173 30.106 1.00 18.51  ? 86  LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 85  ? 27.491 -17.632 28.780 1.00 18.45  ? 86  LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 85  ? 28.495 -17.992 27.702 1.00 22.55  ? 86  LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 85  ? 28.082 -18.281 26.573 1.00 20.83  ? 86  LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 85  ? 27.243 -16.130 28.864 1.00 18.88  ? 86  LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 85  ? 25.946 -15.768 29.634 1.00 24.20  ? 86  LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 85  ? 25.847 -14.285 29.768 1.00 25.14  ? 86  LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 85  ? 24.671 -16.319 28.927 1.00 25.22  ? 86  LEU   A CD2 1 
ATOM   732  N  N   . LEU   A 1 86  ? 29.814 -18.007 28.030 1.00 19.08  ? 87  LEU   A N   1 
ATOM   733  C  CA  . LEU   A 1 86  ? 30.838 -18.417 27.066 1.00 19.14  ? 87  LEU   A CA  1 
ATOM   734  C  C   . LEU   A 1 86  ? 30.618 -19.888 26.662 1.00 21.64  ? 87  LEU   A C   1 
ATOM   735  O  O   . LEU   A 1 86  ? 30.631 -20.228 25.472 1.00 19.34  ? 87  LEU   A O   1 
ATOM   736  C  CB  . LEU   A 1 86  ? 32.236 -18.186 27.661 1.00 19.17  ? 87  LEU   A CB  1 
ATOM   737  C  CG  . LEU   A 1 86  ? 33.420 -18.486 26.716 1.00 23.28  ? 87  LEU   A CG  1 
ATOM   738  C  CD1 . LEU   A 1 86  ? 33.390 -17.588 25.467 1.00 22.52  ? 87  LEU   A CD1 1 
ATOM   739  C  CD2 . LEU   A 1 86  ? 34.767 -18.351 27.466 1.00 24.76  ? 87  LEU   A CD2 1 
ATOM   740  N  N   . ASP   A 1 87  ? 30.350 -20.741 27.643 1.00 19.48  ? 88  ASP   A N   1 
ATOM   741  C  CA  . ASP   A 1 87  ? 30.017 -22.134 27.363 1.00 19.45  ? 88  ASP   A CA  1 
ATOM   742  C  C   . ASP   A 1 87  ? 28.786 -22.221 26.444 1.00 22.34  ? 88  ASP   A C   1 
ATOM   743  O  O   . ASP   A 1 87  ? 28.799 -23.004 25.499 1.00 21.69  ? 88  ASP   A O   1 
ATOM   744  C  CB  . ASP   A 1 87  ? 29.740 -22.868 28.676 1.00 22.56  ? 88  ASP   A CB  1 
ATOM   745  C  CG  . ASP   A 1 87  ? 30.974 -23.216 29.486 1.00 34.90  ? 88  ASP   A CG  1 
ATOM   746  O  OD1 . ASP   A 1 87  ? 32.100 -23.134 28.930 1.00 35.09  ? 88  ASP   A OD1 1 
ATOM   747  O  OD2 . ASP   A 1 87  ? 30.816 -23.586 30.672 1.00 34.84  ? 88  ASP   A OD2 1 
ATOM   748  N  N   . PHE   A 1 88  ? 27.724 -21.439 26.722 1.00 20.00  ? 89  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 88  ? 26.528 -21.422 25.861 1.00 18.31  ? 89  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 88  ? 26.900 -21.025 24.426 1.00 19.15  ? 89  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 88  ? 26.393 -21.615 23.467 1.00 18.60  ? 89  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 88  ? 25.459 -20.458 26.407 1.00 19.25  ? 89  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 88  ? 24.363 -20.172 25.410 1.00 19.01  ? 89  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 88  ? 23.381 -21.123 25.137 1.00 21.30  ? 89  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 88  ? 24.350 -18.982 24.687 1.00 21.75  ? 89  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 88  ? 22.404 -20.878 24.172 1.00 21.45  ? 89  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 88  ? 23.360 -18.736 23.725 1.00 23.78  ? 89  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 88  ? 22.387 -19.677 23.489 1.00 21.70  ? 89  PHE   A CZ  1 
ATOM   759  N  N   . MET   A 1 89  ? 27.738 -19.987 24.267 1.00 15.97  ? 90  MET   A N   1 
ATOM   760  C  CA  . MET   A 1 89  ? 28.140 -19.563 22.908 1.00 15.53  ? 90  MET   A CA  1 
ATOM   761  C  C   . MET   A 1 89  ? 28.688 -20.712 22.080 1.00 19.28  ? 90  MET   A C   1 
ATOM   762  O  O   . MET   A 1 89  ? 28.370 -20.818 20.894 1.00 18.52  ? 90  MET   A O   1 
ATOM   763  C  CB  . MET   A 1 89  ? 29.230 -18.482 23.003 1.00 16.46  ? 90  MET   A CB  1 
ATOM   764  C  CG  . MET   A 1 89  ? 28.705 -17.172 23.601 1.00 17.68  ? 90  MET   A CG  1 
ATOM   765  S  SD  . MET   A 1 89  ? 30.055 -15.937 23.505 1.00 21.69  ? 90  MET   A SD  1 
ATOM   766  C  CE  . MET   A 1 89  ? 29.382 -14.629 24.645 1.00 22.16  ? 90  MET   A CE  1 
ATOM   767  N  N   . TYR   A 1 90  ? 29.557 -21.534 22.691 1.00 16.83  ? 91  TYR   A N   1 
ATOM   768  C  CA  . TYR   A 1 90  ? 30.227 -22.623 21.993 1.00 16.73  ? 91  TYR   A CA  1 
ATOM   769  C  C   . TYR   A 1 90  ? 29.488 -23.934 21.988 1.00 20.98  ? 91  TYR   A C   1 
ATOM   770  O  O   . TYR   A 1 90  ? 29.967 -24.886 21.363 1.00 19.70  ? 91  TYR   A O   1 
ATOM   771  C  CB  . TYR   A 1 90  ? 31.615 -22.845 22.598 1.00 18.17  ? 91  TYR   A CB  1 
ATOM   772  C  CG  . TYR   A 1 90  ? 32.651 -21.845 22.123 1.00 19.28  ? 91  TYR   A CG  1 
ATOM   773  C  CD1 . TYR   A 1 90  ? 32.787 -20.599 22.739 1.00 21.34  ? 91  TYR   A CD1 1 
ATOM   774  C  CD2 . TYR   A 1 90  ? 33.509 -22.148 21.060 1.00 19.82  ? 91  TYR   A CD2 1 
ATOM   775  C  CE1 . TYR   A 1 90  ? 33.760 -19.682 22.316 1.00 21.15  ? 91  TYR   A CE1 1 
ATOM   776  C  CE2 . TYR   A 1 90  ? 34.523 -21.265 20.669 1.00 20.73  ? 91  TYR   A CE2 1 
ATOM   777  C  CZ  . TYR   A 1 90  ? 34.614 -20.017 21.265 1.00 23.63  ? 91  TYR   A CZ  1 
ATOM   778  O  OH  . TYR   A 1 90  ? 35.646 -19.189 20.874 1.00 21.12  ? 91  TYR   A OH  1 
ATOM   779  N  N   . THR   A 1 91  ? 28.335 -24.016 22.671 1.00 17.59  ? 92  THR   A N   1 
ATOM   780  C  CA  . THR   A 1 91  ? 27.638 -25.318 22.751 1.00 17.90  ? 92  THR   A CA  1 
ATOM   781  C  C   . THR   A 1 91  ? 26.129 -25.323 22.516 1.00 20.26  ? 92  THR   A C   1 
ATOM   782  O  O   . THR   A 1 91  ? 25.564 -26.412 22.312 1.00 19.75  ? 92  THR   A O   1 
ATOM   783  C  CB  . THR   A 1 91  ? 27.837 -25.979 24.152 1.00 21.31  ? 92  THR   A CB  1 
ATOM   784  O  OG1 . THR   A 1 91  ? 27.144 -25.220 25.146 1.00 21.28  ? 92  THR   A OG1 1 
ATOM   785  C  CG2 . THR   A 1 91  ? 29.318 -26.189 24.545 1.00 20.81  ? 92  THR   A CG2 1 
ATOM   786  N  N   A SER   A 1 92  ? 25.477 -24.153 22.592 0.67 17.84  ? 93  SER   A N   1 
ATOM   787  N  N   B SER   A 1 92  ? 25.483 -24.146 22.621 0.33 17.33  ? 93  SER   A N   1 
ATOM   788  C  CA  A SER   A 1 92  ? 24.002 -23.954 22.552 0.67 17.92  ? 93  SER   A CA  1 
ATOM   789  C  CA  B SER   A 1 92  ? 24.022 -23.935 22.561 0.33 17.42  ? 93  SER   A CA  1 
ATOM   790  C  C   A SER   A 1 92  ? 23.352 -24.344 23.895 0.67 20.42  ? 93  SER   A C   1 
ATOM   791  C  C   B SER   A 1 92  ? 23.338 -24.438 23.855 0.33 21.10  ? 93  SER   A C   1 
ATOM   792  O  O   A SER   A 1 92  ? 22.150 -24.141 24.056 0.67 19.46  ? 93  SER   A O   1 
ATOM   793  O  O   B SER   A 1 92  ? 22.109 -24.452 23.929 0.33 20.84  ? 93  SER   A O   1 
ATOM   794  C  CB  A SER   A 1 92  ? 23.320 -24.746 21.431 0.67 19.73  ? 93  SER   A CB  1 
ATOM   795  C  CB  B SER   A 1 92  ? 23.395 -24.573 21.316 0.33 19.83  ? 93  SER   A CB  1 
ATOM   796  O  OG  A SER   A 1 92  ? 23.931 -24.551 20.170 0.67 16.48  ? 93  SER   A OG  1 
ATOM   797  O  OG  B SER   A 1 92  ? 23.073 -25.941 21.513 0.33 22.34  ? 93  SER   A OG  1 
ATOM   798  N  N   A ARG   A 1 93  ? 24.141 -24.859 24.862 0.67 17.87  ? 94  ARG   A N   1 
ATOM   799  N  N   B ARG   A 1 93  ? 24.141 -24.817 24.877 0.33 18.33  ? 94  ARG   A N   1 
ATOM   800  C  CA  A ARG   A 1 93  ? 23.602 -25.291 26.159 0.67 18.54  ? 94  ARG   A CA  1 
ATOM   801  C  CA  B ARG   A 1 93  ? 23.660 -25.337 26.164 0.33 19.12  ? 94  ARG   A CA  1 
ATOM   802  C  C   A ARG   A 1 93  ? 23.837 -24.255 27.222 0.67 22.42  ? 94  ARG   A C   1 
ATOM   803  C  C   B ARG   A 1 93  ? 23.860 -24.297 27.254 0.33 22.89  ? 94  ARG   A C   1 
ATOM   804  O  O   A ARG   A 1 93  ? 24.963 -23.766 27.395 0.67 20.30  ? 94  ARG   A O   1 
ATOM   805  O  O   B ARG   A 1 93  ? 24.983 -23.820 27.455 0.33 21.57  ? 94  ARG   A O   1 
ATOM   806  C  CB  A ARG   A 1 93  ? 24.177 -26.647 26.601 0.67 21.06  ? 94  ARG   A CB  1 
ATOM   807  C  CB  B ARG   A 1 93  ? 24.375 -26.658 26.537 0.33 21.04  ? 94  ARG   A CB  1 
ATOM   808  C  CG  A ARG   A 1 93  ? 23.896 -27.796 25.628 0.67 26.21  ? 94  ARG   A CG  1 
ATOM   809  C  CG  B ARG   A 1 93  ? 24.268 -27.767 25.482 0.33 29.00  ? 94  ARG   A CG  1 
ATOM   810  C  CD  A ARG   A 1 93  ? 24.875 -28.945 25.854 0.67 33.34  ? 94  ARG   A CD  1 
ATOM   811  C  CD  B ARG   A 1 93  ? 23.075 -28.674 25.706 0.33 34.93  ? 94  ARG   A CD  1 
ATOM   812  N  NE  A ARG   A 1 93  ? 24.800 -29.455 27.227 0.67 44.65  ? 94  ARG   A NE  1 
ATOM   813  N  NE  B ARG   A 1 93  ? 22.946 -29.698 24.664 0.33 37.87  ? 94  ARG   A NE  1 
ATOM   814  C  CZ  A ARG   A 1 93  ? 23.998 -30.441 27.610 0.67 57.38  ? 94  ARG   A CZ  1 
ATOM   815  C  CZ  B ARG   A 1 93  ? 23.236 -30.985 24.830 0.33 50.46  ? 94  ARG   A CZ  1 
ATOM   816  N  NH1 A ARG   A 1 93  ? 23.213 -31.048 26.728 0.67 46.00  ? 94  ARG   A NH1 1 
ATOM   817  N  NH1 B ARG   A 1 93  ? 23.074 -31.841 23.830 0.33 40.07  ? 94  ARG   A NH1 1 
ATOM   818  N  NH2 A ARG   A 1 93  ? 23.978 -30.834 28.875 0.67 44.52  ? 94  ARG   A NH2 1 
ATOM   819  N  NH2 B ARG   A 1 93  ? 23.668 -31.431 26.003 0.33 33.60  ? 94  ARG   A NH2 1 
ATOM   820  N  N   . LEU   A 1 94  ? 22.772 -23.945 27.958 1.00 19.99  ? 95  LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 94  ? 22.810 -22.933 29.016 1.00 20.33  ? 95  LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 94  ? 22.577 -23.562 30.376 1.00 24.98  ? 95  LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 94  ? 21.518 -24.166 30.607 1.00 24.46  ? 95  LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 94  ? 21.770 -21.845 28.707 1.00 21.08  ? 95  LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 94  ? 21.763 -20.635 29.664 1.00 24.14  ? 95  LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 94  ? 23.025 -19.780 29.453 1.00 22.35  ? 95  LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 94  ? 20.491 -19.808 29.499 1.00 26.99  ? 95  LEU   A CD2 1 
ATOM   828  N  N   . ASN   A 1 95  ? 23.572 -23.435 31.274 1.00 24.25  ? 96  ASN   A N   1 
ATOM   829  C  CA  . ASN   A 1 95  ? 23.477 -23.993 32.633 1.00 25.58  ? 96  ASN   A CA  1 
ATOM   830  C  C   . ASN   A 1 95  ? 22.780 -22.981 33.560 1.00 30.90  ? 96  ASN   A C   1 
ATOM   831  O  O   . ASN   A 1 95  ? 23.429 -22.279 34.343 1.00 31.30  ? 96  ASN   A O   1 
ATOM   832  C  CB  . ASN   A 1 95  ? 24.863 -24.417 33.156 1.00 29.38  ? 96  ASN   A CB  1 
ATOM   833  C  CG  . ASN   A 1 95  ? 24.822 -25.047 34.541 1.00 45.69  ? 96  ASN   A CG  1 
ATOM   834  O  OD1 . ASN   A 1 95  ? 23.804 -25.591 34.976 1.00 37.60  ? 96  ASN   A OD1 1 
ATOM   835  N  ND2 . ASN   A 1 95  ? 25.925 -24.978 35.266 1.00 38.96  ? 96  ASN   A ND2 1 
ATOM   836  N  N   . LEU   A 1 96  ? 21.465 -22.863 33.397 1.00 27.70  ? 97  LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 96  ? 20.633 -21.928 34.147 1.00 29.15  ? 97  LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 96  ? 20.109 -22.585 35.418 1.00 32.90  ? 97  LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 96  ? 19.446 -23.635 35.367 1.00 31.61  ? 97  LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 96  ? 19.507 -21.426 33.232 1.00 30.05  ? 97  LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 96  ? 18.790 -20.149 33.597 1.00 36.13  ? 97  LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 96  ? 19.792 -18.957 33.734 1.00 36.44  ? 97  LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 96  ? 17.692 -19.859 32.576 1.00 35.70  ? 97  LEU   A CD2 1 
ATOM   844  N  N   . ARG   A 1 97  ? 20.485 -22.001 36.573 1.00 30.88  ? 98  ARG   A N   1 
ATOM   845  C  CA  . ARG   A 1 97  ? 20.130 -22.516 37.901 1.00 32.61  ? 98  ARG   A CA  1 
ATOM   846  C  C   . ARG   A 1 97  ? 19.597 -21.399 38.789 1.00 34.00  ? 98  ARG   A C   1 
ATOM   847  O  O   . ARG   A 1 97  ? 19.941 -20.227 38.581 1.00 31.34  ? 98  ARG   A O   1 
ATOM   848  C  CB  . ARG   A 1 97  ? 21.354 -23.177 38.571 1.00 35.06  ? 98  ARG   A CB  1 
ATOM   849  C  CG  . ARG   A 1 97  ? 21.965 -24.339 37.783 1.00 40.68  ? 98  ARG   A CG  1 
ATOM   850  C  CD  . ARG   A 1 97  ? 23.200 -24.934 38.450 1.00 56.98  ? 98  ARG   A CD  1 
ATOM   851  N  NE  . ARG   A 1 97  ? 22.903 -25.546 39.752 1.00 74.55  ? 98  ARG   A NE  1 
ATOM   852  C  CZ  . ARG   A 1 97  ? 22.471 -26.793 39.925 1.00 95.82  ? 98  ARG   A CZ  1 
ATOM   853  N  NH1 . ARG   A 1 97  ? 22.221 -27.251 41.145 1.00 83.98  ? 98  ARG   A NH1 1 
ATOM   854  N  NH2 . ARG   A 1 97  ? 22.270 -27.587 38.878 1.00 85.91  ? 98  ARG   A NH2 1 
ATOM   855  N  N   . GLU   A 1 98  ? 18.770 -21.748 39.791 1.00 32.26  ? 99  GLU   A N   1 
ATOM   856  C  CA  . GLU   A 1 98  ? 18.232 -20.737 40.719 1.00 31.99  ? 99  GLU   A CA  1 
ATOM   857  C  C   . GLU   A 1 98  ? 19.340 -19.833 41.287 1.00 35.77  ? 99  GLU   A C   1 
ATOM   858  O  O   . GLU   A 1 98  ? 19.165 -18.617 41.342 1.00 36.19  ? 99  GLU   A O   1 
ATOM   859  C  CB  . GLU   A 1 98  ? 17.440 -21.405 41.867 1.00 35.31  ? 99  GLU   A CB  1 
ATOM   860  C  CG  . GLU   A 1 98  ? 16.746 -20.419 42.788 1.00 46.28  ? 99  GLU   A CG  1 
ATOM   861  C  CD  . GLU   A 1 98  ? 16.009 -21.045 43.958 1.00 74.36  ? 99  GLU   A CD  1 
ATOM   862  O  OE1 . GLU   A 1 98  ? 16.574 -21.948 44.619 1.00 67.17  ? 99  GLU   A OE1 1 
ATOM   863  O  OE2 . GLU   A 1 98  ? 14.861 -20.622 44.220 1.00 75.12  ? 99  GLU   A OE2 1 
ATOM   864  N  N   . GLY   A 1 99  ? 20.468 -20.434 41.658 1.00 33.72  ? 100 GLY   A N   1 
ATOM   865  C  CA  . GLY   A 1 99  ? 21.607 -19.722 42.233 1.00 34.87  ? 100 GLY   A CA  1 
ATOM   866  C  C   . GLY   A 1 99  ? 22.393 -18.834 41.287 1.00 36.71  ? 100 GLY   A C   1 
ATOM   867  O  O   . GLY   A 1 99  ? 23.128 -17.957 41.745 1.00 36.51  ? 100 GLY   A O   1 
ATOM   868  N  N   . ASN   A 1 100 ? 22.250 -19.027 39.961 1.00 31.20  ? 101 ASN   A N   1 
ATOM   869  C  CA  . ASN   A 1 100 ? 23.035 -18.210 39.026 1.00 29.33  ? 101 ASN   A CA  1 
ATOM   870  C  C   . ASN   A 1 100 ? 22.199 -17.344 38.067 1.00 31.85  ? 101 ASN   A C   1 
ATOM   871  O  O   . ASN   A 1 100 ? 22.773 -16.540 37.325 1.00 30.24  ? 101 ASN   A O   1 
ATOM   872  C  CB  . ASN   A 1 100 ? 24.011 -19.117 38.245 1.00 29.51  ? 101 ASN   A CB  1 
ATOM   873  C  CG  . ASN   A 1 100 ? 23.356 -20.062 37.248 1.00 38.35  ? 101 ASN   A CG  1 
ATOM   874  O  OD1 . ASN   A 1 100 ? 22.294 -19.776 36.693 1.00 27.81  ? 101 ASN   A OD1 1 
ATOM   875  N  ND2 . ASN   A 1 100 ? 23.992 -21.198 36.976 1.00 30.62  ? 101 ASN   A ND2 1 
ATOM   876  N  N   . ILE   A 1 101 ? 20.860 -17.539 38.038 1.00 29.05  ? 102 ILE   A N   1 
ATOM   877  C  CA  . ILE   A 1 101 ? 19.988 -16.881 37.049 1.00 28.75  ? 102 ILE   A CA  1 
ATOM   878  C  C   . ILE   A 1 101 ? 20.094 -15.358 37.042 1.00 29.99  ? 102 ILE   A C   1 
ATOM   879  O  O   . ILE   A 1 101 ? 20.129 -14.765 35.953 1.00 27.75  ? 102 ILE   A O   1 
ATOM   880  C  CB  . ILE   A 1 101 ? 18.510 -17.349 37.125 1.00 33.02  ? 102 ILE   A CB  1 
ATOM   881  C  CG1 . ILE   A 1 101 ? 17.676 -16.771 35.942 1.00 33.57  ? 102 ILE   A CG1 1 
ATOM   882  C  CG2 . ILE   A 1 101 ? 17.873 -17.081 38.497 1.00 33.35  ? 102 ILE   A CG2 1 
ATOM   883  C  CD1 . ILE   A 1 101 ? 16.493 -17.614 35.510 1.00 35.28  ? 102 ILE   A CD1 1 
ATOM   884  N  N   . MET   A 1 102 ? 20.169 -14.724 38.220 1.00 28.43  ? 103 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 102 ? 20.292 -13.264 38.259 1.00 28.99  ? 103 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 102 ? 21.589 -12.789 37.603 1.00 31.58  ? 103 MET   A C   1 
ATOM   887  O  O   . MET   A 1 102 ? 21.554 -11.842 36.803 1.00 29.53  ? 103 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 102 ? 20.142 -12.719 39.696 1.00 33.39  ? 103 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 102 ? 18.780 -13.023 40.322 1.00 40.27  ? 103 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 102 ? 17.344 -12.659 39.272 1.00 46.21  ? 103 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 102 ? 17.348 -10.879 39.299 1.00 44.32  ? 103 MET   A CE  1 
ATOM   892  N  N   . ALA   A 1 103 ? 22.728 -13.467 37.904 1.00 29.15  ? 104 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 103 ? 24.045 -13.102 37.343 1.00 28.19  ? 104 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 103 ? 24.079 -13.409 35.852 1.00 28.35  ? 104 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 103 ? 24.600 -12.615 35.071 1.00 27.27  ? 104 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 103 ? 25.164 -13.855 38.055 1.00 29.56  ? 104 ALA   A CB  1 
ATOM   897  N  N   . VAL   A 1 104 ? 23.502 -14.551 35.447 1.00 23.35  ? 105 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 104 ? 23.471 -14.902 34.015 1.00 21.43  ? 105 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 104 ? 22.651 -13.862 33.227 1.00 25.07  ? 105 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 104 ? 23.115 -13.413 32.170 1.00 23.53  ? 105 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 104 ? 22.944 -16.355 33.822 1.00 25.01  ? 105 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 104 ? 22.640 -16.662 32.350 1.00 23.02  ? 105 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 104 ? 23.956 -17.359 34.360 1.00 26.05  ? 105 VAL   A CG2 1 
ATOM   904  N  N   A MET   A 1 105 ? 21.450 -13.491 33.729 0.20 24.08  ? 106 MET   A N   1 
ATOM   905  N  N   B MET   A 1 105 ? 21.449 -13.488 33.726 0.80 24.17  ? 106 MET   A N   1 
ATOM   906  C  CA  A MET   A 1 105 ? 20.587 -12.510 33.068 0.20 25.01  ? 106 MET   A CA  1 
ATOM   907  C  CA  B MET   A 1 105 ? 20.617 -12.511 33.020 0.80 25.30  ? 106 MET   A CA  1 
ATOM   908  C  C   A MET   A 1 105 ? 21.288 -11.163 32.923 0.20 29.13  ? 106 MET   A C   1 
ATOM   909  C  C   B MET   A 1 105 ? 21.314 -11.154 32.911 0.80 28.27  ? 106 MET   A C   1 
ATOM   910  O  O   A MET   A 1 105 ? 21.283 -10.598 31.829 0.20 28.02  ? 106 MET   A O   1 
ATOM   911  O  O   B MET   A 1 105 ? 21.317 -10.566 31.830 0.80 26.12  ? 106 MET   A O   1 
ATOM   912  C  CB  A MET   A 1 105 ? 19.250 -12.341 33.801 0.20 28.78  ? 106 MET   A CB  1 
ATOM   913  C  CB  B MET   A 1 105 ? 19.245 -12.348 33.670 0.80 29.06  ? 106 MET   A CB  1 
ATOM   914  C  CG  A MET   A 1 105 ? 18.280 -11.469 33.041 0.20 33.12  ? 106 MET   A CG  1 
ATOM   915  C  CG  B MET   A 1 105 ? 18.328 -11.431 32.874 0.80 33.00  ? 106 MET   A CG  1 
ATOM   916  S  SD  A MET   A 1 105 ? 16.734 -11.197 33.911 0.20 38.84  ? 106 MET   A SD  1 
ATOM   917  S  SD  B MET   A 1 105 ? 16.642 -11.408 33.516 0.80 37.68  ? 106 MET   A SD  1 
ATOM   918  C  CE  A MET   A 1 105 ? 16.180 -9.749  33.085 0.20 36.25  ? 106 MET   A CE  1 
ATOM   919  C  CE  B MET   A 1 105 ? 16.858 -10.429 35.090 0.80 35.82  ? 106 MET   A CE  1 
ATOM   920  N  N   . ALA   A 1 106 ? 21.903 -10.667 34.014 1.00 26.93  ? 107 ALA   A N   1 
ATOM   921  C  CA  . ALA   A 1 106 ? 22.632 -9.381  34.011 1.00 27.54  ? 107 ALA   A CA  1 
ATOM   922  C  C   . ALA   A 1 106 ? 23.805 -9.415  33.003 1.00 28.37  ? 107 ALA   A C   1 
ATOM   923  O  O   . ALA   A 1 106 ? 24.007 -8.449  32.242 1.00 26.91  ? 107 ALA   A O   1 
ATOM   924  C  CB  . ALA   A 1 106 ? 23.137 -9.069  35.414 1.00 29.16  ? 107 ALA   A CB  1 
ATOM   925  N  N   . THR   A 1 107 ? 24.542 -10.544 32.962 1.00 23.33  ? 108 THR   A N   1 
ATOM   926  C  CA  . THR   A 1 107 ? 25.657 -10.697 32.022 1.00 22.74  ? 108 THR   A CA  1 
ATOM   927  C  C   . THR   A 1 107 ? 25.122 -10.732 30.578 1.00 24.07  ? 108 THR   A C   1 
ATOM   928  O  O   . THR   A 1 107 ? 25.701 -10.079 29.714 1.00 22.81  ? 108 THR   A O   1 
ATOM   929  C  CB  . THR   A 1 107 ? 26.574 -11.893 32.385 1.00 26.23  ? 108 THR   A CB  1 
ATOM   930  O  OG1 . THR   A 1 107 ? 26.876 -11.875 33.786 1.00 26.25  ? 108 THR   A OG1 1 
ATOM   931  C  CG2 . THR   A 1 107 ? 27.889 -11.892 31.591 1.00 26.74  ? 108 THR   A CG2 1 
ATOM   932  N  N   . ALA   A 1 108 ? 24.019 -11.488 30.310 1.00 21.53  ? 109 ALA   A N   1 
ATOM   933  C  CA  . ALA   A 1 108 ? 23.452 -11.558 28.953 1.00 20.44  ? 109 ALA   A CA  1 
ATOM   934  C  C   . ALA   A 1 108 ? 22.913 -10.199 28.484 1.00 23.51  ? 109 ALA   A C   1 
ATOM   935  O  O   . ALA   A 1 108 ? 23.063 -9.852  27.307 1.00 22.92  ? 109 ALA   A O   1 
ATOM   936  C  CB  . ALA   A 1 108 ? 22.376 -12.638 28.875 1.00 21.30  ? 109 ALA   A CB  1 
ATOM   937  N  N   . MET   A 1 109 ? 22.358 -9.389  29.407 1.00 22.79  ? 110 MET   A N   1 
ATOM   938  C  CA  . MET   A 1 109 ? 21.906 -8.044  29.021 1.00 22.68  ? 110 MET   A CA  1 
ATOM   939  C  C   . MET   A 1 109 ? 23.105 -7.171  28.591 1.00 25.40  ? 110 MET   A C   1 
ATOM   940  O  O   . MET   A 1 109 ? 23.075 -6.520  27.543 1.00 25.53  ? 110 MET   A O   1 
ATOM   941  C  CB  . MET   A 1 109 ? 21.124 -7.391  30.180 1.00 25.53  ? 110 MET   A CB  1 
ATOM   942  C  CG  . MET   A 1 109 ? 19.763 -8.040  30.439 1.00 29.85  ? 110 MET   A CG  1 
ATOM   943  S  SD  . MET   A 1 109 ? 19.040 -7.440  31.993 1.00 36.82  ? 110 MET   A SD  1 
ATOM   944  C  CE  . MET   A 1 109 ? 18.765 -5.699  31.557 1.00 34.67  ? 110 MET   A CE  1 
ATOM   945  N  N   . TYR   A 1 110 ? 24.182 -7.215  29.376 1.00 23.84  ? 111 TYR   A N   1 
ATOM   946  C  CA  . TYR   A 1 110 ? 25.424 -6.477  29.104 1.00 23.08  ? 111 TYR   A CA  1 
ATOM   947  C  C   . TYR   A 1 110 ? 26.032 -6.933  27.760 1.00 25.02  ? 111 TYR   A C   1 
ATOM   948  O  O   . TYR   A 1 110 ? 26.429 -6.097  26.939 1.00 24.15  ? 111 TYR   A O   1 
ATOM   949  C  CB  . TYR   A 1 110 ? 26.415 -6.742  30.237 1.00 23.08  ? 111 TYR   A CB  1 
ATOM   950  C  CG  . TYR   A 1 110 ? 27.820 -6.233  29.994 1.00 23.10  ? 111 TYR   A CG  1 
ATOM   951  C  CD1 . TYR   A 1 110 ? 28.114 -4.870  30.072 1.00 25.99  ? 111 TYR   A CD1 1 
ATOM   952  C  CD2 . TYR   A 1 110 ? 28.872 -7.118  29.761 1.00 22.72  ? 111 TYR   A CD2 1 
ATOM   953  C  CE1 . TYR   A 1 110 ? 29.422 -4.401  29.887 1.00 25.22  ? 111 TYR   A CE1 1 
ATOM   954  C  CE2 . TYR   A 1 110 ? 30.179 -6.666  29.608 1.00 23.14  ? 111 TYR   A CE2 1 
ATOM   955  C  CZ  . TYR   A 1 110 ? 30.449 -5.305  29.674 1.00 25.75  ? 111 TYR   A CZ  1 
ATOM   956  O  OH  . TYR   A 1 110 ? 31.743 -4.884  29.537 1.00 25.67  ? 111 TYR   A OH  1 
ATOM   957  N  N   . LEU   A 1 111 ? 26.093 -8.263  27.539 1.00 21.20  ? 112 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 111 ? 26.651 -8.842  26.318 1.00 19.89  ? 112 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 111 ? 25.725 -8.725  25.118 1.00 23.22  ? 112 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 111 ? 26.147 -9.010  23.993 1.00 22.88  ? 112 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 111 ? 27.072 -10.311 26.547 1.00 18.43  ? 112 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 111 ? 28.208 -10.573 27.560 1.00 20.90  ? 112 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 111 ? 28.510 -12.094 27.646 1.00 22.03  ? 112 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 111 ? 29.521 -9.824  27.164 1.00 22.17  ? 112 LEU   A CD2 1 
ATOM   965  N  N   . GLN   A 1 112 ? 24.454 -8.335  25.344 1.00 20.42  ? 113 GLN   A N   1 
ATOM   966  C  CA  . GLN   A 1 112 ? 23.454 -8.213  24.273 1.00 21.57  ? 113 GLN   A CA  1 
ATOM   967  C  C   . GLN   A 1 112 ? 23.219 -9.586  23.602 1.00 24.14  ? 113 GLN   A C   1 
ATOM   968  O  O   . GLN   A 1 112 ? 23.479 -9.780  22.413 1.00 23.40  ? 113 GLN   A O   1 
ATOM   969  C  CB  . GLN   A 1 112 ? 23.824 -7.111  23.261 1.00 23.09  ? 113 GLN   A CB  1 
ATOM   970  C  CG  . GLN   A 1 112 ? 23.986 -5.721  23.899 1.00 24.47  ? 113 GLN   A CG  1 
ATOM   971  C  CD  . GLN   A 1 112 ? 24.698 -4.761  22.973 1.00 33.31  ? 113 GLN   A CD  1 
ATOM   972  O  OE1 . GLN   A 1 112 ? 24.616 -4.865  21.754 1.00 28.58  ? 113 GLN   A OE1 1 
ATOM   973  N  NE2 . GLN   A 1 112 ? 25.438 -3.820  23.531 1.00 34.35  ? 113 GLN   A NE2 1 
ATOM   974  N  N   . MET   A 1 113 ? 22.771 -10.543 24.411 1.00 21.55  ? 114 MET   A N   1 
ATOM   975  C  CA  . MET   A 1 113 ? 22.438 -11.914 23.992 1.00 21.51  ? 114 MET   A CA  1 
ATOM   976  C  C   . MET   A 1 113 ? 20.943 -12.069 24.262 1.00 26.75  ? 114 MET   A C   1 
ATOM   977  O  O   . MET   A 1 113 ? 20.506 -12.535 25.328 1.00 24.51  ? 114 MET   A O   1 
ATOM   978  C  CB  . MET   A 1 113 ? 23.284 -12.925 24.767 1.00 22.99  ? 114 MET   A CB  1 
ATOM   979  C  CG  . MET   A 1 113 ? 24.768 -12.764 24.484 1.00 23.87  ? 114 MET   A CG  1 
ATOM   980  S  SD  . MET   A 1 113 ? 25.819 -13.809 25.502 1.00 25.61  ? 114 MET   A SD  1 
ATOM   981  C  CE  . MET   A 1 113 ? 25.478 -15.495 24.737 1.00 22.73  ? 114 MET   A CE  1 
ATOM   982  N  N   . GLU   A 1 114 ? 20.157 -11.580 23.302 1.00 26.56  ? 115 GLU   A N   1 
ATOM   983  C  CA  . GLU   A 1 114 ? 18.696 -11.440 23.405 1.00 28.01  ? 115 GLU   A CA  1 
ATOM   984  C  C   . GLU   A 1 114 ? 17.926 -12.710 23.758 1.00 29.14  ? 115 GLU   A C   1 
ATOM   985  O  O   . GLU   A 1 114 ? 17.013 -12.626 24.576 1.00 28.55  ? 115 GLU   A O   1 
ATOM   986  C  CB  . GLU   A 1 114 ? 18.106 -10.817 22.128 1.00 30.85  ? 115 GLU   A CB  1 
ATOM   987  C  CG  . GLU   A 1 114 ? 18.596 -9.400  21.876 1.00 43.96  ? 115 GLU   A CG  1 
ATOM   988  N  N   . HIS   A 1 115 ? 18.259 -13.861 23.151 1.00 25.79  ? 116 HIS   A N   1 
ATOM   989  C  CA  . HIS   A 1 115 ? 17.516 -15.097 23.445 1.00 27.44  ? 116 HIS   A CA  1 
ATOM   990  C  C   . HIS   A 1 115 ? 17.748 -15.571 24.884 1.00 28.73  ? 116 HIS   A C   1 
ATOM   991  O  O   . HIS   A 1 115 ? 16.809 -16.041 25.540 1.00 29.18  ? 116 HIS   A O   1 
ATOM   992  C  CB  . HIS   A 1 115 ? 17.830 -16.185 22.416 1.00 29.38  ? 116 HIS   A CB  1 
ATOM   993  C  CG  . HIS   A 1 115 ? 17.374 -15.826 21.038 1.00 34.27  ? 116 HIS   A CG  1 
ATOM   994  N  ND1 . HIS   A 1 115 ? 16.045 -15.556 20.768 1.00 37.93  ? 116 HIS   A ND1 1 
ATOM   995  C  CD2 . HIS   A 1 115 ? 18.084 -15.721 19.891 1.00 36.07  ? 116 HIS   A CD2 1 
ATOM   996  C  CE1 . HIS   A 1 115 ? 15.989 -15.271 19.477 1.00 37.83  ? 116 HIS   A CE1 1 
ATOM   997  N  NE2 . HIS   A 1 115 ? 17.188 -15.368 18.905 1.00 36.90  ? 116 HIS   A NE2 1 
ATOM   998  N  N   . VAL   A 1 116 ? 18.995 -15.426 25.380 1.00 22.75  ? 117 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 116 ? 19.320 -15.780 26.766 1.00 23.42  ? 117 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 116 ? 18.538 -14.870 27.723 1.00 28.91  ? 117 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 116 ? 17.917 -15.370 28.668 1.00 26.14  ? 117 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 116 ? 20.843 -15.778 27.068 1.00 26.16  ? 117 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 116 ? 21.102 -16.000 28.563 1.00 26.15  ? 117 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 116 ? 21.565 -16.830 26.230 1.00 25.57  ? 117 VAL   A CG2 1 
ATOM   1005 N  N   . VAL   A 1 117 ? 18.551 -13.539 27.475 1.00 25.33  ? 118 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 117 ? 17.794 -12.581 28.306 1.00 25.59  ? 118 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 117 ? 16.312 -13.010 28.382 1.00 30.57  ? 118 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 117 ? 15.774 -13.107 29.477 1.00 30.23  ? 118 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 117 ? 17.964 -11.107 27.840 1.00 28.64  ? 118 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 117 ? 17.113 -10.152 28.694 1.00 29.52  ? 118 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 117 ? 19.429 -10.686 27.893 1.00 27.27  ? 118 VAL   A CG2 1 
ATOM   1012 N  N   A ASP   A 1 118 ? 15.715 -13.363 27.229 0.61 28.90  ? 119 ASP   A N   1 
ATOM   1013 N  N   B ASP   A 1 118 ? 15.673 -13.241 27.216 0.39 28.60  ? 119 ASP   A N   1 
ATOM   1014 C  CA  A ASP   A 1 118 ? 14.331 -13.832 27.114 0.61 30.09  ? 119 ASP   A CA  1 
ATOM   1015 C  CA  B ASP   A 1 118 ? 14.267 -13.649 27.087 0.39 29.86  ? 119 ASP   A CA  1 
ATOM   1016 C  C   A ASP   A 1 118 ? 14.014 -15.061 27.990 0.61 33.29  ? 119 ASP   A C   1 
ATOM   1017 C  C   B ASP   A 1 118 ? 13.901 -14.859 27.953 0.39 33.87  ? 119 ASP   A C   1 
ATOM   1018 O  O   A ASP   A 1 118 ? 13.027 -15.014 28.731 0.61 33.88  ? 119 ASP   A O   1 
ATOM   1019 O  O   B ASP   A 1 118 ? 12.886 -14.817 28.652 0.39 34.60  ? 119 ASP   A O   1 
ATOM   1020 C  CB  A ASP   A 1 118 ? 13.971 -14.092 25.639 0.61 32.38  ? 119 ASP   A CB  1 
ATOM   1021 C  CB  B ASP   A 1 118 ? 13.921 -13.939 25.612 0.39 31.92  ? 119 ASP   A CB  1 
ATOM   1022 C  CG  A ASP   A 1 118 ? 12.516 -14.461 25.412 0.61 44.40  ? 119 ASP   A CG  1 
ATOM   1023 C  CG  B ASP   A 1 118 ? 13.703 -12.724 24.728 0.39 42.57  ? 119 ASP   A CG  1 
ATOM   1024 O  OD1 A ASP   A 1 118 ? 11.636 -13.640 25.745 0.61 47.34  ? 119 ASP   A OD1 1 
ATOM   1025 O  OD1 B ASP   A 1 118 ? 13.311 -11.664 25.258 0.39 44.97  ? 119 ASP   A OD1 1 
ATOM   1026 O  OD2 A ASP   A 1 118 ? 12.261 -15.566 24.891 0.61 49.77  ? 119 ASP   A OD2 1 
ATOM   1027 O  OD2 B ASP   A 1 118 ? 13.898 -12.843 23.499 0.39 48.80  ? 119 ASP   A OD2 1 
ATOM   1028 N  N   A THR   A 1 119 ? 14.832 -16.146 27.923 0.61 28.84  ? 120 THR   A N   1 
ATOM   1029 N  N   B THR   A 1 119 ? 14.729 -15.922 27.916 0.39 29.46  ? 120 THR   A N   1 
ATOM   1030 C  CA  A THR   A 1 119 ? 14.558 -17.336 28.756 0.61 28.95  ? 120 THR   A CA  1 
ATOM   1031 C  CA  B THR   A 1 119 ? 14.489 -17.157 28.670 0.39 29.71  ? 120 THR   A CA  1 
ATOM   1032 C  C   A THR   A 1 119 ? 14.762 -17.045 30.237 0.61 31.60  ? 120 THR   A C   1 
ATOM   1033 C  C   B THR   A 1 119 ? 14.691 -16.942 30.175 0.39 32.37  ? 120 THR   A C   1 
ATOM   1034 O  O   A THR   A 1 119 ? 14.068 -17.634 31.063 0.61 31.44  ? 120 THR   A O   1 
ATOM   1035 O  O   B THR   A 1 119 ? 13.909 -17.477 30.960 0.39 32.65  ? 120 THR   A O   1 
ATOM   1036 C  CB  A THR   A 1 119 ? 15.304 -18.604 28.306 0.61 28.06  ? 120 THR   A CB  1 
ATOM   1037 C  CB  B THR   A 1 119 ? 15.295 -18.326 28.097 0.39 34.45  ? 120 THR   A CB  1 
ATOM   1038 O  OG1 A THR   A 1 119 ? 14.678 -19.731 28.936 0.61 28.79  ? 120 THR   A OG1 1 
ATOM   1039 O  OG1 B THR   A 1 119 ? 15.318 -18.221 26.670 0.39 32.95  ? 120 THR   A OG1 1 
ATOM   1040 C  CG2 A THR   A 1 119 ? 16.801 -18.586 28.653 0.61 22.97  ? 120 THR   A CG2 1 
ATOM   1041 C  CG2 B THR   A 1 119 ? 14.702 -19.672 28.478 0.39 34.16  ? 120 THR   A CG2 1 
ATOM   1042 N  N   . CYS   A 1 120 ? 15.715 -16.150 30.573 1.00 27.99  ? 121 CYS   A N   1 
ATOM   1043 C  CA  . CYS   A 1 120 ? 15.965 -15.782 31.985 1.00 28.25  ? 121 CYS   A CA  1 
ATOM   1044 C  C   . CYS   A 1 120 ? 14.746 -15.069 32.540 1.00 35.01  ? 121 CYS   A C   1 
ATOM   1045 O  O   . CYS   A 1 120 ? 14.295 -15.417 33.640 1.00 33.53  ? 121 CYS   A O   1 
ATOM   1046 C  CB  . CYS   A 1 120 ? 17.208 -14.908 32.109 1.00 27.69  ? 121 CYS   A CB  1 
ATOM   1047 S  SG  . CYS   A 1 120 ? 18.759 -15.810 31.915 1.00 30.00  ? 121 CYS   A SG  1 
ATOM   1048 N  N   A ARG   A 1 121 ? 14.195 -14.102 31.763 0.48 32.89  ? 122 ARG   A N   1 
ATOM   1049 N  N   B ARG   A 1 121 ? 14.198 -14.089 31.782 0.52 33.29  ? 122 ARG   A N   1 
ATOM   1050 C  CA  A ARG   A 1 121 ? 12.997 -13.327 32.103 0.48 34.32  ? 122 ARG   A CA  1 
ATOM   1051 C  CA  B ARG   A 1 121 ? 13.003 -13.338 32.172 0.52 34.89  ? 122 ARG   A CA  1 
ATOM   1052 C  C   A ARG   A 1 121 ? 11.811 -14.260 32.375 0.48 38.08  ? 122 ARG   A C   1 
ATOM   1053 C  C   B ARG   A 1 121 ? 11.802 -14.269 32.392 0.52 38.29  ? 122 ARG   A C   1 
ATOM   1054 O  O   A ARG   A 1 121 ? 11.103 -14.083 33.368 0.48 38.56  ? 122 ARG   A O   1 
ATOM   1055 O  O   B ARG   A 1 121 ? 11.076 -14.102 33.374 0.52 38.74  ? 122 ARG   A O   1 
ATOM   1056 C  CB  A ARG   A 1 121 ? 12.634 -12.352 30.967 0.48 35.22  ? 122 ARG   A CB  1 
ATOM   1057 C  CB  B ARG   A 1 121 ? 12.671 -12.254 31.139 0.52 36.66  ? 122 ARG   A CB  1 
ATOM   1058 C  CG  A ARG   A 1 121 ? 13.569 -11.161 30.843 0.48 46.98  ? 122 ARG   A CG  1 
ATOM   1059 C  CG  B ARG   A 1 121 ? 13.432 -10.953 31.359 0.52 50.83  ? 122 ARG   A CG  1 
ATOM   1060 C  CD  A ARG   A 1 121 ? 12.939 -10.013 30.074 0.48 59.36  ? 122 ARG   A CD  1 
ATOM   1061 C  CD  B ARG   A 1 121 ? 12.707 -9.767  30.744 0.52 62.32  ? 122 ARG   A CD  1 
ATOM   1062 N  NE  A ARG   A 1 121 ? 13.937 -9.014  29.686 0.48 62.58  ? 122 ARG   A NE  1 
ATOM   1063 N  NE  B ARG   A 1 121 ? 12.854 -9.724  29.286 0.52 67.39  ? 122 ARG   A NE  1 
ATOM   1064 C  CZ  A ARG   A 1 121 ? 14.308 -7.980  30.435 0.48 72.63  ? 122 ARG   A CZ  1 
ATOM   1065 C  CZ  B ARG   A 1 121 ? 13.641 -8.875  28.634 0.52 76.20  ? 122 ARG   A CZ  1 
ATOM   1066 N  NH1 A ARG   A 1 121 ? 13.757 -7.781  31.627 0.48 64.77  ? 122 ARG   A NH1 1 
ATOM   1067 N  NH1 B ARG   A 1 121 ? 14.359 -7.976  29.299 0.52 58.97  ? 122 ARG   A NH1 1 
ATOM   1068 N  NH2 A ARG   A 1 121 ? 15.230 -7.134  29.997 0.48 52.17  ? 122 ARG   A NH2 1 
ATOM   1069 N  NH2 B ARG   A 1 121 ? 13.713 -8.912  27.310 0.52 61.42  ? 122 ARG   A NH2 1 
ATOM   1070 N  N   . LYS   A 1 122 ? 11.625 -15.266 31.504 1.00 33.93  ? 123 LYS   A N   1 
ATOM   1071 C  CA  . LYS   A 1 122 ? 10.536 -16.260 31.599 1.00 35.62  ? 123 LYS   A CA  1 
ATOM   1072 C  C   . LYS   A 1 122 ? 10.693 -17.184 32.807 1.00 39.61  ? 123 LYS   A C   1 
ATOM   1073 O  O   . LYS   A 1 122 ? 9.702  -17.436 33.500 1.00 40.08  ? 123 LYS   A O   1 
ATOM   1074 C  CB  . LYS   A 1 122 ? 10.388 -17.058 30.294 1.00 37.54  ? 123 LYS   A CB  1 
ATOM   1075 C  CG  . LYS   A 1 122 ? 9.844  -16.201 29.157 1.00 57.08  ? 123 LYS   A CG  1 
ATOM   1076 C  CD  . LYS   A 1 122 ? 9.748  -16.937 27.834 1.00 68.51  ? 123 LYS   A CD  1 
ATOM   1077 C  CE  . LYS   A 1 122 ? 9.337  -15.988 26.732 1.00 81.89  ? 123 LYS   A CE  1 
ATOM   1078 N  NZ  . LYS   A 1 122 ? 8.453  -16.643 25.734 1.00 94.52  ? 123 LYS   A NZ  1 
ATOM   1079 N  N   . PHE   A 1 123 ? 11.931 -17.664 33.077 1.00 34.82  ? 124 PHE   A N   1 
ATOM   1080 C  CA  . PHE   A 1 123 ? 12.198 -18.529 34.237 1.00 34.98  ? 124 PHE   A CA  1 
ATOM   1081 C  C   . PHE   A 1 123 ? 12.010 -17.772 35.546 1.00 39.55  ? 124 PHE   A C   1 
ATOM   1082 O  O   . PHE   A 1 123 ? 11.497 -18.345 36.510 1.00 38.86  ? 124 PHE   A O   1 
ATOM   1083 C  CB  . PHE   A 1 123 ? 13.595 -19.155 34.163 1.00 34.96  ? 124 PHE   A CB  1 
ATOM   1084 C  CG  . PHE   A 1 123 ? 13.718 -20.422 33.335 1.00 36.20  ? 124 PHE   A CG  1 
ATOM   1085 C  CD1 . PHE   A 1 123 ? 13.134 -20.513 32.071 1.00 39.07  ? 124 PHE   A CD1 1 
ATOM   1086 C  CD2 . PHE   A 1 123 ? 14.463 -21.504 33.795 1.00 38.59  ? 124 PHE   A CD2 1 
ATOM   1087 C  CE1 . PHE   A 1 123 ? 13.269 -21.676 31.299 1.00 39.68  ? 124 PHE   A CE1 1 
ATOM   1088 C  CE2 . PHE   A 1 123 ? 14.602 -22.664 33.017 1.00 40.49  ? 124 PHE   A CE2 1 
ATOM   1089 C  CZ  . PHE   A 1 123 ? 14.000 -22.743 31.780 1.00 37.98  ? 124 PHE   A CZ  1 
ATOM   1090 N  N   . ILE   A 1 124 ? 12.387 -16.478 35.574 1.00 35.14  ? 125 ILE   A N   1 
ATOM   1091 C  CA  . ILE   A 1 124 ? 12.183 -15.644 36.773 1.00 36.14  ? 125 ILE   A CA  1 
ATOM   1092 C  C   . ILE   A 1 124 ? 10.687 -15.402 37.026 1.00 43.63  ? 125 ILE   A C   1 
ATOM   1093 O  O   . ILE   A 1 124 ? 10.234 -15.559 38.166 1.00 45.01  ? 125 ILE   A O   1 
ATOM   1094 C  CB  . ILE   A 1 124 ? 13.024 -14.341 36.715 1.00 38.25  ? 125 ILE   A CB  1 
ATOM   1095 C  CG1 . ILE   A 1 124 ? 14.523 -14.689 36.816 1.00 37.12  ? 125 ILE   A CG1 1 
ATOM   1096 C  CG2 . ILE   A 1 124 ? 12.611 -13.345 37.833 1.00 41.20  ? 125 ILE   A CG2 1 
ATOM   1097 C  CD1 . ILE   A 1 124 ? 15.475 -13.617 36.314 1.00 41.17  ? 125 ILE   A CD1 1 
ATOM   1098 N  N   . LYS   A 1 125 ? 9.921  -15.073 35.957 1.00 42.00  ? 126 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 125 ? 8.475  -14.827 36.016 1.00 44.83  ? 126 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 125 ? 7.713  -16.049 36.554 1.00 48.72  ? 126 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 125 ? 6.756  -15.881 37.306 1.00 48.24  ? 126 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 125 ? 7.932  -14.425 34.637 1.00 48.31  ? 126 LYS   A CB  1 
ATOM   1103 N  N   . ALA   A 1 126 ? 8.158  -17.268 36.193 1.00 44.41  ? 127 ALA   A N   1 
ATOM   1104 C  CA  . ALA   A 1 126 ? 7.532  -18.513 36.655 1.00 45.97  ? 127 ALA   A CA  1 
ATOM   1105 C  C   . ALA   A 1 126 ? 7.685  -18.745 38.169 1.00 52.35  ? 127 ALA   A C   1 
ATOM   1106 O  O   . ALA   A 1 126 ? 6.807  -19.346 38.774 1.00 53.36  ? 127 ALA   A O   1 
ATOM   1107 C  CB  . ALA   A 1 126 ? 8.096  -19.701 35.884 1.00 45.26  ? 127 ALA   A CB  1 
ATOM   1108 N  N   . SER   A 1 127 ? 8.799  -18.298 38.766 1.00 50.77  ? 128 SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 127 ? 9.084  -18.503 40.188 1.00 53.55  ? 128 SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 127 ? 8.503  -17.426 41.123 1.00 61.70  ? 128 SER   A C   1 
ATOM   1111 O  O   . SER   A 1 127 ? 8.479  -17.644 42.338 1.00 63.95  ? 128 SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 127 ? 10.585 -18.661 40.413 1.00 56.94  ? 128 SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 127 ? 10.982 -20.013 40.247 1.00 67.31  ? 128 SER   A OG  1 
ATOM   1114 N  N   . GLU   A 1 128 ? 8.011  -16.291 40.574 1.00 58.33  ? 129 GLU   A N   1 
ATOM   1115 C  CA  . GLU   A 1 128 ? 7.443  -15.199 41.382 1.00 75.69  ? 129 GLU   A CA  1 
ATOM   1116 C  C   . GLU   A 1 128 ? 6.010  -15.475 41.864 1.00 116.63 ? 129 GLU   A C   1 
ATOM   1117 O  O   . GLU   A 1 128 ? 5.572  -16.622 41.930 1.00 84.26  ? 129 GLU   A O   1 
ATOM   1118 C  CB  . GLU   A 1 128 ? 7.541  -13.843 40.652 1.00 76.24  ? 129 GLU   A CB  1 
ATOM   1119 C  CG  . GLU   A 1 128 ? 6.492  -13.608 39.573 1.00 86.08  ? 129 GLU   A CG  1 
ATOM   1120 C  CD  . GLU   A 1 128 ? 6.654  -12.368 38.712 1.00 105.04 ? 129 GLU   A CD  1 
ATOM   1121 O  OE1 . GLU   A 1 128 ? 7.791  -11.853 38.592 1.00 94.31  ? 129 GLU   A OE1 1 
ATOM   1122 O  OE2 . GLU   A 1 128 ? 5.635  -11.919 38.138 1.00 98.06  ? 129 GLU   A OE2 1 
HETATM 1123 C  C   . ACE   B 2 1   ? 21.221 -35.147 5.855  1.00 25.95  ? 0   ACE   D C   1 
HETATM 1124 O  O   . ACE   B 2 1   ? 21.302 -34.014 6.352  1.00 26.97  ? 0   ACE   D O   1 
HETATM 1125 C  CH3 . ACE   B 2 1   ? 21.421 -36.384 6.718  1.00 25.02  ? 0   ACE   D CH3 1 
ATOM   1126 N  N   A TRP   B 2 2   ? 20.949 -35.369 4.571  0.66 23.47  ? 1   TRP   D N   1 
ATOM   1127 N  N   B TRP   B 2 2   ? 20.965 -35.369 4.565  0.34 24.63  ? 1   TRP   D N   1 
ATOM   1128 C  CA  A TRP   B 2 2   ? 20.733 -34.302 3.593  0.66 22.91  ? 1   TRP   D CA  1 
ATOM   1129 C  CA  B TRP   B 2 2   ? 20.697 -34.287 3.617  0.34 24.50  ? 1   TRP   D CA  1 
ATOM   1130 C  C   A TRP   B 2 2   ? 19.225 -34.151 3.301  0.66 27.31  ? 1   TRP   D C   1 
ATOM   1131 C  C   B TRP   B 2 2   ? 19.191 -34.130 3.435  0.34 27.26  ? 1   TRP   D C   1 
ATOM   1132 O  O   A TRP   B 2 2   ? 18.505 -35.155 3.230  0.66 27.42  ? 1   TRP   D O   1 
ATOM   1133 O  O   B TRP   B 2 2   ? 18.444 -35.112 3.526  0.34 26.71  ? 1   TRP   D O   1 
ATOM   1134 C  CB  A TRP   B 2 2   ? 21.516 -34.601 2.295  0.66 22.00  ? 1   TRP   D CB  1 
ATOM   1135 C  CB  B TRP   B 2 2   ? 21.385 -34.509 2.246  0.34 23.94  ? 1   TRP   D CB  1 
ATOM   1136 C  CG  A TRP   B 2 2   ? 23.015 -34.599 2.477  0.66 22.16  ? 1   TRP   D CG  1 
ATOM   1137 C  CG  B TRP   B 2 2   ? 20.776 -35.582 1.390  0.34 25.23  ? 1   TRP   D CG  1 
ATOM   1138 C  CD1 A TRP   B 2 2   ? 23.797 -35.644 2.878  0.66 24.48  ? 1   TRP   D CD1 1 
ATOM   1139 C  CD1 B TRP   B 2 2   ? 21.154 -36.889 1.331  0.34 28.36  ? 1   TRP   D CD1 1 
ATOM   1140 C  CD2 A TRP   B 2 2   ? 23.908 -33.493 2.257  0.66 21.92  ? 1   TRP   D CD2 1 
ATOM   1141 C  CD2 B TRP   B 2 2   ? 19.689 -35.436 0.460  0.34 25.26  ? 1   TRP   D CD2 1 
ATOM   1142 N  NE1 A TRP   B 2 2   ? 25.109 -35.239 2.986  0.66 23.18  ? 1   TRP   D NE1 1 
ATOM   1143 N  NE1 B TRP   B 2 2   ? 20.350 -37.577 0.455  0.34 28.05  ? 1   TRP   D NE1 1 
ATOM   1144 C  CE2 A TRP   B 2 2   ? 25.210 -33.934 2.585  0.66 24.37  ? 1   TRP   D CE2 1 
ATOM   1145 C  CE2 B TRP   B 2 2   ? 19.443 -36.710 -0.099 0.34 29.32  ? 1   TRP   D CE2 1 
ATOM   1146 C  CE3 A TRP   B 2 2   ? 23.725 -32.151 1.875  0.66 22.67  ? 1   TRP   D CE3 1 
ATOM   1147 C  CE3 B TRP   B 2 2   ? 18.868 -34.360 0.076  0.34 26.25  ? 1   TRP   D CE3 1 
ATOM   1148 C  CZ2 A TRP   B 2 2   ? 26.335 -33.109 2.455  0.66 23.99  ? 1   TRP   D CZ2 1 
ATOM   1149 C  CZ2 B TRP   B 2 2   ? 18.430 -36.933 -1.039 0.34 28.61  ? 1   TRP   D CZ2 1 
ATOM   1150 C  CZ3 A TRP   B 2 2   ? 24.842 -31.338 1.741  0.66 23.50  ? 1   TRP   D CZ3 1 
ATOM   1151 C  CZ3 B TRP   B 2 2   ? 17.858 -34.585 -0.848 0.34 27.78  ? 1   TRP   D CZ3 1 
ATOM   1152 C  CH2 A TRP   B 2 2   ? 26.123 -31.810 2.051  0.66 24.04  ? 1   TRP   D CH2 1 
ATOM   1153 C  CH2 B TRP   B 2 2   ? 17.649 -35.858 -1.397 0.34 28.32  ? 1   TRP   D CH2 1 
ATOM   1154 N  N   . VAL   B 2 3   ? 18.746 -32.904 3.147  1.00 22.81  ? 2   VAL   D N   1 
ATOM   1155 C  CA  . VAL   B 2 3   ? 17.315 -32.613 2.900  1.00 22.69  ? 2   VAL   D CA  1 
ATOM   1156 C  C   . VAL   B 2 3   ? 17.169 -31.561 1.793  1.00 24.84  ? 2   VAL   D C   1 
ATOM   1157 O  O   . VAL   B 2 3   ? 18.146 -30.881 1.450  1.00 24.19  ? 2   VAL   D O   1 
ATOM   1158 C  CB  . VAL   B 2 3   ? 16.604 -32.111 4.205  1.00 26.30  ? 2   VAL   D CB  1 
ATOM   1159 C  CG1 . VAL   B 2 3   ? 16.653 -33.159 5.326  1.00 26.63  ? 2   VAL   D CG1 1 
ATOM   1160 C  CG2 . VAL   B 2 3   ? 17.187 -30.767 4.691  1.00 25.58  ? 2   VAL   D CG2 1 
ATOM   1161 N  N   . ILE   B 2 4   ? 15.928 -31.365 1.333  1.00 23.41  ? 3   ILE   D N   1 
ATOM   1162 C  CA  . ILE   B 2 4   ? 15.545 -30.283 0.438  1.00 23.34  ? 3   ILE   D CA  1 
ATOM   1163 C  C   . ILE   B 2 4   ? 15.168 -29.144 1.425  1.00 27.34  ? 3   ILE   D C   1 
ATOM   1164 O  O   . ILE   B 2 4   ? 14.142 -29.259 2.113  1.00 27.12  ? 3   ILE   D O   1 
ATOM   1165 C  CB  . ILE   B 2 4   ? 14.335 -30.661 -0.470 1.00 25.17  ? 3   ILE   D CB  1 
ATOM   1166 C  CG1 . ILE   B 2 4   ? 14.633 -31.933 -1.358 1.00 22.85  ? 3   ILE   D CG1 1 
ATOM   1167 C  CG2 . ILE   B 2 4   ? 13.901 -29.429 -1.320 1.00 27.17  ? 3   ILE   D CG2 1 
ATOM   1168 C  CD1 . ILE   B 2 4   ? 15.904 -31.822 -2.347 1.00 28.15  ? 3   ILE   D CD1 1 
ATOM   1169 N  N   . PRO   B 2 5   ? 15.966 -28.055 1.530  1.00 26.16  ? 4   PRO   D N   1 
ATOM   1170 C  CA  . PRO   B 2 5   ? 15.639 -27.003 2.512  1.00 26.56  ? 4   PRO   D CA  1 
ATOM   1171 C  C   . PRO   B 2 5   ? 14.389 -26.200 2.141  1.00 30.91  ? 4   PRO   D C   1 
ATOM   1172 O  O   . PRO   B 2 5   ? 14.092 -26.035 0.958  1.00 29.52  ? 4   PRO   D O   1 
ATOM   1173 C  CB  . PRO   B 2 5   ? 16.903 -26.134 2.526  1.00 28.02  ? 4   PRO   D CB  1 
ATOM   1174 C  CG  . PRO   B 2 5   ? 17.459 -26.295 1.113  1.00 32.50  ? 4   PRO   D CG  1 
ATOM   1175 C  CD  . PRO   B 2 5   ? 17.231 -27.751 0.816  1.00 28.07  ? 4   PRO   D CD  1 
ATOM   1176 N  N   . ALA   B 2 6   ? 13.652 -25.719 3.151  1.00 29.65  ? 5   ALA   D N   1 
HETATM 1177 C  C4  . A1ACA C 3 .   ? 25.501 -10.206 16.503 1.00 23.52  ? 201 A1ACA A C4  1 
HETATM 1178 C  C5  . A1ACA C 3 .   ? 24.909 -8.939  16.547 1.00 22.56  ? 201 A1ACA A C5  1 
HETATM 1179 C  C6  . A1ACA C 3 .   ? 23.892 -8.659  17.453 1.00 25.95  ? 201 A1ACA A C6  1 
HETATM 1180 C  C7  . A1ACA C 3 .   ? 23.453 -9.676  18.297 1.00 26.16  ? 201 A1ACA A C7  1 
HETATM 1181 C  C8  . A1ACA C 3 .   ? 22.285 -10.866 19.859 1.00 29.81  ? 201 A1ACA A C8  1 
HETATM 1182 C  C10 . A1ACA C 3 .   ? 23.991 -10.957 18.225 1.00 25.46  ? 201 A1ACA A C10 1 
HETATM 1183 C  C1  . A1ACA C 3 .   ? 27.286 -10.324 11.949 1.00 24.32  ? 201 A1ACA A C1  1 
HETATM 1184 C  C2  . A1ACA C 3 .   ? 27.434 -10.647 13.288 1.00 23.32  ? 201 A1ACA A C2  1 
HETATM 1185 C  C3  . A1ACA C 3 .   ? 26.396 -10.303 14.180 1.00 23.67  ? 201 A1ACA A C3  1 
HETATM 1186 C  C9  . A1ACA C 3 .   ? 23.280 -11.818 19.229 1.00 27.42  ? 201 A1ACA A C9  1 
HETATM 1187 O  O   . A1ACA C 3 .   ? 21.455 -11.134 20.725 1.00 29.47  ? 201 A1ACA A O   1 
HETATM 1188 N  N2  . A1ACA C 3 .   ? 22.454 -9.648  19.278 1.00 26.10  ? 201 A1ACA A N2  1 
HETATM 1189 C  C11 . A1ACA C 3 .   ? 25.013 -11.230 17.321 1.00 23.44  ? 201 A1ACA A C11 1 
HETATM 1190 N  N1  . A1ACA C 3 .   ? 26.404 -10.611 15.501 1.00 21.49  ? 201 A1ACA A N1  1 
HETATM 1191 N  N3  . A1ACA C 3 .   ? 25.299 -9.697  13.693 1.00 26.27  ? 201 A1ACA A N3  1 
HETATM 1192 C  C   . A1ACA C 3 .   ? 25.282 -9.453  12.396 1.00 28.28  ? 201 A1ACA A C   1 
HETATM 1193 CL CL  . A1ACA C 3 .   ? 23.831 -8.692  11.815 0.65 30.66  ? 201 A1ACA A CL  1 
HETATM 1194 BR BR  . A1ACA C 3 .   ? 28.991 -11.539 13.872 0.79 23.59  ? 201 A1ACA A BR  1 
HETATM 1195 N  N   . A1ACA C 3 .   ? 26.192 -9.711  11.474 1.00 28.36  ? 201 A1ACA A N   1 
HETATM 1196 CL CL  . CL    D 4 .   ? 21.375 -15.417 22.715 1.00 34.46  ? 202 CL    A CL  1 
HETATM 1197 S  S   A DMS   E 5 .   ? 17.523 -35.391 -1.280 0.66 40.88  ? 101 DMS   D S   1 
HETATM 1198 O  O   A DMS   E 5 .   ? 16.216 -35.200 -0.655 0.66 41.70  ? 101 DMS   D O   1 
HETATM 1199 C  C1  A DMS   E 5 .   ? 18.621 -34.473 -0.233 0.66 40.42  ? 101 DMS   D C1  1 
HETATM 1200 C  C2  A DMS   E 5 .   ? 17.980 -37.010 -0.785 0.66 40.25  ? 101 DMS   D C2  1 
HETATM 1201 O  O   . HOH   F 6 .   ? 35.640 -25.858 25.549 1.00 36.05  ? 301 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 6 .   ? 25.838 -3.544  26.540 1.00 32.11  ? 302 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 6 .   ? 20.820 -5.952  26.255 1.00 37.11  ? 303 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 6 .   ? 41.107 -21.729 25.233 1.00 38.74  ? 304 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 6 .   ? 38.452 -15.003 15.523 1.00 32.19  ? 305 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 6 .   ? 44.315 -0.868  17.929 1.00 48.05  ? 306 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 6 .   ? 16.443 -27.544 -3.208 1.00 43.86  ? 307 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 6 .   ? 37.208 -12.377 40.384 1.00 54.44  ? 308 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 6 .   ? 22.817 -5.497  19.886 1.00 48.74  ? 309 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 6 .   ? 37.894 2.366   19.859 1.00 34.59  ? 310 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 6 .   ? 45.019 -11.314 18.791 1.00 54.79  ? 311 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 6 .   ? 15.436 -10.055 24.997 1.00 48.32  ? 312 HOH   A O   1 
HETATM 1213 O  O   A HOH   F 6 .   ? 19.084 -22.983 4.380  0.67 47.04  ? 313 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 6 .   ? 33.377 -20.869 29.620 1.00 42.42  ? 314 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 6 .   ? 29.815 -32.271 9.513  1.00 44.28  ? 315 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 6 .   ? 26.827 -32.093 16.181 1.00 38.05  ? 316 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 6 .   ? 23.446 -5.926  32.997 1.00 33.89  ? 317 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 6 .   ? 37.700 -20.515 27.027 1.00 33.78  ? 318 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 6 .   ? 21.682 -29.553 -5.237 1.00 35.16  ? 319 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 6 .   ? 19.888 -9.740  37.134 1.00 37.29  ? 320 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 6 .   ? 20.330 -13.591 20.679 1.00 44.06  ? 321 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 6 .   ? 17.909 -29.499 7.688  1.00 30.56  ? 322 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 6 .   ? 25.715 -3.014  20.117 1.00 54.42  ? 323 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 6 .   ? 21.515 -27.196 14.683 0.50 33.22  ? 324 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 6 .   ? 22.666 -27.722 17.779 1.00 46.76  ? 325 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 6 .   ? 32.814 -24.564 32.214 1.00 55.39  ? 326 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 6 .   ? 43.638 -6.672  32.026 1.00 44.96  ? 327 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 6 .   ? 31.709 -0.968  15.943 1.00 39.12  ? 328 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 6 .   ? 28.859 -21.981 41.632 1.00 66.29  ? 329 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 6 .   ? 28.393 -9.025  40.010 1.00 43.26  ? 330 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 6 .   ? 41.326 -16.988 15.237 1.00 32.01  ? 331 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 6 .   ? 30.363 1.345   33.957 1.00 62.29  ? 332 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 6 .   ? 41.478 -12.829 14.254 1.00 80.60  ? 333 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 6 .   ? 27.338 -28.255 18.651 1.00 24.08  ? 334 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 6 .   ? 22.979 -28.297 12.680 1.00 21.63  ? 335 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 6 .   ? 41.218 -1.458  11.715 1.00 54.89  ? 336 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 6 .   ? 36.826 -5.797  12.323 1.00 33.92  ? 337 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 6 .   ? 27.224 -10.263 35.962 1.00 34.39  ? 338 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 6 .   ? 21.562 -30.069 14.197 1.00 70.38  ? 339 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 6 .   ? 34.508 -23.894 29.973 1.00 67.22  ? 340 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 6 .   ? 21.937 -25.071 18.369 1.00 21.32  ? 341 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 6 .   ? 23.341 -17.145 44.350 1.00 60.59  ? 342 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 6 .   ? 28.309 -23.832 31.746 1.00 37.38  ? 343 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 6 .   ? 12.269 -18.099 25.932 1.00 53.50  ? 344 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 6 .   ? 26.152 -21.953 38.718 1.00 35.43  ? 345 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 6 .   ? 28.949 -0.500  16.978 1.00 66.41  ? 346 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 6 .   ? 27.000 -35.399 11.669 1.00 51.63  ? 347 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 6 .   ? 29.383 -27.486 20.671 1.00 22.28  ? 348 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 6 .   ? 24.021 -15.944 21.347 1.00 27.11  ? 349 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 6 .   ? 26.907 -16.740 38.742 1.00 45.76  ? 350 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 6 .   ? 12.802 -20.666 42.383 1.00 52.57  ? 351 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 6 .   ? 18.028 -34.585 8.321  1.00 31.54  ? 352 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 6 .   ? 29.019 -31.205 7.200  1.00 31.72  ? 353 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 6 .   ? 42.471 -10.602 15.567 1.00 46.20  ? 354 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 6 .   ? 45.880 -14.287 21.581 1.00 49.82  ? 355 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 6 .   ? 20.296 -16.100 40.981 1.00 34.48  ? 356 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 6 .   ? 43.926 -4.370  25.790 1.00 41.16  ? 357 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 6 .   ? 30.419 -0.713  37.150 1.00 43.87  ? 358 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 6 .   ? 10.808 -11.612 34.623 1.00 45.67  ? 359 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 6 .   ? 30.711 -29.016 22.662 1.00 36.73  ? 360 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 6 .   ? 28.510 -24.368 34.414 1.00 48.89  ? 361 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 6 .   ? 44.400 -12.761 41.455 1.00 49.04  ? 362 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 6 .   ? 20.931 -7.377  19.841 1.00 43.63  ? 363 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 6 .   ? 26.171 -22.760 29.993 1.00 25.96  ? 364 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 6 .   ? 24.932 -26.911 19.052 1.00 31.10  ? 365 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 6 .   ? 46.866 -21.535 18.305 1.00 42.97  ? 366 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 6 .   ? 37.355 -6.488  34.407 1.00 37.65  ? 367 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 6 .   ? 37.524 3.311   15.877 1.00 39.67  ? 368 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 6 .   ? 38.994 -18.922 33.505 1.00 42.25  ? 369 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 6 .   ? 41.304 -7.801  46.526 1.00 51.89  ? 370 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 6 .   ? 11.673 -15.488 40.589 1.00 71.51  ? 371 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 6 .   ? 24.085 -28.701 21.584 1.00 47.85  ? 372 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 6 .   ? 46.199 -15.841 27.637 1.00 62.87  ? 373 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 6 .   ? 44.659 -16.372 29.810 1.00 47.19  ? 374 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 6 .   ? 34.797 -19.026 13.898 0.50 17.79  ? 375 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 6 .   ? 45.259 -12.658 23.634 1.00 44.01  ? 376 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 6 .   ? 27.211 -2.478  16.109 1.00 59.73  ? 377 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 6 .   ? 37.986 -16.627 13.163 0.50 24.36  ? 378 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 6 .   ? 45.511 -10.935 30.263 1.00 54.99  ? 379 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 6 .   ? 34.161 -8.039  35.765 1.00 30.73  ? 380 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 6 .   ? 47.192 -25.331 21.617 1.00 47.64  ? 381 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 6 .   ? 14.319 -16.986 23.533 1.00 38.83  ? 382 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 6 .   ? 26.216 -8.152  9.087  1.00 37.24  ? 383 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 6 .   ? 16.788 -6.539  27.681 1.00 60.54  ? 384 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 6 .   ? 26.117 -19.310 41.795 1.00 53.86  ? 385 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 6 .   ? 41.323 -7.071  36.024 1.00 41.59  ? 386 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 6 .   ? 46.329 -19.009 19.698 1.00 45.45  ? 387 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 6 .   ? 19.870 -25.625 41.336 1.00 74.09  ? 388 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 6 .   ? 43.875 -10.660 35.233 1.00 67.41  ? 389 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 6 .   ? 27.662 -23.145 13.898 0.50 25.15  ? 390 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 6 .   ? 4.358  -20.549 37.871 1.00 59.08  ? 391 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 6 .   ? 26.546 -30.876 18.978 1.00 58.99  ? 392 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 6 .   ? 29.663 -22.729 36.931 1.00 59.51  ? 393 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 6 .   ? 34.767 -29.151 26.065 1.00 60.83  ? 394 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 6 .   ? 21.294 -31.343 29.845 1.00 63.69  ? 395 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 6 .   ? 31.932 -31.957 14.539 1.00 32.88  ? 396 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 6 .   ? 47.349 -6.762  20.402 1.00 65.71  ? 397 HOH   A O   1 
HETATM 1298 O  O   A HOH   F 6 .   ? 12.224 -21.035 28.001 0.66 43.01  ? 398 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 6 .   ? 23.655 -15.699 17.942 1.00 38.37  ? 399 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 6 .   ? 33.154 -29.871 21.501 1.00 40.37  ? 400 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 6 .   ? 40.452 -19.658 29.089 1.00 31.50  ? 401 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 6 .   ? 44.628 -8.754  17.991 1.00 57.28  ? 402 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 6 .   ? 27.192 -25.449 28.521 1.00 52.55  ? 403 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 6 .   ? 46.143 -9.031  44.147 1.00 46.72  ? 404 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 6 .   ? 41.291 -17.119 35.226 1.00 40.26  ? 405 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 6 .   ? 35.267 1.828   13.569 1.00 51.17  ? 406 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 6 .   ? 45.798 -17.076 17.259 1.00 62.54  ? 407 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 6 .   ? 42.065 -6.060  11.830 1.00 63.14  ? 408 HOH   A O   1 
HETATM 1309 O  O   . HOH   F 6 .   ? 25.641 -4.700  17.997 1.00 47.18  ? 409 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 6 .   ? 47.033 -20.309 21.956 1.00 59.68  ? 410 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 6 .   ? 35.154 -29.796 23.448 1.00 40.68  ? 411 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 6 .   ? 30.463 -10.680 40.647 1.00 39.57  ? 412 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 6 .   ? 27.000 -1.657  22.099 1.00 50.58  ? 413 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 6 .   ? 21.128 -23.347 42.156 1.00 43.55  ? 414 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 6 .   ? 37.040 -2.288  11.555 1.00 53.94  ? 415 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 6 .   ? 23.025 -15.078 40.470 1.00 30.70  ? 416 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 6 .   ? 10.455 -11.744 40.062 1.00 60.32  ? 417 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 6 .   ? 32.233 -15.774 39.894 1.00 31.86  ? 418 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 6 .   ? 34.091 -33.000 21.842 1.00 58.48  ? 419 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 6 .   ? 19.643 -27.385 10.027 1.00 47.73  ? 420 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 6 .   ? 34.592 -18.906 36.253 1.00 66.09  ? 421 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 6 .   ? 32.469 -9.067  39.791 1.00 54.00  ? 422 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 6 .   ? 33.561 -33.087 12.115 1.00 43.44  ? 423 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 6 .   ? 41.991 -8.008  13.749 1.00 55.91  ? 424 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 6 .   ? 29.502 -0.862  22.315 1.00 48.77  ? 425 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 6 .   ? 33.527 -0.375  20.202 1.00 40.26  ? 426 HOH   A O   1 
HETATM 1327 O  O   . HOH   F 6 .   ? 25.618 -16.100 41.110 1.00 46.06  ? 427 HOH   A O   1 
HETATM 1328 O  O   . HOH   F 6 .   ? 31.885 -26.189 27.109 1.00 52.34  ? 428 HOH   A O   1 
HETATM 1329 O  O   . HOH   F 6 .   ? 39.909 -5.597  34.017 1.00 38.23  ? 429 HOH   A O   1 
HETATM 1330 O  O   . HOH   F 6 .   ? 45.876 -5.581  23.790 1.00 44.08  ? 430 HOH   A O   1 
HETATM 1331 O  O   . HOH   F 6 .   ? 32.020 -0.107  13.363 1.00 58.91  ? 431 HOH   A O   1 
HETATM 1332 O  O   . HOH   F 6 .   ? 42.827 -18.337 30.742 1.00 45.92  ? 432 HOH   A O   1 
HETATM 1333 O  O   . HOH   F 6 .   ? 26.416 -29.569 22.713 1.00 53.79  ? 433 HOH   A O   1 
HETATM 1334 O  O   . HOH   F 6 .   ? 22.265 -10.531 14.676 1.00 42.05  ? 434 HOH   A O   1 
HETATM 1335 O  O   . HOH   F 6 .   ? 23.511 -30.600 19.379 1.00 60.89  ? 435 HOH   A O   1 
HETATM 1336 O  O   . HOH   F 6 .   ? 44.427 -4.271  28.976 1.00 60.37  ? 436 HOH   A O   1 
HETATM 1337 O  O   . HOH   F 6 .   ? 37.118 -31.651 23.437 1.00 75.79  ? 437 HOH   A O   1 
HETATM 1338 O  O   . HOH   F 6 .   ? 19.520 -31.871 14.015 1.00 59.03  ? 438 HOH   A O   1 
HETATM 1339 O  O   . HOH   F 6 .   ? 23.110 -3.149  26.890 1.00 62.84  ? 439 HOH   A O   1 
HETATM 1340 O  O   . HOH   F 6 .   ? 27.004 -34.496 18.001 1.00 61.13  ? 440 HOH   A O   1 
HETATM 1341 O  O   . HOH   F 6 .   ? 28.760 -2.775  12.926 1.00 67.36  ? 441 HOH   A O   1 
HETATM 1342 O  O   . HOH   F 6 .   ? 30.673 -34.452 14.885 1.00 57.69  ? 442 HOH   A O   1 
HETATM 1343 O  O   . HOH   F 6 .   ? 47.968 -23.524 19.784 1.00 56.91  ? 443 HOH   A O   1 
HETATM 1344 O  O   . HOH   F 6 .   ? 36.718 -24.571 27.669 1.00 52.61  ? 444 HOH   A O   1 
HETATM 1345 O  O   . HOH   F 6 .   ? 19.815 -8.185  24.599 1.00 48.63  ? 445 HOH   A O   1 
HETATM 1346 O  O   . HOH   F 6 .   ? 35.419 -4.258  10.641 1.00 44.09  ? 446 HOH   A O   1 
HETATM 1347 O  O   . HOH   F 6 .   ? 24.495 -21.745 41.079 1.00 51.48  ? 447 HOH   A O   1 
HETATM 1348 O  O   . HOH   F 6 .   ? 34.211 -17.722 39.460 1.00 60.15  ? 448 HOH   A O   1 
HETATM 1349 O  O   . HOH   F 6 .   ? 47.440 -28.488 17.631 1.00 57.75  ? 449 HOH   A O   1 
HETATM 1350 O  O   . HOH   F 6 .   ? 46.702 -14.692 18.223 1.00 62.81  ? 450 HOH   A O   1 
HETATM 1351 O  O   . HOH   F 6 .   ? 11.963 -18.897 22.792 1.00 60.92  ? 451 HOH   A O   1 
HETATM 1352 O  O   . HOH   F 6 .   ? 35.908 -21.292 30.564 1.00 51.73  ? 452 HOH   A O   1 
HETATM 1353 O  O   . HOH   F 6 .   ? 47.264 -11.926 25.325 1.00 56.82  ? 453 HOH   A O   1 
HETATM 1354 O  O   . HOH   F 6 .   ? 32.162 -1.129  22.409 1.00 55.31  ? 454 HOH   A O   1 
HETATM 1355 O  O   . HOH   F 6 .   ? 19.500 -7.761  35.371 1.00 49.38  ? 455 HOH   A O   1 
HETATM 1356 O  O   . HOH   F 6 .   ? 45.566 -8.465  31.337 1.00 61.27  ? 456 HOH   A O   1 
HETATM 1357 O  O   . HOH   F 6 .   ? 25.417 -5.759  35.046 1.00 56.37  ? 457 HOH   A O   1 
HETATM 1358 O  O   . HOH   F 6 .   ? 47.112 -12.564 28.397 1.00 58.36  ? 458 HOH   A O   1 
HETATM 1359 O  O   . HOH   F 6 .   ? 17.194 -8.071  25.176 1.00 62.84  ? 459 HOH   A O   1 
HETATM 1360 O  O   . HOH   F 6 .   ? 44.059 -13.678 13.899 0.50 70.33  ? 460 HOH   A O   1 
HETATM 1361 O  O   . HOH   F 6 .   ? 19.887 -15.009 43.416 1.00 47.07  ? 461 HOH   A O   1 
HETATM 1362 O  O   . HOH   F 6 .   ? 17.102 -28.226 9.954  1.00 45.81  ? 462 HOH   A O   1 
HETATM 1363 O  O   . HOH   F 6 .   ? 43.251 -3.081  34.011 1.00 59.98  ? 463 HOH   A O   1 
HETATM 1364 O  O   . HOH   F 6 .   ? 19.148 -28.297 13.854 0.50 63.83  ? 464 HOH   A O   1 
HETATM 1365 O  O   . HOH   F 6 .   ? 32.100 -23.874 34.945 1.00 64.69  ? 465 HOH   A O   1 
HETATM 1366 O  O   . HOH   F 6 .   ? 32.657 -20.669 36.997 1.00 67.31  ? 466 HOH   A O   1 
HETATM 1367 O  O   . HOH   F 6 .   ? 28.385 -29.890 24.585 1.00 64.22  ? 467 HOH   A O   1 
HETATM 1368 O  O   . HOH   F 6 .   ? 33.875 -14.124 41.695 0.50 37.94  ? 468 HOH   A O   1 
HETATM 1369 O  O   . HOH   F 6 .   ? 33.875 -11.252 41.695 0.50 58.13  ? 469 HOH   A O   1 
HETATM 1370 O  O   . HOH   F 6 .   ? 21.323 -5.824  34.826 1.00 45.42  ? 470 HOH   A O   1 
HETATM 1371 O  O   . HOH   F 6 .   ? 16.763 -6.984  34.987 1.00 66.17  ? 471 HOH   A O   1 
HETATM 1372 O  O   . HOH   F 6 .   ? 12.487 -18.342 19.999 1.00 60.94  ? 472 HOH   A O   1 
HETATM 1373 O  O   . HOH   F 6 .   ? 45.183 -12.349 16.005 1.00 64.71  ? 473 HOH   A O   1 
HETATM 1374 O  O   . HOH   F 6 .   ? 39.381 -5.677  11.471 1.00 55.52  ? 474 HOH   A O   1 
HETATM 1375 O  O   . HOH   F 6 .   ? 16.659 -30.169 12.414 1.00 52.37  ? 475 HOH   A O   1 
HETATM 1376 O  O   . HOH   G 6 .   ? 12.208 -24.273 0.073  1.00 45.15  ? 201 HOH   D O   1 
HETATM 1377 O  O   . HOH   G 6 .   ? 22.627 -34.087 8.856  1.00 31.22  ? 202 HOH   D O   1 
HETATM 1378 O  O   . HOH   G 6 .   ? 14.976 -25.800 -1.740 1.00 39.94  ? 203 HOH   D O   1 
HETATM 1379 O  O   . HOH   G 6 .   ? 17.704 -36.332 6.085  1.00 40.33  ? 204 HOH   D O   1 
HETATM 1380 O  O   . HOH   G 6 .   ? 20.923 -38.294 3.996  1.00 45.72  ? 205 HOH   D O   1 
HETATM 1381 O  O   . HOH   G 6 .   ? 11.452 -23.654 3.207  1.00 50.20  ? 206 HOH   D O   1 
HETATM 1382 O  O   . HOH   G 6 .   ? 20.846 -39.634 -2.074 1.00 49.99  ? 207 HOH   D O   1 
HETATM 1383 O  O   . HOH   G 6 .   ? 10.625 -24.714 5.588  1.00 52.91  ? 208 HOH   D O   1 
HETATM 1384 O  O   . HOH   G 6 .   ? 20.137 -35.377 10.122 1.00 36.88  ? 209 HOH   D O   1 
HETATM 1385 O  O   . HOH   G 6 .   ? 23.664 -36.531 10.005 1.00 46.83  ? 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   ? 0.7540 0.9326 0.6723 0.0340  -0.1247 -0.0164 6   ASP A N   
2    C CA  . ASP A 5   ? 0.7466 0.9207 0.6494 0.0185  -0.1163 -0.0196 6   ASP A CA  
3    C C   . ASP A 5   ? 0.7239 0.9261 0.6498 0.0078  -0.1123 -0.0358 6   ASP A C   
4    O O   . ASP A 5   ? 0.7195 0.9450 0.6725 0.0115  -0.1158 -0.0445 6   ASP A O   
5    C CB  . ASP A 5   ? 0.7695 0.9162 0.6640 0.0104  -0.1002 -0.0137 6   ASP A CB  
6    C CG  . ASP A 5   ? 0.9592 1.0885 0.8226 0.0005  -0.0953 -0.0099 6   ASP A CG  
7    O OD1 . ASP A 5   ? 0.9567 1.0984 0.8194 -0.0103 -0.0922 -0.0190 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.0669 1.1697 0.9067 0.0026  -0.0933 0.0014  6   ASP A OD2 
9    N N   . SER A 6   ? 0.6144 0.8137 0.5292 -0.0061 -0.1040 -0.0405 7   SER A N   
10   C CA  . SER A 6   ? 0.5671 0.7869 0.4994 -0.0179 -0.0981 -0.0555 7   SER A CA  
11   C C   . SER A 6   ? 0.5144 0.7205 0.4579 -0.0276 -0.0806 -0.0582 7   SER A C   
12   O O   . SER A 6   ? 0.5009 0.7119 0.4485 -0.0391 -0.0727 -0.0680 7   SER A O   
13   C CB  . SER A 6   ? 0.6424 0.8693 0.5543 -0.0259 -0.1021 -0.0603 7   SER A CB  
14   O OG  . SER A 6   ? 0.7995 1.0019 0.6847 -0.0319 -0.0948 -0.0531 7   SER A OG  
15   N N   . CYS A 7   ? 0.4087 0.5974 0.3568 -0.0222 -0.0754 -0.0499 8   CYS A N   
16   C CA  . CYS A 7   ? 0.3709 0.5462 0.3285 -0.0291 -0.0613 -0.0515 8   CYS A CA  
17   C C   . CYS A 7   ? 0.3646 0.5537 0.3466 -0.0349 -0.0557 -0.0632 8   CYS A C   
18   O O   . CYS A 7   ? 0.3481 0.5568 0.3445 -0.0319 -0.0618 -0.0689 8   CYS A O   
19   C CB  . CYS A 7   ? 0.3841 0.5403 0.3411 -0.0216 -0.0586 -0.0407 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.4677 0.5987 0.3943 -0.0201 -0.0580 -0.0282 8   CYS A SG  
21   N N   . ILE A 8   ? 0.2753 0.4535 0.2614 -0.0432 -0.0442 -0.0671 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2357 0.4165 0.2401 -0.0486 -0.0368 -0.0754 9   ILE A CA  
23   C C   . ILE A 8   ? 0.2589 0.4210 0.2670 -0.0441 -0.0315 -0.0675 9   ILE A C   
24   O O   . ILE A 8   ? 0.2616 0.4092 0.2585 -0.0401 -0.0312 -0.0586 9   ILE A O   
25   C CB  . ILE A 8   ? 0.2742 0.4544 0.2797 -0.0602 -0.0287 -0.0861 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.2808 0.4418 0.2749 -0.0626 -0.0220 -0.0828 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.2856 0.4877 0.2898 -0.0657 -0.0341 -0.0958 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3334 0.4903 0.3295 -0.0722 -0.0135 -0.0933 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2016 0.3628 0.2238 -0.0460 -0.0264 -0.0713 10  GLN A N   
30   N N   B GLN A 9   ? 0.2088 0.3720 0.2315 -0.0453 -0.0274 -0.0712 10  GLN A N   
31   C CA  A GLN A 9   ? 0.1962 0.3401 0.2204 -0.0422 -0.0219 -0.0643 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2014 0.3487 0.2274 -0.0415 -0.0230 -0.0647 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2369 0.3685 0.2658 -0.0493 -0.0127 -0.0692 10  GLN A C   
34   C C   B GLN A 9   ? 0.2489 0.3832 0.2789 -0.0487 -0.0136 -0.0693 10  GLN A C   
35   O O   A GLN A 9   ? 0.2430 0.3823 0.2793 -0.0563 -0.0094 -0.0783 10  GLN A O   
36   O O   B GLN A 9   ? 0.2500 0.3911 0.2869 -0.0561 -0.0099 -0.0786 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2100 0.3620 0.2436 -0.0348 -0.0263 -0.0614 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2086 0.3666 0.2458 -0.0351 -0.0273 -0.0638 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2678 0.4054 0.3067 -0.0339 -0.0200 -0.0582 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.2243 0.3662 0.2603 -0.0288 -0.0252 -0.0548 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5371 0.6745 0.5790 -0.0245 -0.0239 -0.0516 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.3964 0.5396 0.4459 -0.0304 -0.0202 -0.0588 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4457 0.5923 0.4857 -0.0168 -0.0322 -0.0484 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.2783 0.4402 0.3410 -0.0315 -0.0215 -0.0668 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.4901 0.6150 0.5349 -0.0245 -0.0181 -0.0492 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.3473 0.4714 0.3933 -0.0309 -0.0142 -0.0540 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2165 0.3285 0.2403 -0.0476 -0.0087 -0.0634 11  PHE A N   
48   N N   B PHE A 10  ? 0.2175 0.3323 0.2423 -0.0466 -0.0098 -0.0630 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2007 0.2970 0.2258 -0.0522 -0.0016 -0.0663 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2106 0.3089 0.2360 -0.0511 -0.0026 -0.0654 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2327 0.3224 0.2617 -0.0500 0.0001  -0.0626 11  PHE A C   
52   C C   B PHE A 10  ? 0.2433 0.3354 0.2731 -0.0493 -0.0007 -0.0623 11  PHE A C   
53   O O   A PHE A 10  ? 0.2163 0.2976 0.2424 -0.0441 -0.0013 -0.0548 11  PHE A O   
54   O O   B PHE A 10  ? 0.2329 0.3191 0.2606 -0.0430 -0.0026 -0.0545 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2145 0.2952 0.2327 -0.0510 0.0005  -0.0640 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2323 0.3158 0.2504 -0.0492 -0.0011 -0.0619 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2323 0.2955 0.2499 -0.0544 0.0060  -0.0674 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.2592 0.3471 0.2739 -0.0534 -0.0002 -0.0681 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.2662 0.3285 0.2842 -0.0616 0.0101  -0.0761 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3015 0.4043 0.3119 -0.0538 -0.0044 -0.0688 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.2451 0.2908 0.2598 -0.0502 0.0067  -0.0619 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3058 0.3813 0.3202 -0.0566 0.0048  -0.0733 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.2854 0.3265 0.2996 -0.0640 0.0150  -0.0784 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3186 0.4252 0.3245 -0.0588 -0.0027 -0.0753 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.2737 0.3002 0.2846 -0.0520 0.0103  -0.0640 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3497 0.4294 0.3619 -0.0607 0.0067  -0.0802 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.2584 0.2810 0.2683 -0.0586 0.0146  -0.0718 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3203 0.4160 0.3282 -0.0625 0.0034  -0.0815 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2030 0.2975 0.2386 -0.0559 0.0040  -0.0693 12  THR A N   
70   C CA  . THR A 11  ? 0.2060 0.2966 0.2458 -0.0563 0.0074  -0.0684 12  THR A CA  
71   C C   . THR A 11  ? 0.2487 0.3157 0.2798 -0.0535 0.0098  -0.0607 12  THR A C   
72   O O   . THR A 11  ? 0.2448 0.3111 0.2775 -0.0489 0.0089  -0.0558 12  THR A O   
73   C CB  . THR A 11  ? 0.2979 0.3921 0.3429 -0.0669 0.0144  -0.0788 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3110 0.4307 0.3658 -0.0692 0.0109  -0.0870 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3377 0.4297 0.3872 -0.0692 0.0195  -0.0798 12  THR A CG2 
76   N N   . ARG A 12  ? 0.2248 0.2734 0.2470 -0.0557 0.0123  -0.0603 13  ARG A N   
77   C CA  . ARG A 12  ? 0.2294 0.2562 0.2428 -0.0529 0.0132  -0.0540 13  ARG A CA  
78   C C   . ARG A 12  ? 0.2505 0.2760 0.2622 -0.0447 0.0080  -0.0471 13  ARG A C   
79   O O   . ARG A 12  ? 0.2453 0.2555 0.2509 -0.0420 0.0076  -0.0428 13  ARG A O   
80   C CB  . ARG A 12  ? 0.2985 0.3040 0.3024 -0.0571 0.0169  -0.0565 13  ARG A CB  
81   C CG  . ARG A 12  ? 0.4286 0.4268 0.4291 -0.0674 0.0245  -0.0630 13  ARG A CG  
82   C CD  . ARG A 12  ? 0.7067 0.6960 0.7025 -0.0705 0.0287  -0.0607 13  ARG A CD  
83   N NE  . ARG A 12  ? 0.8772 0.8412 0.8587 -0.0666 0.0273  -0.0534 13  ARG A NE  
84   C CZ  . ARG A 12  ? 1.0228 0.9783 0.9981 -0.0671 0.0290  -0.0494 13  ARG A CZ  
85   N NH1 . ARG A 12  ? 0.8795 0.8125 0.8403 -0.0634 0.0264  -0.0431 13  ARG A NH1 
86   N NH2 . ARG A 12  ? 0.8092 0.7798 0.7932 -0.0708 0.0330  -0.0525 13  ARG A NH2 
87   N N   . HIS A 13  ? 0.2019 0.2425 0.2176 -0.0416 0.0042  -0.0466 14  HIS A N   
88   C CA  . HIS A 13  ? 0.2082 0.2464 0.2211 -0.0363 0.0012  -0.0416 14  HIS A CA  
89   C C   . HIS A 13  ? 0.2366 0.2678 0.2478 -0.0323 0.0006  -0.0352 14  HIS A C   
90   O O   . HIS A 13  ? 0.2181 0.2395 0.2262 -0.0300 0.0000  -0.0331 14  HIS A O   
91   C CB  . HIS A 13  ? 0.2029 0.2557 0.2161 -0.0351 -0.0018 -0.0416 14  HIS A CB  
92   C CG  . HIS A 13  ? 0.2281 0.2773 0.2372 -0.0320 -0.0026 -0.0378 14  HIS A CG  
93   N ND1 . HIS A 13  ? 0.2313 0.2759 0.2403 -0.0329 -0.0011 -0.0412 14  HIS A ND1 
94   C CD2 . HIS A 13  ? 0.2329 0.2828 0.2383 -0.0288 -0.0041 -0.0320 14  HIS A CD2 
95   C CE1 . HIS A 13  ? 0.2285 0.2731 0.2349 -0.0312 -0.0012 -0.0383 14  HIS A CE1 
96   N NE2 . HIS A 13  ? 0.2205 0.2664 0.2231 -0.0292 -0.0026 -0.0323 14  HIS A NE2 
97   N N   . ALA A 14  ? 0.1997 0.2372 0.2140 -0.0310 0.0005  -0.0332 15  ALA A N   
98   C CA  . ALA A 14  ? 0.2024 0.2328 0.2149 -0.0277 0.0008  -0.0279 15  ALA A CA  
99   C C   . ALA A 14  ? 0.2341 0.2485 0.2413 -0.0298 0.0033  -0.0275 15  ALA A C   
100  O O   . ALA A 14  ? 0.2261 0.2322 0.2293 -0.0275 0.0023  -0.0240 15  ALA A O   
101  C CB  . ALA A 14  ? 0.2104 0.2501 0.2287 -0.0255 0.0007  -0.0274 15  ALA A CB  
102  N N   A SER A 15  ? 0.2250 0.2342 0.2306 -0.0348 0.0064  -0.0314 16  SER A N   
103  N N   B SER A 15  ? 0.2164 0.2256 0.2221 -0.0348 0.0064  -0.0314 16  SER A N   
104  N N   C SER A 15  ? 0.2177 0.2268 0.2234 -0.0348 0.0064  -0.0313 16  SER A N   
105  C CA  A SER A 15  ? 0.2276 0.2179 0.2236 -0.0373 0.0085  -0.0304 16  SER A CA  
106  C CA  B SER A 15  ? 0.2197 0.2100 0.2156 -0.0374 0.0086  -0.0306 16  SER A CA  
107  C CA  C SER A 15  ? 0.2221 0.2122 0.2180 -0.0372 0.0085  -0.0303 16  SER A CA  
108  C C   A SER A 15  ? 0.2751 0.2547 0.2656 -0.0339 0.0045  -0.0291 16  SER A C   
109  C C   B SER A 15  ? 0.2753 0.2545 0.2656 -0.0341 0.0046  -0.0292 16  SER A C   
110  C C   C SER A 15  ? 0.2769 0.2560 0.2671 -0.0340 0.0046  -0.0292 16  SER A C   
111  O O   A SER A 15  ? 0.2561 0.2238 0.2396 -0.0317 0.0025  -0.0259 16  SER A O   
112  O O   B SER A 15  ? 0.2632 0.2300 0.2462 -0.0320 0.0027  -0.0261 16  SER A O   
113  O O   C SER A 15  ? 0.2655 0.2318 0.2482 -0.0320 0.0026  -0.0261 16  SER A O   
114  C CB  A SER A 15  ? 0.2805 0.2652 0.2733 -0.0448 0.0138  -0.0353 16  SER A CB  
115  C CB  B SER A 15  ? 0.2634 0.2485 0.2565 -0.0449 0.0139  -0.0356 16  SER A CB  
116  C CB  C SER A 15  ? 0.2721 0.2565 0.2648 -0.0448 0.0141  -0.0350 16  SER A CB  
117  O OG  A SER A 15  ? 0.3309 0.2930 0.3095 -0.0475 0.0158  -0.0334 16  SER A OG  
118  O OG  B SER A 15  ? 0.2817 0.2793 0.2827 -0.0481 0.0178  -0.0387 16  SER A OG  
119  O OG  C SER A 15  ? 0.3077 0.2940 0.3016 -0.0476 0.0145  -0.0396 16  SER A OG  
120  N N   . ASP A 16  ? 0.2407 0.2258 0.2351 -0.0332 0.0031  -0.0324 17  ASP A N   
121  C CA  . ASP A 16  ? 0.2456 0.2235 0.2386 -0.0292 -0.0006 -0.0333 17  ASP A CA  
122  C C   . ASP A 16  ? 0.2535 0.2378 0.2503 -0.0244 -0.0039 -0.0309 17  ASP A C   
123  O O   . ASP A 16  ? 0.2554 0.2318 0.2501 -0.0206 -0.0075 -0.0306 17  ASP A O   
124  C CB  . ASP A 16  ? 0.2663 0.2513 0.2643 -0.0303 0.0002  -0.0389 17  ASP A CB  
125  C CG  . ASP A 16  ? 0.3687 0.3433 0.3617 -0.0355 0.0038  -0.0428 17  ASP A CG  
126  O OD1 . ASP A 16  ? 0.3623 0.3214 0.3461 -0.0384 0.0060  -0.0409 17  ASP A OD1 
127  O OD2 . ASP A 16  ? 0.4033 0.3841 0.4002 -0.0379 0.0053  -0.0483 17  ASP A OD2 
128  N N   . VAL A 17  ? 0.2002 0.1981 0.2018 -0.0248 -0.0028 -0.0294 18  VAL A N   
129  C CA  . VAL A 17  ? 0.1878 0.1898 0.1912 -0.0223 -0.0040 -0.0274 18  VAL A CA  
130  C C   . VAL A 17  ? 0.2521 0.2440 0.2508 -0.0212 -0.0050 -0.0242 18  VAL A C   
131  O O   . VAL A 17  ? 0.2289 0.2190 0.2282 -0.0189 -0.0078 -0.0250 18  VAL A O   
132  C CB  . VAL A 17  ? 0.2130 0.2256 0.2177 -0.0231 -0.0023 -0.0251 18  VAL A CB  
133  C CG1 . VAL A 17  ? 0.2137 0.2254 0.2170 -0.0222 -0.0017 -0.0224 18  VAL A CG1 
134  C CG2 . VAL A 17  ? 0.2122 0.2345 0.2187 -0.0246 -0.0020 -0.0286 18  VAL A CG2 
135  N N   . LEU A 18  ? 0.2197 0.2069 0.2144 -0.0233 -0.0027 -0.0217 19  LEU A N   
136  C CA  . LEU A 18  ? 0.2405 0.2179 0.2290 -0.0235 -0.0026 -0.0191 19  LEU A CA  
137  C C   . LEU A 18  ? 0.2540 0.2175 0.2343 -0.0223 -0.0066 -0.0195 19  LEU A C   
138  O O   . LEU A 18  ? 0.2479 0.2075 0.2250 -0.0204 -0.0098 -0.0187 19  LEU A O   
139  C CB  . LEU A 18  ? 0.2502 0.2262 0.2371 -0.0267 0.0020  -0.0180 19  LEU A CB  
140  C CG  . LEU A 18  ? 0.2982 0.2663 0.2793 -0.0277 0.0037  -0.0159 19  LEU A CG  
141  C CD1 . LEU A 18  ? 0.2953 0.2692 0.2805 -0.0253 0.0036  -0.0142 19  LEU A CD1 
142  C CD2 . LEU A 18  ? 0.3352 0.3023 0.3160 -0.0315 0.0095  -0.0169 19  LEU A CD2 
143  N N   . LEU A 19  ? 0.2398 0.1956 0.2163 -0.0230 -0.0068 -0.0211 20  LEU A N   
144  C CA  . LEU A 19  ? 0.2607 0.1996 0.2272 -0.0203 -0.0115 -0.0210 20  LEU A CA  
145  C C   . LEU A 19  ? 0.2889 0.2344 0.2628 -0.0135 -0.0182 -0.0233 20  LEU A C   
146  O O   . LEU A 19  ? 0.2876 0.2250 0.2554 -0.0098 -0.0241 -0.0224 20  LEU A O   
147  C CB  . LEU A 19  ? 0.2936 0.2235 0.2563 -0.0222 -0.0095 -0.0232 20  LEU A CB  
148  C CG  . LEU A 19  ? 0.4061 0.3134 0.3555 -0.0186 -0.0145 -0.0224 20  LEU A CG  
149  C CD1 . LEU A 19  ? 0.4476 0.3348 0.3778 -0.0215 -0.0143 -0.0177 20  LEU A CD1 
150  C CD2 . LEU A 19  ? 0.4517 0.3494 0.3977 -0.0216 -0.0107 -0.0253 20  LEU A CD2 
151  N N   . ASN A 20  ? 0.2424 0.2040 0.2295 -0.0125 -0.0172 -0.0271 21  ASN A N   
152  C CA  . ASN A 20  ? 0.2152 0.1864 0.2121 -0.0075 -0.0218 -0.0316 21  ASN A CA  
153  C C   . ASN A 20  ? 0.2470 0.2254 0.2463 -0.0080 -0.0226 -0.0311 21  ASN A C   
154  O O   . ASN A 20  ? 0.2509 0.2319 0.2541 -0.0038 -0.0283 -0.0345 21  ASN A O   
155  C CB  . ASN A 20  ? 0.2256 0.2108 0.2337 -0.0083 -0.0187 -0.0367 21  ASN A CB  
156  C CG  . ASN A 20  ? 0.3428 0.3206 0.3508 -0.0059 -0.0198 -0.0401 21  ASN A CG  
157  O OD1 . ASN A 20  ? 0.3208 0.2827 0.3220 -0.0014 -0.0246 -0.0395 21  ASN A OD1 
158  N ND2 . ASN A 20  ? 0.2906 0.2781 0.3045 -0.0090 -0.0154 -0.0438 21  ASN A ND2 
159  N N   . LEU A 21  ? 0.2349 0.2164 0.2323 -0.0129 -0.0172 -0.0275 22  LEU A N   
160  C CA  . LEU A 21  ? 0.2218 0.2073 0.2198 -0.0144 -0.0167 -0.0272 22  LEU A CA  
161  C C   . LEU A 21  ? 0.2558 0.2294 0.2442 -0.0128 -0.0217 -0.0256 22  LEU A C   
162  O O   . LEU A 21  ? 0.2516 0.2295 0.2421 -0.0119 -0.0251 -0.0284 22  LEU A O   
163  C CB  . LEU A 21  ? 0.2198 0.2068 0.2159 -0.0188 -0.0099 -0.0233 22  LEU A CB  
164  C CG  . LEU A 21  ? 0.2380 0.2351 0.2397 -0.0203 -0.0060 -0.0240 22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.2569 0.2524 0.2549 -0.0221 -0.0014 -0.0191 22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.2664 0.2732 0.2748 -0.0215 -0.0052 -0.0290 22  LEU A CD2 
167  N N   . ASN A 22  ? 0.2345 0.1930 0.2109 -0.0134 -0.0217 -0.0218 23  ASN A N   
168  C CA  . ASN A 22  ? 0.2580 0.2015 0.2201 -0.0126 -0.0265 -0.0196 23  ASN A CA  
169  C C   . ASN A 22  ? 0.3103 0.2509 0.2722 -0.0050 -0.0370 -0.0225 23  ASN A C   
170  O O   . ASN A 22  ? 0.3207 0.2584 0.2769 -0.0027 -0.0435 -0.0230 23  ASN A O   
171  C CB  . ASN A 22  ? 0.2988 0.2251 0.2461 -0.0167 -0.0226 -0.0155 23  ASN A CB  
172  C CG  . ASN A 22  ? 0.4012 0.3115 0.3305 -0.0186 -0.0250 -0.0129 23  ASN A CG  
173  O OD1 . ASN A 22  ? 0.3633 0.2783 0.2926 -0.0192 -0.0265 -0.0136 23  ASN A OD1 
174  N ND2 . ASN A 22  ? 0.4268 0.3167 0.3387 -0.0205 -0.0249 -0.0101 23  ASN A ND2 
175  N N   . ARG A 23  ? 0.2757 0.2184 0.2450 -0.0006 -0.0389 -0.0252 24  ARG A N   
176  C CA  . ARG A 23  ? 0.2854 0.2273 0.2586 0.0087  -0.0491 -0.0293 24  ARG A CA  
177  C C   . ARG A 23  ? 0.3251 0.2883 0.3143 0.0109  -0.0526 -0.0360 24  ARG A C   
178  O O   . ARG A 23  ? 0.3191 0.2825 0.3081 0.0174  -0.0626 -0.0388 24  ARG A O   
179  C CB  . ARG A 23  ? 0.2887 0.2307 0.2694 0.0120  -0.0481 -0.0324 24  ARG A CB  
180  C CG  . ARG A 23  ? 0.3499 0.2674 0.3131 0.0106  -0.0463 -0.0273 24  ARG A CG  
181  C CD  . ARG A 23  ? 0.3418 0.2614 0.3133 0.0109  -0.0424 -0.0311 24  ARG A CD  
182  N NE  . ARG A 23  ? 0.4707 0.3649 0.4249 0.0093  -0.0408 -0.0276 24  ARG A NE  
183  C CZ  . ARG A 23  ? 0.6597 0.5515 0.6156 0.0055  -0.0344 -0.0299 24  ARG A CZ  
184  N NH1 . ARG A 23  ? 0.4916 0.4055 0.4649 0.0031  -0.0297 -0.0350 24  ARG A NH1 
185  N NH2 . ARG A 23  ? 0.5813 0.4480 0.5201 0.0029  -0.0322 -0.0273 24  ARG A NH2 
186  N N   . LEU A 24  ? 0.2663 0.2469 0.2681 0.0049  -0.0444 -0.0389 25  LEU A N   
187  C CA  . LEU A 24  ? 0.2579 0.2580 0.2740 0.0041  -0.0451 -0.0462 25  LEU A CA  
188  C C   . LEU A 24  ? 0.3111 0.3078 0.3185 0.0020  -0.0481 -0.0445 25  LEU A C   
189  O O   . LEU A 24  ? 0.3127 0.3200 0.3274 0.0052  -0.0552 -0.0511 25  LEU A O   
190  C CB  . LEU A 24  ? 0.2452 0.2579 0.2697 -0.0035 -0.0343 -0.0478 25  LEU A CB  
191  C CG  . LEU A 24  ? 0.2937 0.3136 0.3274 -0.0030 -0.0306 -0.0513 25  LEU A CG  
192  C CD1 . LEU A 24  ? 0.2921 0.3220 0.3294 -0.0111 -0.0207 -0.0522 25  LEU A CD1 
193  C CD2 . LEU A 24  ? 0.2845 0.3146 0.3324 0.0044  -0.0374 -0.0608 25  LEU A CD2 
194  N N   . ARG A 25  ? 0.2752 0.2584 0.2678 -0.0037 -0.0427 -0.0370 26  ARG A N   
195  C CA  . ARG A 25  ? 0.2910 0.2689 0.2733 -0.0067 -0.0443 -0.0356 26  ARG A CA  
196  C C   . ARG A 25  ? 0.3559 0.3246 0.3279 0.0003  -0.0573 -0.0359 26  ARG A C   
197  O O   . ARG A 25  ? 0.3576 0.3344 0.3314 0.0010  -0.0634 -0.0406 26  ARG A O   
198  C CB  . ARG A 25  ? 0.3037 0.2680 0.2727 -0.0132 -0.0359 -0.0286 26  ARG A CB  
199  C CG  . ARG A 25  ? 0.3453 0.3043 0.3035 -0.0172 -0.0367 -0.0284 26  ARG A CG  
200  C CD  . ARG A 25  ? 0.4109 0.3592 0.3593 -0.0237 -0.0272 -0.0236 26  ARG A CD  
201  N NE  . ARG A 25  ? 0.3951 0.3270 0.3300 -0.0237 -0.0266 -0.0186 26  ARG A NE  
202  C CZ  . ARG A 25  ? 0.5073 0.4236 0.4243 -0.0278 -0.0251 -0.0159 26  ARG A CZ  
203  N NH1 . ARG A 25  ? 0.4387 0.3537 0.3486 -0.0313 -0.0255 -0.0176 26  ARG A NH1 
204  N NH2 . ARG A 25  ? 0.4333 0.3348 0.3385 -0.0295 -0.0224 -0.0123 26  ARG A NH2 
205  N N   A SER A 26  ? 0.3352 0.2862 0.2952 0.0053  -0.0615 -0.0311 27  SER A N   
206  N N   B SER A 26  ? 0.3302 0.2813 0.2904 0.0053  -0.0615 -0.0311 27  SER A N   
207  N N   C SER A 26  ? 0.3339 0.2850 0.2940 0.0053  -0.0615 -0.0311 27  SER A N   
208  C CA  A SER A 26  ? 0.3618 0.2975 0.3066 0.0130  -0.0743 -0.0294 27  SER A CA  
209  C CA  B SER A 26  ? 0.3545 0.2900 0.2997 0.0132  -0.0743 -0.0293 27  SER A CA  
210  C CA  C SER A 26  ? 0.3600 0.2955 0.3048 0.0131  -0.0743 -0.0293 27  SER A CA  
211  C C   A SER A 26  ? 0.4213 0.3735 0.3819 0.0231  -0.0867 -0.0378 27  SER A C   
212  C C   B SER A 26  ? 0.4159 0.3681 0.3765 0.0230  -0.0865 -0.0378 27  SER A C   
213  C C   C SER A 26  ? 0.4194 0.3716 0.3800 0.0230  -0.0866 -0.0378 27  SER A C   
214  O O   A SER A 26  ? 0.4386 0.3865 0.3898 0.0285  -0.0986 -0.0385 27  SER A O   
215  O O   B SER A 26  ? 0.4315 0.3793 0.3825 0.0283  -0.0983 -0.0384 27  SER A O   
216  O O   C SER A 26  ? 0.4360 0.3838 0.3872 0.0285  -0.0985 -0.0385 27  SER A O   
217  C CB  A SER A 26  ? 0.4124 0.3241 0.3420 0.0157  -0.0744 -0.0232 27  SER A CB  
218  C CB  B SER A 26  ? 0.3993 0.3134 0.3324 0.0167  -0.0745 -0.0240 27  SER A CB  
219  C CB  C SER A 26  ? 0.4103 0.3227 0.3409 0.0159  -0.0743 -0.0234 27  SER A CB  
220  O OG  A SER A 26  ? 0.4883 0.4067 0.4330 0.0221  -0.0757 -0.0270 27  SER A OG  
221  O OG  B SER A 26  ? 0.4689 0.3657 0.3848 0.0078  -0.0649 -0.0173 27  SER A OG  
222  O OG  C SER A 26  ? 0.5224 0.4147 0.4343 0.0240  -0.0870 -0.0205 27  SER A OG  
223  N N   . ARG A 27  ? 0.3550 0.3272 0.3396 0.0252  -0.0839 -0.0450 28  ARG A N   
224  C CA  . ARG A 27  ? 0.3584 0.3511 0.3634 0.0341  -0.0937 -0.0558 28  ARG A CA  
225  C C   . ARG A 27  ? 0.3682 0.3879 0.3912 0.0275  -0.0897 -0.0650 28  ARG A C   
226  O O   . ARG A 27  ? 0.3612 0.4033 0.4053 0.0326  -0.0956 -0.0764 28  ARG A O   
227  C CB  . ARG A 27  ? 0.3730 0.3703 0.3928 0.0397  -0.0919 -0.0597 28  ARG A CB  
228  C CG  . ARG A 27  ? 0.4594 0.4280 0.4607 0.0459  -0.0956 -0.0516 28  ARG A CG  
229  C CD  . ARG A 27  ? 0.5149 0.4868 0.5293 0.0485  -0.0908 -0.0555 28  ARG A CD  
230  N NE  . ARG A 27  ? 0.6478 0.6404 0.6865 0.0585  -0.0983 -0.0676 28  ARG A NE  
231  C CZ  . ARG A 27  ? 0.8116 0.8206 0.8707 0.0580  -0.0918 -0.0759 28  ARG A CZ  
232  N NH1 . ARG A 27  ? 0.6619 0.6915 0.7447 0.0668  -0.0982 -0.0886 28  ARG A NH1 
233  N NH2 . ARG A 27  ? 0.6197 0.6263 0.6764 0.0483  -0.0788 -0.0726 28  ARG A NH2 
234  N N   . ASP A 28  ? 0.2998 0.3172 0.3149 0.0158  -0.0792 -0.0610 29  ASP A N   
235  C CA  . ASP A 28  ? 0.2990 0.3358 0.3261 0.0070  -0.0727 -0.0683 29  ASP A CA  
236  C C   . ASP A 28  ? 0.3451 0.4036 0.3955 0.0040  -0.0649 -0.0775 29  ASP A C   
237  O O   . ASP A 28  ? 0.3504 0.4306 0.4172 0.0007  -0.0643 -0.0889 29  ASP A O   
238  C CB  . ASP A 28  ? 0.3355 0.3821 0.3634 0.0096  -0.0841 -0.0751 29  ASP A CB  
239  C CG  . ASP A 28  ? 0.4252 0.4850 0.4584 -0.0022 -0.0759 -0.0811 29  ASP A CG  
240  O OD1 . ASP A 28  ? 0.4357 0.4849 0.4598 -0.0117 -0.0631 -0.0749 29  ASP A OD1 
241  O OD2 . ASP A 28  ? 0.4648 0.5454 0.5117 -0.0017 -0.0822 -0.0927 29  ASP A OD2 
242  N N   . ILE A 29  ? 0.2630 0.3155 0.3140 0.0043  -0.0586 -0.0735 30  ILE A N   
243  C CA  . ILE A 29  ? 0.2508 0.3202 0.3194 0.0008  -0.0506 -0.0812 30  ILE A CA  
244  C C   . ILE A 29  ? 0.2787 0.3465 0.3425 -0.0114 -0.0361 -0.0778 30  ILE A C   
245  O O   . ILE A 29  ? 0.2387 0.2898 0.2878 -0.0138 -0.0312 -0.0672 30  ILE A O   
246  C CB  . ILE A 29  ? 0.2879 0.3526 0.3598 0.0081  -0.0523 -0.0803 30  ILE A CB  
247  C CG1 . ILE A 29  ? 0.3098 0.3757 0.3883 0.0219  -0.0672 -0.0852 30  ILE A CG1 
248  C CG2 . ILE A 29  ? 0.2770 0.3571 0.3633 0.0020  -0.0417 -0.0876 30  ILE A CG2 
249  C CD1 . ILE A 29  ? 0.3675 0.4198 0.4429 0.0294  -0.0692 -0.0819 30  ILE A CD1 
250  N N   . LEU A 30  ? 0.2615 0.3465 0.3374 -0.0192 -0.0294 -0.0874 31  LEU A N   
251  C CA  . LEU A 30  ? 0.2739 0.3559 0.3441 -0.0310 -0.0155 -0.0853 31  LEU A CA  
252  C C   . LEU A 30  ? 0.2874 0.3522 0.3403 -0.0356 -0.0119 -0.0758 31  LEU A C   
253  O O   . LEU A 30  ? 0.2604 0.3164 0.3048 -0.0426 -0.0017 -0.0710 31  LEU A O   
254  C CB  . LEU A 30  ? 0.2861 0.3644 0.3541 -0.0328 -0.0081 -0.0818 31  LEU A CB  
255  C CG  . LEU A 30  ? 0.3709 0.4686 0.4569 -0.0333 -0.0059 -0.0942 31  LEU A CG  
256  C CD1 . LEU A 30  ? 0.3886 0.4809 0.4679 -0.0377 0.0029  -0.0904 31  LEU A CD1 
257  C CD2 . LEU A 30  ? 0.4494 0.5651 0.5480 -0.0420 -0.0001 -0.1073 31  LEU A CD2 
258  N N   . THR A 31  ? 0.2571 0.3173 0.3047 -0.0318 -0.0202 -0.0743 32  THR A N   
259  C CA  . THR A 31  ? 0.2556 0.3021 0.2889 -0.0371 -0.0162 -0.0683 32  THR A CA  
260  C C   . THR A 31  ? 0.3138 0.3698 0.3530 -0.0477 -0.0075 -0.0768 32  THR A C   
261  O O   . THR A 31  ? 0.3045 0.3803 0.3592 -0.0495 -0.0092 -0.0888 32  THR A O   
262  C CB  . THR A 31  ? 0.3023 0.3429 0.3276 -0.0317 -0.0271 -0.0666 32  THR A CB  
263  O OG1 . THR A 31  ? 0.3497 0.4084 0.3878 -0.0284 -0.0365 -0.0775 32  THR A OG1 
264  C CG2 . THR A 31  ? 0.3094 0.3349 0.3242 -0.0235 -0.0331 -0.0574 32  THR A CG2 
265  N N   . ASP A 32  ? 0.2721 0.3143 0.3001 -0.0549 0.0028  -0.0714 33  ASP A N   
266  C CA  . ASP A 32  ? 0.2688 0.3144 0.2986 -0.0663 0.0134  -0.0783 33  ASP A CA  
267  C C   . ASP A 32  ? 0.3122 0.3449 0.3309 -0.0723 0.0183  -0.0765 33  ASP A C   
268  O O   . ASP A 32  ? 0.3159 0.3449 0.3320 -0.0825 0.0291  -0.0804 33  ASP A O   
269  C CB  . ASP A 32  ? 0.2816 0.3203 0.3074 -0.0706 0.0240  -0.0746 33  ASP A CB  
270  C CG  . ASP A 32  ? 0.4017 0.4206 0.4135 -0.0655 0.0254  -0.0607 33  ASP A CG  
271  O OD1 . ASP A 32  ? 0.3514 0.3606 0.3565 -0.0607 0.0211  -0.0543 33  ASP A OD1 
272  O OD2 . ASP A 32  ? 0.5025 0.5167 0.5100 -0.0667 0.0308  -0.0569 33  ASP A OD2 
273  N N   . VAL A 33  ? 0.2656 0.2897 0.2761 -0.0670 0.0116  -0.0710 34  VAL A N   
274  C CA  . VAL A 33  ? 0.2680 0.2804 0.2681 -0.0729 0.0163  -0.0705 34  VAL A CA  
275  C C   . VAL A 33  ? 0.3248 0.3366 0.3193 -0.0680 0.0056  -0.0698 34  VAL A C   
276  O O   . VAL A 33  ? 0.3166 0.3276 0.3096 -0.0591 -0.0034 -0.0647 34  VAL A O   
277  C CB  . VAL A 33  ? 0.3036 0.2937 0.2915 -0.0738 0.0265  -0.0604 34  VAL A CB  
278  C CG1 . VAL A 33  ? 0.2816 0.2622 0.2635 -0.0646 0.0217  -0.0502 34  VAL A CG1 
279  C CG2 . VAL A 33  ? 0.3169 0.2948 0.2963 -0.0819 0.0351  -0.0627 34  VAL A CG2 
280  N N   A VAL A 34  ? 0.2923 0.3027 0.2816 -0.0746 0.0071  -0.0751 35  VAL A N   
281  N N   B VAL A 34  ? 0.2853 0.2957 0.2745 -0.0745 0.0069  -0.0750 35  VAL A N   
282  C CA  A VAL A 34  ? 0.2982 0.3042 0.2768 -0.0726 -0.0010 -0.0744 35  VAL A CA  
283  C CA  B VAL A 34  ? 0.2872 0.2928 0.2657 -0.0719 -0.0015 -0.0737 35  VAL A CA  
284  C C   A VAL A 34  ? 0.3417 0.3276 0.3070 -0.0778 0.0096  -0.0694 35  VAL A C   
285  C C   B VAL A 34  ? 0.3393 0.3259 0.3044 -0.0778 0.0088  -0.0699 35  VAL A C   
286  O O   A VAL A 34  ? 0.3444 0.3260 0.3102 -0.0860 0.0205  -0.0731 35  VAL A O   
287  O O   B VAL A 34  ? 0.3431 0.3269 0.3088 -0.0865 0.0190  -0.0746 35  VAL A O   
288  C CB  A VAL A 34  ? 0.3584 0.3819 0.3421 -0.0764 -0.0090 -0.0866 35  VAL A CB  
289  C CB  B VAL A 34  ? 0.3403 0.3639 0.3237 -0.0719 -0.0134 -0.0842 35  VAL A CB  
290  C CG1 A VAL A 34  ? 0.3691 0.3849 0.3369 -0.0746 -0.0179 -0.0848 35  VAL A CG1 
291  C CG1 B VAL A 34  ? 0.3395 0.3737 0.3293 -0.0836 -0.0067 -0.0962 35  VAL A CG1 
292  C CG2 A VAL A 34  ? 0.3504 0.3965 0.3515 -0.0704 -0.0191 -0.0936 35  VAL A CG2 
293  C CG2 B VAL A 34  ? 0.3503 0.3643 0.3171 -0.0677 -0.0236 -0.0801 35  VAL A CG2 
294  N N   . ILE A 35  ? 0.2935 0.2661 0.2470 -0.0733 0.0073  -0.0617 36  ILE A N   
295  C CA  . ILE A 35  ? 0.3025 0.2579 0.2449 -0.0773 0.0167  -0.0585 36  ILE A CA  
296  C C   . ILE A 35  ? 0.3647 0.3188 0.2949 -0.0814 0.0114  -0.0631 36  ILE A C   
297  O O   . ILE A 35  ? 0.3627 0.3171 0.2850 -0.0767 0.0007  -0.0607 36  ILE A O   
298  C CB  . ILE A 35  ? 0.3222 0.2657 0.2608 -0.0711 0.0194  -0.0489 36  ILE A CB  
299  C CG1 . ILE A 35  ? 0.3154 0.2621 0.2650 -0.0660 0.0219  -0.0442 36  ILE A CG1 
300  C CG2 . ILE A 35  ? 0.3423 0.2705 0.2729 -0.0752 0.0300  -0.0481 36  ILE A CG2 
301  C CD1 . ILE A 35  ? 0.3187 0.2629 0.2731 -0.0706 0.0319  -0.0462 36  ILE A CD1 
302  N N   . VAL A 36  ? 0.3334 0.2846 0.2603 -0.0905 0.0189  -0.0698 37  VAL A N   
303  C CA  . VAL A 36  ? 0.3385 0.2887 0.2523 -0.0961 0.0146  -0.0754 37  VAL A CA  
304  C C   . VAL A 36  ? 0.4168 0.3477 0.3166 -0.0992 0.0236  -0.0719 37  VAL A C   
305  O O   . VAL A 36  ? 0.3970 0.3180 0.2995 -0.1027 0.0367  -0.0721 37  VAL A O   
306  C CB  . VAL A 36  ? 0.3898 0.3523 0.3090 -0.1056 0.0161  -0.0876 37  VAL A CB  
307  C CG1 . VAL A 36  ? 0.4022 0.3646 0.3064 -0.1114 0.0104  -0.0938 37  VAL A CG1 
308  C CG2 . VAL A 36  ? 0.3828 0.3678 0.3187 -0.1025 0.0073  -0.0930 37  VAL A CG2 
309  N N   . VAL A 37  ? 0.3908 0.3153 0.2745 -0.0980 0.0168  -0.0691 38  VAL A N   
310  C CA  . VAL A 37  ? 0.3949 0.3024 0.2644 -0.1018 0.0253  -0.0671 38  VAL A CA  
311  C C   . VAL A 37  ? 0.4953 0.4007 0.3452 -0.1088 0.0193  -0.0726 38  VAL A C   
312  O O   . VAL A 37  ? 0.4645 0.3675 0.3000 -0.1056 0.0076  -0.0691 38  VAL A O   
313  C CB  . VAL A 37  ? 0.4317 0.3313 0.2984 -0.0949 0.0247  -0.0580 38  VAL A CB  
314  C CG1 . VAL A 37  ? 0.4430 0.3280 0.3012 -0.0996 0.0372  -0.0580 38  VAL A CG1 
315  C CG2 . VAL A 37  ? 0.4045 0.3113 0.2904 -0.0869 0.0255  -0.0530 38  VAL A CG2 
316  N N   A SER A 38  ? 0.4972 0.4037 0.3463 -0.1181 0.0260  -0.0816 39  SER A N   
317  N N   B SER A 38  ? 0.4895 0.3936 0.3374 -0.1183 0.0276  -0.0811 39  SER A N   
318  C CA  A SER A 38  ? 0.5199 0.4269 0.3513 -0.1263 0.0207  -0.0890 39  SER A CA  
319  C CA  B SER A 38  ? 0.5098 0.4132 0.3398 -0.1271 0.0237  -0.0886 39  SER A CA  
320  C C   A SER A 38  ? 0.5321 0.4566 0.3643 -0.1218 0.0017  -0.0914 39  SER A C   
321  C C   B SER A 38  ? 0.5328 0.4484 0.3560 -0.1226 0.0039  -0.0889 39  SER A C   
322  O O   A SER A 38  ? 0.5148 0.4563 0.3665 -0.1205 -0.0006 -0.0963 39  SER A O   
323  O O   B SER A 38  ? 0.5414 0.4480 0.3432 -0.1209 -0.0052 -0.0847 39  SER A O   
324  C CB  A SER A 38  ? 0.6037 0.4927 0.4106 -0.1301 0.0234  -0.0860 39  SER A CB  
325  C CB  B SER A 38  ? 0.5797 0.4644 0.3896 -0.1332 0.0324  -0.0879 39  SER A CB  
326  O OG  A SER A 38  ? 0.7964 0.6727 0.6070 -0.1330 0.0407  -0.0854 39  SER A OG  
327  O OG  B SER A 38  ? 0.6774 0.5545 0.4955 -0.1388 0.0498  -0.0924 39  SER A OG  
328  N N   A ARG A 39  ? 0.4897 0.4092 0.3008 -0.1189 -0.0117 -0.0881 40  ARG A N   
329  N N   B ARG A 39  ? 0.4518 0.3871 0.2944 -0.1196 -0.0024 -0.0935 40  ARG A N   
330  C CA  A ARG A 39  ? 0.4861 0.4203 0.2961 -0.1122 -0.0320 -0.0901 40  ARG A CA  
331  C CA  B ARG A 39  ? 0.4484 0.4022 0.2949 -0.1137 -0.0209 -0.0969 40  ARG A CA  
332  C C   A ARG A 39  ? 0.5111 0.4495 0.3325 -0.0986 -0.0412 -0.0820 40  ARG A C   
333  C C   B ARG A 39  ? 0.4748 0.4277 0.3232 -0.1002 -0.0321 -0.0869 40  ARG A C   
334  O O   A ARG A 39  ? 0.5007 0.4531 0.3265 -0.0908 -0.0579 -0.0843 40  ARG A O   
335  O O   B ARG A 39  ? 0.4716 0.4429 0.3340 -0.0931 -0.0442 -0.0901 40  ARG A O   
336  C CB  A ARG A 39  ? 0.5121 0.4351 0.2898 -0.1147 -0.0433 -0.0897 40  ARG A CB  
337  C CB  B ARG A 39  ? 0.4721 0.4290 0.2990 -0.1188 -0.0322 -0.1038 40  ARG A CB  
338  C CG  A ARG A 39  ? 0.5857 0.5133 0.3539 -0.1273 -0.0405 -0.1013 40  ARG A CG  
339  C CG  B ARG A 39  ? 0.6017 0.5672 0.4331 -0.1322 -0.0232 -0.1171 40  ARG A CG  
340  C CD  A ARG A 39  ? 0.6245 0.5448 0.3606 -0.1278 -0.0564 -0.1011 40  ARG A CD  
341  C CD  B ARG A 39  ? 0.6948 0.6733 0.5142 -0.1360 -0.0381 -0.1268 40  ARG A CD  
342  N NE  A ARG A 39  ? 0.6515 0.5723 0.3739 -0.1417 -0.0516 -0.1118 40  ARG A NE  
343  N NE  B ARG A 39  ? 0.7590 0.7446 0.5816 -0.1507 -0.0279 -0.1404 40  ARG A NE  
344  C CZ  A ARG A 39  ? 0.8233 0.7661 0.5526 -0.1455 -0.0607 -0.1241 40  ARG A CZ  
345  C CZ  B ARG A 39  ? 0.9084 0.8779 0.7115 -0.1619 -0.0175 -0.1433 40  ARG A CZ  
346  N NH1 A ARG A 39  ? 0.7008 0.6421 0.4157 -0.1594 -0.0550 -0.1339 40  ARG A NH1 
347  N NH1 B ARG A 39  ? 0.7169 0.6632 0.4960 -0.1607 -0.0154 -0.1339 40  ARG A NH1 
348  N NH2 A ARG A 39  ? 0.6236 0.5915 0.3755 -0.1362 -0.0749 -0.1280 40  ARG A NH2 
349  N NH2 B ARG A 39  ? 0.7506 0.7267 0.5579 -0.1754 -0.0079 -0.1567 40  ARG A NH2 
350  N N   A GLU A 40  ? 0.4424 0.3695 0.2693 -0.0955 -0.0309 -0.0735 41  GLU A N   
351  N N   B GLU A 40  ? 0.4283 0.3616 0.2655 -0.0970 -0.0269 -0.0762 41  GLU A N   
352  C CA  A GLU A 40  ? 0.4227 0.3517 0.2592 -0.0839 -0.0377 -0.0660 41  GLU A CA  
353  C CA  B GLU A 40  ? 0.4205 0.3502 0.2590 -0.0855 -0.0350 -0.0670 41  GLU A CA  
354  C C   A GLU A 40  ? 0.4477 0.3923 0.3135 -0.0813 -0.0313 -0.0680 41  GLU A C   
355  C C   B GLU A 40  ? 0.4476 0.3906 0.3141 -0.0809 -0.0296 -0.0668 41  GLU A C   
356  O O   A GLU A 40  ? 0.4236 0.3685 0.2988 -0.0880 -0.0172 -0.0710 41  GLU A O   
357  O O   B GLU A 40  ? 0.4241 0.3651 0.3004 -0.0859 -0.0151 -0.0675 41  GLU A O   
358  C CB  A GLU A 40  ? 0.4471 0.3538 0.2680 -0.0823 -0.0323 -0.0557 41  GLU A CB  
359  C CB  B GLU A 40  ? 0.4507 0.3566 0.2702 -0.0863 -0.0283 -0.0579 41  GLU A CB  
360  C CG  A GLU A 40  ? 0.6440 0.5314 0.4315 -0.0857 -0.0383 -0.0527 41  GLU A CG  
361  C CG  B GLU A 40  ? 0.6229 0.5124 0.4099 -0.0893 -0.0361 -0.0560 41  GLU A CG  
362  C CD  A GLU A 40  ? 1.1110 0.9893 0.8839 -0.0758 -0.0542 -0.0457 41  GLU A CD  
363  C CD  B GLU A 40  ? 1.0669 0.9472 0.8402 -0.0794 -0.0512 -0.0483 41  GLU A CD  
364  O OE1 A GLU A 40  ? 1.1153 0.9824 0.8874 -0.0718 -0.0508 -0.0381 41  GLU A OE1 
365  O OE1 B GLU A 40  ? 1.0906 0.9763 0.8558 -0.0741 -0.0682 -0.0504 41  GLU A OE1 
366  O OE2 A GLU A 40  ? 1.1234 1.0054 0.8852 -0.0719 -0.0705 -0.0481 41  GLU A OE2 
367  O OE2 B GLU A 40  ? 1.0779 0.9453 0.8485 -0.0765 -0.0462 -0.0406 41  GLU A OE2 
368  N N   . GLN A 41  ? 0.3908 0.3462 0.2690 -0.0713 -0.0415 -0.0663 42  GLN A N   
369  C CA  . GLN A 41  ? 0.3670 0.3368 0.2704 -0.0681 -0.0371 -0.0679 42  GLN A CA  
370  C C   . GLN A 41  ? 0.3996 0.3626 0.3053 -0.0591 -0.0389 -0.0588 42  GLN A C   
371  O O   . GLN A 41  ? 0.4047 0.3607 0.2988 -0.0519 -0.0505 -0.0545 42  GLN A O   
372  C CB  . GLN A 41  ? 0.3865 0.3813 0.3063 -0.0659 -0.0477 -0.0784 42  GLN A CB  
373  C CG  . GLN A 41  ? 0.5971 0.6028 0.5194 -0.0769 -0.0438 -0.0899 42  GLN A CG  
374  C CD  . GLN A 41  ? 0.8101 0.8443 0.7540 -0.0765 -0.0510 -0.1026 42  GLN A CD  
375  O OE1 . GLN A 41  ? 0.7121 0.7598 0.6709 -0.0673 -0.0596 -0.1037 42  GLN A OE1 
376  N NE2 . GLN A 41  ? 0.8200 0.8650 0.7672 -0.0873 -0.0469 -0.1140 42  GLN A NE2 
377  N N   . PHE A 42  ? 0.3290 0.2925 0.2479 -0.0594 -0.0277 -0.0559 43  PHE A N   
378  C CA  . PHE A 42  ? 0.3262 0.2848 0.2487 -0.0522 -0.0279 -0.0483 43  PHE A CA  
379  C C   . PHE A 42  ? 0.3696 0.3433 0.3134 -0.0502 -0.0247 -0.0510 43  PHE A C   
380  O O   . PHE A 42  ? 0.3752 0.3506 0.3261 -0.0560 -0.0136 -0.0527 43  PHE A O   
381  C CB  . PHE A 42  ? 0.3439 0.2858 0.2577 -0.0551 -0.0166 -0.0413 43  PHE A CB  
382  C CG  . PHE A 42  ? 0.3780 0.3036 0.2694 -0.0591 -0.0168 -0.0394 43  PHE A CG  
383  C CD1 . PHE A 42  ? 0.4036 0.3250 0.2877 -0.0675 -0.0098 -0.0436 43  PHE A CD1 
384  C CD2 . PHE A 42  ? 0.4191 0.3317 0.2951 -0.0555 -0.0229 -0.0336 43  PHE A CD2 
385  C CE1 . PHE A 42  ? 0.4359 0.3420 0.2975 -0.0725 -0.0092 -0.0426 43  PHE A CE1 
386  C CE2 . PHE A 42  ? 0.4726 0.3680 0.3245 -0.0609 -0.0221 -0.0320 43  PHE A CE2 
387  C CZ  . PHE A 42  ? 0.4487 0.3417 0.2937 -0.0695 -0.0151 -0.0367 43  PHE A CZ  
388  N N   . ARG A 43  ? 0.3245 0.3078 0.2773 -0.0424 -0.0341 -0.0520 44  ARG A N   
389  C CA  . ARG A 43  ? 0.2984 0.2963 0.2705 -0.0411 -0.0307 -0.0554 44  ARG A CA  
390  C C   . ARG A 43  ? 0.3334 0.3217 0.3051 -0.0388 -0.0239 -0.0470 44  ARG A C   
391  O O   . ARG A 43  ? 0.3238 0.2999 0.2854 -0.0344 -0.0272 -0.0405 44  ARG A O   
392  C CB  . ARG A 43  ? 0.3075 0.3219 0.2918 -0.0336 -0.0432 -0.0621 44  ARG A CB  
393  C CG  . ARG A 43  ? 0.3728 0.4026 0.3620 -0.0358 -0.0507 -0.0728 44  ARG A CG  
394  C CD  . ARG A 43  ? 0.4359 0.4903 0.4475 -0.0308 -0.0579 -0.0836 44  ARG A CD  
395  N NE  . ARG A 43  ? 0.5539 0.6165 0.5802 -0.0352 -0.0461 -0.0859 44  ARG A NE  
396  C CZ  . ARG A 43  ? 0.7205 0.7943 0.7567 -0.0456 -0.0354 -0.0938 44  ARG A CZ  
397  N NH1 . ARG A 43  ? 0.6266 0.7087 0.6636 -0.0528 -0.0353 -0.1021 44  ARG A NH1 
398  N NH2 . ARG A 43  ? 0.5115 0.5878 0.5556 -0.0495 -0.0248 -0.0941 44  ARG A NH2 
399  N N   . ALA A 44  ? 0.2887 0.2821 0.2701 -0.0421 -0.0147 -0.0476 45  ALA A N   
400  C CA  . ALA A 44  ? 0.2863 0.2726 0.2674 -0.0396 -0.0094 -0.0403 45  ALA A CA  
401  C C   . ALA A 44  ? 0.2969 0.2923 0.2888 -0.0416 -0.0033 -0.0426 45  ALA A C   
402  O O   . ALA A 44  ? 0.2720 0.2785 0.2718 -0.0460 -0.0019 -0.0503 45  ALA A O   
403  C CB  . ALA A 44  ? 0.3030 0.2745 0.2737 -0.0424 -0.0017 -0.0344 45  ALA A CB  
404  N N   . HIS A 45  ? 0.2524 0.2433 0.2439 -0.0391 0.0001  -0.0366 46  HIS A N   
405  C CA  . HIS A 45  ? 0.2356 0.2309 0.2320 -0.0414 0.0063  -0.0369 46  HIS A CA  
406  C C   . HIS A 45  ? 0.2624 0.2449 0.2506 -0.0445 0.0149  -0.0315 46  HIS A C   
407  O O   . HIS A 45  ? 0.2620 0.2355 0.2449 -0.0412 0.0153  -0.0255 46  HIS A O   
408  C CB  . HIS A 45  ? 0.2301 0.2282 0.2295 -0.0362 0.0036  -0.0339 46  HIS A CB  
409  C CG  . HIS A 45  ? 0.2575 0.2648 0.2645 -0.0316 -0.0048 -0.0388 46  HIS A CG  
410  N ND1 . HIS A 45  ? 0.2763 0.2766 0.2783 -0.0262 -0.0119 -0.0358 46  HIS A ND1 
411  C CD2 . HIS A 45  ? 0.2704 0.2921 0.2891 -0.0316 -0.0071 -0.0473 46  HIS A CD2 
412  C CE1 . HIS A 45  ? 0.2691 0.2777 0.2788 -0.0217 -0.0191 -0.0414 46  HIS A CE1 
413  N NE2 . HIS A 45  ? 0.2609 0.2845 0.2829 -0.0243 -0.0168 -0.0490 46  HIS A NE2 
414  N N   . LYS A 46  ? 0.2594 0.2404 0.2465 -0.0510 0.0222  -0.0344 47  LYS A N   
415  C CA  . LYS A 46  ? 0.2672 0.2325 0.2450 -0.0530 0.0303  -0.0292 47  LYS A CA  
416  C C   . LYS A 46  ? 0.2985 0.2583 0.2730 -0.0465 0.0296  -0.0209 47  LYS A C   
417  O O   . LYS A 46  ? 0.2734 0.2228 0.2435 -0.0430 0.0313  -0.0160 47  LYS A O   
418  C CB  . LYS A 46  ? 0.2979 0.2603 0.2726 -0.0614 0.0388  -0.0330 47  LYS A CB  
419  C CG  . LYS A 46  ? 0.3509 0.3171 0.3281 -0.0694 0.0415  -0.0419 47  LYS A CG  
420  C CD  . LYS A 46  ? 0.3400 0.3047 0.3148 -0.0795 0.0511  -0.0473 47  LYS A CD  
421  C CE  . LYS A 46  ? 0.3606 0.3336 0.3408 -0.0884 0.0535  -0.0585 47  LYS A CE  
422  N NZ  . LYS A 46  ? 0.3653 0.3376 0.3437 -0.1005 0.0645  -0.0655 47  LYS A NZ  
423  N N   . THR A 47  ? 0.2725 0.2404 0.2501 -0.0448 0.0272  -0.0206 48  THR A N   
424  C CA  . THR A 47  ? 0.2699 0.2345 0.2442 -0.0392 0.0259  -0.0138 48  THR A CA  
425  C C   . THR A 47  ? 0.2807 0.2458 0.2581 -0.0331 0.0213  -0.0110 48  THR A C   
426  O O   . THR A 47  ? 0.2741 0.2336 0.2489 -0.0288 0.0220  -0.0061 48  THR A O   
427  C CB  . THR A 47  ? 0.3086 0.2823 0.2848 -0.0397 0.0245  -0.0153 48  THR A CB  
428  O OG1 . THR A 47  ? 0.3329 0.3194 0.3193 -0.0389 0.0192  -0.0209 48  THR A OG1 
429  C CG2 . THR A 47  ? 0.3493 0.3190 0.3185 -0.0471 0.0316  -0.0173 48  THR A CG2 
430  N N   . VAL A 48  ? 0.2202 0.1915 0.2025 -0.0328 0.0167  -0.0143 49  VAL A N   
431  C CA  . VAL A 48  ? 0.2222 0.1917 0.2049 -0.0293 0.0141  -0.0124 49  VAL A CA  
432  C C   . VAL A 48  ? 0.2597 0.2197 0.2386 -0.0300 0.0184  -0.0112 49  VAL A C   
433  O O   . VAL A 48  ? 0.2422 0.2001 0.2222 -0.0268 0.0197  -0.0089 49  VAL A O   
434  C CB  . VAL A 48  ? 0.2431 0.2164 0.2272 -0.0292 0.0083  -0.0155 49  VAL A CB  
435  C CG1 . VAL A 48  ? 0.2496 0.2170 0.2301 -0.0281 0.0078  -0.0137 49  VAL A CG1 
436  C CG2 . VAL A 48  ? 0.2474 0.2296 0.2369 -0.0274 0.0047  -0.0173 49  VAL A CG2 
437  N N   . LEU A 49  ? 0.2529 0.2083 0.2285 -0.0344 0.0211  -0.0140 50  LEU A N   
438  C CA  . LEU A 49  ? 0.2514 0.1967 0.2230 -0.0358 0.0263  -0.0140 50  LEU A CA  
439  C C   . LEU A 49  ? 0.2915 0.2297 0.2629 -0.0318 0.0309  -0.0098 50  LEU A C   
440  O O   . LEU A 49  ? 0.2915 0.2259 0.2646 -0.0285 0.0330  -0.0090 50  LEU A O   
441  C CB  . LEU A 49  ? 0.2472 0.1893 0.2151 -0.0422 0.0290  -0.0186 50  LEU A CB  
442  C CG  . LEU A 49  ? 0.2776 0.2269 0.2452 -0.0451 0.0228  -0.0235 50  LEU A CG  
443  C CD1 . LEU A 49  ? 0.2821 0.2308 0.2476 -0.0520 0.0257  -0.0295 50  LEU A CD1 
444  C CD2 . LEU A 49  ? 0.3000 0.2453 0.2623 -0.0438 0.0198  -0.0225 50  LEU A CD2 
445  N N   . MET A 50  ? 0.2563 0.1925 0.2252 -0.0315 0.0320  -0.0075 51  MET A N   
446  C CA  . MET A 50  ? 0.2716 0.1978 0.2368 -0.0264 0.0346  -0.0024 51  MET A CA  
447  C C   . MET A 50  ? 0.3069 0.2406 0.2781 -0.0185 0.0298  0.0005  51  MET A C   
448  O O   . MET A 50  ? 0.3079 0.2365 0.2810 -0.0123 0.0308  0.0024  51  MET A O   
449  C CB  . MET A 50  ? 0.2992 0.2203 0.2563 -0.0290 0.0365  -0.0002 51  MET A CB  
450  C CG  . MET A 50  ? 0.3329 0.2471 0.2848 -0.0381 0.0428  -0.0045 51  MET A CG  
451  S SD  . MET A 50  ? 0.3770 0.2907 0.3211 -0.0443 0.0456  -0.0045 51  MET A SD  
452  C CE  . MET A 50  ? 0.3551 0.2437 0.2828 -0.0403 0.0502  0.0039  51  MET A CE  
453  N N   . ALA A 51  ? 0.2617 0.2083 0.2374 -0.0187 0.0247  -0.0004 52  ALA A N   
454  C CA  . ALA A 51  ? 0.2560 0.2121 0.2382 -0.0130 0.0204  0.0007  52  ALA A CA  
455  C C   . ALA A 51  ? 0.2948 0.2535 0.2842 -0.0115 0.0218  -0.0022 52  ALA A C   
456  O O   . ALA A 51  ? 0.2916 0.2578 0.2882 -0.0064 0.0198  -0.0025 52  ALA A O   
457  C CB  . ALA A 51  ? 0.2549 0.2223 0.2393 -0.0153 0.0161  -0.0009 52  ALA A CB  
458  N N   . CYS A 52  ? 0.2392 0.1928 0.2265 -0.0167 0.0252  -0.0054 53  CYS A N   
459  C CA  . CYS A 52  ? 0.2566 0.2110 0.2477 -0.0179 0.0282  -0.0091 53  CYS A CA  
460  C C   . CYS A 52  ? 0.3013 0.2468 0.2927 -0.0171 0.0344  -0.0108 53  CYS A C   
461  O O   . CYS A 52  ? 0.2780 0.2258 0.2743 -0.0178 0.0379  -0.0149 53  CYS A O   
462  C CB  . CYS A 52  ? 0.2518 0.2051 0.2370 -0.0245 0.0272  -0.0115 53  CYS A CB  
463  S SG  . CYS A 52  ? 0.2716 0.2335 0.2576 -0.0247 0.0207  -0.0108 53  CYS A SG  
464  N N   . SER A 53  ? 0.2713 0.2059 0.2567 -0.0177 0.0370  -0.0091 54  SER A N   
465  C CA  . SER A 53  ? 0.2716 0.1951 0.2553 -0.0187 0.0439  -0.0118 54  SER A CA  
466  C C   . SER A 53  ? 0.3253 0.2369 0.3064 -0.0133 0.0460  -0.0082 54  SER A C   
467  O O   . SER A 53  ? 0.3112 0.2170 0.2843 -0.0155 0.0453  -0.0050 54  SER A O   
468  C CB  . SER A 53  ? 0.2885 0.2071 0.2633 -0.0280 0.0459  -0.0148 54  SER A CB  
469  O OG  . SER A 53  ? 0.3326 0.2386 0.3026 -0.0311 0.0525  -0.0172 54  SER A OG  
470  N N   . GLY A 54  ? 0.2990 0.2053 0.2858 -0.0067 0.0495  -0.0095 55  GLY A N   
471  C CA  . GLY A 54  ? 0.3046 0.1943 0.2866 -0.0004 0.0517  -0.0058 55  GLY A CA  
472  C C   . GLY A 54  ? 0.3481 0.2212 0.3181 -0.0089 0.0586  -0.0068 55  GLY A C   
473  O O   . GLY A 54  ? 0.3481 0.2063 0.3077 -0.0084 0.0600  -0.0024 55  GLY A O   
474  N N   . LEU A 55  ? 0.3218 0.1971 0.2915 -0.0179 0.0630  -0.0131 56  LEU A N   
475  C CA  . LEU A 55  ? 0.3265 0.1893 0.2859 -0.0273 0.0692  -0.0159 56  LEU A CA  
476  C C   . LEU A 55  ? 0.3650 0.2315 0.3176 -0.0337 0.0660  -0.0139 56  LEU A C   
477  O O   . LEU A 55  ? 0.3405 0.1935 0.2844 -0.0374 0.0706  -0.0130 56  LEU A O   
478  C CB  . LEU A 55  ? 0.3204 0.1865 0.2797 -0.0355 0.0732  -0.0235 56  LEU A CB  
479  C CG  . LEU A 55  ? 0.4006 0.2554 0.3503 -0.0457 0.0797  -0.0282 56  LEU A CG  
480  C CD1 . LEU A 55  ? 0.4288 0.2626 0.3758 -0.0430 0.0888  -0.0291 56  LEU A CD1 
481  C CD2 . LEU A 55  ? 0.3939 0.2554 0.3408 -0.0543 0.0802  -0.0349 56  LEU A CD2 
482  N N   . PHE A 56  ? 0.3063 0.1899 0.2629 -0.0352 0.0589  -0.0138 57  PHE A N   
483  C CA  . PHE A 56  ? 0.2874 0.1770 0.2407 -0.0405 0.0560  -0.0136 57  PHE A CA  
484  C C   . PHE A 56  ? 0.3315 0.2146 0.2804 -0.0364 0.0557  -0.0076 57  PHE A C   
485  O O   . PHE A 56  ? 0.3230 0.2017 0.2653 -0.0428 0.0588  -0.0084 57  PHE A O   
486  C CB  . PHE A 56  ? 0.2929 0.2003 0.2514 -0.0418 0.0483  -0.0154 57  PHE A CB  
487  C CG  . PHE A 56  ? 0.2954 0.2056 0.2523 -0.0479 0.0481  -0.0213 57  PHE A CG  
488  C CD1 . PHE A 56  ? 0.3243 0.2312 0.2767 -0.0561 0.0517  -0.0268 57  PHE A CD1 
489  C CD2 . PHE A 56  ? 0.3024 0.2179 0.2603 -0.0465 0.0443  -0.0218 57  PHE A CD2 
490  C CE1 . PHE A 56  ? 0.3254 0.2349 0.2743 -0.0616 0.0504  -0.0323 57  PHE A CE1 
491  C CE2 . PHE A 56  ? 0.3345 0.2499 0.2865 -0.0524 0.0435  -0.0264 57  PHE A CE2 
492  C CZ  . PHE A 56  ? 0.3059 0.2189 0.2535 -0.0593 0.0457  -0.0315 57  PHE A CZ  
493  N N   . TYR A 57  ? 0.3097 0.1919 0.2614 -0.0263 0.0524  -0.0023 58  TYR A N   
494  C CA  . TYR A 57  ? 0.3261 0.1997 0.2700 -0.0214 0.0509  0.0044  58  TYR A CA  
495  C C   . TYR A 57  ? 0.3832 0.2319 0.3135 -0.0243 0.0592  0.0060  58  TYR A C   
496  O O   . TYR A 57  ? 0.3660 0.2056 0.2844 -0.0293 0.0618  0.0084  58  TYR A O   
497  C CB  . TYR A 57  ? 0.3500 0.2278 0.3005 -0.0089 0.0450  0.0085  58  TYR A CB  
498  C CG  . TYR A 57  ? 0.4104 0.2767 0.3502 -0.0020 0.0421  0.0161  58  TYR A CG  
499  C CD1 . TYR A 57  ? 0.4282 0.2983 0.3601 -0.0055 0.0392  0.0190  58  TYR A CD1 
500  C CD2 . TYR A 57  ? 0.4720 0.3224 0.4084 0.0085  0.0420  0.0201  58  TYR A CD2 
501  C CE1 . TYR A 57  ? 0.4547 0.3121 0.3727 0.0002  0.0363  0.0264  58  TYR A CE1 
502  C CE2 . TYR A 57  ? 0.5215 0.3586 0.4445 0.0159  0.0378  0.0280  58  TYR A CE2 
503  C CZ  . TYR A 57  ? 0.6075 0.4479 0.5201 0.0113  0.0349  0.0315  58  TYR A CZ  
504  O OH  . TYR A 57  ? 0.6843 0.5097 0.5802 0.0182  0.0305  0.0397  58  TYR A OH  
505  N N   A SER A 58  ? 0.3629 0.1994 0.2940 -0.0221 0.0642  0.0040  59  SER A N   
506  N N   B SER A 58  ? 0.3626 0.1992 0.2937 -0.0221 0.0642  0.0040  59  SER A N   
507  C CA  A SER A 58  ? 0.3837 0.1935 0.3015 -0.0250 0.0731  0.0048  59  SER A CA  
508  C CA  B SER A 58  ? 0.3844 0.1943 0.3023 -0.0250 0.0731  0.0047  59  SER A CA  
509  C C   A SER A 58  ? 0.4521 0.2599 0.3630 -0.0405 0.0802  -0.0011 59  SER A C   
510  C C   B SER A 58  ? 0.4505 0.2588 0.3616 -0.0405 0.0800  -0.0010 59  SER A C   
511  O O   A SER A 58  ? 0.4805 0.2698 0.3767 -0.0459 0.0864  0.0009  59  SER A O   
512  O O   B SER A 58  ? 0.4765 0.2667 0.3729 -0.0458 0.0859  0.0011  59  SER A O   
513  C CB  A SER A 58  ? 0.4165 0.2166 0.3396 -0.0196 0.0773  0.0018  59  SER A CB  
514  C CB  B SER A 58  ? 0.4196 0.2205 0.3431 -0.0204 0.0776  0.0013  59  SER A CB  
515  O OG  A SER A 58  ? 0.4508 0.2502 0.3800 -0.0045 0.0716  0.0066  59  SER A OG  
516  O OG  B SER A 58  ? 0.4971 0.2697 0.4070 -0.0233 0.0868  0.0016  59  SER A OG  
517  N N   . ILE A 59  ? 0.3953 0.2223 0.3162 -0.0477 0.0791  -0.0088 60  ILE A N   
518  C CA  . ILE A 59  ? 0.3848 0.2163 0.3034 -0.0617 0.0838  -0.0165 60  ILE A CA  
519  C C   . ILE A 59  ? 0.4212 0.2588 0.3361 -0.0669 0.0830  -0.0158 60  ILE A C   
520  O O   . ILE A 59  ? 0.4509 0.2769 0.3562 -0.0769 0.0915  -0.0189 60  ILE A O   
521  C CB  . ILE A 59  ? 0.4042 0.2567 0.3337 -0.0659 0.0794  -0.0241 60  ILE A CB  
522  C CG1 . ILE A 59  ? 0.4067 0.2514 0.3370 -0.0647 0.0831  -0.0271 60  ILE A CG1 
523  C CG2 . ILE A 59  ? 0.3868 0.2501 0.3170 -0.0786 0.0812  -0.0330 60  ILE A CG2 
524  C CD1 . ILE A 59  ? 0.4246 0.2871 0.3612 -0.0673 0.0774  -0.0324 60  ILE A CD1 
525  N N   . PHE A 60  ? 0.3572 0.2126 0.2795 -0.0614 0.0741  -0.0130 61  PHE A N   
526  C CA  . PHE A 60  ? 0.3526 0.2167 0.2735 -0.0675 0.0741  -0.0146 61  PHE A CA  
527  C C   . PHE A 60  ? 0.4187 0.2647 0.3241 -0.0659 0.0774  -0.0070 61  PHE A C   
528  O O   . PHE A 60  ? 0.4378 0.2891 0.3398 -0.0727 0.0794  -0.0091 61  PHE A O   
529  C CB  . PHE A 60  ? 0.3374 0.2277 0.2722 -0.0642 0.0643  -0.0168 61  PHE A CB  
530  C CG  . PHE A 60  ? 0.3366 0.2411 0.2818 -0.0670 0.0609  -0.0243 61  PHE A CG  
531  C CD1 . PHE A 60  ? 0.3725 0.2820 0.3194 -0.0775 0.0651  -0.0337 61  PHE A CD1 
532  C CD2 . PHE A 60  ? 0.3364 0.2493 0.2884 -0.0596 0.0533  -0.0225 61  PHE A CD2 
533  C CE1 . PHE A 60  ? 0.3765 0.2985 0.3307 -0.0793 0.0602  -0.0403 61  PHE A CE1 
534  C CE2 . PHE A 60  ? 0.3684 0.2909 0.3253 -0.0623 0.0497  -0.0284 61  PHE A CE2 
535  C CZ  . PHE A 60  ? 0.3553 0.2824 0.3129 -0.0714 0.0523  -0.0369 61  PHE A CZ  
536  N N   . THR A 61  ? 0.4038 0.2279 0.2990 -0.0572 0.0782  0.0012  62  THR A N   
537  C CA  . THR A 61  ? 0.4218 0.2227 0.2969 -0.0556 0.0811  0.0093  62  THR A CA  
538  C C   . THR A 61  ? 0.5115 0.2836 0.3698 -0.0646 0.0935  0.0082  62  THR A C   
539  O O   . THR A 61  ? 0.5228 0.2693 0.3591 -0.0662 0.0983  0.0145  62  THR A O   
540  C CB  . THR A 61  ? 0.5219 0.3159 0.3943 -0.0394 0.0726  0.0192  62  THR A CB  
541  O OG1 . THR A 61  ? 0.4906 0.2788 0.3707 -0.0313 0.0722  0.0190  62  THR A OG1 
542  C CG2 . THR A 61  ? 0.4680 0.2877 0.3523 -0.0332 0.0619  0.0204  62  THR A CG2 
543  N N   . ASP A 62  ? 0.4627 0.2370 0.3288 -0.0714 0.0991  -0.0001 63  ASP A N   
544  C CA  . ASP A 62  ? 0.4885 0.2365 0.3396 -0.0822 0.1122  -0.0033 63  ASP A CA  
545  C C   . ASP A 62  ? 0.5670 0.3203 0.4126 -0.0989 0.1199  -0.0104 63  ASP A C   
546  O O   . ASP A 62  ? 0.5292 0.3130 0.3920 -0.1045 0.1164  -0.0191 63  ASP A O   
547  C CB  . ASP A 62  ? 0.4959 0.2471 0.3575 -0.0854 0.1157  -0.0115 63  ASP A CB  
548  C CG  . ASP A 62  ? 0.6428 0.3688 0.4899 -0.0988 0.1302  -0.0168 63  ASP A CG  
549  O OD1 . ASP A 62  ? 0.7110 0.4039 0.5424 -0.0939 0.1358  -0.0106 63  ASP A OD1 
550  O OD2 . ASP A 62  ? 0.6548 0.3939 0.5062 -0.1141 0.1360  -0.0277 63  ASP A OD2 
551  N N   . GLN A 63  ? 0.6082 0.3307 0.4296 -0.1071 0.1308  -0.0074 64  GLN A N   
552  C CA  . GLN A 63  ? 0.6265 0.3504 0.4397 -0.1247 0.1408  -0.0145 64  GLN A CA  
553  C C   . GLN A 63  ? 0.6484 0.3948 0.4783 -0.1402 0.1473  -0.0311 64  GLN A C   
554  O O   . GLN A 63  ? 0.6628 0.4264 0.4974 -0.1524 0.1516  -0.0401 64  GLN A O   
555  C CB  . GLN A 63  ? 0.7023 0.3822 0.4817 -0.1313 0.1529  -0.0076 64  GLN A CB  
556  C CG  . GLN A 63  ? 0.9355 0.5991 0.6964 -0.1190 0.1455  0.0071  64  GLN A CG  
557  N N   . LEU A 64  ? 0.5477 0.2953 0.3867 -0.1400 0.1479  -0.0363 65  LEU A N   
558  C CA  . LEU A 64  ? 0.5313 0.3033 0.3869 -0.1531 0.1513  -0.0523 65  LEU A CA  
559  C C   . LEU A 64  ? 0.5574 0.3666 0.4385 -0.1442 0.1365  -0.0560 65  LEU A C   
560  O O   . LEU A 64  ? 0.5595 0.3984 0.4566 -0.1513 0.1338  -0.0673 65  LEU A O   
561  C CB  . LEU A 64  ? 0.5553 0.3061 0.4034 -0.1611 0.1619  -0.0577 65  LEU A CB  
562  C CG  . LEU A 64  ? 0.6602 0.3779 0.4853 -0.1771 0.1799  -0.0605 65  LEU A CG  
563  C CD1 . LEU A 64  ? 0.6726 0.3702 0.4922 -0.1829 0.1890  -0.0658 65  LEU A CD1 
564  C CD2 . LEU A 64  ? 0.7180 0.4552 0.5483 -0.1964 0.1881  -0.0745 65  LEU A CD2 
565  N N   . LYS A 65  ? 0.4680 0.2751 0.3526 -0.1289 0.1273  -0.0476 66  LYS A N   
566  C CA  . LYS A 65  ? 0.4397 0.2762 0.3437 -0.1217 0.1147  -0.0506 66  LYS A CA  
567  C C   . LYS A 65  ? 0.4921 0.3522 0.4069 -0.1154 0.1043  -0.0484 66  LYS A C   
568  O O   . LYS A 65  ? 0.4712 0.3573 0.4016 -0.1136 0.0953  -0.0542 66  LYS A O   
569  C CB  . LYS A 65  ? 0.4464 0.2736 0.3507 -0.1098 0.1102  -0.0441 66  LYS A CB  
570  C CG  . LYS A 65  ? 0.4678 0.2735 0.3637 -0.1159 0.1204  -0.0482 66  LYS A CG  
571  C CD  . LYS A 65  ? 0.4419 0.2436 0.3415 -0.1039 0.1157  -0.0435 66  LYS A CD  
572  C CE  . LYS A 65  ? 0.5420 0.3183 0.4326 -0.1072 0.1264  -0.0461 66  LYS A CE  
573  N NZ  . LYS A 65  ? 0.5513 0.2941 0.4261 -0.1034 0.1342  -0.0382 66  LYS A NZ  
574  N N   . CYS A 66  ? 0.4861 0.3359 0.3911 -0.1126 0.1056  -0.0407 67  CYS A N   
575  C CA  . CYS A 66  ? 0.4708 0.3414 0.3848 -0.1077 0.0973  -0.0393 67  CYS A CA  
576  C C   . CYS A 66  ? 0.5155 0.4143 0.4452 -0.1172 0.0967  -0.0529 67  CYS A C   
577  O O   . CYS A 66  ? 0.5087 0.4298 0.4518 -0.1113 0.0873  -0.0543 67  CYS A O   
578  C CB  . CYS A 66  ? 0.5073 0.3603 0.4046 -0.1062 0.1007  -0.0304 67  CYS A CB  
579  S SG  . CYS A 66  ? 0.5961 0.4304 0.4751 -0.1249 0.1176  -0.0360 67  CYS A SG  
580  N N   . ASN A 67  ? 0.4627 0.3602 0.3912 -0.1318 0.1071  -0.0638 68  ASN A N   
581  C CA  . ASN A 67  ? 0.4558 0.3811 0.4006 -0.1421 0.1080  -0.0792 68  ASN A CA  
582  C C   . ASN A 67  ? 0.4839 0.4310 0.4451 -0.1421 0.1004  -0.0891 68  ASN A C   
583  O O   . ASN A 67  ? 0.4601 0.4335 0.4375 -0.1488 0.0989  -0.1031 68  ASN A O   
584  C CB  . ASN A 67  ? 0.4954 0.4089 0.4295 -0.1600 0.1247  -0.0871 68  ASN A CB  
585  C CG  . ASN A 67  ? 0.6814 0.5783 0.5992 -0.1611 0.1307  -0.0791 68  ASN A CG  
586  O OD1 . ASN A 67  ? 0.6962 0.5631 0.5913 -0.1699 0.1434  -0.0753 68  ASN A OD1 
587  N ND2 . ASN A 67  ? 0.5648 0.4778 0.4910 -0.1519 0.1214  -0.0756 68  ASN A ND2 
588  N N   . LEU A 68  ? 0.4552 0.3923 0.4123 -0.1345 0.0954  -0.0828 69  LEU A N   
589  C CA  . LEU A 68  ? 0.4320 0.3865 0.3999 -0.1347 0.0878  -0.0912 69  LEU A CA  
590  C C   . LEU A 68  ? 0.4498 0.4275 0.4314 -0.1230 0.0720  -0.0904 69  LEU A C   
591  O O   . LEU A 68  ? 0.4330 0.4053 0.4120 -0.1120 0.0666  -0.0794 69  LEU A O   
592  C CB  . LEU A 68  ? 0.4432 0.3772 0.3997 -0.1323 0.0897  -0.0856 69  LEU A CB  
593  C CG  . LEU A 68  ? 0.5163 0.4241 0.4584 -0.1433 0.1054  -0.0872 69  LEU A CG  
594  C CD1 . LEU A 68  ? 0.5280 0.4160 0.4610 -0.1381 0.1065  -0.0812 69  LEU A CD1 
595  C CD2 . LEU A 68  ? 0.5378 0.4584 0.4858 -0.1600 0.1125  -0.1039 69  LEU A CD2 
596  N N   A SER A 69  ? 0.4009 0.4037 0.3965 -0.1250 0.0640  -0.1022 70  SER A N   
597  N N   B SER A 69  ? 0.4004 0.4032 0.3960 -0.1251 0.0641  -0.1023 70  SER A N   
598  C CA  A SER A 69  ? 0.3851 0.4072 0.3919 -0.1132 0.0480  -0.1019 70  SER A CA  
599  C CA  B SER A 69  ? 0.3847 0.4074 0.3918 -0.1136 0.0481  -0.1024 70  SER A CA  
600  C C   A SER A 69  ? 0.3989 0.4161 0.3988 -0.1072 0.0390  -0.0979 70  SER A C   
601  C C   B SER A 69  ? 0.3992 0.4168 0.3993 -0.1074 0.0390  -0.0982 70  SER A C   
602  O O   A SER A 69  ? 0.3695 0.3944 0.3723 -0.0968 0.0261  -0.0947 70  SER A O   
603  O O   B SER A 69  ? 0.3697 0.3953 0.3729 -0.0970 0.0260  -0.0951 70  SER A O   
604  C CB  A SER A 69  ? 0.4301 0.4829 0.4566 -0.1167 0.0429  -0.1173 70  SER A CB  
605  C CB  B SER A 69  ? 0.4290 0.4823 0.4556 -0.1176 0.0432  -0.1182 70  SER A CB  
606  O OG  A SER A 69  ? 0.5352 0.5981 0.5656 -0.1270 0.0450  -0.1301 70  SER A OG  
607  O OG  B SER A 69  ? 0.5245 0.5837 0.5579 -0.1228 0.0515  -0.1222 70  SER A OG  
608  N N   . VAL A 70  ? 0.3658 0.3686 0.3550 -0.1146 0.0466  -0.0988 71  VAL A N   
609  C CA  . VAL A 70  ? 0.3616 0.3573 0.3413 -0.1117 0.0410  -0.0963 71  VAL A CA  
610  C C   . VAL A 70  ? 0.3912 0.3592 0.3568 -0.1133 0.0525  -0.0881 71  VAL A C   
611  O O   . VAL A 70  ? 0.3959 0.3519 0.3576 -0.1222 0.0654  -0.0909 71  VAL A O   
612  C CB  . VAL A 70  ? 0.4202 0.4314 0.4033 -0.1199 0.0370  -0.1100 71  VAL A CB  
613  C CG1 . VAL A 70  ? 0.4334 0.4345 0.4027 -0.1184 0.0324  -0.1072 71  VAL A CG1 
614  C CG2 . VAL A 70  ? 0.4116 0.4526 0.4114 -0.1163 0.0239  -0.1194 71  VAL A CG2 
615  N N   . ILE A 71  ? 0.3111 0.2684 0.2691 -0.1048 0.0483  -0.0789 72  ILE A N   
616  C CA  . ILE A 71  ? 0.3238 0.2580 0.2713 -0.1042 0.0576  -0.0725 72  ILE A CA  
617  C C   . ILE A 71  ? 0.3762 0.3078 0.3156 -0.1049 0.0540  -0.0743 72  ILE A C   
618  O O   . ILE A 71  ? 0.3658 0.3038 0.3037 -0.0985 0.0436  -0.0709 72  ILE A O   
619  C CB  . ILE A 71  ? 0.3454 0.2693 0.2926 -0.0940 0.0585  -0.0606 72  ILE A CB  
620  C CG1 . ILE A 71  ? 0.3638 0.2876 0.3149 -0.0945 0.0626  -0.0585 72  ILE A CG1 
621  C CG2 . ILE A 71  ? 0.3703 0.2736 0.3098 -0.0914 0.0661  -0.0555 72  ILE A CG2 
622  C CD1 . ILE A 71  ? 0.4225 0.3304 0.3671 -0.1038 0.0760  -0.0616 72  ILE A CD1 
623  N N   . ASN A 72  ? 0.3571 0.2764 0.2892 -0.1129 0.0635  -0.0791 73  ASN A N   
624  C CA  . ASN A 72  ? 0.3659 0.2808 0.2881 -0.1158 0.0625  -0.0821 73  ASN A CA  
625  C C   . ASN A 72  ? 0.4042 0.3000 0.3209 -0.1110 0.0703  -0.0753 73  ASN A C   
626  O O   . ASN A 72  ? 0.3929 0.2733 0.3096 -0.1122 0.0817  -0.0747 73  ASN A O   
627  C CB  . ASN A 72  ? 0.4203 0.3353 0.3384 -0.1288 0.0687  -0.0941 73  ASN A CB  
628  C CG  . ASN A 72  ? 0.6230 0.5600 0.5495 -0.1346 0.0620  -0.1036 73  ASN A CG  
629  O OD1 . ASN A 72  ? 0.4886 0.4432 0.4179 -0.1303 0.0479  -0.1049 73  ASN A OD1 
630  N ND2 . ASN A 72  ? 0.5696 0.5053 0.4999 -0.1446 0.0721  -0.1113 73  ASN A ND2 
631  N N   . LEU A 73  ? 0.3489 0.2450 0.2608 -0.1057 0.0644  -0.0710 74  LEU A N   
632  C CA  . LEU A 73  ? 0.3407 0.2226 0.2501 -0.1019 0.0722  -0.0670 74  LEU A CA  
633  C C   . LEU A 73  ? 0.4096 0.2807 0.3093 -0.1105 0.0809  -0.0745 74  LEU A C   
634  O O   . LEU A 73  ? 0.4087 0.2846 0.3006 -0.1193 0.0784  -0.0820 74  LEU A O   
635  C CB  . LEU A 73  ? 0.3281 0.2137 0.2359 -0.0949 0.0649  -0.0606 74  LEU A CB  
636  C CG  . LEU A 73  ? 0.3677 0.2631 0.2846 -0.0861 0.0567  -0.0534 74  LEU A CG  
637  C CD1 . LEU A 73  ? 0.3717 0.2661 0.2867 -0.0807 0.0539  -0.0481 74  LEU A CD1 
638  C CD2 . LEU A 73  ? 0.3491 0.2418 0.2764 -0.0819 0.0618  -0.0500 74  LEU A CD2 
639  N N   . ASP A 74  ? 0.3777 0.2353 0.2786 -0.1076 0.0909  -0.0734 75  ASP A N   
640  C CA  . ASP A 74  ? 0.3962 0.2421 0.2892 -0.1150 0.1012  -0.0811 75  ASP A CA  
641  C C   . ASP A 74  ? 0.4498 0.3016 0.3283 -0.1222 0.0953  -0.0852 75  ASP A C   
642  O O   . ASP A 74  ? 0.4395 0.2974 0.3151 -0.1177 0.0870  -0.0798 75  ASP A O   
643  C CB  . ASP A 74  ? 0.4190 0.2542 0.3189 -0.1075 0.1100  -0.0788 75  ASP A CB  
644  C CG  . ASP A 74  ? 0.5404 0.3622 0.4355 -0.1136 0.1229  -0.0876 75  ASP A CG  
645  O OD1 . ASP A 74  ? 0.5534 0.3766 0.4374 -0.1214 0.1238  -0.0931 75  ASP A OD1 
646  O OD2 . ASP A 74  ? 0.5397 0.3479 0.4410 -0.1106 0.1323  -0.0890 75  ASP A OD2 
647  N N   . PRO A 75  ? 0.4590 0.3075 0.3265 -0.1335 0.0992  -0.0946 76  PRO A N   
648  C CA  . PRO A 75  ? 0.4779 0.3302 0.3275 -0.1402 0.0921  -0.0979 76  PRO A CA  
649  C C   . PRO A 75  ? 0.5250 0.3695 0.3655 -0.1395 0.0958  -0.0957 76  PRO A C   
650  O O   . PRO A 75  ? 0.5359 0.3814 0.3590 -0.1433 0.0880  -0.0952 76  PRO A O   
651  C CB  . PRO A 75  ? 0.5198 0.3689 0.3604 -0.1530 0.0980  -0.1094 76  PRO A CB  
652  C CG  . PRO A 75  ? 0.5813 0.4193 0.4338 -0.1532 0.1121  -0.1124 76  PRO A CG  
653  C CD  . PRO A 75  ? 0.4958 0.3357 0.3643 -0.1412 0.1098  -0.1027 76  PRO A CD  
654  N N   . GLU A 76  ? 0.4824 0.3189 0.3338 -0.1346 0.1072  -0.0948 77  GLU A N   
655  C CA  . GLU A 76  ? 0.5089 0.3403 0.3553 -0.1348 0.1128  -0.0948 77  GLU A CA  
656  C C   . GLU A 76  ? 0.5020 0.3407 0.3498 -0.1273 0.1026  -0.0854 77  GLU A C   
657  O O   . GLU A 76  ? 0.4936 0.3288 0.3323 -0.1298 0.1050  -0.0852 77  GLU A O   
658  C CB  . GLU A 76  ? 0.5402 0.3644 0.4028 -0.1302 0.1273  -0.0983 77  GLU A CB  
659  C CG  . GLU A 76  ? 0.7992 0.6175 0.6560 -0.1356 0.1384  -0.1051 77  GLU A CG  
660  C CD  . GLU A 76  ? 1.1602 0.9686 1.0033 -0.1482 0.1485  -0.1163 77  GLU A CD  
661  O OE1 . GLU A 76  ? 1.1663 0.9676 1.0190 -0.1475 0.1576  -0.1218 77  GLU A OE1 
662  O OE2 . GLU A 76  ? 1.0867 0.8926 0.9076 -0.1589 0.1476  -0.1196 77  GLU A OE2 
663  N N   . ILE A 77  ? 0.4282 0.2761 0.2866 -0.1192 0.0925  -0.0784 78  ILE A N   
664  C CA  . ILE A 77  ? 0.4031 0.2573 0.2641 -0.1119 0.0836  -0.0701 78  ILE A CA  
665  C C   . ILE A 77  ? 0.4598 0.3132 0.2997 -0.1161 0.0727  -0.0681 78  ILE A C   
666  O O   . ILE A 77  ? 0.4602 0.3172 0.2914 -0.1191 0.0639  -0.0697 78  ILE A O   
667  C CB  . ILE A 77  ? 0.4216 0.2852 0.3005 -0.1021 0.0775  -0.0640 78  ILE A CB  
668  C CG1 . ILE A 77  ? 0.4305 0.2903 0.3261 -0.0969 0.0878  -0.0648 78  ILE A CG1 
669  C CG2 . ILE A 77  ? 0.4005 0.2705 0.2819 -0.0951 0.0685  -0.0563 78  ILE A CG2 
670  C CD1 . ILE A 77  ? 0.4807 0.3373 0.3847 -0.0927 0.0967  -0.0657 78  ILE A CD1 
671  N N   . ASN A 78  ? 0.4659 0.3144 0.2978 -0.1160 0.0732  -0.0647 79  ASN A N   
672  C CA  . ASN A 78  ? 0.4858 0.3276 0.2937 -0.1194 0.0638  -0.0613 79  ASN A CA  
673  C C   . ASN A 78  ? 0.4853 0.3348 0.2983 -0.1100 0.0490  -0.0536 79  ASN A C   
674  O O   . ASN A 78  ? 0.4494 0.3046 0.2789 -0.1028 0.0498  -0.0493 79  ASN A O   
675  C CB  . ASN A 78  ? 0.5264 0.3573 0.3235 -0.1246 0.0731  -0.0617 79  ASN A CB  
676  C CG  . ASN A 78  ? 0.6966 0.5148 0.4647 -0.1286 0.0648  -0.0570 79  ASN A CG  
677  O OD1 . ASN A 78  ? 0.5891 0.4053 0.3569 -0.1242 0.0607  -0.0510 79  ASN A OD1 
678  N ND2 . ASN A 78  ? 0.6284 0.4360 0.3697 -0.1370 0.0619  -0.0598 79  ASN A ND2 
679  N N   . PRO A 79  ? 0.4676 0.3183 0.2674 -0.1095 0.0350  -0.0525 80  PRO A N   
680  C CA  . PRO A 79  ? 0.4514 0.3101 0.2581 -0.0997 0.0212  -0.0465 80  PRO A CA  
681  C C   . PRO A 79  ? 0.4871 0.3367 0.2871 -0.0959 0.0195  -0.0394 80  PRO A C   
682  O O   . PRO A 79  ? 0.4587 0.3166 0.2746 -0.0876 0.0151  -0.0353 80  PRO A O   
683  C CB  . PRO A 79  ? 0.4990 0.3592 0.2900 -0.1004 0.0069  -0.0485 80  PRO A CB  
684  C CG  . PRO A 79  ? 0.5632 0.4225 0.3478 -0.1105 0.0143  -0.0568 80  PRO A CG  
685  C CD  . PRO A 79  ? 0.5163 0.3629 0.2959 -0.1172 0.0306  -0.0577 80  PRO A CD  
686  N N   . GLU A 80  ? 0.4644 0.2963 0.2403 -0.1033 0.0242  -0.0386 81  GLU A N   
687  C CA  . GLU A 80  ? 0.4643 0.2852 0.2318 -0.1020 0.0247  -0.0329 81  GLU A CA  
688  C C   . GLU A 80  ? 0.4759 0.3069 0.2695 -0.0995 0.0361  -0.0337 81  GLU A C   
689  O O   . GLU A 80  ? 0.4491 0.2834 0.2516 -0.0932 0.0321  -0.0292 81  GLU A O   
690  C CB  . GLU A 80  ? 0.5122 0.3098 0.2454 -0.1126 0.0291  -0.0326 81  GLU A CB  
691  C CG  . GLU A 80  ? 0.6059 0.3897 0.3278 -0.1119 0.0288  -0.0267 81  GLU A CG  
692  C CD  . GLU A 80  ? 0.9036 0.6621 0.5922 -0.1242 0.0372  -0.0265 81  GLU A CD  
693  O OE1 . GLU A 80  ? 0.8780 0.6181 0.5456 -0.1236 0.0316  -0.0201 81  GLU A OE1 
694  O OE2 . GLU A 80  ? 0.8127 0.5685 0.4954 -0.1350 0.0503  -0.0333 81  GLU A OE2 
695  N N   . GLY A 81  ? 0.4384 0.2744 0.2440 -0.1038 0.0492  -0.0398 82  GLY A N   
696  C CA  . GLY A 81  ? 0.4182 0.2654 0.2498 -0.0997 0.0582  -0.0412 82  GLY A CA  
697  C C   . GLY A 81  ? 0.4213 0.2832 0.2749 -0.0888 0.0503  -0.0372 82  GLY A C   
698  O O   . GLY A 81  ? 0.3918 0.2608 0.2594 -0.0834 0.0505  -0.0347 82  GLY A O   
699  N N   . PHE A 82  ? 0.3674 0.2345 0.2235 -0.0865 0.0436  -0.0376 83  PHE A N   
700  C CA  . PHE A 82  ? 0.3326 0.2129 0.2073 -0.0779 0.0370  -0.0347 83  PHE A CA  
701  C C   . PHE A 82  ? 0.3748 0.2560 0.2464 -0.0726 0.0264  -0.0293 83  PHE A C   
702  O O   . PHE A 82  ? 0.3443 0.2337 0.2309 -0.0665 0.0256  -0.0266 83  PHE A O   
703  C CB  . PHE A 82  ? 0.3467 0.2328 0.2239 -0.0788 0.0332  -0.0381 83  PHE A CB  
704  C CG  . PHE A 82  ? 0.3368 0.2355 0.2326 -0.0719 0.0294  -0.0361 83  PHE A CG  
705  C CD1 . PHE A 82  ? 0.3610 0.2626 0.2720 -0.0689 0.0373  -0.0356 83  PHE A CD1 
706  C CD2 . PHE A 82  ? 0.3480 0.2544 0.2452 -0.0675 0.0178  -0.0345 83  PHE A CD2 
707  C CE1 . PHE A 82  ? 0.3616 0.2722 0.2858 -0.0635 0.0343  -0.0332 83  PHE A CE1 
708  C CE2 . PHE A 82  ? 0.3567 0.2746 0.2703 -0.0623 0.0157  -0.0335 83  PHE A CE2 
709  C CZ  . PHE A 82  ? 0.3397 0.2589 0.2653 -0.0610 0.0243  -0.0325 83  PHE A CZ  
710  N N   . CYS A 83  ? 0.3940 0.2655 0.2451 -0.0745 0.0180  -0.0279 84  CYS A N   
711  C CA  . CYS A 83  ? 0.4107 0.2789 0.2562 -0.0687 0.0075  -0.0229 84  CYS A CA  
712  C C   . CYS A 83  ? 0.4257 0.2897 0.2743 -0.0685 0.0136  -0.0201 84  CYS A C   
713  O O   . CYS A 83  ? 0.3929 0.2635 0.2528 -0.0619 0.0089  -0.0174 84  CYS A O   
714  C CB  . CYS A 83  ? 0.4618 0.3149 0.2800 -0.0707 -0.0019 -0.0215 84  CYS A CB  
715  S SG  . CYS A 83  ? 0.5339 0.3807 0.3449 -0.0611 -0.0171 -0.0157 84  CYS A SG  
716  N N   . ILE A 84  ? 0.3912 0.2460 0.2312 -0.0764 0.0248  -0.0221 85  ILE A N   
717  C CA  . ILE A 84  ? 0.3738 0.2265 0.2174 -0.0785 0.0324  -0.0219 85  ILE A CA  
718  C C   . ILE A 84  ? 0.3600 0.2322 0.2327 -0.0718 0.0348  -0.0227 85  ILE A C   
719  O O   . ILE A 84  ? 0.3548 0.2312 0.2353 -0.0686 0.0334  -0.0209 85  ILE A O   
720  C CB  . ILE A 84  ? 0.4228 0.2652 0.2542 -0.0895 0.0454  -0.0266 85  ILE A CB  
721  C CG1 . ILE A 84  ? 0.4532 0.2711 0.2488 -0.0969 0.0423  -0.0241 85  ILE A CG1 
722  C CG2 . ILE A 84  ? 0.4226 0.2715 0.2678 -0.0919 0.0557  -0.0299 85  ILE A CG2 
723  C CD1 . ILE A 84  ? 0.5509 0.3572 0.3297 -0.1095 0.0549  -0.0296 85  ILE A CD1 
724  N N   . LEU A 85  ? 0.3116 0.1937 0.1982 -0.0701 0.0385  -0.0255 86  LEU A N   
725  C CA  . LEU A 85  ? 0.2976 0.1951 0.2082 -0.0631 0.0400  -0.0254 86  LEU A CA  
726  C C   . LEU A 85  ? 0.3444 0.2499 0.2626 -0.0560 0.0303  -0.0214 86  LEU A C   
727  O O   . LEU A 85  ? 0.3151 0.2300 0.2465 -0.0513 0.0298  -0.0201 86  LEU A O   
728  C CB  . LEU A 85  ? 0.2988 0.1998 0.2189 -0.0630 0.0471  -0.0290 86  LEU A CB  
729  C CG  . LEU A 85  ? 0.3672 0.2648 0.2873 -0.0685 0.0588  -0.0348 86  LEU A CG  
730  C CD1 . LEU A 85  ? 0.3761 0.2745 0.3046 -0.0674 0.0651  -0.0385 86  LEU A CD1 
731  C CD2 . LEU A 85  ? 0.3722 0.2794 0.3066 -0.0661 0.0627  -0.0364 86  LEU A CD2 
732  N N   . LEU A 86  ? 0.3036 0.2070 0.2142 -0.0554 0.0224  -0.0206 87  LEU A N   
733  C CA  . LEU A 86  ? 0.2986 0.2110 0.2175 -0.0493 0.0138  -0.0188 87  LEU A CA  
734  C C   . LEU A 86  ? 0.3321 0.2419 0.2483 -0.0465 0.0092  -0.0160 87  LEU A C   
735  O O   . LEU A 86  ? 0.2956 0.2148 0.2243 -0.0420 0.0075  -0.0150 87  LEU A O   
736  C CB  . LEU A 86  ? 0.3009 0.2137 0.2135 -0.0496 0.0063  -0.0207 87  LEU A CB  
737  C CG  . LEU A 86  ? 0.3451 0.2702 0.2692 -0.0439 -0.0017 -0.0214 87  LEU A CG  
738  C CD1 . LEU A 86  ? 0.3263 0.2623 0.2669 -0.0428 0.0040  -0.0220 87  LEU A CD1 
739  C CD2 . LEU A 86  ? 0.3645 0.2925 0.2836 -0.0443 -0.0100 -0.0253 87  LEU A CD2 
740  N N   . ASP A 87  ? 0.3157 0.2107 0.2138 -0.0501 0.0082  -0.0149 88  ASP A N   
741  C CA  . ASP A 87  ? 0.3196 0.2073 0.2120 -0.0490 0.0057  -0.0125 88  ASP A CA  
742  C C   . ASP A 87  ? 0.3486 0.2450 0.2551 -0.0499 0.0137  -0.0137 88  ASP A C   
743  O O   . ASP A 87  ? 0.3364 0.2376 0.2502 -0.0462 0.0108  -0.0129 88  ASP A O   
744  C CB  . ASP A 87  ? 0.3751 0.2407 0.2413 -0.0549 0.0060  -0.0110 88  ASP A CB  
745  C CG  . ASP A 87  ? 0.5407 0.3956 0.3898 -0.0517 -0.0057 -0.0089 88  ASP A CG  
746  O OD1 . ASP A 87  ? 0.5352 0.4019 0.3960 -0.0441 -0.0148 -0.0095 88  ASP A OD1 
747  O OD2 . ASP A 87  ? 0.5551 0.3900 0.3788 -0.0570 -0.0059 -0.0073 88  ASP A OD2 
748  N N   . PHE A 88  ? 0.3165 0.2158 0.2275 -0.0544 0.0233  -0.0166 89  PHE A N   
749  C CA  . PHE A 88  ? 0.2859 0.1970 0.2128 -0.0541 0.0296  -0.0191 89  PHE A CA  
750  C C   . PHE A 88  ? 0.2852 0.2122 0.2301 -0.0462 0.0251  -0.0176 89  PHE A C   
751  O O   . PHE A 88  ? 0.2724 0.2079 0.2265 -0.0443 0.0247  -0.0181 89  PHE A O   
752  C CB  . PHE A 88  ? 0.2950 0.2091 0.2272 -0.0582 0.0397  -0.0237 89  PHE A CB  
753  C CG  . PHE A 88  ? 0.2795 0.2104 0.2326 -0.0547 0.0436  -0.0269 89  PHE A CG  
754  C CD1 . PHE A 88  ? 0.3057 0.2410 0.2628 -0.0583 0.0472  -0.0304 89  PHE A CD1 
755  C CD2 . PHE A 88  ? 0.3054 0.2472 0.2736 -0.0476 0.0429  -0.0265 89  PHE A CD2 
756  C CE1 . PHE A 88  ? 0.2946 0.2484 0.2722 -0.0542 0.0489  -0.0341 89  PHE A CE1 
757  C CE2 . PHE A 88  ? 0.3202 0.2772 0.3063 -0.0426 0.0441  -0.0289 89  PHE A CE2 
758  C CZ  . PHE A 88  ? 0.2893 0.2539 0.2811 -0.0456 0.0465  -0.0331 89  PHE A CZ  
759  N N   . MET A 89  ? 0.2424 0.1731 0.1913 -0.0429 0.0227  -0.0165 90  MET A N   
760  C CA  . MET A 89  ? 0.2285 0.1712 0.1904 -0.0369 0.0196  -0.0150 90  MET A CA  
761  C C   . MET A 89  ? 0.2744 0.2207 0.2377 -0.0343 0.0133  -0.0138 90  MET A C   
762  O O   . MET A 89  ? 0.2581 0.2143 0.2311 -0.0312 0.0128  -0.0135 90  MET A O   
763  C CB  . MET A 89  ? 0.2405 0.1828 0.2020 -0.0361 0.0183  -0.0146 90  MET A CB  
764  C CG  . MET A 89  ? 0.2571 0.1955 0.2190 -0.0380 0.0253  -0.0162 90  MET A CG  
765  S SD  . MET A 89  ? 0.3084 0.2459 0.2698 -0.0385 0.0247  -0.0166 90  MET A SD  
766  C CE  . MET A 89  ? 0.3188 0.2467 0.2764 -0.0424 0.0339  -0.0197 90  MET A CE  
767  N N   . TYR A 90  ? 0.2495 0.1875 0.2026 -0.0349 0.0080  -0.0134 91  TYR A N   
768  C CA  . TYR A 90  ? 0.2469 0.1869 0.2017 -0.0314 0.0018  -0.0132 91  TYR A CA  
769  C C   . TYR A 90  ? 0.3051 0.2378 0.2544 -0.0332 0.0026  -0.0132 91  TYR A C   
770  O O   . TYR A 90  ? 0.2882 0.2213 0.2392 -0.0302 -0.0018 -0.0135 91  TYR A O   
771  C CB  . TYR A 90  ? 0.2688 0.2042 0.2173 -0.0291 -0.0058 -0.0136 91  TYR A CB  
772  C CG  . TYR A 90  ? 0.2756 0.2229 0.2340 -0.0273 -0.0074 -0.0157 91  TYR A CG  
773  C CD1 . TYR A 90  ? 0.3023 0.2494 0.2590 -0.0305 -0.0041 -0.0165 91  TYR A CD1 
774  C CD2 . TYR A 90  ? 0.2752 0.2335 0.2442 -0.0238 -0.0109 -0.0180 91  TYR A CD2 
775  C CE1 . TYR A 90  ? 0.2942 0.2506 0.2587 -0.0307 -0.0040 -0.0192 91  TYR A CE1 
776  C CE2 . TYR A 90  ? 0.2806 0.2493 0.2577 -0.0241 -0.0109 -0.0212 91  TYR A CE2 
777  C CZ  . TYR A 90  ? 0.3187 0.2860 0.2932 -0.0280 -0.0071 -0.0217 91  TYR A CZ  
778  O OH  . TYR A 90  ? 0.2815 0.2580 0.2630 -0.0299 -0.0060 -0.0259 91  TYR A OH  
779  N N   . THR A 91  ? 0.2666 0.1923 0.2096 -0.0388 0.0091  -0.0139 92  THR A N   
780  C CA  . THR A 91  ? 0.2762 0.1925 0.2116 -0.0428 0.0115  -0.0148 92  THR A CA  
781  C C   . THR A 91  ? 0.3012 0.2248 0.2439 -0.0482 0.0202  -0.0187 92  THR A C   
782  O O   . THR A 91  ? 0.2973 0.2164 0.2368 -0.0522 0.0228  -0.0208 92  THR A O   
783  C CB  . THR A 91  ? 0.3351 0.2277 0.2470 -0.0470 0.0108  -0.0129 92  THR A CB  
784  O OG1 . THR A 91  ? 0.3382 0.2267 0.2437 -0.0533 0.0179  -0.0142 92  THR A OG1 
785  C CG2 . THR A 91  ? 0.3344 0.2187 0.2374 -0.0408 0.0001  -0.0099 92  THR A CG2 
786  N N   A SER A 92  ? 0.2637 0.1979 0.2162 -0.0485 0.0249  -0.0205 93  SER A N   
787  N N   B SER A 92  ? 0.2574 0.1913 0.2096 -0.0485 0.0249  -0.0205 93  SER A N   
788  C CA  A SER A 92  ? 0.2582 0.2022 0.2206 -0.0527 0.0330  -0.0259 93  SER A CA  
789  C CA  B SER A 92  ? 0.2518 0.1958 0.2142 -0.0526 0.0329  -0.0258 93  SER A CA  
790  C C   A SER A 92  ? 0.2996 0.2288 0.2475 -0.0626 0.0412  -0.0291 93  SER A C   
791  C C   B SER A 92  ? 0.3082 0.2373 0.2560 -0.0628 0.0412  -0.0291 93  SER A C   
792  O O   A SER A 92  ? 0.2817 0.2195 0.2383 -0.0674 0.0495  -0.0354 93  SER A O   
793  O O   B SER A 92  ? 0.2996 0.2369 0.2555 -0.0681 0.0493  -0.0356 93  SER A O   
794  C CB  A SER A 92  ? 0.2731 0.2297 0.2467 -0.0528 0.0330  -0.0293 93  SER A CB  
795  C CB  B SER A 92  ? 0.2732 0.2318 0.2486 -0.0514 0.0322  -0.0288 93  SER A CB  
796  O OG  A SER A 92  ? 0.2250 0.1930 0.2081 -0.0452 0.0259  -0.0266 93  SER A OG  
797  O OG  B SER A 92  ? 0.3114 0.2600 0.2774 -0.0585 0.0352  -0.0313 93  SER A OG  
798  N N   A ARG A 93  ? 0.2820 0.1894 0.2076 -0.0656 0.0390  -0.0252 94  ARG A N   
799  N N   B ARG A 93  ? 0.2877 0.1954 0.2135 -0.0655 0.0390  -0.0252 94  ARG A N   
800  C CA  A ARG A 93  ? 0.3033 0.1920 0.2091 -0.0761 0.0468  -0.0272 94  ARG A CA  
801  C CA  B ARG A 93  ? 0.3113 0.1991 0.2161 -0.0760 0.0464  -0.0269 94  ARG A CA  
802  C C   A ARG A 93  ? 0.3570 0.2401 0.2548 -0.0778 0.0489  -0.0269 94  ARG A C   
803  C C   B ARG A 93  ? 0.3636 0.2458 0.2604 -0.0779 0.0487  -0.0267 94  ARG A C   
804  O O   A ARG A 93  ? 0.3326 0.2127 0.2259 -0.0720 0.0409  -0.0223 94  ARG A O   
805  O O   B ARG A 93  ? 0.3497 0.2284 0.2414 -0.0723 0.0408  -0.0222 94  ARG A O   
806  C CB  A ARG A 93  ? 0.3520 0.2154 0.2329 -0.0790 0.0431  -0.0230 94  ARG A CB  
807  C CB  B ARG A 93  ? 0.3517 0.2150 0.2326 -0.0775 0.0412  -0.0221 94  ARG A CB  
808  C CG  A ARG A 93  ? 0.4148 0.2801 0.3011 -0.0791 0.0428  -0.0244 94  ARG A CG  
809  C CG  B ARG A 93  ? 0.4497 0.3155 0.3368 -0.0759 0.0393  -0.0227 94  ARG A CG  
810  C CD  A ARG A 93  ? 0.5204 0.3611 0.3854 -0.0765 0.0350  -0.0186 94  ARG A CD  
811  C CD  B ARG A 93  ? 0.5300 0.3874 0.4099 -0.0879 0.0504  -0.0282 94  ARG A CD  
812  N NE  A ARG A 93  ? 0.6840 0.4946 0.5177 -0.0846 0.0386  -0.0162 94  ARG A NE  
813  N NE  B ARG A 93  ? 0.5639 0.4246 0.4506 -0.0872 0.0492  -0.0299 94  ARG A NE  
814  C CZ  A ARG A 93  ? 0.8574 0.6488 0.6740 -0.0956 0.0476  -0.0185 94  ARG A CZ  
815  C CZ  B ARG A 93  ? 0.7381 0.5742 0.6050 -0.0902 0.0485  -0.0276 94  ARG A CZ  
816  N NH1 A ARG A 93  ? 0.7055 0.5068 0.5355 -0.0998 0.0538  -0.0240 94  ARG A NH1 
817  N NH1 B ARG A 93  ? 0.6023 0.4430 0.4773 -0.0901 0.0485  -0.0305 94  ARG A NH1 
818  N NH2 A ARG A 93  ? 0.7154 0.4765 0.4996 -0.1035 0.0509  -0.0155 94  ARG A NH2 
819  N NH2 B ARG A 93  ? 0.5449 0.3499 0.3819 -0.0935 0.0479  -0.0226 94  ARG A NH2 
820  N N   . LEU A 94  ? 0.3268 0.2094 0.2233 -0.0865 0.0603  -0.0331 95  LEU A N   
821  C CA  . LEU A 94  ? 0.3352 0.2127 0.2245 -0.0899 0.0647  -0.0347 95  LEU A CA  
822  C C   . LEU A 94  ? 0.4122 0.2651 0.2719 -0.1023 0.0716  -0.0357 95  LEU A C   
823  O O   . LEU A 94  ? 0.4077 0.2575 0.2643 -0.1123 0.0823  -0.0415 95  LEU A O   
824  C CB  . LEU A 94  ? 0.3291 0.2279 0.2439 -0.0886 0.0728  -0.0423 95  LEU A CB  
825  C CG  . LEU A 94  ? 0.3698 0.2657 0.2818 -0.0909 0.0784  -0.0453 95  LEU A CG  
826  C CD1 . LEU A 94  ? 0.3470 0.2428 0.2594 -0.0821 0.0686  -0.0391 95  LEU A CD1 
827  C CD2 . LEU A 94  ? 0.3918 0.3060 0.3279 -0.0906 0.0883  -0.0549 95  LEU A CD2 
828  N N   . ASN A 95  ? 0.4165 0.2517 0.2531 -0.1025 0.0655  -0.0304 96  ASN A N   
829  C CA  . ASN A 95  ? 0.4539 0.2617 0.2561 -0.1141 0.0704  -0.0299 96  ASN A CA  
830  C C   . ASN A 95  ? 0.5209 0.3309 0.3223 -0.1229 0.0827  -0.0374 96  ASN A C   
831  O O   . ASN A 95  ? 0.5323 0.3355 0.3213 -0.1232 0.0798  -0.0360 96  ASN A O   
832  C CB  . ASN A 95  ? 0.5172 0.3052 0.2938 -0.1091 0.0562  -0.0211 96  ASN A CB  
833  C CG  . ASN A 95  ? 0.7482 0.5038 0.4839 -0.1201 0.0592  -0.0189 96  ASN A CG  
834  O OD1 . ASN A 95  ? 0.6544 0.3972 0.3768 -0.1325 0.0720  -0.0227 96  ASN A OD1 
835  N ND2 . ASN A 95  ? 0.6749 0.4166 0.3888 -0.1164 0.0476  -0.0133 96  ASN A ND2 
836  N N   . LEU A 96  ? 0.4708 0.2931 0.2884 -0.1295 0.0963  -0.0465 97  LEU A N   
837  C CA  . LEU A 96  ? 0.4856 0.3137 0.3085 -0.1375 0.1098  -0.0562 97  LEU A CA  
838  C C   . LEU A 96  ? 0.5522 0.3556 0.3423 -0.1549 0.1217  -0.0597 97  LEU A C   
839  O O   . LEU A 96  ? 0.5414 0.3365 0.3231 -0.1637 0.1286  -0.0621 97  LEU A O   
840  C CB  . LEU A 96  ? 0.4742 0.3319 0.3356 -0.1336 0.1170  -0.0654 97  LEU A CB  
841  C CG  . LEU A 96  ? 0.5402 0.4124 0.4203 -0.1343 0.1272  -0.0754 97  LEU A CG  
842  C CD1 . LEU A 96  ? 0.5442 0.4154 0.4248 -0.1255 0.1195  -0.0704 97  LEU A CD1 
843  C CD2 . LEU A 96  ? 0.5123 0.4139 0.4304 -0.1280 0.1311  -0.0839 97  LEU A CD2 
844  N N   . ARG A 97  ? 0.5388 0.3277 0.3068 -0.1609 0.1240  -0.0599 98  ARG A N   
845  C CA  . ARG A 97  ? 0.5825 0.3438 0.3126 -0.1782 0.1348  -0.0624 98  ARG A CA  
846  C C   . ARG A 97  ? 0.5977 0.3641 0.3301 -0.1867 0.1481  -0.0729 98  ARG A C   
847  O O   . ARG A 97  ? 0.5514 0.3346 0.3049 -0.1775 0.1443  -0.0744 98  ARG A O   
848  C CB  . ARG A 97  ? 0.6376 0.3680 0.3264 -0.1774 0.1211  -0.0501 98  ARG A CB  
849  C CG  . ARG A 97  ? 0.7132 0.4351 0.3973 -0.1684 0.1076  -0.0400 98  ARG A CG  
850  C CD  . ARG A 97  ? 0.9421 0.6349 0.5879 -0.1649 0.0923  -0.0285 98  ARG A CD  
851  N NE  . ARG A 97  ? 1.1922 0.8493 0.7911 -0.1807 0.1000  -0.0275 98  ARG A NE  
852  C CZ  . ARG A 97  ? 1.4797 1.1094 1.0518 -0.1895 0.1051  -0.0247 98  ARG A CZ  
853  N NH1 . ARG A 97  ? 1.3567 0.9514 0.8827 -0.2048 0.1128  -0.0236 98  ARG A NH1 
854  N NH2 . ARG A 97  ? 1.3464 0.9821 0.9358 -0.1841 0.1035  -0.0232 98  ARG A NH2 
855  N N   . GLU A 98  ? 0.5887 0.3390 0.2980 -0.2051 0.1645  -0.0806 99  GLU A N   
856  C CA  . GLU A 98  ? 0.5841 0.3379 0.2936 -0.2149 0.1790  -0.0921 99  GLU A CA  
857  C C   . GLU A 98  ? 0.6385 0.3857 0.3350 -0.2094 0.1689  -0.0868 99  GLU A C   
858  O O   . GLU A 98  ? 0.6305 0.3948 0.3497 -0.2062 0.1740  -0.0946 99  GLU A O   
859  C CB  . GLU A 98  ? 0.6457 0.3754 0.3205 -0.2378 0.1971  -0.0993 99  GLU A CB  
860  C CG  . GLU A 98  ? 0.7820 0.5172 0.4594 -0.2495 0.2149  -0.1138 99  GLU A CG  
861  C CD  . GLU A 98  ? 1.1585 0.8684 0.7985 -0.2740 0.2341  -0.1215 99  GLU A CD  
862  O OE1 . GLU A 98  ? 1.0957 0.7696 0.6867 -0.2823 0.2291  -0.1109 99  GLU A OE1 
863  O OE2 . GLU A 98  ? 1.1563 0.8820 0.8157 -0.2849 0.2543  -0.1386 99  GLU A OE2 
864  N N   . GLY A 99  ? 0.6318 0.3555 0.2940 -0.2074 0.1541  -0.0742 100 GLY A N   
865  C CA  . GLY A 99  ? 0.6534 0.3709 0.3006 -0.2030 0.1427  -0.0695 100 GLY A CA  
866  C C   . GLY A 99  ? 0.6572 0.3991 0.3385 -0.1854 0.1300  -0.0665 100 GLY A C   
867  O O   . GLY A 99  ? 0.6558 0.3987 0.3329 -0.1836 0.1252  -0.0670 100 GLY A O   
868  N N   . ASN A 100 ? 0.5699 0.3314 0.2842 -0.1731 0.1251  -0.0641 101 ASN A N   
869  C CA  . ASN A 100 ? 0.5299 0.3116 0.2729 -0.1575 0.1135  -0.0609 101 ASN A CA  
870  C C   . ASN A 100 ? 0.5387 0.3469 0.3243 -0.1503 0.1215  -0.0682 101 ASN A C   
871  O O   . ASN A 100 ? 0.5066 0.3288 0.3137 -0.1388 0.1141  -0.0660 101 ASN A O   
872  C CB  . ASN A 100 ? 0.5338 0.3134 0.2741 -0.1464 0.0957  -0.0493 101 ASN A CB  
873  C CG  . ASN A 100 ? 0.6387 0.4247 0.3939 -0.1431 0.0968  -0.0477 101 ASN A CG  
874  O OD1 . ASN A 100 ? 0.4909 0.2937 0.2722 -0.1435 0.1074  -0.0549 101 ASN A OD1 
875  N ND2 . ASN A 100 ? 0.5499 0.3235 0.2900 -0.1389 0.0852  -0.0389 101 ASN A ND2 
876  N N   . ILE A 101 ? 0.4970 0.3120 0.2946 -0.1569 0.1359  -0.0770 102 ILE A N   
877  C CA  . ILE A 101 ? 0.4709 0.3119 0.3096 -0.1482 0.1412  -0.0838 102 ILE A CA  
878  C C   . ILE A 101 ? 0.4769 0.3281 0.3346 -0.1416 0.1436  -0.0887 102 ILE A C   
879  O O   . ILE A 101 ? 0.4337 0.3013 0.3194 -0.1280 0.1379  -0.0869 102 ILE A O   
880  C CB  . ILE A 101 ? 0.5186 0.3678 0.3683 -0.1572 0.1565  -0.0950 102 ILE A CB  
881  C CG1 . ILE A 101 ? 0.5008 0.3798 0.3949 -0.1448 0.1576  -0.1012 102 ILE A CG1 
882  C CG2 . ILE A 101 ? 0.5323 0.3704 0.3646 -0.1739 0.1737  -0.1061 102 ILE A CG2 
883  C CD1 . ILE A 101 ? 0.5129 0.4054 0.4221 -0.1496 0.1654  -0.1090 102 ILE A CD1 
884  N N   . MET A 102 ? 0.4666 0.3063 0.3075 -0.1514 0.1519  -0.0945 103 MET A N   
885  C CA  . MET A 102 ? 0.4660 0.3124 0.3232 -0.1459 0.1553  -0.0997 103 MET A CA  
886  C C   . MET A 102 ? 0.4977 0.3447 0.3574 -0.1347 0.1402  -0.0898 103 MET A C   
887  O O   . MET A 102 ? 0.4596 0.3178 0.3447 -0.1236 0.1392  -0.0906 103 MET A O   
888  C CB  . MET A 102 ? 0.5329 0.3661 0.3696 -0.1602 0.1680  -0.1090 103 MET A CB  
889  C CG  . MET A 102 ? 0.6191 0.4539 0.4570 -0.1724 0.1860  -0.1216 103 MET A CG  
890  S SD  . MET A 102 ? 0.6682 0.5320 0.5555 -0.1617 0.1943  -0.1321 103 MET A SD  
891  C CE  . MET A 102 ? 0.6347 0.5046 0.5447 -0.1526 0.1991  -0.1396 103 MET A CE  
892  N N   . ALA A 103 ? 0.4798 0.3144 0.3133 -0.1371 0.1283  -0.0809 104 ALA A N   
893  C CA  . ALA A 103 ? 0.4662 0.3031 0.3017 -0.1282 0.1143  -0.0732 104 ALA A CA  
894  C C   . ALA A 103 ? 0.4555 0.3066 0.3149 -0.1150 0.1059  -0.0667 104 ALA A C   
895  O O   . ALA A 103 ? 0.4339 0.2927 0.3093 -0.1061 0.1014  -0.0646 104 ALA A O   
896  C CB  . ALA A 103 ? 0.4987 0.3217 0.3026 -0.1332 0.1030  -0.0668 104 ALA A CB  
897  N N   . VAL A 104 ? 0.3912 0.2445 0.2515 -0.1147 0.1048  -0.0642 105 VAL A N   
898  C CA  . VAL A 104 ? 0.3551 0.2223 0.2369 -0.1031 0.0972  -0.0588 105 VAL A CA  
899  C C   . VAL A 104 ? 0.3861 0.2684 0.2981 -0.0949 0.1033  -0.0638 105 VAL A C   
900  O O   . VAL A 104 ? 0.3591 0.2492 0.2856 -0.0843 0.0960  -0.0590 105 VAL A O   
901  C CB  . VAL A 104 ? 0.4032 0.2685 0.2786 -0.1063 0.0964  -0.0566 105 VAL A CB  
902  C CG1 . VAL A 104 ? 0.3642 0.2463 0.2643 -0.0957 0.0911  -0.0537 105 VAL A CG1 
903  C CG2 . VAL A 104 ? 0.4319 0.2801 0.2779 -0.1101 0.0866  -0.0493 105 VAL A CG2 
904  N N   A MET A 105 ? 0.3694 0.2553 0.2903 -0.0994 0.1164  -0.0738 106 MET A N   
905  N N   B MET A 105 ? 0.3705 0.2564 0.2915 -0.0993 0.1165  -0.0738 106 MET A N   
906  C CA  A MET A 105 ? 0.3668 0.2666 0.3169 -0.0900 0.1216  -0.0795 106 MET A CA  
907  C CA  B MET A 105 ? 0.3703 0.2703 0.3207 -0.0895 0.1210  -0.0791 106 MET A CA  
908  C C   A MET A 105 ? 0.4192 0.3143 0.3732 -0.0835 0.1198  -0.0779 106 MET A C   
909  C C   B MET A 105 ? 0.4085 0.3034 0.3624 -0.0834 0.1196  -0.0777 106 MET A C   
910  O O   A MET A 105 ? 0.3970 0.2992 0.3686 -0.0713 0.1148  -0.0744 106 MET A O   
911  O O   B MET A 105 ? 0.3730 0.2749 0.3444 -0.0713 0.1147  -0.0743 106 MET A O   
912  C CB  A MET A 105 ? 0.4098 0.3148 0.3688 -0.0967 0.1367  -0.0927 106 MET A CB  
913  C CB  B MET A 105 ? 0.4123 0.3186 0.3732 -0.0955 0.1358  -0.0921 106 MET A CB  
914  C CG  A MET A 105 ? 0.4482 0.3700 0.4402 -0.0845 0.1399  -0.0992 106 MET A CG  
915  C CG  B MET A 105 ? 0.4458 0.3685 0.4396 -0.0826 0.1383  -0.0981 106 MET A CG  
916  S SD  A MET A 105 ? 0.5122 0.4439 0.5197 -0.0917 0.1582  -0.1175 106 MET A SD  
917  S SD  B MET A 105 ? 0.4941 0.4307 0.5068 -0.0886 0.1551  -0.1159 106 MET A SD  
918  C CE  A MET A 105 ? 0.4642 0.4078 0.5052 -0.0727 0.1572  -0.1216 106 MET A CE  
919  C CE  B MET A 105 ? 0.4821 0.4009 0.4778 -0.1003 0.1689  -0.1244 106 MET A CE  
920  N N   . ALA A 106 ? 0.4021 0.2836 0.3376 -0.0924 0.1240  -0.0805 107 ALA A N   
921  C CA  . ALA A 106 ? 0.4118 0.2865 0.3482 -0.0892 0.1241  -0.0804 107 ALA A CA  
922  C C   . ALA A 106 ? 0.4221 0.2977 0.3581 -0.0819 0.1111  -0.0700 107 ALA A C   
923  O O   . ALA A 106 ? 0.3998 0.2750 0.3476 -0.0736 0.1103  -0.0682 107 ALA A O   
924  C CB  . ALA A 106 ? 0.4442 0.3057 0.3579 -0.1022 0.1300  -0.0855 107 ALA A CB  
925  N N   . THR A 107 ? 0.3627 0.2385 0.2851 -0.0848 0.1013  -0.0635 108 THR A N   
926  C CA  . THR A 107 ? 0.3539 0.2329 0.2773 -0.0787 0.0896  -0.0554 108 THR A CA  
927  C C   . THR A 107 ? 0.3604 0.2500 0.3043 -0.0671 0.0864  -0.0512 108 THR A C   
928  O O   . THR A 107 ? 0.3423 0.2321 0.2924 -0.0609 0.0828  -0.0474 108 THR A O   
929  C CB  . THR A 107 ? 0.4051 0.2816 0.3100 -0.0834 0.0797  -0.0507 108 THR A CB  
930  O OG1 . THR A 107 ? 0.4159 0.2817 0.2996 -0.0939 0.0824  -0.0548 108 THR A OG1 
931  C CG2 . THR A 107 ? 0.4094 0.2904 0.3163 -0.0785 0.0689  -0.0453 108 THR A CG2 
932  N N   . ALA A 108 ? 0.3224 0.2204 0.2753 -0.0650 0.0880  -0.0525 109 ALA A N   
933  C CA  . ALA A 108 ? 0.2984 0.2082 0.2702 -0.0540 0.0839  -0.0493 109 ALA A CA  
934  C C   . ALA A 108 ? 0.3321 0.2419 0.3192 -0.0451 0.0883  -0.0517 109 ALA A C   
935  O O   . ALA A 108 ? 0.3211 0.2335 0.3162 -0.0356 0.0824  -0.0462 109 ALA A O   
936  C CB  . ALA A 108 ? 0.3035 0.2237 0.2822 -0.0553 0.0855  -0.0523 109 ALA A CB  
937  N N   . MET A 109 ? 0.3242 0.2285 0.3132 -0.0483 0.0986  -0.0597 110 MET A N   
938  C CA  . MET A 109 ? 0.3197 0.2202 0.3220 -0.0388 0.1027  -0.0620 110 MET A CA  
939  C C   . MET A 109 ? 0.3619 0.2487 0.3546 -0.0372 0.0994  -0.0557 110 MET A C   
940  O O   . MET A 109 ? 0.3622 0.2459 0.3618 -0.0267 0.0959  -0.0510 110 MET A O   
941  C CB  . MET A 109 ? 0.3557 0.2525 0.3619 -0.0434 0.1155  -0.0734 110 MET A CB  
942  C CG  . MET A 109 ? 0.4004 0.3126 0.4211 -0.0439 0.1208  -0.0819 110 MET A CG  
943  S SD  . MET A 109 ? 0.4904 0.3976 0.5109 -0.0539 0.1378  -0.0968 110 MET A SD  
944  C CE  . MET A 109 ? 0.4602 0.3596 0.4976 -0.0395 0.1410  -0.0995 110 MET A CE  
945  N N   . TYR A 110 ? 0.3505 0.2293 0.3261 -0.0480 0.1001  -0.0559 111 TYR A N   
946  C CA  . TYR A 110 ? 0.3475 0.2156 0.3138 -0.0498 0.0981  -0.0523 111 TYR A CA  
947  C C   . TYR A 110 ? 0.3698 0.2433 0.3376 -0.0439 0.0881  -0.0433 111 TYR A C   
948  O O   . TYR A 110 ? 0.3615 0.2266 0.3295 -0.0393 0.0878  -0.0395 111 TYR A O   
949  C CB  . TYR A 110 ? 0.3544 0.2190 0.3036 -0.0628 0.0984  -0.0554 111 TYR A CB  
950  C CG  . TYR A 110 ? 0.3592 0.2184 0.3001 -0.0667 0.0954  -0.0534 111 TYR A CG  
951  C CD1 . TYR A 110 ? 0.4007 0.2466 0.3402 -0.0685 0.1030  -0.0568 111 TYR A CD1 
952  C CD2 . TYR A 110 ? 0.3537 0.2211 0.2885 -0.0696 0.0856  -0.0496 111 TYR A CD2 
953  C CE1 . TYR A 110 ? 0.3948 0.2366 0.3268 -0.0744 0.1017  -0.0568 111 TYR A CE1 
954  C CE2 . TYR A 110 ? 0.3613 0.2272 0.2908 -0.0744 0.0835  -0.0502 111 TYR A CE2 
955  C CZ  . TYR A 110 ? 0.3989 0.2525 0.3270 -0.0777 0.0920  -0.0542 111 TYR A CZ  
956  O OH  . TYR A 110 ? 0.3996 0.2530 0.3229 -0.0843 0.0910  -0.0564 111 TYR A OH  
957  N N   . LEU A 111 ? 0.3175 0.2031 0.2849 -0.0446 0.0806  -0.0401 112 LEU A N   
958  C CA  . LEU A 111 ? 0.2982 0.1905 0.2672 -0.0400 0.0716  -0.0329 112 LEU A CA  
959  C C   . LEU A 111 ? 0.3346 0.2317 0.3161 -0.0285 0.0692  -0.0292 112 LEU A C   
960  O O   . LEU A 111 ? 0.3291 0.2297 0.3106 -0.0246 0.0627  -0.0233 112 LEU A O   
961  C CB  . LEU A 111 ? 0.2784 0.1799 0.2418 -0.0446 0.0646  -0.0316 112 LEU A CB  
962  C CG  . LEU A 111 ? 0.3158 0.2135 0.2649 -0.0539 0.0627  -0.0338 112 LEU A CG  
963  C CD1 . LEU A 111 ? 0.3298 0.2341 0.2734 -0.0553 0.0545  -0.0314 112 LEU A CD1 
964  C CD2 . LEU A 111 ? 0.3337 0.2286 0.2800 -0.0559 0.0611  -0.0333 112 LEU A CD2 
965  N N   . GLN A 112 ? 0.2948 0.1936 0.2873 -0.0231 0.0740  -0.0335 113 GLN A N   
966  C CA  . GLN A 112 ? 0.3026 0.2084 0.3087 -0.0107 0.0703  -0.0312 113 GLN A CA  
967  C C   . GLN A 112 ? 0.3280 0.2505 0.3386 -0.0099 0.0626  -0.0287 113 GLN A C   
968  O O   . GLN A 112 ? 0.3178 0.2433 0.3281 -0.0045 0.0554  -0.0225 113 GLN A O   
969  C CB  . GLN A 112 ? 0.3275 0.2198 0.3299 -0.0027 0.0683  -0.0249 113 GLN A CB  
970  C CG  . GLN A 112 ? 0.3530 0.2260 0.3506 -0.0035 0.0770  -0.0280 113 GLN A CG  
971  C CD  . GLN A 112 ? 0.4747 0.3294 0.4615 0.0000  0.0761  -0.0210 113 GLN A CD  
972  O OE1 . GLN A 112 ? 0.4150 0.2703 0.4008 0.0077  0.0691  -0.0140 113 GLN A OE1 
973  N NE2 . GLN A 112 ? 0.4972 0.3343 0.4737 -0.0068 0.0838  -0.0231 113 GLN A NE2 
974  N N   . MET A 113 ? 0.2918 0.2230 0.3042 -0.0167 0.0651  -0.0340 114 MET A N   
975  C CA  . MET A 113 ? 0.2854 0.2304 0.3013 -0.0180 0.0601  -0.0335 114 MET A CA  
976  C C   . MET A 113 ? 0.3423 0.2998 0.3743 -0.0159 0.0649  -0.0417 114 MET A C   
977  O O   . MET A 113 ? 0.3142 0.2727 0.3445 -0.0247 0.0721  -0.0485 114 MET A O   
978  C CB  . MET A 113 ? 0.3108 0.2513 0.3115 -0.0290 0.0596  -0.0329 114 MET A CB  
979  C CG  . MET A 113 ? 0.3284 0.2609 0.3175 -0.0304 0.0544  -0.0269 114 MET A CG  
980  S SD  . MET A 113 ? 0.3582 0.2849 0.3300 -0.0406 0.0518  -0.0268 114 MET A SD  
981  C CE  . MET A 113 ? 0.3173 0.2542 0.2922 -0.0393 0.0455  -0.0245 114 MET A CE  
982  N N   . GLU A 114 ? 0.3316 0.2985 0.3789 -0.0041 0.0611  -0.0418 115 GLU A N   
983  C CA  . GLU A 114 ? 0.3381 0.3202 0.4061 0.0012  0.0646  -0.0511 115 GLU A CA  
984  C C   . GLU A 114 ? 0.3446 0.3427 0.4197 -0.0071 0.0679  -0.0587 115 GLU A C   
985  O O   . GLU A 114 ? 0.3314 0.3364 0.4170 -0.0107 0.0769  -0.0693 115 GLU A O   
986  C CB  . GLU A 114 ? 0.3669 0.3570 0.4484 0.0173  0.0561  -0.0484 115 GLU A CB  
987  C CG  . GLU A 114 ? 0.5415 0.5124 0.6164 0.0259  0.0553  -0.0425 115 GLU A CG  
988  N N   . HIS A 115 ? 0.3024 0.3058 0.3717 -0.0107 0.0620  -0.0545 116 HIS A N   
989  C CA  . HIS A 115 ? 0.3175 0.3334 0.3916 -0.0197 0.0661  -0.0620 116 HIS A CA  
990  C C   . HIS A 115 ? 0.3435 0.3461 0.4018 -0.0343 0.0761  -0.0656 116 HIS A C   
991  O O   . HIS A 115 ? 0.3447 0.3548 0.4091 -0.0424 0.0851  -0.0757 116 HIS A O   
992  C CB  . HIS A 115 ? 0.3410 0.3634 0.4119 -0.0199 0.0577  -0.0569 116 HIS A CB  
993  C CG  . HIS A 115 ? 0.3929 0.4306 0.4786 -0.0069 0.0483  -0.0553 116 HIS A CG  
994  N ND1 . HIS A 115 ? 0.4246 0.4830 0.5334 -0.0002 0.0485  -0.0645 116 HIS A ND1 
995  C CD2 . HIS A 115 ? 0.4187 0.4536 0.4981 0.0001  0.0385  -0.0460 116 HIS A CD2 
996  C CE1 . HIS A 115 ? 0.4189 0.4853 0.5332 0.0116  0.0375  -0.0596 116 HIS A CE1 
997  N NE2 . HIS A 115 ? 0.4182 0.4700 0.5139 0.0114  0.0318  -0.0483 116 HIS A NE2 
998  N N   . VAL A 116 ? 0.2813 0.2643 0.3186 -0.0382 0.0747  -0.0580 117 VAL A N   
999  C CA  . VAL A 116 ? 0.3012 0.2691 0.3194 -0.0511 0.0823  -0.0602 117 VAL A CA  
1000 C C   . VAL A 116 ? 0.3684 0.3363 0.3937 -0.0537 0.0936  -0.0698 117 VAL A C   
1001 O O   . VAL A 116 ? 0.3355 0.3019 0.3558 -0.0649 0.1035  -0.0776 117 VAL A O   
1002 C CB  . VAL A 116 ? 0.3494 0.2993 0.3455 -0.0533 0.0765  -0.0511 117 VAL A CB  
1003 C CG1 . VAL A 116 ? 0.3615 0.2955 0.3366 -0.0655 0.0834  -0.0538 117 VAL A CG1 
1004 C CG2 . VAL A 116 ? 0.3436 0.2941 0.3337 -0.0517 0.0668  -0.0438 117 VAL A CG2 
1005 N N   . VAL A 117 ? 0.3195 0.2876 0.3555 -0.0439 0.0931  -0.0697 118 VAL A N   
1006 C CA  . VAL A 117 ? 0.3195 0.2879 0.3649 -0.0446 0.1040  -0.0797 118 VAL A CA  
1007 C C   . VAL A 117 ? 0.3690 0.3573 0.4352 -0.0463 0.1113  -0.0923 118 VAL A C   
1008 O O   . VAL A 117 ? 0.3661 0.3528 0.4297 -0.0573 0.1235  -0.1021 118 VAL A O   
1009 C CB  . VAL A 117 ? 0.3563 0.3205 0.4113 -0.0316 0.1015  -0.0774 118 VAL A CB  
1010 C CG1 . VAL A 117 ? 0.3634 0.3280 0.4304 -0.0314 0.1133  -0.0892 118 VAL A CG1 
1011 C CG2 . VAL A 117 ? 0.3523 0.2974 0.3866 -0.0332 0.0969  -0.0675 118 VAL A CG2 
1012 N N   A ASP A 118 ? 0.3353 0.3426 0.4202 -0.0372 0.1039  -0.0924 119 ASP A N   
1013 N N   B ASP A 118 ? 0.3307 0.3385 0.4173 -0.0361 0.1040  -0.0928 119 ASP A N   
1014 C CA  A ASP A 118 ? 0.3348 0.3659 0.4428 -0.0382 0.1091  -0.1053 119 ASP A CA  
1015 C CA  B ASP A 118 ? 0.3307 0.3627 0.4414 -0.0363 0.1090  -0.1058 119 ASP A CA  
1016 C C   A ASP A 118 ? 0.3797 0.4092 0.4758 -0.0569 0.1195  -0.1121 119 ASP A C   
1017 C C   B ASP A 118 ? 0.3849 0.4167 0.4852 -0.0549 0.1197  -0.1132 119 ASP A C   
1018 O O   A ASP A 118 ? 0.3803 0.4193 0.4878 -0.0643 0.1322  -0.1261 119 ASP A O   
1019 O O   B ASP A 118 ? 0.3865 0.4288 0.4994 -0.0617 0.1320  -0.1275 119 ASP A O   
1020 C CB  A ASP A 118 ? 0.3515 0.4019 0.4770 -0.0257 0.0967  -0.1024 119 ASP A CB  
1021 C CB  B ASP A 118 ? 0.3448 0.3958 0.4723 -0.0240 0.0965  -0.1027 119 ASP A CB  
1022 C CG  A ASP A 118 ? 0.4845 0.5641 0.6382 -0.0250 0.1004  -0.1172 119 ASP A CG  
1023 C CG  B ASP A 118 ? 0.4721 0.5290 0.6165 -0.0046 0.0877  -0.1002 119 ASP A CG  
1024 O OD1 A ASP A 118 ? 0.5106 0.6021 0.6858 -0.0191 0.1061  -0.1285 119 ASP A OD1 
1025 O OD1 B ASP A 118 ? 0.4998 0.5544 0.6542 0.0008  0.0935  -0.1063 119 ASP A OD1 
1026 O OD2 A ASP A 118 ? 0.5481 0.6395 0.7036 -0.0302 0.0977  -0.1186 119 ASP A OD2 
1027 O OD2 B ASP A 118 ? 0.5484 0.6110 0.6948 0.0053  0.0752  -0.0923 119 ASP A OD2 
1028 N N   A THR A 119 ? 0.3356 0.3518 0.4082 -0.0649 0.1151  -0.1028 120 THR A N   
1029 N N   B THR A 119 ? 0.3415 0.3597 0.4180 -0.0631 0.1155  -0.1039 120 THR A N   
1030 C CA  A THR A 119 ? 0.3449 0.3537 0.4013 -0.0827 0.1250  -0.1080 120 THR A CA  
1031 C CA  B THR A 119 ? 0.3523 0.3638 0.4129 -0.0806 0.1245  -0.1085 120 THR A CA  
1032 C C   A THR A 119 ? 0.3920 0.3811 0.4276 -0.0949 0.1365  -0.1111 120 THR A C   
1033 C C   B THR A 119 ? 0.4000 0.3913 0.4388 -0.0936 0.1364  -0.1118 120 THR A C   
1034 O O   A THR A 119 ? 0.3928 0.3800 0.4219 -0.1096 0.1494  -0.1208 120 THR A O   
1035 O O   B THR A 119 ? 0.4044 0.3962 0.4398 -0.1077 0.1496  -0.1225 120 THR A O   
1036 C CB  A THR A 119 ? 0.3437 0.3417 0.3807 -0.0869 0.1173  -0.0980 120 THR A CB  
1037 C CB  B THR A 119 ? 0.4215 0.4233 0.4641 -0.0829 0.1154  -0.0977 120 THR A CB  
1038 O OG1 A THR A 119 ? 0.3577 0.3516 0.3844 -0.1032 0.1281  -0.1056 120 THR A OG1 
1039 O OG1 B THR A 119 ? 0.3911 0.4093 0.4517 -0.0691 0.1032  -0.0932 120 THR A OG1 
1040 C CG2 A THR A 119 ? 0.2972 0.2697 0.3059 -0.0867 0.1099  -0.0844 120 THR A CG2 
1041 C CG2 B THR A 119 ? 0.4214 0.4214 0.4550 -0.0983 0.1240  -0.1042 120 THR A CG2 
1042 N N   . CYS A 120 ? 0.3553 0.3293 0.3790 -0.0901 0.1324  -0.1036 121 CYS A N   
1043 C CA  . CYS A 120 ? 0.3718 0.3272 0.3745 -0.1015 0.1425  -0.1068 121 CYS A CA  
1044 C C   . CYS A 120 ? 0.4461 0.4148 0.4693 -0.1043 0.1569  -0.1229 121 CYS A C   
1045 O O   . CYS A 120 ? 0.4344 0.3954 0.4442 -0.1200 0.1705  -0.1316 121 CYS A O   
1046 C CB  . CYS A 120 ? 0.3740 0.3144 0.3638 -0.0953 0.1348  -0.0970 121 CYS A CB  
1047 S SG  . CYS A 120 ? 0.4189 0.3412 0.3798 -0.0962 0.1207  -0.0812 121 CYS A SG  
1048 N N   A ARG A 121 ? 0.4022 0.3902 0.4573 -0.0889 0.1539  -0.1272 122 ARG A N   
1049 N N   B ARG A 121 ? 0.4074 0.3952 0.4623 -0.0890 0.1540  -0.1273 122 ARG A N   
1050 C CA  A ARG A 121 ? 0.4058 0.4106 0.4877 -0.0870 0.1655  -0.1435 122 ARG A CA  
1051 C CA  B ARG A 121 ? 0.4137 0.4177 0.4944 -0.0879 0.1662  -0.1438 122 ARG A CA  
1052 C C   A ARG A 121 ? 0.4442 0.4657 0.5368 -0.0993 0.1771  -0.1578 122 ARG A C   
1053 C C   B ARG A 121 ? 0.4469 0.4685 0.5394 -0.0995 0.1773  -0.1580 122 ARG A C   
1054 O O   A ARG A 121 ? 0.4489 0.4723 0.5440 -0.1105 0.1931  -0.1720 122 ARG A O   
1055 O O   B ARG A 121 ? 0.4509 0.4747 0.5463 -0.1108 0.1934  -0.1724 122 ARG A O   
1056 C CB  A ARG A 121 ? 0.4008 0.4232 0.5142 -0.0653 0.1559  -0.1434 122 ARG A CB  
1057 C CB  B ARG A 121 ? 0.4205 0.4405 0.5320 -0.0664 0.1575  -0.1440 122 ARG A CB  
1058 C CG  A ARG A 121 ? 0.5579 0.5632 0.6638 -0.0545 0.1494  -0.1336 122 ARG A CG  
1059 C CG  B ARG A 121 ? 0.6081 0.6105 0.7127 -0.0585 0.1556  -0.1381 122 ARG A CG  
1060 C CD  A ARG A 121 ? 0.7005 0.7186 0.8362 -0.0348 0.1450  -0.1374 122 ARG A CD  
1061 C CD  B ARG A 121 ? 0.7387 0.7547 0.8747 -0.0399 0.1534  -0.1442 122 ARG A CD  
1062 N NE  A ARG A 121 ? 0.7513 0.7501 0.8763 -0.0245 0.1370  -0.1253 122 ARG A NE  
1063 N NE  B ARG A 121 ? 0.7966 0.8207 0.9432 -0.0231 0.1370  -0.1339 122 ARG A NE  
1064 C CZ  A ARG A 121 ? 0.8869 0.8684 1.0042 -0.0257 0.1441  -0.1271 122 ARG A CZ  
1065 C CZ  B ARG A 121 ? 0.9152 0.9248 1.0553 -0.0108 0.1274  -0.1221 122 ARG A CZ  
1066 N NH1 A ARG A 121 ? 0.7867 0.7682 0.9060 -0.0361 0.1592  -0.1407 122 ARG A NH1 
1067 N NH1 B ARG A 121 ? 0.7093 0.6967 0.8345 -0.0132 0.1323  -0.1195 122 ARG A NH1 
1068 N NH2 A ARG A 121 ? 0.6372 0.6009 0.7442 -0.0176 0.1372  -0.1164 122 ARG A NH2 
1069 N NH2 B ARG A 121 ? 0.7234 0.7398 0.8706 0.0028  0.1133  -0.1133 122 ARG A NH2 
1070 N N   . LYS A 122 ? 0.3860 0.4191 0.4839 -0.0985 0.1700  -0.1549 123 LYS A N   
1071 C CA  . LYS A 122 ? 0.3983 0.4482 0.5067 -0.1109 0.1803  -0.1684 123 LYS A CA  
1072 C C   . LYS A 122 ? 0.4684 0.4947 0.5420 -0.1344 0.1937  -0.1700 123 LYS A C   
1073 O O   . LYS A 122 ? 0.4694 0.5042 0.5494 -0.1484 0.2105  -0.1863 123 LYS A O   
1074 C CB  . LYS A 122 ? 0.4127 0.4796 0.5341 -0.1039 0.1684  -0.1643 123 LYS A CB  
1075 C CG  . LYS A 122 ? 0.6385 0.7333 0.7971 -0.0825 0.1576  -0.1674 123 LYS A CG  
1076 C CD  . LYS A 122 ? 0.7742 0.8855 0.9434 -0.0754 0.1448  -0.1630 123 LYS A CD  
1077 C CE  . LYS A 122 ? 0.9259 1.0599 1.1258 -0.0528 0.1319  -0.1636 123 LYS A CE  
1078 N NZ  . LYS A 122 ? 1.0671 1.2324 1.2918 -0.0494 0.1262  -0.1720 123 LYS A NZ  
1079 N N   . PHE A 123 ? 0.4301 0.4264 0.4665 -0.1385 0.1865  -0.1538 124 PHE A N   
1080 C CA  . PHE A 123 ? 0.4544 0.4227 0.4518 -0.1590 0.1967  -0.1527 124 PHE A CA  
1081 C C   . PHE A 123 ? 0.5195 0.4773 0.5061 -0.1690 0.2109  -0.1614 124 PHE A C   
1082 O O   . PHE A 123 ? 0.5206 0.4674 0.4885 -0.1885 0.2266  -0.1702 124 PHE A O   
1083 C CB  . PHE A 123 ? 0.4749 0.4155 0.4379 -0.1575 0.1829  -0.1335 124 PHE A CB  
1084 C CG  . PHE A 123 ? 0.4923 0.4322 0.4508 -0.1578 0.1754  -0.1270 124 PHE A CG  
1085 C CD1 . PHE A 123 ? 0.5081 0.4764 0.5000 -0.1474 0.1697  -0.1307 124 PHE A CD1 
1086 C CD2 . PHE A 123 ? 0.5456 0.4551 0.4656 -0.1673 0.1729  -0.1169 124 PHE A CD2 
1087 C CE1 . PHE A 123 ? 0.5177 0.4849 0.5049 -0.1484 0.1633  -0.1256 124 PHE A CE1 
1088 C CE2 . PHE A 123 ? 0.5718 0.4789 0.4879 -0.1670 0.1664  -0.1114 124 PHE A CE2 
1089 C CZ  . PHE A 123 ? 0.5190 0.4552 0.4689 -0.1583 0.1623  -0.1162 124 PHE A CZ  
1090 N N   . ILE A 124 ? 0.4590 0.4194 0.4567 -0.1568 0.2066  -0.1598 125 ILE A N   
1091 C CA  . ILE A 124 ? 0.4768 0.4289 0.4672 -0.1655 0.2205  -0.1696 125 ILE A CA  
1092 C C   . ILE A 124 ? 0.5533 0.5301 0.5742 -0.1714 0.2382  -0.1918 125 ILE A C   
1093 O O   . ILE A 124 ? 0.5792 0.5466 0.5842 -0.1901 0.2558  -0.2029 125 ILE A O   
1094 C CB  . ILE A 124 ? 0.5046 0.4510 0.4979 -0.1515 0.2118  -0.1624 125 ILE A CB  
1095 C CG1 . ILE A 124 ? 0.5108 0.4311 0.4684 -0.1516 0.1981  -0.1440 125 ILE A CG1 
1096 C CG2 . ILE A 124 ? 0.5428 0.4859 0.5368 -0.1589 0.2277  -0.1760 125 ILE A CG2 
1097 C CD1 . ILE A 124 ? 0.5606 0.4790 0.5245 -0.1359 0.1857  -0.1346 125 ILE A CD1 
1098 N N   . LYS A 125 ? 0.5077 0.5165 0.5718 -0.1561 0.2333  -0.1986 126 LYS A N   
1099 C CA  . LYS A 125 ? 0.5210 0.5602 0.6221 -0.1580 0.2473  -0.2211 126 LYS A CA  
1100 C C   . LYS A 125 ? 0.5732 0.6140 0.6638 -0.1813 0.2633  -0.2328 126 LYS A C   
1101 O O   . LYS A 125 ? 0.5594 0.6114 0.6619 -0.1936 0.2824  -0.2525 126 LYS A O   
1102 C CB  . LYS A 125 ? 0.5395 0.6114 0.6846 -0.1356 0.2344  -0.2233 126 LYS A CB  
1103 N N   . ALA A 126 ? 0.5308 0.5585 0.5979 -0.1880 0.2566  -0.2212 127 ALA A N   
1104 C CA  . ALA A 126 ? 0.5574 0.5804 0.6089 -0.2110 0.2716  -0.2303 127 ALA A CA  
1105 C C   . ALA A 126 ? 0.6631 0.6539 0.6723 -0.2344 0.2889  -0.2331 127 ALA A C   
1106 O O   . ALA A 126 ? 0.6767 0.6692 0.6815 -0.2551 0.3083  -0.2485 127 ALA A O   
1107 C CB  . ALA A 126 ? 0.5580 0.5697 0.5919 -0.2107 0.2589  -0.2155 127 ALA A CB  
1108 N N   . SER A 127 ? 0.6637 0.6250 0.6404 -0.2322 0.2820  -0.2187 128 SER A N   
1109 C CA  . SER A 127 ? 0.7252 0.6530 0.6563 -0.2531 0.2952  -0.2188 128 SER A CA  
1110 C C   . SER A 127 ? 0.8223 0.7575 0.7643 -0.2595 0.3122  -0.2359 128 SER A C   
1111 O O   . SER A 127 ? 0.8709 0.7818 0.7770 -0.2804 0.3273  -0.2404 128 SER A O   
1112 C CB  . SER A 127 ? 0.7938 0.6869 0.6828 -0.2488 0.2787  -0.1959 128 SER A CB  
1113 O OG  . SER A 127 ? 0.9425 0.8139 0.8010 -0.2561 0.2730  -0.1843 128 SER A OG  
1114 N N   . GLU A 128 ? 0.7533 0.7203 0.7428 -0.2420 0.3104  -0.2458 129 GLU A N   
1115 C CA  . GLU A 128 ? 0.9651 0.9408 0.9698 -0.2454 0.3262  -0.2632 129 GLU A CA  
1116 C C   . GLU A 128 ? 1.4698 1.4668 1.4948 -0.2629 0.3507  -0.2894 129 GLU A C   
1117 O O   . GLU A 128 ? 1.0651 1.0594 1.0772 -0.2797 0.3591  -0.2932 129 GLU A O   
1118 C CB  . GLU A 128 ? 0.9521 0.9483 0.9964 -0.2189 0.3144  -0.2628 129 GLU A CB  
1119 C CG  . GLU A 128 ? 1.0443 1.0822 1.1443 -0.2028 0.3115  -0.2753 129 GLU A CG  
1120 C CD  . GLU A 128 ? 1.2680 1.3209 1.4020 -0.1745 0.2967  -0.2714 129 GLU A CD  
1121 O OE1 . GLU A 128 ? 1.1461 1.1769 1.2602 -0.1649 0.2835  -0.2537 129 GLU A OE1 
1122 O OE2 . GLU A 128 ? 1.1529 1.2395 1.3333 -0.1620 0.2980  -0.2864 129 GLU A OE2 
1126 N N   A TRP B 2   ? 0.1752 0.4364 0.2802 -0.0428 -0.0033 -0.0780 1   TRP D N   
1127 N N   B TRP B 2   ? 0.1899 0.4511 0.2948 -0.0428 -0.0033 -0.0780 1   TRP D N   
1128 C CA  A TRP B 2   ? 0.1683 0.4285 0.2735 -0.0429 -0.0034 -0.0787 1   TRP D CA  
1129 C CA  B TRP B 2   ? 0.1885 0.4488 0.2938 -0.0429 -0.0034 -0.0787 1   TRP D CA  
1130 C C   A TRP B 2   ? 0.2233 0.4832 0.3313 -0.0437 -0.0044 -0.0777 1   TRP D C   
1131 C C   B TRP B 2   ? 0.2224 0.4826 0.3308 -0.0437 -0.0043 -0.0777 1   TRP D C   
1132 O O   A TRP B 2   ? 0.2247 0.4835 0.3337 -0.0440 -0.0055 -0.0771 1   TRP D O   
1133 O O   B TRP B 2   ? 0.2154 0.4747 0.3247 -0.0442 -0.0052 -0.0769 1   TRP D O   
1134 C CB  A TRP B 2   ? 0.1587 0.4165 0.2607 -0.0425 -0.0050 -0.0797 1   TRP D CB  
1135 C CB  B TRP B 2   ? 0.1832 0.4410 0.2856 -0.0426 -0.0050 -0.0796 1   TRP D CB  
1136 C CG  A TRP B 2   ? 0.1620 0.4199 0.2601 -0.0420 -0.0042 -0.0821 1   TRP D CG  
1137 C CG  B TRP B 2   ? 0.1993 0.4563 0.3032 -0.0426 -0.0074 -0.0791 1   TRP D CG  
1138 C CD1 A TRP B 2   ? 0.1923 0.4499 0.2879 -0.0416 -0.0051 -0.0832 1   TRP D CD1 
1139 C CD1 B TRP B 2   ? 0.2389 0.4955 0.3431 -0.0426 -0.0091 -0.0795 1   TRP D CD1 
1140 C CD2 A TRP B 2   ? 0.1596 0.4179 0.2556 -0.0418 -0.0023 -0.0841 1   TRP D CD2 
1141 C CD2 B TRP B 2   ? 0.1987 0.4561 0.3049 -0.0423 -0.0082 -0.0788 1   TRP D CD2 
1142 N NE1 A TRP B 2   ? 0.1771 0.4351 0.2685 -0.0410 -0.0039 -0.0865 1   TRP D NE1 
1143 N NE1 B TRP B 2   ? 0.2334 0.4909 0.3414 -0.0424 -0.0108 -0.0796 1   TRP D NE1 
1144 C CE2 A TRP B 2   ? 0.1919 0.4503 0.2836 -0.0412 -0.0020 -0.0873 1   TRP D CE2 
1145 C CE2 B TRP B 2   ? 0.2489 0.5072 0.3579 -0.0420 -0.0101 -0.0794 1   TRP D CE2 
1146 C CE3 A TRP B 2   ? 0.1684 0.4269 0.2662 -0.0419 -0.0006 -0.0838 1   TRP D CE3 
1147 C CE3 B TRP B 2   ? 0.2111 0.4686 0.3179 -0.0419 -0.0075 -0.0783 1   TRP D CE3 
1148 C CZ2 A TRP B 2   ? 0.1880 0.4467 0.2766 -0.0409 0.0002  -0.0908 1   TRP D CZ2 
1149 C CZ2 B TRP B 2   ? 0.2381 0.4984 0.3505 -0.0410 -0.0107 -0.0802 1   TRP D CZ2 
1150 C CZ3 A TRP B 2   ? 0.1796 0.4380 0.2752 -0.0417 0.0016  -0.0865 1   TRP D CZ3 
1151 C CZ3 B TRP B 2   ? 0.2294 0.4880 0.3382 -0.0409 -0.0084 -0.0788 1   TRP D CZ3 
1152 C CH2 A TRP B 2   ? 0.1879 0.4466 0.2789 -0.0412 0.0022  -0.0902 1   TRP D CH2 
1153 C CH2 B TRP B 2   ? 0.2347 0.4951 0.3463 -0.0403 -0.0097 -0.0800 1   TRP D CH2 
1154 N N   . VAL B 3   ? 0.1654 0.4262 0.2752 -0.0438 -0.0039 -0.0781 2   VAL D N   
1155 C CA  . VAL B 3   ? 0.1633 0.4239 0.2749 -0.0443 -0.0050 -0.0782 2   VAL D CA  
1156 C C   . VAL B 3   ? 0.1913 0.4503 0.3024 -0.0433 -0.0051 -0.0783 2   VAL D C   
1157 O O   . VAL B 3   ? 0.1835 0.4420 0.2937 -0.0428 -0.0041 -0.0779 2   VAL D O   
1158 C CB  . VAL B 3   ? 0.2063 0.4712 0.3217 -0.0457 -0.0048 -0.0789 2   VAL D CB  
1159 C CG1 . VAL B 3   ? 0.2094 0.4768 0.3254 -0.0464 -0.0044 -0.0781 2   VAL D CG1 
1160 C CG2 . VAL B 3   ? 0.1948 0.4635 0.3137 -0.0455 -0.0034 -0.0798 2   VAL D CG2 
1161 N N   . ILE B 4   ? 0.1732 0.4316 0.2848 -0.0431 -0.0063 -0.0790 3   ILE D N   
1162 C CA  . ILE B 4   ? 0.1728 0.4300 0.2840 -0.0419 -0.0065 -0.0788 3   ILE D CA  
1163 C C   . ILE B 4   ? 0.2215 0.4807 0.3366 -0.0432 -0.0065 -0.0798 3   ILE D C   
1164 O O   . ILE B 4   ? 0.2175 0.4787 0.3342 -0.0444 -0.0078 -0.0817 3   ILE D O   
1165 C CB  . ILE B 4   ? 0.1966 0.4533 0.3065 -0.0403 -0.0076 -0.0801 3   ILE D CB  
1166 C CG1 . ILE B 4   ? 0.1672 0.4248 0.2763 -0.0390 -0.0078 -0.0802 3   ILE D CG1 
1167 C CG2 . ILE B 4   ? 0.2225 0.4781 0.3316 -0.0386 -0.0079 -0.0797 3   ILE D CG2 
1168 C CD1 . ILE B 4   ? 0.2344 0.4928 0.3422 -0.0380 -0.0076 -0.0783 3   ILE D CD1 
1169 N N   . PRO B 5   ? 0.2055 0.4653 0.3231 -0.0432 -0.0052 -0.0790 4   PRO D N   
1170 C CA  . PRO B 5   ? 0.2071 0.4710 0.3312 -0.0444 -0.0053 -0.0807 4   PRO D CA  
1171 C C   . PRO B 5   ? 0.2621 0.5250 0.3874 -0.0442 -0.0075 -0.0818 4   PRO D C   
1172 O O   . PRO B 5   ? 0.2472 0.5058 0.3686 -0.0425 -0.0079 -0.0805 4   PRO D O   
1173 C CB  . PRO B 5   ? 0.2244 0.4888 0.3514 -0.0439 -0.0026 -0.0801 4   PRO D CB  
1174 C CG  . PRO B 5   ? 0.2850 0.5438 0.4059 -0.0425 -0.0020 -0.0775 4   PRO D CG  
1175 C CD  . PRO B 5   ? 0.2310 0.4888 0.3468 -0.0422 -0.0034 -0.0774 4   PRO D CD  
1176 N N   . ALA B 6   ? 0.2425 0.5105 0.3735 -0.0460 -0.0093 -0.0846 5   ALA D N   
# 
