data_7GUO
# 
_entry.id   7GUO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   7GUO         pdb_00007guo 10.2210/pdb7guo/pdb 
WWPDB D_1001406659 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7GUO 
_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           Y 
_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-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' 260.679   1   ? ? ? ? 
4 non-polymer nat 'CHLORIDE ION'                                                35.453    1   ? ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                          78.133    1   ? ? ? ? 
6 water       nat water                                                         18.015    181 ? ? ? ? 
# 
_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-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' 7ZO 
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 
7ZO non-polymer         . '5-[(5-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' ? 'C12 H9 Cl N4 O' 260.679 
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 7ZO 1   201 1   7ZO 375 A . 
D 4 CL  1   202 1   CL  CL  A . 
E 5 DMS 1   101 1   DMS DMS D . 
F 6 HOH 1   301 42  HOH HOH A . 
F 6 HOH 2   302 88  HOH HOH A . 
F 6 HOH 3   303 81  HOH HOH A . 
F 6 HOH 4   304 15  HOH HOH A . 
F 6 HOH 5   305 32  HOH HOH A . 
F 6 HOH 6   306 84  HOH HOH A . 
F 6 HOH 7   307 230 HOH HOH A . 
F 6 HOH 8   308 159 HOH HOH A . 
F 6 HOH 9   309 63  HOH HOH A . 
F 6 HOH 10  310 166 HOH HOH A . 
F 6 HOH 11  311 130 HOH HOH A . 
F 6 HOH 12  312 114 HOH HOH A . 
F 6 HOH 13  313 92  HOH HOH A . 
F 6 HOH 14  314 23  HOH HOH A . 
F 6 HOH 15  315 189 HOH HOH A . 
F 6 HOH 16  316 5   HOH HOH A . 
F 6 HOH 17  317 24  HOH HOH A . 
F 6 HOH 18  318 85  HOH HOH A . 
F 6 HOH 19  319 103 HOH HOH A . 
F 6 HOH 20  320 87  HOH HOH A . 
F 6 HOH 21  321 143 HOH HOH A . 
F 6 HOH 22  322 149 HOH HOH A . 
F 6 HOH 23  323 33  HOH HOH A . 
F 6 HOH 24  324 196 HOH HOH A . 
F 6 HOH 25  325 83  HOH HOH A . 
F 6 HOH 26  326 187 HOH HOH A . 
F 6 HOH 27  327 14  HOH HOH A . 
F 6 HOH 28  328 49  HOH HOH A . 
F 6 HOH 29  329 109 HOH HOH A . 
F 6 HOH 30  330 165 HOH HOH A . 
F 6 HOH 31  331 134 HOH HOH A . 
F 6 HOH 32  332 141 HOH HOH A . 
F 6 HOH 33  333 135 HOH HOH A . 
F 6 HOH 34  334 117 HOH HOH A . 
F 6 HOH 35  335 90  HOH HOH A . 
F 6 HOH 36  336 113 HOH HOH A . 
F 6 HOH 37  337 97  HOH HOH A . 
F 6 HOH 38  338 13  HOH HOH A . 
F 6 HOH 39  339 105 HOH HOH A . 
F 6 HOH 40  340 35  HOH HOH A . 
F 6 HOH 41  341 50  HOH HOH A . 
F 6 HOH 42  342 112 HOH HOH A . 
F 6 HOH 43  343 136 HOH HOH A . 
F 6 HOH 44  344 94  HOH HOH A . 
F 6 HOH 45  345 100 HOH HOH A . 
F 6 HOH 46  346 26  HOH HOH A . 
F 6 HOH 47  347 123 HOH HOH A . 
F 6 HOH 48  348 110 HOH HOH A . 
F 6 HOH 49  349 3   HOH HOH A . 
F 6 HOH 50  350 115 HOH HOH A . 
F 6 HOH 51  351 184 HOH HOH A . 
F 6 HOH 52  352 51  HOH HOH A . 
F 6 HOH 53  353 121 HOH HOH A . 
F 6 HOH 54  354 25  HOH HOH A . 
F 6 HOH 55  355 74  HOH HOH A . 
F 6 HOH 56  356 28  HOH HOH A . 
F 6 HOH 57  357 213 HOH HOH A . 
F 6 HOH 58  358 11  HOH HOH A . 
F 6 HOH 59  359 151 HOH HOH A . 
F 6 HOH 60  360 116 HOH HOH A . 
F 6 HOH 61  361 231 HOH HOH A . 
F 6 HOH 62  362 6   HOH HOH A . 
F 6 HOH 63  363 180 HOH HOH A . 
F 6 HOH 64  364 102 HOH HOH A . 
F 6 HOH 65  365 18  HOH HOH A . 
F 6 HOH 66  366 95  HOH HOH A . 
F 6 HOH 67  367 101 HOH HOH A . 
F 6 HOH 68  368 62  HOH HOH A . 
F 6 HOH 69  369 150 HOH HOH A . 
F 6 HOH 70  370 86  HOH HOH A . 
F 6 HOH 71  371 147 HOH HOH A . 
F 6 HOH 72  372 66  HOH HOH A . 
F 6 HOH 73  373 10  HOH HOH A . 
F 6 HOH 74  374 22  HOH HOH A . 
F 6 HOH 75  375 104 HOH HOH A . 
F 6 HOH 76  376 107 HOH HOH A . 
F 6 HOH 77  377 89  HOH HOH A . 
F 6 HOH 78  378 168 HOH HOH A . 
F 6 HOH 79  379 244 HOH HOH A . 
F 6 HOH 80  380 20  HOH HOH A . 
F 6 HOH 81  381 40  HOH HOH A . 
F 6 HOH 82  382 29  HOH HOH A . 
F 6 HOH 83  383 178 HOH HOH A . 
F 6 HOH 84  384 57  HOH HOH A . 
F 6 HOH 85  385 164 HOH HOH A . 
F 6 HOH 86  386 192 HOH HOH A . 
F 6 HOH 87  387 21  HOH HOH A . 
F 6 HOH 88  388 99  HOH HOH A . 
F 6 HOH 89  389 44  HOH HOH A . 
F 6 HOH 90  390 119 HOH HOH A . 
F 6 HOH 91  391 30  HOH HOH A . 
F 6 HOH 92  392 60  HOH HOH A . 
F 6 HOH 93  393 238 HOH HOH A . 
F 6 HOH 94  394 39  HOH HOH A . 
F 6 HOH 95  395 38  HOH HOH A . 
F 6 HOH 96  396 56  HOH HOH A . 
F 6 HOH 97  397 96  HOH HOH A . 
F 6 HOH 98  398 36  HOH HOH A . 
F 6 HOH 99  399 27  HOH HOH A . 
F 6 HOH 100 400 82  HOH HOH A . 
F 6 HOH 101 401 167 HOH HOH A . 
F 6 HOH 102 402 75  HOH HOH A . 
F 6 HOH 103 403 146 HOH HOH A . 
F 6 HOH 104 404 93  HOH HOH A . 
F 6 HOH 105 405 246 HOH HOH A . 
F 6 HOH 106 406 242 HOH HOH A . 
F 6 HOH 107 407 52  HOH HOH A . 
F 6 HOH 108 408 53  HOH HOH A . 
F 6 HOH 109 409 237 HOH HOH A . 
F 6 HOH 110 410 37  HOH HOH A . 
F 6 HOH 111 411 209 HOH HOH A . 
F 6 HOH 112 412 17  HOH HOH A . 
F 6 HOH 113 413 193 HOH HOH A . 
F 6 HOH 114 414 203 HOH HOH A . 
F 6 HOH 115 415 239 HOH HOH A . 
F 6 HOH 116 416 69  HOH HOH A . 
F 6 HOH 117 417 45  HOH HOH A . 
F 6 HOH 118 418 200 HOH HOH A . 
F 6 HOH 119 419 55  HOH HOH A . 
F 6 HOH 120 420 153 HOH HOH A . 
F 6 HOH 121 421 54  HOH HOH A . 
F 6 HOH 122 422 176 HOH HOH A . 
F 6 HOH 123 423 241 HOH HOH A . 
F 6 HOH 124 424 98  HOH HOH A . 
F 6 HOH 125 425 79  HOH HOH A . 
F 6 HOH 126 426 186 HOH HOH A . 
F 6 HOH 127 427 148 HOH HOH A . 
F 6 HOH 128 428 185 HOH HOH A . 
F 6 HOH 129 429 43  HOH HOH A . 
F 6 HOH 130 430 171 HOH HOH A . 
F 6 HOH 131 431 188 HOH HOH A . 
F 6 HOH 132 432 31  HOH HOH A . 
F 6 HOH 133 433 145 HOH HOH A . 
F 6 HOH 134 434 191 HOH HOH A . 
F 6 HOH 135 435 106 HOH HOH A . 
F 6 HOH 136 436 232 HOH HOH A . 
F 6 HOH 137 437 139 HOH HOH A . 
F 6 HOH 138 438 80  HOH HOH A . 
F 6 HOH 139 439 158 HOH HOH A . 
F 6 HOH 140 440 204 HOH HOH A . 
F 6 HOH 141 441 221 HOH HOH A . 
F 6 HOH 142 442 76  HOH HOH A . 
F 6 HOH 143 443 137 HOH HOH A . 
F 6 HOH 144 444 111 HOH HOH A . 
F 6 HOH 145 445 140 HOH HOH A . 
F 6 HOH 146 446 206 HOH HOH A . 
F 6 HOH 147 447 108 HOH HOH A . 
F 6 HOH 148 448 243 HOH HOH A . 
F 6 HOH 149 449 247 HOH HOH A . 
F 6 HOH 150 450 161 HOH HOH A . 
F 6 HOH 151 451 169 HOH HOH A . 
F 6 HOH 152 452 131 HOH HOH A . 
F 6 HOH 153 453 70  HOH HOH A . 
F 6 HOH 154 454 183 HOH HOH A . 
F 6 HOH 155 455 228 HOH HOH A . 
F 6 HOH 156 456 212 HOH HOH A . 
F 6 HOH 157 457 215 HOH HOH A . 
F 6 HOH 158 458 59  HOH HOH A . 
F 6 HOH 159 459 73  HOH HOH A . 
F 6 HOH 160 460 179 HOH HOH A . 
F 6 HOH 161 461 142 HOH HOH A . 
F 6 HOH 162 462 175 HOH HOH A . 
F 6 HOH 163 463 245 HOH HOH A . 
F 6 HOH 164 464 65  HOH HOH A . 
F 6 HOH 165 465 181 HOH HOH A . 
F 6 HOH 166 466 170 HOH HOH A . 
F 6 HOH 167 467 195 HOH HOH A . 
F 6 HOH 168 468 152 HOH HOH A . 
F 6 HOH 169 469 208 HOH HOH A . 
F 6 HOH 170 470 61  HOH HOH A . 
F 6 HOH 171 471 233 HOH HOH A . 
F 6 HOH 172 472 225 HOH HOH A . 
F 6 HOH 173 473 144 HOH HOH A . 
G 6 HOH 1   201 77  HOH HOH D . 
G 6 HOH 2   202 71  HOH HOH D . 
G 6 HOH 3   203 68  HOH HOH D . 
G 6 HOH 4   204 47  HOH HOH D . 
G 6 HOH 5   205 58  HOH HOH D . 
G 6 HOH 6   206 240 HOH HOH D . 
G 6 HOH 7   207 220 HOH HOH D . 
G 6 HOH 8   208 210 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 D ALA 5   ? CA  ? B ALA 6   CA  
8  1 Y 1 D ALA 5   ? C   ? B ALA 6   C   
9  1 Y 1 D ALA 5   ? O   ? B ALA 6   O   
10 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           7GUO 
_cell.length_a           67.540 
_cell.length_b           67.540 
_cell.length_c           166.210 
_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                         7GUO 
_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          7GUO 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.61 
_exptl_crystal.density_percent_sol   65.95 
_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                     7GUO 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.870 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   21699 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.111 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        8.600 
_reflns.B_iso_Wilson_estimate        33.280 
_reflns.pdbx_redundancy              9.000 
_reflns.pdbx_Rrim_I_all              0.118 
_reflns.pdbx_Rpim_I_all              0.039 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     195714 
_reflns.pdbx_scaling_rejects         356 
_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 1.800 1.840  ? 11520 1243 ? 2.294 ? ? ? 9.300 ? 1.000  ? ? ? ? ? ? 100.000 2.429 0.790 0.536 ? 
1 2 9.000 33.870 ? 1579  237  ? 0.061 ? ? ? 6.700 ? 21.200 ? ? ? ? ? ? 98.800  0.065 0.024 0.996 ? 
# 
_refine.entry_id                                 7GUO 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.8000 
_refine.ls_d_res_low                             33.8800 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.8000 
_refine.ls_number_reflns_obs                     21601 
_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                          0.1830 
_refine.ls_R_factor_R_work                       0.1810 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2130 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.2000 
_refine.ls_number_reflns_R_free                  1123 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               39.5300 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -1.4674 
_refine.aniso_B[2][2]                            -1.4674 
_refine.aniso_B[3][3]                            2.9349 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9610 
_refine.correlation_coeff_Fo_to_Fc_free          0.9490 
_refine.overall_SU_R_Cruickshank_DPI             0.0950 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0970 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1090 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.1060 
_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                                139.280 
_refine.B_iso_min                                20.720 
_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                        7GUO 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.200 
_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                       1.8000 
_refine_hist.d_res_low                        33.8800 
_refine_hist.pdbx_number_atoms_ligand         23 
_refine_hist.number_atoms_solvent             181 
_refine_hist.number_atoms_total               1230 
_refine_hist.pdbx_number_residues_total       130 
_refine_hist.pdbx_B_iso_mean_ligand           34.03 
_refine_hist.pdbx_B_iso_mean_solvent          58.08 
_refine_hist.pdbx_number_atoms_protein        1026 
_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        451  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              233  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1236 ?      ? 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        7    ?      ? 1.000  HARMONIC     
'X-RAY DIFFRACTION' t_utility_angle           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_torsion         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_ideal_dist_contact      1643 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1236 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1693 0.910  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.320  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    15.980 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       1.8000 
_refine_ls_shell.d_res_low                        1.8900 
_refine_ls_shell.pdbx_total_number_of_bins_used   11 
_refine_ls_shell.percent_reflns_obs               99.2900 
_refine_ls_shell.number_reflns_R_work             2667 
_refine_ls_shell.R_factor_all                     0.2729 
_refine_ls_shell.R_factor_R_work                  0.2706 
_refine_ls_shell.R_factor_R_free                  0.3184 
_refine_ls_shell.percent_reflns_R_free            4.6100 
_refine_ls_shell.number_reflns_R_free             129 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2796 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUO 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 1 at 18.12 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUO 
_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 7GUO       7GUO   ? 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 7GUO A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUO D 1 ? 6   ? 7GUO   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 7GUO GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUO PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUO 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)' 6360  ? 
1 MORE         -68   ? 
1 'SSA (A^2)'  13290 ? 
# 
_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 33.7700000000 0.8660254038 
-0.5000000000 0.0000000000 -58.4913557716 0.0000000000 0.0000000000 -1.0000000000 27.7016666667 
# 
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 ? ? ? ? ? ? ? 1.326 ? ? 
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 GLU A 40 ? O GLU A 41 N VAL A 37 ? N VAL A 38 
AA1 2 3 N VAL A 36 ? N VAL A 37 O ILE A 71 ? O ILE A 72 
# 
_pdbx_entry_details.entry_id                   7GUO 
_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 38.24   48.85   
2 1 SER A 39  ? B 61.11   -108.41 
3 1 SER A 93  ? ? 77.15   -1.76   
4 1 SER A 93  ? ? 77.15   -4.59   
5 1 GLN A 113 ? ? 61.17   64.36   
6 1 MET A 114 ? ? -119.74 79.73   
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             VAL 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              38 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   10.10 
# 
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 330 ? F HOH . 
2 1 A HOH 385 ? F HOH . 
3 1 A HOH 451 ? F HOH . 
4 1 A HOH 460 ? F HOH . 
5 1 A HOH 462 ? F HOH . 
6 1 A HOH 467 ? F HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 29.2805 -16.6200 24.3685 -0.0128 -0.0724 -0.0299 -0.0413 0.0231  -0.0166 1.0764 1.8833 2.2425 
0.4409 -0.3255 1.2314 0.1502 -0.1023 -0.0479 -0.0619 0.1024 0.0811 0.2569  0.0062  -0.0510 
'X-RAY DIFFRACTION' 2 ? refined 18.9623 -32.3913 1.8231  -0.1498 0.0963  -0.0196 -0.0500 -0.0098 -0.0832 0.7656 0.3571 0.0000 
0.5303 0.2690  1.1186 0.0285 -0.0003 -0.0281 -0.0060 0.0175 0.0561 -0.0375 -0.0011 -0.0030 
# 
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 
7ZO C4   C  Y N 1   
7ZO C5   C  Y N 2   
7ZO C6   C  Y N 3   
7ZO C7   C  Y N 4   
7ZO C8   C  Y N 5   
7ZO C10  C  Y N 6   
7ZO C1   C  Y N 7   
7ZO C2   C  Y N 8   
7ZO C3   C  Y N 9   
7ZO C9   C  Y N 10  
7ZO C11  C  N N 11  
7ZO C12  C  N N 12  
7ZO N13  N  Y N 13  
7ZO N14  N  Y N 14  
7ZO N15  N  N N 15  
7ZO N16  N  N N 16  
7ZO O17  O  N N 17  
7ZO CL1  CL N N 18  
7ZO H1   H  N N 19  
7ZO H2   H  N N 20  
7ZO H3   H  N N 21  
7ZO H4   H  N N 22  
7ZO H5   H  N N 23  
7ZO H6   H  N N 24  
7ZO H7   H  N N 25  
7ZO H8   H  N N 26  
7ZO H9   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 
7ZO O17 C11  doub N N 1   
7ZO C11 C12  sing N N 2   
7ZO C11 N15  sing N N 3   
7ZO C12 C6   sing N N 4   
7ZO N15 C7   sing N N 5   
7ZO C6  C7   doub Y N 6   
7ZO C6  C3   sing Y N 7   
7ZO C7  C1   sing Y N 8   
7ZO C3  C8   doub Y N 9   
7ZO C1  C2   doub Y N 10  
7ZO C8  C2   sing Y N 11  
7ZO C8  N16  sing N N 12  
7ZO N16 C10  sing N N 13  
7ZO C10 N14  doub Y N 14  
7ZO C10 C9   sing Y N 15  
7ZO CL1 C9   sing N N 16  
7ZO N14 C5   sing Y N 17  
7ZO C9  C4   doub Y N 18  
7ZO C5  N13  doub Y N 19  
7ZO C4  N13  sing Y N 20  
7ZO C4  H1   sing N N 21  
7ZO C5  H2   sing N N 22  
7ZO C1  H3   sing N N 23  
7ZO C2  H4   sing N N 24  
7ZO C3  H5   sing N N 25  
7ZO C12 H6   sing N N 26  
7ZO C12 H7   sing N N 27  
7ZO N15 H8   sing N N 28  
7ZO N16 H9   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_1002059 
_pdbx_deposit_group.group_title         'X-ray dose series of B-cell lymphoma 6 protein BTB domain in complex with ligand 1' 
_pdbx_deposit_group.group_description   
;Crystal structures of B-cell lymphoma 6 protein BTB domain in complex with ligand 1 solved at increasing X-ray dose using Many Structures One Crystal (MSOX) crystallography.
;
_pdbx_deposit_group.group_type          undefined 
# 
_atom_sites.entry_id                    7GUO 
_atom_sites.fract_transf_matrix[1][1]   0.014806 
_atom_sites.fract_transf_matrix[1][2]   0.008548 
_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]   0.017097 
_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]   0.006016 
_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 
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   ? 17.556 -21.159 -4.951 1.00 71.96  ? 6   ASP A N   1 
ATOM   2    C  CA  . ASP A 1 5   ? 18.428 -22.072 -5.692 1.00 70.85  ? 6   ASP A CA  1 
ATOM   3    C  C   . ASP A 1 5   ? 17.934 -23.537 -5.595 1.00 70.58  ? 6   ASP A C   1 
ATOM   4    O  O   . ASP A 1 5   ? 16.855 -23.793 -5.049 1.00 71.24  ? 6   ASP A O   1 
ATOM   5    C  CB  . ASP A 1 5   ? 19.885 -21.941 -5.184 1.00 71.50  ? 6   ASP A CB  1 
ATOM   6    C  CG  . ASP A 1 5   ? 20.935 -22.012 -6.282 1.00 85.40  ? 6   ASP A CG  1 
ATOM   7    O  OD1 . ASP A 1 5   ? 21.019 -23.065 -6.962 1.00 86.02  ? 6   ASP A OD1 1 
ATOM   8    O  OD2 . ASP A 1 5   ? 21.683 -21.023 -6.453 1.00 92.41  ? 6   ASP A OD2 1 
ATOM   9    N  N   . SER A 1 6   ? 18.718 -24.484 -6.145 1.00 61.99  ? 7   SER A N   1 
ATOM   10   C  CA  . SER A 1 6   ? 18.422 -25.916 -6.114 1.00 59.45  ? 7   SER A CA  1 
ATOM   11   C  C   . SER A 1 6   ? 19.398 -26.670 -5.157 1.00 55.13  ? 7   SER A C   1 
ATOM   12   O  O   . SER A 1 6   ? 19.683 -27.854 -5.361 1.00 54.34  ? 7   SER A O   1 
ATOM   13   C  CB  . SER A 1 6   ? 18.470 -26.491 -7.525 1.00 64.95  ? 7   SER A CB  1 
ATOM   14   O  OG  . SER A 1 6   ? 19.732 -26.276 -8.138 1.00 76.95  ? 7   SER A OG  1 
ATOM   15   N  N   . CYS A 1 7   ? 19.877 -25.984 -4.100 1.00 45.51  ? 8   CYS A N   1 
ATOM   16   C  CA  . CYS A 1 7   ? 20.807 -26.560 -3.121 1.00 42.29  ? 8   CYS A CA  1 
ATOM   17   C  C   . CYS A 1 7   ? 20.186 -27.723 -2.320 1.00 41.25  ? 8   CYS A C   1 
ATOM   18   O  O   . CYS A 1 7   ? 18.965 -27.804 -2.175 1.00 41.04  ? 8   CYS A O   1 
ATOM   19   C  CB  . CYS A 1 7   ? 21.308 -25.472 -2.170 1.00 42.87  ? 8   CYS A CB  1 
ATOM   20   S  SG  . CYS A 1 7   ? 22.415 -24.246 -2.927 1.00 47.80  ? 8   CYS A SG  1 
ATOM   21   N  N   . ILE A 1 8   ? 21.032 -28.614 -1.804 1.00 32.02  ? 9   ILE A N   1 
ATOM   22   C  CA  . ILE A 1 8   ? 20.665 -29.622 -0.809 1.00 29.26  ? 9   ILE A CA  1 
ATOM   23   C  C   . ILE A 1 8   ? 21.255 -29.072 0.495  1.00 31.10  ? 9   ILE A C   1 
ATOM   24   O  O   . ILE A 1 8   ? 22.185 -28.260 0.452  1.00 29.97  ? 9   ILE A O   1 
ATOM   25   C  CB  . ILE A 1 8   ? 21.035 -31.099 -1.123 1.00 32.06  ? 9   ILE A CB  1 
ATOM   26   C  CG1 . ILE A 1 8   ? 22.556 -31.278 -1.409 1.00 32.34  ? 9   ILE A CG1 1 
ATOM   27   C  CG2 . ILE A 1 8   ? 20.157 -31.629 -2.275 1.00 33.37  ? 9   ILE A CG2 1 
ATOM   28   C  CD1 . ILE A 1 8   ? 23.045 -32.729 -1.585 1.00 37.37  ? 9   ILE A CD1 1 
ATOM   29   N  N   A GLN A 1 9   ? 20.760 -29.509 1.646  0.57 26.20  ? 10  GLN A N   1 
ATOM   30   N  N   B GLN A 1 9   ? 20.671 -29.453 1.631  0.43 26.42  ? 10  GLN A N   1 
ATOM   31   C  CA  A GLN A 1 9   ? 21.268 -28.979 2.907  0.57 24.94  ? 10  GLN A CA  1 
ATOM   32   C  CA  B GLN A 1 9   ? 21.080 -28.980 2.947  0.43 25.05  ? 10  GLN A CA  1 
ATOM   33   C  C   A GLN A 1 9   ? 21.598 -30.092 3.894  0.57 27.92  ? 10  GLN A C   1 
ATOM   34   C  C   B GLN A 1 9   ? 21.541 -30.135 3.820  0.43 27.49  ? 10  GLN A C   1 
ATOM   35   O  O   A GLN A 1 9   ? 20.796 -31.007 4.076  0.57 27.87  ? 10  GLN A O   1 
ATOM   36   O  O   B GLN A 1 9   ? 20.929 -31.201 3.808  0.43 27.71  ? 10  GLN A O   1 
ATOM   37   C  CB  A GLN A 1 9   ? 20.240 -27.986 3.497  0.57 26.41  ? 10  GLN A CB  1 
ATOM   38   C  CB  B GLN A 1 9   ? 19.911 -28.222 3.623  0.43 26.42  ? 10  GLN A CB  1 
ATOM   39   C  CG  A GLN A 1 9   ? 20.657 -27.332 4.817  0.57 27.05  ? 10  GLN A CG  1 
ATOM   40   C  CG  B GLN A 1 9   ? 20.104 -27.952 5.135  0.43 31.73  ? 10  GLN A CG  1 
ATOM   41   C  CD  A GLN A 1 9   ? 19.489 -26.667 5.504  0.57 52.64  ? 10  GLN A CD  1 
ATOM   42   C  CD  B GLN A 1 9   ? 20.052 -26.499 5.533  0.43 42.95  ? 10  GLN A CD  1 
ATOM   43   O  OE1 A GLN A 1 9   ? 18.522 -27.310 5.928  0.57 43.05  ? 10  GLN A OE1 1 
ATOM   44   O  OE1 B GLN A 1 9   ? 19.724 -25.608 4.737  0.43 33.65  ? 10  GLN A OE1 1 
ATOM   45   N  NE2 A GLN A 1 9   ? 19.553 -25.356 5.634  0.57 55.08  ? 10  GLN A NE2 1 
ATOM   46   N  NE2 B GLN A 1 9   ? 20.370 -26.229 6.797  0.43 33.17  ? 10  GLN A NE2 1 
ATOM   47   N  N   A PHE A 1 10  ? 22.770 -30.007 4.541  0.78 25.55  ? 11  PHE A N   1 
ATOM   48   N  N   B PHE A 1 10  ? 22.601 -29.902 4.594  0.22 23.86  ? 11  PHE A N   1 
ATOM   49   C  CA  A PHE A 1 10  ? 23.148 -31.001 5.546  0.78 25.07  ? 11  PHE A CA  1 
ATOM   50   C  CA  B PHE A 1 10  ? 23.122 -30.867 5.549  0.22 23.30  ? 11  PHE A CA  1 
ATOM   51   C  C   A PHE A 1 10  ? 22.669 -30.508 6.914  0.78 26.96  ? 11  PHE A C   1 
ATOM   52   C  C   B PHE A 1 10  ? 22.616 -30.413 6.901  0.22 26.45  ? 11  PHE A C   1 
ATOM   53   O  O   A PHE A 1 10  ? 23.236 -29.566 7.478  0.78 25.91  ? 11  PHE A O   1 
ATOM   54   O  O   B PHE A 1 10  ? 23.080 -29.394 7.425  0.22 25.46  ? 11  PHE A O   1 
ATOM   55   C  CB  A PHE A 1 10  ? 24.668 -31.310 5.511  0.78 26.02  ? 11  PHE A CB  1 
ATOM   56   C  CB  B PHE A 1 10  ? 24.655 -30.923 5.468  0.22 24.37  ? 11  PHE A CB  1 
ATOM   57   C  CG  A PHE A 1 10  ? 25.050 -32.514 6.348  0.78 27.09  ? 11  PHE A CG  1 
ATOM   58   C  CG  B PHE A 1 10  ? 25.134 -31.832 4.362  0.22 26.40  ? 11  PHE A CG  1 
ATOM   59   C  CD1 A PHE A 1 10  ? 24.639 -33.797 5.987  0.78 30.61  ? 11  PHE A CD1 1 
ATOM   60   C  CD1 B PHE A 1 10  ? 24.913 -31.510 3.026  0.22 29.75  ? 11  PHE A CD1 1 
ATOM   61   C  CD2 A PHE A 1 10  ? 25.833 -32.368 7.490  0.78 27.94  ? 11  PHE A CD2 1 
ATOM   62   C  CD2 B PHE A 1 10  ? 25.797 -33.016 4.653  0.22 29.14  ? 11  PHE A CD2 1 
ATOM   63   C  CE1 A PHE A 1 10  ? 24.984 -34.911 6.775  0.78 31.84  ? 11  PHE A CE1 1 
ATOM   64   C  CE1 B PHE A 1 10  ? 25.349 -32.355 2.005  0.22 31.27  ? 11  PHE A CE1 1 
ATOM   65   C  CE2 A PHE A 1 10  ? 26.153 -33.473 8.288  0.78 30.16  ? 11  PHE A CE2 1 
ATOM   66   C  CE2 B PHE A 1 10  ? 26.225 -33.863 3.629  0.22 32.61  ? 11  PHE A CE2 1 
ATOM   67   C  CZ  A PHE A 1 10  ? 25.734 -34.737 7.925  0.78 28.46  ? 11  PHE A CZ  1 
ATOM   68   C  CZ  B PHE A 1 10  ? 26.006 -33.522 2.316  0.22 30.74  ? 11  PHE A CZ  1 
ATOM   69   N  N   . THR A 1 11  ? 21.589 -31.112 7.419  1.00 23.40  ? 12  THR A N   1 
ATOM   70   C  CA  . THR A 1 11  ? 20.924 -30.729 8.684  1.00 24.15  ? 12  THR A CA  1 
ATOM   71   C  C   . THR A 1 11  ? 21.878 -30.495 9.888  1.00 28.18  ? 12  THR A C   1 
ATOM   72   O  O   . THR A 1 11  ? 21.759 -29.467 10.576 1.00 27.48  ? 12  THR A O   1 
ATOM   73   C  CB  . THR A 1 11  ? 19.857 -31.777 9.017  1.00 32.28  ? 12  THR A CB  1 
ATOM   74   O  OG1 . THR A 1 11  ? 18.942 -31.848 7.910  1.00 33.22  ? 12  THR A OG1 1 
ATOM   75   C  CG2 . THR A 1 11  ? 19.081 -31.447 10.313 1.00 35.76  ? 12  THR A CG2 1 
ATOM   76   N  N   A ARG A 1 12  ? 22.812 -31.433 10.117 0.50 25.18  ? 13  ARG A N   1 
ATOM   77   N  N   B ARG A 1 12  ? 22.806 -31.437 10.123 0.50 25.53  ? 13  ARG A N   1 
ATOM   78   C  CA  A ARG A 1 12  ? 23.736 -31.382 11.260 0.50 25.18  ? 13  ARG A CA  1 
ATOM   79   C  CA  B ARG A 1 12  ? 23.744 -31.395 11.256 0.50 25.66  ? 13  ARG A CA  1 
ATOM   80   C  C   A ARG A 1 12  ? 24.984 -30.504 11.064 0.50 27.14  ? 13  ARG A C   1 
ATOM   81   C  C   B ARG A 1 12  ? 24.985 -30.506 11.064 0.50 27.38  ? 13  ARG A C   1 
ATOM   82   O  O   A ARG A 1 12  ? 25.795 -30.405 11.993 0.50 25.79  ? 13  ARG A O   1 
ATOM   83   O  O   B ARG A 1 12  ? 25.796 -30.408 11.992 0.50 26.04  ? 13  ARG A O   1 
ATOM   84   C  CB  A ARG A 1 12  ? 24.159 -32.813 11.667 0.50 27.08  ? 13  ARG A CB  1 
ATOM   85   C  CB  B ARG A 1 12  ? 24.181 -32.826 11.615 0.50 28.36  ? 13  ARG A CB  1 
ATOM   86   C  CG  A ARG A 1 12  ? 23.022 -33.710 12.198 0.50 34.38  ? 13  ARG A CG  1 
ATOM   87   C  CG  B ARG A 1 12  ? 23.248 -33.529 12.604 0.50 39.32  ? 13  ARG A CG  1 
ATOM   88   C  CD  A ARG A 1 12  ? 22.445 -33.234 13.525 0.50 47.31  ? 13  ARG A CD  1 
ATOM   89   C  CD  B ARG A 1 12  ? 23.038 -35.009 12.328 0.50 46.94  ? 13  ARG A CD  1 
ATOM   90   N  NE  A ARG A 1 12  ? 23.393 -33.357 14.637 0.50 53.70  ? 13  ARG A NE  1 
ATOM   91   N  NE  B ARG A 1 12  ? 24.265 -35.735 11.979 0.50 51.37  ? 13  ARG A NE  1 
ATOM   92   C  CZ  A ARG A 1 12  ? 23.310 -32.673 15.774 0.50 60.44  ? 13  ARG A CZ  1 
ATOM   93   C  CZ  B ARG A 1 12  ? 24.428 -36.427 10.855 0.50 61.73  ? 13  ARG A CZ  1 
ATOM   94   N  NH1 A ARG A 1 12  ? 22.335 -31.790 15.958 0.50 41.53  ? 13  ARG A NH1 1 
ATOM   95   N  NH1 B ARG A 1 12  ? 25.567 -37.066 10.621 0.50 54.46  ? 13  ARG A NH1 1 
ATOM   96   N  NH2 A ARG A 1 12  ? 24.204 -32.860 16.733 0.50 47.69  ? 13  ARG A NH2 1 
ATOM   97   N  NH2 B ARG A 1 12  ? 23.448 -36.498 9.962  0.50 37.00  ? 13  ARG A NH2 1 
ATOM   98   N  N   . HIS A 1 13  ? 25.151 -29.879 9.879  1.00 23.57  ? 14  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 13  ? 26.359 -29.070 9.569  1.00 22.23  ? 14  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 13  ? 26.653 -27.959 10.574 1.00 24.81  ? 14  HIS A C   1 
ATOM   101  O  O   . HIS A 1 13  ? 27.792 -27.887 11.055 1.00 24.41  ? 14  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 13  ? 26.336 -28.499 8.142  1.00 22.33  ? 14  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 13  ? 27.602 -27.747 7.819  1.00 23.92  ? 14  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 13  ? 28.786 -28.409 7.624  1.00 24.46  ? 14  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 13  ? 27.812 -26.415 7.690  1.00 24.90  ? 14  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 13  ? 29.694 -27.474 7.366  1.00 23.82  ? 14  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 13  ? 29.156 -26.253 7.404  1.00 23.84  ? 14  HIS A NE2 1 
ATOM   108  N  N   . ALA A 1 14  ? 25.676 -27.070 10.848 1.00 22.11  ? 15  ALA A N   1 
ATOM   109  C  CA  . ALA A 1 14  ? 25.890 -25.945 11.783 1.00 22.60  ? 15  ALA A CA  1 
ATOM   110  C  C   . ALA A 1 14  ? 26.281 -26.419 13.191 1.00 24.84  ? 15  ALA A C   1 
ATOM   111  O  O   . ALA A 1 14  ? 27.181 -25.838 13.788 1.00 23.01  ? 15  ALA A O   1 
ATOM   112  C  CB  . ALA A 1 14  ? 24.655 -25.053 11.833 1.00 24.01  ? 15  ALA A CB  1 
ATOM   113  N  N   A SER A 1 15  ? 25.619 -27.469 13.700 0.38 22.58  ? 16  SER A N   1 
ATOM   114  N  N   B SER A 1 15  ? 25.621 -27.478 13.698 0.33 22.66  ? 16  SER A N   1 
ATOM   115  N  N   C SER A 1 15  ? 25.618 -27.472 13.709 0.29 22.69  ? 16  SER A N   1 
ATOM   116  C  CA  A SER A 1 15  ? 25.912 -28.033 15.016 0.38 22.82  ? 16  SER A CA  1 
ATOM   117  C  CA  B SER A 1 15  ? 25.900 -28.063 15.011 0.33 22.94  ? 16  SER A CA  1 
ATOM   118  C  CA  C SER A 1 15  ? 25.916 -28.029 15.031 0.29 22.96  ? 16  SER A CA  1 
ATOM   119  C  C   A SER A 1 15  ? 27.321 -28.635 15.044 0.38 27.07  ? 16  SER A C   1 
ATOM   120  C  C   B SER A 1 15  ? 27.308 -28.656 15.050 0.33 27.22  ? 16  SER A C   1 
ATOM   121  C  C   C SER A 1 15  ? 27.314 -28.657 15.059 0.29 27.28  ? 16  SER A C   1 
ATOM   122  O  O   A SER A 1 15  ? 28.042 -28.437 16.025 0.38 25.50  ? 16  SER A O   1 
ATOM   123  O  O   B SER A 1 15  ? 28.016 -28.472 16.043 0.33 25.84  ? 16  SER A O   1 
ATOM   124  O  O   C SER A 1 15  ? 28.025 -28.495 16.053 0.29 26.04  ? 16  SER A O   1 
ATOM   125  C  CB  A SER A 1 15  ? 24.875 -29.088 15.393 0.38 26.33  ? 16  SER A CB  1 
ATOM   126  C  CB  B SER A 1 15  ? 24.873 -29.143 15.345 0.33 26.56  ? 16  SER A CB  1 
ATOM   127  C  CB  C SER A 1 15  ? 24.855 -29.045 15.448 0.29 26.83  ? 16  SER A CB  1 
ATOM   128  O  OG  A SER A 1 15  ? 25.123 -29.565 16.703 0.38 31.10  ? 16  SER A OG  1 
ATOM   129  O  OG  B SER A 1 15  ? 23.572 -28.592 15.429 0.33 32.26  ? 16  SER A OG  1 
ATOM   130  O  OG  C SER A 1 15  ? 24.856 -30.177 14.596 0.29 33.25  ? 16  SER A OG  1 
ATOM   131  N  N   . ASP A 1 16  ? 27.715 -29.345 13.963 1.00 24.83  ? 17  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 16  ? 29.053 -29.969 13.828 1.00 25.87  ? 17  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 16  ? 30.127 -28.877 13.789 1.00 25.97  ? 17  ASP A C   1 
ATOM   134  O  O   . ASP A 1 16  ? 31.172 -29.044 14.413 1.00 25.77  ? 17  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 16  ? 29.148 -30.844 12.560 1.00 28.03  ? 17  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 16  ? 28.376 -32.162 12.624 1.00 39.54  ? 17  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 16  ? 27.846 -32.491 13.709 1.00 39.43  ? 17  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 16  ? 28.295 -32.858 11.579 1.00 39.94  ? 17  ASP A OD2 1 
ATOM   139  N  N   . VAL A 1 17  ? 29.867 -27.772 13.057 1.00 21.20  ? 18  VAL A N   1 
ATOM   140  C  CA  . VAL A 1 17  ? 30.814 -26.644 13.012 1.00 21.03  ? 18  VAL A CA  1 
ATOM   141  C  C   . VAL A 1 17  ? 31.007 -26.088 14.439 1.00 23.76  ? 18  VAL A C   1 
ATOM   142  O  O   . VAL A 1 17  ? 32.135 -25.889 14.886 1.00 21.99  ? 18  VAL A O   1 
ATOM   143  C  CB  . VAL A 1 17  ? 30.338 -25.525 12.040 1.00 23.63  ? 18  VAL A CB  1 
ATOM   144  C  CG1 . VAL A 1 17  ? 31.114 -24.223 12.279 1.00 23.08  ? 18  VAL A CG1 1 
ATOM   145  C  CG2 . VAL A 1 17  ? 30.475 -25.979 10.587 1.00 23.52  ? 18  VAL A CG2 1 
ATOM   146  N  N   . LEU A 1 18  ? 29.906 -25.817 15.150 1.00 22.27  ? 19  LEU A N   1 
ATOM   147  C  CA  . LEU A 1 18  ? 29.998 -25.244 16.494 1.00 23.01  ? 19  LEU A CA  1 
ATOM   148  C  C   . LEU A 1 18  ? 30.735 -26.178 17.473 1.00 25.03  ? 19  LEU A C   1 
ATOM   149  O  O   . LEU A 1 18  ? 31.566 -25.708 18.267 1.00 22.90  ? 19  LEU A O   1 
ATOM   150  C  CB  . LEU A 1 18  ? 28.605 -24.875 17.022 1.00 24.00  ? 19  LEU A CB  1 
ATOM   151  C  CG  . LEU A 1 18  ? 28.595 -23.995 18.294 1.00 27.74  ? 19  LEU A CG  1 
ATOM   152  C  CD1 . LEU A 1 18  ? 29.106 -22.587 17.996 1.00 26.62  ? 19  LEU A CD1 1 
ATOM   153  C  CD2 . LEU A 1 18  ? 27.184 -23.916 18.878 1.00 31.06  ? 19  LEU A CD2 1 
ATOM   154  N  N   . LEU A 1 19  ? 30.466 -27.494 17.372 1.00 23.38  ? 20  LEU A N   1 
ATOM   155  C  CA  . LEU A 1 19  ? 31.137 -28.512 18.181 1.00 24.60  ? 20  LEU A CA  1 
ATOM   156  C  C   . LEU A 1 19  ? 32.648 -28.451 17.927 1.00 26.16  ? 20  LEU A C   1 
ATOM   157  O  O   . LEU A 1 19  ? 33.433 -28.441 18.884 1.00 25.28  ? 20  LEU A O   1 
ATOM   158  C  CB  . LEU A 1 19  ? 30.585 -29.899 17.830 1.00 26.74  ? 20  LEU A CB  1 
ATOM   159  C  CG  . LEU A 1 19  ? 31.181 -31.070 18.603 1.00 35.56  ? 20  LEU A CG  1 
ATOM   160  C  CD1 . LEU A 1 19  ? 30.658 -31.080 20.052 1.00 38.27  ? 20  LEU A CD1 1 
ATOM   161  C  CD2 . LEU A 1 19  ? 30.798 -32.387 17.939 1.00 41.56  ? 20  LEU A CD2 1 
ATOM   162  N  N   . ASN A 1 20  ? 33.055 -28.357 16.648 1.00 21.40  ? 21  ASN A N   1 
ATOM   163  C  CA  . ASN A 1 20  ? 34.487 -28.249 16.321 1.00 20.86  ? 21  ASN A CA  1 
ATOM   164  C  C   . ASN A 1 20  ? 35.111 -26.950 16.805 1.00 23.50  ? 21  ASN A C   1 
ATOM   165  O  O   . ASN A 1 20  ? 36.259 -26.957 17.245 1.00 23.83  ? 21  ASN A O   1 
ATOM   166  C  CB  . ASN A 1 20  ? 34.720 -28.479 14.837 1.00 23.47  ? 21  ASN A CB  1 
ATOM   167  C  CG  . ASN A 1 20  ? 34.611 -29.949 14.493 1.00 33.03  ? 21  ASN A CG  1 
ATOM   168  O  OD1 . ASN A 1 20  ? 34.752 -30.819 15.358 1.00 29.81  ? 21  ASN A OD1 1 
ATOM   169  N  ND2 . ASN A 1 20  ? 34.339 -30.265 13.237 1.00 27.29  ? 21  ASN A ND2 1 
ATOM   170  N  N   . LEU A 1 21  ? 34.364 -25.836 16.740 1.00 22.02  ? 22  LEU A N   1 
ATOM   171  C  CA  . LEU A 1 21  ? 34.861 -24.557 17.252 1.00 22.34  ? 22  LEU A CA  1 
ATOM   172  C  C   . LEU A 1 21  ? 35.060 -24.680 18.753 1.00 23.89  ? 22  LEU A C   1 
ATOM   173  O  O   . LEU A 1 21  ? 36.046 -24.164 19.280 1.00 22.52  ? 22  LEU A O   1 
ATOM   174  C  CB  . LEU A 1 21  ? 33.880 -23.417 16.932 1.00 21.66  ? 22  LEU A CB  1 
ATOM   175  C  CG  . LEU A 1 21  ? 33.765 -23.063 15.422 1.00 24.03  ? 22  LEU A CG  1 
ATOM   176  C  CD1 . LEU A 1 21  ? 32.701 -21.971 15.214 1.00 24.32  ? 22  LEU A CD1 1 
ATOM   177  C  CD2 . LEU A 1 21  ? 35.123 -22.624 14.831 1.00 27.00  ? 22  LEU A CD2 1 
ATOM   178  N  N   . ASN A 1 22  ? 34.133 -25.371 19.452 1.00 21.72  ? 23  ASN A N   1 
ATOM   179  C  CA  . ASN A 1 22  ? 34.311 -25.556 20.909 1.00 22.42  ? 23  ASN A CA  1 
ATOM   180  C  C   . ASN A 1 22  ? 35.551 -26.432 21.219 1.00 27.24  ? 23  ASN A C   1 
ATOM   181  O  O   . ASN A 1 22  ? 36.268 -26.174 22.192 1.00 26.68  ? 23  ASN A O   1 
ATOM   182  C  CB  . ASN A 1 22  ? 33.060 -26.150 21.539 1.00 24.62  ? 23  ASN A CB  1 
ATOM   183  C  CG  . ASN A 1 22  ? 33.067 -25.991 23.043 1.00 30.62  ? 23  ASN A CG  1 
ATOM   184  O  OD1 . ASN A 1 22  ? 33.540 -24.993 23.589 1.00 28.19  ? 23  ASN A OD1 1 
ATOM   185  N  ND2 . ASN A 1 22  ? 32.559 -26.972 23.721 1.00 31.61  ? 23  ASN A ND2 1 
ATOM   186  N  N   . ARG A 1 23  ? 35.812 -27.464 20.387 1.00 24.82  ? 24  ARG A N   1 
ATOM   187  C  CA  . ARG A 1 23  ? 37.009 -28.319 20.537 1.00 25.23  ? 24  ARG A CA  1 
ATOM   188  C  C   . ARG A 1 23  ? 38.281 -27.488 20.345 1.00 28.65  ? 24  ARG A C   1 
ATOM   189  O  O   . ARG A 1 23  ? 39.234 -27.690 21.078 1.00 28.58  ? 24  ARG A O   1 
ATOM   190  C  CB  . ARG A 1 23  ? 37.003 -29.476 19.525 1.00 26.89  ? 24  ARG A CB  1 
ATOM   191  C  CG  . ARG A 1 23  ? 36.002 -30.575 19.859 1.00 33.48  ? 24  ARG A CG  1 
ATOM   192  C  CD  . ARG A 1 23  ? 35.742 -31.469 18.651 1.00 34.25  ? 24  ARG A CD  1 
ATOM   193  N  NE  . ARG A 1 23  ? 34.889 -32.603 18.994 1.00 42.87  ? 24  ARG A NE  1 
ATOM   194  C  CZ  . ARG A 1 23  ? 34.406 -33.480 18.121 1.00 62.33  ? 24  ARG A CZ  1 
ATOM   195  N  NH1 . ARG A 1 23  ? 34.622 -33.321 16.818 1.00 46.37  ? 24  ARG A NH1 1 
ATOM   196  N  NH2 . ARG A 1 23  ? 33.685 -34.512 18.540 1.00 50.22  ? 24  ARG A NH2 1 
ATOM   197  N  N   . LEU A 1 24  ? 38.290 -26.529 19.386 1.00 24.79  ? 25  LEU A N   1 
ATOM   198  C  CA  . LEU A 1 24  ? 39.450 -25.646 19.215 1.00 24.66  ? 25  LEU A CA  1 
ATOM   199  C  C   . LEU A 1 24  ? 39.607 -24.781 20.472 1.00 29.38  ? 25  LEU A C   1 
ATOM   200  O  O   . LEU A 1 24  ? 40.732 -24.604 20.963 1.00 29.47  ? 25  LEU A O   1 
ATOM   201  C  CB  . LEU A 1 24  ? 39.272 -24.740 17.997 1.00 24.49  ? 25  LEU A CB  1 
ATOM   202  C  CG  . LEU A 1 24  ? 39.226 -25.441 16.612 1.00 28.90  ? 25  LEU A CG  1 
ATOM   203  C  CD1 . LEU A 1 24  ? 39.065 -24.394 15.500 1.00 28.17  ? 25  LEU A CD1 1 
ATOM   204  C  CD2 . LEU A 1 24  ? 40.480 -26.299 16.375 1.00 30.37  ? 25  LEU A CD2 1 
ATOM   205  N  N   . ARG A 1 25  ? 38.481 -24.244 21.000 1.00 25.38  ? 26  ARG A N   1 
ATOM   206  C  CA  . ARG A 1 25  ? 38.544 -23.451 22.234 1.00 26.24  ? 26  ARG A CA  1 
ATOM   207  C  C   . ARG A 1 25  ? 39.154 -24.252 23.413 1.00 31.03  ? 26  ARG A C   1 
ATOM   208  O  O   . ARG A 1 25  ? 40.027 -23.721 24.122 1.00 31.22  ? 26  ARG A O   1 
ATOM   209  C  CB  . ARG A 1 25  ? 37.154 -22.899 22.623 1.00 26.72  ? 26  ARG A CB  1 
ATOM   210  C  CG  . ARG A 1 25  ? 37.244 -22.051 23.901 1.00 32.76  ? 26  ARG A CG  1 
ATOM   211  C  CD  . ARG A 1 25  ? 35.935 -21.411 24.249 1.00 34.37  ? 26  ARG A CD  1 
ATOM   212  N  NE  . ARG A 1 25  ? 34.916 -22.389 24.620 1.00 32.23  ? 26  ARG A NE  1 
ATOM   213  C  CZ  . ARG A 1 25  ? 34.323 -22.446 25.810 1.00 46.41  ? 26  ARG A CZ  1 
ATOM   214  N  NH1 . ARG A 1 25  ? 34.701 -21.629 26.789 1.00 38.52  ? 26  ARG A NH1 1 
ATOM   215  N  NH2 . ARG A 1 25  ? 33.367 -23.333 26.038 1.00 34.63  ? 26  ARG A NH2 1 
ATOM   216  N  N   A SER A 1 26  ? 38.685 -25.493 23.625 0.40 28.94  ? 27  SER A N   1 
ATOM   217  N  N   B SER A 1 26  ? 38.686 -25.494 23.627 0.35 28.73  ? 27  SER A N   1 
ATOM   218  N  N   C SER A 1 26  ? 38.686 -25.498 23.619 0.25 28.51  ? 27  SER A N   1 
ATOM   219  C  CA  A SER A 1 26  ? 39.159 -26.383 24.696 0.40 30.88  ? 27  SER A CA  1 
ATOM   220  C  CA  B SER A 1 26  ? 39.152 -26.372 24.710 0.35 30.52  ? 27  SER A CA  1 
ATOM   221  C  CA  C SER A 1 26  ? 39.134 -26.404 24.688 0.25 30.11  ? 27  SER A CA  1 
ATOM   222  C  C   A SER A 1 26  ? 40.667 -26.600 24.616 0.40 36.76  ? 27  SER A C   1 
ATOM   223  C  C   B SER A 1 26  ? 40.652 -26.676 24.619 0.35 36.65  ? 27  SER A C   1 
ATOM   224  C  C   C SER A 1 26  ? 40.633 -26.716 24.610 0.25 36.32  ? 27  SER A C   1 
ATOM   225  O  O   A SER A 1 26  ? 41.349 -26.583 25.644 0.40 37.52  ? 27  SER A O   1 
ATOM   226  O  O   B SER A 1 26  ? 41.315 -26.797 25.651 0.35 37.56  ? 27  SER A O   1 
ATOM   227  O  O   C SER A 1 26  ? 41.274 -26.894 25.648 0.25 37.21  ? 27  SER A O   1 
ATOM   228  C  CB  A SER A 1 26  ? 38.467 -27.740 24.609 0.40 35.08  ? 27  SER A CB  1 
ATOM   229  C  CB  B SER A 1 26  ? 38.347 -27.668 24.742 0.35 34.26  ? 27  SER A CB  1 
ATOM   230  C  CB  C SER A 1 26  ? 38.326 -27.698 24.662 0.25 33.47  ? 27  SER A CB  1 
ATOM   231  O  OG  A SER A 1 26  ? 37.073 -27.648 24.840 0.40 43.20  ? 27  SER A OG  1 
ATOM   232  O  OG  B SER A 1 26  ? 38.615 -28.495 23.622 0.35 41.47  ? 27  SER A OG  1 
ATOM   233  O  OG  C SER A 1 26  ? 38.683 -28.562 25.729 0.25 41.09  ? 27  SER A OG  1 
ATOM   234  N  N   . ARG A 1 27  ? 41.184 -26.777 23.386 1.00 33.02  ? 28  ARG A N   1 
ATOM   235  C  CA  . ARG A 1 27  ? 42.608 -27.047 23.139 1.00 34.65  ? 28  ARG A CA  1 
ATOM   236  C  C   . ARG A 1 27  ? 43.419 -25.758 22.949 1.00 37.54  ? 28  ARG A C   1 
ATOM   237  O  O   . ARG A 1 27  ? 44.629 -25.816 22.715 1.00 38.79  ? 28  ARG A O   1 
ATOM   238  C  CB  . ARG A 1 27  ? 42.751 -28.010 21.963 1.00 37.16  ? 28  ARG A CB  1 
ATOM   239  C  CG  . ARG A 1 27  ? 41.990 -29.320 22.182 1.00 46.90  ? 28  ARG A CG  1 
ATOM   240  C  CD  . ARG A 1 27  ? 42.008 -30.196 20.955 1.00 55.94  ? 28  ARG A CD  1 
ATOM   241  N  NE  . ARG A 1 27  ? 43.340 -30.762 20.737 1.00 75.39  ? 28  ARG A NE  1 
ATOM   242  C  CZ  . ARG A 1 27  ? 43.898 -30.912 19.543 1.00 93.39  ? 28  ARG A CZ  1 
ATOM   243  N  NH1 . ARG A 1 27  ? 45.113 -31.430 19.433 1.00 86.14  ? 28  ARG A NH1 1 
ATOM   244  N  NH2 . ARG A 1 27  ? 43.248 -30.545 18.451 1.00 78.42  ? 28  ARG A NH2 1 
ATOM   245  N  N   . ASP A 1 28  ? 42.758 -24.598 23.091 1.00 32.07  ? 29  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 28  ? 43.353 -23.262 22.958 1.00 33.00  ? 29  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 28  ? 43.971 -23.047 21.547 1.00 36.85  ? 29  ASP A C   1 
ATOM   248  O  O   . ASP A 1 28  ? 45.051 -22.458 21.406 1.00 37.20  ? 29  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 28  ? 44.383 -22.993 24.095 1.00 36.24  ? 29  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 28  ? 44.729 -21.529 24.266 1.00 45.07  ? 29  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 28  ? 43.831 -20.677 24.061 1.00 44.50  ? 29  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 28  ? 45.899 -21.231 24.589 1.00 52.24  ? 29  ASP A OD2 1 
ATOM   253  N  N   . ILE A 1 29  ? 43.305 -23.574 20.518 1.00 30.54  ? 30  ILE A N   1 
ATOM   254  C  CA  . ILE A 1 29  ? 43.780 -23.487 19.134 1.00 29.26  ? 30  ILE A CA  1 
ATOM   255  C  C   . ILE A 1 29  ? 43.170 -22.295 18.426 1.00 31.97  ? 30  ILE A C   1 
ATOM   256  O  O   . ILE A 1 29  ? 41.935 -22.187 18.338 1.00 27.74  ? 30  ILE A O   1 
ATOM   257  C  CB  . ILE A 1 29  ? 43.541 -24.805 18.345 1.00 32.10  ? 30  ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 29  ? 44.351 -25.985 18.953 1.00 33.23  ? 30  ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 29  ? 43.853 -24.629 16.834 1.00 31.49  ? 30  ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 29  ? 43.831 -27.382 18.470 1.00 35.00  ? 30  ILE A CD1 1 
ATOM   261  N  N   A LEU A 1 30  ? 44.037 -21.401 17.910 0.54 30.19  ? 31  LEU A N   1 
ATOM   262  N  N   B LEU A 1 30  ? 44.045 -21.405 17.918 0.46 30.57  ? 31  LEU A N   1 
ATOM   263  C  CA  A LEU A 1 30  ? 43.679 -20.196 17.148 0.54 29.86  ? 31  LEU A CA  1 
ATOM   264  C  CA  B LEU A 1 30  ? 43.720 -20.193 17.162 0.46 30.53  ? 31  LEU A CA  1 
ATOM   265  C  C   A LEU A 1 30  ? 42.812 -19.194 17.919 0.54 32.28  ? 31  LEU A C   1 
ATOM   266  C  C   B LEU A 1 30  ? 42.824 -19.200 17.916 0.46 32.64  ? 31  LEU A C   1 
ATOM   267  O  O   A LEU A 1 30  ? 42.182 -18.330 17.301 0.54 30.11  ? 31  LEU A O   1 
ATOM   268  O  O   B LEU A 1 30  ? 42.189 -18.347 17.288 0.46 30.71  ? 31  LEU A O   1 
ATOM   269  C  CB  A LEU A 1 30  ? 43.040 -20.535 15.783 0.54 29.65  ? 31  LEU A CB  1 
ATOM   270  C  CB  B LEU A 1 30  ? 43.149 -20.520 15.778 0.46 30.60  ? 31  LEU A CB  1 
ATOM   271  C  CG  A LEU A 1 30  ? 43.945 -21.198 14.712 0.54 35.37  ? 31  LEU A CG  1 
ATOM   272  C  CG  B LEU A 1 30  ? 44.179 -20.405 14.658 0.46 36.71  ? 31  LEU A CG  1 
ATOM   273  C  CD1 A LEU A 1 30  ? 43.413 -20.915 13.350 0.54 34.05  ? 31  LEU A CD1 1 
ATOM   274  C  CD1 B LEU A 1 30  ? 44.524 -21.767 14.074 0.46 37.13  ? 31  LEU A CD1 1 
ATOM   275  C  CD2 A LEU A 1 30  ? 45.382 -20.689 14.759 0.54 37.93  ? 31  LEU A CD2 1 
ATOM   276  C  CD2 B LEU A 1 30  ? 43.695 -19.469 13.590 0.46 38.33  ? 31  LEU A CD2 1 
ATOM   277  N  N   . THR A 1 31  ? 42.832 -19.260 19.263 1.00 28.91  ? 32  THR A N   1 
ATOM   278  C  CA  . THR A 1 31  ? 42.119 -18.274 20.102 1.00 28.48  ? 32  THR A CA  1 
ATOM   279  C  C   . THR A 1 31  ? 42.927 -16.977 19.905 1.00 33.93  ? 32  THR A C   1 
ATOM   280  O  O   . THR A 1 31  ? 44.155 -17.025 19.755 1.00 34.57  ? 32  THR A O   1 
ATOM   281  C  CB  . THR A 1 31  ? 42.060 -18.696 21.574 1.00 33.72  ? 32  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 31  ? 43.366 -19.078 21.972 1.00 35.60  ? 32  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 31  ? 41.066 -19.842 21.812 1.00 31.62  ? 32  THR A CG2 1 
ATOM   284  N  N   . ASP A 1 32  ? 42.240 -15.861 19.724 1.00 30.70  ? 33  ASP A N   1 
ATOM   285  C  CA  . ASP A 1 32  ? 42.927 -14.619 19.376 1.00 30.91  ? 33  ASP A CA  1 
ATOM   286  C  C   . ASP A 1 32  ? 42.594 -13.476 20.300 1.00 32.47  ? 33  ASP A C   1 
ATOM   287  O  O   . ASP A 1 32  ? 42.934 -12.324 20.008 1.00 31.87  ? 33  ASP A O   1 
ATOM   288  C  CB  . ASP A 1 32  ? 42.626 -14.263 17.909 1.00 32.42  ? 33  ASP A CB  1 
ATOM   289  C  CG  . ASP A 1 32  ? 41.141 -14.294 17.542 1.00 41.32  ? 33  ASP A CG  1 
ATOM   290  O  OD1 . ASP A 1 32  ? 40.291 -14.340 18.467 1.00 38.06  ? 33  ASP A OD1 1 
ATOM   291  O  OD2 . ASP A 1 32  ? 40.831 -14.282 16.338 1.00 50.09  ? 33  ASP A OD2 1 
ATOM   292  N  N   . VAL A 1 33  ? 41.944 -13.782 21.427 1.00 27.42  ? 34  VAL A N   1 
ATOM   293  C  CA  . VAL A 1 33  ? 41.610 -12.744 22.406 1.00 26.88  ? 34  VAL A CA  1 
ATOM   294  C  C   . VAL A 1 33  ? 41.427 -13.324 23.788 1.00 30.19  ? 34  VAL A C   1 
ATOM   295  O  O   . VAL A 1 33  ? 41.018 -14.493 23.936 1.00 29.47  ? 34  VAL A O   1 
ATOM   296  C  CB  . VAL A 1 33  ? 40.344 -11.917 21.957 1.00 29.47  ? 34  VAL A CB  1 
ATOM   297  C  CG1 . VAL A 1 33  ? 39.038 -12.702 22.134 1.00 27.95  ? 34  VAL A CG1 1 
ATOM   298  C  CG2 . VAL A 1 33  ? 40.267 -10.547 22.667 1.00 29.65  ? 34  VAL A CG2 1 
ATOM   299  N  N   A VAL A 1 34  ? 41.717 -12.497 24.802 0.53 27.15  ? 35  VAL A N   1 
ATOM   300  N  N   B VAL A 1 34  ? 41.725 -12.516 24.807 0.47 27.52  ? 35  VAL A N   1 
ATOM   301  C  CA  A VAL A 1 34  ? 41.497 -12.792 26.210 0.53 26.78  ? 35  VAL A CA  1 
ATOM   302  C  CA  B VAL A 1 34  ? 41.456 -12.871 26.187 0.47 27.33  ? 35  VAL A CA  1 
ATOM   303  C  C   A VAL A 1 34  ? 40.429 -11.805 26.687 0.53 29.93  ? 35  VAL A C   1 
ATOM   304  C  C   B VAL A 1 34  ? 40.477 -11.834 26.757 0.47 30.51  ? 35  VAL A C   1 
ATOM   305  O  O   A VAL A 1 34  ? 40.565 -10.594 26.481 0.53 30.55  ? 35  VAL A O   1 
ATOM   306  O  O   B VAL A 1 34  ? 40.688 -10.625 26.624 0.47 31.34  ? 35  VAL A O   1 
ATOM   307  C  CB  A VAL A 1 34  ? 42.799 -12.676 27.058 0.53 31.55  ? 35  VAL A CB  1 
ATOM   308  C  CB  B VAL A 1 34  ? 42.707 -13.162 27.069 0.47 32.31  ? 35  VAL A CB  1 
ATOM   309  C  CG1 A VAL A 1 34  ? 42.529 -12.905 28.546 0.53 31.57  ? 35  VAL A CG1 1 
ATOM   310  C  CG1 B VAL A 1 34  ? 43.569 -11.924 27.287 0.47 33.20  ? 35  VAL A CG1 1 
ATOM   311  C  CG2 A VAL A 1 34  ? 43.864 -13.638 26.563 0.53 32.07  ? 35  VAL A CG2 1 
ATOM   312  C  CG2 B VAL A 1 34  ? 42.312 -13.793 28.401 0.47 32.39  ? 35  VAL A CG2 1 
ATOM   313  N  N   . ILE A 1 35  ? 39.374 -12.318 27.316 1.00 26.03  ? 36  ILE A N   1 
ATOM   314  C  CA  . ILE A 1 35  ? 38.335 -11.485 27.912 1.00 25.17  ? 36  ILE A CA  1 
ATOM   315  C  C   . ILE A 1 35  ? 38.620 -11.509 29.413 1.00 30.48  ? 36  ILE A C   1 
ATOM   316  O  O   . ILE A 1 35  ? 38.633 -12.587 30.023 1.00 30.16  ? 36  ILE A O   1 
ATOM   317  C  CB  . ILE A 1 35  ? 36.899 -11.977 27.587 1.00 26.32  ? 36  ILE A CB  1 
ATOM   318  C  CG1 . ILE A 1 35  ? 36.673 -12.127 26.036 1.00 26.06  ? 36  ILE A CG1 1 
ATOM   319  C  CG2 . ILE A 1 35  ? 35.870 -11.064 28.241 1.00 27.89  ? 36  ILE A CG2 1 
ATOM   320  C  CD1 . ILE A 1 35  ? 36.958 -10.864 25.170 1.00 28.67  ? 36  ILE A CD1 1 
ATOM   321  N  N   . VAL A 1 36  ? 38.842 -10.327 29.993 1.00 27.45  ? 37  VAL A N   1 
ATOM   322  C  CA  . VAL A 1 36  ? 39.147 -10.178 31.422 1.00 27.90  ? 37  VAL A CA  1 
ATOM   323  C  C   . VAL A 1 36  ? 37.877 -9.740  32.158 1.00 32.93  ? 37  VAL A C   1 
ATOM   324  O  O   . VAL A 1 36  ? 37.280 -8.696  31.838 1.00 31.17  ? 37  VAL A O   1 
ATOM   325  C  CB  . VAL A 1 36  ? 40.350 -9.217  31.660 1.00 32.74  ? 37  VAL A CB  1 
ATOM   326  C  CG1 . VAL A 1 36  ? 40.669 -9.064  33.148 1.00 33.13  ? 37  VAL A CG1 1 
ATOM   327  C  CG2 . VAL A 1 36  ? 41.587 -9.703  30.915 1.00 33.53  ? 37  VAL A CG2 1 
ATOM   328  N  N   . VAL A 1 37  ? 37.485 -10.534 33.171 1.00 30.07  ? 38  VAL A N   1 
ATOM   329  C  CA  . VAL A 1 37  ? 36.293 -10.304 33.986 1.00 30.35  ? 38  VAL A CA  1 
ATOM   330  C  C   . VAL A 1 37  ? 36.773 -10.378 35.431 1.00 36.48  ? 38  VAL A C   1 
ATOM   331  O  O   . VAL A 1 37  ? 37.008 -11.475 35.948 1.00 34.20  ? 38  VAL A O   1 
ATOM   332  C  CB  . VAL A 1 37  ? 35.178 -11.339 33.660 1.00 33.44  ? 38  VAL A CB  1 
ATOM   333  C  CG1 . VAL A 1 37  ? 33.857 -10.935 34.302 1.00 33.68  ? 38  VAL A CG1 1 
ATOM   334  C  CG2 . VAL A 1 37  ? 35.011 -11.513 32.143 1.00 32.06  ? 38  VAL A CG2 1 
ATOM   335  N  N   A SER A 1 38  ? 36.686 -9.266  36.189 0.50 35.86  ? 39  SER A N   1 
ATOM   336  N  N   B SER A 1 38  ? 37.279 -9.191  35.840 0.50 33.43  ? 39  SER A N   1 
ATOM   337  C  CA  A SER A 1 38  ? 37.046 -9.250  37.622 0.50 37.52  ? 39  SER A CA  1 
ATOM   338  C  CA  B SER A 1 38  ? 37.956 -8.834  37.074 0.50 34.10  ? 39  SER A CA  1 
ATOM   339  C  C   A SER A 1 38  ? 38.296 -10.134 37.931 0.50 41.60  ? 39  SER A C   1 
ATOM   340  C  C   B SER A 1 38  ? 39.243 -9.652  37.221 0.50 37.07  ? 39  SER A C   1 
ATOM   341  O  O   A SER A 1 38  ? 38.247 -10.993 38.817 0.50 41.08  ? 39  SER A O   1 
ATOM   342  O  O   B SER A 1 38  ? 40.166 -9.418  36.440 0.50 35.15  ? 39  SER A O   1 
ATOM   343  C  CB  A SER A 1 38  ? 35.851 -9.674  38.484 0.50 42.99  ? 39  SER A CB  1 
ATOM   344  C  CB  B SER A 1 38  ? 37.014 -8.894  38.270 0.50 38.67  ? 39  SER A CB  1 
ATOM   345  O  OG  A SER A 1 38  ? 34.738 -8.802  38.359 0.50 54.07  ? 39  SER A OG  1 
ATOM   346  O  OG  B SER A 1 38  ? 36.091 -7.821  38.171 0.50 47.36  ? 39  SER A OG  1 
ATOM   347  N  N   A ARG A 1 39  ? 39.380 -9.955  37.135 0.50 38.28  ? 40  ARG A N   1 
ATOM   348  N  N   B ARG A 1 39  ? 39.308 -10.628 38.143 0.50 35.04  ? 40  ARG A N   1 
ATOM   349  C  CA  A ARG A 1 39  ? 40.665 -10.678 37.209 0.50 39.26  ? 40  ARG A CA  1 
ATOM   350  C  CA  B ARG A 1 39  ? 40.528 -11.424 38.291 0.50 36.17  ? 40  ARG A CA  1 
ATOM   351  C  C   A ARG A 1 39  ? 40.547 -12.209 36.940 0.50 42.51  ? 40  ARG A C   1 
ATOM   352  C  C   B ARG A 1 39  ? 40.665 -12.477 37.160 0.50 41.12  ? 40  ARG A C   1 
ATOM   353  O  O   A ARG A 1 39  ? 41.349 -13.014 37.447 0.50 44.12  ? 40  ARG A O   1 
ATOM   354  O  O   B ARG A 1 39  ? 41.743 -12.604 36.559 0.50 42.46  ? 40  ARG A O   1 
ATOM   355  C  CB  A ARG A 1 39  ? 41.424 -10.397 38.523 0.50 40.66  ? 40  ARG A CB  1 
ATOM   356  C  CB  B ARG A 1 39  ? 40.645 -12.031 39.713 0.50 36.81  ? 40  ARG A CB  1 
ATOM   357  C  CG  A ARG A 1 39  ? 41.945 -8.973  38.668 0.50 52.16  ? 40  ARG A CG  1 
ATOM   358  C  CG  B ARG A 1 39  ? 40.942 -10.978 40.796 0.50 44.80  ? 40  ARG A CG  1 
ATOM   359  C  CD  A ARG A 1 39  ? 43.038 -8.919  39.718 0.50 59.92  ? 40  ARG A CD  1 
ATOM   360  C  CD  B ARG A 1 39  ? 41.306 -11.574 42.149 0.50 43.47  ? 40  ARG A CD  1 
ATOM   361  N  NE  A ARG A 1 39  ? 43.417 -7.550  40.072 0.50 67.48  ? 40  ARG A NE  1 
ATOM   362  N  NE  B ARG A 1 39  ? 41.474 -10.555 43.189 0.50 44.27  ? 40  ARG A NE  1 
ATOM   363  C  CZ  A ARG A 1 39  ? 42.856 -6.841  41.047 0.50 80.55  ? 40  ARG A CZ  1 
ATOM   364  C  CZ  B ARG A 1 39  ? 42.632 -9.995  43.535 0.50 58.10  ? 40  ARG A CZ  1 
ATOM   365  N  NH1 A ARG A 1 39  ? 41.861 -7.354  41.762 0.50 64.80  ? 40  ARG A NH1 1 
ATOM   366  N  NH1 B ARG A 1 39  ? 43.753 -10.326 42.907 0.50 45.44  ? 40  ARG A NH1 1 
ATOM   367  N  NH2 A ARG A 1 39  ? 43.274 -5.610  41.307 0.50 68.64  ? 40  ARG A NH2 1 
ATOM   368  N  NH2 B ARG A 1 39  ? 42.675 -9.091  44.502 0.50 49.01  ? 40  ARG A NH2 1 
ATOM   369  N  N   A GLU A 1 40  ? 39.543 -12.598 36.148 0.50 35.27  ? 41  GLU A N   1 
ATOM   370  N  N   B GLU A 1 40  ? 39.553 -13.138 36.802 0.50 34.49  ? 41  GLU A N   1 
ATOM   371  C  CA  A GLU A 1 40  ? 39.339 -13.964 35.668 0.50 34.26  ? 41  GLU A CA  1 
ATOM   372  C  CA  B GLU A 1 40  ? 39.519 -14.215 35.808 0.50 33.20  ? 41  GLU A CA  1 
ATOM   373  C  C   A GLU A 1 40  ? 39.475 -13.836 34.156 0.50 34.85  ? 41  GLU A C   1 
ATOM   374  C  C   B GLU A 1 40  ? 39.754 -13.767 34.352 0.50 33.97  ? 41  GLU A C   1 
ATOM   375  O  O   A GLU A 1 40  ? 38.895 -12.922 33.562 0.50 31.72  ? 41  GLU A O   1 
ATOM   376  O  O   B GLU A 1 40  ? 39.435 -12.644 33.972 0.50 30.74  ? 41  GLU A O   1 
ATOM   377  C  CB  A GLU A 1 40  ? 37.976 -14.541 36.094 0.50 35.47  ? 41  GLU A CB  1 
ATOM   378  C  CB  B GLU A 1 40  ? 38.213 -15.029 35.921 0.50 34.31  ? 41  GLU A CB  1 
ATOM   379  C  CG  A GLU A 1 40  ? 37.882 -14.767 37.597 0.50 49.79  ? 41  GLU A CG  1 
ATOM   380  C  CG  B GLU A 1 40  ? 37.730 -15.211 37.357 0.50 50.06  ? 41  GLU A CG  1 
ATOM   381  C  CD  A GLU A 1 40  ? 37.854 -16.212 38.054 0.50 84.63  ? 41  GLU A CD  1 
ATOM   382  C  CD  B GLU A 1 40  ? 37.923 -16.559 38.026 0.50 87.88  ? 41  GLU A CD  1 
ATOM   383  O  OE1 A GLU A 1 40  ? 36.822 -16.628 38.631 0.50 88.85  ? 41  GLU A OE1 1 
ATOM   384  O  OE1 B GLU A 1 40  ? 38.988 -17.189 37.829 0.50 89.89  ? 41  GLU A OE1 1 
ATOM   385  O  OE2 A GLU A 1 40  ? 38.864 -16.926 37.849 0.50 85.09  ? 41  GLU A OE2 1 
ATOM   386  O  OE2 B GLU A 1 40  ? 37.008 -16.974 38.773 0.50 90.44  ? 41  GLU A OE2 1 
ATOM   387  N  N   . GLN A 1 41  ? 40.298 -14.694 33.545 1.00 31.38  ? 42  GLN A N   1 
ATOM   388  C  CA  . GLN A 1 41  ? 40.627 -14.558 32.135 1.00 30.78  ? 42  GLN A CA  1 
ATOM   389  C  C   . GLN A 1 41  ? 40.015 -15.685 31.331 1.00 34.14  ? 42  GLN A C   1 
ATOM   390  O  O   . GLN A 1 41  ? 40.093 -16.841 31.744 1.00 35.27  ? 42  GLN A O   1 
ATOM   391  C  CB  . GLN A 1 41  ? 42.158 -14.561 31.984 1.00 33.46  ? 42  GLN A CB  1 
ATOM   392  C  CG  . GLN A 1 41  ? 42.817 -13.300 32.534 1.00 48.05  ? 42  GLN A CG  1 
ATOM   393  C  CD  . GLN A 1 41  ? 44.299 -13.193 32.256 1.00 69.51  ? 42  GLN A CD  1 
ATOM   394  O  OE1 . GLN A 1 41  ? 44.883 -13.922 31.441 1.00 63.06  ? 42  GLN A OE1 1 
ATOM   395  N  NE2 . GLN A 1 41  ? 44.938 -12.255 32.932 1.00 72.78  ? 42  GLN A NE2 1 
ATOM   396  N  N   . PHE A 1 42  ? 39.412 -15.351 30.183 1.00 27.29  ? 43  PHE A N   1 
ATOM   397  C  CA  . PHE A 1 42  ? 38.759 -16.346 29.315 1.00 26.76  ? 43  PHE A CA  1 
ATOM   398  C  C   . PHE A 1 42  ? 39.292 -16.180 27.909 1.00 30.77  ? 43  PHE A C   1 
ATOM   399  O  O   . PHE A 1 42  ? 39.179 -15.095 27.348 1.00 30.53  ? 43  PHE A O   1 
ATOM   400  C  CB  . PHE A 1 42  ? 37.238 -16.118 29.324 1.00 28.11  ? 43  PHE A CB  1 
ATOM   401  C  CG  . PHE A 1 42  ? 36.618 -16.231 30.695 1.00 30.26  ? 43  PHE A CG  1 
ATOM   402  C  CD1 . PHE A 1 42  ? 36.504 -15.114 31.521 1.00 31.80  ? 43  PHE A CD1 1 
ATOM   403  C  CD2 . PHE A 1 42  ? 36.124 -17.450 31.153 1.00 32.25  ? 43  PHE A CD2 1 
ATOM   404  C  CE1 . PHE A 1 42  ? 35.948 -15.223 32.799 1.00 34.08  ? 43  PHE A CE1 1 
ATOM   405  C  CE2 . PHE A 1 42  ? 35.559 -17.555 32.426 1.00 35.48  ? 43  PHE A CE2 1 
ATOM   406  C  CZ  . PHE A 1 42  ? 35.466 -16.441 33.238 1.00 33.41  ? 43  PHE A CZ  1 
ATOM   407  N  N   . ARG A 1 43  ? 39.884 -17.236 27.339 1.00 27.46  ? 44  ARG A N   1 
ATOM   408  C  CA  . ARG A 1 43  ? 40.402 -17.186 25.970 1.00 26.34  ? 44  ARG A CA  1 
ATOM   409  C  C   . ARG A 1 43  ? 39.268 -17.584 25.017 1.00 30.04  ? 44  ARG A C   1 
ATOM   410  O  O   . ARG A 1 43  ? 38.463 -18.467 25.334 1.00 29.04  ? 44  ARG A O   1 
ATOM   411  C  CB  . ARG A 1 43  ? 41.634 -18.109 25.807 1.00 28.59  ? 44  ARG A CB  1 
ATOM   412  C  CG  . ARG A 1 43  ? 42.873 -17.641 26.615 1.00 37.34  ? 44  ARG A CG  1 
ATOM   413  C  CD  . ARG A 1 43  ? 44.196 -18.035 25.952 1.00 46.91  ? 44  ARG A CD  1 
ATOM   414  N  NE  . ARG A 1 43  ? 44.205 -17.613 24.544 1.00 58.85  ? 44  ARG A NE  1 
ATOM   415  C  CZ  . ARG A 1 43  ? 44.812 -16.530 24.069 1.00 71.92  ? 44  ARG A CZ  1 
ATOM   416  N  NH1 . ARG A 1 43  ? 45.563 -15.779 24.862 1.00 65.10  ? 44  ARG A NH1 1 
ATOM   417  N  NH2 . ARG A 1 43  ? 44.715 -16.219 22.785 1.00 54.33  ? 44  ARG A NH2 1 
ATOM   418  N  N   . ALA A 1 44  ? 39.167 -16.917 23.860 1.00 26.09  ? 45  ALA A N   1 
ATOM   419  C  CA  . ALA A 1 44  ? 38.092 -17.236 22.905 1.00 26.08  ? 45  ALA A CA  1 
ATOM   420  C  C   . ALA A 1 44  ? 38.502 -16.828 21.503 1.00 27.10  ? 45  ALA A C   1 
ATOM   421  O  O   . ALA A 1 44  ? 39.594 -16.270 21.305 1.00 26.90  ? 45  ALA A O   1 
ATOM   422  C  CB  . ALA A 1 44  ? 36.810 -16.490 23.306 1.00 26.44  ? 45  ALA A CB  1 
ATOM   423  N  N   . HIS A 1 45  ? 37.597 -17.057 20.542 1.00 23.83  ? 46  HIS A N   1 
ATOM   424  C  CA  . HIS A 1 45  ? 37.768 -16.647 19.160 1.00 22.71  ? 46  HIS A CA  1 
ATOM   425  C  C   . HIS A 1 45  ? 36.888 -15.412 18.976 1.00 26.23  ? 46  HIS A C   1 
ATOM   426  O  O   . HIS A 1 45  ? 35.675 -15.464 19.248 1.00 24.93  ? 46  HIS A O   1 
ATOM   427  C  CB  . HIS A 1 45  ? 37.310 -17.762 18.196 1.00 22.25  ? 46  HIS A CB  1 
ATOM   428  C  CG  . HIS A 1 45  ? 38.052 -19.049 18.391 1.00 26.16  ? 46  HIS A CG  1 
ATOM   429  N  ND1 . HIS A 1 45  ? 37.519 -20.082 19.139 1.00 27.95  ? 46  HIS A ND1 1 
ATOM   430  C  CD2 . HIS A 1 45  ? 39.299 -19.401 17.983 1.00 27.15  ? 46  HIS A CD2 1 
ATOM   431  C  CE1 . HIS A 1 45  ? 38.447 -21.033 19.157 1.00 27.59  ? 46  HIS A CE1 1 
ATOM   432  N  NE2 . HIS A 1 45  ? 39.537 -20.667 18.479 1.00 27.20  ? 46  HIS A NE2 1 
ATOM   433  N  N   . LYS A 1 46  ? 37.495 -14.307 18.551 1.00 23.92  ? 47  LYS A N   1 
ATOM   434  C  CA  . LYS A 1 46  ? 36.763 -13.064 18.257 1.00 24.64  ? 47  LYS A CA  1 
ATOM   435  C  C   . LYS A 1 46  ? 35.535 -13.309 17.376 1.00 26.93  ? 47  LYS A C   1 
ATOM   436  O  O   . LYS A 1 46  ? 34.462 -12.794 17.687 1.00 24.68  ? 47  LYS A O   1 
ATOM   437  C  CB  . LYS A 1 46  ? 37.675 -12.055 17.539 1.00 27.18  ? 47  LYS A CB  1 
ATOM   438  C  CG  . LYS A 1 46  ? 38.707 -11.426 18.454 1.00 28.11  ? 47  LYS A CG  1 
ATOM   439  C  CD  . LYS A 1 46  ? 39.626 -10.496 17.664 1.00 29.33  ? 47  LYS A CD  1 
ATOM   440  C  CE  . LYS A 1 46  ? 40.792 -10.087 18.522 1.00 34.44  ? 47  LYS A CE  1 
ATOM   441  N  NZ  . LYS A 1 46  ? 41.696 -9.138  17.814 1.00 35.61  ? 47  LYS A NZ  1 
ATOM   442  N  N   . THR A 1 47  ? 35.670 -14.103 16.293 1.00 24.15  ? 48  THR A N   1 
ATOM   443  C  CA  . THR A 1 47  ? 34.513 -14.311 15.413 1.00 24.40  ? 48  THR A CA  1 
ATOM   444  C  C   . THR A 1 47  ? 33.340 -14.984 16.089 1.00 25.14  ? 48  THR A C   1 
ATOM   445  O  O   . THR A 1 47  ? 32.201 -14.599 15.814 1.00 23.60  ? 48  THR A O   1 
ATOM   446  C  CB  . THR A 1 47  ? 34.895 -15.030 14.129 1.00 30.40  ? 48  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 47  ? 35.493 -16.258 14.489 1.00 30.36  ? 48  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 47  ? 35.822 -14.178 13.251 1.00 32.71  ? 48  THR A CG2 1 
ATOM   449  N  N   . VAL A 1 48  ? 33.596 -15.960 16.967 1.00 22.14  ? 49  VAL A N   1 
ATOM   450  C  CA  . VAL A 1 48  ? 32.494 -16.640 17.674 1.00 21.81  ? 49  VAL A CA  1 
ATOM   451  C  C   . VAL A 1 48  ? 31.813 -15.634 18.633 1.00 24.17  ? 49  VAL A C   1 
ATOM   452  O  O   . VAL A 1 48  ? 30.576 -15.593 18.721 1.00 23.27  ? 49  VAL A O   1 
ATOM   453  C  CB  . VAL A 1 48  ? 32.985 -17.905 18.430 1.00 24.59  ? 49  VAL A CB  1 
ATOM   454  C  CG1 . VAL A 1 48  ? 31.845 -18.491 19.285 1.00 24.28  ? 49  VAL A CG1 1 
ATOM   455  C  CG2 . VAL A 1 48  ? 33.512 -18.953 17.436 1.00 24.73  ? 49  VAL A CG2 1 
ATOM   456  N  N   . LEU A 1 49  ? 32.631 -14.841 19.364 1.00 21.98  ? 50  LEU A N   1 
ATOM   457  C  CA  . LEU A 1 49  ? 32.083 -13.828 20.286 1.00 21.99  ? 50  LEU A CA  1 
ATOM   458  C  C   . LEU A 1 49  ? 31.190 -12.843 19.518 1.00 24.67  ? 50  LEU A C   1 
ATOM   459  O  O   . LEU A 1 49  ? 30.083 -12.548 19.958 1.00 24.05  ? 50  LEU A O   1 
ATOM   460  C  CB  . LEU A 1 49  ? 33.230 -13.053 20.977 1.00 22.08  ? 50  LEU A CB  1 
ATOM   461  C  CG  . LEU A 1 49  ? 34.163 -13.859 21.908 1.00 24.36  ? 50  LEU A CG  1 
ATOM   462  C  CD1 . LEU A 1 49  ? 35.227 -12.928 22.525 1.00 24.77  ? 50  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A 1 49  ? 33.360 -14.594 22.998 1.00 24.97  ? 50  LEU A CD2 1 
ATOM   464  N  N   . MET A 1 50  ? 31.635 -12.399 18.343 1.00 21.85  ? 51  MET A N   1 
ATOM   465  C  CA  . MET A 1 50  ? 30.861 -11.460 17.502 1.00 22.85  ? 51  MET A CA  1 
ATOM   466  C  C   . MET A 1 50  ? 29.580 -12.100 17.007 1.00 25.91  ? 51  MET A C   1 
ATOM   467  O  O   . MET A 1 50  ? 28.540 -11.450 17.020 1.00 26.32  ? 51  MET A O   1 
ATOM   468  C  CB  . MET A 1 50  ? 31.675 -11.010 16.289 1.00 25.14  ? 51  MET A CB  1 
ATOM   469  C  CG  . MET A 1 50  ? 32.895 -10.217 16.672 1.00 28.64  ? 51  MET A CG  1 
ATOM   470  S  SD  . MET A 1 50  ? 33.920 -10.075 15.209 1.00 32.79  ? 51  MET A SD  1 
ATOM   471  C  CE  . MET A 1 50  ? 33.126 -8.697  14.457 1.00 29.29  ? 51  MET A CE  1 
ATOM   472  N  N   . ALA A 1 51  ? 29.633 -13.384 16.602 1.00 22.85  ? 52  ALA A N   1 
ATOM   473  C  CA  . ALA A 1 51  ? 28.457 -14.101 16.083 1.00 23.10  ? 52  ALA A CA  1 
ATOM   474  C  C   . ALA A 1 51  ? 27.352 -14.280 17.149 1.00 26.69  ? 52  ALA A C   1 
ATOM   475  O  O   . ALA A 1 51  ? 26.188 -14.476 16.794 1.00 25.76  ? 52  ALA A O   1 
ATOM   476  C  CB  . ALA A 1 51  ? 28.886 -15.480 15.555 1.00 23.17  ? 52  ALA A CB  1 
ATOM   477  N  N   . CYS A 1 52  ? 27.729 -14.240 18.440 1.00 23.96  ? 53  CYS A N   1 
ATOM   478  C  CA  . CYS A 1 52  ? 26.836 -14.472 19.578 1.00 24.35  ? 53  CYS A CA  1 
ATOM   479  C  C   . CYS A 1 52  ? 26.391 -13.246 20.359 1.00 26.49  ? 53  CYS A C   1 
ATOM   480  O  O   . CYS A 1 52  ? 25.443 -13.356 21.145 1.00 25.69  ? 53  CYS A O   1 
ATOM   481  C  CB  . CYS A 1 52  ? 27.508 -15.453 20.525 1.00 24.73  ? 53  CYS A CB  1 
ATOM   482  S  SG  . CYS A 1 52  ? 27.802 -17.080 19.807 1.00 27.46  ? 53  CYS A SG  1 
ATOM   483  N  N   . SER A 1 53  ? 27.161 -12.154 20.292 1.00 23.64  ? 54  SER A N   1 
ATOM   484  C  CA  . SER A 1 53  ? 26.954 -11.010 21.176 1.00 22.00  ? 54  SER A CA  1 
ATOM   485  C  C   . SER A 1 53  ? 26.979 -9.690  20.422 1.00 27.08  ? 54  SER A C   1 
ATOM   486  O  O   . SER A 1 53  ? 27.941 -9.423  19.702 1.00 25.76  ? 54  SER A O   1 
ATOM   487  C  CB  . SER A 1 53  ? 28.070 -11.056 22.223 1.00 23.14  ? 54  SER A CB  1 
ATOM   488  O  OG  . SER A 1 53  ? 28.404 -9.809  22.806 1.00 27.98  ? 54  SER A OG  1 
ATOM   489  N  N   . GLY A 1 54  ? 25.946 -8.867  20.624 1.00 26.20  ? 55  GLY A N   1 
ATOM   490  C  CA  . GLY A 1 54  ? 25.873 -7.534  20.035 1.00 26.69  ? 55  GLY A CA  1 
ATOM   491  C  C   . GLY A 1 54  ? 26.991 -6.652  20.553 1.00 29.71  ? 55  GLY A C   1 
ATOM   492  O  O   . GLY A 1 54  ? 27.533 -5.825  19.808 1.00 28.59  ? 55  GLY A O   1 
ATOM   493  N  N   . LEU A 1 55  ? 27.395 -6.862  21.832 1.00 26.40  ? 56  LEU A N   1 
ATOM   494  C  CA  . LEU A 1 55  ? 28.504 -6.080  22.402 1.00 25.86  ? 56  LEU A CA  1 
ATOM   495  C  C   . LEU A 1 55  ? 29.832 -6.419  21.703 1.00 27.59  ? 56  LEU A C   1 
ATOM   496  O  O   . LEU A 1 55  ? 30.528 -5.507  21.252 1.00 26.58  ? 56  LEU A O   1 
ATOM   497  C  CB  . LEU A 1 55  ? 28.620 -6.280  23.926 1.00 25.46  ? 56  LEU A CB  1 
ATOM   498  C  CG  . LEU A 1 55  ? 29.666 -5.360  24.611 1.00 30.51  ? 56  LEU A CG  1 
ATOM   499  C  CD1 . LEU A 1 55  ? 29.219 -3.873  24.611 1.00 32.23  ? 56  LEU A CD1 1 
ATOM   500  C  CD2 . LEU A 1 55  ? 29.970 -5.829  26.013 1.00 31.25  ? 56  LEU A CD2 1 
ATOM   501  N  N   . PHE A 1 56  ? 30.166 -7.717  21.590 1.00 23.81  ? 57  PHE A N   1 
ATOM   502  C  CA  . PHE A 1 56  ? 31.415 -8.112  20.917 1.00 22.77  ? 57  PHE A CA  1 
ATOM   503  C  C   . PHE A 1 56  ? 31.389 -7.786  19.449 1.00 27.41  ? 57  PHE A C   1 
ATOM   504  O  O   . PHE A 1 56  ? 32.418 -7.405  18.917 1.00 26.44  ? 57  PHE A O   1 
ATOM   505  C  CB  . PHE A 1 56  ? 31.789 -9.565  21.178 1.00 23.21  ? 57  PHE A CB  1 
ATOM   506  C  CG  . PHE A 1 56  ? 32.224 -9.802  22.612 1.00 24.16  ? 57  PHE A CG  1 
ATOM   507  C  CD1 . PHE A 1 56  ? 33.312 -9.111  23.153 1.00 26.66  ? 57  PHE A CD1 1 
ATOM   508  C  CD2 . PHE A 1 56  ? 31.585 -10.760 23.403 1.00 25.94  ? 57  PHE A CD2 1 
ATOM   509  C  CE1 . PHE A 1 56  ? 33.707 -9.316  24.485 1.00 27.93  ? 57  PHE A CE1 1 
ATOM   510  C  CE2 . PHE A 1 56  ? 32.009 -10.996 24.725 1.00 28.51  ? 57  PHE A CE2 1 
ATOM   511  C  CZ  . PHE A 1 56  ? 33.048 -10.248 25.265 1.00 26.21  ? 57  PHE A CZ  1 
ATOM   512  N  N   . TYR A 1 57  ? 30.208 -7.862  18.806 1.00 26.10  ? 58  TYR A N   1 
ATOM   513  C  CA  . TYR A 1 57  ? 30.099 -7.450  17.403 1.00 26.78  ? 58  TYR A CA  1 
ATOM   514  C  C   . TYR A 1 57  ? 30.543 -5.976  17.241 1.00 31.16  ? 58  TYR A C   1 
ATOM   515  O  O   . TYR A 1 57  ? 31.342 -5.657  16.351 1.00 29.57  ? 58  TYR A O   1 
ATOM   516  C  CB  . TYR A 1 57  ? 28.663 -7.652  16.915 1.00 28.67  ? 58  TYR A CB  1 
ATOM   517  C  CG  . TYR A 1 57  ? 28.454 -7.154  15.507 1.00 32.46  ? 58  TYR A CG  1 
ATOM   518  C  CD1 . TYR A 1 57  ? 29.025 -7.812  14.421 1.00 33.81  ? 58  TYR A CD1 1 
ATOM   519  C  CD2 . TYR A 1 57  ? 27.683 -6.025  15.259 1.00 37.02  ? 58  TYR A CD2 1 
ATOM   520  C  CE1 . TYR A 1 57  ? 28.839 -7.347  13.118 1.00 35.87  ? 58  TYR A CE1 1 
ATOM   521  C  CE2 . TYR A 1 57  ? 27.494 -5.552  13.965 1.00 40.47  ? 58  TYR A CE2 1 
ATOM   522  C  CZ  . TYR A 1 57  ? 28.062 -6.225  12.901 1.00 46.96  ? 58  TYR A CZ  1 
ATOM   523  O  OH  . TYR A 1 57  ? 27.849 -5.751  11.642 1.00 54.22  ? 58  TYR A OH  1 
ATOM   524  N  N   A SER A 1 58  ? 30.033 -5.085  18.107 0.52 29.01  ? 59  SER A N   1 
ATOM   525  N  N   B SER A 1 58  ? 30.026 -5.097  18.111 0.48 29.18  ? 59  SER A N   1 
ATOM   526  C  CA  A SER A 1 58  ? 30.368 -3.661  18.085 0.52 29.91  ? 59  SER A CA  1 
ATOM   527  C  CA  B SER A 1 58  ? 30.345 -3.675  18.121 0.48 30.19  ? 59  SER A CA  1 
ATOM   528  C  C   A SER A 1 58  ? 31.847 -3.412  18.412 0.52 34.78  ? 59  SER A C   1 
ATOM   529  C  C   B SER A 1 58  ? 31.842 -3.454  18.383 0.48 34.63  ? 59  SER A C   1 
ATOM   530  O  O   A SER A 1 58  ? 32.476 -2.587  17.755 0.52 36.27  ? 59  SER A O   1 
ATOM   531  O  O   B SER A 1 58  ? 32.480 -2.709  17.643 0.48 35.73  ? 59  SER A O   1 
ATOM   532  C  CB  A SER A 1 58  ? 29.459 -2.887  19.036 0.52 32.62  ? 59  SER A CB  1 
ATOM   533  C  CB  B SER A 1 58  ? 29.503 -2.959  19.175 0.48 33.55  ? 59  SER A CB  1 
ATOM   534  O  OG  A SER A 1 58  ? 28.116 -2.957  18.588 0.52 34.86  ? 59  SER A OG  1 
ATOM   535  O  OG  B SER A 1 58  ? 29.772 -1.568  19.180 0.48 40.06  ? 59  SER A OG  1 
ATOM   536  N  N   . ILE A 1 59  ? 32.402 -4.140  19.402 1.00 30.43  ? 60  ILE A N   1 
ATOM   537  C  CA  . ILE A 1 59  ? 33.816 -4.027  19.811 1.00 29.90  ? 60  ILE A CA  1 
ATOM   538  C  C   . ILE A 1 59  ? 34.762 -4.429  18.680 1.00 32.66  ? 60  ILE A C   1 
ATOM   539  O  O   . ILE A 1 59  ? 35.682 -3.672  18.369 1.00 33.60  ? 60  ILE A O   1 
ATOM   540  C  CB  . ILE A 1 59  ? 34.130 -4.869  21.108 1.00 31.44  ? 60  ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 59  ? 33.413 -4.314  22.357 1.00 31.71  ? 60  ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 59  ? 35.650 -5.014  21.353 1.00 29.89  ? 60  ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 59  ? 33.417 -5.305  23.587 1.00 33.85  ? 60  ILE A CD1 1 
ATOM   544  N  N   . PHE A 1 60  ? 34.560 -5.615  18.083 1.00 28.09  ? 61  PHE A N   1 
ATOM   545  C  CA  . PHE A 1 60  ? 35.533 -6.075  17.104 1.00 27.87  ? 61  PHE A CA  1 
ATOM   546  C  C   . PHE A 1 60  ? 35.300 -5.531  15.692 1.00 32.06  ? 61  PHE A C   1 
ATOM   547  O  O   . PHE A 1 60  ? 36.123 -5.800  14.829 1.00 32.56  ? 61  PHE A O   1 
ATOM   548  C  CB  . PHE A 1 60  ? 35.671 -7.609  17.139 1.00 27.68  ? 61  PHE A CB  1 
ATOM   549  C  CG  . PHE A 1 60  ? 36.088 -8.112  18.506 1.00 27.72  ? 61  PHE A CG  1 
ATOM   550  C  CD1 . PHE A 1 60  ? 37.290 -7.701  19.085 1.00 31.37  ? 61  PHE A CD1 1 
ATOM   551  C  CD2 . PHE A 1 60  ? 35.284 -8.998  19.212 1.00 28.88  ? 61  PHE A CD2 1 
ATOM   552  C  CE1 . PHE A 1 60  ? 37.668 -8.165  20.355 1.00 31.96  ? 61  PHE A CE1 1 
ATOM   553  C  CE2 . PHE A 1 60  ? 35.673 -9.479  20.469 1.00 31.79  ? 61  PHE A CE2 1 
ATOM   554  C  CZ  . PHE A 1 60  ? 36.846 -9.041  21.044 1.00 30.08  ? 61  PHE A CZ  1 
ATOM   555  N  N   . THR A 1 61  ? 34.253 -4.712  15.465 1.00 29.68  ? 62  THR A N   1 
ATOM   556  C  CA  . THR A 1 61  ? 34.098 -4.035  14.166 1.00 30.66  ? 62  THR A CA  1 
ATOM   557  C  C   . THR A 1 61  ? 34.636 -2.605  14.289 1.00 37.62  ? 62  THR A C   1 
ATOM   558  O  O   . THR A 1 61  ? 34.702 -1.870  13.301 1.00 38.15  ? 62  THR A O   1 
ATOM   559  C  CB  . THR A 1 61  ? 32.672 -4.066  13.613 1.00 37.49  ? 62  THR A CB  1 
ATOM   560  O  OG1 . THR A 1 61  ? 31.781 -3.581  14.603 1.00 34.72  ? 62  THR A OG1 1 
ATOM   561  C  CG2 . THR A 1 61  ? 32.255 -5.452  13.106 1.00 33.68  ? 62  THR A CG2 1 
ATOM   562  N  N   . ASP A 1 62  ? 35.069 -2.230  15.496 1.00 33.89  ? 63  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 62  ? 35.667 -0.919  15.714 1.00 35.63  ? 63  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 62  ? 37.105 -1.003  15.210 1.00 42.18  ? 63  ASP A C   1 
ATOM   565  O  O   . ASP A 1 62  ? 37.846 -1.891  15.634 1.00 40.42  ? 63  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 62  ? 35.630 -0.532  17.198 1.00 36.91  ? 63  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 62  ? 36.406 0.741   17.432 1.00 52.82  ? 63  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 62  ? 35.812 1.825   17.295 1.00 57.89  ? 63  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 62  ? 37.631 0.653   17.679 1.00 55.81  ? 63  ASP A OD2 1 
ATOM   570  N  N   . GLN A 1 63  ? 37.502 -0.055  14.339 1.00 43.42  ? 64  GLN A N   1 
ATOM   571  C  CA  . GLN A 1 63  ? 38.813 0.014   13.690 1.00 45.21  ? 64  GLN A CA  1 
ATOM   572  C  C   . GLN A 1 63  ? 40.009 -0.045  14.647 1.00 50.07  ? 64  GLN A C   1 
ATOM   573  O  O   . GLN A 1 63  ? 41.051 -0.554  14.237 1.00 52.48  ? 64  GLN A O   1 
ATOM   574  C  CB  . GLN A 1 63  ? 38.913 1.243   12.772 1.00 49.07  ? 64  GLN A CB  1 
ATOM   575  C  CG  . GLN A 1 63  ? 38.045 1.145   11.519 1.00 71.11  ? 64  GLN A CG  1 
ATOM   576  N  N   . LEU A 1 64  ? 39.882 0.467   15.903 1.00 43.21  ? 65  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 64  ? 40.976 0.391   16.883 1.00 42.20  ? 65  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 64  ? 40.887 -0.858  17.739 1.00 45.09  ? 65  LEU A C   1 
ATOM   579  O  O   . LEU A 1 64  ? 41.908 -1.475  18.023 1.00 47.08  ? 65  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 64  ? 40.986 1.604   17.835 1.00 43.15  ? 65  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 64  ? 41.628 2.891   17.364 1.00 50.31  ? 65  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 64  ? 41.425 3.966   18.396 1.00 50.71  ? 65  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 64  ? 43.123 2.719   17.093 1.00 54.78  ? 65  LEU A CD2 1 
ATOM   584  N  N   . LYS A 1 65  ? 39.684 -1.187  18.227 1.00 37.39  ? 66  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 65  ? 39.512 -2.305  19.149 1.00 35.79  ? 66  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 65  ? 39.635 -3.667  18.473 1.00 40.41  ? 66  LYS A C   1 
ATOM   587  O  O   . LYS A 1 65  ? 39.998 -4.625  19.150 1.00 39.02  ? 66  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 65  ? 38.194 -2.196  19.936 1.00 36.33  ? 66  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 65  ? 38.049 -0.909  20.747 1.00 34.70  ? 66  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 65  ? 36.801 -1.017  21.626 1.00 33.14  ? 66  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 65  ? 36.491 0.309   22.290 1.00 38.11  ? 66  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 65  ? 35.901 1.289   21.355 1.00 41.25  ? 66  LYS A NZ  1 
ATOM   593  N  N   . CYS A 1 66  ? 39.362 -3.754  17.146 1.00 40.00  ? 67  CYS A N   1 
ATOM   594  C  CA  . CYS A 1 66  ? 39.455 -5.018  16.388 1.00 40.45  ? 67  CYS A CA  1 
ATOM   595  C  C   . CYS A 1 66  ? 40.842 -5.666  16.518 1.00 45.47  ? 67  CYS A C   1 
ATOM   596  O  O   . CYS A 1 66  ? 40.963 -6.882  16.347 1.00 45.59  ? 67  CYS A O   1 
ATOM   597  C  CB  . CYS A 1 66  ? 39.072 -4.814  14.923 1.00 42.29  ? 67  CYS A CB  1 
ATOM   598  S  SG  . CYS A 1 66  ? 40.249 -3.808  13.967 1.00 48.54  ? 67  CYS A SG  1 
ATOM   599  N  N   . ASN A 1 67  ? 41.875 -4.837  16.806 1.00 41.95  ? 68  ASN A N   1 
ATOM   600  C  CA  . ASN A 1 67  ? 43.284 -5.209  16.929 1.00 43.16  ? 68  ASN A CA  1 
ATOM   601  C  C   . ASN A 1 67  ? 43.769 -5.507  18.353 1.00 46.18  ? 68  ASN A C   1 
ATOM   602  O  O   . ASN A 1 67  ? 44.936 -5.867  18.541 1.00 46.12  ? 68  ASN A O   1 
ATOM   603  C  CB  . ASN A 1 67  ? 44.164 -4.132  16.280 1.00 45.31  ? 68  ASN A CB  1 
ATOM   604  C  CG  . ASN A 1 67  ? 43.988 -4.088  14.775 1.00 61.96  ? 68  ASN A CG  1 
ATOM   605  O  OD1 . ASN A 1 67  ? 43.950 -3.020  14.164 1.00 62.17  ? 68  ASN A OD1 1 
ATOM   606  N  ND2 . ASN A 1 67  ? 43.840 -5.248  14.144 1.00 50.62  ? 68  ASN A ND2 1 
ATOM   607  N  N   . LEU A 1 68  ? 42.888 -5.374  19.344 1.00 41.03  ? 69  LEU A N   1 
ATOM   608  C  CA  . LEU A 1 68  ? 43.254 -5.637  20.729 1.00 39.92  ? 69  LEU A CA  1 
ATOM   609  C  C   . LEU A 1 68  ? 43.236 -7.143  21.002 1.00 40.67  ? 69  LEU A C   1 
ATOM   610  O  O   . LEU A 1 68  ? 42.327 -7.835  20.521 1.00 38.37  ? 69  LEU A O   1 
ATOM   611  C  CB  . LEU A 1 68  ? 42.263 -4.930  21.681 1.00 39.92  ? 69  LEU A CB  1 
ATOM   612  C  CG  . LEU A 1 68  ? 42.258 -3.390  21.653 1.00 45.13  ? 69  LEU A CG  1 
ATOM   613  C  CD1 . LEU A 1 68  ? 41.217 -2.840  22.606 1.00 44.89  ? 69  LEU A CD1 1 
ATOM   614  C  CD2 . LEU A 1 68  ? 43.645 -2.807  21.989 1.00 47.19  ? 69  LEU A CD2 1 
ATOM   615  N  N   . SER A 1 69  ? 44.229 -7.628  21.783 1.00 36.65  ? 70  SER A N   1 
ATOM   616  C  CA  A SER A 1 69  ? 44.342 -9.037  22.174 0.42 36.17  ? 70  SER A CA  1 
ATOM   617  C  CA  B SER A 1 69  ? 44.307 -9.044  22.156 0.58 36.40  ? 70  SER A CA  1 
ATOM   618  C  C   . SER A 1 69  ? 43.701 -9.244  23.552 1.00 37.79  ? 70  SER A C   1 
ATOM   619  O  O   . SER A 1 69  ? 43.489 -10.374 23.975 1.00 34.27  ? 70  SER A O   1 
ATOM   620  C  CB  A SER A 1 69  ? 45.808 -9.463  22.209 0.42 40.88  ? 70  SER A CB  1 
ATOM   621  C  CB  B SER A 1 69  ? 45.752 -9.540  22.111 0.58 41.23  ? 70  SER A CB  1 
ATOM   622  O  OG  A SER A 1 69  ? 46.408 -9.357  20.930 0.42 47.99  ? 70  SER A OG  1 
ATOM   623  O  OG  B SER A 1 69  ? 46.575 -8.801  22.996 0.58 48.97  ? 70  SER A OG  1 
ATOM   624  N  N   . VAL A 1 70  ? 43.430 -8.136  24.273 1.00 34.70  ? 71  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 70  ? 42.825 -8.165  25.615 1.00 33.55  ? 71  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 70  ? 41.634 -7.202  25.663 1.00 34.77  ? 71  VAL A C   1 
ATOM   627  O  O   . VAL A 1 70  ? 41.771 -6.034  25.266 1.00 34.95  ? 71  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 70  ? 43.862 -7.835  26.738 1.00 39.66  ? 71  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 70  ? 43.225 -7.895  28.130 1.00 39.61  ? 71  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 70  ? 45.089 -8.750  26.669 1.00 40.42  ? 71  VAL A CG2 1 
ATOM   631  N  N   . ILE A 1 71  ? 40.484 -7.683  26.177 1.00 28.17  ? 72  ILE A N   1 
ATOM   632  C  CA  . ILE A 1 71  ? 39.278 -6.873  26.376 1.00 27.47  ? 72  ILE A CA  1 
ATOM   633  C  C   . ILE A 1 71  ? 38.880 -6.974  27.845 1.00 31.91  ? 72  ILE A C   1 
ATOM   634  O  O   . ILE A 1 71  ? 38.647 -8.080  28.337 1.00 31.54  ? 72  ILE A O   1 
ATOM   635  C  CB  . ILE A 1 71  ? 38.098 -7.245  25.412 1.00 29.11  ? 72  ILE A CB  1 
ATOM   636  C  CG1 . ILE A 1 71  ? 38.479 -7.107  23.901 1.00 30.40  ? 72  ILE A CG1 1 
ATOM   637  C  CG2 . ILE A 1 71  ? 36.812 -6.461  25.742 1.00 30.69  ? 72  ILE A CG2 1 
ATOM   638  C  CD1 . ILE A 1 71  ? 38.836 -5.646  23.390 1.00 36.80  ? 72  ILE A CD1 1 
ATOM   639  N  N   . ASN A 1 72  ? 38.760 -5.829  28.528 1.00 28.72  ? 73  ASN A N   1 
ATOM   640  C  CA  . ASN A 1 72  ? 38.347 -5.792  29.923 1.00 28.43  ? 73  ASN A CA  1 
ATOM   641  C  C   . ASN A 1 72  ? 36.863 -5.470  30.034 1.00 31.84  ? 73  ASN A C   1 
ATOM   642  O  O   . ASN A 1 72  ? 36.430 -4.394  29.605 1.00 31.18  ? 73  ASN A O   1 
ATOM   643  C  CB  . ASN A 1 72  ? 39.165 -4.742  30.711 1.00 32.83  ? 73  ASN A CB  1 
ATOM   644  C  CG  . ASN A 1 72  ? 40.646 -4.950  30.649 1.00 51.23  ? 73  ASN A CG  1 
ATOM   645  O  OD1 . ASN A 1 72  ? 41.163 -5.980  31.050 1.00 42.12  ? 73  ASN A OD1 1 
ATOM   646  N  ND2 . ASN A 1 72  ? 41.365 -3.971  30.153 1.00 49.35  ? 73  ASN A ND2 1 
ATOM   647  N  N   . LEU A 1 73  ? 36.095 -6.358  30.660 1.00 27.16  ? 74  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 73  ? 34.674 -6.096  30.865 1.00 26.60  ? 74  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 73  ? 34.443 -5.201  32.078 1.00 30.02  ? 74  LEU A C   1 
ATOM   650  O  O   . LEU A 1 73  ? 35.321 -5.063  32.945 1.00 31.14  ? 74  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 73  ? 33.861 -7.394  30.995 1.00 26.50  ? 74  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 73  ? 33.935 -8.381  29.807 1.00 29.70  ? 74  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 73  ? 32.827 -9.442  29.931 1.00 29.14  ? 74  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 73  ? 33.874 -7.664  28.429 1.00 30.92  ? 74  LEU A CD2 1 
ATOM   655  N  N   . ASP A 1 74  ? 33.251 -4.603  32.137 1.00 26.70  ? 75  ASP A N   1 
ATOM   656  C  CA  . ASP A 1 74  ? 32.831 -3.701  33.220 1.00 28.34  ? 75  ASP A CA  1 
ATOM   657  C  C   . ASP A 1 74  ? 33.006 -4.446  34.559 1.00 34.80  ? 75  ASP A C   1 
ATOM   658  O  O   . ASP A 1 74  ? 32.640 -5.622  34.628 1.00 32.79  ? 75  ASP A O   1 
ATOM   659  C  CB  . ASP A 1 74  ? 31.357 -3.315  32.999 1.00 29.86  ? 75  ASP A CB  1 
ATOM   660  C  CG  . ASP A 1 74  ? 30.805 -2.302  33.988 1.00 41.66  ? 75  ASP A CG  1 
ATOM   661  O  OD1 . ASP A 1 74  ? 30.646 -2.654  35.179 1.00 42.76  ? 75  ASP A OD1 1 
ATOM   662  O  OD2 . ASP A 1 74  ? 30.493 -1.179  33.565 1.00 43.58  ? 75  ASP A OD2 1 
ATOM   663  N  N   . PRO A 1 75  ? 33.589 -3.812  35.606 1.00 35.97  ? 76  PRO A N   1 
ATOM   664  C  CA  . PRO A 1 75  ? 33.792 -4.529  36.887 1.00 36.62  ? 76  PRO A CA  1 
ATOM   665  C  C   . PRO A 1 75  ? 32.547 -5.104  37.545 1.00 39.85  ? 76  PRO A C   1 
ATOM   666  O  O   . PRO A 1 75  ? 32.685 -5.982  38.389 1.00 40.33  ? 76  PRO A O   1 
ATOM   667  C  CB  . PRO A 1 75  ? 34.468 -3.491  37.794 1.00 39.58  ? 76  PRO A CB  1 
ATOM   668  C  CG  . PRO A 1 75  ? 34.199 -2.165  37.149 1.00 44.28  ? 76  PRO A CG  1 
ATOM   669  C  CD  . PRO A 1 75  ? 34.120 -2.431  35.674 1.00 38.17  ? 76  PRO A CD  1 
ATOM   670  N  N   . GLU A 1 76  ? 31.343 -4.651  37.165 1.00 36.66  ? 77  GLU A N   1 
ATOM   671  C  CA  . GLU A 1 76  ? 30.110 -5.189  37.739 1.00 37.63  ? 77  GLU A CA  1 
ATOM   672  C  C   . GLU A 1 76  ? 29.797 -6.588  37.185 1.00 37.89  ? 77  GLU A C   1 
ATOM   673  O  O   . GLU A 1 76  ? 28.951 -7.285  37.743 1.00 37.58  ? 77  GLU A O   1 
ATOM   674  C  CB  . GLU A 1 76  ? 28.923 -4.240  37.486 1.00 40.29  ? 77  GLU A CB  1 
ATOM   675  C  CG  . GLU A 1 76  ? 28.890 -3.027  38.406 1.00 60.37  ? 77  GLU A CG  1 
ATOM   676  C  CD  . GLU A 1 76  ? 28.365 -3.306  39.802 1.00 94.04  ? 77  GLU A CD  1 
ATOM   677  O  OE1 . GLU A 1 76  ? 27.134 -3.487  39.950 1.00 94.17  ? 77  GLU A OE1 1 
ATOM   678  O  OE2 . GLU A 1 76  ? 29.186 -3.352  40.747 1.00 93.35  ? 77  GLU A OE2 1 
ATOM   679  N  N   . ILE A 1 77  ? 30.470 -6.993  36.085 1.00 31.53  ? 78  ILE A N   1 
ATOM   680  C  CA  . ILE A 1 77  ? 30.222 -8.308  35.481 1.00 30.18  ? 78  ILE A CA  1 
ATOM   681  C  C   . ILE A 1 77  ? 30.824 -9.414  36.329 1.00 34.15  ? 78  ILE A C   1 
ATOM   682  O  O   . ILE A 1 77  ? 32.004 -9.384  36.665 1.00 32.86  ? 78  ILE A O   1 
ATOM   683  C  CB  . ILE A 1 77  ? 30.663 -8.377  33.988 1.00 32.25  ? 78  ILE A CB  1 
ATOM   684  C  CG1 . ILE A 1 77  ? 29.957 -7.282  33.137 1.00 33.59  ? 78  ILE A CG1 1 
ATOM   685  C  CG2 . ILE A 1 77  ? 30.459 -9.796  33.397 1.00 29.16  ? 78  ILE A CG2 1 
ATOM   686  C  CD1 . ILE A 1 77  ? 28.332 -7.268  33.208 1.00 40.81  ? 78  ILE A CD1 1 
ATOM   687  N  N   . ASN A 1 78  ? 30.006 -10.398 36.615 1.00 34.10  ? 79  ASN A N   1 
ATOM   688  C  CA  . ASN A 1 78  ? 30.337 -11.573 37.401 1.00 34.66  ? 79  ASN A CA  1 
ATOM   689  C  C   . ASN A 1 78  ? 31.056 -12.613 36.518 1.00 34.34  ? 79  ASN A C   1 
ATOM   690  O  O   . ASN A 1 78  ? 30.506 -12.999 35.489 1.00 31.41  ? 79  ASN A O   1 
ATOM   691  C  CB  . ASN A 1 78  ? 29.033 -12.143 37.978 1.00 38.89  ? 79  ASN A CB  1 
ATOM   692  C  CG  . ASN A 1 78  ? 29.209 -13.436 38.724 1.00 56.65  ? 79  ASN A CG  1 
ATOM   693  O  OD1 . ASN A 1 78  ? 28.850 -14.501 38.225 1.00 44.18  ? 79  ASN A OD1 1 
ATOM   694  N  ND2 . ASN A 1 78  ? 29.771 -13.365 39.930 1.00 47.24  ? 79  ASN A ND2 1 
ATOM   695  N  N   . PRO A 1 79  ? 32.257 -13.115 36.919 1.00 32.01  ? 80  PRO A N   1 
ATOM   696  C  CA  . PRO A 1 79  ? 32.959 -14.123 36.090 1.00 31.17  ? 80  PRO A CA  1 
ATOM   697  C  C   . PRO A 1 79  ? 32.168 -15.407 35.838 1.00 34.37  ? 80  PRO A C   1 
ATOM   698  O  O   . PRO A 1 79  ? 32.259 -15.953 34.738 1.00 33.55  ? 80  PRO A O   1 
ATOM   699  C  CB  . PRO A 1 79  ? 34.224 -14.423 36.900 1.00 34.39  ? 80  PRO A CB  1 
ATOM   700  C  CG  . PRO A 1 79  ? 34.431 -13.181 37.733 1.00 39.76  ? 80  PRO A CG  1 
ATOM   701  C  CD  . PRO A 1 79  ? 33.050 -12.761 38.114 1.00 35.30  ? 80  PRO A CD  1 
ATOM   702  N  N   . GLU A 1 80  ? 31.397 -15.887 36.833 1.00 31.82  ? 81  GLU A N   1 
ATOM   703  C  CA  . GLU A 1 80  ? 30.622 -17.120 36.634 1.00 31.65  ? 81  GLU A CA  1 
ATOM   704  C  C   . GLU A 1 80  ? 29.531 -16.919 35.565 1.00 33.15  ? 81  GLU A C   1 
ATOM   705  O  O   . GLU A 1 80  ? 29.382 -17.772 34.696 1.00 31.89  ? 81  GLU A O   1 
ATOM   706  C  CB  . GLU A 1 80  ? 30.029 -17.632 37.954 1.00 34.44  ? 81  GLU A CB  1 
ATOM   707  C  CG  . GLU A 1 80  ? 29.438 -19.027 37.797 1.00 45.86  ? 81  GLU A CG  1 
ATOM   708  C  CD  . GLU A 1 80  ? 28.556 -19.539 38.923 1.00 73.96  ? 81  GLU A CD  1 
ATOM   709  O  OE1 . GLU A 1 80  ? 28.480 -20.778 39.085 1.00 69.57  ? 81  GLU A OE1 1 
ATOM   710  O  OE2 . GLU A 1 80  ? 27.934 -18.715 39.635 1.00 70.44  ? 81  GLU A OE2 1 
ATOM   711  N  N   . GLY A 1 81  ? 28.806 -15.791 35.632 1.00 30.08  ? 82  GLY A N   1 
ATOM   712  C  CA  . GLY A 1 81  ? 27.794 -15.446 34.635 1.00 29.50  ? 82  GLY A CA  1 
ATOM   713  C  C   . GLY A 1 81  ? 28.433 -15.371 33.257 1.00 30.58  ? 82  GLY A C   1 
ATOM   714  O  O   . GLY A 1 81  ? 27.880 -15.892 32.277 1.00 28.46  ? 82  GLY A O   1 
ATOM   715  N  N   . PHE A 1 82  ? 29.640 -14.781 33.174 1.00 26.48  ? 83  PHE A N   1 
ATOM   716  C  CA  . PHE A 1 82  ? 30.331 -14.724 31.879 1.00 24.93  ? 83  PHE A CA  1 
ATOM   717  C  C   . PHE A 1 82  ? 30.683 -16.131 31.397 1.00 28.21  ? 83  PHE A C   1 
ATOM   718  O  O   . PHE A 1 82  ? 30.477 -16.450 30.236 1.00 25.95  ? 83  PHE A O   1 
ATOM   719  C  CB  . PHE A 1 82  ? 31.610 -13.859 31.925 1.00 26.17  ? 83  PHE A CB  1 
ATOM   720  C  CG  . PHE A 1 82  ? 32.197 -13.729 30.535 1.00 26.43  ? 83  PHE A CG  1 
ATOM   721  C  CD1 . PHE A 1 82  ? 31.609 -12.891 29.589 1.00 29.03  ? 83  PHE A CD1 1 
ATOM   722  C  CD2 . PHE A 1 82  ? 33.266 -14.525 30.136 1.00 26.51  ? 83  PHE A CD2 1 
ATOM   723  C  CE1 . PHE A 1 82  ? 32.104 -12.828 28.284 1.00 29.10  ? 83  PHE A CE1 1 
ATOM   724  C  CE2 . PHE A 1 82  ? 33.770 -14.449 28.837 1.00 27.91  ? 83  PHE A CE2 1 
ATOM   725  C  CZ  . PHE A 1 82  ? 33.179 -13.612 27.915 1.00 27.28  ? 83  PHE A CZ  1 
ATOM   726  N  N   . CYS A 1 83  ? 31.268 -16.942 32.271 1.00 28.84  ? 84  CYS A N   1 
ATOM   727  C  CA  . CYS A 1 83  ? 31.675 -18.312 31.946 1.00 30.22  ? 84  CYS A CA  1 
ATOM   728  C  C   . CYS A 1 83  ? 30.488 -19.138 31.386 1.00 31.20  ? 84  CYS A C   1 
ATOM   729  O  O   . CYS A 1 83  ? 30.638 -19.834 30.374 1.00 29.43  ? 84  CYS A O   1 
ATOM   730  C  CB  . CYS A 1 83  ? 32.293 -18.979 33.171 1.00 34.09  ? 84  CYS A CB  1 
ATOM   731  S  SG  . CYS A 1 83  ? 32.916 -20.651 32.848 1.00 40.11  ? 84  CYS A SG  1 
ATOM   732  N  N   . ILE A 1 84  ? 29.310 -19.029 32.034 1.00 28.12  ? 85  ILE A N   1 
ATOM   733  C  CA  . ILE A 1 84  ? 28.083 -19.739 31.618 1.00 26.35  ? 85  ILE A CA  1 
ATOM   734  C  C   . ILE A 1 84  ? 27.679 -19.266 30.211 1.00 26.46  ? 85  ILE A C   1 
ATOM   735  O  O   . ILE A 1 84  ? 27.296 -20.085 29.356 1.00 24.85  ? 85  ILE A O   1 
ATOM   736  C  CB  . ILE A 1 84  ? 26.958 -19.521 32.677 1.00 29.89  ? 85  ILE A CB  1 
ATOM   737  C  CG1 . ILE A 1 84  ? 27.251 -20.354 33.965 1.00 31.74  ? 85  ILE A CG1 1 
ATOM   738  C  CG2 . ILE A 1 84  ? 25.537 -19.840 32.112 1.00 29.61  ? 85  ILE A CG2 1 
ATOM   739  C  CD1 . ILE A 1 84  ? 26.580 -19.763 35.195 1.00 40.02  ? 85  ILE A CD1 1 
ATOM   740  N  N   . LEU A 1 85  ? 27.761 -17.958 29.973 1.00 24.00  ? 86  LEU A N   1 
ATOM   741  C  CA  . LEU A 1 85  ? 27.416 -17.411 28.657 1.00 24.16  ? 86  LEU A CA  1 
ATOM   742  C  C   . LEU A 1 85  ? 28.418 -17.785 27.589 1.00 27.41  ? 86  LEU A C   1 
ATOM   743  O  O   . LEU A 1 85  ? 28.023 -18.052 26.452 1.00 25.33  ? 86  LEU A O   1 
ATOM   744  C  CB  . LEU A 1 85  ? 27.181 -15.906 28.738 1.00 25.50  ? 86  LEU A CB  1 
ATOM   745  C  CG  . LEU A 1 85  ? 25.864 -15.554 29.474 1.00 31.85  ? 86  LEU A CG  1 
ATOM   746  C  CD1 . LEU A 1 85  ? 25.777 -14.100 29.686 1.00 33.63  ? 86  LEU A CD1 1 
ATOM   747  C  CD2 . LEU A 1 85  ? 24.633 -16.029 28.678 1.00 32.85  ? 86  LEU A CD2 1 
ATOM   748  N  N   . LEU A 1 86  ? 29.721 -17.824 27.942 1.00 24.86  ? 87  LEU A N   1 
ATOM   749  C  CA  . LEU A 1 86  ? 30.760 -18.232 26.990 1.00 23.81  ? 87  LEU A CA  1 
ATOM   750  C  C   . LEU A 1 86  ? 30.521 -19.691 26.590 1.00 26.63  ? 87  LEU A C   1 
ATOM   751  O  O   . LEU A 1 86  ? 30.587 -20.033 25.411 1.00 25.13  ? 87  LEU A O   1 
ATOM   752  C  CB  . LEU A 1 86  ? 32.158 -18.042 27.601 1.00 23.59  ? 87  LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 86  ? 33.322 -18.334 26.634 1.00 28.56  ? 87  LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 86  ? 33.281 -17.381 25.407 1.00 27.48  ? 87  LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 86  ? 34.688 -18.233 27.378 1.00 31.66  ? 87  LEU A CD2 1 
ATOM   756  N  N   . ASP A 1 87  ? 30.202 -20.549 27.569 1.00 24.48  ? 88  ASP A N   1 
ATOM   757  C  CA  . ASP A 1 87  ? 29.884 -21.938 27.287 1.00 24.36  ? 88  ASP A CA  1 
ATOM   758  C  C   . ASP A 1 87  ? 28.671 -22.034 26.351 1.00 26.57  ? 88  ASP A C   1 
ATOM   759  O  O   . ASP A 1 87  ? 28.697 -22.827 25.421 1.00 27.16  ? 88  ASP A O   1 
ATOM   760  C  CB  . ASP A 1 87  ? 29.593 -22.671 28.598 1.00 27.88  ? 88  ASP A CB  1 
ATOM   761  C  CG  . ASP A 1 87  ? 30.837 -23.042 29.387 1.00 42.90  ? 88  ASP A CG  1 
ATOM   762  O  OD1 . ASP A 1 87  ? 31.959 -22.941 28.820 1.00 42.93  ? 88  ASP A OD1 1 
ATOM   763  O  OD2 . ASP A 1 87  ? 30.694 -23.437 30.575 1.00 46.32  ? 88  ASP A OD2 1 
ATOM   764  N  N   . PHE A 1 88  ? 27.615 -21.241 26.600 1.00 23.61  ? 89  PHE A N   1 
ATOM   765  C  CA  . PHE A 1 88  ? 26.426 -21.191 25.731 1.00 22.93  ? 89  PHE A CA  1 
ATOM   766  C  C   . PHE A 1 88  ? 26.809 -20.810 24.287 1.00 23.65  ? 89  PHE A C   1 
ATOM   767  O  O   . PHE A 1 88  ? 26.319 -21.401 23.317 1.00 22.66  ? 89  PHE A O   1 
ATOM   768  C  CB  . PHE A 1 88  ? 25.368 -20.216 26.306 1.00 24.32  ? 89  PHE A CB  1 
ATOM   769  C  CG  . PHE A 1 88  ? 24.258 -19.942 25.322 1.00 24.97  ? 89  PHE A CG  1 
ATOM   770  C  CD1 . PHE A 1 88  ? 23.281 -20.904 25.063 1.00 26.67  ? 89  PHE A CD1 1 
ATOM   771  C  CD2 . PHE A 1 88  ? 24.231 -18.755 24.590 1.00 26.23  ? 89  PHE A CD2 1 
ATOM   772  C  CE1 . PHE A 1 88  ? 22.283 -20.667 24.122 1.00 26.97  ? 89  PHE A CE1 1 
ATOM   773  C  CE2 . PHE A 1 88  ? 23.238 -18.529 23.629 1.00 29.45  ? 89  PHE A CE2 1 
ATOM   774  C  CZ  . PHE A 1 88  ? 22.275 -19.484 23.398 1.00 27.68  ? 89  PHE A CZ  1 
ATOM   775  N  N   . MET A 1 89  ? 27.647 -19.790 24.138 1.00 21.50  ? 90  MET A N   1 
ATOM   776  C  CA  . MET A 1 89  ? 28.068 -19.353 22.788 1.00 20.72  ? 90  MET A CA  1 
ATOM   777  C  C   . MET A 1 89  ? 28.626 -20.508 21.972 1.00 24.46  ? 90  MET A C   1 
ATOM   778  O  O   . MET A 1 89  ? 28.287 -20.642 20.794 1.00 24.68  ? 90  MET A O   1 
ATOM   779  C  CB  . MET A 1 89  ? 29.150 -18.271 22.919 1.00 21.35  ? 90  MET A CB  1 
ATOM   780  C  CG  . MET A 1 89  ? 28.618 -16.966 23.468 1.00 23.68  ? 90  MET A CG  1 
ATOM   781  S  SD  . MET A 1 89  ? 29.990 -15.761 23.372 1.00 27.41  ? 90  MET A SD  1 
ATOM   782  C  CE  . MET A 1 89  ? 29.345 -14.465 24.497 1.00 27.16  ? 90  MET A CE  1 
ATOM   783  N  N   . TYR A 1 90  ? 29.468 -21.347 22.608 1.00 21.29  ? 91  TYR A N   1 
ATOM   784  C  CA  . TYR A 1 90  ? 30.148 -22.446 21.936 1.00 21.30  ? 91  TYR A CA  1 
ATOM   785  C  C   . TYR A 1 90  ? 29.394 -23.755 21.921 1.00 25.37  ? 91  TYR A C   1 
ATOM   786  O  O   . TYR A 1 90  ? 29.885 -24.710 21.306 1.00 24.57  ? 91  TYR A O   1 
ATOM   787  C  CB  . TYR A 1 90  ? 31.522 -22.665 22.576 1.00 23.20  ? 91  TYR A CB  1 
ATOM   788  C  CG  . TYR A 1 90  ? 32.579 -21.693 22.096 1.00 24.68  ? 91  TYR A CG  1 
ATOM   789  C  CD1 . TYR A 1 90  ? 32.732 -20.444 22.695 1.00 25.79  ? 91  TYR A CD1 1 
ATOM   790  C  CD2 . TYR A 1 90  ? 33.419 -22.017 21.031 1.00 25.07  ? 91  TYR A CD2 1 
ATOM   791  C  CE1 . TYR A 1 90  ? 33.715 -19.554 22.266 1.00 24.90  ? 91  TYR A CE1 1 
ATOM   792  C  CE2 . TYR A 1 90  ? 34.447 -21.162 20.636 1.00 25.37  ? 91  TYR A CE2 1 
ATOM   793  C  CZ  . TYR A 1 90  ? 34.565 -19.916 21.226 1.00 28.10  ? 91  TYR A CZ  1 
ATOM   794  O  OH  . TYR A 1 90  ? 35.596 -19.096 20.839 1.00 26.98  ? 91  TYR A OH  1 
ATOM   795  N  N   . THR A 1 91  ? 28.246 -23.844 22.627 1.00 21.81  ? 92  THR A N   1 
ATOM   796  C  CA  . THR A 1 91  ? 27.551 -25.142 22.691 1.00 23.20  ? 92  THR A CA  1 
ATOM   797  C  C   . THR A 1 91  ? 26.048 -25.103 22.437 1.00 25.24  ? 92  THR A C   1 
ATOM   798  O  O   . THR A 1 91  ? 25.461 -26.167 22.269 1.00 25.88  ? 92  THR A O   1 
ATOM   799  C  CB  . THR A 1 91  ? 27.760 -25.820 24.081 1.00 29.08  ? 92  THR A CB  1 
ATOM   800  O  OG1 . THR A 1 91  ? 27.105 -25.042 25.085 1.00 28.79  ? 92  THR A OG1 1 
ATOM   801  C  CG2 . THR A 1 91  ? 29.232 -26.051 24.452 1.00 28.87  ? 92  THR A CG2 1 
ATOM   802  N  N   . SER A 1 92  ? 25.409 -23.931 22.532 1.00 21.55  ? 93  SER A N   1 
ATOM   803  C  CA  . SER A 1 92  ? 23.929 -23.761 22.479 1.00 21.44  ? 93  SER A CA  1 
ATOM   804  C  C   . SER A 1 92  ? 23.272 -24.167 23.829 1.00 26.46  ? 93  SER A C   1 
ATOM   805  O  O   . SER A 1 92  ? 22.067 -24.016 23.969 1.00 26.61  ? 93  SER A O   1 
ATOM   806  C  CB  . SER A 1 92  ? 23.290 -24.588 21.350 1.00 23.78  ? 93  SER A CB  1 
ATOM   807  O  OG  . SER A 1 92  ? 23.934 -24.384 20.100 1.00 30.21  ? 93  SER A OG  1 
ATOM   808  N  N   A ARG A 1 93  ? 24.073 -24.630 24.805 0.60 24.65  ? 94  ARG A N   1 
ATOM   809  N  N   B ARG A 1 93  ? 24.050 -24.688 24.801 0.40 23.76  ? 94  ARG A N   1 
ATOM   810  C  CA  A ARG A 1 93  ? 23.580 -25.094 26.106 0.60 25.78  ? 94  ARG A CA  1 
ATOM   811  C  CA  B ARG A 1 93  ? 23.488 -25.114 26.089 0.40 24.44  ? 94  ARG A CA  1 
ATOM   812  C  C   A ARG A 1 93  ? 23.781 -24.033 27.174 0.60 29.48  ? 94  ARG A C   1 
ATOM   813  C  C   B ARG A 1 93  ? 23.767 -24.107 27.187 0.40 28.88  ? 94  ARG A C   1 
ATOM   814  O  O   A ARG A 1 93  ? 24.898 -23.529 27.360 0.60 27.15  ? 94  ARG A O   1 
ATOM   815  O  O   B ARG A 1 93  ? 24.915 -23.684 27.380 0.40 27.10  ? 94  ARG A O   1 
ATOM   816  C  CB  A ARG A 1 93  ? 24.279 -26.400 26.524 0.60 28.04  ? 94  ARG A CB  1 
ATOM   817  C  CB  B ARG A 1 93  ? 23.919 -26.539 26.476 0.40 24.81  ? 94  ARG A CB  1 
ATOM   818  C  CG  A ARG A 1 93  ? 24.138 -27.541 25.506 0.60 34.09  ? 94  ARG A CG  1 
ATOM   819  C  CG  B ARG A 1 93  ? 23.273 -27.593 25.582 0.40 24.11  ? 94  ARG A CG  1 
ATOM   820  C  CD  A ARG A 1 93  ? 25.091 -28.684 25.815 0.60 40.88  ? 94  ARG A CD  1 
ATOM   821  C  CD  B ARG A 1 93  ? 23.835 -28.981 25.779 0.40 33.80  ? 94  ARG A CD  1 
ATOM   822  N  NE  A ARG A 1 93  ? 24.855 -29.234 27.154 0.60 44.57  ? 94  ARG A NE  1 
ATOM   823  N  NE  B ARG A 1 93  ? 23.268 -29.922 24.810 0.40 38.49  ? 94  ARG A NE  1 
ATOM   824  C  CZ  A ARG A 1 93  ? 23.974 -30.191 27.428 0.60 56.25  ? 94  ARG A CZ  1 
ATOM   825  C  CZ  B ARG A 1 93  ? 23.294 -31.245 24.938 0.40 50.18  ? 94  ARG A CZ  1 
ATOM   826  N  NH1 A ARG A 1 93  ? 23.815 -30.616 28.672 0.60 42.56  ? 94  ARG A NH1 1 
ATOM   827  N  NH1 B ARG A 1 93  ? 22.753 -32.018 24.004 0.40 40.26  ? 94  ARG A NH1 1 
ATOM   828  N  NH2 A ARG A 1 93  ? 23.242 -30.728 26.458 0.60 41.19  ? 94  ARG A NH2 1 
ATOM   829  N  NH2 B ARG A 1 93  ? 23.846 -31.805 26.005 0.40 38.37  ? 94  ARG A NH2 1 
ATOM   830  N  N   . LEU A 1 94  ? 22.698 -23.696 27.875 1.00 26.39  ? 95  LEU A N   1 
ATOM   831  C  CA  . LEU A 1 94  ? 22.744 -22.692 28.928 1.00 26.20  ? 95  LEU A CA  1 
ATOM   832  C  C   . LEU A 1 94  ? 22.501 -23.326 30.297 1.00 31.91  ? 95  LEU A C   1 
ATOM   833  O  O   . LEU A 1 94  ? 21.421 -23.880 30.549 1.00 30.32  ? 95  LEU A O   1 
ATOM   834  C  CB  . LEU A 1 94  ? 21.717 -21.596 28.615 1.00 26.85  ? 95  LEU A CB  1 
ATOM   835  C  CG  . LEU A 1 94  ? 21.714 -20.379 29.557 1.00 31.19  ? 95  LEU A CG  1 
ATOM   836  C  CD1 . LEU A 1 94  ? 22.958 -19.518 29.333 1.00 29.82  ? 95  LEU A CD1 1 
ATOM   837  C  CD2 . LEU A 1 94  ? 20.443 -19.572 29.386 1.00 32.81  ? 95  LEU A CD2 1 
ATOM   838  N  N   . ASN A 1 95  ? 23.508 -23.237 31.188 1.00 30.46  ? 96  ASN A N   1 
ATOM   839  C  CA  . ASN A 1 95  ? 23.422 -23.794 32.545 1.00 31.66  ? 96  ASN A CA  1 
ATOM   840  C  C   . ASN A 1 95  ? 22.709 -22.785 33.462 1.00 35.95  ? 96  ASN A C   1 
ATOM   841  O  O   . ASN A 1 95  ? 23.348 -22.085 34.252 1.00 36.43  ? 96  ASN A O   1 
ATOM   842  C  CB  . ASN A 1 95  ? 24.829 -24.169 33.076 1.00 33.92  ? 96  ASN A CB  1 
ATOM   843  C  CG  . ASN A 1 95  ? 24.809 -24.785 34.475 1.00 53.32  ? 96  ASN A CG  1 
ATOM   844  O  OD1 . ASN A 1 95  ? 23.820 -25.369 34.914 1.00 45.42  ? 96  ASN A OD1 1 
ATOM   845  N  ND2 . ASN A 1 95  ? 25.898 -24.660 35.212 1.00 46.33  ? 96  ASN A ND2 1 
ATOM   846  N  N   . LEU A 1 96  ? 21.395 -22.657 33.288 1.00 33.28  ? 97  LEU A N   1 
ATOM   847  C  CA  . LEU A 1 96  ? 20.595 -21.683 34.029 1.00 34.90  ? 97  LEU A CA  1 
ATOM   848  C  C   . LEU A 1 96  ? 20.059 -22.316 35.296 1.00 40.01  ? 97  LEU A C   1 
ATOM   849  O  O   . LEU A 1 96  ? 19.415 -23.370 35.231 1.00 38.75  ? 97  LEU A O   1 
ATOM   850  C  CB  . LEU A 1 96  ? 19.459 -21.195 33.121 1.00 35.67  ? 97  LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 96  ? 18.757 -19.905 33.459 1.00 41.90  ? 97  LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 96  ? 19.759 -18.725 33.542 1.00 41.37  ? 97  LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 96  ? 17.660 -19.634 32.437 1.00 42.69  ? 97  LEU A CD2 1 
ATOM   854  N  N   . ARG A 1 97  ? 20.372 -21.702 36.459 1.00 36.92  ? 98  ARG A N   1 
ATOM   855  C  CA  . ARG A 1 97  ? 19.965 -22.223 37.780 1.00 38.60  ? 98  ARG A CA  1 
ATOM   856  C  C   . ARG A 1 97  ? 19.436 -21.109 38.667 1.00 41.39  ? 98  ARG A C   1 
ATOM   857  O  O   . ARG A 1 97  ? 19.790 -19.948 38.452 1.00 38.54  ? 98  ARG A O   1 
ATOM   858  C  CB  . ARG A 1 97  ? 21.156 -22.914 38.481 1.00 40.14  ? 98  ARG A CB  1 
ATOM   859  C  CG  . ARG A 1 97  ? 21.768 -24.085 37.693 1.00 47.08  ? 98  ARG A CG  1 
ATOM   860  C  CD  . ARG A 1 97  ? 23.036 -24.644 38.331 1.00 65.85  ? 98  ARG A CD  1 
ATOM   861  N  NE  . ARG A 1 97  ? 22.809 -25.149 39.691 1.00 85.54  ? 98  ARG A NE  1 
ATOM   862  C  CZ  . ARG A 1 97  ? 22.369 -26.371 39.985 1.00 105.58 ? 98  ARG A CZ  1 
ATOM   863  N  NH1 . ARG A 1 97  ? 22.185 -26.728 41.250 1.00 94.12  ? 98  ARG A NH1 1 
ATOM   864  N  NH2 . ARG A 1 97  ? 22.108 -27.244 39.018 1.00 94.50  ? 98  ARG A NH2 1 
ATOM   865  N  N   . GLU A 1 98  ? 18.598 -21.441 39.678 1.00 39.06  ? 99  GLU A N   1 
ATOM   866  C  CA  . GLU A 1 98  ? 18.079 -20.424 40.618 1.00 40.21  ? 99  GLU A CA  1 
ATOM   867  C  C   . GLU A 1 98  ? 19.212 -19.538 41.180 1.00 44.43  ? 99  GLU A C   1 
ATOM   868  O  O   . GLU A 1 98  ? 19.049 -18.318 41.272 1.00 45.01  ? 99  GLU A O   1 
ATOM   869  C  CB  . GLU A 1 98  ? 17.305 -21.097 41.773 1.00 43.85  ? 99  GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 98  ? 16.593 -20.122 42.695 1.00 54.73  ? 99  GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 98  ? 15.881 -20.751 43.880 1.00 90.89  ? 99  GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 98  ? 16.449 -21.673 44.512 1.00 90.46  ? 99  GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 98  ? 14.752 -20.306 44.184 1.00 93.58  ? 99  GLU A OE2 1 
ATOM   874  N  N   . GLY A 1 99  ? 20.339 -20.162 41.524 1.00 41.81  ? 100 GLY A N   1 
ATOM   875  C  CA  . GLY A 1 99  ? 21.501 -19.482 42.091 1.00 42.57  ? 100 GLY A CA  1 
ATOM   876  C  C   . GLY A 1 99  ? 22.311 -18.616 41.143 1.00 43.66  ? 100 GLY A C   1 
ATOM   877  O  O   . GLY A 1 99  ? 23.132 -17.815 41.592 1.00 43.38  ? 100 GLY A O   1 
ATOM   878  N  N   . ASN A 1 100 ? 22.102 -18.742 39.824 1.00 38.22  ? 101 ASN A N   1 
ATOM   879  C  CA  . ASN A 1 100 ? 22.907 -17.927 38.904 1.00 35.97  ? 101 ASN A CA  1 
ATOM   880  C  C   . ASN A 1 100 ? 22.084 -17.057 37.948 1.00 39.01  ? 101 ASN A C   1 
ATOM   881  O  O   . ASN A 1 100 ? 22.664 -16.248 37.214 1.00 38.00  ? 101 ASN A O   1 
ATOM   882  C  CB  . ASN A 1 100 ? 23.882 -18.836 38.130 1.00 34.52  ? 101 ASN A CB  1 
ATOM   883  C  CG  . ASN A 1 100 ? 23.233 -19.786 37.136 1.00 42.06  ? 101 ASN A CG  1 
ATOM   884  O  OD1 . ASN A 1 100 ? 22.181 -19.496 36.556 1.00 32.86  ? 101 ASN A OD1 1 
ATOM   885  N  ND2 . ASN A 1 100 ? 23.869 -20.928 36.872 1.00 35.50  ? 101 ASN A ND2 1 
ATOM   886  N  N   . ILE A 1 101 ? 20.744 -17.247 37.926 1.00 36.30  ? 102 ILE A N   1 
ATOM   887  C  CA  . ILE A 1 101 ? 19.860 -16.599 36.948 1.00 36.15  ? 102 ILE A CA  1 
ATOM   888  C  C   . ILE A 1 101 ? 19.983 -15.072 36.927 1.00 38.42  ? 102 ILE A C   1 
ATOM   889  O  O   . ILE A 1 101 ? 19.989 -14.488 35.836 1.00 35.97  ? 102 ILE A O   1 
ATOM   890  C  CB  . ILE A 1 101 ? 18.381 -17.058 37.050 1.00 40.50  ? 102 ILE A CB  1 
ATOM   891  C  CG1 . ILE A 1 101 ? 17.537 -16.477 35.878 1.00 41.14  ? 102 ILE A CG1 1 
ATOM   892  C  CG2 . ILE A 1 101 ? 17.761 -16.781 38.432 1.00 40.74  ? 102 ILE A CG2 1 
ATOM   893  C  CD1 . ILE A 1 101 ? 16.402 -17.332 35.397 1.00 42.94  ? 102 ILE A CD1 1 
ATOM   894  N  N   . MET A 1 102 ? 20.094 -14.426 38.094 1.00 36.46  ? 103 MET A N   1 
ATOM   895  C  CA  . MET A 1 102 ? 20.228 -12.973 38.115 1.00 37.37  ? 103 MET A CA  1 
ATOM   896  C  C   . MET A 1 102 ? 21.526 -12.513 37.470 1.00 38.16  ? 103 MET A C   1 
ATOM   897  O  O   . MET A 1 102 ? 21.487 -11.577 36.677 1.00 36.49  ? 103 MET A O   1 
ATOM   898  C  CB  . MET A 1 102 ? 20.066 -12.399 39.539 1.00 41.97  ? 103 MET A CB  1 
ATOM   899  C  CG  . MET A 1 102 ? 18.705 -12.684 40.163 1.00 48.83  ? 103 MET A CG  1 
ATOM   900  S  SD  . MET A 1 102 ? 17.262 -12.341 39.106 1.00 55.17  ? 103 MET A SD  1 
ATOM   901  C  CE  . MET A 1 102 ? 17.246 -10.514 39.164 1.00 52.53  ? 103 MET A CE  1 
ATOM   902  N  N   . ALA A 1 103 ? 22.667 -13.186 37.778 1.00 34.34  ? 104 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 103 ? 23.988 -12.851 37.213 1.00 33.58  ? 104 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 103 ? 24.000 -13.135 35.712 1.00 34.61  ? 104 ALA A C   1 
ATOM   905  O  O   . ALA A 1 103 ? 24.515 -12.332 34.932 1.00 33.04  ? 104 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 103 ? 25.077 -13.669 37.891 1.00 34.87  ? 104 ALA A CB  1 
ATOM   907  N  N   . VAL A 1 104 ? 23.427 -14.281 35.313 1.00 29.51  ? 105 VAL A N   1 
ATOM   908  C  CA  . VAL A 1 104 ? 23.351 -14.669 33.890 1.00 27.73  ? 105 VAL A CA  1 
ATOM   909  C  C   . VAL A 1 104 ? 22.549 -13.641 33.091 1.00 31.23  ? 105 VAL A C   1 
ATOM   910  O  O   . VAL A 1 104 ? 23.044 -13.192 32.048 1.00 30.71  ? 105 VAL A O   1 
ATOM   911  C  CB  . VAL A 1 104 ? 22.861 -16.125 33.679 1.00 31.09  ? 105 VAL A CB  1 
ATOM   912  C  CG1 . VAL A 1 104 ? 22.637 -16.418 32.193 1.00 29.03  ? 105 VAL A CG1 1 
ATOM   913  C  CG2 . VAL A 1 104 ? 23.866 -17.120 34.262 1.00 31.03  ? 105 VAL A CG2 1 
ATOM   914  N  N   A MET A 1 105 ? 21.358 -13.234 33.584 0.65 29.33  ? 106 MET A N   1 
ATOM   915  N  N   B MET A 1 105 ? 21.356 -13.237 33.580 0.35 29.74  ? 106 MET A N   1 
ATOM   916  C  CA  A MET A 1 105 ? 20.537 -12.239 32.885 0.65 30.24  ? 106 MET A CA  1 
ATOM   917  C  CA  B MET A 1 105 ? 20.533 -12.242 32.884 0.35 30.60  ? 106 MET A CA  1 
ATOM   918  C  C   A MET A 1 105 ? 21.241 -10.891 32.764 0.65 34.39  ? 106 MET A C   1 
ATOM   919  C  C   B MET A 1 105 ? 21.240 -10.894 32.762 0.35 34.67  ? 106 MET A C   1 
ATOM   920  O  O   A MET A 1 105 ? 21.213 -10.289 31.688 0.65 33.21  ? 106 MET A O   1 
ATOM   921  O  O   B MET A 1 105 ? 21.226 -10.305 31.680 0.35 33.65  ? 106 MET A O   1 
ATOM   922  C  CB  A MET A 1 105 ? 19.168 -12.058 33.547 0.65 34.31  ? 106 MET A CB  1 
ATOM   923  C  CB  B MET A 1 105 ? 19.161 -12.066 33.545 0.35 34.65  ? 106 MET A CB  1 
ATOM   924  C  CG  A MET A 1 105 ? 18.231 -11.191 32.718 0.65 38.86  ? 106 MET A CG  1 
ATOM   925  C  CG  B MET A 1 105 ? 18.221 -11.216 32.712 0.35 39.20  ? 106 MET A CG  1 
ATOM   926  S  SD  A MET A 1 105 ? 16.549 -11.197 33.354 0.65 45.38  ? 106 MET A SD  1 
ATOM   927  S  SD  B MET A 1 105 ? 16.603 -11.037 33.466 0.35 45.85  ? 106 MET A SD  1 
ATOM   928  C  CE  A MET A 1 105 ? 16.714 -10.057 34.778 0.65 43.42  ? 106 MET A CE  1 
ATOM   929  C  CE  B MET A 1 105 ? 16.176 -9.421  32.886 0.35 43.47  ? 106 MET A CE  1 
ATOM   930  N  N   . ALA A 1 106 ? 21.863 -10.415 33.857 1.00 32.24  ? 107 ALA A N   1 
ATOM   931  C  CA  . ALA A 1 106 ? 22.599 -9.128  33.855 1.00 32.26  ? 107 ALA A CA  1 
ATOM   932  C  C   . ALA A 1 106 ? 23.769 -9.180  32.867 1.00 32.46  ? 107 ALA A C   1 
ATOM   933  O  O   . ALA A 1 106 ? 23.969 -8.230  32.096 1.00 30.38  ? 107 ALA A O   1 
ATOM   934  C  CB  . ALA A 1 106 ? 23.088 -8.793  35.257 1.00 33.97  ? 107 ALA A CB  1 
ATOM   935  N  N   . THR A 1 107 ? 24.491 -10.320 32.827 1.00 28.11  ? 108 THR A N   1 
ATOM   936  C  CA  . THR A 1 107 ? 25.596 -10.501 31.887 1.00 26.99  ? 108 THR A CA  1 
ATOM   937  C  C   . THR A 1 107 ? 25.073 -10.540 30.436 1.00 30.39  ? 108 THR A C   1 
ATOM   938  O  O   . THR A 1 107 ? 25.667 -9.903  29.568 1.00 27.90  ? 108 THR A O   1 
ATOM   939  C  CB  . THR A 1 107 ? 26.498 -11.702 32.251 1.00 33.30  ? 108 THR A CB  1 
ATOM   940  O  OG1 . THR A 1 107 ? 26.806 -11.682 33.650 1.00 32.22  ? 108 THR A OG1 1 
ATOM   941  C  CG2 . THR A 1 107 ? 27.809 -11.711 31.447 1.00 30.12  ? 108 THR A CG2 1 
ATOM   942  N  N   . ALA A 1 108 ? 23.965 -11.276 30.177 1.00 26.30  ? 109 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 108 ? 23.380 -11.375 28.832 1.00 25.30  ? 109 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 108 ? 22.877 -10.001 28.362 1.00 28.56  ? 109 ALA A C   1 
ATOM   945  O  O   . ALA A 1 108 ? 23.008 -9.673  27.181 1.00 26.98  ? 109 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 108 ? 22.255 -12.417 28.817 1.00 25.91  ? 109 ALA A CB  1 
ATOM   947  N  N   . MET A 1 109 ? 22.347 -9.171  29.282 1.00 27.60  ? 110 MET A N   1 
ATOM   948  C  CA  . MET A 1 109 ? 21.899 -7.827  28.894 1.00 28.42  ? 110 MET A CA  1 
ATOM   949  C  C   . MET A 1 109 ? 23.088 -6.964  28.456 1.00 31.04  ? 110 MET A C   1 
ATOM   950  O  O   . MET A 1 109 ? 23.029 -6.304  27.421 1.00 31.37  ? 110 MET A O   1 
ATOM   951  C  CB  . MET A 1 109 ? 21.134 -7.156  30.046 1.00 31.99  ? 110 MET A CB  1 
ATOM   952  C  CG  . MET A 1 109 ? 19.737 -7.734  30.228 1.00 37.49  ? 110 MET A CG  1 
ATOM   953  S  SD  . MET A 1 109 ? 18.969 -7.155  31.763 1.00 45.37  ? 110 MET A SD  1 
ATOM   954  C  CE  . MET A 1 109 ? 18.721 -5.417  31.367 1.00 43.62  ? 110 MET A CE  1 
ATOM   955  N  N   . TYR A 1 110 ? 24.171 -7.010  29.221 1.00 29.00  ? 111 TYR A N   1 
ATOM   956  C  CA  . TYR A 1 110 ? 25.404 -6.268  28.941 1.00 28.42  ? 111 TYR A CA  1 
ATOM   957  C  C   . TYR A 1 110 ? 26.035 -6.749  27.611 1.00 30.58  ? 111 TYR A C   1 
ATOM   958  O  O   . TYR A 1 110 ? 26.441 -5.929  26.782 1.00 30.00  ? 111 TYR A O   1 
ATOM   959  C  CB  . TYR A 1 110 ? 26.368 -6.505  30.102 1.00 28.96  ? 111 TYR A CB  1 
ATOM   960  C  CG  . TYR A 1 110 ? 27.784 -6.032  29.866 1.00 29.24  ? 111 TYR A CG  1 
ATOM   961  C  CD1 . TYR A 1 110 ? 28.110 -4.679  29.932 1.00 31.51  ? 111 TYR A CD1 1 
ATOM   962  C  CD2 . TYR A 1 110 ? 28.814 -6.943  29.652 1.00 28.39  ? 111 TYR A CD2 1 
ATOM   963  C  CE1 . TYR A 1 110 ? 29.422 -4.242  29.735 1.00 28.76  ? 111 TYR A CE1 1 
ATOM   964  C  CE2 . TYR A 1 110 ? 30.132 -6.522  29.486 1.00 28.09  ? 111 TYR A CE2 1 
ATOM   965  C  CZ  . TYR A 1 110 ? 30.431 -5.171  29.553 1.00 30.38  ? 111 TYR A CZ  1 
ATOM   966  O  OH  . TYR A 1 110 ? 31.725 -4.769  29.416 1.00 30.17  ? 111 TYR A OH  1 
ATOM   967  N  N   . LEU A 1 111 ? 26.090 -8.077  27.400 1.00 25.51  ? 112 LEU A N   1 
ATOM   968  C  CA  . LEU A 1 111 ? 26.670 -8.676  26.193 1.00 24.47  ? 112 LEU A CA  1 
ATOM   969  C  C   . LEU A 1 111 ? 25.750 -8.545  24.973 1.00 29.10  ? 112 LEU A C   1 
ATOM   970  O  O   . LEU A 1 111 ? 26.187 -8.812  23.852 1.00 28.25  ? 112 LEU A O   1 
ATOM   971  C  CB  . LEU A 1 111 ? 27.019 -10.158 26.448 1.00 23.08  ? 112 LEU A CB  1 
ATOM   972  C  CG  . LEU A 1 111 ? 28.161 -10.443 27.453 1.00 26.56  ? 112 LEU A CG  1 
ATOM   973  C  CD1 . LEU A 1 111 ? 28.435 -11.962 27.530 1.00 26.76  ? 112 LEU A CD1 1 
ATOM   974  C  CD2 . LEU A 1 111 ? 29.475 -9.662  27.063 1.00 28.39  ? 112 LEU A CD2 1 
ATOM   975  N  N   . GLN A 1 112 ? 24.469 -8.174  25.195 1.00 27.08  ? 113 GLN A N   1 
ATOM   976  C  CA  . GLN A 1 112 ? 23.445 -8.047  24.144 1.00 27.97  ? 113 GLN A CA  1 
ATOM   977  C  C   . GLN A 1 112 ? 23.221 -9.399  23.454 1.00 30.35  ? 113 GLN A C   1 
ATOM   978  O  O   . GLN A 1 112 ? 23.540 -9.582  22.271 1.00 28.27  ? 113 GLN A O   1 
ATOM   979  C  CB  . GLN A 1 112 ? 23.787 -6.930  23.137 1.00 29.70  ? 113 GLN A CB  1 
ATOM   980  C  CG  . GLN A 1 112 ? 23.986 -5.546  23.776 1.00 31.70  ? 113 GLN A CG  1 
ATOM   981  C  CD  . GLN A 1 112 ? 24.714 -4.610  22.829 1.00 42.07  ? 113 GLN A CD  1 
ATOM   982  O  OE1 . GLN A 1 112 ? 24.597 -4.711  21.614 1.00 35.66  ? 113 GLN A OE1 1 
ATOM   983  N  NE2 . GLN A 1 112 ? 25.500 -3.691  23.361 1.00 39.43  ? 113 GLN A NE2 1 
ATOM   984  N  N   . MET A 1 113 ? 22.720 -10.362 24.241 1.00 27.21  ? 114 MET A N   1 
ATOM   985  C  CA  . MET A 1 113 ? 22.410 -11.741 23.818 1.00 26.72  ? 114 MET A CA  1 
ATOM   986  C  C   . MET A 1 113 ? 20.912 -11.889 24.076 1.00 32.79  ? 114 MET A C   1 
ATOM   987  O  O   . MET A 1 113 ? 20.478 -12.333 25.153 1.00 30.67  ? 114 MET A O   1 
ATOM   988  C  CB  . MET A 1 113 ? 23.266 -12.716 24.639 1.00 27.80  ? 114 MET A CB  1 
ATOM   989  C  CG  . MET A 1 113 ? 24.768 -12.574 24.332 1.00 28.82  ? 114 MET A CG  1 
ATOM   990  S  SD  . MET A 1 113 ? 25.787 -13.632 25.374 1.00 31.37  ? 114 MET A SD  1 
ATOM   991  C  CE  . MET A 1 113 ? 25.417 -15.279 24.611 1.00 27.95  ? 114 MET A CE  1 
ATOM   992  N  N   . GLU A 1 114 ? 20.122 -11.346 23.133 1.00 32.31  ? 115 GLU A N   1 
ATOM   993  C  CA  . GLU A 1 114 ? 18.666 -11.195 23.266 1.00 34.94  ? 115 GLU A CA  1 
ATOM   994  C  C   . GLU A 1 114 ? 17.894 -12.475 23.581 1.00 36.42  ? 115 GLU A C   1 
ATOM   995  O  O   . GLU A 1 114 ? 16.966 -12.418 24.389 1.00 36.01  ? 115 GLU A O   1 
ATOM   996  C  CB  . GLU A 1 114 ? 18.063 -10.512 22.031 1.00 38.45  ? 115 GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 114 ? 18.585 -9.098  21.826 1.00 52.84  ? 115 GLU A CG  1 
ATOM   998  N  N   . HIS A 1 115 ? 18.260 -13.616 22.976 1.00 31.89  ? 116 HIS A N   1 
ATOM   999  C  CA  . HIS A 1 115 ? 17.528 -14.856 23.258 1.00 33.79  ? 116 HIS A CA  1 
ATOM   1000 C  C   . HIS A 1 115 ? 17.747 -15.330 24.693 1.00 34.84  ? 116 HIS A C   1 
ATOM   1001 O  O   . HIS A 1 115 ? 16.793 -15.777 25.332 1.00 35.41  ? 116 HIS A O   1 
ATOM   1002 C  CB  . HIS A 1 115 ? 17.849 -15.943 22.234 1.00 35.37  ? 116 HIS A CB  1 
ATOM   1003 C  CG  . HIS A 1 115 ? 17.361 -15.613 20.859 1.00 40.13  ? 116 HIS A CG  1 
ATOM   1004 N  ND1 . HIS A 1 115 ? 16.016 -15.399 20.605 1.00 43.72  ? 116 HIS A ND1 1 
ATOM   1005 C  CD2 . HIS A 1 115 ? 18.051 -15.491 19.702 1.00 41.59  ? 116 HIS A CD2 1 
ATOM   1006 C  CE1 . HIS A 1 115 ? 15.933 -15.133 19.312 1.00 43.71  ? 116 HIS A CE1 1 
ATOM   1007 N  NE2 . HIS A 1 115 ? 17.131 -15.179 18.728 1.00 42.76  ? 116 HIS A NE2 1 
ATOM   1008 N  N   . VAL A 1 116 ? 18.980 -15.166 25.221 1.00 28.94  ? 117 VAL A N   1 
ATOM   1009 C  CA  . VAL A 1 116 ? 19.280 -15.506 26.617 1.00 28.60  ? 117 VAL A CA  1 
ATOM   1010 C  C   . VAL A 1 116 ? 18.497 -14.588 27.571 1.00 34.33  ? 117 VAL A C   1 
ATOM   1011 O  O   . VAL A 1 116 ? 17.874 -15.072 28.531 1.00 32.25  ? 117 VAL A O   1 
ATOM   1012 C  CB  . VAL A 1 116 ? 20.800 -15.528 26.927 1.00 30.52  ? 117 VAL A CB  1 
ATOM   1013 C  CG1 . VAL A 1 116 ? 21.040 -15.777 28.417 1.00 30.35  ? 117 VAL A CG1 1 
ATOM   1014 C  CG2 . VAL A 1 116 ? 21.511 -16.589 26.086 1.00 29.72  ? 117 VAL A CG2 1 
ATOM   1015 N  N   . VAL A 1 117 ? 18.508 -13.268 27.303 1.00 31.66  ? 118 VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 117 ? 17.752 -12.300 28.118 1.00 32.45  ? 118 VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 117 ? 16.259 -12.720 28.183 1.00 38.38  ? 118 VAL A C   1 
ATOM   1018 O  O   . VAL A 1 117 ? 15.701 -12.790 29.279 1.00 38.18  ? 118 VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 117 ? 17.932 -10.838 27.620 1.00 35.70  ? 118 VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 117 ? 17.080 -9.858  28.436 1.00 36.39  ? 118 VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 117 ? 19.400 -10.421 27.675 1.00 34.25  ? 118 VAL A CG2 1 
ATOM   1022 N  N   A ASP A 1 118 ? 15.616 -12.916 27.014 0.41 36.63  ? 119 ASP A N   1 
ATOM   1023 N  N   B ASP A 1 118 ? 15.681 -13.103 27.029 0.59 36.08  ? 119 ASP A N   1 
ATOM   1024 C  CA  A ASP A 1 118 ? 14.195 -13.276 26.895 0.41 38.28  ? 119 ASP A CA  1 
ATOM   1025 C  CA  B ASP A 1 118 ? 14.296 -13.573 26.898 0.59 37.19  ? 119 ASP A CA  1 
ATOM   1026 C  C   A ASP A 1 118 ? 13.781 -14.483 27.735 0.41 42.88  ? 119 ASP A C   1 
ATOM   1027 C  C   B ASP A 1 118 ? 13.985 -14.790 27.780 0.59 40.06  ? 119 ASP A C   1 
ATOM   1028 O  O   A ASP A 1 118 ? 12.719 -14.455 28.348 0.41 44.40  ? 119 ASP A O   1 
ATOM   1029 O  O   B ASP A 1 118 ? 13.013 -14.736 28.528 0.59 40.25  ? 119 ASP A O   1 
ATOM   1030 C  CB  A ASP A 1 118 ? 13.801 -13.485 25.421 0.41 40.33  ? 119 ASP A CB  1 
ATOM   1031 C  CB  B ASP A 1 118 ? 13.956 -13.864 25.425 0.59 39.31  ? 119 ASP A CB  1 
ATOM   1032 C  CG  A ASP A 1 118 ? 13.622 -12.209 24.619 0.41 52.45  ? 119 ASP A CG  1 
ATOM   1033 C  CG  B ASP A 1 118 ? 12.502 -14.226 25.169 0.59 54.71  ? 119 ASP A CG  1 
ATOM   1034 O  OD1 A ASP A 1 118 ? 13.054 -11.238 25.162 0.41 56.11  ? 119 ASP A OD1 1 
ATOM   1035 O  OD1 B ASP A 1 118 ? 11.614 -13.434 25.553 0.59 58.51  ? 119 ASP A OD1 1 
ATOM   1036 O  OD2 A ASP A 1 118 ? 14.043 -12.183 23.444 0.41 56.66  ? 119 ASP A OD2 1 
ATOM   1037 O  OD2 B ASP A 1 118 ? 12.256 -15.292 24.567 0.59 59.59  ? 119 ASP A OD2 1 
ATOM   1038 N  N   A THR A 1 119 ? 14.625 -15.524 27.780 0.41 37.80  ? 120 THR A N   1 
ATOM   1039 N  N   B THR A 1 119 ? 14.799 -15.872 27.715 0.59 34.66  ? 120 THR A N   1 
ATOM   1040 C  CA  A THR A 1 119 ? 14.362 -16.754 28.532 0.41 37.77  ? 120 THR A CA  1 
ATOM   1041 C  CA  B THR A 1 119 ? 14.522 -17.059 28.539 0.59 34.56  ? 120 THR A CA  1 
ATOM   1042 C  C   A THR A 1 119 ? 14.535 -16.546 30.015 0.41 40.14  ? 120 THR A C   1 
ATOM   1043 C  C   B THR A 1 119 ? 14.701 -16.783 30.043 0.59 38.55  ? 120 THR A C   1 
ATOM   1044 O  O   A THR A 1 119 ? 13.688 -17.002 30.783 0.41 40.46  ? 120 THR A O   1 
ATOM   1045 O  O   B THR A 1 119 ? 13.997 -17.401 30.840 0.59 38.31  ? 120 THR A O   1 
ATOM   1046 C  CB  A THR A 1 119 ? 15.193 -17.879 27.969 0.41 46.09  ? 120 THR A CB  1 
ATOM   1047 C  CB  B THR A 1 119 ? 15.284 -18.313 28.076 0.59 35.55  ? 120 THR A CB  1 
ATOM   1048 O  OG1 A THR A 1 119 ? 14.797 -17.965 26.618 0.41 47.00  ? 120 THR A OG1 1 
ATOM   1049 O  OG1 B THR A 1 119 ? 14.622 -19.445 28.642 0.59 36.04  ? 120 THR A OG1 1 
ATOM   1050 C  CG2 A THR A 1 119 ? 14.924 -19.208 28.649 0.41 45.73  ? 120 THR A CG2 1 
ATOM   1051 C  CG2 B THR A 1 119 ? 16.752 -18.325 28.497 0.59 27.32  ? 120 THR A CG2 1 
ATOM   1052 N  N   . CYS A 1 120 ? 15.627 -15.865 30.423 1.00 34.72  ? 121 CYS A N   1 
ATOM   1053 C  CA  . CYS A 1 120 ? 15.868 -15.515 31.836 1.00 35.49  ? 121 CYS A CA  1 
ATOM   1054 C  C   . CYS A 1 120 ? 14.656 -14.790 32.376 1.00 41.99  ? 121 CYS A C   1 
ATOM   1055 O  O   . CYS A 1 120 ? 14.152 -15.157 33.447 1.00 41.52  ? 121 CYS A O   1 
ATOM   1056 C  CB  . CYS A 1 120 ? 17.117 -14.654 31.962 1.00 34.45  ? 121 CYS A CB  1 
ATOM   1057 S  SG  . CYS A 1 120 ? 18.650 -15.577 31.748 1.00 36.71  ? 121 CYS A SG  1 
ATOM   1058 N  N   . ARG A 1 121 ? 14.146 -13.803 31.593 1.00 40.47  ? 122 ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 121 ? 12.939 -13.038 31.931 1.00 42.41  ? 122 ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 121 ? 11.744 -13.981 32.189 1.00 47.21  ? 122 ARG A C   1 
ATOM   1061 O  O   . ARG A 1 121 ? 11.034 -13.818 33.187 1.00 47.60  ? 122 ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 121 ? 12.588 -12.056 30.806 1.00 43.99  ? 122 ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 121 ? 13.442 -10.804 30.798 1.00 60.22  ? 122 ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 121 ? 12.620 -9.580  30.439 1.00 76.06  ? 122 ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 121 ? 13.018 -9.012  29.149 1.00 84.17  ? 122 ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 121 ? 13.938 -8.063  28.994 1.00 93.29  ? 122 ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 121 ? 14.578 -7.568  30.048 1.00 72.14  ? 122 ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 121 ? 14.230 -7.607  27.783 1.00 81.54  ? 122 ARG A NH2 1 
ATOM   1069 N  N   . LYS A 1 122 ? 11.548 -14.970 31.296 1.00 44.56  ? 123 LYS A N   1 
ATOM   1070 C  CA  . LYS A 1 122 ? 10.465 -15.958 31.384 1.00 46.06  ? 123 LYS A CA  1 
ATOM   1071 C  C   . LYS A 1 122 ? 10.626 -16.864 32.601 1.00 49.61  ? 123 LYS A C   1 
ATOM   1072 O  O   . LYS A 1 122 ? 9.645  -17.108 33.288 1.00 49.35  ? 123 LYS A O   1 
ATOM   1073 C  CB  . LYS A 1 122 ? 10.365 -16.796 30.094 1.00 47.52  ? 123 LYS A CB  1 
ATOM   1074 C  CG  . LYS A 1 122 ? 9.842  -16.008 28.897 1.00 66.06  ? 123 LYS A CG  1 
ATOM   1075 C  CD  . LYS A 1 122 ? 9.523  -16.915 27.710 1.00 77.53  ? 123 LYS A CD  1 
ATOM   1076 C  CE  . LYS A 1 122 ? 9.580  -16.201 26.375 1.00 87.41  ? 123 LYS A CE  1 
ATOM   1077 N  NZ  . LYS A 1 122 ? 8.546  -15.139 26.238 1.00 96.68  ? 123 LYS A NZ  1 
ATOM   1078 N  N   . PHE A 1 123 ? 11.860 -17.357 32.872 1.00 45.42  ? 124 PHE A N   1 
ATOM   1079 C  CA  . PHE A 1 123 ? 12.137 -18.223 34.025 1.00 46.05  ? 124 PHE A CA  1 
ATOM   1080 C  C   . PHE A 1 123 ? 11.929 -17.474 35.348 1.00 51.13  ? 124 PHE A C   1 
ATOM   1081 O  O   . PHE A 1 123 ? 11.406 -18.059 36.301 1.00 51.38  ? 124 PHE A O   1 
ATOM   1082 C  CB  . PHE A 1 123 ? 13.542 -18.834 33.930 1.00 46.38  ? 124 PHE A CB  1 
ATOM   1083 C  CG  . PHE A 1 123 ? 13.669 -20.138 33.158 1.00 48.52  ? 124 PHE A CG  1 
ATOM   1084 C  CD1 . PHE A 1 123 ? 13.143 -20.265 31.874 1.00 52.04  ? 124 PHE A CD1 1 
ATOM   1085 C  CD2 . PHE A 1 123 ? 14.354 -21.221 33.698 1.00 51.15  ? 124 PHE A CD2 1 
ATOM   1086 C  CE1 . PHE A 1 123 ? 13.265 -21.466 31.163 1.00 52.24  ? 124 PHE A CE1 1 
ATOM   1087 C  CE2 . PHE A 1 123 ? 14.488 -22.418 32.979 1.00 53.08  ? 124 PHE A CE2 1 
ATOM   1088 C  CZ  . PHE A 1 123 ? 13.945 -22.530 31.717 1.00 50.52  ? 124 PHE A CZ  1 
ATOM   1089 N  N   . ILE A 1 124 ? 12.278 -16.168 35.386 1.00 46.33  ? 125 ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 124 ? 12.074 -15.323 36.572 1.00 47.70  ? 125 ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 124 ? 10.579 -15.069 36.820 1.00 54.42  ? 125 ILE A C   1 
ATOM   1092 O  O   . ILE A 1 124 ? 10.132 -15.173 37.966 1.00 55.13  ? 125 ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 124 ? 12.921 -14.025 36.499 1.00 49.77  ? 125 ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 124 ? 14.406 -14.364 36.677 1.00 48.11  ? 125 ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 124 ? 12.477 -12.963 37.549 1.00 52.95  ? 125 ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 124 ? 15.359 -13.311 36.123 1.00 51.68  ? 125 ILE A CD1 1 
ATOM   1097 N  N   . LYS A 1 125 ? 9.811  -14.771 35.743 1.00 52.65  ? 126 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 125 ? 8.363  -14.511 35.800 1.00 55.39  ? 126 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 125 ? 7.590  -15.746 36.312 1.00 60.42  ? 126 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 125 ? 6.598  -15.595 37.023 1.00 61.03  ? 126 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 125 ? 7.842  -14.067 34.423 1.00 58.63  ? 126 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 125 ? 6.478  -13.384 34.464 1.00 76.95  ? 126 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 125 ? 5.864  -13.278 33.075 1.00 89.51  ? 126 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 125 ? 4.428  -12.816 33.122 1.00 104.28 ? 126 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 125 ? 3.773  -12.922 31.790 1.00 115.17 ? 126 LYS A NZ  1 
ATOM   1106 N  N   . ALA A 1 126 ? 8.068  -16.960 35.976 1.00 55.96  ? 127 ALA A N   1 
ATOM   1107 C  CA  . ALA A 1 126 ? 7.463  -18.218 36.423 1.00 57.44  ? 127 ALA A CA  1 
ATOM   1108 C  C   . ALA A 1 126 ? 7.635  -18.430 37.942 1.00 64.26  ? 127 ALA A C   1 
ATOM   1109 O  O   . ALA A 1 126 ? 6.785  -19.059 38.558 1.00 64.86  ? 127 ALA A O   1 
ATOM   1110 C  CB  . ALA A 1 126 ? 8.072  -19.386 35.657 1.00 56.45  ? 127 ALA A CB  1 
ATOM   1111 N  N   . SER A 1 127 ? 8.730  -17.913 38.533 1.00 63.05  ? 128 SER A N   1 
ATOM   1112 C  CA  . SER A 1 127 ? 9.029  -18.054 39.964 1.00 65.91  ? 128 SER A CA  1 
ATOM   1113 C  C   . SER A 1 127 ? 8.332  -17.018 40.874 1.00 74.04  ? 128 SER A C   1 
ATOM   1114 O  O   . SER A 1 127 ? 8.265  -17.240 42.086 1.00 76.67  ? 128 SER A O   1 
ATOM   1115 C  CB  . SER A 1 127 ? 10.537 -18.049 40.202 1.00 69.52  ? 128 SER A CB  1 
ATOM   1116 O  OG  . SER A 1 127 ? 11.094 -19.333 39.973 1.00 80.10  ? 128 SER A OG  1 
ATOM   1117 N  N   . GLU A 1 128 ? 7.803  -15.910 40.305 1.00 70.42  ? 129 GLU A N   1 
ATOM   1118 C  CA  . GLU A 1 128 ? 7.124  -14.865 41.080 1.00 94.76  ? 129 GLU A CA  1 
ATOM   1119 C  C   . GLU A 1 128 ? 5.679  -15.239 41.435 1.00 139.28 ? 129 GLU A C   1 
ATOM   1120 O  O   . GLU A 1 128 ? 5.434  -16.273 42.054 1.00 107.15 ? 129 GLU A O   1 
ATOM   1121 C  CB  . GLU A 1 128 ? 7.211  -13.492 40.380 1.00 95.19  ? 129 GLU A CB  1 
ATOM   1122 C  CG  . GLU A 1 128 ? 6.236  -13.281 39.229 1.00 105.40 ? 129 GLU A CG  1 
ATOM   1123 C  CD  . GLU A 1 128 ? 6.421  -12.039 38.375 1.00 126.86 ? 129 GLU A CD  1 
ATOM   1124 O  OE1 . GLU A 1 128 ? 7.509  -11.419 38.428 1.00 120.48 ? 129 GLU A OE1 1 
ATOM   1125 O  OE2 . GLU A 1 128 ? 5.472  -11.695 37.633 1.00 121.11 ? 129 GLU A OE2 1 
HETATM 1126 C  C   . ACE B 2 1   ? 21.212 -35.085 5.886  1.00 32.03  ? 0   ACE D C   1 
HETATM 1127 O  O   . ACE B 2 1   ? 21.244 -33.936 6.342  1.00 33.39  ? 0   ACE D O   1 
HETATM 1128 C  CH3 . ACE B 2 1   ? 21.414 -36.290 6.793  1.00 31.51  ? 0   ACE D CH3 1 
ATOM   1129 N  N   A TRP B 2 2   ? 20.963 -35.347 4.610  0.78 29.33  ? 1   TRP D N   1 
ATOM   1130 N  N   B TRP B 2 2   ? 20.999 -35.366 4.599  0.22 29.72  ? 1   TRP D N   1 
ATOM   1131 C  CA  A TRP B 2 2   ? 20.758 -34.296 3.621  0.78 28.69  ? 1   TRP D CA  1 
ATOM   1132 C  CA  B TRP B 2 2   ? 20.747 -34.334 3.592  0.22 29.15  ? 1   TRP D CA  1 
ATOM   1133 C  C   A TRP B 2 2   ? 19.268 -34.146 3.317  0.78 32.20  ? 1   TRP D C   1 
ATOM   1134 C  C   B TRP B 2 2   ? 19.248 -34.145 3.392  0.22 31.95  ? 1   TRP D C   1 
ATOM   1135 O  O   A TRP B 2 2   ? 18.535 -35.140 3.291  0.78 33.23  ? 1   TRP D O   1 
ATOM   1136 O  O   B TRP B 2 2   ? 18.493 -35.118 3.477  0.22 31.83  ? 1   TRP D O   1 
ATOM   1137 C  CB  A TRP B 2 2   ? 21.548 -34.623 2.338  0.78 27.47  ? 1   TRP D CB  1 
ATOM   1138 C  CB  B TRP B 2 2   ? 21.446 -34.648 2.245  0.22 27.99  ? 1   TRP D CB  1 
ATOM   1139 C  CG  A TRP B 2 2   ? 23.046 -34.584 2.528  0.78 27.87  ? 1   TRP D CG  1 
ATOM   1140 C  CG  B TRP B 2 2   ? 20.780 -35.700 1.404  0.22 29.01  ? 1   TRP D CG  1 
ATOM   1141 C  CD1 A TRP B 2 2   ? 23.845 -35.596 2.980  0.78 30.59  ? 1   TRP D CD1 1 
ATOM   1142 C  CD1 B TRP B 2 2   ? 21.058 -37.034 1.392  0.22 32.09  ? 1   TRP D CD1 1 
ATOM   1143 C  CD2 A TRP B 2 2   ? 23.913 -33.466 2.288  0.78 27.45  ? 1   TRP D CD2 1 
ATOM   1144 C  CD2 B TRP B 2 2   ? 19.733 -35.500 0.440  0.22 28.90  ? 1   TRP D CD2 1 
ATOM   1145 N  NE1 A TRP B 2 2   ? 25.154 -35.161 3.070  0.78 29.75  ? 1   TRP D NE1 1 
ATOM   1146 N  NE1 B TRP B 2 2   ? 20.221 -37.686 0.518  0.22 31.57  ? 1   TRP D NE1 1 
ATOM   1147 C  CE2 A TRP B 2 2   ? 25.235 -33.888 2.571  0.78 30.77  ? 1   TRP D CE2 1 
ATOM   1148 C  CE2 B TRP B 2 2   ? 19.413 -36.766 -0.098 0.22 32.86  ? 1   TRP D CE2 1 
ATOM   1149 C  CE3 A TRP B 2 2   ? 23.706 -32.146 1.849  0.78 28.14  ? 1   TRP D CE3 1 
ATOM   1150 C  CE3 B TRP B 2 2   ? 19.016 -34.375 -0.005 0.22 30.00  ? 1   TRP D CE3 1 
ATOM   1151 C  CZ2 A TRP B 2 2   ? 26.340 -33.038 2.437  0.78 29.86  ? 1   TRP D CZ2 1 
ATOM   1152 C  CZ2 B TRP B 2 2   ? 18.415 -36.938 -1.066 0.22 32.08  ? 1   TRP D CZ2 1 
ATOM   1153 C  CZ3 A TRP B 2 2   ? 24.807 -31.326 1.661  0.78 29.11  ? 1   TRP D CZ3 1 
ATOM   1154 C  CZ3 B TRP B 2 2   ? 18.026 -34.548 -0.960 0.22 31.70  ? 1   TRP D CZ3 1 
ATOM   1155 C  CH2 A TRP B 2 2   ? 26.102 -31.764 1.977  0.78 29.97  ? 1   TRP D CH2 1 
ATOM   1156 C  CH2 B TRP B 2 2   ? 17.736 -35.816 -1.482 0.22 32.20  ? 1   TRP D CH2 1 
ATOM   1157 N  N   . VAL B 2 3   ? 18.818 -32.906 3.103  1.00 27.52  ? 2   VAL D N   1 
ATOM   1158 C  CA  . VAL B 2 3   ? 17.401 -32.578 2.862  1.00 27.11  ? 2   VAL D CA  1 
ATOM   1159 C  C   . VAL B 2 3   ? 17.260 -31.525 1.769  1.00 29.53  ? 2   VAL D C   1 
ATOM   1160 O  O   . VAL B 2 3   ? 18.231 -30.835 1.426  1.00 28.70  ? 2   VAL D O   1 
ATOM   1161 C  CB  . VAL B 2 3   ? 16.673 -32.079 4.166  1.00 30.17  ? 2   VAL D CB  1 
ATOM   1162 C  CG1 . VAL B 2 3   ? 16.686 -33.124 5.290  1.00 30.23  ? 2   VAL D CG1 1 
ATOM   1163 C  CG2 . VAL B 2 3   ? 17.220 -30.725 4.661  1.00 29.43  ? 2   VAL D CG2 1 
ATOM   1164 N  N   . ILE B 2 4   ? 16.028 -31.352 1.290  1.00 27.48  ? 3   ILE D N   1 
ATOM   1165 C  CA  . ILE B 2 4   ? 15.658 -30.254 0.407  1.00 28.76  ? 3   ILE D CA  1 
ATOM   1166 C  C   . ILE B 2 4   ? 15.285 -29.106 1.391  1.00 31.97  ? 3   ILE D C   1 
ATOM   1167 O  O   . ILE B 2 4   ? 14.290 -29.240 2.116  1.00 31.64  ? 3   ILE D O   1 
ATOM   1168 C  CB  . ILE B 2 4   ? 14.459 -30.623 -0.503 1.00 31.32  ? 3   ILE D CB  1 
ATOM   1169 C  CG1 . ILE B 2 4   ? 14.750 -31.899 -1.380 1.00 30.15  ? 3   ILE D CG1 1 
ATOM   1170 C  CG2 . ILE B 2 4   ? 14.031 -29.389 -1.346 1.00 33.16  ? 3   ILE D CG2 1 
ATOM   1171 C  CD1 . ILE B 2 4   ? 16.042 -31.828 -2.341 1.00 32.42  ? 3   ILE D CD1 1 
ATOM   1172 N  N   . PRO B 2 5   ? 16.081 -28.014 1.472  1.00 31.28  ? 4   PRO D N   1 
ATOM   1173 C  CA  . PRO B 2 5   ? 15.764 -26.937 2.433  1.00 31.72  ? 4   PRO D CA  1 
ATOM   1174 C  C   . PRO B 2 5   ? 14.489 -26.165 2.082  1.00 37.34  ? 4   PRO D C   1 
ATOM   1175 O  O   . PRO B 2 5   ? 14.177 -26.012 0.904  1.00 36.37  ? 4   PRO D O   1 
ATOM   1176 C  CB  . PRO B 2 5   ? 17.009 -26.037 2.385  1.00 33.52  ? 4   PRO D CB  1 
ATOM   1177 C  CG  . PRO B 2 5   ? 17.569 -26.250 0.994  1.00 36.95  ? 4   PRO D CG  1 
ATOM   1178 C  CD  . PRO B 2 5   ? 17.296 -27.701 0.681  1.00 32.63  ? 4   PRO D CD  1 
ATOM   1179 N  N   . ALA B 2 6   ? 13.848 -25.553 3.093  1.00 35.10  ? 5   ALA D N   1 
HETATM 1180 C  C4  . 7ZO C 3 .   ? 27.264 -10.294 11.832 1.00 30.46  ? 201 7ZO A C4  1 
HETATM 1181 C  C5  . 7ZO C 3 .   ? 25.247 -9.365  12.204 1.00 33.49  ? 201 7ZO A C5  1 
HETATM 1182 C  C6  . 7ZO C 3 .   ? 23.937 -10.713 18.089 1.00 30.60  ? 201 7ZO A C6  1 
HETATM 1183 C  C7  . 7ZO C 3 .   ? 23.438 -9.416  18.136 1.00 32.81  ? 201 7ZO A C7  1 
HETATM 1184 C  C8  . 7ZO C 3 .   ? 25.497 -10.033 16.380 1.00 28.97  ? 201 7ZO A C8  1 
HETATM 1185 C  C10 . 7ZO C 3 .   ? 26.342 -10.199 14.022 1.00 29.04  ? 201 7ZO A C10 1 
HETATM 1186 C  C1  . 7ZO C 3 .   ? 23.913 -8.427  17.278 1.00 31.59  ? 201 7ZO A C1  1 
HETATM 1187 C  C2  . 7ZO C 3 .   ? 24.934 -8.751  16.391 1.00 29.06  ? 201 7ZO A C2  1 
HETATM 1188 C  C3  . 7ZO C 3 .   ? 24.963 -11.030 17.204 1.00 28.89  ? 201 7ZO A C3  1 
HETATM 1189 C  C9  . 7ZO C 3 .   ? 27.386 -10.590 13.178 1.00 28.25  ? 201 7ZO A C9  1 
HETATM 1190 C  C11 . 7ZO C 3 .   ? 22.225 -10.542 19.710 1.00 35.52  ? 201 7ZO A C11 1 
HETATM 1191 C  C12 . 7ZO C 3 .   ? 23.192 -11.535 19.101 1.00 32.98  ? 201 7ZO A C12 1 
HETATM 1192 N  N13 . 7ZO C 3 .   ? 26.195 -9.677  11.324 1.00 34.13  ? 201 7ZO A N13 1 
HETATM 1193 N  N14 . 7ZO C 3 .   ? 25.247 -9.586  13.522 1.00 31.82  ? 201 7ZO A N14 1 
HETATM 1194 N  N15 . 7ZO C 3 .   ? 22.436 -9.340  19.111 1.00 32.66  ? 201 7ZO A N15 1 
HETATM 1195 N  N16 . 7ZO C 3 .   ? 26.349 -10.494 15.351 1.00 26.21  ? 201 7ZO A N16 1 
HETATM 1196 O  O17 . 7ZO C 3 .   ? 21.388 -10.768 20.581 1.00 35.62  ? 201 7ZO A O17 1 
HETATM 1197 CL CL1 . 7ZO C 3 .   ? 28.808 -11.374 13.758 0.99 29.40  ? 201 7ZO A CL1 1 
HETATM 1198 CL CL  . CL  D 4 .   ? 21.314 -15.199 22.569 1.00 38.37  ? 202 CL  A CL  1 
HETATM 1199 S  S   A DMS E 5 .   ? 17.553 -35.341 -1.240 0.78 50.65  ? 101 DMS D S   1 
HETATM 1200 O  O   A DMS E 5 .   ? 16.289 -35.116 -0.554 0.78 52.45  ? 101 DMS D O   1 
HETATM 1201 C  C1  A DMS E 5 .   ? 18.727 -34.495 -0.215 0.78 49.49  ? 101 DMS D C1  1 
HETATM 1202 C  C2  A DMS E 5 .   ? 17.958 -37.001 -0.821 0.78 49.46  ? 101 DMS D C2  1 
HETATM 1203 O  O   . HOH F 6 .   ? 35.638 -25.593 25.602 1.00 43.44  ? 301 HOH A O   1 
HETATM 1204 O  O   . HOH F 6 .   ? 41.283 -21.635 25.160 1.00 48.77  ? 302 HOH A O   1 
HETATM 1205 O  O   . HOH F 6 .   ? 25.856 -3.382  26.347 1.00 39.18  ? 303 HOH A O   1 
HETATM 1206 O  O   . HOH F 6 .   ? 38.405 -14.869 15.438 1.00 37.77  ? 304 HOH A O   1 
HETATM 1207 O  O   . HOH F 6 .   ? 37.574 -20.387 26.939 1.00 35.15  ? 305 HOH A O   1 
HETATM 1208 O  O   . HOH F 6 .   ? 37.828 2.489   19.597 1.00 43.87  ? 306 HOH A O   1 
HETATM 1209 O  O   . HOH F 6 .   ? 27.350 -35.343 11.811 1.00 60.13  ? 307 HOH A O   1 
HETATM 1210 O  O   . HOH F 6 .   ? 44.510 -0.890  17.883 1.00 59.93  ? 308 HOH A O   1 
HETATM 1211 O  O   . HOH F 6 .   ? 29.848 -32.081 9.545  1.00 49.46  ? 309 HOH A O   1 
HETATM 1212 O  O   . HOH F 6 .   ? 22.719 -5.365  19.821 1.00 61.80  ? 310 HOH A O   1 
HETATM 1213 O  O   . HOH F 6 .   ? 43.630 -6.571  31.913 1.00 50.19  ? 311 HOH A O   1 
HETATM 1214 O  O   . HOH F 6 .   ? 16.559 -27.645 -3.345 1.00 56.98  ? 312 HOH A O   1 
HETATM 1215 O  O   . HOH F 6 .   ? 44.963 -11.188 18.675 1.00 60.12  ? 313 HOH A O   1 
HETATM 1216 O  O   . HOH F 6 .   ? 19.804 -9.505  36.965 1.00 46.83  ? 314 HOH A O   1 
HETATM 1217 O  O   . HOH F 6 .   ? 33.428 -20.826 29.583 1.00 56.31  ? 315 HOH A O   1 
HETATM 1218 O  O   . HOH F 6 .   ? 22.939 -28.202 12.635 1.00 28.11  ? 316 HOH A O   1 
HETATM 1219 O  O   . HOH F 6 .   ? 27.285 -10.142 35.814 1.00 43.59  ? 317 HOH A O   1 
HETATM 1220 O  O   . HOH F 6 .   ? 31.797 -0.815  15.834 1.00 43.62  ? 318 HOH A O   1 
HETATM 1221 O  O   . HOH F 6 .   ? 22.551 -27.639 17.741 1.00 55.41  ? 319 HOH A O   1 
HETATM 1222 O  O   . HOH F 6 .   ? 26.744 -31.959 16.120 1.00 55.16  ? 320 HOH A O   1 
HETATM 1223 O  O   . HOH F 6 .   ? 30.343 1.497   33.929 1.00 66.73  ? 321 HOH A O   1 
HETATM 1224 O  O   . HOH F 6 .   ? 20.785 -5.829  25.985 1.00 43.85  ? 322 HOH A O   1 
HETATM 1225 O  O   . HOH F 6 .   ? 17.985 -29.324 7.654  1.00 39.31  ? 323 HOH A O   1 
HETATM 1226 O  O   . HOH F 6 .   ? 13.439 -14.219 21.764 1.00 73.46  ? 324 HOH A O   1 
HETATM 1227 O  O   . HOH F 6 .   ? 23.467 -5.698  32.921 1.00 42.57  ? 325 HOH A O   1 
HETATM 1228 O  O   . HOH F 6 .   ? 32.436 -24.690 32.232 1.00 67.15  ? 326 HOH A O   1 
HETATM 1229 O  O   . HOH F 6 .   ? 41.320 -16.852 15.193 1.00 40.96  ? 327 HOH A O   1 
HETATM 1230 O  O   . HOH F 6 .   ? 26.003 -21.781 38.600 1.00 42.28  ? 328 HOH A O   1 
HETATM 1231 O  O   . HOH F 6 .   ? 20.548 -13.346 20.403 1.00 57.94  ? 329 HOH A O   1 
HETATM 1232 O  O   . HOH F 6 .   ? 34.913 -18.837 13.851 0.50 32.46  ? 330 HOH A O   1 
HETATM 1233 O  O   . HOH F 6 .   ? 21.739 -29.636 -5.262 1.00 41.03  ? 331 HOH A O   1 
HETATM 1234 O  O   . HOH F 6 .   ? 29.648 -2.129  13.730 1.00 65.21  ? 332 HOH A O   1 
HETATM 1235 O  O   . HOH F 6 .   ? 32.335 -8.867  39.642 1.00 58.23  ? 333 HOH A O   1 
HETATM 1236 O  O   . HOH F 6 .   ? 27.148 -2.435  16.092 1.00 65.56  ? 334 HOH A O   1 
HETATM 1237 O  O   . HOH F 6 .   ? 26.768 -16.434 38.693 1.00 54.55  ? 335 HOH A O   1 
HETATM 1238 O  O   . HOH F 6 .   ? 41.536 -12.864 14.113 1.00 96.98  ? 336 HOH A O   1 
HETATM 1239 O  O   . HOH F 6 .   ? 14.255 -16.745 23.402 1.00 46.94  ? 337 HOH A O   1 
HETATM 1240 O  O   . HOH F 6 .   ? 27.253 -28.102 18.644 1.00 34.62  ? 338 HOH A O   1 
HETATM 1241 O  O   . HOH F 6 .   ? 4.335  -20.073 37.898 1.00 65.77  ? 339 HOH A O   1 
HETATM 1242 O  O   . HOH F 6 .   ? 28.187 -23.724 31.624 1.00 44.55  ? 340 HOH A O   1 
HETATM 1243 O  O   . HOH F 6 .   ? 28.233 -8.774  39.924 1.00 54.25  ? 341 HOH A O   1 
HETATM 1244 O  O   . HOH F 6 .   ? 12.609 -20.486 42.491 1.00 67.05  ? 342 HOH A O   1 
HETATM 1245 O  O   . HOH F 6 .   ? 25.769 -2.743  19.981 1.00 68.64  ? 343 HOH A O   1 
HETATM 1246 O  O   . HOH F 6 .   ? 30.408 -0.492  36.846 1.00 60.43  ? 344 HOH A O   1 
HETATM 1247 O  O   . HOH F 6 .   ? 15.386 -9.835  24.795 1.00 56.72  ? 345 HOH A O   1 
HETATM 1248 O  O   . HOH F 6 .   ? 24.060 -15.750 21.162 1.00 34.37  ? 346 HOH A O   1 
HETATM 1249 O  O   . HOH F 6 .   ? 23.300 -17.191 44.282 1.00 72.24  ? 347 HOH A O   1 
HETATM 1250 O  O   . HOH F 6 .   ? 43.918 -4.379  25.829 1.00 55.86  ? 348 HOH A O   1 
HETATM 1251 O  O   . HOH F 6 .   ? 21.895 -24.958 18.316 1.00 26.16  ? 349 HOH A O   1 
HETATM 1252 O  O   . HOH F 6 .   ? 21.434 -29.866 14.175 1.00 79.12  ? 350 HOH A O   1 
HETATM 1253 O  O   . HOH F 6 .   ? 41.150 -7.704  46.362 1.00 63.10  ? 351 HOH A O   1 
HETATM 1254 O  O   . HOH F 6 .   ? 41.278 -6.932  35.893 1.00 48.00  ? 352 HOH A O   1 
HETATM 1255 O  O   . HOH F 6 .   ? 28.480 -24.205 34.289 1.00 57.84  ? 353 HOH A O   1 
HETATM 1256 O  O   . HOH F 6 .   ? 39.107 -18.968 33.240 1.00 53.01  ? 354 HOH A O   1 
HETATM 1257 O  O   . HOH F 6 .   ? 46.007 -14.145 21.450 1.00 66.17  ? 355 HOH A O   1 
HETATM 1258 O  O   . HOH F 6 .   ? 37.398 -6.414  34.216 1.00 46.27  ? 356 HOH A O   1 
HETATM 1259 O  O   . HOH F 6 .   ? 7.072  -16.721 32.291 1.00 62.16  ? 357 HOH A O   1 
HETATM 1260 O  O   . HOH F 6 .   ? 26.060 -22.528 29.890 1.00 30.90  ? 358 HOH A O   1 
HETATM 1261 O  O   . HOH F 6 .   ? 21.421 -27.071 14.506 0.50 43.85  ? 359 HOH A O   1 
HETATM 1262 O  O   . HOH F 6 .   ? 44.331 -12.479 41.220 1.00 54.25  ? 360 HOH A O   1 
HETATM 1263 O  O   A HOH F 6 .   ? 19.076 -22.953 4.285  0.60 38.79  ? 361 HOH A O   1 
HETATM 1264 O  O   . HOH F 6 .   ? 29.379 -27.371 20.607 1.00 29.58  ? 362 HOH A O   1 
HETATM 1265 O  O   . HOH F 6 .   ? 29.053 -31.171 7.242  1.00 34.79  ? 363 HOH A O   1 
HETATM 1266 O  O   . HOH F 6 .   ? 20.753 -7.158  19.628 1.00 65.20  ? 364 HOH A O   1 
HETATM 1267 O  O   . HOH F 6 .   ? 36.812 -5.573  12.118 1.00 42.95  ? 365 HOH A O   1 
HETATM 1268 O  O   . HOH F 6 .   ? 42.457 -10.450 15.452 1.00 52.17  ? 366 HOH A O   1 
HETATM 1269 O  O   . HOH F 6 .   ? 10.923 -11.330 34.491 1.00 56.65  ? 367 HOH A O   1 
HETATM 1270 O  O   . HOH F 6 .   ? 22.237 -34.091 26.325 1.00 80.86  ? 368 HOH A O   1 
HETATM 1271 O  O   . HOH F 6 .   ? 46.225 -15.867 27.596 1.00 68.70  ? 369 HOH A O   1 
HETATM 1272 O  O   . HOH F 6 .   ? 24.834 -26.815 19.004 1.00 40.60  ? 370 HOH A O   1 
HETATM 1273 O  O   . HOH F 6 .   ? 46.312 -29.805 21.395 1.00 78.51  ? 371 HOH A O   1 
HETATM 1274 O  O   . HOH F 6 .   ? 46.824 -21.842 17.788 1.00 44.72  ? 372 HOH A O   1 
HETATM 1275 O  O   . HOH F 6 .   ? 20.083 -15.735 40.795 1.00 37.96  ? 373 HOH A O   1 
HETATM 1276 O  O   . HOH F 6 .   ? 34.137 -7.849  35.603 1.00 38.29  ? 374 HOH A O   1 
HETATM 1277 O  O   . HOH F 6 .   ? 44.606 -8.607  17.883 1.00 64.83  ? 375 HOH A O   1 
HETATM 1278 O  O   . HOH F 6 .   ? 25.821 -4.498  17.920 1.00 54.42  ? 376 HOH A O   1 
HETATM 1279 O  O   . HOH F 6 .   ? 30.660 -28.787 22.620 1.00 43.90  ? 377 HOH A O   1 
HETATM 1280 O  O   . HOH F 6 .   ? 37.516 3.431   15.669 1.00 46.52  ? 378 HOH A O   1 
HETATM 1281 O  O   . HOH F 6 .   ? 21.324 -31.200 29.937 1.00 68.97  ? 379 HOH A O   1 
HETATM 1282 O  O   . HOH F 6 .   ? 22.695 -33.986 8.826  1.00 37.06  ? 380 HOH A O   1 
HETATM 1283 O  O   . HOH F 6 .   ? 31.867 -31.808 14.655 1.00 49.25  ? 381 HOH A O   1 
HETATM 1284 O  O   . HOH F 6 .   ? 18.043 -34.546 8.329  1.00 37.05  ? 382 HOH A O   1 
HETATM 1285 O  O   . HOH F 6 .   ? 46.303 -18.944 19.661 1.00 57.96  ? 383 HOH A O   1 
HETATM 1286 O  O   . HOH F 6 .   ? 26.335 -7.865  9.080  1.00 50.71  ? 384 HOH A O   1 
HETATM 1287 O  O   . HOH F 6 .   ? 27.723 -22.988 13.851 0.50 31.78  ? 385 HOH A O   1 
HETATM 1288 O  O   . HOH F 6 .   ? 47.230 -25.189 21.569 1.00 58.99  ? 386 HOH A O   1 
HETATM 1289 O  O   . HOH F 6 .   ? 40.325 -19.591 28.995 1.00 39.90  ? 387 HOH A O   1 
HETATM 1290 O  O   . HOH F 6 .   ? 32.990 -29.639 21.506 1.00 44.90  ? 388 HOH A O   1 
HETATM 1291 O  O   . HOH F 6 .   ? 43.506 -10.618 35.307 1.00 68.34  ? 389 HOH A O   1 
HETATM 1292 O  O   . HOH F 6 .   ? 26.061 -19.171 41.859 1.00 78.81  ? 390 HOH A O   1 
HETATM 1293 O  O   . HOH F 6 .   ? 23.726 -15.773 17.766 1.00 48.17  ? 391 HOH A O   1 
HETATM 1294 O  O   . HOH F 6 .   ? 46.049 -8.874  44.055 1.00 57.99  ? 392 HOH A O   1 
HETATM 1295 O  O   . HOH F 6 .   ? 42.172 -6.053  11.845 1.00 72.77  ? 393 HOH A O   1 
HETATM 1296 O  O   . HOH F 6 .   ? 45.261 -12.710 23.613 1.00 52.69  ? 394 HOH A O   1 
HETATM 1297 O  O   . HOH F 6 .   ? 27.031 -1.528  22.051 1.00 60.29  ? 395 HOH A O   1 
HETATM 1298 O  O   . HOH F 6 .   ? 21.042 -22.993 42.052 1.00 54.38  ? 396 HOH A O   1 
HETATM 1299 O  O   . HOH F 6 .   ? 46.904 -20.081 22.035 1.00 66.45  ? 397 HOH A O   1 
HETATM 1300 O  O   . HOH F 6 .   ? 41.262 -17.010 35.173 1.00 47.64  ? 398 HOH A O   1 
HETATM 1301 O  O   . HOH F 6 .   ? 22.818 -14.779 40.324 1.00 37.23  ? 399 HOH A O   1 
HETATM 1302 O  O   . HOH F 6 .   ? 37.932 -16.292 12.717 1.00 62.61  ? 400 HOH A O   1 
HETATM 1303 O  O   . HOH F 6 .   ? 37.159 -2.567  11.686 1.00 65.07  ? 401 HOH A O   1 
HETATM 1304 O  O   . HOH F 6 .   ? 34.770 -33.386 21.921 1.00 61.56  ? 402 HOH A O   1 
HETATM 1305 O  O   . HOH F 6 .   ? 23.474 -30.255 19.159 1.00 72.18  ? 403 HOH A O   1 
HETATM 1306 O  O   . HOH F 6 .   ? 22.401 -10.116 14.447 1.00 46.14  ? 404 HOH A O   1 
HETATM 1307 O  O   . HOH F 6 .   ? 11.483 -14.835 40.669 1.00 93.18  ? 405 HOH A O   1 
HETATM 1308 O  O   . HOH F 6 .   ? 19.596 -27.367 10.102 1.00 58.37  ? 406 HOH A O   1 
HETATM 1309 O  O   . HOH F 6 .   ? 33.808 -33.127 12.311 1.00 46.00  ? 407 HOH A O   1 
HETATM 1310 O  O   . HOH F 6 .   ? 44.560 -16.395 29.676 1.00 54.71  ? 408 HOH A O   1 
HETATM 1311 O  O   . HOH F 6 .   ? 41.790 -8.106  13.668 1.00 69.64  ? 409 HOH A O   1 
HETATM 1312 O  O   . HOH F 6 .   ? 32.040 -15.543 39.809 1.00 40.44  ? 410 HOH A O   1 
HETATM 1313 O  O   . HOH F 6 .   ? 29.572 -0.815  22.150 1.00 61.04  ? 411 HOH A O   1 
HETATM 1314 O  O   . HOH F 6 .   ? 30.329 -10.405 40.541 1.00 48.22  ? 412 HOH A O   1 
HETATM 1315 O  O   . HOH F 6 .   ? 35.443 2.121   13.591 1.00 61.05  ? 413 HOH A O   1 
HETATM 1316 O  O   . HOH F 6 .   ? 10.213 -11.650 39.909 1.00 70.76  ? 414 HOH A O   1 
HETATM 1317 O  O   . HOH F 6 .   ? 45.508 -10.550 30.416 1.00 64.06  ? 415 HOH A O   1 
HETATM 1318 O  O   . HOH F 6 .   ? 39.958 -5.546  33.880 1.00 47.42  ? 416 HOH A O   1 
HETATM 1319 O  O   . HOH F 6 .   ? 35.183 -29.731 23.517 1.00 52.05  ? 417 HOH A O   1 
HETATM 1320 O  O   . HOH F 6 .   ? 44.317 -25.977 26.507 1.00 64.23  ? 418 HOH A O   1 
HETATM 1321 O  O   . HOH F 6 .   ? 27.387 -25.565 28.197 1.00 60.07  ? 419 HOH A O   1 
HETATM 1322 O  O   . HOH F 6 .   ? 44.817 -8.079  15.200 1.00 78.42  ? 420 HOH A O   1 
HETATM 1323 O  O   . HOH F 6 .   ? 33.500 -0.268  19.931 1.00 52.03  ? 421 HOH A O   1 
HETATM 1324 O  O   B HOH F 6 .   ? 37.240 -11.964 40.192 0.50 39.17  ? 422 HOH A O   1 
HETATM 1325 O  O   . HOH F 6 .   ? 28.472 -15.909 41.387 1.00 73.24  ? 423 HOH A O   1 
HETATM 1326 O  O   . HOH F 6 .   ? 42.783 -18.251 30.701 1.00 52.76  ? 424 HOH A O   1 
HETATM 1327 O  O   . HOH F 6 .   ? 45.926 -17.079 17.076 1.00 71.53  ? 425 HOH A O   1 
HETATM 1328 O  O   . HOH F 6 .   ? 33.852 -17.556 39.453 1.00 64.97  ? 426 HOH A O   1 
HETATM 1329 O  O   . HOH F 6 .   ? 28.227 -2.548  11.323 1.00 75.69  ? 427 HOH A O   1 
HETATM 1330 O  O   . HOH F 6 .   ? 32.385 -3.706  41.131 1.00 69.92  ? 428 HOH A O   1 
HETATM 1331 O  O   . HOH F 6 .   ? 25.622 -15.804 41.078 1.00 55.66  ? 429 HOH A O   1 
HETATM 1332 O  O   . HOH F 6 .   ? 26.223 -29.305 22.597 1.00 63.14  ? 430 HOH A O   1 
HETATM 1333 O  O   . HOH F 6 .   ? 37.626 -27.050 28.447 1.00 71.58  ? 431 HOH A O   1 
HETATM 1334 O  O   . HOH F 6 .   ? 45.842 -5.512  23.732 1.00 56.83  ? 432 HOH A O   1 
HETATM 1335 O  O   . HOH F 6 .   ? 29.967 -22.596 36.753 1.00 74.94  ? 433 HOH A O   1 
HETATM 1336 O  O   . HOH F 6 .   ? 47.922 -23.188 19.866 1.00 66.19  ? 434 HOH A O   1 
HETATM 1337 O  O   . HOH F 6 .   ? 31.845 -26.197 26.994 1.00 51.66  ? 435 HOH A O   1 
HETATM 1338 O  O   . HOH F 6 .   ? 28.270 -29.118 26.887 1.00 91.78  ? 436 HOH A O   1 
HETATM 1339 O  O   . HOH F 6 .   ? 31.898 0.166   13.287 1.00 65.22  ? 437 HOH A O   1 
HETATM 1340 O  O   . HOH F 6 .   ? 35.143 -4.082  10.657 1.00 51.88  ? 438 HOH A O   1 
HETATM 1341 O  O   . HOH F 6 .   ? 27.089 -34.557 17.935 1.00 80.62  ? 439 HOH A O   1 
HETATM 1342 O  O   . HOH F 6 .   ? 19.408 -31.654 13.881 1.00 77.09  ? 440 HOH A O   1 
HETATM 1343 O  O   . HOH F 6 .   ? 47.042 -12.981 28.692 1.00 70.57  ? 441 HOH A O   1 
HETATM 1344 O  O   . HOH F 6 .   ? 20.048 -35.257 10.156 1.00 46.04  ? 442 HOH A O   1 
HETATM 1345 O  O   . HOH F 6 .   ? 37.103 -24.265 27.480 1.00 63.04  ? 443 HOH A O   1 
HETATM 1346 O  O   . HOH F 6 .   ? 24.236 -21.540 41.000 1.00 65.86  ? 444 HOH A O   1 
HETATM 1347 O  O   . HOH F 6 .   ? 22.970 -2.728  26.237 1.00 66.06  ? 445 HOH A O   1 
HETATM 1348 O  O   . HOH F 6 .   ? 46.602 -14.616 18.044 1.00 74.45  ? 446 HOH A O   1 
HETATM 1349 O  O   . HOH F 6 .   ? 31.066 -34.404 14.802 1.00 65.05  ? 447 HOH A O   1 
HETATM 1350 O  O   . HOH F 6 .   ? 32.230 -1.070  22.185 1.00 66.55  ? 448 HOH A O   1 
HETATM 1351 O  O   . HOH F 6 .   ? 11.930 -18.645 22.519 1.00 65.31  ? 449 HOH A O   1 
HETATM 1352 O  O   . HOH F 6 .   ? 47.062 -11.848 25.472 1.00 72.58  ? 450 HOH A O   1 
HETATM 1353 O  O   . HOH F 6 .   ? 33.770 -10.973 41.552 0.50 62.74  ? 451 HOH A O   1 
HETATM 1354 O  O   . HOH F 6 .   ? 47.345 -28.614 17.709 1.00 70.68  ? 452 HOH A O   1 
HETATM 1355 O  O   . HOH F 6 .   ? 34.551 -18.984 36.111 1.00 67.54  ? 453 HOH A O   1 
HETATM 1356 O  O   . HOH F 6 .   ? 19.227 -7.523  35.220 1.00 62.94  ? 454 HOH A O   1 
HETATM 1357 O  O   A HOH F 6 .   ? 12.162 -20.911 27.945 0.78 47.04  ? 455 HOH A O   1 
HETATM 1358 O  O   . HOH F 6 .   ? 13.821 -16.175 39.878 1.00 75.73  ? 456 HOH A O   1 
HETATM 1359 O  O   . HOH F 6 .   ? 43.083 -3.068  33.849 1.00 64.19  ? 457 HOH A O   1 
HETATM 1360 O  O   . HOH F 6 .   ? 15.998 -15.458 41.338 1.00 75.41  ? 458 HOH A O   1 
HETATM 1361 O  O   . HOH F 6 .   ? 25.418 -5.717  35.142 1.00 59.00  ? 459 HOH A O   1 
HETATM 1362 O  O   . HOH F 6 .   ? 44.182 -13.486 13.851 0.50 84.68  ? 460 HOH A O   1 
HETATM 1363 O  O   . HOH F 6 .   ? 17.049 -28.113 9.873  1.00 56.96  ? 461 HOH A O   1 
HETATM 1364 O  O   . HOH F 6 .   ? 33.770 -13.935 41.553 0.50 44.76  ? 462 HOH A O   1 
HETATM 1365 O  O   . HOH F 6 .   ? 17.359 -8.030  24.778 1.00 66.40  ? 463 HOH A O   1 
HETATM 1366 O  O   . HOH F 6 .   ? 32.065 -23.841 34.817 1.00 74.05  ? 464 HOH A O   1 
HETATM 1367 O  O   . HOH F 6 .   ? 32.455 -20.501 37.003 1.00 85.16  ? 465 HOH A O   1 
HETATM 1368 O  O   . HOH F 6 .   ? 28.264 -29.897 24.280 1.00 70.63  ? 466 HOH A O   1 
HETATM 1369 O  O   . HOH F 6 .   ? 18.951 -28.053 13.851 0.50 74.31  ? 467 HOH A O   1 
HETATM 1370 O  O   . HOH F 6 .   ? 45.437 -12.768 16.173 1.00 81.52  ? 468 HOH A O   1 
HETATM 1371 O  O   . HOH F 6 .   ? 23.196 -4.576  17.177 1.00 76.86  ? 469 HOH A O   1 
HETATM 1372 O  O   . HOH F 6 .   ? 21.088 -5.597  34.673 1.00 62.49  ? 470 HOH A O   1 
HETATM 1373 O  O   . HOH F 6 .   ? 34.930 -23.616 32.889 1.00 68.65  ? 471 HOH A O   1 
HETATM 1374 O  O   . HOH F 6 .   ? 32.885 -0.764  42.854 1.00 63.16  ? 472 HOH A O   1 
HETATM 1375 O  O   . HOH F 6 .   ? 16.693 -6.515  34.558 1.00 90.09  ? 473 HOH A O   1 
HETATM 1376 O  O   . HOH G 6 .   ? 12.335 -24.214 0.010  1.00 54.56  ? 201 HOH D O   1 
HETATM 1377 O  O   . HOH G 6 .   ? 15.054 -25.904 -1.870 1.00 46.25  ? 202 HOH D O   1 
HETATM 1378 O  O   . HOH G 6 .   ? 11.697 -23.589 3.059  1.00 59.26  ? 203 HOH D O   1 
HETATM 1379 O  O   . HOH G 6 .   ? 21.060 -38.308 4.053  1.00 50.69  ? 204 HOH D O   1 
HETATM 1380 O  O   . HOH G 6 .   ? 17.716 -36.378 6.212  1.00 46.62  ? 205 HOH D O   1 
HETATM 1381 O  O   . HOH G 6 .   ? 20.910 -39.331 -2.192 1.00 63.85  ? 206 HOH D O   1 
HETATM 1382 O  O   . HOH G 6 .   ? 18.683 -40.648 0.783  1.00 71.55  ? 207 HOH D O   1 
HETATM 1383 O  O   . HOH G 6 .   ? 10.778 -24.852 5.498  1.00 62.12  ? 208 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   ? 0.8707 1.0670 0.7963 0.0466  -0.1389 -0.0247 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8650 1.0537 0.7732 0.0295  -0.1296 -0.0272 6   ASP A CA  
3    C C   . ASP A 5   ? 0.8425 1.0630 0.7762 0.0162  -0.1254 -0.0447 6   ASP A C   
4    O O   . ASP A 5   ? 0.8315 1.0810 0.7943 0.0197  -0.1304 -0.0549 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8873 1.0437 0.7857 0.0203  -0.1116 -0.0193 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0824 1.2166 0.9459 0.0107  -0.1063 -0.0144 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0868 1.2335 0.9481 -0.0010 -0.1037 -0.0238 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1898 1.2934 1.0279 0.0137  -0.1033 -0.0020 6   ASP A OD2 
9    N N   . SER A 6   ? 0.7396 0.9538 0.6619 0.0003  -0.1153 -0.0491 7   SER A N   
10   C CA  . SER A 6   ? 0.6937 0.9303 0.6349 -0.0141 -0.1089 -0.0651 7   SER A CA  
11   C C   . SER A 6   ? 0.6402 0.8609 0.5937 -0.0261 -0.0894 -0.0670 7   SER A C   
12   O O   . SER A 6   ? 0.6281 0.8521 0.5847 -0.0398 -0.0807 -0.0769 7   SER A O   
13   C CB  . SER A 6   ? 0.7689 1.0113 0.6874 -0.0221 -0.1136 -0.0706 7   SER A CB  
14   O OG  . SER A 6   ? 0.9408 1.1534 0.8294 -0.0272 -0.1056 -0.0618 7   SER A OG  
15   N N   . CYS A 7   ? 0.5219 0.7251 0.4822 -0.0202 -0.0834 -0.0579 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4830 0.6704 0.4536 -0.0287 -0.0677 -0.0584 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4559 0.6594 0.4519 -0.0375 -0.0616 -0.0711 8   CYS A C   
18   O O   . CYS A 7   ? 0.4398 0.6678 0.4516 -0.0355 -0.0684 -0.0788 8   CYS A O   
19   C CB  . CYS A 7   ? 0.4963 0.6646 0.4680 -0.0198 -0.0649 -0.0467 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5792 0.7186 0.5185 -0.0147 -0.0652 -0.0321 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3429 0.5317 0.3422 -0.0473 -0.0487 -0.0740 9   ILE A N   
22   C CA  . ILE A 8   ? 0.3004 0.4927 0.3186 -0.0556 -0.0406 -0.0829 9   ILE A CA  
23   C C   . ILE A 8   ? 0.3282 0.5016 0.3517 -0.0505 -0.0349 -0.0739 9   ILE A C   
24   O O   . ILE A 8   ? 0.3231 0.4801 0.3357 -0.0442 -0.0347 -0.0636 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3380 0.5255 0.3545 -0.0693 -0.0315 -0.0933 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3542 0.5175 0.3571 -0.0705 -0.0243 -0.0884 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3473 0.5587 0.3618 -0.0756 -0.0376 -0.1047 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.4211 0.5752 0.4237 -0.0817 -0.0147 -0.0986 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2607 0.4354 0.2993 -0.0543 -0.0295 -0.0783 10  GLN A N   
30   N N   B GLN A 9   ? 0.2627 0.4392 0.3018 -0.0539 -0.0302 -0.0784 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2495 0.4069 0.2914 -0.0499 -0.0248 -0.0703 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2492 0.4095 0.2930 -0.0500 -0.0252 -0.0712 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2913 0.4332 0.3365 -0.0592 -0.0144 -0.0745 10  GLN A C   
34   C C   B GLN A 9   ? 0.2853 0.4286 0.3306 -0.0596 -0.0146 -0.0752 10  GLN A C   
35   O O   A GLN A 9   ? 0.2855 0.4357 0.3376 -0.0686 -0.0106 -0.0846 10  GLN A O   
36   O O   B GLN A 9   ? 0.2845 0.4340 0.3343 -0.0698 -0.0105 -0.0855 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2591 0.4311 0.3131 -0.0418 -0.0302 -0.0689 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2561 0.4332 0.3146 -0.0442 -0.0294 -0.0724 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2718 0.4273 0.3288 -0.0375 -0.0255 -0.0613 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.3262 0.4888 0.3906 -0.0437 -0.0224 -0.0684 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5852 0.7571 0.6576 -0.0327 -0.0280 -0.0644 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4681 0.6294 0.5343 -0.0312 -0.0272 -0.0597 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4541 0.6415 0.5400 -0.0401 -0.0246 -0.0751 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3478 0.5190 0.4116 -0.0213 -0.0367 -0.0563 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.6178 0.7862 0.6889 -0.0206 -0.0331 -0.0560 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.3483 0.4951 0.4168 -0.0313 -0.0209 -0.0559 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2710 0.3896 0.3102 -0.0568 -0.0100 -0.0671 11  PHE A N   
48   N N   B PHE A 10  ? 0.2483 0.3693 0.2888 -0.0563 -0.0106 -0.0672 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2714 0.3709 0.3102 -0.0632 -0.0020 -0.0694 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2485 0.3492 0.2877 -0.0623 -0.0026 -0.0687 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2947 0.3906 0.3392 -0.0618 -0.0001 -0.0662 11  PHE A C   
52   C C   B PHE A 10  ? 0.2875 0.3848 0.3325 -0.0613 -0.0005 -0.0660 11  PHE A C   
53   O O   A PHE A 10  ? 0.2844 0.3723 0.3276 -0.0542 -0.0017 -0.0576 11  PHE A O   
54   O O   B PHE A 10  ? 0.2772 0.3686 0.3216 -0.0534 -0.0026 -0.0575 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2932 0.3717 0.3237 -0.0607 0.0004  -0.0653 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2712 0.3525 0.3021 -0.0584 -0.0011 -0.0633 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.3150 0.3719 0.3423 -0.0658 0.0066  -0.0683 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.2989 0.3795 0.3247 -0.0630 0.0007  -0.0697 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3615 0.4154 0.3864 -0.0752 0.0111  -0.0777 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3372 0.4339 0.3592 -0.0631 -0.0034 -0.0718 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3332 0.3708 0.3576 -0.0612 0.0075  -0.0619 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3405 0.4030 0.3636 -0.0670 0.0062  -0.0740 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3879 0.4161 0.4059 -0.0793 0.0167  -0.0796 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3585 0.4546 0.3749 -0.0685 -0.0007 -0.0789 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3714 0.3855 0.3890 -0.0645 0.0116  -0.0636 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3861 0.4477 0.4054 -0.0711 0.0088  -0.0814 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3534 0.3610 0.3668 -0.0732 0.0163  -0.0720 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3575 0.4367 0.3738 -0.0726 0.0059  -0.0841 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2452 0.3479 0.2958 -0.0705 0.0043  -0.0742 12  THR A N   
70   C CA  . THR A 11  ? 0.2531 0.3552 0.3094 -0.0720 0.0081  -0.0741 12  THR A CA  
71   C C   . THR A 11  ? 0.3161 0.3915 0.3631 -0.0687 0.0109  -0.0650 12  THR A C   
72   O O   . THR A 11  ? 0.3053 0.3827 0.3561 -0.0630 0.0098  -0.0602 12  THR A O   
73   C CB  . THR A 11  ? 0.3530 0.4604 0.4131 -0.0862 0.0159  -0.0861 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3512 0.4884 0.4225 -0.0884 0.0116  -0.0956 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3950 0.5031 0.4606 -0.0904 0.0220  -0.0883 12  THR A CG2 
76   N N   A ARG A 12  ? 0.2903 0.3413 0.3253 -0.0714 0.0139  -0.0633 13  ARG A N   
77   N N   B ARG A 12  ? 0.2946 0.3456 0.3296 -0.0715 0.0139  -0.0633 13  ARG A N   
78   C CA  A ARG A 12  ? 0.3020 0.3277 0.3270 -0.0682 0.0150  -0.0558 13  ARG A CA  
79   C CA  B ARG A 12  ? 0.3082 0.3338 0.3331 -0.0682 0.0150  -0.0558 13  ARG A CA  
80   C C   A ARG A 12  ? 0.3278 0.3507 0.3527 -0.0569 0.0090  -0.0476 13  ARG A C   
81   C C   B ARG A 12  ? 0.3308 0.3537 0.3557 -0.0569 0.0090  -0.0476 13  ARG A C   
82   O O   A ARG A 12  ? 0.3188 0.3240 0.3370 -0.0535 0.0086  -0.0424 13  ARG A O   
83   O O   B ARG A 12  ? 0.3221 0.3272 0.3402 -0.0535 0.0086  -0.0424 13  ARG A O   
84   C CB  A ARG A 12  ? 0.3396 0.3384 0.3509 -0.0746 0.0195  -0.0580 13  ARG A CB  
85   C CB  B ARG A 12  ? 0.3557 0.3547 0.3671 -0.0745 0.0194  -0.0581 13  ARG A CB  
86   C CG  A ARG A 12  ? 0.4358 0.4285 0.4419 -0.0885 0.0282  -0.0656 13  ARG A CG  
87   C CG  B ARG A 12  ? 0.5015 0.4878 0.5046 -0.0865 0.0277  -0.0625 13  ARG A CG  
88   C CD  A ARG A 12  ? 0.6027 0.5897 0.6052 -0.0924 0.0326  -0.0637 13  ARG A CD  
89   C CD  B ARG A 12  ? 0.6065 0.5771 0.5998 -0.0969 0.0337  -0.0697 13  ARG A CD  
90   N NE  A ARG A 12  ? 0.6998 0.6557 0.6849 -0.0886 0.0316  -0.0552 13  ARG A NE  
91   N NE  B ARG A 12  ? 0.6727 0.6220 0.6569 -0.0905 0.0303  -0.0668 13  ARG A NE  
92   C CZ  A ARG A 12  ? 0.7887 0.7385 0.7690 -0.0882 0.0328  -0.0508 13  ARG A CZ  
93   C CZ  B ARG A 12  ? 0.8016 0.7553 0.7887 -0.0920 0.0305  -0.0730 13  ARG A CZ  
94   N NH1 A ARG A 12  ? 0.5376 0.5098 0.5307 -0.0907 0.0358  -0.0543 13  ARG A NH1 
95   N NH1 B ARG A 12  ? 0.7181 0.6525 0.6987 -0.0853 0.0280  -0.0715 13  ARG A NH1 
96   N NH2 A ARG A 12  ? 0.6426 0.5641 0.6052 -0.0845 0.0304  -0.0435 13  ARG A NH2 
97   N NH2 B ARG A 12  ? 0.4769 0.4551 0.4739 -0.1001 0.0331  -0.0818 13  ARG A NH2 
98   N N   . HIS A 13  ? 0.2752 0.3146 0.3058 -0.0519 0.0047  -0.0471 14  HIS A N   
99   C CA  . HIS A 13  ? 0.2595 0.2961 0.2889 -0.0438 0.0012  -0.0409 14  HIS A CA  
100  C C   . HIS A 13  ? 0.2941 0.3252 0.3236 -0.0387 0.0003  -0.0342 14  HIS A C   
101  O O   . HIS A 13  ? 0.2941 0.3129 0.3204 -0.0355 -0.0004 -0.0311 14  HIS A O   
102  C CB  . HIS A 13  ? 0.2551 0.3075 0.2858 -0.0411 -0.0021 -0.0411 14  HIS A CB  
103  C CG  . HIS A 13  ? 0.2780 0.3252 0.3055 -0.0358 -0.0032 -0.0362 14  HIS A CG  
104  N ND1 . HIS A 13  ? 0.2882 0.3269 0.3144 -0.0361 -0.0014 -0.0387 14  HIS A ND1 
105  C CD2 . HIS A 13  ? 0.2904 0.3397 0.3161 -0.0309 -0.0050 -0.0301 14  HIS A CD2 
106  C CE1 . HIS A 13  ? 0.2804 0.3190 0.3055 -0.0327 -0.0015 -0.0352 14  HIS A CE1 
107  N NE2 . HIS A 13  ? 0.2800 0.3228 0.3031 -0.0300 -0.0033 -0.0294 14  HIS A NE2 
108  N N   . ALA A 14  ? 0.2546 0.2962 0.2890 -0.0374 0.0000  -0.0330 15  ALA A N   
109  C CA  . ALA A 14  ? 0.2628 0.2988 0.2971 -0.0330 0.0000  -0.0275 15  ALA A CA  
110  C C   . ALA A 14  ? 0.2992 0.3175 0.3273 -0.0362 0.0029  -0.0266 15  ALA A C   
111  O O   . ALA A 14  ? 0.2801 0.2892 0.3050 -0.0327 0.0017  -0.0223 15  ALA A O   
112  C CB  . ALA A 14  ? 0.2733 0.3236 0.3154 -0.0305 -0.0004 -0.0283 15  ALA A CB  
113  N N   A SER A 15  ? 0.2736 0.2861 0.2981 -0.0436 0.0066  -0.0310 16  SER A N   
114  N N   B SER A 15  ? 0.2746 0.2871 0.2991 -0.0436 0.0066  -0.0310 16  SER A N   
115  N N   C SER A 15  ? 0.2750 0.2874 0.2995 -0.0436 0.0066  -0.0310 16  SER A N   
116  C CA  A SER A 15  ? 0.2876 0.2788 0.3005 -0.0474 0.0091  -0.0296 16  SER A CA  
117  C CA  B SER A 15  ? 0.2892 0.2803 0.3020 -0.0475 0.0092  -0.0297 16  SER A CA  
118  C CA  C SER A 15  ? 0.2896 0.2806 0.3024 -0.0474 0.0091  -0.0295 16  SER A CA  
119  C C   A SER A 15  ? 0.3494 0.3245 0.3547 -0.0431 0.0049  -0.0269 16  SER A C   
120  C C   B SER A 15  ? 0.3514 0.3262 0.3565 -0.0432 0.0049  -0.0269 16  SER A C   
121  C C   C SER A 15  ? 0.3523 0.3270 0.3574 -0.0432 0.0049  -0.0269 16  SER A C   
122  O O   A SER A 15  ? 0.3365 0.2979 0.3343 -0.0404 0.0026  -0.0231 16  SER A O   
123  O O   B SER A 15  ? 0.3412 0.3021 0.3387 -0.0407 0.0028  -0.0231 16  SER A O   
124  O O   C SER A 15  ? 0.3439 0.3043 0.3411 -0.0407 0.0027  -0.0232 16  SER A O   
125  C CB  A SER A 15  ? 0.3358 0.3214 0.3433 -0.0579 0.0154  -0.0354 16  SER A CB  
126  C CB  B SER A 15  ? 0.3387 0.3244 0.3462 -0.0581 0.0154  -0.0356 16  SER A CB  
127  C CB  C SER A 15  ? 0.3421 0.3278 0.3496 -0.0579 0.0155  -0.0353 16  SER A CB  
128  O OG  A SER A 15  ? 0.4100 0.3708 0.4010 -0.0620 0.0180  -0.0330 16  SER A OG  
129  O OG  B SER A 15  ? 0.4014 0.4053 0.4192 -0.0620 0.0196  -0.0404 16  SER A OG  
130  O OG  C SER A 15  ? 0.4244 0.4086 0.4305 -0.0615 0.0159  -0.0396 16  SER A OG  
131  N N   . ASP A 16  ? 0.3190 0.2973 0.3272 -0.0421 0.0034  -0.0299 17  ASP A N   
132  C CA  . ASP A 16  ? 0.3371 0.3037 0.3423 -0.0368 -0.0006 -0.0297 17  ASP A CA  
133  C C   . ASP A 16  ? 0.3337 0.3077 0.3455 -0.0296 -0.0045 -0.0266 17  ASP A C   
134  O O   . ASP A 16  ? 0.3354 0.2992 0.3446 -0.0249 -0.0085 -0.0257 17  ASP A O   
135  C CB  . ASP A 16  ? 0.3614 0.3331 0.3703 -0.0380 0.0002  -0.0353 17  ASP A CB  
136  C CG  . ASP A 16  ? 0.5142 0.4734 0.5147 -0.0457 0.0044  -0.0398 17  ASP A CG  
137  O OD1 . ASP A 16  ? 0.5217 0.4650 0.5114 -0.0504 0.0070  -0.0382 17  ASP A OD1 
138  O OD2 . ASP A 16  ? 0.5166 0.4808 0.5200 -0.0482 0.0061  -0.0455 17  ASP A OD2 
139  N N   . VAL A 17  ? 0.2650 0.2561 0.2844 -0.0290 -0.0035 -0.0255 18  VAL A N   
140  C CA  . VAL A 17  ? 0.2598 0.2557 0.2834 -0.0246 -0.0050 -0.0230 18  VAL A CA  
141  C C   . VAL A 17  ? 0.2989 0.2854 0.3183 -0.0236 -0.0062 -0.0196 18  VAL A C   
142  O O   . VAL A 17  ? 0.2773 0.2605 0.2977 -0.0203 -0.0092 -0.0198 18  VAL A O   
143  C CB  . VAL A 17  ? 0.2871 0.2966 0.3140 -0.0245 -0.0033 -0.0212 18  VAL A CB  
144  C CG1 . VAL A 17  ? 0.2801 0.2892 0.3076 -0.0221 -0.0029 -0.0180 18  VAL A CG1 
145  C CG2 . VAL A 17  ? 0.2826 0.3005 0.3107 -0.0256 -0.0029 -0.0247 18  VAL A CG2 
146  N N   . LEU A 18  ? 0.2822 0.2663 0.2977 -0.0268 -0.0036 -0.0177 19  LEU A N   
147  C CA  . LEU A 18  ? 0.2966 0.2715 0.3063 -0.0271 -0.0037 -0.0151 19  LEU A CA  
148  C C   . LEU A 18  ? 0.3316 0.2890 0.3306 -0.0264 -0.0078 -0.0149 19  LEU A C   
149  O O   . LEU A 18  ? 0.3071 0.2598 0.3033 -0.0238 -0.0114 -0.0137 19  LEU A O   
150  C CB  . LEU A 18  ? 0.3088 0.2856 0.3173 -0.0315 0.0013  -0.0151 19  LEU A CB  
151  C CG  . LEU A 18  ? 0.3602 0.3300 0.3636 -0.0324 0.0030  -0.0132 19  LEU A CG  
152  C CD1 . LEU A 18  ? 0.3414 0.3185 0.3516 -0.0281 0.0027  -0.0114 19  LEU A CD1 
153  C CD2 . LEU A 18  ? 0.4020 0.3734 0.4047 -0.0380 0.0093  -0.0157 19  LEU A CD2 
154  N N   . LEU A 19  ? 0.3163 0.2634 0.3086 -0.0284 -0.0078 -0.0165 20  LEU A N   
155  C CA  . LEU A 19  ? 0.3433 0.2691 0.3222 -0.0261 -0.0129 -0.0157 20  LEU A CA  
156  C C   . LEU A 19  ? 0.3588 0.2892 0.3459 -0.0171 -0.0204 -0.0173 20  LEU A C   
157  O O   . LEU A 19  ? 0.3532 0.2739 0.3335 -0.0127 -0.0269 -0.0160 20  LEU A O   
158  C CB  . LEU A 19  ? 0.3772 0.2904 0.3483 -0.0298 -0.0104 -0.0179 20  LEU A CB  
159  C CG  . LEU A 19  ? 0.5043 0.3894 0.4575 -0.0266 -0.0157 -0.0163 20  LEU A CG  
160  C CD1 . LEU A 19  ? 0.5531 0.4168 0.4843 -0.0323 -0.0141 -0.0120 20  LEU A CD1 
161  C CD2 . LEU A 19  ? 0.5857 0.4594 0.5340 -0.0297 -0.0125 -0.0197 20  LEU A CD2 
162  N N   . ASN A 20  ? 0.2882 0.2350 0.2901 -0.0150 -0.0194 -0.0211 21  ASN A N   
163  C CA  . ASN A 20  ? 0.2747 0.2302 0.2878 -0.0080 -0.0245 -0.0252 21  ASN A CA  
164  C C   . ASN A 20  ? 0.3030 0.2683 0.3216 -0.0074 -0.0257 -0.0247 21  ASN A C   
165  O O   . ASN A 20  ? 0.3049 0.2722 0.3282 -0.0018 -0.0321 -0.0280 21  ASN A O   
166  C CB  . ASN A 20  ? 0.2992 0.2685 0.3242 -0.0081 -0.0211 -0.0303 21  ASN A CB  
167  C CG  . ASN A 20  ? 0.4255 0.3831 0.4464 -0.0064 -0.0220 -0.0334 21  ASN A CG  
168  O OD1 . ASN A 20  ? 0.3948 0.3327 0.4050 -0.0027 -0.0269 -0.0321 21  ASN A OD1 
169  N ND2 . ASN A 20  ? 0.3478 0.3146 0.3744 -0.0095 -0.0172 -0.0373 21  ASN A ND2 
170  N N   . LEU A 21  ? 0.2822 0.2538 0.3008 -0.0126 -0.0198 -0.0215 22  LEU A N   
171  C CA  . LEU A 21  ? 0.2833 0.2607 0.3048 -0.0134 -0.0194 -0.0212 22  LEU A CA  
172  C C   . LEU A 21  ? 0.3107 0.2755 0.3215 -0.0122 -0.0250 -0.0195 22  LEU A C   
173  O O   . LEU A 21  ? 0.2907 0.2600 0.3051 -0.0102 -0.0291 -0.0223 22  LEU A O   
174  C CB  . LEU A 21  ? 0.2734 0.2551 0.2945 -0.0180 -0.0123 -0.0176 22  LEU A CB  
175  C CG  . LEU A 21  ? 0.2975 0.2903 0.3253 -0.0189 -0.0079 -0.0184 22  LEU A CG  
176  C CD1 . LEU A 21  ? 0.3017 0.2955 0.3268 -0.0207 -0.0032 -0.0140 22  LEU A CD1 
177  C CD2 . LEU A 21  ? 0.3294 0.3312 0.3655 -0.0188 -0.0073 -0.0231 22  LEU A CD2 
178  N N   . ASN A 22  ? 0.2935 0.2421 0.2897 -0.0143 -0.0247 -0.0157 23  ASN A N   
179  C CA  . ASN A 22  ? 0.3130 0.2455 0.2933 -0.0139 -0.0300 -0.0135 23  ASN A CA  
180  C C   . ASN A 22  ? 0.3767 0.3031 0.3552 -0.0052 -0.0414 -0.0159 23  ASN A C   
181  O O   . ASN A 22  ? 0.3726 0.2956 0.3454 -0.0022 -0.0488 -0.0163 23  ASN A O   
182  C CB  . ASN A 22  ? 0.3526 0.2673 0.3153 -0.0200 -0.0255 -0.0097 23  ASN A CB  
183  C CG  . ASN A 22  ? 0.4406 0.3389 0.3840 -0.0225 -0.0282 -0.0071 23  ASN A CG  
184  O OD1 . ASN A 22  ? 0.4068 0.3116 0.3525 -0.0224 -0.0297 -0.0080 23  ASN A OD1 
185  N ND2 . ASN A 22  ? 0.4678 0.3432 0.3900 -0.0256 -0.0283 -0.0043 23  ASN A ND2 
186  N N   . ARG A 23  ? 0.3444 0.2701 0.3285 -0.0005 -0.0435 -0.0182 24  ARG A N   
187  C CA  . ARG A 23  ? 0.3503 0.2719 0.3365 0.0102  -0.0547 -0.0219 24  ARG A CA  
188  C C   . ARG A 23  ? 0.3788 0.3243 0.3853 0.0145  -0.0588 -0.0290 24  ARG A C   
189  O O   . ARG A 23  ? 0.3784 0.3230 0.3846 0.0223  -0.0699 -0.0319 24  ARG A O   
190  C CB  . ARG A 23  ? 0.3708 0.2889 0.3619 0.0139  -0.0538 -0.0247 24  ARG A CB  
191  C CG  . ARG A 23  ? 0.4711 0.3611 0.4399 0.0106  -0.0517 -0.0194 24  ARG A CG  
192  C CD  . ARG A 23  ? 0.4783 0.3689 0.4541 0.0103  -0.0469 -0.0232 24  ARG A CD  
193  N NE  . ARG A 23  ? 0.6045 0.4662 0.5583 0.0064  -0.0444 -0.0195 24  ARG A NE  
194  C CZ  . ARG A 23  ? 0.8523 0.7092 0.8067 0.0031  -0.0387 -0.0225 24  ARG A CZ  
195  N NH1 . ARG A 23  ? 0.6354 0.5156 0.6107 0.0034  -0.0350 -0.0286 24  ARG A NH1 
196  N NH2 . ARG A 23  ? 0.7161 0.5438 0.6483 -0.0017 -0.0358 -0.0198 24  ARG A NH2 
197  N N   . LEU A 24  ? 0.3175 0.2840 0.3405 0.0087  -0.0500 -0.0322 25  LEU A N   
198  C CA  . LEU A 24  ? 0.3027 0.2910 0.3435 0.0093  -0.0510 -0.0400 25  LEU A CA  
199  C C   . LEU A 24  ? 0.3658 0.3519 0.3987 0.0070  -0.0546 -0.0385 25  LEU A C   
200  O O   . LEU A 24  ? 0.3603 0.3576 0.4020 0.0114  -0.0626 -0.0453 25  LEU A O   
201  C CB  . LEU A 24  ? 0.2917 0.2952 0.3438 0.0016  -0.0392 -0.0419 25  LEU A CB  
202  C CG  . LEU A 24  ? 0.3428 0.3520 0.4032 0.0023  -0.0347 -0.0450 25  LEU A CG  
203  C CD1 . LEU A 24  ? 0.3278 0.3488 0.3936 -0.0060 -0.0237 -0.0457 25  LEU A CD1 
204  C CD2 . LEU A 24  ? 0.3531 0.3721 0.4285 0.0108  -0.0415 -0.0550 25  LEU A CD2 
205  N N   . ARG A 25  ? 0.3243 0.2980 0.3420 0.0000  -0.0486 -0.0310 26  ARG A N   
206  C CA  . ARG A 25  ? 0.3398 0.3093 0.3477 -0.0032 -0.0509 -0.0300 26  ARG A CA  
207  C C   . ARG A 25  ? 0.4087 0.3665 0.4037 0.0043  -0.0650 -0.0300 26  ARG A C   
208  O O   . ARG A 25  ? 0.4073 0.3738 0.4051 0.0056  -0.0718 -0.0350 26  ARG A O   
209  C CB  . ARG A 25  ? 0.3547 0.3118 0.3486 -0.0112 -0.0417 -0.0230 26  ARG A CB  
210  C CG  . ARG A 25  ? 0.4363 0.3887 0.4195 -0.0153 -0.0429 -0.0232 26  ARG A CG  
211  C CD  . ARG A 25  ? 0.4632 0.4063 0.4364 -0.0229 -0.0326 -0.0186 26  ARG A CD  
212  N NE  . ARG A 25  ? 0.4475 0.3729 0.4043 -0.0240 -0.0316 -0.0135 26  ARG A NE  
213  C CZ  . ARG A 25  ? 0.6392 0.5483 0.5757 -0.0289 -0.0306 -0.0110 26  ARG A CZ  
214  N NH1 . ARG A 25  ? 0.5420 0.4501 0.4716 -0.0319 -0.0319 -0.0130 26  ARG A NH1 
215  N NH2 . ARG A 25  ? 0.5003 0.3934 0.4221 -0.0321 -0.0273 -0.0074 26  ARG A NH2 
216  N N   A SER A 26  ? 0.3945 0.3313 0.3736 0.0088  -0.0694 -0.0248 27  SER A N   
217  N N   B SER A 26  ? 0.3920 0.3287 0.3710 0.0088  -0.0694 -0.0248 27  SER A N   
218  N N   C SER A 26  ? 0.3892 0.3259 0.3683 0.0088  -0.0694 -0.0248 27  SER A N   
219  C CA  A SER A 26  ? 0.4316 0.3497 0.3921 0.0170  -0.0835 -0.0228 27  SER A CA  
220  C CA  B SER A 26  ? 0.4272 0.3452 0.3874 0.0169  -0.0835 -0.0228 27  SER A CA  
221  C CA  C SER A 26  ? 0.4220 0.3397 0.3822 0.0170  -0.0834 -0.0227 27  SER A CA  
222  C C   A SER A 26  ? 0.4944 0.4298 0.4726 0.0289  -0.0968 -0.0316 27  SER A C   
223  C C   B SER A 26  ? 0.4937 0.4278 0.4710 0.0293  -0.0971 -0.0313 27  SER A C   
224  C C   C SER A 26  ? 0.4900 0.4233 0.4669 0.0295  -0.0972 -0.0312 27  SER A C   
225  O O   A SER A 26  ? 0.5077 0.4405 0.4774 0.0345  -0.1094 -0.0332 27  SER A O   
226  O O   B SER A 26  ? 0.5103 0.4393 0.4775 0.0358  -0.1105 -0.0323 27  SER A O   
227  O O   C SER A 26  ? 0.5070 0.4340 0.4728 0.0363  -0.1107 -0.0318 27  SER A O   
228  C CB  A SER A 26  ? 0.4997 0.3912 0.4421 0.0196  -0.0839 -0.0167 27  SER A CB  
229  C CB  B SER A 26  ? 0.4909 0.3804 0.4304 0.0183  -0.0832 -0.0158 27  SER A CB  
230  C CB  C SER A 26  ? 0.4804 0.3704 0.4208 0.0183  -0.0827 -0.0159 27  SER A CB  
231  O OG  A SER A 26  ? 0.6133 0.4893 0.5388 0.0082  -0.0723 -0.0102 27  SER A OG  
232  O OG  B SER A 26  ? 0.5757 0.4702 0.5298 0.0246  -0.0833 -0.0191 27  SER A OG  
233  O OG  C SER A 26  ? 0.5936 0.4582 0.5093 0.0260  -0.0959 -0.0122 27  SER A OG  
234  N N   . ARG A 27  ? 0.4321 0.3869 0.4356 0.0324  -0.0938 -0.0386 28  ARG A N   
235  C CA  . ARG A 27  ? 0.4383 0.4141 0.4643 0.0436  -0.1047 -0.0498 28  ARG A CA  
236  C C   . ARG A 27  ? 0.4565 0.4641 0.5058 0.0375  -0.1008 -0.0599 28  ARG A C   
237  O O   . ARG A 27  ? 0.4568 0.4879 0.5291 0.0445  -0.1078 -0.0719 28  ARG A O   
238  C CB  . ARG A 27  ? 0.4647 0.4429 0.5043 0.0498  -0.1025 -0.0534 28  ARG A CB  
239  C CG  . ARG A 27  ? 0.6076 0.5517 0.6227 0.0548  -0.1057 -0.0443 28  ARG A CG  
240  C CD  . ARG A 27  ? 0.7172 0.6631 0.7451 0.0586  -0.1011 -0.0484 28  ARG A CD  
241  N NE  . ARG A 27  ? 0.9517 0.9122 1.0005 0.0734  -0.1125 -0.0596 28  ARG A NE  
242  C CZ  . ARG A 27  ? 1.1636 1.1460 1.2386 0.0751  -0.1070 -0.0702 28  ARG A CZ  
243  N NH1 . ARG A 27  ? 1.0599 1.0572 1.1559 0.0892  -0.1175 -0.0820 28  ARG A NH1 
244  N NH2 . ARG A 27  ? 0.9696 0.9599 1.0501 0.0628  -0.0912 -0.0697 28  ARG A NH2 
245  N N   . ASP A 28  ? 0.3893 0.3970 0.4324 0.0245  -0.0895 -0.0560 29  ASP A N   
246  C CA  . ASP A 28  ? 0.3877 0.4190 0.4472 0.0158  -0.0830 -0.0643 29  ASP A CA  
247  C C   . ASP A 28  ? 0.4199 0.4745 0.5057 0.0131  -0.0741 -0.0738 29  ASP A C   
248  O O   . ASP A 28  ? 0.4094 0.4888 0.5154 0.0108  -0.0740 -0.0862 29  ASP A O   
249  C CB  . ASP A 28  ? 0.4242 0.4667 0.4862 0.0199  -0.0965 -0.0720 29  ASP A CB  
250  C CG  . ASP A 28  ? 0.5276 0.5866 0.5982 0.0076  -0.0883 -0.0788 29  ASP A CG  
251  O OD1 . ASP A 28  ? 0.5268 0.5758 0.5881 -0.0034 -0.0744 -0.0724 29  ASP A OD1 
252  O OD2 . ASP A 28  ? 0.6052 0.6874 0.6922 0.0092  -0.0959 -0.0914 29  ASP A OD2 
253  N N   . ILE A 29  ? 0.3428 0.3900 0.4277 0.0127  -0.0665 -0.0691 30  ILE A N   
254  C CA  . ILE A 29  ? 0.3140 0.3793 0.4186 0.0096  -0.0574 -0.0771 30  ILE A CA  
255  C C   . ILE A 29  ? 0.3496 0.4145 0.4504 -0.0038 -0.0417 -0.0734 30  ILE A C   
256  O O   . ILE A 29  ? 0.3077 0.3547 0.3918 -0.0070 -0.0365 -0.0622 30  ILE A O   
257  C CB  . ILE A 29  ? 0.3519 0.4102 0.4577 0.0173  -0.0589 -0.0759 30  ILE A CB  
258  C CG1 . ILE A 29  ? 0.3643 0.4224 0.4758 0.0327  -0.0751 -0.0813 30  ILE A CG1 
259  C CG2 . ILE A 29  ? 0.3333 0.4079 0.4552 0.0113  -0.0469 -0.0833 30  ILE A CG2 
260  C CD1 . ILE A 29  ? 0.3955 0.4352 0.4993 0.0405  -0.0772 -0.0768 30  ILE A CD1 
261  N N   A LEU A 30  ? 0.3157 0.3998 0.4316 -0.0117 -0.0341 -0.0835 31  LEU A N   
262  N N   B LEU A 30  ? 0.3204 0.4047 0.4364 -0.0116 -0.0342 -0.0836 31  LEU A N   
263  C CA  A LEU A 30  ? 0.3139 0.3958 0.4249 -0.0245 -0.0190 -0.0813 31  LEU A CA  
264  C CA  B LEU A 30  ? 0.3219 0.4044 0.4335 -0.0244 -0.0191 -0.0817 31  LEU A CA  
265  C C   A LEU A 30  ? 0.3560 0.4211 0.4493 -0.0299 -0.0157 -0.0719 31  LEU A C   
266  C C   B LEU A 30  ? 0.3604 0.4257 0.4539 -0.0298 -0.0158 -0.0720 31  LEU A C   
267  O O   A LEU A 30  ? 0.3349 0.3904 0.4189 -0.0373 -0.0047 -0.0664 31  LEU A O   
268  O O   B LEU A 30  ? 0.3423 0.3980 0.4265 -0.0372 -0.0047 -0.0664 31  LEU A O   
269  C CB  A LEU A 30  ? 0.3147 0.3906 0.4213 -0.0262 -0.0107 -0.0765 31  LEU A CB  
270  C CB  B LEU A 30  ? 0.3256 0.4032 0.4337 -0.0263 -0.0107 -0.0776 31  LEU A CB  
271  C CG  A LEU A 30  ? 0.3754 0.4691 0.4996 -0.0254 -0.0081 -0.0880 31  LEU A CG  
272  C CG  B LEU A 30  ? 0.3913 0.4879 0.5156 -0.0323 -0.0023 -0.0902 31  LEU A CG  
273  C CD1 A LEU A 30  ? 0.3635 0.4512 0.4790 -0.0330 0.0041  -0.0842 31  LEU A CD1 
274  C CD1 B LEU A 30  ? 0.3897 0.4950 0.5261 -0.0236 -0.0073 -0.0960 31  LEU A CD1 
275  C CD2 A LEU A 30  ? 0.3928 0.5107 0.5376 -0.0304 -0.0056 -0.1041 31  LEU A CD2 
276  C CD2 B LEU A 30  ? 0.4191 0.5065 0.5307 -0.0436 0.0120  -0.0853 31  LEU A CD2 
277  N N   . THR A 31  ? 0.3165 0.3776 0.4045 -0.0260 -0.0252 -0.0708 32  THR A N   
278  C CA  . THR A 31  ? 0.3209 0.3678 0.3936 -0.0318 -0.0215 -0.0644 32  THR A CA  
279  C C   . THR A 31  ? 0.3836 0.4413 0.4644 -0.0428 -0.0123 -0.0734 32  THR A C   
280  O O   . THR A 31  ? 0.3788 0.4576 0.4771 -0.0443 -0.0142 -0.0861 32  THR A O   
281  C CB  . THR A 31  ? 0.3927 0.4329 0.4558 -0.0264 -0.0336 -0.0626 32  THR A CB  
282  O OG1 . THR A 31  ? 0.4055 0.4643 0.4828 -0.0218 -0.0441 -0.0738 32  THR A OG1 
283  C CG2 . THR A 31  ? 0.3767 0.3991 0.4255 -0.0187 -0.0393 -0.0525 32  THR A CG2 
284  N N   . ASP A 32  ? 0.3513 0.3948 0.4205 -0.0506 -0.0012 -0.0677 33  ASP A N   
285  C CA  . ASP A 32  ? 0.3513 0.3991 0.4242 -0.0626 0.0101  -0.0753 33  ASP A CA  
286  C C   . ASP A 32  ? 0.3791 0.4141 0.4406 -0.0690 0.0145  -0.0738 33  ASP A C   
287  O O   . ASP A 32  ? 0.3736 0.4045 0.4329 -0.0799 0.0260  -0.0781 33  ASP A O   
288  C CB  . ASP A 32  ? 0.3745 0.4146 0.4428 -0.0672 0.0220  -0.0715 33  ASP A CB  
289  C CG  . ASP A 32  ? 0.4996 0.5187 0.5516 -0.0618 0.0235  -0.0568 33  ASP A CG  
290  O OD1 . ASP A 32  ? 0.4643 0.4733 0.5084 -0.0569 0.0187  -0.0503 33  ASP A OD1 
291  O OD2 . ASP A 32  ? 0.6140 0.6279 0.6612 -0.0626 0.0294  -0.0528 33  ASP A OD2 
292  N N   . VAL A 33  ? 0.3209 0.3476 0.3733 -0.0633 0.0065  -0.0684 34  VAL A N   
293  C CA  . VAL A 33  ? 0.3217 0.3364 0.3631 -0.0693 0.0107  -0.0681 34  VAL A CA  
294  C C   . VAL A 33  ? 0.3663 0.3801 0.4009 -0.0643 -0.0009 -0.0672 34  VAL A C   
295  O O   . VAL A 33  ? 0.3587 0.3708 0.3902 -0.0551 -0.0102 -0.0615 34  VAL A O   
296  C CB  . VAL A 33  ? 0.3669 0.3582 0.3944 -0.0705 0.0219  -0.0578 34  VAL A CB  
297  C CG1 . VAL A 33  ? 0.3537 0.3351 0.3733 -0.0610 0.0169  -0.0471 34  VAL A CG1 
298  C CG2 . VAL A 33  ? 0.3763 0.3551 0.3952 -0.0792 0.0305  -0.0607 34  VAL A CG2 
299  N N   A VAL A 34  ? 0.3298 0.3423 0.3593 -0.0714 0.0003  -0.0730 35  VAL A N   
300  N N   B VAL A 34  ? 0.3345 0.3472 0.3641 -0.0713 0.0001  -0.0730 35  VAL A N   
301  C CA  A VAL A 34  ? 0.3308 0.3385 0.3483 -0.0693 -0.0088 -0.0723 35  VAL A CA  
302  C CA  B VAL A 34  ? 0.3379 0.3454 0.3553 -0.0686 -0.0092 -0.0717 35  VAL A CA  
303  C C   A VAL A 34  ? 0.3825 0.3694 0.3852 -0.0748 0.0022  -0.0675 35  VAL A C   
304  C C   B VAL A 34  ? 0.3897 0.3773 0.3923 -0.0748 0.0014  -0.0679 35  VAL A C   
305  O O   A VAL A 34  ? 0.3915 0.3739 0.3952 -0.0834 0.0135  -0.0716 35  VAL A O   
306  O O   B VAL A 34  ? 0.4009 0.3852 0.4047 -0.0837 0.0122  -0.0729 35  VAL A O   
307  C CB  A VAL A 34  ? 0.3827 0.4090 0.4069 -0.0730 -0.0179 -0.0853 35  VAL A CB  
308  C CB  B VAL A 34  ? 0.3927 0.4189 0.4160 -0.0687 -0.0222 -0.0828 35  VAL A CB  
309  C CG1 A VAL A 34  ? 0.3919 0.4097 0.3980 -0.0717 -0.0273 -0.0839 35  VAL A CG1 
310  C CG1 B VAL A 34  ? 0.3979 0.4348 0.4286 -0.0811 -0.0153 -0.0954 35  VAL A CG1 
311  C CG2 A VAL A 34  ? 0.3755 0.4248 0.4180 -0.0657 -0.0292 -0.0918 35  VAL A CG2 
312  C CG2 B VAL A 34  ? 0.4035 0.4193 0.4080 -0.0639 -0.0338 -0.0785 35  VAL A CG2 
313  N N   . ILE A 35  ? 0.3423 0.3157 0.3312 -0.0703 -0.0003 -0.0596 36  ILE A N   
314  C CA  . ILE A 35  ? 0.3412 0.2973 0.3178 -0.0745 0.0094  -0.0569 36  ILE A CA  
315  C C   . ILE A 35  ? 0.4134 0.3680 0.3767 -0.0788 0.0030  -0.0618 36  ILE A C   
316  O O   . ILE A 35  ? 0.4125 0.3669 0.3665 -0.0741 -0.0084 -0.0591 36  ILE A O   
317  C CB  . ILE A 35  ? 0.3614 0.3057 0.3329 -0.0683 0.0129  -0.0470 36  ILE A CB  
318  C CG1 . ILE A 35  ? 0.3531 0.3008 0.3364 -0.0630 0.0163  -0.0420 36  ILE A CG1 
319  C CG2 . ILE A 35  ? 0.3893 0.3188 0.3515 -0.0722 0.0233  -0.0468 36  ILE A CG2 
320  C CD1 . ILE A 35  ? 0.3852 0.3298 0.3743 -0.0673 0.0267  -0.0441 36  ILE A CD1 
321  N N   . VAL A 36  ? 0.3773 0.3285 0.3372 -0.0881 0.0104  -0.0690 37  VAL A N   
322  C CA  . VAL A 36  ? 0.3882 0.3381 0.3339 -0.0941 0.0053  -0.0752 37  VAL A CA  
323  C C   . VAL A 36  ? 0.4637 0.3939 0.3936 -0.0973 0.0151  -0.0720 37  VAL A C   
324  O O   . VAL A 36  ? 0.4437 0.3639 0.3767 -0.1005 0.0289  -0.0726 37  VAL A O   
325  C CB  . VAL A 36  ? 0.4429 0.4052 0.3959 -0.1038 0.0065  -0.0881 37  VAL A CB  
326  C CG1 . VAL A 36  ? 0.4532 0.4153 0.3902 -0.1102 0.0001  -0.0951 37  VAL A CG1 
327  C CG2 . VAL A 36  ? 0.4388 0.4244 0.4108 -0.1008 -0.0023 -0.0934 37  VAL A CG2 
328  N N   . VAL A 37  ? 0.4359 0.3592 0.3475 -0.0965 0.0080  -0.0692 38  VAL A N   
329  C CA  . VAL A 37  ? 0.4505 0.3568 0.3459 -0.1007 0.0172  -0.0677 38  VAL A CA  
330  C C   . VAL A 37  ? 0.5366 0.4395 0.4101 -0.1078 0.0099  -0.0732 38  VAL A C   
331  O O   . VAL A 37  ? 0.5133 0.4142 0.3718 -0.1044 -0.0031 -0.0694 38  VAL A O   
332  C CB  . VAL A 37  ? 0.4933 0.3922 0.3851 -0.0941 0.0176  -0.0582 38  VAL A CB  
333  C CG1 . VAL A 37  ? 0.5043 0.3895 0.3860 -0.0991 0.0307  -0.0590 38  VAL A CG1 
334  C CG2 . VAL A 37  ? 0.4661 0.3727 0.3792 -0.0857 0.0194  -0.0528 38  VAL A CG2 
335  N N   A SER A 38  ? 0.5331 0.4300 0.3995 -0.1178 0.0193  -0.0813 39  SER A N   
336  N N   B SER A 38  ? 0.4965 0.4019 0.3716 -0.1167 0.0157  -0.0831 39  SER A N   
337  C CA  A SER A 38  ? 0.5635 0.4560 0.4060 -0.1260 0.0135  -0.0874 39  SER A CA  
338  C CA  B SER A 38  ? 0.5100 0.4165 0.3691 -0.1257 0.0105  -0.0921 39  SER A CA  
339  C C   A SER A 38  ? 0.6128 0.5180 0.4497 -0.1218 -0.0079 -0.0880 39  SER A C   
340  C C   B SER A 38  ? 0.5420 0.4653 0.4013 -0.1211 -0.0099 -0.0939 39  SER A C   
341  O O   A SER A 38  ? 0.6177 0.5136 0.4296 -0.1209 -0.0185 -0.0844 39  SER A O   
342  O O   B SER A 38  ? 0.5043 0.4457 0.3854 -0.1194 -0.0129 -0.0988 39  SER A O   
343  C CB  A SER A 38  ? 0.6470 0.5206 0.4657 -0.1294 0.0194  -0.0835 39  SER A CB  
344  C CB  B SER A 38  ? 0.5829 0.4710 0.4154 -0.1319 0.0159  -0.0916 39  SER A CB  
345  O OG  A SER A 38  ? 0.7882 0.6529 0.6135 -0.1329 0.0383  -0.0857 39  SER A OG  
346  O OG  B SER A 38  ? 0.6945 0.5725 0.5327 -0.1369 0.0351  -0.0949 39  SER A OG  
347  N N   A ARG A 39  ? 0.5562 0.4818 0.4163 -0.1185 -0.0139 -0.0926 40  ARG A N   
348  N N   B ARG A 39  ? 0.5264 0.4432 0.3619 -0.1185 -0.0237 -0.0904 40  ARG A N   
349  C CA  A ARG A 39  ? 0.5610 0.5051 0.4255 -0.1125 -0.0338 -0.0959 40  ARG A CA  
350  C CA  B ARG A 39  ? 0.5354 0.4676 0.3714 -0.1112 -0.0452 -0.0923 40  ARG A CA  
351  C C   A ARG A 39  ? 0.6054 0.5455 0.4642 -0.0991 -0.0475 -0.0849 40  ARG A C   
352  C C   B ARG A 39  ? 0.5902 0.5292 0.4431 -0.0975 -0.0527 -0.0842 40  ARG A C   
353  O O   A ARG A 39  ? 0.6265 0.5729 0.4770 -0.0925 -0.0665 -0.0858 40  ARG A O   
354  O O   B ARG A 39  ? 0.5925 0.5538 0.4670 -0.0920 -0.0622 -0.0897 40  ARG A O   
355  C CB  A ARG A 39  ? 0.5830 0.5320 0.4301 -0.1196 -0.0442 -0.1057 40  ARG A CB  
356  C CB  B ARG A 39  ? 0.5594 0.4793 0.3601 -0.1125 -0.0591 -0.0915 40  ARG A CB  
357  C CG  A ARG A 39  ? 0.7215 0.6809 0.5793 -0.1327 -0.0339 -0.1197 40  ARG A CG  
358  C CG  B ARG A 39  ? 0.6645 0.5858 0.4521 -0.1259 -0.0561 -0.1032 40  ARG A CG  
359  C CD  A ARG A 39  ? 0.8181 0.7925 0.6662 -0.1371 -0.0498 -0.1312 40  ARG A CD  
360  C CD  B ARG A 39  ? 0.6625 0.5747 0.4143 -0.1265 -0.0735 -0.1034 40  ARG A CD  
361  N NE  A ARG A 39  ? 0.9101 0.8910 0.7629 -0.1524 -0.0387 -0.1456 40  ARG A NE  
362  N NE  B ARG A 39  ? 0.6776 0.5898 0.4147 -0.1409 -0.0689 -0.1149 40  ARG A NE  
363  C CZ  A ARG A 39  ? 1.0885 1.0526 0.9193 -0.1639 -0.0290 -0.1494 40  ARG A CZ  
364  C CZ  B ARG A 39  ? 0.8423 0.7773 0.5880 -0.1448 -0.0790 -0.1282 40  ARG A CZ  
365  N NH1 A ARG A 39  ? 0.9062 0.8470 0.7089 -0.1625 -0.0282 -0.1401 40  ARG A NH1 
366  N NH1 B ARG A 39  ? 0.6644 0.6264 0.4358 -0.1351 -0.0939 -0.1326 40  ARG A NH1 
367  N NH2 A ARG A 39  ? 0.9340 0.9039 0.7702 -0.1780 -0.0188 -0.1635 40  ARG A NH2 
368  N NH2 B ARG A 39  ? 0.7333 0.6658 0.4631 -0.1591 -0.0733 -0.1388 40  ARG A NH2 
369  N N   A GLU A 40  ? 0.5161 0.4450 0.3790 -0.0947 -0.0382 -0.0751 41  GLU A N   
370  N N   B GLU A 40  ? 0.5142 0.4360 0.3602 -0.0935 -0.0461 -0.0730 41  GLU A N   
371  C CA  A GLU A 40  ? 0.5057 0.4297 0.3664 -0.0833 -0.0473 -0.0653 41  GLU A CA  
372  C CA  B GLU A 40  ? 0.4932 0.4174 0.3507 -0.0816 -0.0520 -0.0650 41  GLU A CA  
373  C C   A GLU A 40  ? 0.4980 0.4365 0.3895 -0.0783 -0.0413 -0.0647 41  GLU A C   
374  C C   B GLU A 40  ? 0.4863 0.4276 0.3770 -0.0790 -0.0440 -0.0670 41  GLU A C   
375  O O   A GLU A 40  ? 0.4550 0.3924 0.3578 -0.0833 -0.0257 -0.0653 41  GLU A O   
376  O O   B GLU A 40  ? 0.4413 0.3839 0.3428 -0.0861 -0.0291 -0.0705 41  GLU A O   
377  C CB  A GLU A 40  ? 0.5372 0.4361 0.3745 -0.0851 -0.0402 -0.0560 41  GLU A CB  
378  C CB  B GLU A 40  ? 0.5216 0.4221 0.3600 -0.0804 -0.0464 -0.0540 41  GLU A CB  
379  C CG  A GLU A 40  ? 0.7363 0.6177 0.5380 -0.0911 -0.0461 -0.0561 41  GLU A CG  
380  C CG  B GLU A 40  ? 0.7405 0.6192 0.5424 -0.0878 -0.0474 -0.0526 41  GLU A CG  
381  C CD  A GLU A 40  ? 1.1923 1.0557 0.9675 -0.0844 -0.0598 -0.0473 41  GLU A CD  
382  C CD  B GLU A 40  ? 1.2351 1.0962 1.0076 -0.0818 -0.0634 -0.0454 41  GLU A CD  
383  O OE1 A GLU A 40  ? 1.2623 1.1021 1.0116 -0.0902 -0.0523 -0.0417 41  GLU A OE1 
384  O OE1 B GLU A 40  ? 1.2555 1.1263 1.0335 -0.0709 -0.0813 -0.0455 41  GLU A OE1 
385  O OE2 A GLU A 40  ? 1.1938 1.0656 0.9735 -0.0734 -0.0776 -0.0466 41  GLU A OE2 
386  O OE2 B GLU A 40  ? 1.2858 1.1222 1.0284 -0.0882 -0.0577 -0.0402 41  GLU A OE2 
387  N N   . GLN A 41  ? 0.4454 0.3971 0.3497 -0.0684 -0.0540 -0.0645 42  GLN A N   
388  C CA  . GLN A 41  ? 0.4233 0.3906 0.3556 -0.0651 -0.0488 -0.0659 42  GLN A CA  
389  C C   . GLN A 41  ? 0.4678 0.4277 0.4016 -0.0559 -0.0501 -0.0562 42  GLN A C   
390  O O   . GLN A 41  ? 0.4893 0.4411 0.4098 -0.0484 -0.0625 -0.0516 42  GLN A O   
391  C CB  . GLN A 41  ? 0.4423 0.4356 0.3933 -0.0623 -0.0604 -0.0770 42  GLN A CB  
392  C CG  . GLN A 41  ? 0.6220 0.6268 0.5771 -0.0737 -0.0563 -0.0891 42  GLN A CG  
393  C CD  . GLN A 41  ? 0.8758 0.9109 0.8544 -0.0731 -0.0650 -0.1028 42  GLN A CD  
394  O OE1 . GLN A 41  ? 0.7830 0.8331 0.7799 -0.0643 -0.0717 -0.1042 42  GLN A OE1 
395  N NE2 . GLN A 41  ? 0.9132 0.9592 0.8930 -0.0834 -0.0642 -0.1147 42  GLN A NE2 
396  N N   . PHE A 42  ? 0.3761 0.3370 0.3240 -0.0566 -0.0375 -0.0530 43  PHE A N   
397  C CA  . PHE A 42  ? 0.3702 0.3257 0.3208 -0.0494 -0.0372 -0.0448 43  PHE A CA  
398  C C   . PHE A 42  ? 0.4075 0.3795 0.3822 -0.0470 -0.0337 -0.0477 43  PHE A C   
399  O O   . PHE A 42  ? 0.4005 0.3756 0.3840 -0.0529 -0.0222 -0.0499 43  PHE A O   
400  C CB  . PHE A 42  ? 0.3960 0.3352 0.3367 -0.0533 -0.0246 -0.0381 43  PHE A CB  
401  C CG  . PHE A 42  ? 0.4373 0.3595 0.3531 -0.0582 -0.0247 -0.0364 43  PHE A CG  
402  C CD1 . PHE A 42  ? 0.4602 0.3791 0.3691 -0.0667 -0.0178 -0.0414 43  PHE A CD1 
403  C CD2 . PHE A 42  ? 0.4738 0.3807 0.3708 -0.0555 -0.0303 -0.0302 43  PHE A CD2 
404  C CE1 . PHE A 42  ? 0.5027 0.4055 0.3867 -0.0725 -0.0170 -0.0407 43  PHE A CE1 
405  C CE2 . PHE A 42  ? 0.5296 0.4184 0.3999 -0.0619 -0.0290 -0.0290 43  PHE A CE2 
406  C CZ  . PHE A 42  ? 0.5058 0.3936 0.3700 -0.0704 -0.0223 -0.0344 43  PHE A CZ  
407  N N   . ARG A 43  ? 0.3598 0.3401 0.3433 -0.0385 -0.0431 -0.0479 44  ARG A N   
408  C CA  . ARG A 43  ? 0.3332 0.3292 0.3385 -0.0369 -0.0391 -0.0514 44  ARG A CA  
409  C C   . ARG A 43  ? 0.3838 0.3700 0.3878 -0.0349 -0.0314 -0.0426 44  ARG A C   
410  O O   . ARG A 43  ? 0.3799 0.3524 0.3710 -0.0312 -0.0344 -0.0358 44  ARG A O   
411  C CB  . ARG A 43  ? 0.3519 0.3643 0.3702 -0.0285 -0.0525 -0.0582 44  ARG A CB  
412  C CG  . ARG A 43  ? 0.4549 0.4841 0.4800 -0.0301 -0.0611 -0.0697 44  ARG A CG  
413  C CD  . ARG A 43  ? 0.5587 0.6143 0.6092 -0.0247 -0.0680 -0.0812 44  ARG A CD  
414  N NE  . ARG A 43  ? 0.7018 0.7660 0.7683 -0.0302 -0.0540 -0.0834 44  ARG A NE  
415  C CZ  . ARG A 43  ? 0.8581 0.9366 0.9380 -0.0409 -0.0435 -0.0926 44  ARG A CZ  
416  N NH1 . ARG A 43  ? 0.7664 0.8569 0.8501 -0.0474 -0.0456 -0.1027 44  ARG A NH1 
417  N NH2 . ARG A 43  ? 0.6320 0.7123 0.7199 -0.0459 -0.0307 -0.0926 44  ARG A NH2 
418  N N   . ALA A 44  ? 0.3281 0.3200 0.3432 -0.0382 -0.0211 -0.0431 45  ALA A N   
419  C CA  . ALA A 44  ? 0.3306 0.3155 0.3447 -0.0359 -0.0151 -0.0356 45  ALA A CA  
420  C C   . ALA A 44  ? 0.3361 0.3307 0.3628 -0.0376 -0.0085 -0.0380 45  ALA A C   
421  O O   . ALA A 44  ? 0.3265 0.3326 0.3628 -0.0418 -0.0069 -0.0459 45  ALA A O   
422  C CB  . ALA A 44  ? 0.3435 0.3144 0.3466 -0.0395 -0.0067 -0.0301 45  ALA A CB  
423  N N   . HIS A 45  ? 0.2967 0.2866 0.3221 -0.0355 -0.0040 -0.0318 46  HIS A N   
424  C CA  . HIS A 45  ? 0.2789 0.2735 0.3103 -0.0375 0.0029  -0.0322 46  HIS A CA  
425  C C   . HIS A 45  ? 0.3305 0.3126 0.3534 -0.0405 0.0118  -0.0270 46  HIS A C   
426  O O   . HIS A 45  ? 0.3190 0.2927 0.3356 -0.0372 0.0121  -0.0211 46  HIS A O   
427  C CB  . HIS A 45  ? 0.2716 0.2687 0.3052 -0.0324 0.0005  -0.0290 46  HIS A CB  
428  C CG  . HIS A 45  ? 0.3161 0.3212 0.3567 -0.0275 -0.0085 -0.0335 46  HIS A CG  
429  N ND1 . HIS A 45  ? 0.3438 0.3408 0.3773 -0.0226 -0.0156 -0.0301 46  HIS A ND1 
430  C CD2 . HIS A 45  ? 0.3196 0.3388 0.3731 -0.0267 -0.0111 -0.0420 46  HIS A CD2 
431  C CE1 . HIS A 45  ? 0.3346 0.3383 0.3753 -0.0175 -0.0234 -0.0353 46  HIS A CE1 
432  N NE2 . HIS A 45  ? 0.3197 0.3390 0.3746 -0.0191 -0.0213 -0.0432 46  HIS A NE2 
433  N N   . LYS A 46  ? 0.3020 0.2823 0.3247 -0.0468 0.0193  -0.0301 47  LYS A N   
434  C CA  . LYS A 46  ? 0.3197 0.2841 0.3324 -0.0486 0.0278  -0.0251 47  LYS A CA  
435  C C   . LYS A 46  ? 0.3522 0.3108 0.3601 -0.0417 0.0275  -0.0168 47  LYS A C   
436  O O   . LYS A 46  ? 0.3287 0.2775 0.3314 -0.0379 0.0290  -0.0122 47  LYS A O   
437  C CB  . LYS A 46  ? 0.3540 0.3145 0.3642 -0.0571 0.0367  -0.0290 47  LYS A CB  
438  C CG  . LYS A 46  ? 0.3632 0.3277 0.3772 -0.0656 0.0393  -0.0383 47  LYS A CG  
439  C CD  . LYS A 46  ? 0.3807 0.3416 0.3922 -0.0764 0.0501  -0.0437 47  LYS A CD  
440  C CE  . LYS A 46  ? 0.4389 0.4109 0.4588 -0.0859 0.0518  -0.0560 47  LYS A CE  
441  N NZ  . LYS A 46  ? 0.4560 0.4240 0.4730 -0.0993 0.0646  -0.0631 47  LYS A NZ  
442  N N   . THR A 47  ? 0.3134 0.2799 0.3243 -0.0399 0.0253  -0.0160 48  THR A N   
443  C CA  . THR A 47  ? 0.3193 0.2823 0.3255 -0.0338 0.0241  -0.0091 48  THR A CA  
444  C C   . THR A 47  ? 0.3268 0.2924 0.3359 -0.0279 0.0191  -0.0066 48  THR A C   
445  O O   . THR A 47  ? 0.3100 0.2709 0.3159 -0.0230 0.0195  -0.0022 48  THR A O   
446  C CB  . THR A 47  ? 0.3923 0.3631 0.3995 -0.0343 0.0233  -0.0098 48  THR A CB  
447  O OG1 . THR A 47  ? 0.3839 0.3679 0.4019 -0.0341 0.0181  -0.0152 48  THR A OG1 
448  C CG2 . THR A 47  ? 0.4259 0.3907 0.4260 -0.0415 0.0311  -0.0117 48  THR A CG2 
449  N N   . VAL A 48  ? 0.2849 0.2571 0.2991 -0.0284 0.0144  -0.0099 49  VAL A N   
450  C CA  . VAL A 48  ? 0.2808 0.2529 0.2949 -0.0255 0.0115  -0.0084 49  VAL A CA  
451  C C   . VAL A 48  ? 0.3148 0.2783 0.3252 -0.0259 0.0157  -0.0078 49  VAL A C   
452  O O   . VAL A 48  ? 0.3031 0.2665 0.3144 -0.0227 0.0169  -0.0062 49  VAL A O   
453  C CB  . VAL A 48  ? 0.3149 0.2897 0.3297 -0.0263 0.0057  -0.0112 49  VAL A CB  
454  C CG1 . VAL A 48  ? 0.3141 0.2843 0.3243 -0.0263 0.0052  -0.0099 49  VAL A CG1 
455  C CG2 . VAL A 48  ? 0.3125 0.2950 0.3322 -0.0247 0.0021  -0.0126 49  VAL A CG2 
456  N N   . LEU A 49  ? 0.2898 0.2479 0.2974 -0.0301 0.0181  -0.0105 50  LEU A N   
457  C CA  . LEU A 49  ? 0.2944 0.2432 0.2980 -0.0312 0.0232  -0.0112 50  LEU A CA  
458  C C   . LEU A 49  ? 0.3307 0.2728 0.3338 -0.0261 0.0277  -0.0075 50  LEU A C   
459  O O   . LEU A 49  ? 0.3231 0.2630 0.3276 -0.0225 0.0298  -0.0075 50  LEU A O   
460  C CB  . LEU A 49  ? 0.2980 0.2425 0.2986 -0.0377 0.0255  -0.0157 50  LEU A CB  
461  C CG  . LEU A 49  ? 0.3247 0.2758 0.3250 -0.0413 0.0191  -0.0202 50  LEU A CG  
462  C CD1 . LEU A 49  ? 0.3308 0.2806 0.3299 -0.0481 0.0215  -0.0263 50  LEU A CD1 
463  C CD2 . LEU A 49  ? 0.3357 0.2834 0.3296 -0.0407 0.0162  -0.0194 50  LEU A CD2 
464  N N   . MET A 50  ? 0.2970 0.2359 0.2975 -0.0252 0.0288  -0.0048 51  MET A N   
465  C CA  . MET A 50  ? 0.3146 0.2432 0.3103 -0.0187 0.0313  0.0000  51  MET A CA  
466  C C   . MET A 50  ? 0.3483 0.2865 0.3498 -0.0105 0.0263  0.0024  51  MET A C   
467  O O   . MET A 50  ? 0.3543 0.2885 0.3571 -0.0032 0.0269  0.0036  51  MET A O   
468  C CB  . MET A 50  ? 0.3492 0.2699 0.3360 -0.0211 0.0335  0.0029  51  MET A CB  
469  C CG  . MET A 50  ? 0.3984 0.3098 0.3800 -0.0306 0.0403  -0.0011 51  MET A CG  
470  S SD  . MET A 50  ? 0.4554 0.3626 0.4279 -0.0366 0.0439  0.0000  51  MET A SD  
471  C CE  . MET A 50  ? 0.4267 0.3059 0.3802 -0.0307 0.0482  0.0083  51  MET A CE  
472  N N   . ALA A 51  ? 0.3033 0.2553 0.3097 -0.0115 0.0214  0.0018  52  ALA A N   
473  C CA  . ALA A 51  ? 0.3004 0.2641 0.3131 -0.0058 0.0169  0.0024  52  ALA A CA  
474  C C   . ALA A 51  ? 0.3413 0.3108 0.3621 -0.0046 0.0182  -0.0016 52  ALA A C   
475  O O   . ALA A 51  ? 0.3237 0.3033 0.3519 0.0009  0.0160  -0.0028 52  ALA A O   
476  C CB  . ALA A 51  ? 0.2969 0.2715 0.3119 -0.0093 0.0130  0.0013  52  ALA A CB  
477  N N   . CYS A 52  ? 0.3090 0.2733 0.3281 -0.0105 0.0219  -0.0047 53  CYS A N   
478  C CA  . CYS A 52  ? 0.3114 0.2791 0.3346 -0.0126 0.0251  -0.0094 53  CYS A CA  
479  C C   . CYS A 52  ? 0.3411 0.3007 0.3649 -0.0107 0.0310  -0.0120 53  CYS A C   
480  O O   . CYS A 52  ? 0.3275 0.2921 0.3566 -0.0118 0.0349  -0.0172 53  CYS A O   
481  C CB  . CYS A 52  ? 0.3191 0.2846 0.3359 -0.0211 0.0245  -0.0113 53  CYS A CB  
482  S SG  . CYS A 52  ? 0.3512 0.3243 0.3681 -0.0227 0.0184  -0.0100 53  CYS A SG  
483  N N   . SER A 53  ? 0.3116 0.2579 0.3288 -0.0103 0.0333  -0.0097 54  SER A N   
484  C CA  . SER A 53  ? 0.2951 0.2303 0.3106 -0.0103 0.0400  -0.0130 54  SER A CA  
485  C C   . SER A 53  ? 0.3653 0.2864 0.3772 -0.0031 0.0417  -0.0094 54  SER A C   
486  O O   . SER A 53  ? 0.3543 0.2669 0.3576 -0.0051 0.0408  -0.0052 54  SER A O   
487  C CB  . SER A 53  ? 0.3147 0.2433 0.3214 -0.0209 0.0422  -0.0155 54  SER A CB  
488  O OG  . SER A 53  ? 0.3823 0.2969 0.3837 -0.0231 0.0485  -0.0180 54  SER A OG  
489  N N   . GLY A 54  ? 0.3536 0.2709 0.3711 0.0051  0.0448  -0.0119 55  GLY A N   
490  C CA  . GLY A 54  ? 0.3683 0.2665 0.3795 0.0136  0.0465  -0.0083 55  GLY A CA  
491  C C   . GLY A 54  ? 0.4176 0.2954 0.4159 0.0049  0.0536  -0.0088 55  GLY A C   
492  O O   . GLY A 54  ? 0.4138 0.2726 0.4000 0.0062  0.0551  -0.0038 55  GLY A O   
493  N N   . LEU A 55  ? 0.3744 0.2556 0.3732 -0.0056 0.0582  -0.0151 56  LEU A N   
494  C CA  . LEU A 55  ? 0.3764 0.2420 0.3643 -0.0156 0.0646  -0.0176 56  LEU A CA  
495  C C   . LEU A 55  ? 0.4003 0.2666 0.3814 -0.0231 0.0618  -0.0143 56  LEU A C   
496  O O   . LEU A 55  ? 0.3965 0.2457 0.3676 -0.0263 0.0666  -0.0130 56  LEU A O   
497  C CB  . LEU A 55  ? 0.3694 0.2400 0.3578 -0.0250 0.0684  -0.0255 56  LEU A CB  
498  C CG  . LEU A 55  ? 0.4416 0.2976 0.4198 -0.0355 0.0752  -0.0302 56  LEU A CG  
499  C CD1 . LEU A 55  ? 0.4725 0.3054 0.4465 -0.0307 0.0840  -0.0318 56  LEU A CD1 
500  C CD2 . LEU A 55  ? 0.4492 0.3130 0.4249 -0.0456 0.0757  -0.0371 56  LEU A CD2 
501  N N   . PHE A 56  ? 0.3445 0.2295 0.3307 -0.0259 0.0549  -0.0137 57  PHE A N   
502  C CA  . PHE A 56  ? 0.3309 0.2200 0.3141 -0.0321 0.0523  -0.0125 57  PHE A CA  
503  C C   . PHE A 56  ? 0.3942 0.2752 0.3720 -0.0271 0.0521  -0.0060 57  PHE A C   
504  O O   . PHE A 56  ? 0.3866 0.2608 0.3574 -0.0339 0.0555  -0.0062 57  PHE A O   
505  C CB  . PHE A 56  ? 0.3279 0.2363 0.3175 -0.0349 0.0449  -0.0139 57  PHE A CB  
506  C CG  . PHE A 56  ? 0.3393 0.2511 0.3277 -0.0420 0.0445  -0.0200 57  PHE A CG  
507  C CD1 . PHE A 56  ? 0.3738 0.2812 0.3580 -0.0506 0.0478  -0.0255 57  PHE A CD1 
508  C CD2 . PHE A 56  ? 0.3589 0.2782 0.3485 -0.0412 0.0407  -0.0208 57  PHE A CD2 
509  C CE1 . PHE A 56  ? 0.3897 0.3006 0.3709 -0.0568 0.0459  -0.0312 57  PHE A CE1 
510  C CE2 . PHE A 56  ? 0.3934 0.3128 0.3770 -0.0479 0.0394  -0.0256 57  PHE A CE2 
511  C CZ  . PHE A 56  ? 0.3669 0.2826 0.3463 -0.0550 0.0414  -0.0306 57  PHE A CZ  
512  N N   . TYR A 57  ? 0.3768 0.2582 0.3568 -0.0157 0.0484  -0.0011 58  TYR A N   
513  C CA  . TYR A 57  ? 0.3922 0.2625 0.3627 -0.0098 0.0471  0.0059  58  TYR A CA  
514  C C   . TYR A 57  ? 0.4627 0.3041 0.4173 -0.0121 0.0554  0.0076  58  TYR A C   
515  O O   . TYR A 57  ? 0.4509 0.2803 0.3923 -0.0175 0.0585  0.0106  58  TYR A O   
516  C CB  . TYR A 57  ? 0.4121 0.2886 0.3886 0.0041  0.0406  0.0094  58  TYR A CB  
517  C CG  . TYR A 57  ? 0.4692 0.3318 0.4324 0.0120  0.0375  0.0172  58  TYR A CG  
518  C CD1 . TYR A 57  ? 0.4866 0.3545 0.4434 0.0082  0.0343  0.0207  58  TYR A CD1 
519  C CD2 . TYR A 57  ? 0.5362 0.3789 0.4916 0.0236  0.0375  0.0210  58  TYR A CD2 
520  C CE1 . TYR A 57  ? 0.5235 0.3761 0.4634 0.0145  0.0314  0.0283  58  TYR A CE1 
521  C CE2 . TYR A 57  ? 0.5911 0.4171 0.5295 0.0316  0.0333  0.0294  58  TYR A CE2 
522  C CZ  . TYR A 57  ? 0.6746 0.5056 0.6042 0.0265  0.0302  0.0332  58  TYR A CZ  
523  O OH  . TYR A 57  ? 0.7795 0.5921 0.6885 0.0338  0.0259  0.0416  58  TYR A OH  
524  N N   A SER A 58  ? 0.4396 0.2685 0.3943 -0.0091 0.0602  0.0048  59  SER A N   
525  N N   B SER A 58  ? 0.4415 0.2706 0.3964 -0.0091 0.0601  0.0048  59  SER A N   
526  C CA  A SER A 58  ? 0.4666 0.2645 0.4054 -0.0113 0.0691  0.0056  59  SER A CA  
527  C CA  B SER A 58  ? 0.4698 0.2683 0.4091 -0.0112 0.0690  0.0054  59  SER A CA  
528  C C   A SER A 58  ? 0.5318 0.3255 0.4642 -0.0288 0.0771  0.0001  59  SER A C   
529  C C   B SER A 58  ? 0.5295 0.3239 0.4622 -0.0287 0.0767  0.0003  59  SER A C   
530  O O   A SER A 58  ? 0.5641 0.3346 0.4795 -0.0345 0.0840  0.0024  59  SER A O   
531  O O   B SER A 58  ? 0.5564 0.3289 0.4722 -0.0342 0.0830  0.0030  59  SER A O   
532  C CB  A SER A 58  ? 0.5026 0.2910 0.4460 -0.0041 0.0726  0.0019  59  SER A CB  
533  C CB  B SER A 58  ? 0.5131 0.3038 0.4579 -0.0053 0.0728  0.0009  59  SER A CB  
534  O OG  A SER A 58  ? 0.5275 0.3193 0.4776 0.0130  0.0655  0.0058  59  SER A OG  
535  O OG  B SER A 58  ? 0.6119 0.3696 0.5406 -0.0068 0.0818  0.0013  59  SER A OG  
536  N N   . ILE A 59  ? 0.4650 0.2809 0.4101 -0.0375 0.0758  -0.0075 60  ILE A N   
537  C CA  . ILE A 59  ? 0.4576 0.2770 0.4014 -0.0533 0.0812  -0.0151 60  ILE A CA  
538  C C   . ILE A 59  ? 0.4919 0.3166 0.4324 -0.0596 0.0810  -0.0137 60  ILE A C   
539  O O   . ILE A 59  ? 0.5117 0.3230 0.4421 -0.0707 0.0900  -0.0170 60  ILE A O   
540  C CB  . ILE A 59  ? 0.4645 0.3082 0.4217 -0.0584 0.0764  -0.0229 60  ILE A CB  
541  C CG1 . ILE A 59  ? 0.4704 0.3067 0.4277 -0.0569 0.0798  -0.0268 60  ILE A CG1 
542  C CG2 . ILE A 59  ? 0.4401 0.2956 0.4001 -0.0724 0.0778  -0.0313 60  ILE A CG2 
543  C CD1 . ILE A 59  ? 0.4876 0.3452 0.4535 -0.0597 0.0735  -0.0321 60  ILE A CD1 
544  N N   . PHE A 60  ? 0.4247 0.2689 0.3735 -0.0538 0.0721  -0.0102 61  PHE A N   
545  C CA  . PHE A 60  ? 0.4196 0.2719 0.3674 -0.0608 0.0728  -0.0113 61  PHE A CA  
546  C C   . PHE A 60  ? 0.4860 0.3168 0.4154 -0.0583 0.0764  -0.0030 61  PHE A C   
547  O O   . PHE A 60  ? 0.4923 0.3269 0.4180 -0.0659 0.0793  -0.0045 61  PHE A O   
548  C CB  . PHE A 60  ? 0.4020 0.2837 0.3660 -0.0579 0.0628  -0.0132 61  PHE A CB  
549  C CG  . PHE A 60  ? 0.3928 0.2912 0.3694 -0.0613 0.0588  -0.0210 61  PHE A CG  
550  C CD1 . PHE A 60  ? 0.4366 0.3395 0.4160 -0.0730 0.0632  -0.0306 61  PHE A CD1 
551  C CD2 . PHE A 60  ? 0.4014 0.3105 0.3854 -0.0537 0.0507  -0.0192 61  PHE A CD2 
552  C CE1 . PHE A 60  ? 0.4360 0.3537 0.4244 -0.0750 0.0575  -0.0374 61  PHE A CE1 
553  C CE2 . PHE A 60  ? 0.4324 0.3528 0.4226 -0.0569 0.0464  -0.0253 61  PHE A CE2 
554  C CZ  . PHE A 60  ? 0.4089 0.3332 0.4007 -0.0667 0.0489  -0.0339 61  PHE A CZ  
555  N N   . THR A 61  ? 0.4681 0.2749 0.3847 -0.0481 0.0768  0.0048  62  THR A N   
556  C CA  . THR A 61  ? 0.4973 0.2772 0.3905 -0.0457 0.0800  0.0134  62  THR A CA  
557  C C   . THR A 61  ? 0.6032 0.3494 0.4767 -0.0550 0.0929  0.0122  62  THR A C   
558  O O   . THR A 61  ? 0.6284 0.3447 0.4765 -0.0563 0.0982  0.0189  62  THR A O   
559  C CB  . THR A 61  ? 0.5874 0.3609 0.4763 -0.0272 0.0705  0.0231  62  THR A CB  
560  O OG1 . THR A 61  ? 0.5509 0.3205 0.4480 -0.0180 0.0691  0.0220  62  THR A OG1 
561  C CG2 . THR A 61  ? 0.5249 0.3276 0.4273 -0.0212 0.0596  0.0244  62  THR A CG2 
562  N N   . ASP A 62  ? 0.5516 0.3013 0.4346 -0.0628 0.0984  0.0033  63  ASP A N   
563  C CA  . ASP A 62  ? 0.5895 0.3089 0.4554 -0.0743 0.1120  -0.0002 63  ASP A CA  
564  C C   . ASP A 62  ? 0.6716 0.3969 0.5339 -0.0936 0.1210  -0.0075 63  ASP A C   
565  O O   . ASP A 62  ? 0.6308 0.3905 0.5145 -0.1005 0.1177  -0.0167 63  ASP A O   
566  C CB  . ASP A 62  ? 0.6003 0.3240 0.4781 -0.0770 0.1147  -0.0087 63  ASP A CB  
567  C CG  . ASP A 62  ? 0.8166 0.5120 0.6782 -0.0921 0.1299  -0.0147 63  ASP A CG  
568  O OD1 . ASP A 62  ? 0.8997 0.5578 0.7420 -0.0865 0.1355  -0.0091 63  ASP A OD1 
569  O OD2 . ASP A 62  ? 0.8476 0.5575 0.7153 -0.1096 0.1361  -0.0255 63  ASP A OD2 
570  N N   . GLN A 63  ? 0.7081 0.3988 0.5429 -0.1025 0.1326  -0.0042 64  GLN A N   
571  C CA  . GLN A 63  ? 0.7331 0.4244 0.5604 -0.1226 0.1442  -0.0117 64  GLN A CA  
572  C C   . GLN A 63  ? 0.7790 0.4962 0.6271 -0.1399 0.1507  -0.0290 64  GLN A C   
573  O O   . GLN A 63  ? 0.7992 0.5383 0.6565 -0.1527 0.1547  -0.0381 64  GLN A O   
574  C CB  . GLN A 63  ? 0.8118 0.4526 0.6002 -0.1302 0.1577  -0.0050 64  GLN A CB  
575  C CG  . GLN A 63  ? 1.1060 0.7249 0.8709 -0.1160 0.1507  0.0110  64  GLN A CG  
576  N N   . LEU A 64  ? 0.6898 0.4060 0.5458 -0.1403 0.1516  -0.0346 65  LEU A N   
577  C CA  . LEU A 64  ? 0.6614 0.4046 0.5373 -0.1556 0.1554  -0.0516 65  LEU A CA  
578  C C   . LEU A 64  ? 0.6739 0.4599 0.5794 -0.1462 0.1396  -0.0555 65  LEU A C   
579  O O   . LEU A 64  ? 0.6818 0.5005 0.6067 -0.1551 0.1374  -0.0677 65  LEU A O   
580  C CB  . LEU A 64  ? 0.6843 0.4039 0.5512 -0.1633 0.1652  -0.0573 65  LEU A CB  
581  C CG  . LEU A 64  ? 0.7959 0.4784 0.6374 -0.1817 0.1847  -0.0613 65  LEU A CG  
582  C CD1 . LEU A 64  ? 0.8109 0.4706 0.6452 -0.1860 0.1923  -0.0662 65  LEU A CD1 
583  C CD2 . LEU A 64  ? 0.8412 0.5474 0.6926 -0.2043 0.1940  -0.0771 65  LEU A CD2 
584  N N   . LYS A 65  ? 0.5757 0.3608 0.4843 -0.1287 0.1289  -0.0464 66  LYS A N   
585  C CA  . LYS A 65  ? 0.5367 0.3555 0.4678 -0.1208 0.1152  -0.0495 66  LYS A CA  
586  C C   . LYS A 65  ? 0.5820 0.4274 0.5261 -0.1143 0.1049  -0.0469 66  LYS A C   
587  O O   . LYS A 65  ? 0.5485 0.4231 0.5109 -0.1126 0.0953  -0.0528 66  LYS A O   
588  C CB  . LYS A 65  ? 0.5471 0.3563 0.4770 -0.1069 0.1097  -0.0426 66  LYS A CB  
589  C CG  . LYS A 65  ? 0.5384 0.3226 0.4575 -0.1125 0.1198  -0.0468 66  LYS A CG  
590  C CD  . LYS A 65  ? 0.5176 0.3008 0.4409 -0.0992 0.1137  -0.0430 66  LYS A CD  
591  C CE  . LYS A 65  ? 0.5940 0.3485 0.5056 -0.1023 0.1245  -0.0464 66  LYS A CE  
592  N NZ  . LYS A 65  ? 0.6526 0.3696 0.5453 -0.0957 0.1316  -0.0374 66  LYS A NZ  
593  N N   . CYS A 66  ? 0.5844 0.4181 0.5173 -0.1106 0.1065  -0.0383 67  CYS A N   
594  C CA  . CYS A 66  ? 0.5790 0.4355 0.5224 -0.1051 0.0981  -0.0363 67  CYS A CA  
595  C C   . CYS A 66  ? 0.6262 0.5133 0.5883 -0.1160 0.0980  -0.0501 67  CYS A C   
596  O O   . CYS A 66  ? 0.6145 0.5261 0.5916 -0.1098 0.0885  -0.0511 67  CYS A O   
597  C CB  . CYS A 66  ? 0.6156 0.4516 0.5398 -0.1026 0.1019  -0.0264 67  CYS A CB  
598  S SG  . CYS A 66  ? 0.7082 0.5234 0.6128 -0.1229 0.1200  -0.0321 67  CYS A SG  
599  N N   . ASN A 67  ? 0.5822 0.4678 0.5440 -0.1321 0.1088  -0.0616 68  ASN A N   
600  C CA  . ASN A 67  ? 0.5811 0.4966 0.5621 -0.1441 0.1105  -0.0779 68  ASN A CA  
601  C C   . ASN A 67  ? 0.6046 0.5451 0.6048 -0.1443 0.1018  -0.0886 68  ASN A C   
602  O O   . ASN A 67  ? 0.5878 0.5573 0.6072 -0.1519 0.1004  -0.1033 68  ASN A O   
603  C CB  . ASN A 67  ? 0.6174 0.5179 0.5864 -0.1638 0.1288  -0.0861 68  ASN A CB  
604  C CG  . ASN A 67  ? 0.8406 0.7224 0.7911 -0.1656 0.1364  -0.0780 68  ASN A CG  
605  O OD1 . ASN A 67  ? 0.8632 0.7111 0.7879 -0.1754 0.1504  -0.0743 68  ASN A OD1 
606  N ND2 . ASN A 67  ? 0.6874 0.5880 0.6479 -0.1560 0.1274  -0.0746 68  ASN A ND2 
607  N N   . LEU A 68  ? 0.5444 0.4750 0.5397 -0.1356 0.0955  -0.0821 69  LEU A N   
608  C CA  . LEU A 68  ? 0.5196 0.4698 0.5275 -0.1357 0.0866  -0.0909 69  LEU A CA  
609  C C   . LEU A 68  ? 0.5153 0.4913 0.5386 -0.1228 0.0697  -0.0896 69  LEU A C   
610  O O   . LEU A 68  ? 0.4896 0.4593 0.5089 -0.1108 0.0645  -0.0777 69  LEU A O   
611  C CB  . LEU A 68  ? 0.5317 0.4592 0.5259 -0.1323 0.0878  -0.0848 69  LEU A CB  
612  C CG  . LEU A 68  ? 0.6129 0.5112 0.5907 -0.1441 0.1040  -0.0869 69  LEU A CG  
613  C CD1 . LEU A 68  ? 0.6199 0.4985 0.5872 -0.1382 0.1041  -0.0816 69  LEU A CD1 
614  C CD2 . LEU A 68  ? 0.6321 0.5438 0.6173 -0.1628 0.1117  -0.1045 69  LEU A CD2 
615  N N   . SER A 69  ? 0.4497 0.4535 0.4895 -0.1252 0.0610  -0.1022 70  SER A N   
616  C CA  A SER A 69  ? 0.4322 0.4577 0.4846 -0.1126 0.0440  -0.1019 70  SER A CA  
617  C CA  B SER A 69  ? 0.4354 0.4603 0.4874 -0.1124 0.0440  -0.1015 70  SER A CA  
618  C C   . SER A 69  ? 0.4575 0.4771 0.5013 -0.1061 0.0340  -0.0975 70  SER A C   
619  O O   . SER A 69  ? 0.4096 0.4368 0.4556 -0.0949 0.0205  -0.0936 70  SER A O   
620  C CB  A SER A 69  ? 0.4732 0.5320 0.5481 -0.1169 0.0385  -0.1187 70  SER A CB  
621  C CB  B SER A 69  ? 0.4778 0.5361 0.5526 -0.1160 0.0384  -0.1176 70  SER A CB  
622  O OG  A SER A 69  ? 0.5581 0.6239 0.6414 -0.1240 0.0488  -0.1241 70  SER A OG  
623  O OG  B SER A 69  ? 0.5702 0.6399 0.6503 -0.1269 0.0396  -0.1314 70  SER A OG  
624  N N   . VAL A 70  ? 0.4274 0.4317 0.4596 -0.1142 0.0417  -0.0991 71  VAL A N   
625  C CA  . VAL A 70  ? 0.4188 0.4156 0.4402 -0.1109 0.0352  -0.0964 71  VAL A CA  
626  C C   . VAL A 70  ? 0.4497 0.4168 0.4547 -0.1122 0.0470  -0.0880 71  VAL A C   
627  O O   . VAL A 70  ? 0.4581 0.4115 0.4585 -0.1216 0.0605  -0.0910 71  VAL A O   
628  C CB  . VAL A 70  ? 0.4891 0.5027 0.5152 -0.1197 0.0302  -0.1111 71  VAL A CB  
629  C CG1 . VAL A 70  ? 0.4967 0.5007 0.5077 -0.1172 0.0236  -0.1082 71  VAL A CG1 
630  C CG2 . VAL A 70  ? 0.4814 0.5274 0.5271 -0.1165 0.0171  -0.1213 71  VAL A CG2 
631  N N   . ILE A 71  ? 0.3727 0.3292 0.3685 -0.1029 0.0424  -0.0784 72  ILE A N   
632  C CA  . ILE A 71  ? 0.3762 0.3081 0.3594 -0.1019 0.0519  -0.0721 72  ILE A CA  
633  C C   . ILE A 71  ? 0.4362 0.3660 0.4104 -0.1026 0.0477  -0.0744 72  ILE A C   
634  O O   . ILE A 71  ? 0.4295 0.3669 0.4019 -0.0963 0.0368  -0.0710 72  ILE A O   
635  C CB  . ILE A 71  ? 0.4009 0.3224 0.3828 -0.0907 0.0532  -0.0595 72  ILE A CB  
636  C CG1 . ILE A 71  ? 0.4159 0.3368 0.4024 -0.0907 0.0578  -0.0568 72  ILE A CG1 
637  C CG2 . ILE A 71  ? 0.4312 0.3313 0.4037 -0.0875 0.0613  -0.0549 72  ILE A CG2 
638  C CD1 . ILE A 71  ? 0.5057 0.4079 0.4847 -0.1003 0.0720  -0.0600 72  ILE A CD1 
639  N N   . ASN A 72  ? 0.4028 0.3194 0.3689 -0.1108 0.0571  -0.0800 73  ASN A N   
640  C CA  . ASN A 72  ? 0.4043 0.3166 0.3593 -0.1134 0.0554  -0.0831 73  ASN A CA  
641  C C   . ASN A 72  ? 0.4563 0.3493 0.4042 -0.1077 0.0636  -0.0765 73  ASN A C   
642  O O   . ASN A 72  ? 0.4539 0.3300 0.4009 -0.1084 0.0755  -0.0762 73  ASN A O   
643  C CB  . ASN A 72  ? 0.4616 0.3732 0.4125 -0.1271 0.0610  -0.0959 73  ASN A CB  
644  C CG  . ASN A 72  ? 0.6837 0.6182 0.6448 -0.1337 0.0536  -0.1057 73  ASN A CG  
645  O OD1 . ASN A 72  ? 0.5610 0.5142 0.5252 -0.1296 0.0387  -0.1069 73  ASN A OD1 
646  N ND2 . ASN A 72  ? 0.6586 0.5916 0.6248 -0.1441 0.0638  -0.1136 73  ASN A ND2 
647  N N   . LEU A 73  ? 0.3985 0.2930 0.3407 -0.1025 0.0577  -0.0722 74  LEU A N   
648  C CA  . LEU A 73  ? 0.3971 0.2779 0.3355 -0.0980 0.0659  -0.0687 74  LEU A CA  
649  C C   . LEU A 73  ? 0.4478 0.3174 0.3753 -0.1066 0.0744  -0.0772 74  LEU A C   
650  O O   . LEU A 73  ? 0.4632 0.3371 0.3828 -0.1161 0.0711  -0.0848 74  LEU A O   
651  C CB  . LEU A 73  ? 0.3947 0.2809 0.3313 -0.0912 0.0590  -0.0621 74  LEU A CB  
652  C CG  . LEU A 73  ? 0.4283 0.3249 0.3752 -0.0825 0.0510  -0.0540 74  LEU A CG  
653  C CD1 . LEU A 73  ? 0.4218 0.3192 0.3663 -0.0771 0.0486  -0.0486 74  LEU A CD1 
654  C CD2 . LEU A 73  ? 0.4414 0.3344 0.3992 -0.0776 0.0568  -0.0506 74  LEU A CD2 
655  N N   . ASP A 74  ? 0.4101 0.2664 0.3379 -0.1028 0.0849  -0.0768 75  ASP A N   
656  C CA  . ASP A 74  ? 0.4380 0.2819 0.3569 -0.1098 0.0955  -0.0855 75  ASP A CA  
657  C C   . ASP A 74  ? 0.5228 0.3730 0.4265 -0.1179 0.0895  -0.0897 75  ASP A C   
658  O O   . ASP A 74  ? 0.4958 0.3533 0.3967 -0.1140 0.0819  -0.0839 75  ASP A O   
659  C CB  . ASP A 74  ? 0.4583 0.2924 0.3839 -0.1008 0.1051  -0.0840 75  ASP A CB  
660  C CG  . ASP A 74  ? 0.6144 0.4346 0.5338 -0.1062 0.1180  -0.0940 75  ASP A CG  
661  O OD1 . ASP A 74  ? 0.6313 0.4541 0.5392 -0.1145 0.1189  -0.0998 75  ASP A OD1 
662  O OD2 . ASP A 74  ? 0.6421 0.4470 0.5667 -0.1019 0.1274  -0.0960 75  ASP A OD2 
663  N N   . PRO A 75  ? 0.5431 0.3891 0.4346 -0.1297 0.0925  -0.0995 76  PRO A N   
664  C CA  . PRO A 75  ? 0.5563 0.4063 0.4288 -0.1373 0.0853  -0.1028 76  PRO A CA  
665  C C   . PRO A 75  ? 0.6027 0.4465 0.4650 -0.1366 0.0899  -0.1012 76  PRO A C   
666  O O   . PRO A 75  ? 0.6146 0.4594 0.4583 -0.1412 0.0819  -0.1003 76  PRO A O   
667  C CB  . PRO A 75  ? 0.5989 0.4438 0.4612 -0.1503 0.0906  -0.1151 76  PRO A CB  
668  C CG  . PRO A 75  ? 0.6585 0.4909 0.5331 -0.1494 0.1052  -0.1186 76  PRO A CG  
669  C CD  . PRO A 75  ? 0.5740 0.4100 0.4661 -0.1374 0.1024  -0.1084 76  PRO A CD  
670  N N   . GLU A 76  ? 0.5608 0.3978 0.4343 -0.1309 0.1022  -0.1011 77  GLU A N   
671  C CA  . GLU A 76  ? 0.5760 0.4104 0.4435 -0.1314 0.1085  -0.1018 77  GLU A CA  
672  C C   . GLU A 76  ? 0.5756 0.4188 0.4454 -0.1246 0.0990  -0.0917 77  GLU A C   
673  O O   . GLU A 76  ? 0.5754 0.4167 0.4358 -0.1278 0.1026  -0.0921 77  GLU A O   
674  C CB  . GLU A 76  ? 0.6065 0.4348 0.4896 -0.1260 0.1241  -0.1072 77  GLU A CB  
675  C CG  . GLU A 76  ? 0.8674 0.6833 0.7430 -0.1349 0.1368  -0.1195 77  GLU A CG  
676  C CD  . GLU A 76  ? 1.3017 1.1138 1.1576 -0.1468 0.1438  -0.1278 77  GLU A CD  
677  O OE1 . GLU A 76  ? 1.3007 1.1142 1.1630 -0.1446 0.1534  -0.1311 77  GLU A OE1 
678  O OE2 . GLU A 76  ? 1.3016 1.1100 1.1351 -0.1589 0.1397  -0.1316 77  GLU A OE2 
679  N N   . ILE A 77  ? 0.4881 0.3400 0.3697 -0.1164 0.0883  -0.0836 78  ILE A N   
680  C CA  . ILE A 77  ? 0.4677 0.3269 0.3520 -0.1099 0.0795  -0.0745 78  ILE A CA  
681  C C   . ILE A 77  ? 0.5264 0.3834 0.3875 -0.1158 0.0683  -0.0721 78  ILE A C   
682  O O   . ILE A 77  ? 0.5124 0.3712 0.3650 -0.1188 0.0586  -0.0732 78  ILE A O   
683  C CB  . ILE A 77  ? 0.4843 0.3527 0.3885 -0.0993 0.0731  -0.0674 78  ILE A CB  
684  C CG1 . ILE A 77  ? 0.4959 0.3618 0.4185 -0.0920 0.0834  -0.0685 78  ILE A CG1 
685  C CG2 . ILE A 77  ? 0.4421 0.3178 0.3480 -0.0934 0.0640  -0.0591 78  ILE A CG2 
686  C CD1 . ILE A 77  ? 0.5847 0.4505 0.5155 -0.0878 0.0935  -0.0711 78  ILE A CD1 
687  N N   . ASN A 78  ? 0.5305 0.3835 0.3815 -0.1171 0.0693  -0.0689 79  ASN A N   
688  C CA  . ASN A 78  ? 0.5494 0.3939 0.3736 -0.1219 0.0597  -0.0650 79  ASN A CA  
689  C C   . ASN A 78  ? 0.5413 0.3923 0.3714 -0.1125 0.0446  -0.0559 79  ASN A C   
690  O O   . ASN A 78  ? 0.4960 0.3538 0.3437 -0.1054 0.0464  -0.0516 79  ASN A O   
691  C CB  . ASN A 78  ? 0.6105 0.4455 0.4217 -0.1287 0.0706  -0.0663 79  ASN A CB  
692  C CG  . ASN A 78  ? 0.8512 0.6711 0.6301 -0.1341 0.0624  -0.0609 79  ASN A CG  
693  O OD1 . ASN A 78  ? 0.6941 0.5120 0.4726 -0.1308 0.0595  -0.0545 79  ASN A OD1 
694  N ND2 . ASN A 78  ? 0.7461 0.5533 0.4955 -0.1427 0.0583  -0.0633 79  ASN A ND2 
695  N N   . PRO A 79  ? 0.5170 0.3667 0.3328 -0.1117 0.0292  -0.0537 80  PRO A N   
696  C CA  . PRO A 79  ? 0.5017 0.3580 0.3248 -0.1017 0.0151  -0.0465 80  PRO A CA  
697  C C   . PRO A 79  ? 0.5482 0.3949 0.3629 -0.0994 0.0149  -0.0392 80  PRO A C   
698  O O   . PRO A 79  ? 0.5292 0.3844 0.3611 -0.0909 0.0107  -0.0346 80  PRO A O   
699  C CB  . PRO A 79  ? 0.5492 0.4035 0.3539 -0.1020 -0.0010 -0.0476 80  PRO A CB  
700  C CG  . PRO A 79  ? 0.6186 0.4738 0.4183 -0.1113 0.0052  -0.0568 80  PRO A CG  
701  C CD  . PRO A 79  ? 0.5677 0.4118 0.3617 -0.1191 0.0233  -0.0589 80  PRO A CD  
702  N N   . GLU A 80  ? 0.5310 0.3594 0.3186 -0.1082 0.0205  -0.0389 81  GLU A N   
703  C CA  . GLU A 80  ? 0.5361 0.3531 0.3135 -0.1086 0.0222  -0.0331 81  GLU A CA  
704  C C   . GLU A 80  ? 0.5409 0.3716 0.3471 -0.1062 0.0347  -0.0346 81  GLU A C   
705  O O   . GLU A 80  ? 0.5210 0.3547 0.3360 -0.1005 0.0312  -0.0296 81  GLU A O   
706  C CB  . GLU A 80  ? 0.5925 0.3847 0.3315 -0.1210 0.0276  -0.0333 81  GLU A CB  
707  C CG  . GLU A 80  ? 0.7478 0.5238 0.4710 -0.1225 0.0280  -0.0269 81  GLU A CG  
708  C CD  . GLU A 80  ? 1.1244 0.8748 0.8111 -0.1377 0.0388  -0.0280 81  GLU A CD  
709  O OE1 . GLU A 80  ? 1.0850 0.8128 0.7456 -0.1396 0.0346  -0.0212 81  GLU A OE1 
710  O OE2 . GLU A 80  ? 1.0808 0.8319 0.7636 -0.1483 0.0525  -0.0361 81  GLU A OE2 
711  N N   . GLY A 81  ? 0.4945 0.3336 0.3150 -0.1099 0.0483  -0.0419 82  GLY A N   
712  C CA  . GLY A 81  ? 0.4725 0.3265 0.3218 -0.1055 0.0582  -0.0443 82  GLY A CA  
713  C C   . GLY A 81  ? 0.4734 0.3418 0.3468 -0.0932 0.0494  -0.0394 82  GLY A C   
714  O O   . GLY A 81  ? 0.4388 0.3156 0.3270 -0.0881 0.0499  -0.0368 82  GLY A O   
715  N N   . PHE A 82  ? 0.4194 0.2910 0.2956 -0.0897 0.0413  -0.0390 83  PHE A N   
716  C CA  . PHE A 82  ? 0.3887 0.2731 0.2855 -0.0800 0.0341  -0.0353 83  PHE A CA  
717  C C   . PHE A 82  ? 0.4318 0.3155 0.3247 -0.0754 0.0235  -0.0290 83  PHE A C   
718  O O   . PHE A 82  ? 0.3946 0.2875 0.3039 -0.0691 0.0228  -0.0261 83  PHE A O   
719  C CB  . PHE A 82  ? 0.4016 0.2906 0.3022 -0.0794 0.0288  -0.0380 83  PHE A CB  
720  C CG  . PHE A 82  ? 0.3938 0.2952 0.3152 -0.0715 0.0248  -0.0354 83  PHE A CG  
721  C CD1 . PHE A 82  ? 0.4196 0.3255 0.3580 -0.0677 0.0332  -0.0354 83  PHE A CD1 
722  C CD2 . PHE A 82  ? 0.3922 0.2999 0.3153 -0.0671 0.0127  -0.0330 83  PHE A CD2 
723  C CE1 . PHE A 82  ? 0.4127 0.3273 0.3658 -0.0615 0.0302  -0.0324 83  PHE A CE1 
724  C CE2 . PHE A 82  ? 0.4000 0.3192 0.3414 -0.0613 0.0107  -0.0317 83  PHE A CE2 
725  C CZ  . PHE A 82  ? 0.3867 0.3085 0.3413 -0.0594 0.0199  -0.0310 83  PHE A CZ  
726  N N   . CYS A 83  ? 0.4516 0.3230 0.3214 -0.0780 0.0147  -0.0269 84  CYS A N   
727  C CA  . CYS A 83  ? 0.4733 0.3392 0.3358 -0.0728 0.0039  -0.0211 84  CYS A CA  
728  C C   . CYS A 83  ? 0.4860 0.3488 0.3508 -0.0739 0.0112  -0.0186 84  CYS A C   
729  O O   . CYS A 83  ? 0.4576 0.3265 0.3341 -0.0673 0.0066  -0.0154 84  CYS A O   
730  C CB  . CYS A 83  ? 0.5387 0.3862 0.3703 -0.0754 -0.0062 -0.0192 84  CYS A CB  
731  S SG  . CYS A 83  ? 0.6227 0.4586 0.4428 -0.0665 -0.0213 -0.0121 84  CYS A SG  
732  N N   . ILE A 84  ? 0.4526 0.3079 0.3079 -0.0831 0.0234  -0.0216 85  ILE A N   
733  C CA  . ILE A 84  ? 0.4291 0.2842 0.2878 -0.0867 0.0323  -0.0220 85  ILE A CA  
734  C C   . ILE A 84  ? 0.4119 0.2898 0.3036 -0.0790 0.0350  -0.0233 85  ILE A C   
735  O O   . ILE A 84  ? 0.3873 0.2699 0.2869 -0.0766 0.0343  -0.0215 85  ILE A O   
736  C CB  . ILE A 84  ? 0.4817 0.3280 0.3262 -0.0994 0.0465  -0.0279 85  ILE A CB  
737  C CG1 . ILE A 84  ? 0.5280 0.3457 0.3321 -0.1084 0.0435  -0.0248 85  ILE A CG1 
738  C CG2 . ILE A 84  ? 0.4695 0.3263 0.3293 -0.1033 0.0585  -0.0326 85  ILE A CG2 
739  C CD1 . ILE A 84  ? 0.6415 0.4504 0.4287 -0.1213 0.0561  -0.0315 85  ILE A CD1 
740  N N   . LEU A 85  ? 0.3711 0.2611 0.2795 -0.0754 0.0380  -0.0263 86  LEU A N   
741  C CA  . LEU A 85  ? 0.3585 0.2661 0.2935 -0.0672 0.0395  -0.0266 86  LEU A CA  
742  C C   . LEU A 85  ? 0.3950 0.3083 0.3380 -0.0593 0.0291  -0.0214 86  LEU A C   
743  O O   . LEU A 85  ? 0.3604 0.2844 0.3177 -0.0544 0.0287  -0.0201 86  LEU A O   
744  C CB  . LEU A 85  ? 0.3698 0.2827 0.3163 -0.0654 0.0463  -0.0309 86  LEU A CB  
745  C CG  . LEU A 85  ? 0.4498 0.3631 0.3971 -0.0713 0.0588  -0.0383 86  LEU A CG  
746  C CD1 . LEU A 85  ? 0.4692 0.3835 0.4249 -0.0689 0.0648  -0.0427 86  LEU A CD1 
747  C CD2 . LEU A 85  ? 0.4523 0.3796 0.4162 -0.0686 0.0629  -0.0407 86  LEU A CD2 
748  N N   . LEU A 86  ? 0.3674 0.2754 0.3016 -0.0584 0.0205  -0.0197 87  LEU A N   
749  C CA  . LEU A 86  ? 0.3489 0.2640 0.2918 -0.0515 0.0112  -0.0168 87  LEU A CA  
750  C C   . LEU A 86  ? 0.3875 0.2986 0.3259 -0.0500 0.0071  -0.0137 87  LEU A C   
751  O O   . LEU A 86  ? 0.3608 0.2815 0.3125 -0.0450 0.0052  -0.0124 87  LEU A O   
752  C CB  . LEU A 86  ? 0.3491 0.2621 0.2852 -0.0511 0.0026  -0.0180 87  LEU A CB  
753  C CG  . LEU A 86  ? 0.4040 0.3281 0.3529 -0.0445 -0.0058 -0.0179 87  LEU A CG  
754  C CD1 . LEU A 86  ? 0.3800 0.3164 0.3479 -0.0425 0.0004  -0.0187 87  LEU A CD1 
755  C CD2 . LEU A 86  ? 0.4445 0.3699 0.3883 -0.0440 -0.0155 -0.0214 87  LEU A CD2 
756  N N   . ASP A 87  ? 0.3727 0.2674 0.2901 -0.0553 0.0067  -0.0126 88  ASP A N   
757  C CA  . ASP A 87  ? 0.3768 0.2626 0.2861 -0.0556 0.0047  -0.0100 88  ASP A CA  
758  C C   . ASP A 87  ? 0.3956 0.2933 0.3205 -0.0571 0.0133  -0.0120 88  ASP A C   
759  O O   . ASP A 87  ? 0.3996 0.3011 0.3312 -0.0537 0.0104  -0.0108 88  ASP A O   
760  C CB  . ASP A 87  ? 0.4396 0.3009 0.3187 -0.0634 0.0055  -0.0086 88  ASP A CB  
761  C CG  . ASP A 87  ? 0.6412 0.4878 0.5011 -0.0594 -0.0074 -0.0054 88  ASP A CG  
762  O OD1 . ASP A 87  ? 0.6333 0.4911 0.5067 -0.0500 -0.0175 -0.0054 88  ASP A OD1 
763  O OD2 . ASP A 87  ? 0.7016 0.5259 0.5324 -0.0656 -0.0077 -0.0037 88  ASP A OD2 
764  N N   . PHE A 88  ? 0.3537 0.2584 0.2851 -0.0617 0.0235  -0.0161 89  PHE A N   
765  C CA  . PHE A 88  ? 0.3337 0.2543 0.2832 -0.0617 0.0304  -0.0196 89  PHE A CA  
766  C C   . PHE A 88  ? 0.3307 0.2676 0.3002 -0.0519 0.0251  -0.0177 89  PHE A C   
767  O O   . PHE A 88  ? 0.3120 0.2582 0.2908 -0.0504 0.0248  -0.0183 89  PHE A O   
768  C CB  . PHE A 88  ? 0.3470 0.2743 0.3030 -0.0657 0.0409  -0.0258 89  PHE A CB  
769  C CG  . PHE A 88  ? 0.3405 0.2887 0.3197 -0.0620 0.0452  -0.0302 89  PHE A CG  
770  C CD1 . PHE A 88  ? 0.3590 0.3132 0.3411 -0.0677 0.0496  -0.0345 89  PHE A CD1 
771  C CD2 . PHE A 88  ? 0.3462 0.3073 0.3430 -0.0524 0.0437  -0.0301 89  PHE A CD2 
772  C CE1 . PHE A 88  ? 0.3477 0.3246 0.3526 -0.0633 0.0515  -0.0397 89  PHE A CE1 
773  C CE2 . PHE A 88  ? 0.3741 0.3541 0.3908 -0.0468 0.0449  -0.0336 89  PHE A CE2 
774  C CZ  . PHE A 88  ? 0.3466 0.3365 0.3686 -0.0519 0.0481  -0.0388 89  PHE A CZ  
775  N N   . MET A 89  ? 0.3009 0.2406 0.2755 -0.0467 0.0220  -0.0160 90  MET A N   
776  C CA  . MET A 89  ? 0.2822 0.2337 0.2714 -0.0392 0.0183  -0.0140 90  MET A CA  
777  C C   . MET A 89  ? 0.3290 0.2819 0.3184 -0.0371 0.0120  -0.0120 90  MET A C   
778  O O   . MET A 89  ? 0.3249 0.2884 0.3246 -0.0338 0.0116  -0.0118 90  MET A O   
779  C CB  . MET A 89  ? 0.2908 0.2403 0.2803 -0.0370 0.0165  -0.0131 90  MET A CB  
780  C CG  . MET A 89  ? 0.3201 0.2681 0.3116 -0.0378 0.0234  -0.0155 90  MET A CG  
781  S SD  . MET A 89  ? 0.3683 0.3132 0.3600 -0.0368 0.0221  -0.0151 90  MET A SD  
782  C CE  . MET A 89  ? 0.3690 0.3058 0.3572 -0.0400 0.0310  -0.0192 90  MET A CE  
783  N N   . TYR A 90  ? 0.2969 0.2381 0.2739 -0.0385 0.0066  -0.0109 91  TYR A N   
784  C CA  . TYR A 90  ? 0.2973 0.2374 0.2744 -0.0352 0.0002  -0.0098 91  TYR A CA  
785  C C   . TYR A 90  ? 0.3542 0.2862 0.3234 -0.0389 0.0017  -0.0101 91  TYR A C   
786  O O   . TYR A 90  ? 0.3447 0.2745 0.3142 -0.0360 -0.0029 -0.0098 91  TYR A O   
787  C CB  . TYR A 90  ? 0.3266 0.2589 0.2961 -0.0323 -0.0081 -0.0094 91  TYR A CB  
788  C CG  . TYR A 90  ? 0.3371 0.2817 0.3191 -0.0286 -0.0103 -0.0111 91  TYR A CG  
789  C CD1 . TYR A 90  ? 0.3508 0.2966 0.3327 -0.0311 -0.0073 -0.0122 91  TYR A CD1 
790  C CD2 . TYR A 90  ? 0.3350 0.2894 0.3283 -0.0241 -0.0140 -0.0128 91  TYR A CD2 
791  C CE1 . TYR A 90  ? 0.3329 0.2883 0.3248 -0.0300 -0.0077 -0.0148 91  TYR A CE1 
792  C CE2 . TYR A 90  ? 0.3318 0.2969 0.3353 -0.0231 -0.0145 -0.0160 91  TYR A CE2 
793  C CZ  . TYR A 90  ? 0.3667 0.3320 0.3692 -0.0265 -0.0109 -0.0168 91  TYR A CZ  
794  O OH  . TYR A 90  ? 0.3463 0.3210 0.3579 -0.0275 -0.0100 -0.0209 91  TYR A OH  
795  N N   . THR A 91  ? 0.3134 0.2400 0.2752 -0.0462 0.0089  -0.0117 92  THR A N   
796  C CA  . THR A 91  ? 0.3380 0.2540 0.2895 -0.0524 0.0120  -0.0129 92  THR A CA  
797  C C   . THR A 91  ? 0.3568 0.2848 0.3172 -0.0592 0.0216  -0.0182 92  THR A C   
798  O O   . THR A 91  ? 0.3687 0.2912 0.3236 -0.0654 0.0251  -0.0207 92  THR A O   
799  C CB  . THR A 91  ? 0.4306 0.3194 0.3549 -0.0580 0.0114  -0.0106 92  THR A CB  
800  O OG1 . THR A 91  ? 0.4293 0.3167 0.3478 -0.0647 0.0187  -0.0127 92  THR A OG1 
801  C CG2 . THR A 91  ? 0.4354 0.3118 0.3496 -0.0503 -0.0003 -0.0064 92  THR A CG2 
802  N N   . SER A 92  ? 0.3012 0.2437 0.2739 -0.0586 0.0262  -0.0210 93  SER A N   
803  C CA  . SER A 92  ? 0.2911 0.2483 0.2751 -0.0640 0.0351  -0.0282 93  SER A CA  
804  C C   . SER A 92  ? 0.3652 0.3077 0.3326 -0.0764 0.0445  -0.0321 93  SER A C   
805  O O   . SER A 92  ? 0.3595 0.3148 0.3367 -0.0825 0.0535  -0.0401 93  SER A O   
806  C CB  . SER A 92  ? 0.3128 0.2832 0.3076 -0.0651 0.0352  -0.0319 93  SER A CB  
807  O OG  . SER A 92  ? 0.3874 0.3679 0.3925 -0.0555 0.0271  -0.0283 93  SER A OG  
808  N N   A ARG A 93  ? 0.3593 0.2758 0.3015 -0.0799 0.0422  -0.0271 94  ARG A N   
809  N N   B ARG A 93  ? 0.3482 0.2644 0.2901 -0.0803 0.0424  -0.0272 94  ARG A N   
810  C CA  A ARG A 93  ? 0.3882 0.2845 0.3070 -0.0927 0.0508  -0.0294 94  ARG A CA  
811  C CA  B ARG A 93  ? 0.3707 0.2678 0.2902 -0.0933 0.0515  -0.0300 94  ARG A CA  
812  C C   A ARG A 93  ? 0.4387 0.3306 0.3507 -0.0934 0.0529  -0.0294 94  ARG A C   
813  C C   B ARG A 93  ? 0.4318 0.3228 0.3427 -0.0939 0.0530  -0.0294 94  ARG A C   
814  O O   A ARG A 93  ? 0.4125 0.2989 0.3200 -0.0858 0.0439  -0.0238 94  ARG A O   
815  O O   B ARG A 93  ? 0.4134 0.2976 0.3186 -0.0864 0.0437  -0.0235 94  ARG A O   
816  C CB  A ARG A 93  ? 0.4369 0.3021 0.3264 -0.0960 0.0459  -0.0234 94  ARG A CB  
817  C CB  B ARG A 93  ? 0.3950 0.2619 0.2857 -0.0990 0.0492  -0.0255 94  ARG A CB  
818  C CG  A ARG A 93  ? 0.5121 0.3774 0.4058 -0.0959 0.0445  -0.0239 94  ARG A CG  
819  C CG  B ARG A 93  ? 0.3827 0.2538 0.2796 -0.1035 0.0527  -0.0292 94  ARG A CG  
820  C CD  A ARG A 93  ? 0.6178 0.4510 0.4844 -0.0941 0.0367  -0.0168 94  ARG A CD  
821  C CD  B ARG A 93  ? 0.5254 0.3640 0.3948 -0.1064 0.0491  -0.0240 94  ARG A CD  
822  N NE  A ARG A 93  ? 0.6871 0.4877 0.5187 -0.1055 0.0423  -0.0152 94  ARG A NE  
823  N NE  B ARG A 93  ? 0.5804 0.4244 0.4578 -0.1107 0.0529  -0.0286 94  ARG A NE  
824  C CZ  A ARG A 93  ? 0.8467 0.6296 0.6607 -0.1198 0.0533  -0.0187 94  ARG A CZ  
825  C CZ  B ARG A 93  ? 0.7458 0.5611 0.5997 -0.1178 0.0551  -0.0274 94  ARG A CZ  
826  N NH1 A ARG A 93  ? 0.6963 0.4464 0.4744 -0.1308 0.0588  -0.0166 94  ARG A NH1 
827  N NH1 B ARG A 93  ? 0.6145 0.4373 0.4780 -0.1225 0.0593  -0.0330 94  ARG A NH1 
828  N NH2 A ARG A 93  ? 0.6457 0.4429 0.4763 -0.1243 0.0593  -0.0250 94  ARG A NH2 
829  N NH2 B ARG A 93  ? 0.6207 0.3978 0.4394 -0.1203 0.0529  -0.0206 94  ARG A NH2 
830  N N   . LEU A 94  ? 0.3983 0.2941 0.3104 -0.1034 0.0655  -0.0373 95  LEU A N   
831  C CA  . LEU A 94  ? 0.3994 0.2912 0.3049 -0.1058 0.0698  -0.0393 95  LEU A CA  
832  C C   . LEU A 94  ? 0.4921 0.3568 0.3637 -0.1210 0.0780  -0.0405 95  LEU A C   
833  O O   . LEU A 94  ? 0.4734 0.3375 0.3413 -0.1337 0.0904  -0.0479 95  LEU A O   
834  C CB  . LEU A 94  ? 0.3887 0.3079 0.3237 -0.1033 0.0780  -0.0485 95  LEU A CB  
835  C CG  . LEU A 94  ? 0.4444 0.3625 0.3780 -0.1042 0.0834  -0.0522 95  LEU A CG  
836  C CD1 . LEU A 94  ? 0.4273 0.3430 0.3628 -0.0926 0.0723  -0.0447 95  LEU A CD1 
837  C CD2 . LEU A 94  ? 0.4478 0.3903 0.4086 -0.1034 0.0938  -0.0638 95  LEU A CD2 
838  N N   . ASN A 95  ? 0.4897 0.3322 0.3355 -0.1205 0.0710  -0.0339 96  ASN A N   
839  C CA  . ASN A 95  ? 0.5282 0.3400 0.3348 -0.1342 0.0766  -0.0332 96  ASN A CA  
840  C C   . ASN A 95  ? 0.5802 0.3982 0.3876 -0.1432 0.0898  -0.0423 96  ASN A C   
841  O O   . ASN A 95  ? 0.5932 0.4031 0.3878 -0.1422 0.0863  -0.0405 96  ASN A O   
842  C CB  . ASN A 95  ? 0.5748 0.3611 0.3529 -0.1280 0.0610  -0.0226 96  ASN A CB  
843  C CG  . ASN A 95  ? 0.8482 0.5980 0.5796 -0.1410 0.0644  -0.0202 96  ASN A CG  
844  O OD1 . ASN A 95  ? 0.7582 0.4946 0.4729 -0.1562 0.0785  -0.0246 96  ASN A OD1 
845  N ND2 . ASN A 95  ? 0.7732 0.5059 0.4812 -0.1361 0.0518  -0.0138 96  ASN A ND2 
846  N N   . LEU A 96  ? 0.5341 0.3701 0.3603 -0.1511 0.1048  -0.0533 97  LEU A N   
847  C CA  . LEU A 96  ? 0.5486 0.3952 0.3823 -0.1585 0.1188  -0.0645 97  LEU A CA  
848  C C   . LEU A 96  ? 0.6340 0.4549 0.4313 -0.1790 0.1325  -0.0689 97  LEU A C   
849  O O   . LEU A 96  ? 0.6243 0.4368 0.4111 -0.1905 0.1405  -0.0715 97  LEU A O   
850  C CB  . LEU A 96  ? 0.5319 0.4148 0.4085 -0.1543 0.1266  -0.0757 97  LEU A CB  
851  C CG  . LEU A 96  ? 0.5965 0.4996 0.4958 -0.1530 0.1367  -0.0873 97  LEU A CG  
852  C CD1 . LEU A 96  ? 0.5897 0.4905 0.4916 -0.1404 0.1270  -0.0812 97  LEU A CD1 
853  C CD2 . LEU A 96  ? 0.5807 0.5194 0.5220 -0.1462 0.1408  -0.0975 97  LEU A CD2 
854  N N   . ARG A 97  ? 0.6075 0.4134 0.3821 -0.1849 0.1357  -0.0697 98  ARG A N   
855  C CA  . ARG A 97  ? 0.6523 0.4291 0.3851 -0.2056 0.1488  -0.0732 98  ARG A CA  
856  C C   . ARG A 97  ? 0.6834 0.4691 0.4201 -0.2134 0.1627  -0.0852 98  ARG A C   
857  O O   . ARG A 97  ? 0.6330 0.4372 0.3942 -0.2010 0.1574  -0.0867 98  ARG A O   
858  C CB  . ARG A 97  ? 0.7011 0.4382 0.3858 -0.2058 0.1347  -0.0588 98  ARG A CB  
859  C CG  . ARG A 97  ? 0.7958 0.5196 0.4733 -0.1972 0.1204  -0.0470 98  ARG A CG  
860  C CD  . ARG A 97  ? 1.0597 0.7477 0.6947 -0.1926 0.1033  -0.0334 98  ARG A CD  
861  N NE  . ARG A 97  ? 1.3397 0.9889 0.9218 -0.2106 0.1116  -0.0326 98  ARG A NE  
862  C CZ  . ARG A 97  ? 1.6161 1.2325 1.1630 -0.2238 0.1187  -0.0297 98  ARG A CZ  
863  N NH1 . ARG A 97  ? 1.5007 1.0794 0.9959 -0.2408 0.1269  -0.0288 98  ARG A NH1 
864  N NH2 . ARG A 97  ? 1.4703 1.0891 1.0310 -0.2210 0.1185  -0.0281 98  ARG A NH2 
865  N N   . GLU A 98  ? 0.6675 0.4382 0.3786 -0.2349 0.1815  -0.0945 99  GLU A N   
866  C CA  . GLU A 98  ? 0.6794 0.4567 0.3915 -0.2442 0.1967  -0.1076 99  GLU A CA  
867  C C   . GLU A 98  ? 0.7412 0.5080 0.4391 -0.2357 0.1844  -0.1006 99  GLU A C   
868  O O   . GLU A 98  ? 0.7336 0.5201 0.4563 -0.2307 0.1892  -0.1095 99  GLU A O   
869  C CB  . GLU A 98  ? 0.7471 0.4994 0.4195 -0.2710 0.2172  -0.1158 99  GLU A CB  
870  C CG  . GLU A 98  ? 0.8802 0.6424 0.5567 -0.2828 0.2364  -0.1326 99  GLU A CG  
871  C CD  . GLU A 98  ? 1.3615 1.0970 0.9949 -0.3113 0.2581  -0.1412 99  GLU A CD  
872  O OE1 . GLU A 98  ? 1.3887 1.0813 0.9670 -0.3215 0.2530  -0.1288 99  GLU A OE1 
873  O OE2 . GLU A 98  ? 1.3814 1.1384 1.0356 -0.3235 0.2803  -0.1610 99  GLU A OE2 
874  N N   . GLY A 99  ? 0.7310 0.4673 0.3903 -0.2337 0.1682  -0.0857 100 GLY A N   
875  C CA  . GLY A 99  ? 0.7495 0.4756 0.3923 -0.2269 0.1547  -0.0794 100 GLY A CA  
876  C C   . GLY A 99  ? 0.7423 0.4934 0.4232 -0.2056 0.1394  -0.0754 100 GLY A C   
877  O O   . GLY A 99  ? 0.7414 0.4906 0.4163 -0.2014 0.1318  -0.0743 100 GLY A O   
878  N N   . ASN A 100 ? 0.6531 0.4273 0.3719 -0.1929 0.1352  -0.0737 101 ASN A N   
879  C CA  . ASN A 100 ? 0.6072 0.4016 0.3578 -0.1741 0.1216  -0.0695 101 ASN A CA  
880  C C   . ASN A 100 ? 0.6191 0.4458 0.4174 -0.1653 0.1295  -0.0781 101 ASN A C   
881  O O   . ASN A 100 ? 0.5936 0.4342 0.4159 -0.1511 0.1207  -0.0754 101 ASN A O   
882  C CB  . ASN A 100 ? 0.5923 0.3805 0.3389 -0.1629 0.1026  -0.0560 101 ASN A CB  
883  C CG  . ASN A 100 ? 0.6801 0.4760 0.4421 -0.1609 0.1044  -0.0545 101 ASN A CG  
884  O OD1 . ASN A 100 ? 0.5462 0.3644 0.3379 -0.1612 0.1157  -0.0631 101 ASN A OD1 
885  N ND2 . ASN A 100 ? 0.6088 0.3877 0.3523 -0.1578 0.0924  -0.0442 101 ASN A ND2 
886  N N   . ILE A 101 ? 0.5765 0.4146 0.3880 -0.1734 0.1457  -0.0888 102 ILE A N   
887  C CA  . ILE A 101 ? 0.5489 0.4188 0.4061 -0.1633 0.1512  -0.0973 102 ILE A CA  
888  C C   . ILE A 101 ? 0.5663 0.4480 0.4454 -0.1533 0.1523  -0.1025 102 ILE A C   
889  O O   . ILE A 101 ? 0.5188 0.4188 0.4293 -0.1374 0.1457  -0.1009 102 ILE A O   
890  C CB  . ILE A 101 ? 0.5956 0.4788 0.4643 -0.1749 0.1688  -0.1109 102 ILE A CB  
891  C CG1 . ILE A 101 ? 0.5753 0.4943 0.4936 -0.1606 0.1697  -0.1187 102 ILE A CG1 
892  C CG2 . ILE A 101 ? 0.6085 0.4817 0.4577 -0.1930 0.1875  -0.1235 102 ILE A CG2 
893  C CD1 . ILE A 101 ? 0.5867 0.5237 0.5212 -0.1670 0.1780  -0.1274 102 ILE A CD1 
894  N N   . MET A 102 ? 0.5518 0.4211 0.4125 -0.1626 0.1606  -0.1086 103 MET A N   
895  C CA  . MET A 102 ? 0.5546 0.4316 0.4339 -0.1541 0.1628  -0.1143 103 MET A CA  
896  C C   . MET A 102 ? 0.5649 0.4383 0.4467 -0.1409 0.1458  -0.1025 103 MET A C   
897  O O   . MET A 102 ? 0.5303 0.4162 0.4399 -0.1275 0.1440  -0.1035 103 MET A O   
898  C CB  . MET A 102 ? 0.6244 0.4882 0.4820 -0.1685 0.1764  -0.1247 103 MET A CB  
899  C CG  . MET A 102 ? 0.7084 0.5789 0.5679 -0.1824 0.1966  -0.1398 103 MET A CG  
900  S SD  . MET A 102 ? 0.7583 0.6656 0.6722 -0.1704 0.2053  -0.1525 103 MET A SD  
901  C CE  . MET A 102 ? 0.7141 0.6285 0.6532 -0.1573 0.2095  -0.1616 103 MET A CE  
902  N N   . ALA A 103 ? 0.5320 0.3881 0.3847 -0.1445 0.1333  -0.0917 104 ALA A N   
903  C CA  . ALA A 103 ? 0.5220 0.3768 0.3770 -0.1340 0.1175  -0.0822 104 ALA A CA  
904  C C   . ALA A 103 ? 0.5211 0.3912 0.4028 -0.1198 0.1089  -0.0753 104 ALA A C   
905  O O   . ALA A 103 ? 0.4927 0.3700 0.3926 -0.1089 0.1034  -0.0727 104 ALA A O   
906  C CB  . ALA A 103 ? 0.5562 0.3924 0.3763 -0.1401 0.1055  -0.0741 104 ALA A CB  
907  N N   . VAL A 104 ? 0.4553 0.3287 0.3373 -0.1214 0.1086  -0.0727 105 VAL A N   
908  C CA  . VAL A 104 ? 0.4199 0.3083 0.3254 -0.1094 0.1009  -0.0671 105 VAL A CA  
909  C C   . VAL A 104 ? 0.4467 0.3543 0.3857 -0.0989 0.1065  -0.0732 105 VAL A C   
910  O O   . VAL A 104 ? 0.4327 0.3469 0.3872 -0.0866 0.0980  -0.0675 105 VAL A O   
911  C CB  . VAL A 104 ? 0.4656 0.3524 0.3633 -0.1149 0.1005  -0.0645 105 VAL A CB  
912  C CG1 . VAL A 104 ? 0.4247 0.3296 0.3488 -0.1032 0.0941  -0.0610 105 VAL A CG1 
913  C CG2 . VAL A 104 ? 0.4837 0.3477 0.3475 -0.1205 0.0908  -0.0557 105 VAL A CG2 
914  N N   A MET A 105 ? 0.4165 0.3320 0.3658 -0.1033 0.1205  -0.0852 106 MET A N   
915  N N   B MET A 105 ? 0.4217 0.3373 0.3711 -0.1033 0.1205  -0.0852 106 MET A N   
916  C CA  A MET A 105 ? 0.4114 0.3447 0.3929 -0.0911 0.1248  -0.0920 106 MET A CA  
917  C CA  B MET A 105 ? 0.4159 0.3494 0.3976 -0.0911 0.1248  -0.0920 106 MET A CA  
918  C C   A MET A 105 ? 0.4651 0.3909 0.4506 -0.0821 0.1220  -0.0899 106 MET A C   
919  C C   B MET A 105 ? 0.4686 0.3944 0.4541 -0.0821 0.1220  -0.0899 106 MET A C   
920  O O   A MET A 105 ? 0.4413 0.3745 0.4462 -0.0678 0.1164  -0.0866 106 MET A O   
921  O O   B MET A 105 ? 0.4469 0.3801 0.4517 -0.0678 0.1162  -0.0864 106 MET A O   
922  C CB  A MET A 105 ? 0.4552 0.4000 0.4484 -0.0976 0.1409  -0.1075 106 MET A CB  
923  C CB  B MET A 105 ? 0.4595 0.4043 0.4528 -0.0975 0.1409  -0.1075 106 MET A CB  
924  C CG  A MET A 105 ? 0.4936 0.4598 0.5232 -0.0819 0.1427  -0.1150 106 MET A CG  
925  C CG  B MET A 105 ? 0.4978 0.4643 0.5275 -0.0820 0.1426  -0.1150 106 MET A CG  
926  S SD  A MET A 105 ? 0.5620 0.5498 0.6124 -0.0888 0.1609  -0.1359 106 MET A SD  
927  S SD  B MET A 105 ? 0.5691 0.5547 0.6182 -0.0888 0.1617  -0.1363 106 MET A SD  
928  C CE  A MET A 105 ? 0.5475 0.5180 0.5841 -0.0967 0.1744  -0.1452 106 MET A CE  
929  C CE  B MET A 105 ? 0.5252 0.5204 0.6059 -0.0671 0.1608  -0.1422 106 MET A CE  
930  N N   . ALA A 106 ? 0.4501 0.3597 0.4152 -0.0912 0.1261  -0.0921 107 ALA A N   
931  C CA  . ALA A 106 ? 0.4533 0.3533 0.4192 -0.0858 0.1251  -0.0916 107 ALA A CA  
932  C C   . ALA A 106 ? 0.4570 0.3542 0.4222 -0.0782 0.1110  -0.0794 107 ALA A C   
933  O O   . ALA A 106 ? 0.4269 0.3228 0.4048 -0.0679 0.1094  -0.0774 107 ALA A O   
934  C CB  . ALA A 106 ? 0.4881 0.3728 0.4298 -0.0995 0.1314  -0.0970 107 ALA A CB  
935  N N   . THR A 107 ? 0.4073 0.3028 0.3578 -0.0829 0.1013  -0.0716 108 THR A N   
936  C CA  . THR A 107 ? 0.3927 0.2885 0.3444 -0.0765 0.0887  -0.0618 108 THR A CA  
937  C C   . THR A 107 ? 0.4242 0.3324 0.3980 -0.0638 0.0852  -0.0576 108 THR A C   
938  O O   . THR A 107 ? 0.3909 0.2976 0.3715 -0.0562 0.0807  -0.0530 108 THR A O   
939  C CB  . THR A 107 ? 0.4809 0.3718 0.4125 -0.0830 0.0788  -0.0558 108 THR A CB  
940  O OG1 . THR A 107 ? 0.4789 0.3577 0.3874 -0.0944 0.0816  -0.0601 108 THR A OG1 
941  C CG2 . THR A 107 ? 0.4393 0.3318 0.3734 -0.0774 0.0670  -0.0488 108 THR A CG2 
942  N N   . ALA A 108 ? 0.3652 0.2852 0.3489 -0.0625 0.0877  -0.0599 109 ALA A N   
943  C CA  . ALA A 108 ? 0.3411 0.2750 0.3451 -0.0506 0.0834  -0.0570 109 ALA A CA  
944  C C   . ALA A 108 ? 0.3767 0.3115 0.3969 -0.0391 0.0870  -0.0602 109 ALA A C   
945  O O   . ALA A 108 ? 0.3531 0.2900 0.3821 -0.0280 0.0804  -0.0543 109 ALA A O   
946  C CB  . ALA A 108 ? 0.3417 0.2898 0.3532 -0.0540 0.0866  -0.0617 109 ALA A CB  
947  N N   . MET A 109 ? 0.3654 0.2959 0.3874 -0.0414 0.0975  -0.0695 110 MET A N   
948  C CA  . MET A 109 ? 0.3723 0.2994 0.4081 -0.0291 0.1009  -0.0727 110 MET A CA  
949  C C   . MET A 109 ? 0.4151 0.3238 0.4405 -0.0262 0.0967  -0.0650 110 MET A C   
950  O O   . MET A 109 ? 0.4184 0.3228 0.4509 -0.0137 0.0926  -0.0603 110 MET A O   
951  C CB  . MET A 109 ? 0.4168 0.3424 0.4564 -0.0332 0.1141  -0.0858 110 MET A CB  
952  C CG  . MET A 109 ? 0.4733 0.4205 0.5308 -0.0330 0.1200  -0.0961 110 MET A CG  
953  S SD  . MET A 109 ? 0.5733 0.5191 0.6315 -0.0428 0.1380  -0.1132 110 MET A SD  
954  C CE  . MET A 109 ? 0.5488 0.4853 0.6232 -0.0246 0.1401  -0.1170 110 MET A CE  
955  N N   . TYR A 110 ? 0.3991 0.2966 0.4062 -0.0382 0.0973  -0.0640 111 TYR A N   
956  C CA  . TYR A 110 ? 0.4002 0.2825 0.3972 -0.0394 0.0948  -0.0592 111 TYR A CA  
957  C C   . TYR A 110 ? 0.4258 0.3120 0.4242 -0.0338 0.0843  -0.0488 111 TYR A C   
958  O O   . TYR A 110 ? 0.4223 0.2975 0.4202 -0.0279 0.0836  -0.0445 111 TYR A O   
959  C CB  . TYR A 110 ? 0.4149 0.2915 0.3940 -0.0542 0.0957  -0.0620 111 TYR A CB  
960  C CG  . TYR A 110 ? 0.4245 0.2919 0.3945 -0.0583 0.0919  -0.0587 111 TYR A CG  
961  C CD1 . TYR A 110 ? 0.4593 0.3109 0.4269 -0.0589 0.0991  -0.0623 111 TYR A CD1 
962  C CD2 . TYR A 110 ? 0.4135 0.2879 0.3774 -0.0627 0.0820  -0.0537 111 TYR A CD2 
963  C CE1 . TYR A 110 ? 0.4295 0.2740 0.3892 -0.0652 0.0972  -0.0613 111 TYR A CE1 
964  C CE2 . TYR A 110 ? 0.4129 0.2831 0.3713 -0.0676 0.0792  -0.0533 111 TYR A CE2 
965  C CZ  . TYR A 110 ? 0.4473 0.3032 0.4036 -0.0701 0.0874  -0.0576 111 TYR A CZ  
966  O OH  . TYR A 110 ? 0.4471 0.3005 0.3988 -0.0772 0.0860  -0.0591 111 TYR A OH  
967  N N   . LEU A 111 ? 0.3570 0.2566 0.3555 -0.0362 0.0773  -0.0452 112 LEU A N   
968  C CA  . LEU A 111 ? 0.3416 0.2465 0.3417 -0.0320 0.0680  -0.0368 112 LEU A CA  
969  C C   . LEU A 111 ? 0.3937 0.3051 0.4069 -0.0190 0.0654  -0.0335 112 LEU A C   
970  O O   . LEU A 111 ? 0.3823 0.2955 0.3954 -0.0149 0.0588  -0.0267 112 LEU A O   
971  C CB  . LEU A 111 ? 0.3226 0.2372 0.3173 -0.0386 0.0617  -0.0349 112 LEU A CB  
972  C CG  . LEU A 111 ? 0.3736 0.2823 0.3533 -0.0492 0.0596  -0.0363 112 LEU A CG  
973  C CD1 . LEU A 111 ? 0.3760 0.2910 0.3496 -0.0523 0.0516  -0.0331 112 LEU A CD1 
974  C CD2 . LEU A 111 ? 0.3997 0.3022 0.3766 -0.0505 0.0576  -0.0349 112 LEU A CD2 
975  N N   . GLN A 112 ? 0.3626 0.2790 0.3873 -0.0124 0.0701  -0.0392 113 GLN A N   
976  C CA  . GLN A 112 ? 0.3658 0.2917 0.4051 0.0016  0.0661  -0.0380 113 GLN A CA  
977  C C   . GLN A 112 ? 0.3882 0.3325 0.4326 0.0010  0.0586  -0.0350 113 GLN A C   
978  O O   . GLN A 112 ? 0.3619 0.3071 0.4050 0.0066  0.0511  -0.0278 113 GLN A O   
979  C CB  . GLN A 112 ? 0.3949 0.3040 0.4295 0.0121  0.0633  -0.0313 113 GLN A CB  
980  C CG  . GLN A 112 ? 0.4297 0.3169 0.4580 0.0124  0.0718  -0.0346 113 GLN A CG  
981  C CD  . GLN A 112 ? 0.5730 0.4372 0.5883 0.0173  0.0701  -0.0265 113 GLN A CD  
982  O OE1 . GLN A 112 ? 0.4922 0.3564 0.5064 0.0261  0.0627  -0.0192 113 GLN A OE1 
983  N NE2 . GLN A 112 ? 0.5506 0.3937 0.5538 0.0102  0.0776  -0.0281 113 GLN A NE2 
984  N N   . MET A 113 ? 0.3433 0.2998 0.3909 -0.0074 0.0619  -0.0411 114 MET A N   
985  C CA  . MET A 113 ? 0.3307 0.3027 0.3819 -0.0107 0.0572  -0.0404 114 MET A CA  
986  C C   . MET A 113 ? 0.3955 0.3858 0.4645 -0.0086 0.0623  -0.0507 114 MET A C   
987  O O   . MET A 113 ? 0.3683 0.3613 0.4356 -0.0191 0.0706  -0.0583 114 MET A O   
988  C CB  . MET A 113 ? 0.3523 0.3171 0.3870 -0.0243 0.0577  -0.0388 114 MET A CB  
989  C CG  . MET A 113 ? 0.3737 0.3258 0.3957 -0.0254 0.0520  -0.0309 114 MET A CG  
990  S SD  . MET A 113 ? 0.4149 0.3587 0.4183 -0.0380 0.0499  -0.0299 114 MET A SD  
991  C CE  . MET A 113 ? 0.3670 0.3218 0.3732 -0.0384 0.0442  -0.0274 114 MET A CE  
992  N N   . GLU A 114 ? 0.3803 0.3818 0.4657 0.0056  0.0579  -0.0518 115 GLU A N   
993  C CA  . GLU A 114 ? 0.3991 0.4214 0.5070 0.0114  0.0617  -0.0636 115 GLU A CA  
994  C C   . GLU A 114 ? 0.4083 0.4512 0.5244 0.0005  0.0658  -0.0721 115 GLU A C   
995  O O   . GLU A 114 ? 0.3952 0.4497 0.5233 -0.0037 0.0754  -0.0847 115 GLU A O   
996  C CB  . GLU A 114 ? 0.4359 0.4670 0.5581 0.0306  0.0522  -0.0618 115 GLU A CB  
997  C CG  . GLU A 114 ? 0.6290 0.6362 0.7425 0.0417  0.0507  -0.0553 115 GLU A CG  
998  N N   . HIS A 115 ? 0.3521 0.3984 0.4612 -0.0051 0.0601  -0.0667 116 HIS A N   
999  C CA  . HIS A 115 ? 0.3691 0.4313 0.4834 -0.0170 0.0651  -0.0750 116 HIS A CA  
1000 C C   . HIS A 115 ? 0.3927 0.4409 0.4902 -0.0341 0.0765  -0.0786 116 HIS A C   
1001 O O   . HIS A 115 ? 0.3935 0.4537 0.4984 -0.0436 0.0865  -0.0904 116 HIS A O   
1002 C CB  . HIS A 115 ? 0.3889 0.4559 0.4991 -0.0185 0.0566  -0.0689 116 HIS A CB  
1003 C CG  . HIS A 115 ? 0.4379 0.5225 0.5645 -0.0036 0.0462  -0.0681 116 HIS A CG  
1004 N ND1 . HIS A 115 ? 0.4657 0.5777 0.6177 0.0033  0.0463  -0.0800 116 HIS A ND1 
1005 C CD2 . HIS A 115 ? 0.4607 0.5394 0.5803 0.0050  0.0354  -0.0574 116 HIS A CD2 
1006 C CE1 . HIS A 115 ? 0.4607 0.5812 0.6188 0.0171  0.0340  -0.0752 116 HIS A CE1 
1007 N NE2 . HIS A 115 ? 0.4624 0.5622 0.6001 0.0177  0.0278  -0.0614 116 HIS A NE2 
1008 N N   . VAL A 116 ? 0.3339 0.3571 0.4085 -0.0381 0.0753  -0.0694 117 VAL A N   
1009 C CA  . VAL A 116 ? 0.3420 0.3487 0.3961 -0.0530 0.0842  -0.0716 117 VAL A CA  
1010 C C   . VAL A 116 ? 0.4106 0.4208 0.4731 -0.0548 0.0959  -0.0830 117 VAL A C   
1011 O O   . VAL A 116 ? 0.3857 0.3967 0.4429 -0.0682 0.1072  -0.0921 117 VAL A O   
1012 C CB  . VAL A 116 ? 0.3823 0.3651 0.4121 -0.0555 0.0780  -0.0603 117 VAL A CB  
1013 C CG1 . VAL A 116 ? 0.3936 0.3591 0.4005 -0.0696 0.0858  -0.0630 117 VAL A CG1 
1014 C CG2 . VAL A 116 ? 0.3753 0.3558 0.3981 -0.0549 0.0681  -0.0515 117 VAL A CG2 
1015 N N   . VAL A 117 ? 0.3725 0.3834 0.4471 -0.0417 0.0942  -0.0831 118 VAL A N   
1016 C CA  . VAL A 117 ? 0.3778 0.3922 0.4631 -0.0409 0.1052  -0.0949 118 VAL A CA  
1017 C C   . VAL A 117 ? 0.4360 0.4776 0.5447 -0.0434 0.1133  -0.1101 118 VAL A C   
1018 O O   . VAL A 117 ? 0.4338 0.4766 0.5404 -0.0555 0.1269  -0.1215 118 VAL A O   
1019 C CB  . VAL A 117 ? 0.4173 0.4263 0.5128 -0.0240 0.1009  -0.0923 118 VAL A CB  
1020 C CG1 . VAL A 117 ? 0.4202 0.4331 0.5292 -0.0217 0.1127  -0.1060 118 VAL A CG1 
1021 C CG2 . VAL A 117 ? 0.4151 0.3985 0.4877 -0.0253 0.0958  -0.0802 118 VAL A CG2 
1022 N N   A ASP A 118 ? 0.3989 0.4630 0.5300 -0.0320 0.1053  -0.1114 119 ASP A N   
1023 N N   B ASP A 118 ? 0.3931 0.4563 0.5215 -0.0341 0.1053  -0.1106 119 ASP A N   
1024 C CA  A ASP A 118 ? 0.4001 0.4958 0.5585 -0.0326 0.1111  -0.1273 119 ASP A CA  
1025 C CA  B ASP A 118 ? 0.3883 0.4824 0.5423 -0.0360 0.1110  -0.1259 119 ASP A CA  
1026 C C   A ASP A 118 ? 0.4606 0.5593 0.6093 -0.0550 0.1237  -0.1358 119 ASP A C   
1027 C C   B ASP A 118 ? 0.4291 0.5228 0.5702 -0.0589 0.1234  -0.1332 119 ASP A C   
1028 O O   A ASP A 118 ? 0.4684 0.5852 0.6334 -0.0619 0.1365  -0.1527 119 ASP A O   
1029 O O   B ASP A 118 ? 0.4225 0.5305 0.5761 -0.0672 0.1372  -0.1494 119 ASP A O   
1030 C CB  A ASP A 118 ? 0.4124 0.5297 0.5903 -0.0182 0.0974  -0.1249 119 ASP A CB  
1031 C CB  B ASP A 118 ? 0.4022 0.5172 0.5744 -0.0227 0.0974  -0.1230 119 ASP A CB  
1032 C CG  A ASP A 118 ? 0.5589 0.6805 0.7536 0.0054  0.0873  -0.1226 119 ASP A CG  
1033 C CG  B ASP A 118 ? 0.5743 0.7265 0.7779 -0.0223 0.1012  -0.1406 119 ASP A CG  
1034 O OD1 A ASP A 118 ? 0.5991 0.7246 0.8082 0.0126  0.0937  -0.1324 119 ASP A OD1 
1035 O OD1 B ASP A 118 ? 0.6091 0.7781 0.8361 -0.0155 0.1074  -0.1545 119 ASP A OD1 
1036 O OD2 A ASP A 118 ? 0.6138 0.7332 0.8057 0.0168  0.0734  -0.1113 119 ASP A OD2 
1037 O OD2 B ASP A 118 ? 0.6307 0.7966 0.8369 -0.0287 0.0980  -0.1416 119 ASP A OD2 
1038 N N   A THR A 119 ? 0.4119 0.4913 0.5331 -0.0666 0.1207  -0.1247 120 THR A N   
1039 N N   B THR A 119 ? 0.3752 0.4511 0.4904 -0.0694 0.1195  -0.1221 120 THR A N   
1040 C CA  A THR A 119 ? 0.4192 0.4927 0.5232 -0.0883 0.1317  -0.1299 120 THR A CA  
1041 C CA  B THR A 119 ? 0.3822 0.4512 0.4796 -0.0913 0.1312  -0.1276 120 THR A CA  
1042 C C   A THR A 119 ? 0.4637 0.5164 0.5450 -0.1025 0.1449  -0.1335 120 THR A C   
1043 C C   B THR A 119 ? 0.4473 0.4952 0.5222 -0.1049 0.1442  -0.1312 120 THR A C   
1044 O O   A THR A 119 ? 0.4661 0.5246 0.5465 -0.1184 0.1600  -0.1468 120 THR A O   
1045 O O   B THR A 119 ? 0.4463 0.4951 0.5143 -0.1225 0.1587  -0.1423 120 THR A O   
1046 C CB  A THR A 119 ? 0.5364 0.5949 0.6199 -0.0922 0.1223  -0.1165 120 THR A CB  
1047 C CB  B THR A 119 ? 0.4074 0.4606 0.4827 -0.0975 0.1234  -0.1155 120 THR A CB  
1048 O OG1 A THR A 119 ? 0.5318 0.6144 0.6397 -0.0798 0.1123  -0.1169 120 THR A OG1 
1049 O OG1 B THR A 119 ? 0.4173 0.4695 0.4826 -0.1172 0.1358  -0.1243 120 THR A OG1 
1050 C CG2 A THR A 119 ? 0.5425 0.5900 0.6050 -0.1137 0.1329  -0.1207 120 THR A CG2 
1051 C CG2 B THR A 119 ? 0.3251 0.3447 0.3681 -0.0980 0.1163  -0.0997 120 THR A CG2 
1052 N N   . CYS A 120 ? 0.4094 0.4381 0.4715 -0.0981 0.1397  -0.1227 121 CYS A N   
1053 C CA  . CYS A 120 ? 0.4336 0.4419 0.4727 -0.1104 0.1508  -0.1260 121 CYS A CA  
1054 C C   . CYS A 120 ? 0.5017 0.5298 0.5640 -0.1122 0.1658  -0.1449 121 CYS A C   
1055 O O   . CYS A 120 ? 0.5018 0.5249 0.5508 -0.1304 0.1813  -0.1552 121 CYS A O   
1056 C CB  . CYS A 120 ? 0.4322 0.4200 0.4568 -0.1019 0.1416  -0.1143 121 CYS A CB  
1057 S SG  . CYS A 120 ? 0.4798 0.4423 0.4725 -0.1039 0.1268  -0.0953 121 CYS A SG  
1058 N N   . ARG A 121 ? 0.4634 0.5139 0.5604 -0.0931 0.1612  -0.1500 122 ARG A N   
1059 C CA  . ARG A 121 ? 0.4702 0.5443 0.5970 -0.0899 0.1733  -0.1693 122 ARG A CA  
1060 C C   . ARG A 121 ? 0.5191 0.6166 0.6583 -0.1054 0.1867  -0.1860 122 ARG A C   
1061 O O   . ARG A 121 ? 0.5212 0.6242 0.6631 -0.1180 0.2043  -0.2022 122 ARG A O   
1062 C CB  . ARG A 121 ? 0.4722 0.5662 0.6332 -0.0641 0.1619  -0.1699 122 ARG A CB  
1063 C CG  . ARG A 121 ? 0.6877 0.7597 0.8408 -0.0506 0.1555  -0.1603 122 ARG A CG  
1064 C CD  . ARG A 121 ? 0.8716 0.9604 1.0578 -0.0306 0.1554  -0.1709 122 ARG A CD  
1065 N NE  . ARG A 121 ? 0.9730 1.0587 1.1664 -0.0087 0.1379  -0.1581 122 ARG A NE  
1066 C CZ  . ARG A 121 ? 1.1022 1.1613 1.2811 0.0005  0.1321  -0.1464 122 ARG A CZ  
1067 N NH1 . ARG A 121 ? 0.8489 0.8845 1.0075 -0.0097 0.1414  -0.1464 122 ARG A NH1 
1068 N NH2 . ARG A 121 ? 0.9535 1.0085 1.1363 0.0188  0.1174  -0.1352 122 ARG A NH2 
1069 N N   . LYS A 122 ? 0.4790 0.5895 0.6246 -0.1059 0.1794  -0.1829 123 LYS A N   
1070 C CA  . LYS A 122 ? 0.4867 0.6196 0.6440 -0.1217 0.1914  -0.1985 123 LYS A CA  
1071 C C   . LYS A 122 ? 0.5532 0.6597 0.6721 -0.1494 0.2071  -0.1997 123 LYS A C   
1072 O O   . LYS A 122 ? 0.5429 0.6629 0.6691 -0.1656 0.2256  -0.2183 123 LYS A O   
1073 C CB  . LYS A 122 ? 0.4957 0.6448 0.6650 -0.1159 0.1786  -0.1933 123 LYS A CB  
1074 C CG  . LYS A 122 ? 0.7061 0.8879 0.9159 -0.0907 0.1652  -0.1971 123 LYS A CG  
1075 C CD  . LYS A 122 ? 0.8400 1.0428 1.0630 -0.0886 0.1553  -0.1966 123 LYS A CD  
1076 C CE  . LYS A 122 ? 0.9523 1.1710 1.1977 -0.0617 0.1354  -0.1897 123 LYS A CE  
1077 N NZ  . LYS A 122 ? 1.0462 1.2965 1.3307 -0.0447 0.1351  -0.2055 123 LYS A NZ  
1078 N N   . PHE A 123 ? 0.5267 0.5950 0.6041 -0.1547 0.1997  -0.1804 124 PHE A N   
1079 C CA  . PHE A 123 ? 0.5597 0.5961 0.5937 -0.1789 0.2115  -0.1785 124 PHE A CA  
1080 C C   . PHE A 123 ? 0.6310 0.6580 0.6536 -0.1891 0.2272  -0.1887 124 PHE A C   
1081 O O   . PHE A 123 ? 0.6442 0.6615 0.6464 -0.2121 0.2451  -0.1988 124 PHE A O   
1082 C CB  . PHE A 123 ? 0.5886 0.5891 0.5846 -0.1775 0.1966  -0.1558 124 PHE A CB  
1083 C CG  . PHE A 123 ? 0.6197 0.6159 0.6078 -0.1811 0.1898  -0.1485 124 PHE A CG  
1084 C CD1 . PHE A 123 ? 0.6420 0.6696 0.6655 -0.1698 0.1827  -0.1522 124 PHE A CD1 
1085 C CD2 . PHE A 123 ? 0.6803 0.6392 0.6241 -0.1947 0.1893  -0.1375 124 PHE A CD2 
1086 C CE1 . PHE A 123 ? 0.6487 0.6717 0.6644 -0.1740 0.1772  -0.1464 124 PHE A CE1 
1087 C CE2 . PHE A 123 ? 0.7094 0.6617 0.6455 -0.1973 0.1834  -0.1310 124 PHE A CE2 
1088 C CZ  . PHE A 123 ? 0.6540 0.6389 0.6265 -0.1877 0.1781  -0.1360 124 PHE A CZ  
1089 N N   . ILE A 124 ? 0.5649 0.5947 0.6008 -0.1731 0.2218  -0.1874 125 ILE A N   
1090 C CA  . ILE A 124 ? 0.5869 0.6098 0.6157 -0.1808 0.2364  -0.1984 125 ILE A CA  
1091 C C   . ILE A 124 ? 0.6492 0.7059 0.7124 -0.1871 0.2555  -0.2242 125 ILE A C   
1092 O O   . ILE A 124 ? 0.6665 0.7154 0.7129 -0.2075 0.2751  -0.2368 125 ILE A O   
1093 C CB  . ILE A 124 ? 0.6151 0.6288 0.6471 -0.1625 0.2254  -0.1898 125 ILE A CB  
1094 C CG1 . ILE A 124 ? 0.6194 0.5979 0.6106 -0.1639 0.2117  -0.1685 125 ILE A CG1 
1095 C CG2 . ILE A 124 ? 0.6537 0.6682 0.6900 -0.1672 0.2416  -0.2054 125 ILE A CG2 
1096 C CD1 . ILE A 124 ? 0.6636 0.6372 0.6627 -0.1439 0.1965  -0.1573 125 ILE A CD1 
1097 N N   . LYS A 125 ? 0.5984 0.6930 0.7089 -0.1698 0.2496  -0.2327 126 LYS A N   
1098 C CA  . LYS A 125 ? 0.6059 0.7405 0.7579 -0.1715 0.2647  -0.2590 126 LYS A CA  
1099 C C   . LYS A 125 ? 0.6715 0.8116 0.8128 -0.1999 0.2833  -0.2723 126 LYS A C   
1100 O O   . LYS A 125 ? 0.6678 0.8268 0.8243 -0.2131 0.3041  -0.2954 126 LYS A O   
1101 C CB  . LYS A 125 ? 0.6186 0.7903 0.8190 -0.1453 0.2495  -0.2620 126 LYS A CB  
1102 C CG  . LYS A 125 ? 0.8198 1.0346 1.0695 -0.1382 0.2606  -0.2891 126 LYS A CG  
1103 C CD  . LYS A 125 ? 0.9514 1.2046 1.2451 -0.1153 0.2446  -0.2928 126 LYS A CD  
1104 C CE  . LYS A 125 ? 1.1054 1.4063 1.4502 -0.1098 0.2553  -0.3224 126 LYS A CE  
1105 N NZ  . LYS A 125 ? 1.2167 1.5573 1.6019 -0.0901 0.2390  -0.3271 126 LYS A NZ  
1106 N N   . ALA A 126 ? 0.6305 0.7519 0.7440 -0.2100 0.2769  -0.2584 127 ALA A N   
1107 C CA  . ALA A 126 ? 0.6564 0.7743 0.7519 -0.2382 0.2941  -0.2682 127 ALA A CA  
1108 C C   . ALA A 126 ? 0.7704 0.8523 0.8190 -0.2643 0.3134  -0.2705 127 ALA A C   
1109 O O   . ALA A 126 ? 0.7788 0.8648 0.8207 -0.2893 0.3353  -0.2874 127 ALA A O   
1110 C CB  . ALA A 126 ? 0.6567 0.7572 0.7311 -0.2396 0.2805  -0.2504 127 ALA A CB  
1111 N N   . SER A 127 ? 0.7779 0.8248 0.7929 -0.2595 0.3055  -0.2541 128 SER A N   
1112 C CA  . SER A 127 ? 0.8431 0.8527 0.8086 -0.2822 0.3203  -0.2539 128 SER A CA  
1113 C C   . SER A 127 ? 0.9360 0.9603 0.9169 -0.2879 0.3396  -0.2752 128 SER A C   
1114 O O   . SER A 127 ? 0.9905 0.9896 0.9330 -0.3118 0.3573  -0.2808 128 SER A O   
1115 C CB  . SER A 127 ? 0.9178 0.8845 0.8391 -0.2754 0.3021  -0.2280 128 SER A CB  
1116 O OG  . SER A 127 ? 1.0727 1.0115 0.9591 -0.2832 0.2938  -0.2121 128 SER A OG  
1117 N N   . GLU A 128 ? 0.8592 0.9224 0.8940 -0.2664 0.3366  -0.2874 129 GLU A N   
1118 C CA  . GLU A 128 ? 1.1552 1.2348 1.2104 -0.2684 0.3542  -0.3090 129 GLU A CA  
1119 C C   . GLU A 128 ? 1.7000 1.8119 1.7802 -0.2880 0.3800  -0.3385 129 GLU A C   
1120 O O   . GLU A 128 ? 1.3098 1.4049 1.3567 -0.3165 0.3958  -0.3423 129 GLU A O   
1121 C CB  . GLU A 128 ? 1.1388 1.2406 1.2375 -0.2362 0.3400  -0.3092 129 GLU A CB  
1122 C CG  . GLU A 128 ? 1.2314 1.3825 1.3908 -0.2167 0.3343  -0.3224 129 GLU A CG  
1123 C CD  . GLU A 128 ? 1.4863 1.6520 1.6817 -0.1826 0.3163  -0.3179 129 GLU A CD  
1124 O OE1 . GLU A 128 ? 1.4233 1.5587 1.5956 -0.1722 0.3042  -0.2996 129 GLU A OE1 
1125 O OE2 . GLU A 128 ? 1.3828 1.5900 1.6289 -0.1663 0.3139  -0.3329 129 GLU A OE2 
1129 N N   A TRP B 2   ? 0.2479 0.4925 0.3741 -0.0516 -0.0134 -0.0837 1   TRP D N   
1130 N N   B TRP B 2   ? 0.2528 0.4974 0.3790 -0.0516 -0.0134 -0.0838 1   TRP D N   
1131 C CA  A TRP B 2   ? 0.2387 0.4849 0.3663 -0.0507 -0.0111 -0.0844 1   TRP D CA  
1132 C CA  B TRP B 2   ? 0.2446 0.4908 0.3722 -0.0507 -0.0112 -0.0844 1   TRP D CA  
1133 C C   A TRP B 2   ? 0.2825 0.5292 0.4119 -0.0513 -0.0108 -0.0830 1   TRP D C   
1134 C C   B TRP B 2   ? 0.2792 0.5261 0.4087 -0.0514 -0.0107 -0.0830 1   TRP D C   
1135 O O   A TRP B 2   ? 0.2956 0.5416 0.4254 -0.0518 -0.0122 -0.0822 1   TRP D O   
1136 O O   B TRP B 2   ? 0.2778 0.5240 0.4076 -0.0520 -0.0120 -0.0822 1   TRP D O   
1137 C CB  A TRP B 2   ? 0.2235 0.4692 0.3510 -0.0501 -0.0125 -0.0866 1   TRP D CB  
1138 C CB  B TRP B 2   ? 0.2300 0.4757 0.3576 -0.0501 -0.0126 -0.0864 1   TRP D CB  
1139 C CG  A TRP B 2   ? 0.2290 0.4743 0.3556 -0.0498 -0.0126 -0.0907 1   TRP D CG  
1140 C CG  B TRP B 2   ? 0.2420 0.4884 0.3720 -0.0502 -0.0149 -0.0856 1   TRP D CG  
1141 C CD1 A TRP B 2   ? 0.2635 0.5076 0.3912 -0.0494 -0.0160 -0.0932 1   TRP D CD1 
1142 C CD1 B TRP B 2   ? 0.2798 0.5267 0.4127 -0.0502 -0.0181 -0.0865 1   TRP D CD1 
1143 C CD2 A TRP B 2   ? 0.2242 0.4698 0.3490 -0.0497 -0.0094 -0.0939 1   TRP D CD2 
1144 C CD2 B TRP B 2   ? 0.2399 0.4872 0.3708 -0.0498 -0.0145 -0.0844 1   TRP D CD2 
1145 N NE1 A TRP B 2   ? 0.2531 0.4970 0.3802 -0.0488 -0.0151 -0.0987 1   TRP D NE1 
1146 N NE1 B TRP B 2   ? 0.2712 0.5205 0.4076 -0.0499 -0.0188 -0.0858 1   TRP D NE1 
1147 C CE2 A TRP B 2   ? 0.2664 0.5115 0.3914 -0.0492 -0.0105 -0.0994 1   TRP D CE2 
1148 C CE2 B TRP B 2   ? 0.2881 0.5377 0.4229 -0.0495 -0.0165 -0.0847 1   TRP D CE2 
1149 C CE3 A TRP B 2   ? 0.2335 0.4791 0.3567 -0.0501 -0.0061 -0.0931 1   TRP D CE3 
1150 C CE3 B TRP B 2   ? 0.2547 0.5010 0.3844 -0.0495 -0.0133 -0.0833 1   TRP D CE3 
1151 C CZ2 A TRP B 2   ? 0.2553 0.5006 0.3788 -0.0490 -0.0072 -0.1050 1   TRP D CZ2 
1152 C CZ2 B TRP B 2   ? 0.2768 0.5284 0.4138 -0.0485 -0.0164 -0.0842 1   TRP D CZ2 
1153 C CZ3 A TRP B 2   ? 0.2466 0.4919 0.3677 -0.0503 -0.0030 -0.0973 1   TRP D CZ3 
1154 C CZ3 B TRP B 2   ? 0.2756 0.5222 0.4065 -0.0486 -0.0143 -0.0827 1   TRP D CZ3 
1155 C CH2 A TRP B 2   ? 0.2575 0.5029 0.3785 -0.0498 -0.0030 -0.1036 1   TRP D CH2 
1156 C CH2 B TRP B 2   ? 0.2797 0.5294 0.4141 -0.0480 -0.0154 -0.0834 1   TRP D CH2 
1157 N N   . VAL B 3   ? 0.2222 0.4700 0.3535 -0.0510 -0.0092 -0.0833 2   VAL D N   
1158 C CA  . VAL B 3   ? 0.2159 0.4640 0.3503 -0.0512 -0.0098 -0.0837 2   VAL D CA  
1159 C C   . VAL B 3   ? 0.2471 0.4931 0.3820 -0.0499 -0.0107 -0.0835 2   VAL D C   
1160 O O   . VAL B 3   ? 0.2376 0.4827 0.3702 -0.0497 -0.0099 -0.0829 2   VAL D O   
1161 C CB  . VAL B 3   ? 0.2519 0.5038 0.3906 -0.0538 -0.0083 -0.0857 2   VAL D CB  
1162 C CG1 . VAL B 3   ? 0.2533 0.5060 0.3892 -0.0566 -0.0077 -0.0854 2   VAL D CG1 
1163 C CG2 . VAL B 3   ? 0.2401 0.4956 0.3827 -0.0539 -0.0064 -0.0865 2   VAL D CG2 
1164 N N   . ILE B 4   ? 0.2205 0.4654 0.3581 -0.0492 -0.0126 -0.0845 3   ILE D N   
1165 C CA  . ILE B 4   ? 0.2376 0.4792 0.3759 -0.0481 -0.0150 -0.0842 3   ILE D CA  
1166 C C   . ILE B 4   ? 0.2749 0.5194 0.4206 -0.0491 -0.0148 -0.0866 3   ILE D C   
1167 O O   . ILE B 4   ? 0.2676 0.5154 0.4193 -0.0503 -0.0150 -0.0904 3   ILE D O   
1168 C CB  . ILE B 4   ? 0.2706 0.5097 0.4097 -0.0463 -0.0181 -0.0854 3   ILE D CB  
1169 C CG1 . ILE B 4   ? 0.2570 0.4966 0.3920 -0.0455 -0.0177 -0.0839 3   ILE D CG1 
1170 C CG2 . ILE B 4   ? 0.2956 0.5295 0.4350 -0.0452 -0.0222 -0.0849 3   ILE D CG2 
1171 C CD1 . ILE B 4   ? 0.2882 0.5268 0.4170 -0.0467 -0.0175 -0.0811 3   ILE D CD1 
1172 N N   . PRO B 5   ? 0.2659 0.5104 0.4122 -0.0493 -0.0139 -0.0855 4   PRO D N   
1173 C CA  . PRO B 5   ? 0.2663 0.5161 0.4227 -0.0504 -0.0136 -0.0884 4   PRO D CA  
1174 C C   . PRO B 5   ? 0.3355 0.5835 0.4998 -0.0500 -0.0186 -0.0914 4   PRO D C   
1175 O O   . PRO B 5   ? 0.3272 0.5676 0.4871 -0.0482 -0.0227 -0.0894 4   PRO D O   
1176 C CB  . PRO B 5   ? 0.2898 0.5394 0.4445 -0.0500 -0.0111 -0.0864 4   PRO D CB  
1177 C CG  . PRO B 5   ? 0.3397 0.5808 0.4833 -0.0494 -0.0124 -0.0829 4   PRO D CG  
1178 C CD  . PRO B 5   ? 0.2867 0.5273 0.4256 -0.0492 -0.0129 -0.0825 4   PRO D CD  
1179 N N   . ALA B 6   ? 0.3005 0.5560 0.4772 -0.0519 -0.0188 -0.0967 5   ALA D N   
# 
