data_7GUQ
# 
_entry.id   7GUQ 
# 
_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   7GUQ         pdb_00007guq 10.2210/pdb7guq/pdb 
WWPDB D_1001406661 ?            ?                   
# 
_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                        7GUQ 
_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 81  HOH HOH A . 
F 6 HOH 3   303 88  HOH HOH A . 
F 6 HOH 4   304 84  HOH HOH A . 
F 6 HOH 5   305 189 HOH HOH A . 
F 6 HOH 6   306 23  HOH HOH A . 
F 6 HOH 7   307 15  HOH HOH A . 
F 6 HOH 8   308 32  HOH HOH A . 
F 6 HOH 9   309 63  HOH HOH A . 
F 6 HOH 10  310 159 HOH HOH A . 
F 6 HOH 11  311 230 HOH HOH A . 
F 6 HOH 12  312 85  HOH HOH A . 
F 6 HOH 13  313 130 HOH HOH A . 
F 6 HOH 14  314 149 HOH HOH A . 
F 6 HOH 15  315 114 HOH HOH A . 
F 6 HOH 16  316 92  HOH HOH A . 
F 6 HOH 17  317 187 HOH HOH A . 
F 6 HOH 18  318 143 HOH HOH A . 
F 6 HOH 19  319 166 HOH HOH A . 
F 6 HOH 20  320 14  HOH HOH A . 
F 6 HOH 21  321 5   HOH HOH A . 
F 6 HOH 22  322 87  HOH HOH A . 
F 6 HOH 23  323 83  HOH HOH A . 
F 6 HOH 24  324 24  HOH HOH A . 
F 6 HOH 25  325 196 HOH HOH A . 
F 6 HOH 26  326 109 HOH HOH A . 
F 6 HOH 27  327 49  HOH HOH A . 
F 6 HOH 28  328 33  HOH HOH A . 
F 6 HOH 29  329 134 HOH HOH A . 
F 6 HOH 30  330 135 HOH HOH A . 
F 6 HOH 31  331 103 HOH HOH A . 
F 6 HOH 32  332 35  HOH HOH A . 
F 6 HOH 33  333 113 HOH HOH A . 
F 6 HOH 34  334 105 HOH HOH A . 
F 6 HOH 35  335 3   HOH HOH A . 
F 6 HOH 36  336 100 HOH HOH A . 
F 6 HOH 37  337 90  HOH HOH A . 
F 6 HOH 38  338 141 HOH HOH A . 
F 6 HOH 39  339 97  HOH HOH A . 
F 6 HOH 40  340 112 HOH HOH A . 
F 6 HOH 41  341 94  HOH HOH A . 
F 6 HOH 42  342 165 HOH HOH A . 
F 6 HOH 43  343 50  HOH HOH A . 
F 6 HOH 44  344 184 HOH HOH A . 
F 6 HOH 45  345 25  HOH HOH A . 
F 6 HOH 46  346 180 HOH HOH A . 
F 6 HOH 47  347 213 HOH HOH A . 
F 6 HOH 48  348 86  HOH HOH A . 
F 6 HOH 49  349 107 HOH HOH A . 
F 6 HOH 50  350 123 HOH HOH A . 
F 6 HOH 51  351 11  HOH HOH A . 
F 6 HOH 52  352 13  HOH HOH A . 
F 6 HOH 53  353 117 HOH HOH A . 
F 6 HOH 54  354 51  HOH HOH A . 
F 6 HOH 55  355 18  HOH HOH A . 
F 6 HOH 56  356 26  HOH HOH A . 
F 6 HOH 57  357 74  HOH HOH A . 
F 6 HOH 58  358 110 HOH HOH A . 
F 6 HOH 59  359 192 HOH HOH A . 
F 6 HOH 60  360 136 HOH HOH A . 
F 6 HOH 61  361 95  HOH HOH A . 
F 6 HOH 62  362 115 HOH HOH A . 
F 6 HOH 63  363 116 HOH HOH A . 
F 6 HOH 64  364 102 HOH HOH A . 
F 6 HOH 65  365 6   HOH HOH A . 
F 6 HOH 66  366 151 HOH HOH A . 
F 6 HOH 67  367 121 HOH HOH A . 
F 6 HOH 68  368 20  HOH HOH A . 
F 6 HOH 69  369 150 HOH HOH A . 
F 6 HOH 70  370 231 HOH HOH A . 
F 6 HOH 71  371 178 HOH HOH A . 
F 6 HOH 72  372 28  HOH HOH A . 
F 6 HOH 73  373 62  HOH HOH A . 
F 6 HOH 74  374 244 HOH HOH A . 
F 6 HOH 75  375 147 HOH HOH A . 
F 6 HOH 76  376 119 HOH HOH A . 
F 6 HOH 77  377 104 HOH HOH A . 
F 6 HOH 78  378 101 HOH HOH A . 
F 6 HOH 79  379 89  HOH HOH A . 
F 6 HOH 80  380 57  HOH HOH A . 
F 6 HOH 81  381 66  HOH HOH A . 
F 6 HOH 82  382 22  HOH HOH A . 
F 6 HOH 83  383 168 HOH HOH A . 
F 6 HOH 84  384 164 HOH HOH A . 
F 6 HOH 85  385 29  HOH HOH A . 
F 6 HOH 86  386 10  HOH HOH A . 
F 6 HOH 87  387 56  HOH HOH A . 
F 6 HOH 88  388 60  HOH HOH A . 
F 6 HOH 89  389 40  HOH HOH A . 
F 6 HOH 90  390 21  HOH HOH A . 
F 6 HOH 91  391 238 HOH HOH A . 
F 6 HOH 92  392 39  HOH HOH A . 
F 6 HOH 93  393 82  HOH HOH A . 
F 6 HOH 94  394 99  HOH HOH A . 
F 6 HOH 95  395 69  HOH HOH A . 
F 6 HOH 96  396 44  HOH HOH A . 
F 6 HOH 97  397 246 HOH HOH A . 
F 6 HOH 98  398 27  HOH HOH A . 
F 6 HOH 99  399 38  HOH HOH A . 
F 6 HOH 100 400 193 HOH HOH A . 
F 6 HOH 101 401 52  HOH HOH A . 
F 6 HOH 102 402 37  HOH HOH A . 
F 6 HOH 103 403 30  HOH HOH A . 
F 6 HOH 104 404 75  HOH HOH A . 
F 6 HOH 105 405 96  HOH HOH A . 
F 6 HOH 106 406 237 HOH HOH A . 
F 6 HOH 107 407 167 HOH HOH A . 
F 6 HOH 108 408 36  HOH HOH A . 
F 6 HOH 109 409 176 HOH HOH A . 
F 6 HOH 110 410 242 HOH HOH A . 
F 6 HOH 111 411 53  HOH HOH A . 
F 6 HOH 112 412 55  HOH HOH A . 
F 6 HOH 113 413 17  HOH HOH A . 
F 6 HOH 114 414 241 HOH HOH A . 
F 6 HOH 115 415 203 HOH HOH A . 
F 6 HOH 116 416 209 HOH HOH A . 
F 6 HOH 117 417 45  HOH HOH A . 
F 6 HOH 118 418 153 HOH HOH A . 
F 6 HOH 119 419 200 HOH HOH A . 
F 6 HOH 120 420 93  HOH HOH A . 
F 6 HOH 121 421 171 HOH HOH A . 
F 6 HOH 122 422 54  HOH HOH A . 
F 6 HOH 123 423 43  HOH HOH A . 
F 6 HOH 124 424 239 HOH HOH A . 
F 6 HOH 125 425 186 HOH HOH A . 
F 6 HOH 126 426 146 HOH HOH A . 
F 6 HOH 127 427 31  HOH HOH A . 
F 6 HOH 128 428 98  HOH HOH A . 
F 6 HOH 129 429 145 HOH HOH A . 
F 6 HOH 130 430 79  HOH HOH A . 
F 6 HOH 131 431 148 HOH HOH A . 
F 6 HOH 132 432 191 HOH HOH A . 
F 6 HOH 133 433 106 HOH HOH A . 
F 6 HOH 134 434 188 HOH HOH A . 
F 6 HOH 135 435 185 HOH HOH A . 
F 6 HOH 136 436 139 HOH HOH A . 
F 6 HOH 137 437 232 HOH HOH A . 
F 6 HOH 138 438 80  HOH HOH A . 
F 6 HOH 139 439 158 HOH HOH A . 
F 6 HOH 140 440 221 HOH HOH A . 
F 6 HOH 141 441 76  HOH HOH A . 
F 6 HOH 142 442 137 HOH HOH A . 
F 6 HOH 143 443 204 HOH HOH A . 
F 6 HOH 144 444 111 HOH HOH A . 
F 6 HOH 145 445 140 HOH HOH A . 
F 6 HOH 146 446 108 HOH HOH A . 
F 6 HOH 147 447 169 HOH HOH A . 
F 6 HOH 148 448 206 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 70  HOH HOH A . 
F 6 HOH 152 452 243 HOH HOH A . 
F 6 HOH 153 453 131 HOH HOH A . 
F 6 HOH 154 454 212 HOH HOH A . 
F 6 HOH 155 455 215 HOH HOH A . 
F 6 HOH 156 456 183 HOH HOH A . 
F 6 HOH 157 457 73  HOH HOH A . 
F 6 HOH 158 458 59  HOH HOH A . 
F 6 HOH 159 459 175 HOH HOH A . 
F 6 HOH 160 460 228 HOH HOH A . 
F 6 HOH 161 461 142 HOH HOH A . 
F 6 HOH 162 462 245 HOH HOH A . 
F 6 HOH 163 463 179 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 61  HOH HOH A . 
F 6 HOH 169 469 152 HOH HOH A . 
F 6 HOH 170 470 208 HOH HOH A . 
F 6 HOH 171 471 233 HOH HOH A . 
F 6 HOH 172 472 144 HOH HOH A . 
F 6 HOH 173 473 225 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   206 220 HOH HOH D . 
G 6 HOH 7   207 240 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           7GUQ 
_cell.length_a           67.570 
_cell.length_b           67.570 
_cell.length_c           166.070 
_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                         7GUQ 
_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          7GUQ 
_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                     7GUQ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.860 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   21706 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.147 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        6.800 
_reflns.B_iso_Wilson_estimate        32.420 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.156 
_reflns.pdbx_Rpim_I_all              0.051 
_reflns.pdbx_CC_half                 0.993 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     196607 
_reflns.pdbx_scaling_rejects         38 
_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  ? 11606 1249 ? 2.116 ? ? ? 9.300 ? 1.000  ? ? ? ? ? ? 100.000 2.240 0.727 0.602 ? 
1 2 9.000 33.860 ? 1655  240  ? 0.117 ? ? ? 6.900 ? 14.800 ? ? ? ? ? ? 98.800  0.126 0.043 0.994 ? 
# 
_refine.entry_id                                 7GUQ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.8000 
_refine.ls_d_res_low                             33.8600 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.9000 
_refine.ls_number_reflns_obs                     21616 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1810 
_refine.ls_R_factor_R_work                       0.1790 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2070 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.2000 
_refine.ls_number_reflns_R_free                  1125 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               39.1300 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.6171 
_refine.aniso_B[2][2]                            -0.6171 
_refine.aniso_B[3][3]                            1.2343 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9620 
_refine.correlation_coeff_Fo_to_Fc_free          0.9530 
_refine.overall_SU_R_Cruickshank_DPI             0.0940 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0940 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1080 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.1030 
_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                                139.890 
_refine.B_iso_min                                20.270 
_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                        7GUQ 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.210 
_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                        33.8600 
_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           33.60 
_refine_hist.pdbx_B_iso_mean_solvent          57.41 
_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      1640 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1236 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1693 0.900  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.350  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    16.240 ? ?      ?            
# 
_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               99.7900 
_refine_ls_shell.number_reflns_R_work             2677 
_refine_ls_shell.R_factor_all                     0.2644 
_refine_ls_shell.R_factor_R_work                  0.2634 
_refine_ls_shell.R_factor_R_free                  0.2832 
_refine_ls_shell.percent_reflns_R_free            4.6700 
_refine_ls_shell.number_reflns_R_free             131 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2808 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUQ 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 1 at 21.14 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUQ 
_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 7GUQ       7GUQ   ? 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 7GUQ A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUQ D 1 ? 6   ? 7GUQ   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 7GUQ GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUQ PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUQ 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)' 6380  ? 
1 MORE         -68   ? 
1 'SSA (A^2)'  13280 ? 
# 
_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 33.7850000000 0.8660254038 
-0.5000000000 0.0000000000 -58.5173365337 0.0000000000 0.0000000000 -1.0000000000 27.6783333333 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ARG A 12  ? ARG A 27  ? ARG A 13  ARG A 28  1 ? 16 
HELX_P HELX_P2 AA2 HIS A 45  ? SER A 53  ? HIS A 46  SER A 54  1 ? 9  
HELX_P HELX_P3 AA3 SER A 53  ? THR A 61  ? SER A 54  THR A 62  1 ? 9  
HELX_P HELX_P4 AA4 LEU A 64  ? LEU A 68  ? LEU A 65  LEU A 69  5 ? 5  
HELX_P HELX_P5 AA5 ASN A 78  ? SER A 92  ? ASN A 79  SER A 93  1 ? 15 
HELX_P HELX_P6 AA6 ASN A 100 ? GLN A 112 ? ASN A 101 GLN A 113 1 ? 13 
HELX_P HELX_P7 AA7 MET A 113 ? GLU A 128 ? MET A 114 GLU A 129 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N A ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 ACE B 1 ? TRP B 2 A ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
2 ACE B 1 ? TRP B 2 B ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 40 ? ALA A 44 ? GLU A 41 ALA A 45 
AA1 2 VAL A 33 ? VAL A 37 ? VAL A 34 VAL A 38 
AA1 3 VAL A 70 ? ASN A 72 ? VAL A 71 ASN A 73 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O 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                   7GUQ 
_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 39.06   49.09   
2 1 SER A 39  ? B 60.25   -111.69 
3 1 SER A 93  ? ? 77.80   -2.48   
4 1 SER A 93  ? ? 77.80   -3.83   
5 1 GLN A 113 ? ? 62.31   63.90   
6 1 MET A 114 ? ? -119.78 79.08   
# 
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 342 ? F HOH . 
2 1 A HOH 384 ? F HOH . 
3 1 A HOH 447 ? F HOH . 
4 1 A HOH 459 ? F HOH . 
5 1 A HOH 463 ? 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 -0.0041 -0.0606 -0.0512 -0.0390 0.0268  -0.0180 1.0429 1.9504 2.2664 
0.4086 -0.3185 1.2906 0.1384 -0.0916 -0.0468 -0.0653 0.0982 0.0793 0.2669  0.0125 -0.0567 
'X-RAY DIFFRACTION' 2 ? refined 18.9623 -32.3913 1.8231  -0.1150 0.1192  -0.0279 -0.0532 -0.0114 -0.0922 0.4341 0.3203 0.0000 
0.4027 -0.1121 0.3692 0.0158 0.0021  -0.0179 -0.0023 0.0152 0.0348 -0.0061 0.0121 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                    7GUQ 
_atom_sites.fract_transf_matrix[1][1]   0.014799 
_atom_sites.fract_transf_matrix[1][2]   0.008544 
_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]   0.017089 
_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]   0.006022 
_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   ? 17.520 -21.173 -4.958 1.00 70.86  ? 6   ASP A N   1 
ATOM   2    C  CA  . ASP A 1 5   ? 18.398 -22.080 -5.702 1.00 69.73  ? 6   ASP A CA  1 
ATOM   3    C  C   . ASP A 1 5   ? 17.906 -23.547 -5.622 1.00 69.50  ? 6   ASP A C   1 
ATOM   4    O  O   . ASP A 1 5   ? 16.813 -23.808 -5.107 1.00 70.11  ? 6   ASP A O   1 
ATOM   5    C  CB  . ASP A 1 5   ? 19.853 -21.953 -5.186 1.00 70.40  ? 6   ASP A CB  1 
ATOM   6    C  CG  . ASP A 1 5   ? 20.907 -22.002 -6.283 1.00 84.04  ? 6   ASP A CG  1 
ATOM   7    O  OD1 . ASP A 1 5   ? 20.996 -23.043 -6.983 1.00 84.65  ? 6   ASP A OD1 1 
ATOM   8    O  OD2 . ASP A 1 5   ? 21.653 -21.008 -6.435 1.00 90.62  ? 6   ASP A OD2 1 
ATOM   9    N  N   . SER A 1 6   ? 18.713 -24.492 -6.144 1.00 60.94  ? 7   SER A N   1 
ATOM   10   C  CA  . SER A 1 6   ? 18.427 -25.926 -6.125 1.00 58.35  ? 7   SER A CA  1 
ATOM   11   C  C   . SER A 1 6   ? 19.412 -26.682 -5.178 1.00 54.46  ? 7   SER A C   1 
ATOM   12   O  O   . SER A 1 6   ? 19.720 -27.858 -5.400 1.00 53.97  ? 7   SER A O   1 
ATOM   13   C  CB  . SER A 1 6   ? 18.483 -26.485 -7.542 1.00 63.75  ? 7   SER A CB  1 
ATOM   14   O  OG  . SER A 1 6   ? 19.757 -26.288 -8.133 1.00 75.29  ? 7   SER A OG  1 
ATOM   15   N  N   . CYS A 1 7   ? 19.881 -26.002 -4.114 1.00 44.93  ? 8   CYS A N   1 
ATOM   16   C  CA  . CYS A 1 7   ? 20.817 -26.566 -3.134 1.00 41.18  ? 8   CYS A CA  1 
ATOM   17   C  C   . CYS A 1 7   ? 20.210 -27.736 -2.334 1.00 40.46  ? 8   CYS A C   1 
ATOM   18   O  O   . CYS A 1 7   ? 18.995 -27.795 -2.162 1.00 41.20  ? 8   CYS A O   1 
ATOM   19   C  CB  . CYS A 1 7   ? 21.286 -25.466 -2.180 1.00 41.74  ? 8   CYS A CB  1 
ATOM   20   S  SG  . CYS A 1 7   ? 22.431 -24.256 -2.912 1.00 46.64  ? 8   CYS A SG  1 
ATOM   21   N  N   . ILE A 1 8   ? 21.056 -28.635 -1.810 1.00 30.99  ? 9   ILE A N   1 
ATOM   22   C  CA  . ILE A 1 8   ? 20.674 -29.637 -0.805 1.00 28.64  ? 9   ILE A CA  1 
ATOM   23   C  C   . ILE A 1 8   ? 21.271 -29.096 0.492  1.00 30.25  ? 9   ILE A C   1 
ATOM   24   O  O   . ILE A 1 8   ? 22.214 -28.309 0.435  1.00 29.32  ? 9   ILE A O   1 
ATOM   25   C  CB  . ILE A 1 8   ? 21.047 -31.116 -1.111 1.00 31.72  ? 9   ILE A CB  1 
ATOM   26   C  CG1 . ILE A 1 8   ? 22.558 -31.283 -1.420 1.00 31.77  ? 9   ILE A CG1 1 
ATOM   27   C  CG2 . ILE A 1 8   ? 20.169 -31.646 -2.252 1.00 33.98  ? 9   ILE A CG2 1 
ATOM   28   C  CD1 . ILE A 1 8   ? 23.068 -32.736 -1.573 1.00 34.44  ? 9   ILE A CD1 1 
ATOM   29   N  N   A GLN A 1 9   ? 20.771 -29.509 1.656  0.57 25.11  ? 10  GLN A N   1 
ATOM   30   N  N   B GLN A 1 9   ? 20.682 -29.450 1.637  0.43 25.69  ? 10  GLN A N   1 
ATOM   31   C  CA  A GLN A 1 9   ? 21.304 -28.980 2.911  0.57 23.42  ? 10  GLN A CA  1 
ATOM   32   C  CA  B GLN A 1 9   ? 21.115 -28.964 2.943  0.43 24.23  ? 10  GLN A CA  1 
ATOM   33   C  C   A GLN A 1 9   ? 21.646 -30.103 3.892  0.57 26.46  ? 10  GLN A C   1 
ATOM   34   C  C   B GLN A 1 9   ? 21.579 -30.116 3.827  0.43 26.79  ? 10  GLN A C   1 
ATOM   35   O  O   A GLN A 1 9   ? 20.851 -31.024 4.063  0.57 25.97  ? 10  GLN A O   1 
ATOM   36   O  O   B GLN A 1 9   ? 20.940 -31.164 3.855  0.43 26.64  ? 10  GLN A O   1 
ATOM   37   C  CB  A GLN A 1 9   ? 20.278 -27.995 3.523  0.57 25.01  ? 10  GLN A CB  1 
ATOM   38   C  CB  B GLN A 1 9   ? 19.952 -28.194 3.620  0.43 25.71  ? 10  GLN A CB  1 
ATOM   39   C  CG  A GLN A 1 9   ? 20.725 -27.318 4.819  0.57 24.38  ? 10  GLN A CG  1 
ATOM   40   C  CG  B GLN A 1 9   ? 20.151 -27.911 5.127  0.43 34.28  ? 10  GLN A CG  1 
ATOM   41   C  CD  A GLN A 1 9   ? 19.568 -26.671 5.542  0.57 52.42  ? 10  GLN A CD  1 
ATOM   42   C  CD  B GLN A 1 9   ? 20.055 -26.458 5.515  0.43 42.36  ? 10  GLN A CD  1 
ATOM   43   O  OE1 A GLN A 1 9   ? 18.601 -27.323 5.951  0.57 44.76  ? 10  GLN A OE1 1 
ATOM   44   O  OE1 B GLN A 1 9   ? 19.711 -25.581 4.708  0.43 31.57  ? 10  GLN A OE1 1 
ATOM   45   N  NE2 A GLN A 1 9   ? 19.645 -25.365 5.726  0.57 55.65  ? 10  GLN A NE2 1 
ATOM   46   N  NE2 B GLN A 1 9   ? 20.362 -26.173 6.780  0.43 32.18  ? 10  GLN A NE2 1 
ATOM   47   N  N   A PHE A 1 10  ? 22.810 -30.018 4.551  0.78 24.49  ? 11  PHE A N   1 
ATOM   48   N  N   B PHE A 1 10  ? 22.659 -29.898 4.579  0.22 23.38  ? 11  PHE A N   1 
ATOM   49   C  CA  A PHE A 1 10  ? 23.198 -31.024 5.541  0.78 24.36  ? 11  PHE A CA  1 
ATOM   50   C  CA  B PHE A 1 10  ? 23.168 -30.872 5.532  0.22 23.07  ? 11  PHE A CA  1 
ATOM   51   C  C   A PHE A 1 10  ? 22.718 -30.534 6.901  0.78 26.96  ? 11  PHE A C   1 
ATOM   52   C  C   B PHE A 1 10  ? 22.653 -30.422 6.882  0.22 26.67  ? 11  PHE A C   1 
ATOM   53   O  O   A PHE A 1 10  ? 23.279 -29.581 7.460  0.78 25.78  ? 11  PHE A O   1 
ATOM   54   O  O   B PHE A 1 10  ? 23.104 -29.394 7.403  0.22 25.54  ? 11  PHE A O   1 
ATOM   55   C  CB  A PHE A 1 10  ? 24.724 -31.314 5.505  0.78 25.52  ? 11  PHE A CB  1 
ATOM   56   C  CB  B PHE A 1 10  ? 24.701 -30.938 5.467  0.22 24.19  ? 11  PHE A CB  1 
ATOM   57   C  CG  A PHE A 1 10  ? 25.106 -32.509 6.356  0.78 26.93  ? 11  PHE A CG  1 
ATOM   58   C  CG  B PHE A 1 10  ? 25.185 -31.854 4.370  0.22 26.31  ? 11  PHE A CG  1 
ATOM   59   C  CD1 A PHE A 1 10  ? 24.686 -33.796 6.013  0.78 31.01  ? 11  PHE A CD1 1 
ATOM   60   C  CD1 B PHE A 1 10  ? 25.038 -31.504 3.030  0.22 30.03  ? 11  PHE A CD1 1 
ATOM   61   C  CD2 A PHE A 1 10  ? 25.912 -32.355 7.479  0.78 28.86  ? 11  PHE A CD2 1 
ATOM   62   C  CD2 B PHE A 1 10  ? 25.760 -33.080 4.671  0.22 29.19  ? 11  PHE A CD2 1 
ATOM   63   C  CE1 A PHE A 1 10  ? 25.023 -34.898 6.816  0.78 32.11  ? 11  PHE A CE1 1 
ATOM   64   C  CE1 B PHE A 1 10  ? 25.480 -32.354 2.016  0.22 31.36  ? 11  PHE A CE1 1 
ATOM   65   C  CE2 A PHE A 1 10  ? 26.237 -33.451 8.285  0.78 30.86  ? 11  PHE A CE2 1 
ATOM   66   C  CE2 B PHE A 1 10  ? 26.192 -33.933 3.653  0.22 32.72  ? 11  PHE A CE2 1 
ATOM   67   C  CZ  A PHE A 1 10  ? 25.799 -34.714 7.946  0.78 29.30  ? 11  PHE A CZ  1 
ATOM   68   C  CZ  B PHE A 1 10  ? 26.063 -33.558 2.337  0.22 30.82  ? 11  PHE A CZ  1 
ATOM   69   N  N   . THR A 1 11  ? 21.631 -31.133 7.398  1.00 24.02  ? 12  THR A N   1 
ATOM   70   C  CA  . THR A 1 11  ? 20.958 -30.756 8.659  1.00 24.08  ? 12  THR A CA  1 
ATOM   71   C  C   . THR A 1 11  ? 21.909 -30.515 9.859  1.00 28.05  ? 12  THR A C   1 
ATOM   72   O  O   . THR A 1 11  ? 21.781 -29.490 10.540 1.00 27.09  ? 12  THR A O   1 
ATOM   73   C  CB  . THR A 1 11  ? 19.883 -31.796 9.014  1.00 31.71  ? 12  THR A CB  1 
ATOM   74   O  OG1 . THR A 1 11  ? 18.946 -31.878 7.918  1.00 32.01  ? 12  THR A OG1 1 
ATOM   75   C  CG2 . THR A 1 11  ? 19.108 -31.430 10.305 1.00 35.38  ? 12  THR A CG2 1 
ATOM   76   N  N   A ARG A 1 12  ? 22.850 -31.445 10.092 0.50 25.31  ? 13  ARG A N   1 
ATOM   77   N  N   B ARG A 1 12  ? 22.846 -31.449 10.098 0.50 25.48  ? 13  ARG A N   1 
ATOM   78   C  CA  A ARG A 1 12  ? 23.763 -31.377 11.241 0.50 25.45  ? 13  ARG A CA  1 
ATOM   79   C  CA  B ARG A 1 12  ? 23.772 -31.385 11.238 0.50 25.70  ? 13  ARG A CA  1 
ATOM   80   C  C   A ARG A 1 12  ? 25.017 -30.505 11.046 0.50 27.40  ? 13  ARG A C   1 
ATOM   81   C  C   B ARG A 1 12  ? 25.009 -30.491 11.053 0.50 27.46  ? 13  ARG A C   1 
ATOM   82   O  O   A ARG A 1 12  ? 25.822 -30.407 11.981 0.50 25.96  ? 13  ARG A O   1 
ATOM   83   O  O   B ARG A 1 12  ? 25.802 -30.372 11.996 0.50 25.97  ? 13  ARG A O   1 
ATOM   84   C  CB  A ARG A 1 12  ? 24.175 -32.802 11.674 0.50 28.06  ? 13  ARG A CB  1 
ATOM   85   C  CB  B ARG A 1 12  ? 24.218 -32.807 11.620 0.50 28.78  ? 13  ARG A CB  1 
ATOM   86   C  CG  A ARG A 1 12  ? 23.022 -33.685 12.198 0.50 37.13  ? 13  ARG A CG  1 
ATOM   87   C  CG  B ARG A 1 12  ? 23.266 -33.513 12.592 0.50 40.68  ? 13  ARG A CG  1 
ATOM   88   C  CD  A ARG A 1 12  ? 22.463 -33.221 13.536 0.50 48.48  ? 13  ARG A CD  1 
ATOM   89   C  CD  B ARG A 1 12  ? 23.002 -34.969 12.247 0.50 48.02  ? 13  ARG A CD  1 
ATOM   90   N  NE  A ARG A 1 12  ? 23.412 -33.397 14.639 0.50 53.58  ? 13  ARG A NE  1 
ATOM   91   N  NE  B ARG A 1 12  ? 24.219 -35.742 11.974 0.50 53.38  ? 13  ARG A NE  1 
ATOM   92   C  CZ  A ARG A 1 12  ? 23.375 -32.713 15.779 0.50 59.82  ? 13  ARG A CZ  1 
ATOM   93   C  CZ  B ARG A 1 12  ? 24.435 -36.429 10.855 0.50 62.47  ? 13  ARG A CZ  1 
ATOM   94   N  NH1 A ARG A 1 12  ? 22.448 -31.783 15.976 0.50 40.17  ? 13  ARG A NH1 1 
ATOM   95   N  NH1 B ARG A 1 12  ? 25.562 -37.109 10.693 0.50 52.98  ? 13  ARG A NH1 1 
ATOM   96   N  NH2 A ARG A 1 12  ? 24.270 -32.948 16.727 0.50 47.04  ? 13  ARG A NH2 1 
ATOM   97   N  NH2 B ARG A 1 12  ? 23.518 -36.453 9.895  0.50 38.76  ? 13  ARG A NH2 1 
ATOM   98   N  N   . HIS A 1 13  ? 25.184 -29.874 9.863  1.00 23.58  ? 14  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 13  ? 26.385 -29.070 9.557  1.00 22.92  ? 14  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 13  ? 26.664 -27.965 10.560 1.00 23.96  ? 14  HIS A C   1 
ATOM   101  O  O   . HIS A 1 13  ? 27.799 -27.876 11.033 1.00 23.41  ? 14  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 13  ? 26.371 -28.494 8.134  1.00 23.07  ? 14  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 13  ? 27.648 -27.761 7.817  1.00 24.56  ? 14  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 13  ? 28.826 -28.439 7.629  1.00 25.38  ? 14  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 13  ? 27.881 -26.435 7.692  1.00 25.64  ? 14  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 13  ? 29.743 -27.520 7.365  1.00 24.67  ? 14  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 13  ? 29.217 -26.296 7.382  1.00 25.07  ? 14  HIS A NE2 1 
ATOM   108  N  N   . ALA A 1 14  ? 25.674 -27.086 10.830 1.00 21.87  ? 15  ALA A N   1 
ATOM   109  C  CA  . ALA A 1 14  ? 25.892 -25.955 11.764 1.00 21.95  ? 15  ALA A CA  1 
ATOM   110  C  C   . ALA A 1 14  ? 26.320 -26.438 13.172 1.00 24.63  ? 15  ALA A C   1 
ATOM   111  O  O   . ALA A 1 14  ? 27.242 -25.865 13.754 1.00 21.73  ? 15  ALA A O   1 
ATOM   112  C  CB  . ALA A 1 14  ? 24.637 -25.081 11.836 1.00 23.59  ? 15  ALA A CB  1 
ATOM   113  N  N   A SER A 1 15  ? 25.650 -27.479 13.695 0.38 22.87  ? 16  SER A N   1 
ATOM   114  N  N   B SER A 1 15  ? 25.654 -27.484 13.697 0.33 22.91  ? 16  SER A N   1 
ATOM   115  N  N   C SER A 1 15  ? 25.650 -27.481 13.705 0.29 22.25  ? 16  SER A N   1 
ATOM   116  C  CA  A SER A 1 15  ? 25.935 -28.071 14.997 0.38 23.39  ? 16  SER A CA  1 
ATOM   117  C  CA  B SER A 1 15  ? 25.943 -28.073 15.003 0.33 23.44  ? 16  SER A CA  1 
ATOM   118  C  CA  C SER A 1 15  ? 25.956 -28.050 15.019 0.29 22.45  ? 16  SER A CA  1 
ATOM   119  C  C   A SER A 1 15  ? 27.349 -28.662 15.027 0.38 26.96  ? 16  SER A C   1 
ATOM   120  C  C   B SER A 1 15  ? 27.351 -28.668 15.032 0.33 27.11  ? 16  SER A C   1 
ATOM   121  C  C   C SER A 1 15  ? 27.354 -28.677 15.043 0.29 26.77  ? 16  SER A C   1 
ATOM   122  O  O   A SER A 1 15  ? 28.072 -28.446 16.002 0.38 24.95  ? 16  SER A O   1 
ATOM   123  O  O   B SER A 1 15  ? 28.072 -28.466 16.012 0.33 25.35  ? 16  SER A O   1 
ATOM   124  O  O   C SER A 1 15  ? 28.071 -28.502 16.030 0.29 25.22  ? 16  SER A O   1 
ATOM   125  C  CB  A SER A 1 15  ? 24.892 -29.136 15.334 0.38 27.81  ? 16  SER A CB  1 
ATOM   126  C  CB  B SER A 1 15  ? 24.906 -29.138 15.355 0.33 28.02  ? 16  SER A CB  1 
ATOM   127  C  CB  C SER A 1 15  ? 24.891 -29.060 15.441 0.29 25.80  ? 16  SER A CB  1 
ATOM   128  O  OG  A SER A 1 15  ? 25.126 -29.701 16.612 0.38 33.38  ? 16  SER A OG  1 
ATOM   129  O  OG  B SER A 1 15  ? 23.596 -28.596 15.348 0.33 34.70  ? 16  SER A OG  1 
ATOM   130  O  OG  C SER A 1 15  ? 24.852 -30.174 14.564 0.29 27.96  ? 16  SER A OG  1 
ATOM   131  N  N   . ASP A 1 16  ? 27.749 -29.373 13.951 1.00 24.69  ? 17  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 16  ? 29.094 -29.984 13.824 1.00 25.63  ? 17  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 16  ? 30.152 -28.879 13.774 1.00 26.54  ? 17  ASP A C   1 
ATOM   134  O  O   . ASP A 1 16  ? 31.213 -29.021 14.389 1.00 26.20  ? 17  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 16  ? 29.196 -30.848 12.560 1.00 27.30  ? 17  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 16  ? 28.419 -32.158 12.616 1.00 39.36  ? 17  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 16  ? 27.852 -32.473 13.690 1.00 39.99  ? 17  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 16  ? 28.372 -32.865 11.582 1.00 38.88  ? 17  ASP A OD2 1 
ATOM   139  N  N   . VAL A 1 17  ? 29.861 -27.772 13.048 1.00 21.82  ? 18  VAL A N   1 
ATOM   140  C  CA  . VAL A 1 17  ? 30.810 -26.642 13.017 1.00 21.12  ? 18  VAL A CA  1 
ATOM   141  C  C   . VAL A 1 17  ? 31.006 -26.081 14.443 1.00 23.69  ? 18  VAL A C   1 
ATOM   142  O  O   . VAL A 1 17  ? 32.134 -25.881 14.887 1.00 22.75  ? 18  VAL A O   1 
ATOM   143  C  CB  . VAL A 1 17  ? 30.356 -25.527 12.032 1.00 22.89  ? 18  VAL A CB  1 
ATOM   144  C  CG1 . VAL A 1 17  ? 31.139 -24.231 12.263 1.00 22.13  ? 18  VAL A CG1 1 
ATOM   145  C  CG2 . VAL A 1 17  ? 30.475 -25.999 10.581 1.00 22.44  ? 18  VAL A CG2 1 
ATOM   146  N  N   . LEU A 1 18  ? 29.909 -25.843 15.166 1.00 21.63  ? 19  LEU A N   1 
ATOM   147  C  CA  . LEU A 1 18  ? 30.016 -25.254 16.505 1.00 21.86  ? 19  LEU A CA  1 
ATOM   148  C  C   . LEU A 1 18  ? 30.758 -26.193 17.480 1.00 25.10  ? 19  LEU A C   1 
ATOM   149  O  O   . LEU A 1 18  ? 31.595 -25.726 18.272 1.00 22.11  ? 19  LEU A O   1 
ATOM   150  C  CB  . LEU A 1 18  ? 28.629 -24.875 17.042 1.00 22.79  ? 19  LEU A CB  1 
ATOM   151  C  CG  . LEU A 1 18  ? 28.656 -23.913 18.259 1.00 25.78  ? 19  LEU A CG  1 
ATOM   152  C  CD1 . LEU A 1 18  ? 29.181 -22.511 17.869 1.00 25.62  ? 19  LEU A CD1 1 
ATOM   153  C  CD2 . LEU A 1 18  ? 27.269 -23.808 18.879 1.00 30.70  ? 19  LEU A CD2 1 
ATOM   154  N  N   . LEU A 1 19  ? 30.495 -27.501 17.361 1.00 23.93  ? 20  LEU A N   1 
ATOM   155  C  CA  . LEU A 1 19  ? 31.159 -28.542 18.162 1.00 25.29  ? 20  LEU A CA  1 
ATOM   156  C  C   . LEU A 1 19  ? 32.676 -28.481 17.922 1.00 25.78  ? 20  LEU A C   1 
ATOM   157  O  O   . LEU A 1 19  ? 33.459 -28.461 18.892 1.00 24.77  ? 20  LEU A O   1 
ATOM   158  C  CB  . LEU A 1 19  ? 30.601 -29.927 17.794 1.00 27.45  ? 20  LEU A CB  1 
ATOM   159  C  CG  . LEU A 1 19  ? 31.160 -31.110 18.583 1.00 36.40  ? 20  LEU A CG  1 
ATOM   160  C  CD1 . LEU A 1 19  ? 30.630 -31.100 20.027 1.00 39.19  ? 20  LEU A CD1 1 
ATOM   161  C  CD2 . LEU A 1 19  ? 30.752 -32.417 17.929 1.00 40.76  ? 20  LEU A CD2 1 
ATOM   162  N  N   . ASN A 1 20  ? 33.088 -28.367 16.642 1.00 21.84  ? 21  ASN A N   1 
ATOM   163  C  CA  . ASN A 1 20  ? 34.511 -28.251 16.303 1.00 22.15  ? 21  ASN A CA  1 
ATOM   164  C  C   . ASN A 1 20  ? 35.133 -26.950 16.796 1.00 24.50  ? 21  ASN A C   1 
ATOM   165  O  O   . ASN A 1 20  ? 36.282 -26.959 17.236 1.00 23.75  ? 21  ASN A O   1 
ATOM   166  C  CB  . ASN A 1 20  ? 34.724 -28.474 14.817 1.00 23.29  ? 21  ASN A CB  1 
ATOM   167  C  CG  . ASN A 1 20  ? 34.647 -29.947 14.482 1.00 33.89  ? 21  ASN A CG  1 
ATOM   168  O  OD1 . ASN A 1 20  ? 34.801 -30.808 15.356 1.00 30.26  ? 21  ASN A OD1 1 
ATOM   169  N  ND2 . ASN A 1 20  ? 34.375 -30.276 13.224 1.00 26.27  ? 21  ASN A ND2 1 
ATOM   170  N  N   . LEU A 1 21  ? 34.388 -25.827 16.717 1.00 22.15  ? 22  LEU A N   1 
ATOM   171  C  CA  . LEU A 1 21  ? 34.872 -24.546 17.242 1.00 22.21  ? 22  LEU A CA  1 
ATOM   172  C  C   . LEU A 1 21  ? 35.085 -24.682 18.749 1.00 24.32  ? 22  LEU A C   1 
ATOM   173  O  O   . LEU A 1 21  ? 36.078 -24.182 19.284 1.00 22.85  ? 22  LEU A O   1 
ATOM   174  C  CB  . LEU A 1 21  ? 33.878 -23.407 16.934 1.00 21.61  ? 22  LEU A CB  1 
ATOM   175  C  CG  . LEU A 1 21  ? 33.778 -23.042 15.436 1.00 24.16  ? 22  LEU A CG  1 
ATOM   176  C  CD1 . LEU A 1 21  ? 32.707 -21.962 15.219 1.00 23.39  ? 22  LEU A CD1 1 
ATOM   177  C  CD2 . LEU A 1 21  ? 35.138 -22.604 14.859 1.00 26.31  ? 22  LEU A CD2 1 
ATOM   178  N  N   . ASN A 1 22  ? 34.149 -25.367 19.445 1.00 21.78  ? 23  ASN A N   1 
ATOM   179  C  CA  . ASN A 1 22  ? 34.329 -25.566 20.892 1.00 22.12  ? 23  ASN A CA  1 
ATOM   180  C  C   . ASN A 1 22  ? 35.564 -26.464 21.200 1.00 26.35  ? 23  ASN A C   1 
ATOM   181  O  O   . ASN A 1 22  ? 36.265 -26.230 22.188 1.00 26.47  ? 23  ASN A O   1 
ATOM   182  C  CB  . ASN A 1 22  ? 33.070 -26.143 21.526 1.00 22.90  ? 23  ASN A CB  1 
ATOM   183  C  CG  . ASN A 1 22  ? 33.086 -26.011 23.033 1.00 30.24  ? 23  ASN A CG  1 
ATOM   184  O  OD1 . ASN A 1 22  ? 33.557 -25.015 23.595 1.00 28.74  ? 23  ASN A OD1 1 
ATOM   185  N  ND2 . ASN A 1 22  ? 32.575 -27.007 23.701 1.00 31.11  ? 23  ASN A ND2 1 
ATOM   186  N  N   . ARG A 1 23  ? 35.845 -27.472 20.345 1.00 23.73  ? 24  ARG A N   1 
ATOM   187  C  CA  . ARG A 1 23  ? 37.033 -28.336 20.507 1.00 24.55  ? 24  ARG A CA  1 
ATOM   188  C  C   . ARG A 1 23  ? 38.303 -27.506 20.332 1.00 28.14  ? 24  ARG A C   1 
ATOM   189  O  O   . ARG A 1 23  ? 39.240 -27.670 21.101 1.00 27.93  ? 24  ARG A O   1 
ATOM   190  C  CB  . ARG A 1 23  ? 37.023 -29.470 19.476 1.00 24.36  ? 24  ARG A CB  1 
ATOM   191  C  CG  . ARG A 1 23  ? 36.049 -30.583 19.842 1.00 30.83  ? 24  ARG A CG  1 
ATOM   192  C  CD  . ARG A 1 23  ? 35.764 -31.454 18.631 1.00 34.16  ? 24  ARG A CD  1 
ATOM   193  N  NE  . ARG A 1 23  ? 34.916 -32.588 18.978 1.00 40.13  ? 24  ARG A NE  1 
ATOM   194  C  CZ  . ARG A 1 23  ? 34.431 -33.463 18.105 1.00 60.76  ? 24  ARG A CZ  1 
ATOM   195  N  NH1 . ARG A 1 23  ? 34.656 -33.310 16.803 1.00 46.44  ? 24  ARG A NH1 1 
ATOM   196  N  NH2 . ARG A 1 23  ? 33.707 -34.493 18.523 1.00 49.68  ? 24  ARG A NH2 1 
ATOM   197  N  N   . LEU A 1 24  ? 38.301 -26.542 19.380 1.00 24.97  ? 25  LEU A N   1 
ATOM   198  C  CA  . LEU A 1 24  ? 39.450 -25.656 19.216 1.00 23.80  ? 25  LEU A CA  1 
ATOM   199  C  C   . LEU A 1 24  ? 39.604 -24.771 20.460 1.00 28.49  ? 25  LEU A C   1 
ATOM   200  O  O   . LEU A 1 24  ? 40.725 -24.598 20.944 1.00 29.39  ? 25  LEU A O   1 
ATOM   201  C  CB  . LEU A 1 24  ? 39.294 -24.774 17.987 1.00 22.99  ? 25  LEU A CB  1 
ATOM   202  C  CG  . LEU A 1 24  ? 39.255 -25.493 16.609 1.00 27.14  ? 25  LEU A CG  1 
ATOM   203  C  CD1 . LEU A 1 24  ? 39.091 -24.443 15.486 1.00 27.02  ? 25  LEU A CD1 1 
ATOM   204  C  CD2 . LEU A 1 24  ? 40.530 -26.331 16.383 1.00 28.83  ? 25  LEU A CD2 1 
ATOM   205  N  N   . ARG A 1 25  ? 38.486 -24.249 21.000 1.00 24.80  ? 26  ARG A N   1 
ATOM   206  C  CA  . ARG A 1 25  ? 38.552 -23.445 22.230 1.00 25.35  ? 26  ARG A CA  1 
ATOM   207  C  C   . ARG A 1 25  ? 39.170 -24.258 23.403 1.00 30.84  ? 26  ARG A C   1 
ATOM   208  O  O   . ARG A 1 25  ? 40.055 -23.732 24.103 1.00 30.75  ? 26  ARG A O   1 
ATOM   209  C  CB  . ARG A 1 25  ? 37.157 -22.918 22.635 1.00 26.62  ? 26  ARG A CB  1 
ATOM   210  C  CG  . ARG A 1 25  ? 37.248 -22.043 23.894 1.00 30.99  ? 26  ARG A CG  1 
ATOM   211  C  CD  . ARG A 1 25  ? 35.924 -21.426 24.256 1.00 32.74  ? 26  ARG A CD  1 
ATOM   212  N  NE  . ARG A 1 25  ? 34.911 -22.418 24.623 1.00 32.60  ? 26  ARG A NE  1 
ATOM   213  C  CZ  . ARG A 1 25  ? 34.309 -22.475 25.807 1.00 46.04  ? 26  ARG A CZ  1 
ATOM   214  N  NH1 . ARG A 1 25  ? 34.671 -21.653 26.786 1.00 40.40  ? 26  ARG A NH1 1 
ATOM   215  N  NH2 . ARG A 1 25  ? 33.364 -23.379 26.033 1.00 30.00  ? 26  ARG A NH2 1 
ATOM   216  N  N   A SER A 1 26  ? 38.687 -25.495 23.619 0.40 28.82  ? 27  SER A N   1 
ATOM   217  N  N   B SER A 1 26  ? 38.688 -25.498 23.625 0.35 28.66  ? 27  SER A N   1 
ATOM   218  N  N   C SER A 1 26  ? 38.691 -25.502 23.619 0.25 28.47  ? 27  SER A N   1 
ATOM   219  C  CA  A SER A 1 26  ? 39.161 -26.399 24.676 0.40 30.58  ? 27  SER A CA  1 
ATOM   220  C  CA  B SER A 1 26  ? 39.157 -26.382 24.703 0.35 30.32  ? 27  SER A CA  1 
ATOM   221  C  CA  C SER A 1 26  ? 39.144 -26.412 24.684 0.25 30.00  ? 27  SER A CA  1 
ATOM   222  C  C   A SER A 1 26  ? 40.669 -26.596 24.600 0.40 36.04  ? 27  SER A C   1 
ATOM   223  C  C   B SER A 1 26  ? 40.653 -26.704 24.605 0.35 35.99  ? 27  SER A C   1 
ATOM   224  C  C   C SER A 1 26  ? 40.642 -26.724 24.599 0.25 35.73  ? 27  SER A C   1 
ATOM   225  O  O   A SER A 1 26  ? 41.351 -26.556 25.626 0.40 37.07  ? 27  SER A O   1 
ATOM   226  O  O   B SER A 1 26  ? 41.309 -26.867 25.635 0.35 37.07  ? 27  SER A O   1 
ATOM   227  O  O   C SER A 1 26  ? 41.284 -26.918 25.632 0.25 36.69  ? 27  SER A O   1 
ATOM   228  C  CB  A SER A 1 26  ? 38.489 -27.763 24.547 0.40 34.30  ? 27  SER A CB  1 
ATOM   229  C  CB  B SER A 1 26  ? 38.332 -27.665 24.751 0.35 33.75  ? 27  SER A CB  1 
ATOM   230  C  CB  C SER A 1 26  ? 38.335 -27.706 24.661 0.25 33.34  ? 27  SER A CB  1 
ATOM   231  O  OG  A SER A 1 26  ? 37.143 -27.746 24.986 0.40 41.80  ? 27  SER A OG  1 
ATOM   232  O  OG  B SER A 1 26  ? 38.548 -28.488 23.616 0.35 40.27  ? 27  SER A OG  1 
ATOM   233  O  OG  C SER A 1 26  ? 38.731 -28.596 25.693 0.25 41.44  ? 27  SER A OG  1 
ATOM   234  N  N   . ARG A 1 27  ? 41.188 -26.783 23.372 1.00 32.23  ? 28  ARG A N   1 
ATOM   235  C  CA  . ARG A 1 27  ? 42.609 -27.051 23.126 1.00 33.86  ? 28  ARG A CA  1 
ATOM   236  C  C   . ARG A 1 27  ? 43.422 -25.767 22.934 1.00 36.83  ? 28  ARG A C   1 
ATOM   237  O  O   . ARG A 1 27  ? 44.632 -25.824 22.704 1.00 37.13  ? 28  ARG A O   1 
ATOM   238  C  CB  . ARG A 1 27  ? 42.744 -28.010 21.950 1.00 36.00  ? 28  ARG A CB  1 
ATOM   239  C  CG  . ARG A 1 27  ? 41.991 -29.313 22.194 1.00 45.16  ? 28  ARG A CG  1 
ATOM   240  C  CD  . ARG A 1 27  ? 41.977 -30.196 20.974 1.00 51.71  ? 28  ARG A CD  1 
ATOM   241  N  NE  . ARG A 1 27  ? 43.313 -30.726 20.698 1.00 70.39  ? 28  ARG A NE  1 
ATOM   242  C  CZ  . ARG A 1 27  ? 43.803 -30.897 19.478 1.00 88.45  ? 28  ARG A CZ  1 
ATOM   243  N  NH1 . ARG A 1 27  ? 45.027 -31.378 19.309 1.00 80.10  ? 28  ARG A NH1 1 
ATOM   244  N  NH2 . ARG A 1 27  ? 43.077 -30.584 18.417 1.00 74.91  ? 28  ARG A NH2 1 
ATOM   245  N  N   . ASP A 1 28  ? 42.760 -24.611 23.088 1.00 31.09  ? 29  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 28  ? 43.349 -23.276 22.947 1.00 32.03  ? 29  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 28  ? 43.966 -23.067 21.536 1.00 35.84  ? 29  ASP A C   1 
ATOM   248  O  O   . ASP A 1 28  ? 45.027 -22.453 21.388 1.00 36.77  ? 29  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 28  ? 44.370 -22.993 24.084 1.00 35.30  ? 29  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 28  ? 44.683 -21.526 24.244 1.00 43.35  ? 29  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 28  ? 43.766 -20.696 24.035 1.00 42.76  ? 29  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 28  ? 45.843 -21.201 24.564 1.00 47.99  ? 29  ASP A OD2 1 
ATOM   253  N  N   . ILE A 1 29  ? 43.304 -23.605 20.507 1.00 29.96  ? 30  ILE A N   1 
ATOM   254  C  CA  . ILE A 1 29  ? 43.798 -23.502 19.134 1.00 28.85  ? 30  ILE A CA  1 
ATOM   255  C  C   . ILE A 1 29  ? 43.204 -22.301 18.427 1.00 31.55  ? 30  ILE A C   1 
ATOM   256  O  O   . ILE A 1 29  ? 41.969 -22.171 18.338 1.00 28.37  ? 30  ILE A O   1 
ATOM   257  C  CB  . ILE A 1 29  ? 43.576 -24.812 18.331 1.00 31.78  ? 30  ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 29  ? 44.364 -25.993 18.967 1.00 33.50  ? 30  ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 29  ? 43.967 -24.624 16.846 1.00 31.72  ? 30  ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 29  ? 43.862 -27.390 18.449 1.00 36.84  ? 30  ILE A CD1 1 
ATOM   261  N  N   A LEU A 1 30  ? 44.086 -21.423 17.914 0.54 29.13  ? 31  LEU A N   1 
ATOM   262  N  N   B LEU A 1 30  ? 44.091 -21.427 17.915 0.46 29.66  ? 31  LEU A N   1 
ATOM   263  C  CA  A LEU A 1 30  ? 43.740 -20.218 17.151 0.54 28.54  ? 31  LEU A CA  1 
ATOM   264  C  CA  B LEU A 1 30  ? 43.771 -20.214 17.157 0.46 29.38  ? 31  LEU A CA  1 
ATOM   265  C  C   A LEU A 1 30  ? 42.862 -19.214 17.910 0.54 30.86  ? 31  LEU A C   1 
ATOM   266  C  C   B LEU A 1 30  ? 42.869 -19.218 17.906 0.46 31.33  ? 31  LEU A C   1 
ATOM   267  O  O   A LEU A 1 30  ? 42.227 -18.362 17.280 0.54 28.45  ? 31  LEU A O   1 
ATOM   268  O  O   B LEU A 1 30  ? 42.232 -18.373 17.270 0.46 29.17  ? 31  LEU A O   1 
ATOM   269  C  CB  A LEU A 1 30  ? 43.120 -20.560 15.784 0.54 28.50  ? 31  LEU A CB  1 
ATOM   270  C  CB  B LEU A 1 30  ? 43.206 -20.542 15.771 0.46 29.56  ? 31  LEU A CB  1 
ATOM   271  C  CG  A LEU A 1 30  ? 44.039 -21.211 14.719 0.54 34.27  ? 31  LEU A CG  1 
ATOM   272  C  CG  B LEU A 1 30  ? 44.242 -20.435 14.652 0.46 35.83  ? 31  LEU A CG  1 
ATOM   273  C  CD1 A LEU A 1 30  ? 43.507 -20.946 13.360 0.54 33.23  ? 31  LEU A CD1 1 
ATOM   274  C  CD1 B LEU A 1 30  ? 44.539 -21.785 14.040 0.46 36.39  ? 31  LEU A CD1 1 
ATOM   275  C  CD2 A LEU A 1 30  ? 45.471 -20.682 14.772 0.54 38.02  ? 31  LEU A CD2 1 
ATOM   276  C  CD2 B LEU A 1 30  ? 43.802 -19.447 13.609 0.46 38.06  ? 31  LEU A CD2 1 
ATOM   277  N  N   . THR A 1 31  ? 42.868 -19.273 19.255 1.00 27.94  ? 32  THR A N   1 
ATOM   278  C  CA  . THR A 1 31  ? 42.149 -18.288 20.084 1.00 27.66  ? 32  THR A CA  1 
ATOM   279  C  C   . THR A 1 31  ? 42.965 -16.996 19.901 1.00 33.73  ? 32  THR A C   1 
ATOM   280  O  O   . THR A 1 31  ? 44.195 -17.049 19.794 1.00 33.49  ? 32  THR A O   1 
ATOM   281  C  CB  . THR A 1 31  ? 42.056 -18.712 21.546 1.00 34.33  ? 32  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 31  ? 43.361 -19.054 21.972 1.00 33.98  ? 32  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 31  ? 41.086 -19.884 21.754 1.00 31.64  ? 32  THR A CG2 1 
ATOM   284  N  N   . ASP A 1 32  ? 42.284 -15.873 19.721 1.00 30.02  ? 33  ASP A N   1 
ATOM   285  C  CA  . ASP A 1 32  ? 42.953 -14.623 19.373 1.00 30.12  ? 33  ASP A CA  1 
ATOM   286  C  C   . ASP A 1 32  ? 42.607 -13.482 20.296 1.00 31.42  ? 33  ASP A C   1 
ATOM   287  O  O   . ASP A 1 32  ? 42.935 -12.328 20.010 1.00 31.66  ? 33  ASP A O   1 
ATOM   288  C  CB  . ASP A 1 32  ? 42.633 -14.273 17.906 1.00 31.12  ? 33  ASP A CB  1 
ATOM   289  C  CG  . ASP A 1 32  ? 41.148 -14.286 17.555 1.00 41.15  ? 33  ASP A CG  1 
ATOM   290  O  OD1 . ASP A 1 32  ? 40.310 -14.336 18.486 1.00 37.43  ? 33  ASP A OD1 1 
ATOM   291  O  OD2 . ASP A 1 32  ? 40.827 -14.260 16.356 1.00 49.25  ? 33  ASP A OD2 1 
ATOM   292  N  N   . VAL A 1 33  ? 41.929 -13.788 21.406 1.00 26.54  ? 34  VAL A N   1 
ATOM   293  C  CA  . VAL A 1 33  ? 41.606 -12.742 22.383 1.00 26.11  ? 34  VAL A CA  1 
ATOM   294  C  C   . VAL A 1 33  ? 41.436 -13.319 23.772 1.00 29.65  ? 34  VAL A C   1 
ATOM   295  O  O   . VAL A 1 33  ? 41.039 -14.485 23.925 1.00 29.39  ? 34  VAL A O   1 
ATOM   296  C  CB  . VAL A 1 33  ? 40.354 -11.894 21.945 1.00 28.62  ? 34  VAL A CB  1 
ATOM   297  C  CG1 . VAL A 1 33  ? 39.036 -12.661 22.126 1.00 26.80  ? 34  VAL A CG1 1 
ATOM   298  C  CG2 . VAL A 1 33  ? 40.296 -10.535 22.683 1.00 28.85  ? 34  VAL A CG2 1 
ATOM   299  N  N   A VAL A 1 34  ? 41.730 -12.493 24.787 0.53 27.10  ? 35  VAL A N   1 
ATOM   300  N  N   B VAL A 1 34  ? 41.740 -12.508 24.791 0.47 27.24  ? 35  VAL A N   1 
ATOM   301  C  CA  A VAL A 1 34  ? 41.506 -12.803 26.193 0.53 26.66  ? 35  VAL A CA  1 
ATOM   302  C  CA  B VAL A 1 34  ? 41.477 -12.865 26.174 0.47 26.92  ? 35  VAL A CA  1 
ATOM   303  C  C   A VAL A 1 34  ? 40.444 -11.808 26.676 0.53 29.85  ? 35  VAL A C   1 
ATOM   304  C  C   B VAL A 1 34  ? 40.493 -11.830 26.747 0.47 30.24  ? 35  VAL A C   1 
ATOM   305  O  O   A VAL A 1 34  ? 40.584 -10.600 26.459 0.53 29.82  ? 35  VAL A O   1 
ATOM   306  O  O   B VAL A 1 34  ? 40.702 -10.622 26.602 0.47 30.42  ? 35  VAL A O   1 
ATOM   307  C  CB  A VAL A 1 34  ? 42.807 -12.704 27.038 0.53 31.14  ? 35  VAL A CB  1 
ATOM   308  C  CB  B VAL A 1 34  ? 42.737 -13.141 27.045 0.47 31.57  ? 35  VAL A CB  1 
ATOM   309  C  CG1 A VAL A 1 34  ? 42.535 -12.937 28.527 0.53 31.08  ? 35  VAL A CG1 1 
ATOM   310  C  CG1 B VAL A 1 34  ? 43.590 -11.894 27.249 0.47 32.42  ? 35  VAL A CG1 1 
ATOM   311  C  CG2 A VAL A 1 34  ? 43.864 -13.670 26.537 0.53 31.65  ? 35  VAL A CG2 1 
ATOM   312  C  CG2 B VAL A 1 34  ? 42.357 -13.763 28.386 0.47 31.68  ? 35  VAL A CG2 1 
ATOM   313  N  N   . ILE A 1 35  ? 39.390 -12.312 27.317 1.00 26.14  ? 36  ILE A N   1 
ATOM   314  C  CA  . ILE A 1 35  ? 38.347 -11.481 27.912 1.00 25.69  ? 36  ILE A CA  1 
ATOM   315  C  C   . ILE A 1 35  ? 38.627 -11.510 29.408 1.00 30.66  ? 36  ILE A C   1 
ATOM   316  O  O   . ILE A 1 35  ? 38.632 -12.586 30.015 1.00 29.63  ? 36  ILE A O   1 
ATOM   317  C  CB  . ILE A 1 35  ? 36.902 -11.956 27.583 1.00 27.09  ? 36  ILE A CB  1 
ATOM   318  C  CG1 . ILE A 1 35  ? 36.661 -12.139 26.058 1.00 26.53  ? 36  ILE A CG1 1 
ATOM   319  C  CG2 . ILE A 1 35  ? 35.872 -11.027 28.206 1.00 28.47  ? 36  ILE A CG2 1 
ATOM   320  C  CD1 . ILE A 1 35  ? 36.970 -10.897 25.134 1.00 27.12  ? 36  ILE A CD1 1 
ATOM   321  N  N   . VAL A 1 36  ? 38.866 -10.330 29.992 1.00 27.34  ? 37  VAL A N   1 
ATOM   322  C  CA  . VAL A 1 36  ? 39.180 -10.200 31.422 1.00 27.77  ? 37  VAL A CA  1 
ATOM   323  C  C   . VAL A 1 36  ? 37.918 -9.762  32.152 1.00 31.94  ? 37  VAL A C   1 
ATOM   324  O  O   . VAL A 1 36  ? 37.320 -8.732  31.808 1.00 30.70  ? 37  VAL A O   1 
ATOM   325  C  CB  . VAL A 1 36  ? 40.374 -9.235  31.663 1.00 32.39  ? 37  VAL A CB  1 
ATOM   326  C  CG1 . VAL A 1 36  ? 40.680 -9.082  33.155 1.00 33.34  ? 37  VAL A CG1 1 
ATOM   327  C  CG2 . VAL A 1 36  ? 41.618 -9.706  30.923 1.00 33.01  ? 37  VAL A CG2 1 
ATOM   328  N  N   . VAL A 1 37  ? 37.507 -10.556 33.158 1.00 29.51  ? 38  VAL A N   1 
ATOM   329  C  CA  . VAL A 1 37  ? 36.303 -10.314 33.957 1.00 29.76  ? 38  VAL A CA  1 
ATOM   330  C  C   . VAL A 1 37  ? 36.771 -10.379 35.401 1.00 36.25  ? 38  VAL A C   1 
ATOM   331  O  O   . VAL A 1 37  ? 37.007 -11.474 35.919 1.00 34.79  ? 38  VAL A O   1 
ATOM   332  C  CB  . VAL A 1 37  ? 35.177 -11.330 33.618 1.00 33.15  ? 38  VAL A CB  1 
ATOM   333  C  CG1 . VAL A 1 37  ? 33.862 -10.922 34.274 1.00 33.19  ? 38  VAL A CG1 1 
ATOM   334  C  CG2 . VAL A 1 37  ? 35.002 -11.480 32.102 1.00 31.92  ? 38  VAL A CG2 1 
ATOM   335  N  N   A SER A 1 38  ? 36.689 -9.258  36.161 0.50 35.32  ? 39  SER A N   1 
ATOM   336  N  N   B SER A 1 38  ? 37.262 -9.186  35.821 0.50 33.54  ? 39  SER A N   1 
ATOM   337  C  CA  A SER A 1 38  ? 37.057 -9.238  37.594 0.50 37.18  ? 39  SER A CA  1 
ATOM   338  C  CA  B SER A 1 38  ? 37.933 -8.844  37.062 0.50 34.22  ? 39  SER A CA  1 
ATOM   339  C  C   A SER A 1 38  ? 38.320 -10.106 37.898 0.50 41.75  ? 39  SER A C   1 
ATOM   340  C  C   B SER A 1 38  ? 39.221 -9.672  37.206 0.50 36.76  ? 39  SER A C   1 
ATOM   341  O  O   A SER A 1 38  ? 38.288 -10.966 38.784 0.50 41.49  ? 39  SER A O   1 
ATOM   342  O  O   B SER A 1 38  ? 40.122 -9.479  36.388 0.50 34.97  ? 39  SER A O   1 
ATOM   343  C  CB  A SER A 1 38  ? 35.874 -9.669  38.470 0.50 42.53  ? 39  SER A CB  1 
ATOM   344  C  CB  B SER A 1 38  ? 36.985 -8.905  38.253 0.50 38.94  ? 39  SER A CB  1 
ATOM   345  O  OG  A SER A 1 38  ? 34.771 -8.776  38.401 0.50 52.48  ? 39  SER A OG  1 
ATOM   346  O  OG  B SER A 1 38  ? 36.077 -7.818  38.149 0.50 45.64  ? 39  SER A OG  1 
ATOM   347  N  N   A ARG A 1 39  ? 39.399 -9.909  37.100 0.50 38.56  ? 40  ARG A N   1 
ATOM   348  N  N   B ARG A 1 39  ? 39.306 -10.616 38.161 0.50 34.22  ? 40  ARG A N   1 
ATOM   349  C  CA  A ARG A 1 39  ? 40.689 -10.625 37.162 0.50 39.48  ? 40  ARG A CA  1 
ATOM   350  C  CA  B ARG A 1 39  ? 40.528 -11.416 38.304 0.50 35.46  ? 40  ARG A CA  1 
ATOM   351  C  C   A ARG A 1 39  ? 40.585 -12.156 36.869 0.50 43.01  ? 40  ARG A C   1 
ATOM   352  C  C   B ARG A 1 39  ? 40.664 -12.491 37.191 0.50 41.17  ? 40  ARG A C   1 
ATOM   353  O  O   A ARG A 1 39  ? 41.441 -12.942 37.307 0.50 45.31  ? 40  ARG A O   1 
ATOM   354  O  O   B ARG A 1 39  ? 41.760 -12.689 36.652 0.50 43.38  ? 40  ARG A O   1 
ATOM   355  C  CB  A ARG A 1 39  ? 41.453 -10.363 38.475 0.50 41.31  ? 40  ARG A CB  1 
ATOM   356  C  CB  B ARG A 1 39  ? 40.655 -12.010 39.728 0.50 35.29  ? 40  ARG A CB  1 
ATOM   357  C  CG  A ARG A 1 39  ? 41.985 -8.943  38.630 0.50 52.49  ? 40  ARG A CG  1 
ATOM   358  C  CG  B ARG A 1 39  ? 40.964 -10.956 40.803 0.50 43.94  ? 40  ARG A CG  1 
ATOM   359  C  CD  A ARG A 1 39  ? 43.052 -8.893  39.705 0.50 58.81  ? 40  ARG A CD  1 
ATOM   360  C  CD  B ARG A 1 39  ? 41.294 -11.570 42.156 0.50 41.91  ? 40  ARG A CD  1 
ATOM   361  N  NE  A ARG A 1 39  ? 43.424 -7.524  40.062 0.50 65.96  ? 40  ARG A NE  1 
ATOM   362  N  NE  B ARG A 1 39  ? 41.514 -10.556 43.191 0.50 45.61  ? 40  ARG A NE  1 
ATOM   363  C  CZ  A ARG A 1 39  ? 42.848 -6.817  41.031 0.50 78.70  ? 40  ARG A CZ  1 
ATOM   364  C  CZ  B ARG A 1 39  ? 42.693 -10.013 43.486 0.50 60.58  ? 40  ARG A CZ  1 
ATOM   365  N  NH1 A ARG A 1 39  ? 41.850 -7.335  41.738 0.50 63.28  ? 40  ARG A NH1 1 
ATOM   366  N  NH1 B ARG A 1 39  ? 43.781 -10.359 42.810 0.50 50.00  ? 40  ARG A NH1 1 
ATOM   367  N  NH2 A ARG A 1 39  ? 43.257 -5.583  41.291 0.50 66.20  ? 40  ARG A NH2 1 
ATOM   368  N  NH2 B ARG A 1 39  ? 42.790 -9.109  44.449 0.50 50.39  ? 40  ARG A NH2 1 
ATOM   369  N  N   A GLU A 1 40  ? 39.543 -12.568 36.142 0.50 35.79  ? 41  GLU A N   1 
ATOM   370  N  N   B GLU A 1 40  ? 39.543 -13.103 36.786 0.50 34.74  ? 41  GLU A N   1 
ATOM   371  C  CA  A GLU A 1 40  ? 39.365 -13.946 35.670 0.50 34.60  ? 41  GLU A CA  1 
ATOM   372  C  CA  B GLU A 1 40  ? 39.526 -14.194 35.802 0.50 33.26  ? 41  GLU A CA  1 
ATOM   373  C  C   A GLU A 1 40  ? 39.499 -13.829 34.158 0.50 34.89  ? 41  GLU A C   1 
ATOM   374  C  C   B GLU A 1 40  ? 39.761 -13.760 34.344 0.50 34.30  ? 41  GLU A C   1 
ATOM   375  O  O   A GLU A 1 40  ? 38.913 -12.923 33.560 0.50 32.04  ? 41  GLU A O   1 
ATOM   376  O  O   B GLU A 1 40  ? 39.436 -12.641 33.950 0.50 31.73  ? 41  GLU A O   1 
ATOM   377  C  CB  A GLU A 1 40  ? 38.011 -14.547 36.092 0.50 35.96  ? 41  GLU A CB  1 
ATOM   378  C  CB  B GLU A 1 40  ? 38.227 -15.021 35.917 0.50 34.40  ? 41  GLU A CB  1 
ATOM   379  C  CG  A GLU A 1 40  ? 37.909 -14.785 37.593 0.50 50.74  ? 41  GLU A CG  1 
ATOM   380  C  CG  B GLU A 1 40  ? 37.751 -15.207 37.354 0.50 50.40  ? 41  GLU A CG  1 
ATOM   381  C  CD  A GLU A 1 40  ? 37.828 -16.236 38.025 0.50 85.86  ? 41  GLU A CD  1 
ATOM   382  C  CD  B GLU A 1 40  ? 37.887 -16.578 37.990 0.50 87.43  ? 41  GLU A CD  1 
ATOM   383  O  OE1 A GLU A 1 40  ? 36.779 -16.626 38.588 0.50 88.43  ? 41  GLU A OE1 1 
ATOM   384  O  OE1 B GLU A 1 40  ? 38.935 -17.236 37.797 0.50 90.84  ? 41  GLU A OE1 1 
ATOM   385  O  OE2 A GLU A 1 40  ? 38.812 -16.981 37.813 0.50 87.14  ? 41  GLU A OE2 1 
ATOM   386  O  OE2 B GLU A 1 40  ? 36.946 -16.981 38.712 0.50 88.70  ? 41  GLU A OE2 1 
ATOM   387  N  N   . GLN A 1 41  ? 40.317 -14.691 33.546 1.00 31.12  ? 42  GLN A N   1 
ATOM   388  C  CA  . GLN A 1 41  ? 40.632 -14.561 32.133 1.00 30.20  ? 42  GLN A CA  1 
ATOM   389  C  C   . GLN A 1 41  ? 40.013 -15.678 31.324 1.00 33.67  ? 42  GLN A C   1 
ATOM   390  O  O   . GLN A 1 41  ? 40.073 -16.830 31.740 1.00 34.30  ? 42  GLN A O   1 
ATOM   391  C  CB  . GLN A 1 41  ? 42.159 -14.566 31.960 1.00 32.84  ? 42  GLN A CB  1 
ATOM   392  C  CG  . GLN A 1 41  ? 42.828 -13.325 32.543 1.00 46.54  ? 42  GLN A CG  1 
ATOM   393  C  CD  . GLN A 1 41  ? 44.307 -13.224 32.262 1.00 66.13  ? 42  GLN A CD  1 
ATOM   394  O  OE1 . GLN A 1 41  ? 44.876 -13.921 31.406 1.00 58.54  ? 42  GLN A OE1 1 
ATOM   395  N  NE2 . GLN A 1 41  ? 44.962 -12.331 32.982 1.00 69.86  ? 42  GLN A NE2 1 
ATOM   396  N  N   . PHE A 1 42  ? 39.425 -15.340 30.168 1.00 26.79  ? 43  PHE A N   1 
ATOM   397  C  CA  . PHE A 1 42  ? 38.789 -16.332 29.288 1.00 26.92  ? 43  PHE A CA  1 
ATOM   398  C  C   . PHE A 1 42  ? 39.308 -16.166 27.891 1.00 30.65  ? 43  PHE A C   1 
ATOM   399  O  O   . PHE A 1 42  ? 39.146 -15.092 27.313 1.00 30.74  ? 43  PHE A O   1 
ATOM   400  C  CB  . PHE A 1 42  ? 37.259 -16.152 29.296 1.00 28.11  ? 43  PHE A CB  1 
ATOM   401  C  CG  . PHE A 1 42  ? 36.634 -16.243 30.668 1.00 30.36  ? 43  PHE A CG  1 
ATOM   402  C  CD1 . PHE A 1 42  ? 36.519 -15.111 31.477 1.00 32.91  ? 43  PHE A CD1 1 
ATOM   403  C  CD2 . PHE A 1 42  ? 36.136 -17.453 31.143 1.00 32.98  ? 43  PHE A CD2 1 
ATOM   404  C  CE1 . PHE A 1 42  ? 35.959 -15.199 32.755 1.00 34.98  ? 43  PHE A CE1 1 
ATOM   405  C  CE2 . PHE A 1 42  ? 35.565 -17.538 32.417 1.00 35.93  ? 43  PHE A CE2 1 
ATOM   406  C  CZ  . PHE A 1 42  ? 35.479 -16.411 33.216 1.00 33.74  ? 43  PHE A CZ  1 
ATOM   407  N  N   . ARG A 1 43  ? 39.907 -17.225 27.319 1.00 27.15  ? 44  ARG A N   1 
ATOM   408  C  CA  . ARG A 1 43  ? 40.419 -17.157 25.946 1.00 26.51  ? 44  ARG A CA  1 
ATOM   409  C  C   . ARG A 1 43  ? 39.290 -17.556 24.992 1.00 29.91  ? 44  ARG A C   1 
ATOM   410  O  O   . ARG A 1 43  ? 38.488 -18.445 25.301 1.00 28.77  ? 44  ARG A O   1 
ATOM   411  C  CB  . ARG A 1 43  ? 41.651 -18.066 25.751 1.00 28.29  ? 44  ARG A CB  1 
ATOM   412  C  CG  . ARG A 1 43  ? 42.884 -17.647 26.603 1.00 37.22  ? 44  ARG A CG  1 
ATOM   413  C  CD  . ARG A 1 43  ? 44.209 -18.053 25.954 1.00 48.30  ? 44  ARG A CD  1 
ATOM   414  N  NE  . ARG A 1 43  ? 44.233 -17.641 24.544 1.00 60.70  ? 44  ARG A NE  1 
ATOM   415  C  CZ  . ARG A 1 43  ? 44.845 -16.562 24.066 1.00 72.65  ? 44  ARG A CZ  1 
ATOM   416  N  NH1 . ARG A 1 43  ? 45.588 -15.805 24.859 1.00 64.90  ? 44  ARG A NH1 1 
ATOM   417  N  NH2 . ARG A 1 43  ? 44.760 -16.262 22.778 1.00 54.18  ? 44  ARG A NH2 1 
ATOM   418  N  N   . ALA A 1 44  ? 39.194 -16.883 23.844 1.00 25.68  ? 45  ALA A N   1 
ATOM   419  C  CA  . ALA A 1 44  ? 38.119 -17.204 22.894 1.00 25.48  ? 45  ALA A CA  1 
ATOM   420  C  C   . ALA A 1 44  ? 38.524 -16.807 21.479 1.00 26.91  ? 45  ALA A C   1 
ATOM   421  O  O   . ALA A 1 44  ? 39.630 -16.290 21.262 1.00 25.87  ? 45  ALA A O   1 
ATOM   422  C  CB  . ALA A 1 44  ? 36.831 -16.475 23.298 1.00 26.41  ? 45  ALA A CB  1 
ATOM   423  N  N   . HIS A 1 45  ? 37.621 -17.060 20.516 1.00 23.15  ? 46  HIS A N   1 
ATOM   424  C  CA  . HIS A 1 45  ? 37.795 -16.652 19.134 1.00 22.34  ? 46  HIS A CA  1 
ATOM   425  C  C   . HIS A 1 45  ? 36.913 -15.408 18.947 1.00 26.31  ? 46  HIS A C   1 
ATOM   426  O  O   . HIS A 1 45  ? 35.703 -15.450 19.219 1.00 25.40  ? 46  HIS A O   1 
ATOM   427  C  CB  . HIS A 1 45  ? 37.356 -17.775 18.172 1.00 21.71  ? 46  HIS A CB  1 
ATOM   428  C  CG  . HIS A 1 45  ? 38.097 -19.067 18.384 1.00 25.17  ? 46  HIS A CG  1 
ATOM   429  N  ND1 . HIS A 1 45  ? 37.564 -20.088 19.154 1.00 26.91  ? 46  HIS A ND1 1 
ATOM   430  C  CD2 . HIS A 1 45  ? 39.333 -19.436 17.962 1.00 25.89  ? 46  HIS A CD2 1 
ATOM   431  C  CE1 . HIS A 1 45  ? 38.480 -21.052 19.164 1.00 26.24  ? 46  HIS A CE1 1 
ATOM   432  N  NE2 . HIS A 1 45  ? 39.558 -20.708 18.455 1.00 25.85  ? 46  HIS A NE2 1 
ATOM   433  N  N   . LYS A 1 46  ? 37.513 -14.309 18.505 1.00 24.58  ? 47  LYS A N   1 
ATOM   434  C  CA  . LYS A 1 46  ? 36.784 -13.059 18.233 1.00 24.02  ? 47  LYS A CA  1 
ATOM   435  C  C   . LYS A 1 46  ? 35.555 -13.304 17.353 1.00 26.68  ? 47  LYS A C   1 
ATOM   436  O  O   . LYS A 1 46  ? 34.496 -12.770 17.658 1.00 24.95  ? 47  LYS A O   1 
ATOM   437  C  CB  . LYS A 1 46  ? 37.699 -12.063 17.496 1.00 26.25  ? 47  LYS A CB  1 
ATOM   438  C  CG  . LYS A 1 46  ? 38.726 -11.433 18.420 1.00 26.43  ? 47  LYS A CG  1 
ATOM   439  C  CD  . LYS A 1 46  ? 39.639 -10.494 17.634 1.00 25.43  ? 47  LYS A CD  1 
ATOM   440  C  CE  . LYS A 1 46  ? 40.772 -10.049 18.519 1.00 30.74  ? 47  LYS A CE  1 
ATOM   441  N  NZ  . LYS A 1 46  ? 41.714 -9.158  17.786 1.00 33.95  ? 47  LYS A NZ  1 
ATOM   442  N  N   . THR A 1 47  ? 35.679 -14.125 16.288 1.00 22.37  ? 48  THR A N   1 
ATOM   443  C  CA  . THR A 1 47  ? 34.521 -14.320 15.390 1.00 22.16  ? 48  THR A CA  1 
ATOM   444  C  C   . THR A 1 47  ? 33.341 -14.993 16.057 1.00 23.02  ? 48  THR A C   1 
ATOM   445  O  O   . THR A 1 47  ? 32.204 -14.625 15.769 1.00 22.37  ? 48  THR A O   1 
ATOM   446  C  CB  . THR A 1 47  ? 34.902 -15.037 14.099 1.00 29.72  ? 48  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 47  ? 35.518 -16.255 14.452 1.00 30.07  ? 48  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 47  ? 35.807 -14.178 13.207 1.00 31.78  ? 48  THR A CG2 1 
ATOM   449  N  N   . VAL A 1 48  ? 33.592 -15.950 16.940 1.00 20.41  ? 49  VAL A N   1 
ATOM   450  C  CA  . VAL A 1 48  ? 32.494 -16.648 17.637 1.00 20.87  ? 49  VAL A CA  1 
ATOM   451  C  C   . VAL A 1 48  ? 31.828 -15.646 18.602 1.00 23.32  ? 49  VAL A C   1 
ATOM   452  O  O   . VAL A 1 48  ? 30.594 -15.599 18.699 1.00 21.99  ? 49  VAL A O   1 
ATOM   453  C  CB  . VAL A 1 48  ? 32.990 -17.923 18.386 1.00 23.76  ? 49  VAL A CB  1 
ATOM   454  C  CG1 . VAL A 1 48  ? 31.856 -18.538 19.223 1.00 23.51  ? 49  VAL A CG1 1 
ATOM   455  C  CG2 . VAL A 1 48  ? 33.517 -18.972 17.394 1.00 23.34  ? 49  VAL A CG2 1 
ATOM   456  N  N   . LEU A 1 49  ? 32.647 -14.864 19.342 1.00 21.01  ? 50  LEU A N   1 
ATOM   457  C  CA  . LEU A 1 49  ? 32.088 -13.847 20.268 1.00 21.09  ? 50  LEU A CA  1 
ATOM   458  C  C   . LEU A 1 49  ? 31.189 -12.852 19.489 1.00 23.12  ? 50  LEU A C   1 
ATOM   459  O  O   . LEU A 1 49  ? 30.095 -12.520 19.938 1.00 22.18  ? 50  LEU A O   1 
ATOM   460  C  CB  . LEU A 1 49  ? 33.241 -13.062 20.946 1.00 21.08  ? 50  LEU A CB  1 
ATOM   461  C  CG  . LEU A 1 49  ? 34.185 -13.855 21.879 1.00 23.86  ? 50  LEU A CG  1 
ATOM   462  C  CD1 . LEU A 1 49  ? 35.242 -12.914 22.480 1.00 23.65  ? 50  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A 1 49  ? 33.400 -14.540 22.997 1.00 25.99  ? 50  LEU A CD2 1 
ATOM   464  N  N   . MET A 1 50  ? 31.651 -12.383 18.329 1.00 20.60  ? 51  MET A N   1 
ATOM   465  C  CA  . MET A 1 50  ? 30.869 -11.460 17.484 1.00 21.68  ? 51  MET A CA  1 
ATOM   466  C  C   . MET A 1 50  ? 29.585 -12.111 17.003 1.00 25.77  ? 51  MET A C   1 
ATOM   467  O  O   . MET A 1 50  ? 28.542 -11.465 16.997 1.00 26.33  ? 51  MET A O   1 
ATOM   468  C  CB  . MET A 1 50  ? 31.677 -11.005 16.267 1.00 23.62  ? 51  MET A CB  1 
ATOM   469  C  CG  . MET A 1 50  ? 32.868 -10.166 16.640 1.00 26.68  ? 51  MET A CG  1 
ATOM   470  S  SD  . MET A 1 50  ? 33.925 -10.077 15.188 1.00 31.32  ? 51  MET A SD  1 
ATOM   471  C  CE  . MET A 1 50  ? 33.148 -8.754  14.366 1.00 27.80  ? 51  MET A CE  1 
ATOM   472  N  N   . ALA A 1 51  ? 29.654 -13.387 16.610 1.00 22.29  ? 52  ALA A N   1 
ATOM   473  C  CA  . ALA A 1 51  ? 28.497 -14.122 16.082 1.00 22.69  ? 52  ALA A CA  1 
ATOM   474  C  C   . ALA A 1 51  ? 27.387 -14.302 17.142 1.00 25.55  ? 52  ALA A C   1 
ATOM   475  O  O   . ALA A 1 51  ? 26.225 -14.493 16.783 1.00 26.74  ? 52  ALA A O   1 
ATOM   476  C  CB  . ALA A 1 51  ? 28.941 -15.486 15.543 1.00 22.56  ? 52  ALA A CB  1 
ATOM   477  N  N   . CYS A 1 52  ? 27.754 -14.242 18.437 1.00 22.80  ? 53  CYS A N   1 
ATOM   478  C  CA  . CYS A 1 52  ? 26.839 -14.480 19.563 1.00 23.12  ? 53  CYS A CA  1 
ATOM   479  C  C   . CYS A 1 52  ? 26.397 -13.256 20.331 1.00 26.35  ? 53  CYS A C   1 
ATOM   480  O  O   . CYS A 1 52  ? 25.430 -13.352 21.096 1.00 26.45  ? 53  CYS A O   1 
ATOM   481  C  CB  . CYS A 1 52  ? 27.483 -15.473 20.524 1.00 23.58  ? 53  CYS A CB  1 
ATOM   482  S  SG  . CYS A 1 52  ? 27.833 -17.088 19.797 1.00 26.86  ? 53  CYS A SG  1 
ATOM   483  N  N   . SER A 1 53  ? 27.167 -12.165 20.255 1.00 22.86  ? 54  SER A N   1 
ATOM   484  C  CA  . SER A 1 53  ? 26.963 -11.016 21.124 1.00 21.43  ? 54  SER A CA  1 
ATOM   485  C  C   . SER A 1 53  ? 26.995 -9.697  20.390 1.00 27.34  ? 54  SER A C   1 
ATOM   486  O  O   . SER A 1 53  ? 27.969 -9.415  19.684 1.00 25.33  ? 54  SER A O   1 
ATOM   487  C  CB  . SER A 1 53  ? 28.059 -11.071 22.189 1.00 22.93  ? 54  SER A CB  1 
ATOM   488  O  OG  . SER A 1 53  ? 28.422 -9.830  22.772 1.00 27.39  ? 54  SER A OG  1 
ATOM   489  N  N   . GLY A 1 54  ? 25.962 -8.879  20.599 1.00 26.23  ? 55  GLY A N   1 
ATOM   490  C  CA  . GLY A 1 54  ? 25.898 -7.538  20.024 1.00 26.15  ? 55  GLY A CA  1 
ATOM   491  C  C   . GLY A 1 54  ? 27.022 -6.655  20.531 1.00 28.81  ? 55  GLY A C   1 
ATOM   492  O  O   . GLY A 1 54  ? 27.561 -5.842  19.773 1.00 28.45  ? 55  GLY A O   1 
ATOM   493  N  N   . LEU A 1 55  ? 27.430 -6.847  21.810 1.00 26.24  ? 56  LEU A N   1 
ATOM   494  C  CA  . LEU A 1 55  ? 28.532 -6.070  22.383 1.00 25.77  ? 56  LEU A CA  1 
ATOM   495  C  C   . LEU A 1 55  ? 29.854 -6.414  21.684 1.00 27.04  ? 56  LEU A C   1 
ATOM   496  O  O   . LEU A 1 55  ? 30.534 -5.497  21.222 1.00 27.06  ? 56  LEU A O   1 
ATOM   497  C  CB  . LEU A 1 55  ? 28.658 -6.273  23.903 1.00 25.88  ? 56  LEU A CB  1 
ATOM   498  C  CG  . LEU A 1 55  ? 29.697 -5.358  24.589 1.00 30.47  ? 56  LEU A CG  1 
ATOM   499  C  CD1 . LEU A 1 55  ? 29.248 -3.871  24.587 1.00 32.34  ? 56  LEU A CD1 1 
ATOM   500  C  CD2 . LEU A 1 55  ? 30.002 -5.846  25.996 1.00 30.05  ? 56  LEU A CD2 1 
ATOM   501  N  N   . PHE A 1 56  ? 30.187 -7.722  21.560 1.00 23.33  ? 57  PHE A N   1 
ATOM   502  C  CA  . PHE A 1 56  ? 31.447 -8.105  20.894 1.00 22.99  ? 57  PHE A CA  1 
ATOM   503  C  C   . PHE A 1 56  ? 31.434 -7.775  19.426 1.00 26.97  ? 57  PHE A C   1 
ATOM   504  O  O   . PHE A 1 56  ? 32.473 -7.419  18.877 1.00 27.05  ? 57  PHE A O   1 
ATOM   505  C  CB  . PHE A 1 56  ? 31.815 -9.562  21.161 1.00 23.51  ? 57  PHE A CB  1 
ATOM   506  C  CG  . PHE A 1 56  ? 32.230 -9.801  22.602 1.00 24.44  ? 57  PHE A CG  1 
ATOM   507  C  CD1 . PHE A 1 56  ? 33.316 -9.121  23.158 1.00 26.79  ? 57  PHE A CD1 1 
ATOM   508  C  CD2 . PHE A 1 56  ? 31.569 -10.746 23.389 1.00 24.78  ? 57  PHE A CD2 1 
ATOM   509  C  CE1 . PHE A 1 56  ? 33.706 -9.348  24.491 1.00 27.31  ? 57  PHE A CE1 1 
ATOM   510  C  CE2 . PHE A 1 56  ? 31.990 -11.007 24.705 1.00 27.57  ? 57  PHE A CE2 1 
ATOM   511  C  CZ  . PHE A 1 56  ? 33.032 -10.277 25.261 1.00 25.48  ? 57  PHE A CZ  1 
ATOM   512  N  N   . TYR A 1 57  ? 30.259 -7.854  18.786 1.00 25.17  ? 58  TYR A N   1 
ATOM   513  C  CA  . TYR A 1 57  ? 30.151 -7.455  17.385 1.00 26.31  ? 58  TYR A CA  1 
ATOM   514  C  C   . TYR A 1 57  ? 30.579 -5.982  17.224 1.00 30.43  ? 58  TYR A C   1 
ATOM   515  O  O   . TYR A 1 57  ? 31.380 -5.673  16.338 1.00 28.11  ? 58  TYR A O   1 
ATOM   516  C  CB  . TYR A 1 57  ? 28.728 -7.693  16.875 1.00 28.68  ? 58  TYR A CB  1 
ATOM   517  C  CG  . TYR A 1 57  ? 28.503 -7.155  15.484 1.00 32.82  ? 58  TYR A CG  1 
ATOM   518  C  CD1 . TYR A 1 57  ? 29.040 -7.796  14.371 1.00 34.53  ? 58  TYR A CD1 1 
ATOM   519  C  CD2 . TYR A 1 57  ? 27.722 -6.026  15.275 1.00 37.02  ? 58  TYR A CD2 1 
ATOM   520  C  CE1 . TYR A 1 57  ? 28.827 -7.304  13.082 1.00 36.92  ? 58  TYR A CE1 1 
ATOM   521  C  CE2 . TYR A 1 57  ? 27.498 -5.530  13.996 1.00 40.09  ? 58  TYR A CE2 1 
ATOM   522  C  CZ  . TYR A 1 57  ? 28.045 -6.178  12.906 1.00 47.55  ? 58  TYR A CZ  1 
ATOM   523  O  OH  . TYR A 1 57  ? 27.801 -5.676  11.662 1.00 55.31  ? 58  TYR A OH  1 
ATOM   524  N  N   A SER A 1 58  ? 30.056 -5.085  18.085 0.52 28.15  ? 59  SER A N   1 
ATOM   525  N  N   B SER A 1 58  ? 30.049 -5.095  18.084 0.48 28.49  ? 59  SER A N   1 
ATOM   526  C  CA  A SER A 1 58  ? 30.382 -3.656  18.080 0.52 29.12  ? 59  SER A CA  1 
ATOM   527  C  CA  B SER A 1 58  ? 30.367 -3.670  18.093 0.48 29.64  ? 59  SER A CA  1 
ATOM   528  C  C   A SER A 1 58  ? 31.863 -3.412  18.388 0.52 34.19  ? 59  SER A C   1 
ATOM   529  C  C   B SER A 1 58  ? 31.863 -3.452  18.355 0.48 34.14  ? 59  SER A C   1 
ATOM   530  O  O   A SER A 1 58  ? 32.496 -2.611  17.706 0.52 35.28  ? 59  SER A O   1 
ATOM   531  O  O   B SER A 1 58  ? 32.506 -2.728  17.600 0.48 34.83  ? 59  SER A O   1 
ATOM   532  C  CB  A SER A 1 58  ? 29.492 -2.907  19.068 0.52 31.32  ? 59  SER A CB  1 
ATOM   533  C  CB  B SER A 1 58  ? 29.526 -2.951  19.145 0.48 32.79  ? 59  SER A CB  1 
ATOM   534  O  OG  A SER A 1 58  ? 28.143 -2.953  18.636 0.52 32.72  ? 59  SER A OG  1 
ATOM   535  O  OG  B SER A 1 58  ? 29.815 -1.564  19.158 0.48 39.49  ? 59  SER A OG  1 
ATOM   536  N  N   . ILE A 1 59  ? 32.418 -4.123  19.388 1.00 29.84  ? 60  ILE A N   1 
ATOM   537  C  CA  . ILE A 1 59  ? 33.832 -4.013  19.782 1.00 28.97  ? 60  ILE A CA  1 
ATOM   538  C  C   . ILE A 1 59  ? 34.771 -4.404  18.649 1.00 31.91  ? 60  ILE A C   1 
ATOM   539  O  O   . ILE A 1 59  ? 35.670 -3.626  18.308 1.00 33.22  ? 60  ILE A O   1 
ATOM   540  C  CB  . ILE A 1 59  ? 34.147 -4.843  21.081 1.00 30.34  ? 60  ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 59  ? 33.456 -4.253  22.319 1.00 30.99  ? 60  ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 59  ? 35.676 -4.987  21.325 1.00 28.04  ? 60  ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 59  ? 33.423 -5.276  23.529 1.00 33.96  ? 60  ILE A CD1 1 
ATOM   544  N  N   . PHE A 1 60  ? 34.574 -5.594  18.065 1.00 26.68  ? 61  PHE A N   1 
ATOM   545  C  CA  . PHE A 1 60  ? 35.532 -6.054  17.076 1.00 26.99  ? 61  PHE A CA  1 
ATOM   546  C  C   . PHE A 1 60  ? 35.288 -5.509  15.667 1.00 31.51  ? 61  PHE A C   1 
ATOM   547  O  O   . PHE A 1 60  ? 36.127 -5.747  14.809 1.00 31.71  ? 61  PHE A O   1 
ATOM   548  C  CB  . PHE A 1 60  ? 35.681 -7.588  17.114 1.00 27.27  ? 61  PHE A CB  1 
ATOM   549  C  CG  . PHE A 1 60  ? 36.126 -8.076  18.480 1.00 27.76  ? 61  PHE A CG  1 
ATOM   550  C  CD1 . PHE A 1 60  ? 37.328 -7.640  19.041 1.00 31.21  ? 61  PHE A CD1 1 
ATOM   551  C  CD2 . PHE A 1 60  ? 35.334 -8.944  19.214 1.00 28.56  ? 61  PHE A CD2 1 
ATOM   552  C  CE1 . PHE A 1 60  ? 37.731 -8.085  20.309 1.00 31.52  ? 61  PHE A CE1 1 
ATOM   553  C  CE2 . PHE A 1 60  ? 35.742 -9.404  20.474 1.00 31.51  ? 61  PHE A CE2 1 
ATOM   554  C  CZ  . PHE A 1 60  ? 36.928 -8.962  21.019 1.00 29.89  ? 61  PHE A CZ  1 
ATOM   555  N  N   . THR A 1 61  ? 34.226 -4.713  15.436 1.00 29.72  ? 62  THR A N   1 
ATOM   556  C  CA  . THR A 1 61  ? 34.079 -4.031  14.133 1.00 30.56  ? 62  THR A CA  1 
ATOM   557  C  C   . THR A 1 61  ? 34.646 -2.606  14.259 1.00 37.89  ? 62  THR A C   1 
ATOM   558  O  O   . THR A 1 61  ? 34.719 -1.858  13.278 1.00 38.06  ? 62  THR A O   1 
ATOM   559  C  CB  . THR A 1 61  ? 32.652 -4.053  13.585 1.00 36.83  ? 62  THR A CB  1 
ATOM   560  O  OG1 . THR A 1 61  ? 31.759 -3.564  14.572 1.00 34.25  ? 62  THR A OG1 1 
ATOM   561  C  CG2 . THR A 1 61  ? 32.220 -5.439  13.083 1.00 32.74  ? 62  THR A CG2 1 
ATOM   562  N  N   . ASP A 1 62  ? 35.090 -2.239  15.469 1.00 34.47  ? 63  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 62  ? 35.695 -0.930  15.679 1.00 35.49  ? 63  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 62  ? 37.131 -0.998  15.159 1.00 41.87  ? 63  ASP A C   1 
ATOM   565  O  O   . ASP A 1 62  ? 37.883 -1.880  15.564 1.00 39.89  ? 63  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 62  ? 35.659 -0.535  17.162 1.00 36.87  ? 63  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 62  ? 36.429 0.742   17.406 1.00 52.17  ? 63  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 62  ? 35.835 1.823   17.256 1.00 57.42  ? 63  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 62  ? 37.650 0.657   17.678 1.00 53.67  ? 63  ASP A OD2 1 
ATOM   570  N  N   . GLN A 1 63  ? 37.518 -0.041  14.297 1.00 43.06  ? 64  GLN A N   1 
ATOM   571  C  CA  . GLN A 1 63  ? 38.834 0.012   13.659 1.00 44.53  ? 64  GLN A CA  1 
ATOM   572  C  C   . GLN A 1 63  ? 40.020 -0.052  14.629 1.00 48.92  ? 64  GLN A C   1 
ATOM   573  O  O   . GLN A 1 63  ? 41.045 -0.607  14.246 1.00 51.17  ? 64  GLN A O   1 
ATOM   574  C  CB  . GLN A 1 63  ? 38.948 1.229   12.731 1.00 48.12  ? 64  GLN A CB  1 
ATOM   575  C  CG  . GLN A 1 63  ? 38.157 1.078   11.435 1.00 67.74  ? 64  GLN A CG  1 
ATOM   576  N  N   . LEU A 1 64  ? 39.900 0.491   15.868 1.00 42.40  ? 65  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 64  ? 40.992 0.411   16.850 1.00 41.33  ? 65  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 64  ? 40.906 -0.832  17.715 1.00 44.07  ? 65  LEU A C   1 
ATOM   579  O  O   . LEU A 1 64  ? 41.935 -1.403  18.067 1.00 45.86  ? 65  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 64  ? 40.987 1.621   17.803 1.00 42.12  ? 65  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 64  ? 41.623 2.904   17.321 1.00 49.01  ? 65  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 64  ? 41.475 3.972   18.364 1.00 49.57  ? 65  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 64  ? 43.107 2.718   16.980 1.00 54.04  ? 65  LEU A CD2 1 
ATOM   584  N  N   . LYS A 1 65  ? 39.697 -1.187  18.162 1.00 36.97  ? 66  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 65  ? 39.526 -2.297  19.096 1.00 35.18  ? 66  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 65  ? 39.650 -3.658  18.437 1.00 39.94  ? 66  LYS A C   1 
ATOM   587  O  O   . LYS A 1 65  ? 40.024 -4.609  19.118 1.00 37.81  ? 66  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 65  ? 38.202 -2.188  19.869 1.00 36.36  ? 66  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 65  ? 38.103 -0.962  20.769 1.00 35.27  ? 66  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 65  ? 36.816 -1.020  21.594 1.00 33.16  ? 66  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 65  ? 36.508 0.325   22.228 1.00 37.14  ? 66  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 65  ? 35.954 1.296   21.256 1.00 41.17  ? 66  LYS A NZ  1 
ATOM   593  N  N   . CYS A 1 66  ? 39.369 -3.751  17.116 1.00 39.70  ? 67  CYS A N   1 
ATOM   594  C  CA  . CYS A 1 66  ? 39.462 -5.014  16.359 1.00 40.16  ? 67  CYS A CA  1 
ATOM   595  C  C   . CYS A 1 66  ? 40.849 -5.658  16.492 1.00 45.39  ? 67  CYS A C   1 
ATOM   596  O  O   . CYS A 1 66  ? 40.975 -6.873  16.314 1.00 44.87  ? 67  CYS A O   1 
ATOM   597  C  CB  . CYS A 1 66  ? 39.085 -4.804  14.892 1.00 41.69  ? 67  CYS A CB  1 
ATOM   598  S  SG  . CYS A 1 66  ? 40.261 -3.787  13.948 1.00 48.02  ? 67  CYS A SG  1 
ATOM   599  N  N   . ASN A 1 67  ? 41.879 -4.826  16.788 1.00 42.44  ? 68  ASN A N   1 
ATOM   600  C  CA  . ASN A 1 67  ? 43.286 -5.210  16.912 1.00 43.22  ? 68  ASN A CA  1 
ATOM   601  C  C   . ASN A 1 67  ? 43.762 -5.495  18.340 1.00 45.22  ? 68  ASN A C   1 
ATOM   602  O  O   . ASN A 1 67  ? 44.928 -5.852  18.536 1.00 44.74  ? 68  ASN A O   1 
ATOM   603  C  CB  . ASN A 1 67  ? 44.186 -4.160  16.244 1.00 45.57  ? 68  ASN A CB  1 
ATOM   604  C  CG  . ASN A 1 67  ? 44.017 -4.117  14.737 1.00 60.85  ? 68  ASN A CG  1 
ATOM   605  O  OD1 . ASN A 1 67  ? 44.023 -3.048  14.130 1.00 60.39  ? 68  ASN A OD1 1 
ATOM   606  N  ND2 . ASN A 1 67  ? 43.834 -5.272  14.097 1.00 49.83  ? 68  ASN A ND2 1 
ATOM   607  N  N   . LEU A 1 68  ? 42.879 -5.354  19.332 1.00 40.38  ? 69  LEU A N   1 
ATOM   608  C  CA  . LEU A 1 68  ? 43.263 -5.626  20.711 1.00 39.65  ? 69  LEU A CA  1 
ATOM   609  C  C   . LEU A 1 68  ? 43.251 -7.130  20.979 1.00 40.19  ? 69  LEU A C   1 
ATOM   610  O  O   . LEU A 1 68  ? 42.361 -7.817  20.475 1.00 37.83  ? 69  LEU A O   1 
ATOM   611  C  CB  . LEU A 1 68  ? 42.288 -4.926  21.672 1.00 39.67  ? 69  LEU A CB  1 
ATOM   612  C  CG  . LEU A 1 68  ? 42.300 -3.389  21.644 1.00 44.83  ? 69  LEU A CG  1 
ATOM   613  C  CD1 . LEU A 1 68  ? 41.223 -2.835  22.548 1.00 44.76  ? 69  LEU A CD1 1 
ATOM   614  C  CD2 . LEU A 1 68  ? 43.681 -2.823  22.033 1.00 46.56  ? 69  LEU A CD2 1 
ATOM   615  N  N   . SER A 1 69  ? 44.226 -7.612  21.788 1.00 36.53  ? 70  SER A N   1 
ATOM   616  C  CA  A SER A 1 69  ? 44.361 -9.018  22.187 0.42 35.73  ? 70  SER A CA  1 
ATOM   617  C  CA  B SER A 1 69  ? 44.328 -9.024  22.169 0.58 36.10  ? 70  SER A CA  1 
ATOM   618  C  C   . SER A 1 69  ? 43.720 -9.241  23.557 1.00 37.25  ? 70  SER A C   1 
ATOM   619  O  O   . SER A 1 69  ? 43.524 -10.380 23.977 1.00 33.65  ? 70  SER A O   1 
ATOM   620  C  CB  A SER A 1 69  ? 45.834 -9.417  22.231 0.42 40.32  ? 70  SER A CB  1 
ATOM   621  C  CB  B SER A 1 69  ? 45.782 -9.493  22.129 0.58 41.43  ? 70  SER A CB  1 
ATOM   622  O  OG  A SER A 1 69  ? 46.423 -9.345  20.944 0.42 46.10  ? 70  SER A OG  1 
ATOM   623  O  OG  B SER A 1 69  ? 46.594 -8.757  23.029 0.58 49.38  ? 70  SER A OG  1 
ATOM   624  N  N   . VAL A 1 70  ? 43.427 -8.140  24.274 1.00 33.51  ? 71  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 70  ? 42.817 -8.163  25.605 1.00 32.37  ? 71  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 70  ? 41.644 -7.188  25.640 1.00 34.11  ? 71  VAL A C   1 
ATOM   627  O  O   . VAL A 1 70  ? 41.796 -6.020  25.254 1.00 33.33  ? 71  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 70  ? 43.856 -7.821  26.725 1.00 37.49  ? 71  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 70  ? 43.220 -7.878  28.117 1.00 37.25  ? 71  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 70  ? 45.078 -8.738  26.659 1.00 38.15  ? 71  VAL A CG2 1 
ATOM   631  N  N   . ILE A 1 71  ? 40.495 -7.651  26.162 1.00 28.38  ? 72  ILE A N   1 
ATOM   632  C  CA  . ILE A 1 71  ? 39.300 -6.834  26.367 1.00 28.01  ? 72  ILE A CA  1 
ATOM   633  C  C   . ILE A 1 71  ? 38.909 -6.942  27.838 1.00 31.17  ? 72  ILE A C   1 
ATOM   634  O  O   . ILE A 1 71  ? 38.753 -8.049  28.349 1.00 30.07  ? 72  ILE A O   1 
ATOM   635  C  CB  . ILE A 1 71  ? 38.128 -7.216  25.393 1.00 29.68  ? 72  ILE A CB  1 
ATOM   636  C  CG1 . ILE A 1 71  ? 38.525 -7.072  23.886 1.00 31.07  ? 72  ILE A CG1 1 
ATOM   637  C  CG2 . ILE A 1 71  ? 36.834 -6.447  25.716 1.00 31.69  ? 72  ILE A CG2 1 
ATOM   638  C  CD1 . ILE A 1 71  ? 38.888 -5.640  23.365 1.00 36.16  ? 72  ILE A CD1 1 
ATOM   639  N  N   . ASN A 1 72  ? 38.753 -5.801  28.517 1.00 28.13  ? 73  ASN A N   1 
ATOM   640  C  CA  . ASN A 1 72  ? 38.356 -5.785  29.913 1.00 28.43  ? 73  ASN A CA  1 
ATOM   641  C  C   . ASN A 1 72  ? 36.876 -5.461  30.021 1.00 30.69  ? 73  ASN A C   1 
ATOM   642  O  O   . ASN A 1 72  ? 36.439 -4.396  29.570 1.00 29.22  ? 73  ASN A O   1 
ATOM   643  C  CB  . ASN A 1 72  ? 39.183 -4.751  30.701 1.00 32.34  ? 73  ASN A CB  1 
ATOM   644  C  CG  . ASN A 1 72  ? 40.663 -4.991  30.660 1.00 50.13  ? 73  ASN A CG  1 
ATOM   645  O  OD1 . ASN A 1 72  ? 41.164 -5.977  31.175 1.00 42.32  ? 73  ASN A OD1 1 
ATOM   646  N  ND2 . ASN A 1 72  ? 41.400 -4.087  30.062 1.00 49.01  ? 73  ASN A ND2 1 
ATOM   647  N  N   . LEU A 1 73  ? 36.107 -6.343  30.644 1.00 25.91  ? 74  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 73  ? 34.681 -6.081  30.823 1.00 25.96  ? 74  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 73  ? 34.447 -5.181  32.020 1.00 29.63  ? 74  LEU A C   1 
ATOM   650  O  O   . LEU A 1 73  ? 35.322 -5.047  32.889 1.00 30.37  ? 74  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 73  ? 33.860 -7.374  30.972 1.00 26.06  ? 74  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 73  ? 33.927 -8.376  29.792 1.00 29.41  ? 74  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 73  ? 32.825 -9.441  29.928 1.00 29.16  ? 74  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 73  ? 33.882 -7.664  28.410 1.00 30.64  ? 74  LEU A CD2 1 
ATOM   655  N  N   . ASP A 1 74  ? 33.246 -4.598  32.085 1.00 26.57  ? 75  ASP A N   1 
ATOM   656  C  CA  . ASP A 1 74  ? 32.828 -3.698  33.172 1.00 28.52  ? 75  ASP A CA  1 
ATOM   657  C  C   . ASP A 1 74  ? 32.990 -4.443  34.524 1.00 34.72  ? 75  ASP A C   1 
ATOM   658  O  O   . ASP A 1 74  ? 32.623 -5.614  34.599 1.00 33.47  ? 75  ASP A O   1 
ATOM   659  C  CB  . ASP A 1 74  ? 31.366 -3.275  32.944 1.00 30.16  ? 75  ASP A CB  1 
ATOM   660  C  CG  . ASP A 1 74  ? 30.832 -2.266  33.952 1.00 42.16  ? 75  ASP A CG  1 
ATOM   661  O  OD1 . ASP A 1 74  ? 30.697 -2.624  35.141 1.00 43.22  ? 75  ASP A OD1 1 
ATOM   662  O  OD2 . ASP A 1 74  ? 30.518 -1.134  33.542 1.00 44.49  ? 75  ASP A OD2 1 
ATOM   663  N  N   . PRO A 1 75  ? 33.573 -3.811  35.574 1.00 35.58  ? 76  PRO A N   1 
ATOM   664  C  CA  . PRO A 1 75  ? 33.787 -4.540  36.847 1.00 35.79  ? 76  PRO A CA  1 
ATOM   665  C  C   . PRO A 1 75  ? 32.546 -5.101  37.518 1.00 39.15  ? 76  PRO A C   1 
ATOM   666  O  O   . PRO A 1 75  ? 32.687 -5.977  38.362 1.00 40.07  ? 76  PRO A O   1 
ATOM   667  C  CB  . PRO A 1 75  ? 34.492 -3.515  37.750 1.00 38.94  ? 76  PRO A CB  1 
ATOM   668  C  CG  . PRO A 1 75  ? 34.220 -2.179  37.124 1.00 44.16  ? 76  PRO A CG  1 
ATOM   669  C  CD  . PRO A 1 75  ? 34.110 -2.434  35.645 1.00 38.25  ? 76  PRO A CD  1 
ATOM   670  N  N   . GLU A 1 76  ? 31.342 -4.655  37.132 1.00 35.56  ? 77  GLU A N   1 
ATOM   671  C  CA  . GLU A 1 76  ? 30.114 -5.190  37.720 1.00 36.48  ? 77  GLU A CA  1 
ATOM   672  C  C   . GLU A 1 76  ? 29.798 -6.585  37.146 1.00 36.54  ? 77  GLU A C   1 
ATOM   673  O  O   . GLU A 1 76  ? 28.950 -7.284  37.696 1.00 35.25  ? 77  GLU A O   1 
ATOM   674  C  CB  . GLU A 1 76  ? 28.929 -4.230  37.498 1.00 39.09  ? 77  GLU A CB  1 
ATOM   675  C  CG  . GLU A 1 76  ? 28.913 -3.034  38.439 1.00 59.77  ? 77  GLU A CG  1 
ATOM   676  C  CD  . GLU A 1 76  ? 28.377 -3.330  39.827 1.00 93.60  ? 77  GLU A CD  1 
ATOM   677  O  OE1 . GLU A 1 76  ? 27.146 -3.517  39.963 1.00 96.14  ? 77  GLU A OE1 1 
ATOM   678  O  OE2 . GLU A 1 76  ? 29.190 -3.381  40.778 1.00 93.73  ? 77  GLU A OE2 1 
ATOM   679  N  N   . ILE A 1 77  ? 30.485 -6.991  36.053 1.00 31.20  ? 78  ILE A N   1 
ATOM   680  C  CA  . ILE A 1 77  ? 30.234 -8.303  35.448 1.00 29.64  ? 78  ILE A CA  1 
ATOM   681  C  C   . ILE A 1 77  ? 30.828 -9.421  36.303 1.00 34.56  ? 78  ILE A C   1 
ATOM   682  O  O   . ILE A 1 77  ? 32.004 -9.399  36.661 1.00 33.65  ? 78  ILE A O   1 
ATOM   683  C  CB  . ILE A 1 77  ? 30.668 -8.371  33.955 1.00 31.37  ? 78  ILE A CB  1 
ATOM   684  C  CG1 . ILE A 1 77  ? 29.944 -7.279  33.107 1.00 32.49  ? 78  ILE A CG1 1 
ATOM   685  C  CG2 . ILE A 1 77  ? 30.465 -9.784  33.366 1.00 27.07  ? 78  ILE A CG2 1 
ATOM   686  C  CD1 . ILE A 1 77  ? 28.327 -7.288  33.164 1.00 37.56  ? 78  ILE A CD1 1 
ATOM   687  N  N   . ASN A 1 78  ? 30.001 -10.401 36.592 1.00 34.07  ? 79  ASN A N   1 
ATOM   688  C  CA  . ASN A 1 78  ? 30.339 -11.566 37.384 1.00 34.57  ? 79  ASN A CA  1 
ATOM   689  C  C   . ASN A 1 78  ? 31.057 -12.606 36.507 1.00 33.78  ? 79  ASN A C   1 
ATOM   690  O  O   . ASN A 1 78  ? 30.522 -12.989 35.466 1.00 31.31  ? 79  ASN A O   1 
ATOM   691  C  CB  . ASN A 1 78  ? 29.043 -12.132 37.990 1.00 39.05  ? 79  ASN A CB  1 
ATOM   692  C  CG  . ASN A 1 78  ? 29.221 -13.452 38.691 1.00 55.62  ? 79  ASN A CG  1 
ATOM   693  O  OD1 . ASN A 1 78  ? 28.839 -14.500 38.170 1.00 43.22  ? 79  ASN A OD1 1 
ATOM   694  N  ND2 . ASN A 1 78  ? 29.813 -13.427 39.879 1.00 48.48  ? 79  ASN A ND2 1 
ATOM   695  N  N   . PRO A 1 79  ? 32.256 -13.107 36.913 1.00 31.25  ? 80  PRO A N   1 
ATOM   696  C  CA  . PRO A 1 79  ? 32.955 -14.109 36.077 1.00 30.97  ? 80  PRO A CA  1 
ATOM   697  C  C   . PRO A 1 79  ? 32.167 -15.402 35.845 1.00 34.24  ? 80  PRO A C   1 
ATOM   698  O  O   . PRO A 1 79  ? 32.237 -15.957 34.749 1.00 33.50  ? 80  PRO A O   1 
ATOM   699  C  CB  . PRO A 1 79  ? 34.248 -14.380 36.853 1.00 34.02  ? 80  PRO A CB  1 
ATOM   700  C  CG  . PRO A 1 79  ? 34.431 -13.166 37.725 1.00 38.82  ? 80  PRO A CG  1 
ATOM   701  C  CD  . PRO A 1 79  ? 33.046 -12.770 38.117 1.00 34.17  ? 80  PRO A CD  1 
ATOM   702  N  N   . GLU A 1 80  ? 31.404 -15.876 36.848 1.00 31.15  ? 81  GLU A N   1 
ATOM   703  C  CA  . GLU A 1 80  ? 30.638 -17.114 36.639 1.00 30.84  ? 81  GLU A CA  1 
ATOM   704  C  C   . GLU A 1 80  ? 29.558 -16.904 35.571 1.00 32.34  ? 81  GLU A C   1 
ATOM   705  O  O   . GLU A 1 80  ? 29.433 -17.741 34.685 1.00 30.40  ? 81  GLU A O   1 
ATOM   706  C  CB  . GLU A 1 80  ? 30.027 -17.636 37.948 1.00 33.69  ? 81  GLU A CB  1 
ATOM   707  C  CG  . GLU A 1 80  ? 29.398 -19.011 37.747 1.00 44.58  ? 81  GLU A CG  1 
ATOM   708  C  CD  . GLU A 1 80  ? 28.572 -19.569 38.893 1.00 72.92  ? 81  GLU A CD  1 
ATOM   709  O  OE1 . GLU A 1 80  ? 28.541 -20.812 39.038 1.00 68.06  ? 81  GLU A OE1 1 
ATOM   710  O  OE2 . GLU A 1 80  ? 27.950 -18.775 39.638 1.00 68.35  ? 81  GLU A OE2 1 
ATOM   711  N  N   . GLY A 1 81  ? 28.839 -15.772 35.638 1.00 30.56  ? 82  GLY A N   1 
ATOM   712  C  CA  . GLY A 1 81  ? 27.834 -15.424 34.633 1.00 30.05  ? 82  GLY A CA  1 
ATOM   713  C  C   . GLY A 1 81  ? 28.462 -15.389 33.247 1.00 30.85  ? 82  GLY A C   1 
ATOM   714  O  O   . GLY A 1 81  ? 27.906 -15.935 32.282 1.00 28.67  ? 82  GLY A O   1 
ATOM   715  N  N   . PHE A 1 82  ? 29.659 -14.790 33.143 1.00 26.59  ? 83  PHE A N   1 
ATOM   716  C  CA  . PHE A 1 82  ? 30.349 -14.743 31.850 1.00 25.22  ? 83  PHE A CA  1 
ATOM   717  C  C   . PHE A 1 82  ? 30.714 -16.143 31.376 1.00 27.27  ? 83  PHE A C   1 
ATOM   718  O  O   . PHE A 1 82  ? 30.534 -16.454 30.204 1.00 25.92  ? 83  PHE A O   1 
ATOM   719  C  CB  . PHE A 1 82  ? 31.626 -13.888 31.903 1.00 26.62  ? 83  PHE A CB  1 
ATOM   720  C  CG  . PHE A 1 82  ? 32.214 -13.744 30.519 1.00 26.92  ? 83  PHE A CG  1 
ATOM   721  C  CD1 . PHE A 1 82  ? 31.644 -12.873 29.590 1.00 29.50  ? 83  PHE A CD1 1 
ATOM   722  C  CD2 . PHE A 1 82  ? 33.291 -14.527 30.118 1.00 27.49  ? 83  PHE A CD2 1 
ATOM   723  C  CE1 . PHE A 1 82  ? 32.147 -12.789 28.286 1.00 29.94  ? 83  PHE A CE1 1 
ATOM   724  C  CE2 . PHE A 1 82  ? 33.797 -14.437 28.819 1.00 29.02  ? 83  PHE A CE2 1 
ATOM   725  C  CZ  . PHE A 1 82  ? 33.211 -13.580 27.908 1.00 28.22  ? 83  PHE A CZ  1 
ATOM   726  N  N   . CYS A 1 83  ? 31.295 -16.956 32.259 1.00 27.56  ? 84  CYS A N   1 
ATOM   727  C  CA  . CYS A 1 83  ? 31.703 -18.328 31.932 1.00 29.73  ? 84  CYS A CA  1 
ATOM   728  C  C   . CYS A 1 83  ? 30.504 -19.136 31.357 1.00 30.22  ? 84  CYS A C   1 
ATOM   729  O  O   . CYS A 1 83  ? 30.643 -19.809 30.327 1.00 28.16  ? 84  CYS A O   1 
ATOM   730  C  CB  . CYS A 1 83  ? 32.288 -19.003 33.169 1.00 33.69  ? 84  CYS A CB  1 
ATOM   731  S  SG  . CYS A 1 83  ? 32.958 -20.656 32.847 1.00 39.69  ? 84  CYS A SG  1 
ATOM   732  N  N   . ILE A 1 84  ? 29.328 -19.052 32.026 1.00 27.37  ? 85  ILE A N   1 
ATOM   733  C  CA  . ILE A 1 84  ? 28.094 -19.745 31.606 1.00 25.66  ? 85  ILE A CA  1 
ATOM   734  C  C   . ILE A 1 84  ? 27.690 -19.284 30.201 1.00 26.88  ? 85  ILE A C   1 
ATOM   735  O  O   . ILE A 1 84  ? 27.323 -20.111 29.351 1.00 24.40  ? 85  ILE A O   1 
ATOM   736  C  CB  . ILE A 1 84  ? 26.955 -19.541 32.654 1.00 28.92  ? 85  ILE A CB  1 
ATOM   737  C  CG1 . ILE A 1 84  ? 27.227 -20.374 33.942 1.00 30.06  ? 85  ILE A CG1 1 
ATOM   738  C  CG2 . ILE A 1 84  ? 25.542 -19.827 32.067 1.00 28.51  ? 85  ILE A CG2 1 
ATOM   739  C  CD1 . ILE A 1 84  ? 26.517 -19.803 35.153 1.00 36.37  ? 85  ILE A CD1 1 
ATOM   740  N  N   . LEU A 1 85  ? 27.770 -17.982 29.951 1.00 23.76  ? 86  LEU A N   1 
ATOM   741  C  CA  . LEU A 1 85  ? 27.414 -17.433 28.637 1.00 23.80  ? 86  LEU A CA  1 
ATOM   742  C  C   . LEU A 1 85  ? 28.417 -17.787 27.565 1.00 26.58  ? 86  LEU A C   1 
ATOM   743  O  O   . LEU A 1 85  ? 28.020 -18.080 26.436 1.00 24.15  ? 86  LEU A O   1 
ATOM   744  C  CB  . LEU A 1 85  ? 27.166 -15.934 28.716 1.00 24.98  ? 86  LEU A CB  1 
ATOM   745  C  CG  . LEU A 1 85  ? 25.858 -15.564 29.452 1.00 31.49  ? 86  LEU A CG  1 
ATOM   746  C  CD1 . LEU A 1 85  ? 25.788 -14.107 29.669 1.00 33.24  ? 86  LEU A CD1 1 
ATOM   747  C  CD2 . LEU A 1 85  ? 24.627 -15.994 28.655 1.00 33.45  ? 86  LEU A CD2 1 
ATOM   748  N  N   . LEU A 1 86  ? 29.718 -17.792 27.916 1.00 24.38  ? 87  LEU A N   1 
ATOM   749  C  CA  . LEU A 1 86  ? 30.768 -18.205 26.965 1.00 23.49  ? 87  LEU A CA  1 
ATOM   750  C  C   . LEU A 1 86  ? 30.530 -19.674 26.572 1.00 26.60  ? 87  LEU A C   1 
ATOM   751  O  O   . LEU A 1 86  ? 30.593 -20.012 25.392 1.00 25.16  ? 87  LEU A O   1 
ATOM   752  C  CB  . LEU A 1 86  ? 32.167 -18.008 27.572 1.00 23.43  ? 87  LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 86  ? 33.340 -18.314 26.618 1.00 28.37  ? 87  LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 86  ? 33.318 -17.387 25.376 1.00 27.63  ? 87  LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 86  ? 34.698 -18.206 27.369 1.00 32.01  ? 87  LEU A CD2 1 
ATOM   756  N  N   . ASP A 1 87  ? 30.224 -20.546 27.556 1.00 25.09  ? 88  ASP A N   1 
ATOM   757  C  CA  . ASP A 1 87  ? 29.900 -21.935 27.272 1.00 24.70  ? 88  ASP A CA  1 
ATOM   758  C  C   . ASP A 1 87  ? 28.694 -22.040 26.338 1.00 27.31  ? 88  ASP A C   1 
ATOM   759  O  O   . ASP A 1 87  ? 28.735 -22.824 25.393 1.00 26.98  ? 88  ASP A O   1 
ATOM   760  C  CB  . ASP A 1 87  ? 29.610 -22.677 28.583 1.00 27.86  ? 88  ASP A CB  1 
ATOM   761  C  CG  . ASP A 1 87  ? 30.856 -23.040 29.370 1.00 41.25  ? 88  ASP A CG  1 
ATOM   762  O  OD1 . ASP A 1 87  ? 31.972 -22.985 28.784 1.00 41.74  ? 88  ASP A OD1 1 
ATOM   763  O  OD2 . ASP A 1 87  ? 30.720 -23.396 30.570 1.00 43.43  ? 88  ASP A OD2 1 
ATOM   764  N  N   . PHE A 1 88  ? 27.633 -21.251 26.590 1.00 24.00  ? 89  PHE A N   1 
ATOM   765  C  CA  . PHE A 1 88  ? 26.437 -21.208 25.719 1.00 22.90  ? 89  PHE A CA  1 
ATOM   766  C  C   . PHE A 1 88  ? 26.813 -20.827 24.274 1.00 24.35  ? 89  PHE A C   1 
ATOM   767  O  O   . PHE A 1 88  ? 26.321 -21.420 23.303 1.00 22.18  ? 89  PHE A O   1 
ATOM   768  C  CB  . PHE A 1 88  ? 25.384 -20.226 26.292 1.00 23.70  ? 89  PHE A CB  1 
ATOM   769  C  CG  . PHE A 1 88  ? 24.264 -19.946 25.315 1.00 24.15  ? 89  PHE A CG  1 
ATOM   770  C  CD1 . PHE A 1 88  ? 23.298 -20.910 25.049 1.00 26.15  ? 89  PHE A CD1 1 
ATOM   771  C  CD2 . PHE A 1 88  ? 24.252 -18.769 24.560 1.00 25.96  ? 89  PHE A CD2 1 
ATOM   772  C  CE1 . PHE A 1 88  ? 22.300 -20.679 24.104 1.00 26.07  ? 89  PHE A CE1 1 
ATOM   773  C  CE2 . PHE A 1 88  ? 23.261 -18.546 23.597 1.00 28.63  ? 89  PHE A CE2 1 
ATOM   774  C  CZ  . PHE A 1 88  ? 22.291 -19.500 23.376 1.00 26.92  ? 89  PHE A CZ  1 
ATOM   775  N  N   . MET A 1 89  ? 27.641 -19.805 24.125 1.00 20.67  ? 90  MET A N   1 
ATOM   776  C  CA  . MET A 1 89  ? 28.067 -19.355 22.784 1.00 20.27  ? 90  MET A CA  1 
ATOM   777  C  C   . MET A 1 89  ? 28.636 -20.507 21.976 1.00 24.36  ? 90  MET A C   1 
ATOM   778  O  O   . MET A 1 89  ? 28.295 -20.661 20.809 1.00 23.65  ? 90  MET A O   1 
ATOM   779  C  CB  . MET A 1 89  ? 29.156 -18.273 22.894 1.00 20.93  ? 90  MET A CB  1 
ATOM   780  C  CG  . MET A 1 89  ? 28.640 -16.969 23.467 1.00 22.93  ? 90  MET A CG  1 
ATOM   781  S  SD  . MET A 1 89  ? 30.004 -15.752 23.353 1.00 26.30  ? 90  MET A SD  1 
ATOM   782  C  CE  . MET A 1 89  ? 29.364 -14.482 24.449 1.00 25.67  ? 90  MET A CE  1 
ATOM   783  N  N   . TYR A 1 90  ? 29.491 -21.322 22.615 1.00 20.82  ? 91  TYR A N   1 
ATOM   784  C  CA  . TYR A 1 90  ? 30.163 -22.426 21.935 1.00 20.88  ? 91  TYR A CA  1 
ATOM   785  C  C   . TYR A 1 90  ? 29.408 -23.749 21.920 1.00 25.60  ? 91  TYR A C   1 
ATOM   786  O  O   . TYR A 1 90  ? 29.891 -24.699 21.289 1.00 24.01  ? 91  TYR A O   1 
ATOM   787  C  CB  . TYR A 1 90  ? 31.538 -22.637 22.572 1.00 22.22  ? 91  TYR A CB  1 
ATOM   788  C  CG  . TYR A 1 90  ? 32.599 -21.673 22.077 1.00 22.92  ? 91  TYR A CG  1 
ATOM   789  C  CD1 . TYR A 1 90  ? 32.771 -20.426 22.674 1.00 23.83  ? 91  TYR A CD1 1 
ATOM   790  C  CD2 . TYR A 1 90  ? 33.432 -22.011 21.009 1.00 24.13  ? 91  TYR A CD2 1 
ATOM   791  C  CE1 . TYR A 1 90  ? 33.763 -19.546 22.236 1.00 23.43  ? 91  TYR A CE1 1 
ATOM   792  C  CE2 . TYR A 1 90  ? 34.463 -21.167 20.601 1.00 24.70  ? 91  TYR A CE2 1 
ATOM   793  C  CZ  . TYR A 1 90  ? 34.606 -19.924 21.198 1.00 26.72  ? 91  TYR A CZ  1 
ATOM   794  O  OH  . TYR A 1 90  ? 35.634 -19.106 20.805 1.00 26.27  ? 91  TYR A OH  1 
ATOM   795  N  N   . THR A 1 91  ? 28.262 -23.854 22.623 1.00 22.57  ? 92  THR A N   1 
ATOM   796  C  CA  . THR A 1 91  ? 27.570 -25.153 22.675 1.00 23.52  ? 92  THR A CA  1 
ATOM   797  C  C   . THR A 1 91  ? 26.058 -25.116 22.403 1.00 25.74  ? 92  THR A C   1 
ATOM   798  O  O   . THR A 1 91  ? 25.474 -26.191 22.227 1.00 25.06  ? 92  THR A O   1 
ATOM   799  C  CB  . THR A 1 91  ? 27.766 -25.826 24.079 1.00 29.20  ? 92  THR A CB  1 
ATOM   800  O  OG1 . THR A 1 91  ? 27.105 -25.036 25.069 1.00 28.49  ? 92  THR A OG1 1 
ATOM   801  C  CG2 . THR A 1 91  ? 29.242 -26.024 24.472 1.00 29.95  ? 92  THR A CG2 1 
ATOM   802  N  N   . SER A 1 92  ? 25.404 -23.936 22.514 1.00 21.65  ? 93  SER A N   1 
ATOM   803  C  CA  . SER A 1 92  ? 23.921 -23.759 22.463 1.00 21.32  ? 93  SER A CA  1 
ATOM   804  C  C   . SER A 1 92  ? 23.265 -24.165 23.810 1.00 25.82  ? 93  SER A C   1 
ATOM   805  O  O   . SER A 1 92  ? 22.056 -24.020 23.945 1.00 26.19  ? 93  SER A O   1 
ATOM   806  C  CB  . SER A 1 92  ? 23.270 -24.584 21.337 1.00 23.09  ? 93  SER A CB  1 
ATOM   807  O  OG  . SER A 1 92  ? 23.923 -24.417 20.089 1.00 30.05  ? 93  SER A OG  1 
ATOM   808  N  N   A ARG A 1 93  ? 24.060 -24.649 24.783 0.60 23.85  ? 94  ARG A N   1 
ATOM   809  N  N   B ARG A 1 93  ? 24.047 -24.678 24.785 0.40 23.05  ? 94  ARG A N   1 
ATOM   810  C  CA  A ARG A 1 93  ? 23.557 -25.092 26.083 0.60 24.83  ? 94  ARG A CA  1 
ATOM   811  C  CA  B ARG A 1 93  ? 23.505 -25.104 26.080 0.40 23.76  ? 94  ARG A CA  1 
ATOM   812  C  C   A ARG A 1 93  ? 23.781 -24.020 27.142 0.60 28.43  ? 94  ARG A C   1 
ATOM   813  C  C   B ARG A 1 93  ? 23.781 -24.088 27.175 0.40 28.04  ? 94  ARG A C   1 
ATOM   814  O  O   A ARG A 1 93  ? 24.904 -23.522 27.312 0.60 27.23  ? 94  ARG A O   1 
ATOM   815  O  O   B ARG A 1 93  ? 24.930 -23.678 27.386 0.40 27.12  ? 94  ARG A O   1 
ATOM   816  C  CB  A ARG A 1 93  ? 24.224 -26.409 26.514 0.60 27.34  ? 94  ARG A CB  1 
ATOM   817  C  CB  B ARG A 1 93  ? 23.971 -26.516 26.468 0.40 24.62  ? 94  ARG A CB  1 
ATOM   818  C  CG  A ARG A 1 93  ? 24.055 -27.558 25.510 0.60 33.11  ? 94  ARG A CG  1 
ATOM   819  C  CG  B ARG A 1 93  ? 23.355 -27.581 25.570 0.40 26.73  ? 94  ARG A CG  1 
ATOM   820  C  CD  A ARG A 1 93  ? 25.022 -28.702 25.798 0.60 41.55  ? 94  ARG A CD  1 
ATOM   821  C  CD  B ARG A 1 93  ? 24.038 -28.925 25.665 0.40 38.14  ? 94  ARG A CD  1 
ATOM   822  N  NE  A ARG A 1 93  ? 24.830 -29.252 27.143 0.60 46.43  ? 94  ARG A NE  1 
ATOM   823  N  NE  B ARG A 1 93  ? 23.463 -29.865 24.703 0.40 44.02  ? 94  ARG A NE  1 
ATOM   824  C  CZ  A ARG A 1 93  ? 23.971 -30.222 27.441 0.60 58.61  ? 94  ARG A CZ  1 
ATOM   825  C  CZ  B ARG A 1 93  ? 23.349 -31.174 24.902 0.40 57.08  ? 94  ARG A CZ  1 
ATOM   826  N  NH1 A ARG A 1 93  ? 23.855 -30.652 28.688 0.60 43.51  ? 94  ARG A NH1 1 
ATOM   827  N  NH1 B ARG A 1 93  ? 22.814 -31.949 23.968 0.40 46.71  ? 94  ARG A NH1 1 
ATOM   828  N  NH2 A ARG A 1 93  ? 23.220 -30.768 26.491 0.60 44.96  ? 94  ARG A NH2 1 
ATOM   829  N  NH2 B ARG A 1 93  ? 23.767 -31.720 26.036 0.40 43.01  ? 94  ARG A NH2 1 
ATOM   830  N  N   . LEU A 1 94  ? 22.707 -23.674 27.856 1.00 25.24  ? 95  LEU A N   1 
ATOM   831  C  CA  . LEU A 1 94  ? 22.745 -22.670 28.903 1.00 25.03  ? 95  LEU A CA  1 
ATOM   832  C  C   . LEU A 1 94  ? 22.497 -23.321 30.263 1.00 31.18  ? 95  LEU A C   1 
ATOM   833  O  O   . LEU A 1 94  ? 21.414 -23.870 30.505 1.00 30.87  ? 95  LEU A O   1 
ATOM   834  C  CB  . LEU A 1 94  ? 21.698 -21.594 28.592 1.00 25.23  ? 95  LEU A CB  1 
ATOM   835  C  CG  . LEU A 1 94  ? 21.717 -20.370 29.538 1.00 29.64  ? 95  LEU A CG  1 
ATOM   836  C  CD1 . LEU A 1 94  ? 22.980 -19.535 29.299 1.00 28.39  ? 95  LEU A CD1 1 
ATOM   837  C  CD2 . LEU A 1 94  ? 20.468 -19.530 29.351 1.00 31.02  ? 95  LEU A CD2 1 
ATOM   838  N  N   . ASN A 1 95  ? 23.496 -23.239 31.163 1.00 30.75  ? 96  ASN A N   1 
ATOM   839  C  CA  . ASN A 1 95  ? 23.409 -23.816 32.511 1.00 32.19  ? 96  ASN A CA  1 
ATOM   840  C  C   . ASN A 1 95  ? 22.700 -22.809 33.436 1.00 36.14  ? 96  ASN A C   1 
ATOM   841  O  O   . ASN A 1 95  ? 23.342 -22.122 34.224 1.00 35.60  ? 96  ASN A O   1 
ATOM   842  C  CB  . ASN A 1 95  ? 24.823 -24.175 33.043 1.00 35.87  ? 96  ASN A CB  1 
ATOM   843  C  CG  . ASN A 1 95  ? 24.805 -24.805 34.433 1.00 53.68  ? 96  ASN A CG  1 
ATOM   844  O  OD1 . ASN A 1 95  ? 23.814 -25.396 34.866 1.00 44.77  ? 96  ASN A OD1 1 
ATOM   845  N  ND2 . ASN A 1 95  ? 25.892 -24.672 35.175 1.00 45.32  ? 96  ASN A ND2 1 
ATOM   846  N  N   . LEU A 1 96  ? 21.392 -22.674 33.272 1.00 33.12  ? 97  LEU A N   1 
ATOM   847  C  CA  . LEU A 1 96  ? 20.591 -21.704 34.016 1.00 34.04  ? 97  LEU A CA  1 
ATOM   848  C  C   . LEU A 1 96  ? 20.061 -22.335 35.286 1.00 38.75  ? 97  LEU A C   1 
ATOM   849  O  O   . LEU A 1 96  ? 19.412 -23.385 35.216 1.00 37.26  ? 97  LEU A O   1 
ATOM   850  C  CB  . LEU A 1 96  ? 19.452 -21.241 33.098 1.00 34.90  ? 97  LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 96  ? 18.746 -19.939 33.415 1.00 41.05  ? 97  LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 96  ? 19.752 -18.756 33.521 1.00 40.55  ? 97  LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 96  ? 17.672 -19.667 32.367 1.00 41.91  ? 97  LEU A CD2 1 
ATOM   854  N  N   . ARG A 1 97  ? 20.379 -21.731 36.455 1.00 35.22  ? 98  ARG A N   1 
ATOM   855  C  CA  . ARG A 1 97  ? 19.975 -22.258 37.774 1.00 37.65  ? 98  ARG A CA  1 
ATOM   856  C  C   . ARG A 1 97  ? 19.440 -21.141 38.660 1.00 40.28  ? 98  ARG A C   1 
ATOM   857  O  O   . ARG A 1 97  ? 19.782 -19.974 38.442 1.00 38.21  ? 98  ARG A O   1 
ATOM   858  C  CB  . ARG A 1 97  ? 21.169 -22.941 38.473 1.00 38.37  ? 98  ARG A CB  1 
ATOM   859  C  CG  . ARG A 1 97  ? 21.811 -24.080 37.659 1.00 46.20  ? 98  ARG A CG  1 
ATOM   860  C  CD  . ARG A 1 97  ? 23.077 -24.646 38.294 1.00 65.51  ? 98  ARG A CD  1 
ATOM   861  N  NE  . ARG A 1 97  ? 22.849 -25.149 39.655 1.00 85.28  ? 98  ARG A NE  1 
ATOM   862  C  CZ  . ARG A 1 97  ? 22.405 -26.369 39.951 1.00 105.44 ? 98  ARG A CZ  1 
ATOM   863  N  NH1 . ARG A 1 97  ? 22.218 -26.724 41.216 1.00 93.59  ? 98  ARG A NH1 1 
ATOM   864  N  NH2 . ARG A 1 97  ? 22.141 -27.242 38.985 1.00 95.30  ? 98  ARG A NH2 1 
ATOM   865  N  N   . GLU A 1 98  ? 18.620 -21.478 39.674 1.00 38.07  ? 99  GLU A N   1 
ATOM   866  C  CA  . GLU A 1 98  ? 18.096 -20.459 40.596 1.00 38.80  ? 99  GLU A CA  1 
ATOM   867  C  C   . GLU A 1 98  ? 19.226 -19.567 41.156 1.00 43.80  ? 99  GLU A C   1 
ATOM   868  O  O   . GLU A 1 98  ? 19.053 -18.351 41.251 1.00 43.55  ? 99  GLU A O   1 
ATOM   869  C  CB  . GLU A 1 98  ? 17.329 -21.130 41.762 1.00 42.50  ? 99  GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 98  ? 16.548 -20.156 42.626 1.00 55.88  ? 99  GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 98  ? 15.887 -20.766 43.849 1.00 90.57  ? 99  GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 98  ? 16.500 -21.651 44.493 1.00 88.54  ? 99  GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 98  ? 14.752 -20.348 44.169 1.00 94.66  ? 99  GLU A OE2 1 
ATOM   874  N  N   . GLY A 1 99  ? 20.365 -20.181 41.489 1.00 41.49  ? 100 GLY A N   1 
ATOM   875  C  CA  . GLY A 1 99  ? 21.517 -19.487 42.067 1.00 41.77  ? 100 GLY A CA  1 
ATOM   876  C  C   . GLY A 1 99  ? 22.330 -18.626 41.116 1.00 42.78  ? 100 GLY A C   1 
ATOM   877  O  O   . GLY A 1 99  ? 23.156 -17.825 41.564 1.00 42.47  ? 100 GLY A O   1 
ATOM   878  N  N   . ASN A 1 100 ? 22.114 -18.752 39.799 1.00 37.53  ? 101 ASN A N   1 
ATOM   879  C  CA  . ASN A 1 100 ? 22.904 -17.935 38.876 1.00 35.13  ? 101 ASN A CA  1 
ATOM   880  C  C   . ASN A 1 100 ? 22.076 -17.068 37.915 1.00 38.42  ? 101 ASN A C   1 
ATOM   881  O  O   . ASN A 1 100 ? 22.659 -16.268 37.175 1.00 36.21  ? 101 ASN A O   1 
ATOM   882  C  CB  . ASN A 1 100 ? 23.881 -18.833 38.088 1.00 32.17  ? 101 ASN A CB  1 
ATOM   883  C  CG  . ASN A 1 100 ? 23.226 -19.773 37.096 1.00 40.19  ? 101 ASN A CG  1 
ATOM   884  O  OD1 . ASN A 1 100 ? 22.175 -19.472 36.514 1.00 32.12  ? 101 ASN A OD1 1 
ATOM   885  N  ND2 . ASN A 1 100 ? 23.856 -20.916 36.839 1.00 33.74  ? 101 ASN A ND2 1 
ATOM   886  N  N   . ILE A 1 101 ? 20.739 -17.256 37.886 1.00 35.44  ? 102 ILE A N   1 
ATOM   887  C  CA  . ILE A 1 101 ? 19.864 -16.600 36.903 1.00 35.13  ? 102 ILE A CA  1 
ATOM   888  C  C   . ILE A 1 101 ? 20.004 -15.070 36.883 1.00 37.15  ? 102 ILE A C   1 
ATOM   889  O  O   . ILE A 1 101 ? 20.049 -14.490 35.789 1.00 34.66  ? 102 ILE A O   1 
ATOM   890  C  CB  . ILE A 1 101 ? 18.384 -17.048 37.002 1.00 39.64  ? 102 ILE A CB  1 
ATOM   891  C  CG1 . ILE A 1 101 ? 17.543 -16.462 35.833 1.00 40.53  ? 102 ILE A CG1 1 
ATOM   892  C  CG2 . ILE A 1 101 ? 17.753 -16.786 38.379 1.00 38.29  ? 102 ILE A CG2 1 
ATOM   893  C  CD1 . ILE A 1 101 ? 16.351 -17.292 35.423 1.00 40.54  ? 102 ILE A CD1 1 
ATOM   894  N  N   . MET A 1 102 ? 20.097 -14.422 38.057 1.00 35.43  ? 103 MET A N   1 
ATOM   895  C  CA  . MET A 1 102 ? 20.246 -12.967 38.090 1.00 36.37  ? 103 MET A CA  1 
ATOM   896  C  C   . MET A 1 102 ? 21.551 -12.514 37.456 1.00 38.01  ? 103 MET A C   1 
ATOM   897  O  O   . MET A 1 102 ? 21.523 -11.574 36.664 1.00 36.30  ? 103 MET A O   1 
ATOM   898  C  CB  . MET A 1 102 ? 20.065 -12.392 39.507 1.00 40.73  ? 103 MET A CB  1 
ATOM   899  C  CG  . MET A 1 102 ? 18.685 -12.678 40.114 1.00 47.78  ? 103 MET A CG  1 
ATOM   900  S  SD  . MET A 1 102 ? 17.244 -12.308 39.057 1.00 54.19  ? 103 MET A SD  1 
ATOM   901  C  CE  . MET A 1 102 ? 17.239 -10.487 39.136 1.00 51.45  ? 103 MET A CE  1 
ATOM   902  N  N   . ALA A 1 103 ? 22.686 -13.192 37.769 1.00 34.94  ? 104 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 103 ? 24.005 -12.858 37.186 1.00 34.32  ? 104 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 103 ? 24.013 -13.145 35.678 1.00 35.24  ? 104 ALA A C   1 
ATOM   905  O  O   . ALA A 1 103 ? 24.528 -12.338 34.893 1.00 32.72  ? 104 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 103 ? 25.103 -13.666 37.867 1.00 35.96  ? 104 ALA A CB  1 
ATOM   907  N  N   . VAL A 1 104 ? 23.439 -14.296 35.276 1.00 30.06  ? 105 VAL A N   1 
ATOM   908  C  CA  . VAL A 1 104 ? 23.374 -14.672 33.854 1.00 28.20  ? 105 VAL A CA  1 
ATOM   909  C  C   . VAL A 1 104 ? 22.576 -13.643 33.054 1.00 30.93  ? 105 VAL A C   1 
ATOM   910  O  O   . VAL A 1 104 ? 23.075 -13.197 32.016 1.00 28.91  ? 105 VAL A O   1 
ATOM   911  C  CB  . VAL A 1 104 ? 22.890 -16.126 33.623 1.00 31.33  ? 105 VAL A CB  1 
ATOM   912  C  CG1 . VAL A 1 104 ? 22.667 -16.406 32.133 1.00 29.74  ? 105 VAL A CG1 1 
ATOM   913  C  CG2 . VAL A 1 104 ? 23.893 -17.119 34.200 1.00 31.11  ? 105 VAL A CG2 1 
ATOM   914  N  N   A MET A 1 105 ? 21.379 -13.247 33.535 0.65 29.63  ? 106 MET A N   1 
ATOM   915  N  N   B MET A 1 105 ? 21.375 -13.248 33.533 0.35 30.07  ? 106 MET A N   1 
ATOM   916  C  CA  A MET A 1 105 ? 20.549 -12.255 32.837 0.65 30.52  ? 106 MET A CA  1 
ATOM   917  C  CA  B MET A 1 105 ? 20.540 -12.256 32.844 0.35 31.07  ? 106 MET A CA  1 
ATOM   918  C  C   A MET A 1 105 ? 21.254 -10.905 32.721 0.65 34.71  ? 106 MET A C   1 
ATOM   919  C  C   B MET A 1 105 ? 21.250 -10.908 32.721 0.35 34.97  ? 106 MET A C   1 
ATOM   920  O  O   A MET A 1 105 ? 21.214 -10.292 31.653 0.65 33.90  ? 106 MET A O   1 
ATOM   921  O  O   B MET A 1 105 ? 21.223 -10.309 31.644 0.35 34.18  ? 106 MET A O   1 
ATOM   922  C  CB  A MET A 1 105 ? 19.186 -12.072 33.510 0.65 34.24  ? 106 MET A CB  1 
ATOM   923  C  CB  B MET A 1 105 ? 19.178 -12.074 33.528 0.35 35.10  ? 106 MET A CB  1 
ATOM   924  C  CG  A MET A 1 105 ? 18.259 -11.166 32.712 0.65 38.49  ? 106 MET A CG  1 
ATOM   925  C  CG  B MET A 1 105 ? 18.238 -11.188 32.731 0.35 39.77  ? 106 MET A CG  1 
ATOM   926  S  SD  A MET A 1 105 ? 16.575 -11.190 33.325 0.65 45.03  ? 106 MET A SD  1 
ATOM   927  S  SD  B MET A 1 105 ? 16.648 -10.945 33.528 0.35 46.66  ? 106 MET A SD  1 
ATOM   928  C  CE  A MET A 1 105 ? 16.719 -10.069 34.763 0.65 42.79  ? 106 MET A CE  1 
ATOM   929  C  CE  B MET A 1 105 ? 16.176 -9.394  32.798 0.35 44.25  ? 106 MET A CE  1 
ATOM   930  N  N   . ALA A 1 106 ? 21.877 -10.436 33.817 1.00 32.09  ? 107 ALA A N   1 
ATOM   931  C  CA  . ALA A 1 106 ? 22.615 -9.150  33.827 1.00 31.57  ? 107 ALA A CA  1 
ATOM   932  C  C   . ALA A 1 106 ? 23.779 -9.184  32.831 1.00 31.04  ? 107 ALA A C   1 
ATOM   933  O  O   . ALA A 1 106 ? 23.955 -8.227  32.064 1.00 29.29  ? 107 ALA A O   1 
ATOM   934  C  CB  . ALA A 1 106 ? 23.111 -8.833  35.230 1.00 32.94  ? 107 ALA A CB  1 
ATOM   935  N  N   . THR A 1 107 ? 24.524 -10.303 32.788 1.00 26.98  ? 108 THR A N   1 
ATOM   936  C  CA  . THR A 1 107 ? 25.630 -10.481 31.845 1.00 26.86  ? 108 THR A CA  1 
ATOM   937  C  C   . THR A 1 107 ? 25.104 -10.530 30.396 1.00 29.80  ? 108 THR A C   1 
ATOM   938  O  O   . THR A 1 107 ? 25.696 -9.885  29.521 1.00 27.84  ? 108 THR A O   1 
ATOM   939  C  CB  . THR A 1 107 ? 26.519 -11.689 32.216 1.00 32.38  ? 108 THR A CB  1 
ATOM   940  O  OG1 . THR A 1 107 ? 26.807 -11.664 33.615 1.00 32.49  ? 108 THR A OG1 1 
ATOM   941  C  CG2 . THR A 1 107 ? 27.841 -11.707 31.423 1.00 30.25  ? 108 THR A CG2 1 
ATOM   942  N  N   . ALA A 1 108 ? 23.988 -11.268 30.149 1.00 26.90  ? 109 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 108 ? 23.392 -11.370 28.804 1.00 25.80  ? 109 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 108 ? 22.888 -9.997  28.333 1.00 28.63  ? 109 ALA A C   1 
ATOM   945  O  O   . ALA A 1 108 ? 23.047 -9.661  27.168 1.00 26.38  ? 109 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 108 ? 22.265 -12.404 28.786 1.00 26.32  ? 109 ALA A CB  1 
ATOM   947  N  N   . MET A 1 109 ? 22.334 -9.175  29.247 1.00 27.32  ? 110 MET A N   1 
ATOM   948  C  CA  . MET A 1 109 ? 21.891 -7.826  28.861 1.00 28.08  ? 110 MET A CA  1 
ATOM   949  C  C   . MET A 1 109 ? 23.083 -6.957  28.414 1.00 30.75  ? 110 MET A C   1 
ATOM   950  O  O   . MET A 1 109 ? 23.015 -6.290  27.382 1.00 30.98  ? 110 MET A O   1 
ATOM   951  C  CB  . MET A 1 109 ? 21.137 -7.168  30.019 1.00 31.83  ? 110 MET A CB  1 
ATOM   952  C  CG  . MET A 1 109 ? 19.726 -7.710  30.174 1.00 37.43  ? 110 MET A CG  1 
ATOM   953  S  SD  . MET A 1 109 ? 18.970 -7.133  31.720 1.00 45.30  ? 110 MET A SD  1 
ATOM   954  C  CE  . MET A 1 109 ? 18.688 -5.399  31.315 1.00 43.69  ? 110 MET A CE  1 
ATOM   955  N  N   . TYR A 1 110 ? 24.175 -7.013  29.173 1.00 28.53  ? 111 TYR A N   1 
ATOM   956  C  CA  . TYR A 1 110 ? 25.418 -6.283  28.902 1.00 28.07  ? 111 TYR A CA  1 
ATOM   957  C  C   . TYR A 1 110 ? 26.047 -6.774  27.583 1.00 29.48  ? 111 TYR A C   1 
ATOM   958  O  O   . TYR A 1 110 ? 26.431 -5.957  26.741 1.00 28.13  ? 111 TYR A O   1 
ATOM   959  C  CB  . TYR A 1 110 ? 26.375 -6.507  30.076 1.00 28.72  ? 111 TYR A CB  1 
ATOM   960  C  CG  . TYR A 1 110 ? 27.790 -6.022  29.852 1.00 28.61  ? 111 TYR A CG  1 
ATOM   961  C  CD1 . TYR A 1 110 ? 28.103 -4.667  29.915 1.00 30.68  ? 111 TYR A CD1 1 
ATOM   962  C  CD2 . TYR A 1 110 ? 28.829 -6.923  29.633 1.00 28.64  ? 111 TYR A CD2 1 
ATOM   963  C  CE1 . TYR A 1 110 ? 29.410 -4.219  29.715 1.00 27.86  ? 111 TYR A CE1 1 
ATOM   964  C  CE2 . TYR A 1 110 ? 30.143 -6.492  29.478 1.00 28.64  ? 111 TYR A CE2 1 
ATOM   965  C  CZ  . TYR A 1 110 ? 30.428 -5.138  29.521 1.00 30.32  ? 111 TYR A CZ  1 
ATOM   966  O  OH  . TYR A 1 110 ? 31.726 -4.726  29.406 1.00 29.67  ? 111 TYR A OH  1 
ATOM   967  N  N   . LEU A 1 111 ? 26.093 -8.099  27.376 1.00 25.94  ? 112 LEU A N   1 
ATOM   968  C  CA  . LEU A 1 111 ? 26.676 -8.681  26.166 1.00 24.17  ? 112 LEU A CA  1 
ATOM   969  C  C   . LEU A 1 111 ? 25.759 -8.543  24.949 1.00 27.37  ? 112 LEU A C   1 
ATOM   970  O  O   . LEU A 1 111 ? 26.195 -8.801  23.827 1.00 26.70  ? 112 LEU A O   1 
ATOM   971  C  CB  . LEU A 1 111 ? 27.030 -10.159 26.410 1.00 22.89  ? 112 LEU A CB  1 
ATOM   972  C  CG  . LEU A 1 111 ? 28.171 -10.434 27.429 1.00 26.17  ? 112 LEU A CG  1 
ATOM   973  C  CD1 . LEU A 1 111 ? 28.451 -11.953 27.505 1.00 25.35  ? 112 LEU A CD1 1 
ATOM   974  C  CD2 . LEU A 1 111 ? 29.490 -9.655  27.042 1.00 27.31  ? 112 LEU A CD2 1 
ATOM   975  N  N   . GLN A 1 112 ? 24.484 -8.188  25.175 1.00 26.38  ? 113 GLN A N   1 
ATOM   976  C  CA  . GLN A 1 112 ? 23.465 -8.042  24.122 1.00 27.04  ? 113 GLN A CA  1 
ATOM   977  C  C   . GLN A 1 112 ? 23.243 -9.395  23.424 1.00 29.45  ? 113 GLN A C   1 
ATOM   978  O  O   . GLN A 1 112 ? 23.547 -9.571  22.241 1.00 27.83  ? 113 GLN A O   1 
ATOM   979  C  CB  . GLN A 1 112 ? 23.833 -6.918  23.124 1.00 28.16  ? 113 GLN A CB  1 
ATOM   980  C  CG  . GLN A 1 112 ? 24.023 -5.539  23.776 1.00 33.25  ? 113 GLN A CG  1 
ATOM   981  C  CD  . GLN A 1 112 ? 24.743 -4.601  22.829 1.00 43.49  ? 113 GLN A CD  1 
ATOM   982  O  OE1 . GLN A 1 112 ? 24.607 -4.690  21.615 1.00 35.05  ? 113 GLN A OE1 1 
ATOM   983  N  NE2 . GLN A 1 112 ? 25.540 -3.693  23.359 1.00 39.12  ? 113 GLN A NE2 1 
ATOM   984  N  N   . MET A 1 113 ? 22.747 -10.360 24.205 1.00 26.81  ? 114 MET A N   1 
ATOM   985  C  CA  . MET A 1 113 ? 22.430 -11.734 23.776 1.00 26.51  ? 114 MET A CA  1 
ATOM   986  C  C   . MET A 1 113 ? 20.930 -11.885 24.045 1.00 32.86  ? 114 MET A C   1 
ATOM   987  O  O   . MET A 1 113 ? 20.518 -12.361 25.110 1.00 31.55  ? 114 MET A O   1 
ATOM   988  C  CB  . MET A 1 113 ? 23.284 -12.714 24.587 1.00 27.02  ? 114 MET A CB  1 
ATOM   989  C  CG  . MET A 1 113 ? 24.785 -12.573 24.284 1.00 28.27  ? 114 MET A CG  1 
ATOM   990  S  SD  . MET A 1 113 ? 25.794 -13.618 25.341 1.00 30.59  ? 114 MET A SD  1 
ATOM   991  C  CE  . MET A 1 113 ? 25.443 -15.294 24.579 1.00 26.95  ? 114 MET A CE  1 
ATOM   992  N  N   . GLU A 1 114 ? 20.118 -11.327 23.125 1.00 32.42  ? 115 GLU A N   1 
ATOM   993  C  CA  . GLU A 1 114 ? 18.659 -11.194 23.265 1.00 34.67  ? 115 GLU A CA  1 
ATOM   994  C  C   . GLU A 1 114 ? 17.897 -12.485 23.571 1.00 35.89  ? 115 GLU A C   1 
ATOM   995  O  O   . GLU A 1 114 ? 16.974 -12.437 24.378 1.00 35.94  ? 115 GLU A O   1 
ATOM   996  C  CB  . GLU A 1 114 ? 18.036 -10.505 22.042 1.00 37.94  ? 115 GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 114 ? 18.585 -9.108  21.798 1.00 51.81  ? 115 GLU A CG  1 
ATOM   998  N  N   . HIS A 1 115 ? 18.254 -13.621 22.953 1.00 31.35  ? 116 HIS A N   1 
ATOM   999  C  CA  . HIS A 1 115 ? 17.528 -14.863 23.238 1.00 33.11  ? 116 HIS A CA  1 
ATOM   1000 C  C   . HIS A 1 115 ? 17.758 -15.344 24.671 1.00 35.01  ? 116 HIS A C   1 
ATOM   1001 O  O   . HIS A 1 115 ? 16.808 -15.795 25.311 1.00 35.96  ? 116 HIS A O   1 
ATOM   1002 C  CB  . HIS A 1 115 ? 17.841 -15.947 22.208 1.00 34.60  ? 116 HIS A CB  1 
ATOM   1003 C  CG  . HIS A 1 115 ? 17.367 -15.613 20.831 1.00 39.41  ? 116 HIS A CG  1 
ATOM   1004 N  ND1 . HIS A 1 115 ? 16.023 -15.441 20.555 1.00 43.18  ? 116 HIS A ND1 1 
ATOM   1005 C  CD2 . HIS A 1 115 ? 18.069 -15.495 19.680 1.00 40.94  ? 116 HIS A CD2 1 
ATOM   1006 C  CE1 . HIS A 1 115 ? 15.953 -15.178 19.260 1.00 42.91  ? 116 HIS A CE1 1 
ATOM   1007 N  NE2 . HIS A 1 115 ? 17.157 -15.208 18.692 1.00 42.09  ? 116 HIS A NE2 1 
ATOM   1008 N  N   . VAL A 1 116 ? 18.991 -15.173 25.200 1.00 28.64  ? 117 VAL A N   1 
ATOM   1009 C  CA  . VAL A 1 116 ? 19.295 -15.520 26.594 1.00 28.30  ? 117 VAL A CA  1 
ATOM   1010 C  C   . VAL A 1 116 ? 18.510 -14.612 27.540 1.00 33.32  ? 117 VAL A C   1 
ATOM   1011 O  O   . VAL A 1 116 ? 17.902 -15.099 28.502 1.00 31.63  ? 117 VAL A O   1 
ATOM   1012 C  CB  . VAL A 1 116 ? 20.805 -15.530 26.916 1.00 30.20  ? 117 VAL A CB  1 
ATOM   1013 C  CG1 . VAL A 1 116 ? 21.033 -15.810 28.403 1.00 30.13  ? 117 VAL A CG1 1 
ATOM   1014 C  CG2 . VAL A 1 116 ? 21.533 -16.568 26.058 1.00 28.78  ? 117 VAL A CG2 1 
ATOM   1015 N  N   . VAL A 1 117 ? 18.512 -13.292 27.262 1.00 30.61  ? 118 VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 117 ? 17.757 -12.313 28.069 1.00 30.97  ? 118 VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 117 ? 16.270 -12.717 28.140 1.00 37.68  ? 118 VAL A C   1 
ATOM   1018 O  O   . VAL A 1 117 ? 15.704 -12.738 29.235 1.00 37.43  ? 118 VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 117 ? 17.930 -10.849 27.568 1.00 33.66  ? 118 VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 117 ? 17.079 -9.868  28.401 1.00 34.33  ? 118 VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 117 ? 19.396 -10.427 27.593 1.00 32.67  ? 118 VAL A CG2 1 
ATOM   1022 N  N   A ASP A 1 118 ? 15.628 -12.945 26.973 0.41 36.13  ? 119 ASP A N   1 
ATOM   1023 N  N   B ASP A 1 118 ? 15.694 -13.130 26.994 0.59 35.25  ? 119 ASP A N   1 
ATOM   1024 C  CA  A ASP A 1 118 ? 14.203 -13.290 26.859 0.41 37.91  ? 119 ASP A CA  1 
ATOM   1025 C  CA  B ASP A 1 118 ? 14.307 -13.587 26.868 0.59 36.46  ? 119 ASP A CA  1 
ATOM   1026 C  C   A ASP A 1 118 ? 13.774 -14.489 27.708 0.41 42.35  ? 119 ASP A C   1 
ATOM   1027 C  C   B ASP A 1 118 ? 13.993 -14.800 27.761 0.59 38.82  ? 119 ASP A C   1 
ATOM   1028 O  O   A ASP A 1 118 ? 12.700 -14.456 28.303 0.41 43.64  ? 119 ASP A O   1 
ATOM   1029 O  O   B ASP A 1 118 ? 13.028 -14.736 28.521 0.59 38.81  ? 119 ASP A O   1 
ATOM   1030 C  CB  A ASP A 1 118 ? 13.805 -13.501 25.387 0.41 40.12  ? 119 ASP A CB  1 
ATOM   1031 C  CB  B ASP A 1 118 ? 13.975 -13.888 25.395 0.59 38.64  ? 119 ASP A CB  1 
ATOM   1032 C  CG  A ASP A 1 118 ? 13.623 -12.228 24.579 0.41 52.82  ? 119 ASP A CG  1 
ATOM   1033 C  CG  B ASP A 1 118 ? 12.523 -14.246 25.134 0.59 52.88  ? 119 ASP A CG  1 
ATOM   1034 O  OD1 A ASP A 1 118 ? 13.105 -11.236 25.136 0.41 56.46  ? 119 ASP A OD1 1 
ATOM   1035 O  OD1 B ASP A 1 118 ? 11.636 -13.439 25.495 0.59 56.37  ? 119 ASP A OD1 1 
ATOM   1036 O  OD2 A ASP A 1 118 ? 13.983 -12.227 23.383 0.41 58.07  ? 119 ASP A OD2 1 
ATOM   1037 O  OD2 B ASP A 1 118 ? 12.275 -15.324 24.555 0.59 57.18  ? 119 ASP A OD2 1 
ATOM   1038 N  N   A THR A 1 119 ? 14.617 -15.531 27.773 0.41 37.73  ? 120 THR A N   1 
ATOM   1039 N  N   B THR A 1 119 ? 14.805 -15.888 27.700 0.59 33.78  ? 120 THR A N   1 
ATOM   1040 C  CA  A THR A 1 119 ? 14.357 -16.757 28.533 0.41 37.95  ? 120 THR A CA  1 
ATOM   1041 C  CA  B THR A 1 119 ? 14.535 -17.071 28.534 0.59 34.28  ? 120 THR A CA  1 
ATOM   1042 C  C   A THR A 1 119 ? 14.531 -16.536 30.009 0.41 40.92  ? 120 THR A C   1 
ATOM   1043 C  C   B THR A 1 119 ? 14.719 -16.787 30.035 0.59 39.03  ? 120 THR A C   1 
ATOM   1044 O  O   A THR A 1 119 ? 13.691 -17.000 30.783 0.41 41.50  ? 120 THR A O   1 
ATOM   1045 O  O   B THR A 1 119 ? 14.038 -17.421 30.840 0.59 39.06  ? 120 THR A O   1 
ATOM   1046 C  CB  A THR A 1 119 ? 15.223 -17.871 28.003 0.41 45.51  ? 120 THR A CB  1 
ATOM   1047 C  CB  B THR A 1 119 ? 15.307 -18.326 28.075 0.59 35.16  ? 120 THR A CB  1 
ATOM   1048 O  OG1 A THR A 1 119 ? 15.025 -17.849 26.609 0.41 45.05  ? 120 THR A OG1 1 
ATOM   1049 O  OG1 B THR A 1 119 ? 14.658 -19.461 28.648 0.59 37.14  ? 120 THR A OG1 1 
ATOM   1050 C  CG2 A THR A 1 119 ? 14.837 -19.230 28.556 0.41 45.30  ? 120 THR A CG2 1 
ATOM   1051 C  CG2 B THR A 1 119 ? 16.777 -18.325 28.500 0.59 28.24  ? 120 THR A CG2 1 
ATOM   1052 N  N   . CYS A 1 120 ? 15.625 -15.846 30.406 1.00 35.83  ? 121 CYS A N   1 
ATOM   1053 C  CA  . CYS A 1 120 ? 15.879 -15.486 31.815 1.00 36.51  ? 121 CYS A CA  1 
ATOM   1054 C  C   . CYS A 1 120 ? 14.661 -14.762 32.352 1.00 42.68  ? 121 CYS A C   1 
ATOM   1055 O  O   . CYS A 1 120 ? 14.148 -15.148 33.411 1.00 43.61  ? 121 CYS A O   1 
ATOM   1056 C  CB  . CYS A 1 120 ? 17.134 -14.628 31.934 1.00 35.50  ? 121 CYS A CB  1 
ATOM   1057 S  SG  . CYS A 1 120 ? 18.674 -15.549 31.718 1.00 37.66  ? 121 CYS A SG  1 
ATOM   1058 N  N   . ARG A 1 121 ? 14.145 -13.774 31.570 1.00 40.06  ? 122 ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 121 ? 12.931 -13.016 31.897 1.00 42.63  ? 122 ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 121 ? 11.744 -13.969 32.153 1.00 48.11  ? 122 ARG A C   1 
ATOM   1061 O  O   . ARG A 1 121 ? 11.027 -13.807 33.143 1.00 48.64  ? 122 ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 121 ? 12.575 -12.049 30.755 1.00 44.91  ? 122 ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 121 ? 13.432 -10.798 30.721 1.00 59.49  ? 122 ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 121 ? 12.612 -9.569  30.381 1.00 74.87  ? 122 ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 121 ? 13.020 -8.975  29.105 1.00 82.98  ? 122 ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 121 ? 13.945 -8.027  28.973 1.00 91.81  ? 122 ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 121 ? 14.580 -7.554  30.040 1.00 70.14  ? 122 ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 121 ? 14.245 -7.548  27.773 1.00 80.53  ? 122 ARG A NH2 1 
ATOM   1069 N  N   . LYS A 1 122 ? 11.560 -14.969 31.266 1.00 44.85  ? 123 LYS A N   1 
ATOM   1070 C  CA  . LYS A 1 122 ? 10.472 -15.951 31.365 1.00 45.96  ? 123 LYS A CA  1 
ATOM   1071 C  C   . LYS A 1 122 ? 10.617 -16.860 32.584 1.00 48.97  ? 123 LYS A C   1 
ATOM   1072 O  O   . LYS A 1 122 ? 9.625  -17.107 33.261 1.00 48.53  ? 123 LYS A O   1 
ATOM   1073 C  CB  . LYS A 1 122 ? 10.364 -16.789 30.075 1.00 47.91  ? 123 LYS A CB  1 
ATOM   1074 C  CG  . LYS A 1 122 ? 9.817  -16.007 28.887 1.00 66.90  ? 123 LYS A CG  1 
ATOM   1075 C  CD  . LYS A 1 122 ? 9.546  -16.907 27.681 1.00 77.80  ? 123 LYS A CD  1 
ATOM   1076 C  CE  . LYS A 1 122 ? 9.602  -16.171 26.358 1.00 86.63  ? 123 LYS A CE  1 
ATOM   1077 N  NZ  . LYS A 1 122 ? 8.522  -15.159 26.209 1.00 94.95  ? 123 LYS A NZ  1 
ATOM   1078 N  N   . PHE A 1 123 ? 11.845 -17.365 32.857 1.00 44.73  ? 124 PHE A N   1 
ATOM   1079 C  CA  . PHE A 1 123 ? 12.126 -18.234 34.008 1.00 45.25  ? 124 PHE A CA  1 
ATOM   1080 C  C   . PHE A 1 123 ? 11.926 -17.481 35.326 1.00 50.12  ? 124 PHE A C   1 
ATOM   1081 O  O   . PHE A 1 123 ? 11.400 -18.064 36.281 1.00 50.19  ? 124 PHE A O   1 
ATOM   1082 C  CB  . PHE A 1 123 ? 13.532 -18.839 33.910 1.00 45.65  ? 124 PHE A CB  1 
ATOM   1083 C  CG  . PHE A 1 123 ? 13.655 -20.141 33.136 1.00 47.44  ? 124 PHE A CG  1 
ATOM   1084 C  CD1 . PHE A 1 123 ? 13.130 -20.265 31.850 1.00 50.53  ? 124 PHE A CD1 1 
ATOM   1085 C  CD2 . PHE A 1 123 ? 14.359 -21.219 33.663 1.00 49.77  ? 124 PHE A CD2 1 
ATOM   1086 C  CE1 . PHE A 1 123 ? 13.254 -21.464 31.133 1.00 50.38  ? 124 PHE A CE1 1 
ATOM   1087 C  CE2 . PHE A 1 123 ? 14.497 -22.412 32.937 1.00 51.25  ? 124 PHE A CE2 1 
ATOM   1088 C  CZ  . PHE A 1 123 ? 13.937 -22.527 31.683 1.00 48.47  ? 124 PHE A CZ  1 
ATOM   1089 N  N   . ILE A 1 124 ? 12.295 -16.181 35.365 1.00 45.71  ? 125 ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 124 ? 12.097 -15.324 36.547 1.00 47.56  ? 125 ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 124 ? 10.600 -15.075 36.790 1.00 54.76  ? 125 ILE A C   1 
ATOM   1092 O  O   . ILE A 1 124 ? 10.144 -15.164 37.935 1.00 55.68  ? 125 ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 124 ? 12.935 -14.017 36.456 1.00 49.53  ? 125 ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 124 ? 14.423 -14.338 36.660 1.00 48.15  ? 125 ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 124 ? 12.475 -12.943 37.486 1.00 52.56  ? 125 ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 124 ? 15.372 -13.321 36.064 1.00 52.72  ? 125 ILE A CD1 1 
ATOM   1097 N  N   . LYS A 1 125 ? 9.839  -14.794 35.705 1.00 53.59  ? 126 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 125 ? 8.391  -14.536 35.754 1.00 56.60  ? 126 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 125 ? 7.610  -15.767 36.258 1.00 62.39  ? 126 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 125 ? 6.616  -15.609 36.960 1.00 63.63  ? 126 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 125 ? 7.879  -14.085 34.376 1.00 59.92  ? 126 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 125 ? 6.527  -13.380 34.417 1.00 78.85  ? 126 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 125 ? 5.897  -13.308 33.033 1.00 91.47  ? 126 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 125 ? 4.469  -12.820 33.086 1.00 106.48 ? 126 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 125 ? 3.799  -12.939 31.764 1.00 116.74 ? 126 LYS A NZ  1 
ATOM   1106 N  N   . ALA A 1 126 ? 8.080  -16.984 35.928 1.00 58.16  ? 127 ALA A N   1 
ATOM   1107 C  CA  . ALA A 1 126 ? 7.454  -18.234 36.371 1.00 59.53  ? 127 ALA A CA  1 
ATOM   1108 C  C   . ALA A 1 126 ? 7.608  -18.458 37.888 1.00 65.82  ? 127 ALA A C   1 
ATOM   1109 O  O   . ALA A 1 126 ? 6.748  -19.090 38.494 1.00 66.83  ? 127 ALA A O   1 
ATOM   1110 C  CB  . ALA A 1 126 ? 8.045  -19.411 35.604 1.00 58.40  ? 127 ALA A CB  1 
ATOM   1111 N  N   . SER A 1 127 ? 8.699  -17.949 38.490 1.00 64.17  ? 128 SER A N   1 
ATOM   1112 C  CA  . SER A 1 127 ? 8.997  -18.093 39.921 1.00 66.91  ? 128 SER A CA  1 
ATOM   1113 C  C   . SER A 1 127 ? 8.306  -17.058 40.834 1.00 74.96  ? 128 SER A C   1 
ATOM   1114 O  O   . SER A 1 127 ? 8.231  -17.288 42.045 1.00 77.09  ? 128 SER A O   1 
ATOM   1115 C  CB  . SER A 1 127 ? 10.506 -18.088 40.158 1.00 70.42  ? 128 SER A CB  1 
ATOM   1116 O  OG  . SER A 1 127 ? 11.051 -19.390 40.014 1.00 81.49  ? 128 SER A OG  1 
ATOM   1117 N  N   . GLU A 1 128 ? 7.796  -15.938 40.270 1.00 71.72  ? 129 GLU A N   1 
ATOM   1118 C  CA  . GLU A 1 128 ? 7.122  -14.893 41.050 1.00 97.56  ? 129 GLU A CA  1 
ATOM   1119 C  C   . GLU A 1 128 ? 5.674  -15.261 41.402 1.00 139.89 ? 129 GLU A C   1 
ATOM   1120 O  O   . GLU A 1 128 ? 5.427  -16.281 42.043 1.00 107.29 ? 129 GLU A O   1 
ATOM   1121 C  CB  . GLU A 1 128 ? 7.214  -13.516 40.360 1.00 98.14  ? 129 GLU A CB  1 
ATOM   1122 C  CG  . GLU A 1 128 ? 6.273  -13.314 39.179 1.00 108.51 ? 129 GLU A CG  1 
ATOM   1123 C  CD  . GLU A 1 128 ? 6.442  -12.048 38.356 1.00 129.42 ? 129 GLU A CD  1 
ATOM   1124 O  OE1 . GLU A 1 128 ? 7.522  -11.417 38.425 1.00 123.35 ? 129 GLU A OE1 1 
ATOM   1125 O  OE2 . GLU A 1 128 ? 5.488  -11.697 37.625 1.00 123.23 ? 129 GLU A OE2 1 
HETATM 1126 C  C   . ACE B 2 1   ? 21.259 -35.102 5.867  1.00 30.32  ? 0   ACE D C   1 
HETATM 1127 O  O   . ACE B 2 1   ? 21.326 -33.950 6.319  1.00 31.59  ? 0   ACE D O   1 
HETATM 1128 C  CH3 . ACE B 2 1   ? 21.448 -36.298 6.778  1.00 29.36  ? 0   ACE D CH3 1 
ATOM   1129 N  N   A TRP B 2 2   ? 20.986 -35.367 4.593  0.78 29.26  ? 1   TRP D N   1 
ATOM   1130 N  N   B TRP B 2 2   ? 21.019 -35.384 4.584  0.22 29.70  ? 1   TRP D N   1 
ATOM   1131 C  CA  A TRP B 2 2   ? 20.788 -34.317 3.600  0.78 28.78  ? 1   TRP D CA  1 
ATOM   1132 C  CA  B TRP B 2 2   ? 20.770 -34.350 3.577  0.22 29.36  ? 1   TRP D CA  1 
ATOM   1133 C  C   A TRP B 2 2   ? 19.291 -34.169 3.303  0.78 33.18  ? 1   TRP D C   1 
ATOM   1134 C  C   B TRP B 2 2   ? 19.268 -34.164 3.387  0.22 32.68  ? 1   TRP D C   1 
ATOM   1135 O  O   A TRP B 2 2   ? 18.556 -35.165 3.294  0.78 33.28  ? 1   TRP D O   1 
ATOM   1136 O  O   B TRP B 2 2   ? 18.513 -35.137 3.479  0.22 32.23  ? 1   TRP D O   1 
ATOM   1137 C  CB  A TRP B 2 2   ? 21.588 -34.636 2.315  0.78 27.92  ? 1   TRP D CB  1 
ATOM   1138 C  CB  B TRP B 2 2   ? 21.465 -34.659 2.225  0.22 28.31  ? 1   TRP D CB  1 
ATOM   1139 C  CG  A TRP B 2 2   ? 23.082 -34.608 2.522  0.78 28.44  ? 1   TRP D CG  1 
ATOM   1140 C  CG  B TRP B 2 2   ? 20.796 -35.709 1.382  0.22 29.34  ? 1   TRP D CG  1 
ATOM   1141 C  CD1 A TRP B 2 2   ? 23.865 -35.622 2.993  0.78 31.12  ? 1   TRP D CD1 1 
ATOM   1142 C  CD1 B TRP B 2 2   ? 21.096 -37.037 1.343  0.22 32.40  ? 1   TRP D CD1 1 
ATOM   1143 C  CD2 A TRP B 2 2   ? 23.965 -33.504 2.267  0.78 28.05  ? 1   TRP D CD2 1 
ATOM   1144 C  CD2 B TRP B 2 2   ? 19.740 -35.508 0.428  0.22 29.19  ? 1   TRP D CD2 1 
ATOM   1145 N  NE1 A TRP B 2 2   ? 25.177 -35.200 3.095  0.78 30.09  ? 1   TRP D NE1 1 
ATOM   1146 N  NE1 B TRP B 2 2   ? 20.260 -37.688 0.467  0.22 31.94  ? 1   TRP D NE1 1 
ATOM   1147 C  CE2 A TRP B 2 2   ? 25.276 -33.928 2.594  0.78 31.41  ? 1   TRP D CE2 1 
ATOM   1148 C  CE2 B TRP B 2 2   ? 19.424 -36.772 -0.118 0.22 33.27  ? 1   TRP D CE2 1 
ATOM   1149 C  CE3 A TRP B 2 2   ? 23.776 -32.185 1.818  0.78 28.48  ? 1   TRP D CE3 1 
ATOM   1150 C  CE3 B TRP B 2 2   ? 19.003 -34.387 0.007  0.22 30.30  ? 1   TRP D CE3 1 
ATOM   1151 C  CZ2 A TRP B 2 2   ? 26.392 -33.092 2.456  0.78 29.98  ? 1   TRP D CZ2 1 
ATOM   1152 C  CZ2 B TRP B 2 2   ? 18.415 -36.945 -1.074 0.22 32.43  ? 1   TRP D CZ2 1 
ATOM   1153 C  CZ3 A TRP B 2 2   ? 24.886 -31.375 1.640  0.78 29.27  ? 1   TRP D CZ3 1 
ATOM   1154 C  CZ3 B TRP B 2 2   ? 17.998 -34.561 -0.932 0.22 32.00  ? 1   TRP D CZ3 1 
ATOM   1155 C  CH2 A TRP B 2 2   ? 26.172 -31.824 1.974  0.78 30.11  ? 1   TRP D CH2 1 
ATOM   1156 C  CH2 B TRP B 2 2   ? 17.720 -35.825 -1.470 0.22 32.54  ? 1   TRP D CH2 1 
ATOM   1157 N  N   . VAL B 2 3   ? 18.837 -32.926 3.103  1.00 28.52  ? 2   VAL D N   1 
ATOM   1158 C  CA  . VAL B 2 3   ? 17.428 -32.589 2.868  1.00 27.87  ? 2   VAL D CA  1 
ATOM   1159 C  C   . VAL B 2 3   ? 17.283 -31.538 1.770  1.00 29.95  ? 2   VAL D C   1 
ATOM   1160 O  O   . VAL B 2 3   ? 18.245 -30.837 1.427  1.00 28.10  ? 2   VAL D O   1 
ATOM   1161 C  CB  . VAL B 2 3   ? 16.700 -32.084 4.171  1.00 30.89  ? 2   VAL D CB  1 
ATOM   1162 C  CG1 . VAL B 2 3   ? 16.717 -33.128 5.293  1.00 31.31  ? 2   VAL D CG1 1 
ATOM   1163 C  CG2 . VAL B 2 3   ? 17.253 -30.727 4.664  1.00 30.16  ? 2   VAL D CG2 1 
ATOM   1164 N  N   . ILE B 2 4   ? 16.048 -31.368 1.298  1.00 27.60  ? 3   ILE D N   1 
ATOM   1165 C  CA  . ILE B 2 4   ? 15.685 -30.274 0.413  1.00 28.01  ? 3   ILE D CA  1 
ATOM   1166 C  C   . ILE B 2 4   ? 15.308 -29.137 1.389  1.00 30.92  ? 3   ILE D C   1 
ATOM   1167 O  O   . ILE B 2 4   ? 14.316 -29.278 2.120  1.00 29.71  ? 3   ILE D O   1 
ATOM   1168 C  CB  . ILE B 2 4   ? 14.478 -30.632 -0.490 1.00 30.00  ? 3   ILE D CB  1 
ATOM   1169 C  CG1 . ILE B 2 4   ? 14.744 -31.914 -1.347 1.00 29.00  ? 3   ILE D CG1 1 
ATOM   1170 C  CG2 . ILE B 2 4   ? 14.078 -29.404 -1.352 1.00 30.95  ? 3   ILE D CG2 1 
ATOM   1171 C  CD1 . ILE B 2 4   ? 16.022 -31.845 -2.330 1.00 32.12  ? 3   ILE D CD1 1 
ATOM   1172 N  N   . PRO B 2 5   ? 16.096 -28.045 1.468  1.00 30.55  ? 4   PRO D N   1 
ATOM   1173 C  CA  . PRO B 2 5   ? 15.769 -26.977 2.433  1.00 31.23  ? 4   PRO D CA  1 
ATOM   1174 C  C   . PRO B 2 5   ? 14.500 -26.202 2.076  1.00 36.46  ? 4   PRO D C   1 
ATOM   1175 O  O   . PRO B 2 5   ? 14.227 -26.002 0.891  1.00 35.71  ? 4   PRO D O   1 
ATOM   1176 C  CB  . PRO B 2 5   ? 17.012 -26.079 2.406  1.00 33.00  ? 4   PRO D CB  1 
ATOM   1177 C  CG  . PRO B 2 5   ? 17.583 -26.275 1.014  1.00 36.23  ? 4   PRO D CG  1 
ATOM   1178 C  CD  . PRO B 2 5   ? 17.306 -27.719 0.676  1.00 31.84  ? 4   PRO D CD  1 
ATOM   1179 N  N   . ALA B 2 6   ? 13.883 -25.559 3.089  1.00 34.34  ? 5   ALA D N   1 
HETATM 1180 C  C4  . 7ZO C 3 .   ? 27.315 -10.308 11.811 1.00 30.97  ? 201 7ZO A C4  1 
HETATM 1181 C  C5  . 7ZO C 3 .   ? 25.318 -9.332  12.179 1.00 33.03  ? 201 7ZO A C5  1 
HETATM 1182 C  C6  . 7ZO C 3 .   ? 23.965 -10.732 18.048 1.00 30.45  ? 201 7ZO A C6  1 
HETATM 1183 C  C7  . 7ZO C 3 .   ? 23.477 -9.431  18.109 1.00 31.15  ? 201 7ZO A C7  1 
HETATM 1184 C  C8  . 7ZO C 3 .   ? 25.532 -10.045 16.350 1.00 28.04  ? 201 7ZO A C8  1 
HETATM 1185 C  C10 . 7ZO C 3 .   ? 26.385 -10.202 13.996 1.00 28.82  ? 201 7ZO A C10 1 
HETATM 1186 C  C1  . 7ZO C 3 .   ? 23.957 -8.437  17.259 1.00 29.42  ? 201 7ZO A C1  1 
HETATM 1187 C  C2  . 7ZO C 3 .   ? 24.977 -8.760  16.370 1.00 27.84  ? 201 7ZO A C2  1 
HETATM 1188 C  C3  . 7ZO C 3 .   ? 24.988 -11.046 17.160 1.00 28.33  ? 201 7ZO A C3  1 
HETATM 1189 C  C9  . 7ZO C 3 .   ? 27.419 -10.622 13.155 1.00 28.50  ? 201 7ZO A C9  1 
HETATM 1190 C  C11 . 7ZO C 3 .   ? 22.251 -10.567 19.667 1.00 36.28  ? 201 7ZO A C11 1 
HETATM 1191 C  C12 . 7ZO C 3 .   ? 23.215 -11.558 19.050 1.00 33.41  ? 201 7ZO A C12 1 
HETATM 1192 N  N13 . 7ZO C 3 .   ? 26.269 -9.652  11.303 1.00 32.94  ? 201 7ZO A N13 1 
HETATM 1193 N  N14 . 7ZO C 3 .   ? 25.307 -9.559  13.497 1.00 32.13  ? 201 7ZO A N14 1 
HETATM 1194 N  N15 . 7ZO C 3 .   ? 22.471 -9.359  19.081 1.00 32.25  ? 201 7ZO A N15 1 
HETATM 1195 N  N16 . 7ZO C 3 .   ? 26.383 -10.511 15.322 1.00 26.43  ? 201 7ZO A N16 1 
HETATM 1196 O  O17 . 7ZO C 3 .   ? 21.398 -10.800 20.521 1.00 36.57  ? 201 7ZO A O17 1 
HETATM 1197 CL CL1 . 7ZO C 3 .   ? 28.846 -11.386 13.749 0.99 29.24  ? 201 7ZO A CL1 1 
HETATM 1198 CL CL  . CL  D 4 .   ? 21.336 -15.196 22.529 1.00 37.70  ? 202 CL  A CL  1 
HETATM 1199 S  S   A DMS E 5 .   ? 17.597 -35.395 -1.250 0.78 49.86  ? 101 DMS D S   1 
HETATM 1200 O  O   A DMS E 5 .   ? 16.322 -35.174 -0.588 0.78 50.70  ? 101 DMS D O   1 
HETATM 1201 C  C1  A DMS E 5 .   ? 18.746 -34.508 -0.228 0.78 48.71  ? 101 DMS D C1  1 
HETATM 1202 C  C2  A DMS E 5 .   ? 18.040 -37.033 -0.784 0.78 48.60  ? 101 DMS D C2  1 
HETATM 1203 O  O   . HOH F 6 .   ? 35.713 -25.630 25.575 1.00 44.88  ? 301 HOH A O   1 
HETATM 1204 O  O   . HOH F 6 .   ? 25.914 -3.410  26.352 1.00 37.60  ? 302 HOH A O   1 
HETATM 1205 O  O   . HOH F 6 .   ? 41.262 -21.636 25.183 1.00 45.52  ? 303 HOH A O   1 
HETATM 1206 O  O   . HOH F 6 .   ? 37.930 2.468   19.606 1.00 42.80  ? 304 HOH A O   1 
HETATM 1207 O  O   . HOH F 6 .   ? 33.329 -20.832 29.593 1.00 53.82  ? 305 HOH A O   1 
HETATM 1208 O  O   . HOH F 6 .   ? 19.853 -9.502  36.968 1.00 44.90  ? 306 HOH A O   1 
HETATM 1209 O  O   . HOH F 6 .   ? 38.404 -14.914 15.419 1.00 37.76  ? 307 HOH A O   1 
HETATM 1210 O  O   . HOH F 6 .   ? 37.576 -20.357 26.946 1.00 37.56  ? 308 HOH A O   1 
HETATM 1211 O  O   . HOH F 6 .   ? 29.923 -32.071 9.540  1.00 47.99  ? 309 HOH A O   1 
HETATM 1212 O  O   . HOH F 6 .   ? 44.562 -0.906  17.822 1.00 58.37  ? 310 HOH A O   1 
HETATM 1213 O  O   . HOH F 6 .   ? 27.337 -35.331 11.833 1.00 64.69  ? 311 HOH A O   1 
HETATM 1214 O  O   . HOH F 6 .   ? 31.790 -0.799  15.853 1.00 42.97  ? 312 HOH A O   1 
HETATM 1215 O  O   . HOH F 6 .   ? 43.682 -6.578  31.895 1.00 51.22  ? 313 HOH A O   1 
HETATM 1216 O  O   . HOH F 6 .   ? 20.784 -5.875  25.941 1.00 45.72  ? 314 HOH A O   1 
HETATM 1217 O  O   . HOH F 6 .   ? 16.562 -27.505 -3.280 1.00 58.48  ? 315 HOH A O   1 
HETATM 1218 O  O   . HOH F 6 .   ? 44.960 -11.132 18.697 1.00 59.27  ? 316 HOH A O   1 
HETATM 1219 O  O   . HOH F 6 .   ? 32.471 -24.665 32.178 1.00 64.96  ? 317 HOH A O   1 
HETATM 1220 O  O   . HOH F 6 .   ? 30.409 1.523   33.991 1.00 63.73  ? 318 HOH A O   1 
HETATM 1221 O  O   . HOH F 6 .   ? 22.699 -5.310  19.811 1.00 63.84  ? 319 HOH A O   1 
HETATM 1222 O  O   . HOH F 6 .   ? 41.312 -16.925 15.187 1.00 39.45  ? 320 HOH A O   1 
HETATM 1223 O  O   . HOH F 6 .   ? 22.946 -28.208 12.611 1.00 28.02  ? 321 HOH A O   1 
HETATM 1224 O  O   . HOH F 6 .   ? 26.819 -32.004 16.142 1.00 52.73  ? 322 HOH A O   1 
HETATM 1225 O  O   . HOH F 6 .   ? 23.471 -5.694  32.879 1.00 43.14  ? 323 HOH A O   1 
HETATM 1226 O  O   . HOH F 6 .   ? 27.275 -10.183 35.843 1.00 43.68  ? 324 HOH A O   1 
HETATM 1227 O  O   . HOH F 6 .   ? 13.477 -14.375 21.795 1.00 72.20  ? 325 HOH A O   1 
HETATM 1228 O  O   . HOH F 6 .   ? 20.520 -13.369 20.370 1.00 52.58  ? 326 HOH A O   1 
HETATM 1229 O  O   . HOH F 6 .   ? 26.046 -21.804 38.606 1.00 41.25  ? 327 HOH A O   1 
HETATM 1230 O  O   . HOH F 6 .   ? 17.976 -29.351 7.653  1.00 38.83  ? 328 HOH A O   1 
HETATM 1231 O  O   . HOH F 6 .   ? 21.791 -29.620 -5.264 1.00 41.05  ? 329 HOH A O   1 
HETATM 1232 O  O   . HOH F 6 .   ? 32.333 -8.902  39.608 1.00 57.16  ? 330 HOH A O   1 
HETATM 1233 O  O   . HOH F 6 .   ? 22.603 -27.544 17.658 1.00 55.15  ? 331 HOH A O   1 
HETATM 1234 O  O   . HOH F 6 .   ? 28.213 -23.713 31.593 1.00 44.47  ? 332 HOH A O   1 
HETATM 1235 O  O   . HOH F 6 .   ? 41.692 -12.797 14.224 1.00 93.02  ? 333 HOH A O   1 
HETATM 1236 O  O   . HOH F 6 .   ? 4.315  -20.116 37.804 1.00 66.30  ? 334 HOH A O   1 
HETATM 1237 O  O   . HOH F 6 .   ? 21.936 -24.966 18.297 1.00 26.40  ? 335 HOH A O   1 
HETATM 1238 O  O   . HOH F 6 .   ? 15.433 -9.832  24.857 1.00 58.45  ? 336 HOH A O   1 
HETATM 1239 O  O   . HOH F 6 .   ? 26.829 -16.490 38.642 1.00 50.74  ? 337 HOH A O   1 
HETATM 1240 O  O   . HOH F 6 .   ? 29.622 -2.057  13.774 1.00 68.53  ? 338 HOH A O   1 
HETATM 1241 O  O   . HOH F 6 .   ? 14.249 -16.780 23.343 1.00 48.71  ? 339 HOH A O   1 
HETATM 1242 O  O   . HOH F 6 .   ? 12.551 -20.462 42.544 1.00 67.08  ? 340 HOH A O   1 
HETATM 1243 O  O   . HOH F 6 .   ? 30.347 -0.473  36.799 1.00 55.81  ? 341 HOH A O   1 
HETATM 1244 O  O   . HOH F 6 .   ? 34.911 -18.856 13.839 0.50 31.02  ? 342 HOH A O   1 
HETATM 1245 O  O   . HOH F 6 .   ? 28.233 -8.795  39.874 1.00 53.50  ? 343 HOH A O   1 
HETATM 1246 O  O   . HOH F 6 .   ? 26.407 -7.760  36.774 1.00 57.92  ? 344 HOH A O   1 
HETATM 1247 O  O   . HOH F 6 .   ? 39.101 -18.930 33.227 1.00 53.02  ? 345 HOH A O   1 
HETATM 1248 O  O   . HOH F 6 .   ? 29.049 -31.156 7.245  1.00 34.03  ? 346 HOH A O   1 
HETATM 1249 O  O   . HOH F 6 .   ? 7.061  -16.827 32.280 1.00 62.22  ? 347 HOH A O   1 
HETATM 1250 O  O   . HOH F 6 .   ? 24.886 -26.751 18.972 1.00 37.53  ? 348 HOH A O   1 
HETATM 1251 O  O   . HOH F 6 .   ? 25.943 -4.436  17.872 1.00 52.68  ? 349 HOH A O   1 
HETATM 1252 O  O   . HOH F 6 .   ? 23.259 -17.146 44.245 1.00 70.46  ? 350 HOH A O   1 
HETATM 1253 O  O   . HOH F 6 .   ? 26.107 -22.538 29.905 1.00 30.76  ? 351 HOH A O   1 
HETATM 1254 O  O   . HOH F 6 .   ? 27.296 -28.093 18.659 1.00 34.93  ? 352 HOH A O   1 
HETATM 1255 O  O   . HOH F 6 .   ? 27.127 -2.443  16.106 1.00 66.36  ? 353 HOH A O   1 
HETATM 1256 O  O   . HOH F 6 .   ? 41.210 -6.980  35.868 1.00 48.45  ? 354 HOH A O   1 
HETATM 1257 O  O   . HOH F 6 .   ? 36.887 -5.546  12.144 1.00 44.46  ? 355 HOH A O   1 
HETATM 1258 O  O   . HOH F 6 .   ? 24.070 -15.776 21.149 1.00 33.11  ? 356 HOH A O   1 
HETATM 1259 O  O   . HOH F 6 .   ? 46.018 -14.171 21.446 1.00 64.71  ? 357 HOH A O   1 
HETATM 1260 O  O   . HOH F 6 .   ? 43.997 -4.407  25.789 1.00 52.07  ? 358 HOH A O   1 
HETATM 1261 O  O   . HOH F 6 .   ? 47.176 -25.333 21.693 1.00 64.03  ? 359 HOH A O   1 
HETATM 1262 O  O   . HOH F 6 .   ? 25.704 -2.723  19.962 1.00 63.33  ? 360 HOH A O   1 
HETATM 1263 O  O   . HOH F 6 .   ? 42.508 -10.401 15.419 1.00 48.97  ? 361 HOH A O   1 
HETATM 1264 O  O   . HOH F 6 .   ? 21.401 -29.935 14.168 1.00 75.96  ? 362 HOH A O   1 
HETATM 1265 O  O   . HOH F 6 .   ? 44.314 -12.546 41.162 1.00 56.39  ? 363 HOH A O   1 
HETATM 1266 O  O   . HOH F 6 .   ? 20.799 -7.175  19.596 1.00 66.46  ? 364 HOH A O   1 
HETATM 1267 O  O   . HOH F 6 .   ? 29.362 -27.356 20.586 1.00 29.14  ? 365 HOH A O   1 
HETATM 1268 O  O   . HOH F 6 .   ? 21.388 -27.102 14.495 0.50 53.42  ? 366 HOH A O   1 
HETATM 1269 O  O   . HOH F 6 .   ? 28.489 -24.127 34.277 1.00 57.42  ? 367 HOH A O   1 
HETATM 1270 O  O   . HOH F 6 .   ? 22.687 -33.992 8.825  1.00 37.22  ? 368 HOH A O   1 
HETATM 1271 O  O   . HOH F 6 .   ? 46.222 -15.848 27.596 1.00 67.11  ? 369 HOH A O   1 
HETATM 1272 O  O   A HOH F 6 .   ? 19.065 -23.017 4.291  0.60 40.71  ? 370 HOH A O   1 
HETATM 1273 O  O   . HOH F 6 .   ? 46.324 -18.881 19.628 1.00 56.80  ? 371 HOH A O   1 
HETATM 1274 O  O   . HOH F 6 .   ? 37.413 -6.387  34.213 1.00 44.82  ? 372 HOH A O   1 
HETATM 1275 O  O   . HOH F 6 .   ? 22.290 -34.099 26.323 1.00 81.91  ? 373 HOH A O   1 
HETATM 1276 O  O   . HOH F 6 .   ? 21.368 -31.158 29.906 1.00 71.80  ? 374 HOH A O   1 
HETATM 1277 O  O   . HOH F 6 .   ? 46.342 -29.776 21.215 1.00 74.93  ? 375 HOH A O   1 
HETATM 1278 O  O   . HOH F 6 .   ? 26.140 -19.307 41.734 1.00 81.30  ? 376 HOH A O   1 
HETATM 1279 O  O   . HOH F 6 .   ? 44.710 -8.569  17.806 1.00 70.44  ? 377 HOH A O   1 
HETATM 1280 O  O   . HOH F 6 .   ? 10.775 -11.280 34.377 1.00 57.89  ? 378 HOH A O   1 
HETATM 1281 O  O   . HOH F 6 .   ? 30.677 -28.779 22.587 1.00 41.27  ? 379 HOH A O   1 
HETATM 1282 O  O   . HOH F 6 .   ? 26.387 -7.879  9.095  1.00 50.44  ? 380 HOH A O   1 
HETATM 1283 O  O   . HOH F 6 .   ? 46.898 -21.849 17.906 1.00 42.75  ? 381 HOH A O   1 
HETATM 1284 O  O   . HOH F 6 .   ? 34.138 -7.821  35.610 1.00 38.20  ? 382 HOH A O   1 
HETATM 1285 O  O   . HOH F 6 .   ? 18.026 -24.278 39.756 1.00 46.70  ? 383 HOH A O   1 
HETATM 1286 O  O   . HOH F 6 .   ? 27.684 -23.029 13.839 0.50 28.67  ? 384 HOH A O   1 
HETATM 1287 O  O   . HOH F 6 .   ? 18.062 -34.588 8.305  1.00 36.65  ? 385 HOH A O   1 
HETATM 1288 O  O   . HOH F 6 .   ? 20.089 -15.708 40.772 1.00 38.46  ? 386 HOH A O   1 
HETATM 1289 O  O   . HOH F 6 .   ? 20.932 -22.964 41.994 1.00 53.45  ? 387 HOH A O   1 
HETATM 1290 O  O   . HOH F 6 .   ? 45.977 -8.901  44.003 1.00 57.95  ? 388 HOH A O   1 
HETATM 1291 O  O   . HOH F 6 .   ? 31.845 -31.860 14.622 1.00 47.81  ? 389 HOH A O   1 
HETATM 1292 O  O   . HOH F 6 .   ? 40.336 -19.603 28.961 1.00 38.59  ? 390 HOH A O   1 
HETATM 1293 O  O   . HOH F 6 .   ? 42.203 -6.110  11.804 1.00 74.54  ? 391 HOH A O   1 
HETATM 1294 O  O   . HOH F 6 .   ? 45.296 -12.693 23.594 1.00 54.18  ? 392 HOH A O   1 
HETATM 1295 O  O   . HOH F 6 .   ? 37.913 -16.267 12.747 1.00 56.58  ? 393 HOH A O   1 
HETATM 1296 O  O   . HOH F 6 .   ? 33.017 -29.669 21.544 1.00 45.92  ? 394 HOH A O   1 
HETATM 1297 O  O   . HOH F 6 .   ? 39.980 -5.582  33.853 1.00 47.92  ? 395 HOH A O   1 
HETATM 1298 O  O   . HOH F 6 .   ? 43.529 -10.731 35.287 1.00 66.74  ? 396 HOH A O   1 
HETATM 1299 O  O   . HOH F 6 .   ? 11.373 -14.841 40.627 1.00 91.85  ? 397 HOH A O   1 
HETATM 1300 O  O   . HOH F 6 .   ? 22.864 -14.753 40.306 1.00 36.79  ? 398 HOH A O   1 
HETATM 1301 O  O   . HOH F 6 .   ? 27.155 -1.579  21.966 1.00 58.27  ? 399 HOH A O   1 
HETATM 1302 O  O   . HOH F 6 .   ? 35.505 2.072   13.560 1.00 63.88  ? 400 HOH A O   1 
HETATM 1303 O  O   . HOH F 6 .   ? 33.723 -33.064 12.274 1.00 43.72  ? 401 HOH A O   1 
HETATM 1304 O  O   . HOH F 6 .   ? 32.014 -15.560 39.787 1.00 39.42  ? 402 HOH A O   1 
HETATM 1305 O  O   . HOH F 6 .   ? 23.686 -15.778 17.793 1.00 44.78  ? 403 HOH A O   1 
HETATM 1306 O  O   . HOH F 6 .   ? 34.773 -33.331 21.921 1.00 64.37  ? 404 HOH A O   1 
HETATM 1307 O  O   . HOH F 6 .   ? 46.943 -20.101 21.950 1.00 66.80  ? 405 HOH A O   1 
HETATM 1308 O  O   . HOH F 6 .   ? 41.885 -8.102  13.684 1.00 66.77  ? 406 HOH A O   1 
HETATM 1309 O  O   . HOH F 6 .   ? 37.212 -2.553  11.640 1.00 61.13  ? 407 HOH A O   1 
HETATM 1310 O  O   . HOH F 6 .   ? 41.104 -17.163 35.179 1.00 47.46  ? 408 HOH A O   1 
HETATM 1311 O  O   B HOH F 6 .   ? 37.241 -11.832 40.073 0.50 38.82  ? 409 HOH A O   1 
HETATM 1312 O  O   . HOH F 6 .   ? 19.644 -27.357 10.009 1.00 61.94  ? 410 HOH A O   1 
HETATM 1313 O  O   . HOH F 6 .   ? 44.577 -16.436 29.663 1.00 53.09  ? 411 HOH A O   1 
HETATM 1314 O  O   . HOH F 6 .   ? 27.472 -25.742 28.045 1.00 56.84  ? 412 HOH A O   1 
HETATM 1315 O  O   . HOH F 6 .   ? 30.326 -10.429 40.531 1.00 44.20  ? 413 HOH A O   1 
HETATM 1316 O  O   . HOH F 6 .   ? 28.652 -15.965 41.257 1.00 71.91  ? 414 HOH A O   1 
HETATM 1317 O  O   . HOH F 6 .   ? 10.229 -11.758 39.948 1.00 68.85  ? 415 HOH A O   1 
HETATM 1318 O  O   . HOH F 6 .   ? 29.696 -0.819  22.195 1.00 66.33  ? 416 HOH A O   1 
HETATM 1319 O  O   . HOH F 6 .   ? 35.270 -29.827 23.554 1.00 53.27  ? 417 HOH A O   1 
HETATM 1320 O  O   . HOH F 6 .   ? 44.884 -8.050  15.132 1.00 77.83  ? 418 HOH A O   1 
HETATM 1321 O  O   . HOH F 6 .   ? 44.292 -25.970 26.612 1.00 62.96  ? 419 HOH A O   1 
HETATM 1322 O  O   . HOH F 6 .   ? 22.362 -10.249 14.428 1.00 47.64  ? 420 HOH A O   1 
HETATM 1323 O  O   . HOH F 6 .   ? 26.180 -29.281 22.559 1.00 61.86  ? 421 HOH A O   1 
HETATM 1324 O  O   . HOH F 6 .   ? 33.488 -0.242  19.921 1.00 51.36  ? 422 HOH A O   1 
HETATM 1325 O  O   . HOH F 6 .   ? 25.630 -15.846 41.017 1.00 56.70  ? 423 HOH A O   1 
HETATM 1326 O  O   . HOH F 6 .   ? 45.472 -10.396 30.465 1.00 63.77  ? 424 HOH A O   1 
HETATM 1327 O  O   . HOH F 6 .   ? 33.816 -17.581 39.407 1.00 67.50  ? 425 HOH A O   1 
HETATM 1328 O  O   . HOH F 6 .   ? 23.416 -30.478 19.242 1.00 69.70  ? 426 HOH A O   1 
HETATM 1329 O  O   . HOH F 6 .   ? 45.819 -5.509  23.688 1.00 51.94  ? 427 HOH A O   1 
HETATM 1330 O  O   . HOH F 6 .   ? 42.825 -18.236 30.700 1.00 53.79  ? 428 HOH A O   1 
HETATM 1331 O  O   . HOH F 6 .   ? 29.889 -22.677 36.719 1.00 77.43  ? 429 HOH A O   1 
HETATM 1332 O  O   . HOH F 6 .   ? 46.053 -17.055 17.099 1.00 69.90  ? 430 HOH A O   1 
HETATM 1333 O  O   . HOH F 6 .   ? 28.325 -2.459  11.273 1.00 73.52  ? 431 HOH A O   1 
HETATM 1334 O  O   . HOH F 6 .   ? 47.868 -23.403 19.911 1.00 70.62  ? 432 HOH A O   1 
HETATM 1335 O  O   . HOH F 6 .   ? 31.924 -26.217 27.062 1.00 52.45  ? 433 HOH A O   1 
HETATM 1336 O  O   . HOH F 6 .   ? 37.629 -27.013 28.441 1.00 70.37  ? 434 HOH A O   1 
HETATM 1337 O  O   . HOH F 6 .   ? 32.451 -4.087  41.229 1.00 63.02  ? 435 HOH A O   1 
HETATM 1338 O  O   . HOH F 6 .   ? 32.000 0.211   13.338 1.00 64.20  ? 436 HOH A O   1 
HETATM 1339 O  O   . HOH F 6 .   ? 28.305 -29.138 26.798 1.00 92.90  ? 437 HOH A O   1 
HETATM 1340 O  O   . HOH F 6 .   ? 35.247 -4.100  10.590 1.00 50.05  ? 438 HOH A O   1 
HETATM 1341 O  O   . HOH F 6 .   ? 27.174 -34.639 17.933 1.00 80.80  ? 439 HOH A O   1 
HETATM 1342 O  O   . HOH F 6 .   ? 47.111 -13.015 28.695 1.00 66.44  ? 440 HOH A O   1 
HETATM 1343 O  O   . HOH F 6 .   ? 20.031 -35.317 10.174 1.00 46.58  ? 441 HOH A O   1 
HETATM 1344 O  O   . HOH F 6 .   ? 37.131 -24.322 27.491 1.00 60.45  ? 442 HOH A O   1 
HETATM 1345 O  O   . HOH F 6 .   ? 19.406 -31.750 13.831 1.00 74.70  ? 443 HOH A O   1 
HETATM 1346 O  O   . HOH F 6 .   ? 24.311 -21.579 41.096 1.00 64.65  ? 444 HOH A O   1 
HETATM 1347 O  O   . HOH F 6 .   ? 23.015 -2.710  26.084 1.00 65.39  ? 445 HOH A O   1 
HETATM 1348 O  O   . HOH F 6 .   ? 30.930 -34.410 14.918 1.00 62.41  ? 446 HOH A O   1 
HETATM 1349 O  O   . HOH F 6 .   ? 33.785 -10.830 41.517 0.50 58.51  ? 447 HOH A O   1 
HETATM 1350 O  O   . HOH F 6 .   ? 46.672 -14.585 18.112 1.00 71.88  ? 448 HOH A O   1 
HETATM 1351 O  O   . HOH F 6 .   ? 11.968 -18.623 22.521 1.00 64.21  ? 449 HOH A O   1 
HETATM 1352 O  O   . HOH F 6 .   ? 47.136 -11.843 25.422 1.00 73.86  ? 450 HOH A O   1 
HETATM 1353 O  O   . HOH F 6 .   ? 34.532 -18.847 36.145 1.00 62.96  ? 451 HOH A O   1 
HETATM 1354 O  O   . HOH F 6 .   ? 32.360 -1.025  22.254 1.00 65.99  ? 452 HOH A O   1 
HETATM 1355 O  O   . HOH F 6 .   ? 47.494 -28.557 17.775 1.00 70.51  ? 453 HOH A O   1 
HETATM 1356 O  O   . HOH F 6 .   ? 13.637 -16.127 39.782 1.00 80.22  ? 454 HOH A O   1 
HETATM 1357 O  O   . HOH F 6 .   ? 43.095 -3.066  33.713 1.00 66.07  ? 455 HOH A O   1 
HETATM 1358 O  O   . HOH F 6 .   ? 19.301 -7.445  35.320 1.00 60.14  ? 456 HOH A O   1 
HETATM 1359 O  O   . HOH F 6 .   ? 25.377 -5.735  35.223 1.00 58.26  ? 457 HOH A O   1 
HETATM 1360 O  O   . HOH F 6 .   ? 15.884 -15.415 41.137 1.00 67.45  ? 458 HOH A O   1 
HETATM 1361 O  O   . HOH F 6 .   ? 33.785 -13.899 41.517 0.50 46.26  ? 459 HOH A O   1 
HETATM 1362 O  O   A HOH F 6 .   ? 11.974 -20.674 27.799 0.78 51.24  ? 460 HOH A O   1 
HETATM 1363 O  O   . HOH F 6 .   ? 17.099 -28.226 9.939  1.00 58.23  ? 461 HOH A O   1 
HETATM 1364 O  O   . HOH F 6 .   ? 17.387 -8.001  24.740 1.00 64.97  ? 462 HOH A O   1 
HETATM 1365 O  O   . HOH F 6 .   ? 44.328 -13.419 13.839 0.50 79.85  ? 463 HOH A O   1 
HETATM 1366 O  O   . HOH F 6 .   ? 32.103 -23.885 34.776 1.00 71.85  ? 464 HOH A O   1 
HETATM 1367 O  O   . HOH F 6 .   ? 32.538 -20.515 36.984 1.00 76.11  ? 465 HOH A O   1 
HETATM 1368 O  O   . HOH F 6 .   ? 28.254 -29.908 24.186 1.00 74.12  ? 466 HOH A O   1 
HETATM 1369 O  O   . HOH F 6 .   ? 18.920 -28.089 13.839 0.50 77.21  ? 467 HOH A O   1 
HETATM 1370 O  O   . HOH F 6 .   ? 21.161 -5.589  34.578 1.00 68.09  ? 468 HOH A O   1 
HETATM 1371 O  O   . HOH F 6 .   ? 45.595 -12.856 16.198 1.00 76.40  ? 469 HOH A O   1 
HETATM 1372 O  O   . HOH F 6 .   ? 23.317 -4.467  17.120 1.00 75.00  ? 470 HOH A O   1 
HETATM 1373 O  O   . HOH F 6 .   ? 34.945 -23.658 32.773 1.00 67.96  ? 471 HOH A O   1 
HETATM 1374 O  O   . HOH F 6 .   ? 16.778 -6.616  34.658 1.00 84.32  ? 472 HOH A O   1 
HETATM 1375 O  O   . HOH F 6 .   ? 33.046 -0.570  42.883 1.00 60.95  ? 473 HOH A O   1 
HETATM 1376 O  O   . HOH G 6 .   ? 12.375 -24.231 -0.046 1.00 54.80  ? 201 HOH D O   1 
HETATM 1377 O  O   . HOH G 6 .   ? 14.954 -25.835 -1.831 1.00 47.38  ? 202 HOH D O   1 
HETATM 1378 O  O   . HOH G 6 .   ? 11.777 -23.554 2.889  1.00 58.04  ? 203 HOH D O   1 
HETATM 1379 O  O   . HOH G 6 .   ? 21.027 -38.287 4.053  1.00 49.71  ? 204 HOH D O   1 
HETATM 1380 O  O   . HOH G 6 .   ? 17.756 -36.319 6.154  1.00 43.09  ? 205 HOH D O   1 
HETATM 1381 O  O   . HOH G 6 .   ? 18.722 -40.551 0.789  1.00 73.45  ? 206 HOH D O   1 
HETATM 1382 O  O   . HOH G 6 .   ? 20.963 -39.476 -2.188 1.00 64.75  ? 207 HOH D O   1 
HETATM 1383 O  O   . HOH G 6 .   ? 10.650 -24.888 5.578  1.00 59.89  ? 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   ? 0.8698 1.0563 0.7661 0.0503  -0.1389 -0.0308 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8643 1.0424 0.7428 0.0331  -0.1295 -0.0325 6   ASP A CA  
3    C C   . ASP A 5   ? 0.8414 1.0525 0.7468 0.0197  -0.1253 -0.0496 6   ASP A C   
4    O O   . ASP A 5   ? 0.8288 1.0706 0.7643 0.0235  -0.1308 -0.0604 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8868 1.0329 0.7553 0.0232  -0.1108 -0.0238 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0798 1.2015 0.9120 0.0138  -0.1054 -0.0183 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0843 1.2180 0.9141 0.0022  -0.1030 -0.0272 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1825 1.2725 0.9882 0.0167  -0.1022 -0.0060 6   ASP A OD2 
9    N N   . SER A 6   ? 0.7390 0.9431 0.6334 0.0036  -0.1146 -0.0531 7   SER A N   
10   C CA  . SER A 6   ? 0.6917 0.9191 0.6062 -0.0110 -0.1081 -0.0687 7   SER A CA  
11   C C   . SER A 6   ? 0.6431 0.8560 0.5702 -0.0239 -0.0880 -0.0697 7   SER A C   
12   O O   . SER A 6   ? 0.6347 0.8509 0.5651 -0.0377 -0.0791 -0.0788 7   SER A O   
13   C CB  . SER A 6   ? 0.7665 0.9979 0.6576 -0.0183 -0.1132 -0.0738 7   SER A CB  
14   O OG  . SER A 6   ? 0.9334 1.1335 0.7938 -0.0240 -0.1046 -0.0646 7   SER A OG  
15   N N   . CYS A 7   ? 0.5256 0.7221 0.4595 -0.0185 -0.0817 -0.0607 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4794 0.6612 0.4240 -0.0276 -0.0655 -0.0604 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4555 0.6549 0.4269 -0.0367 -0.0591 -0.0729 8   CYS A C   
18   O O   . CYS A 7   ? 0.4511 0.6751 0.4392 -0.0342 -0.0660 -0.0808 8   CYS A O   
19   C CB  . CYS A 7   ? 0.4924 0.6558 0.4377 -0.0188 -0.0627 -0.0488 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5762 0.7084 0.4875 -0.0140 -0.0625 -0.0343 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3389 0.5244 0.3141 -0.0470 -0.0459 -0.0752 9   ILE A N   
22   C CA  . ILE A 8   ? 0.3008 0.4915 0.2960 -0.0555 -0.0375 -0.0839 9   ILE A CA  
23   C C   . ILE A 8   ? 0.3256 0.4981 0.3257 -0.0509 -0.0314 -0.0748 9   ILE A C   
24   O O   . ILE A 8   ? 0.3235 0.4789 0.3117 -0.0450 -0.0311 -0.0646 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3417 0.5279 0.3358 -0.0694 -0.0283 -0.0937 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3552 0.5170 0.3348 -0.0708 -0.0213 -0.0882 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3629 0.5724 0.3557 -0.0751 -0.0347 -0.1052 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3921 0.5448 0.3718 -0.0822 -0.0114 -0.0976 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2544 0.4294 0.2702 -0.0548 -0.0258 -0.0791 10  GLN A N   
30   N N   B GLN A 9   ? 0.2610 0.4377 0.2774 -0.0542 -0.0266 -0.0792 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2378 0.3956 0.2563 -0.0506 -0.0208 -0.0709 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2464 0.4073 0.2668 -0.0506 -0.0213 -0.0718 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2800 0.4231 0.3020 -0.0604 -0.0100 -0.0746 10  GLN A C   
34   C C   B GLN A 9   ? 0.2837 0.4283 0.3060 -0.0605 -0.0103 -0.0752 10  GLN A C   
35   O O   A GLN A 9   ? 0.2685 0.4204 0.2980 -0.0698 -0.0060 -0.0847 10  GLN A O   
36   O O   B GLN A 9   ? 0.2776 0.4291 0.3054 -0.0707 -0.0060 -0.0854 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2489 0.4214 0.2798 -0.0425 -0.0260 -0.0701 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2546 0.4325 0.2899 -0.0445 -0.0255 -0.0734 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2458 0.4019 0.2786 -0.0383 -0.0212 -0.0623 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.3657 0.5299 0.4068 -0.0442 -0.0182 -0.0692 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5902 0.7627 0.6389 -0.0335 -0.0234 -0.0658 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4678 0.6313 0.5105 -0.0316 -0.0233 -0.0612 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4830 0.6717 0.5459 -0.0409 -0.0198 -0.0766 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3289 0.5018 0.3689 -0.0214 -0.0331 -0.0584 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.6331 0.8013 0.6800 -0.0215 -0.0283 -0.0577 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.3427 0.4924 0.3876 -0.0317 -0.0168 -0.0573 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2650 0.3850 0.2806 -0.0582 -0.0054 -0.0671 11  PHE A N   
48   N N   B PHE A 10  ? 0.2497 0.3721 0.2664 -0.0575 -0.0061 -0.0670 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2697 0.3712 0.2847 -0.0649 0.0028  -0.0690 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2527 0.3556 0.2681 -0.0639 0.0021  -0.0683 11  PHE A CA  
51   C C   A PHE A 10  ? 0.3017 0.4002 0.3224 -0.0636 0.0051  -0.0660 11  PHE A C   
52   C C   B PHE A 10  ? 0.2973 0.3975 0.3186 -0.0630 0.0045  -0.0659 11  PHE A C   
53   O O   A PHE A 10  ? 0.2900 0.3806 0.3089 -0.0559 0.0033  -0.0576 11  PHE A O   
54   O O   B PHE A 10  ? 0.2852 0.3796 0.3056 -0.0550 0.0024  -0.0576 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2943 0.3747 0.3006 -0.0624 0.0051  -0.0645 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2764 0.3596 0.2831 -0.0602 0.0036  -0.0627 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.3203 0.3796 0.3233 -0.0677 0.0115  -0.0671 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.3054 0.3873 0.3070 -0.0649 0.0053  -0.0688 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3736 0.4299 0.3746 -0.0771 0.0161  -0.0761 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3490 0.4455 0.3466 -0.0645 0.0010  -0.0706 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3522 0.3924 0.3518 -0.0630 0.0124  -0.0607 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3485 0.4131 0.3476 -0.0695 0.0110  -0.0731 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3984 0.4293 0.3921 -0.0814 0.0218  -0.0777 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3680 0.4634 0.3601 -0.0698 0.0036  -0.0773 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3877 0.4047 0.3803 -0.0663 0.0165  -0.0621 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3948 0.4581 0.3902 -0.0736 0.0133  -0.0801 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3713 0.3819 0.3599 -0.0751 0.0213  -0.0701 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3664 0.4460 0.3588 -0.0744 0.0101  -0.0825 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2598 0.3658 0.2872 -0.0722 0.0097  -0.0742 12  THR A N   
70   C CA  . THR A 11  ? 0.2586 0.3646 0.2917 -0.0738 0.0138  -0.0744 12  THR A CA  
71   C C   . THR A 11  ? 0.3211 0.4005 0.3442 -0.0705 0.0167  -0.0651 12  THR A C   
72   O O   . THR A 11  ? 0.3070 0.3887 0.3338 -0.0648 0.0156  -0.0606 12  THR A O   
73   C CB  . THR A 11  ? 0.3518 0.4634 0.3895 -0.0881 0.0220  -0.0864 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3415 0.4831 0.3914 -0.0904 0.0177  -0.0963 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3959 0.5090 0.4394 -0.0920 0.0283  -0.0886 12  THR A CG2 
76   N N   A ARG A 12  ? 0.2987 0.3536 0.3094 -0.0734 0.0197  -0.0630 13  ARG A N   
77   N N   B ARG A 12  ? 0.3009 0.3557 0.3116 -0.0734 0.0197  -0.0630 13  ARG A N   
78   C CA  A ARG A 12  ? 0.3124 0.3421 0.3125 -0.0701 0.0209  -0.0554 13  ARG A CA  
79   C CA  B ARG A 12  ? 0.3156 0.3452 0.3156 -0.0701 0.0208  -0.0554 13  ARG A CA  
80   C C   A ARG A 12  ? 0.3383 0.3648 0.3378 -0.0588 0.0146  -0.0472 13  ARG A C   
81   C C   B ARG A 12  ? 0.3391 0.3658 0.3386 -0.0587 0.0146  -0.0472 13  ARG A C   
82   O O   A ARG A 12  ? 0.3284 0.3372 0.3206 -0.0554 0.0142  -0.0420 13  ARG A O   
83   O O   B ARG A 12  ? 0.3285 0.3375 0.3208 -0.0554 0.0142  -0.0419 13  ARG A O   
84   C CB  A ARG A 12  ? 0.3591 0.3618 0.3451 -0.0767 0.0257  -0.0572 13  ARG A CB  
85   C CB  B ARG A 12  ? 0.3682 0.3710 0.3543 -0.0764 0.0254  -0.0572 13  ARG A CB  
86   C CG  A ARG A 12  ? 0.4775 0.4747 0.4587 -0.0908 0.0348  -0.0648 13  ARG A CG  
87   C CG  B ARG A 12  ? 0.5257 0.5164 0.5036 -0.0886 0.0342  -0.0617 13  ARG A CG  
88   C CD  A ARG A 12  ? 0.6246 0.6157 0.6016 -0.0946 0.0396  -0.0630 13  ARG A CD  
89   C CD  B ARG A 12  ? 0.6261 0.6032 0.5954 -0.0993 0.0404  -0.0691 13  ARG A CD  
90   N NE  A ARG A 12  ? 0.7062 0.6652 0.6644 -0.0910 0.0389  -0.0546 13  ARG A NE  
91   N NE  B ARG A 12  ? 0.7053 0.6590 0.6638 -0.0935 0.0372  -0.0658 13  ARG A NE  
92   C CZ  A ARG A 12  ? 0.7894 0.7415 0.7420 -0.0900 0.0400  -0.0501 13  ARG A CZ  
93   C CZ  B ARG A 12  ? 0.8182 0.7758 0.7797 -0.0946 0.0369  -0.0715 13  ARG A CZ  
94   N NH1 A ARG A 12  ? 0.5285 0.5032 0.4945 -0.0919 0.0428  -0.0533 13  ARG A NH1 
95   N NH1 B ARG A 12  ? 0.7078 0.6442 0.6613 -0.0882 0.0343  -0.0696 13  ARG A NH1 
96   N NH2 A ARG A 12  ? 0.6437 0.5665 0.5773 -0.0864 0.0376  -0.0429 13  ARG A NH2 
97   N NH2 B ARG A 12  ? 0.5054 0.4888 0.4784 -0.1018 0.0388  -0.0800 13  ARG A NH2 
98   N N   . HIS A 13  ? 0.2826 0.3254 0.2880 -0.0537 0.0100  -0.0468 14  HIS A N   
99   C CA  . HIS A 13  ? 0.2758 0.3153 0.2796 -0.0457 0.0062  -0.0407 14  HIS A CA  
100  C C   . HIS A 13  ? 0.2908 0.3251 0.2944 -0.0406 0.0054  -0.0343 14  HIS A C   
101  O O   . HIS A 13  ? 0.2890 0.3112 0.2891 -0.0374 0.0047  -0.0312 14  HIS A O   
102  C CB  . HIS A 13  ? 0.2722 0.3269 0.2775 -0.0430 0.0027  -0.0409 14  HIS A CB  
103  C CG  . HIS A 13  ? 0.2941 0.3431 0.2958 -0.0379 0.0016  -0.0362 14  HIS A CG  
104  N ND1 . HIS A 13  ? 0.3079 0.3483 0.3083 -0.0384 0.0033  -0.0387 14  HIS A ND1 
105  C CD2 . HIS A 13  ? 0.3080 0.3585 0.3076 -0.0329 -0.0002 -0.0305 14  HIS A CD2 
106  C CE1 . HIS A 13  ? 0.2995 0.3394 0.2985 -0.0350 0.0032  -0.0355 14  HIS A CE1 
107  N NE2 . HIS A 13  ? 0.3039 0.3479 0.3007 -0.0323 0.0015  -0.0300 14  HIS A NE2 
108  N N   . ALA A 14  ? 0.2591 0.3041 0.2678 -0.0392 0.0051  -0.0334 15  ALA A N   
109  C CA  . ALA A 14  ? 0.2621 0.3016 0.2704 -0.0346 0.0051  -0.0280 15  ALA A CA  
110  C C   . ALA A 14  ? 0.3042 0.3258 0.3058 -0.0377 0.0081  -0.0270 15  ALA A C   
111  O O   . ALA A 14  ? 0.2718 0.2840 0.2697 -0.0340 0.0068  -0.0228 15  ALA A O   
112  C CB  . ALA A 14  ? 0.2754 0.3293 0.2916 -0.0322 0.0048  -0.0292 15  ALA A CB  
113  N N   A SER A 15  ? 0.2851 0.3010 0.2831 -0.0451 0.0122  -0.0312 16  SER A N   
114  N N   B SER A 15  ? 0.2855 0.3014 0.2835 -0.0451 0.0122  -0.0312 16  SER A N   
115  N N   C SER A 15  ? 0.2772 0.2930 0.2752 -0.0451 0.0122  -0.0311 16  SER A N   
116  C CA  A SER A 15  ? 0.3028 0.2973 0.2885 -0.0489 0.0149  -0.0298 16  SER A CA  
117  C CA  B SER A 15  ? 0.3036 0.2979 0.2892 -0.0489 0.0149  -0.0298 16  SER A CA  
118  C CA  C SER A 15  ? 0.2911 0.2853 0.2767 -0.0488 0.0149  -0.0296 16  SER A CA  
119  C C   A SER A 15  ? 0.3562 0.3343 0.3340 -0.0446 0.0104  -0.0270 16  SER A C   
120  C C   B SER A 15  ? 0.3581 0.3361 0.3358 -0.0446 0.0104  -0.0270 16  SER A C   
121  C C   C SER A 15  ? 0.3539 0.3317 0.3315 -0.0446 0.0104  -0.0269 16  SER A C   
122  O O   A SER A 15  ? 0.3379 0.3023 0.3078 -0.0416 0.0081  -0.0232 16  SER A O   
123  O O   B SER A 15  ? 0.3431 0.3073 0.3129 -0.0416 0.0081  -0.0232 16  SER A O   
124  O O   C SER A 15  ? 0.3417 0.3053 0.3111 -0.0418 0.0082  -0.0233 16  SER A O   
125  C CB  A SER A 15  ? 0.3621 0.3516 0.3428 -0.0595 0.0216  -0.0355 16  SER A CB  
126  C CB  B SER A 15  ? 0.3650 0.3542 0.3455 -0.0595 0.0216  -0.0355 16  SER A CB  
127  C CB  C SER A 15  ? 0.3369 0.3259 0.3173 -0.0594 0.0217  -0.0352 16  SER A CB  
128  O OG  A SER A 15  ? 0.4471 0.4109 0.4102 -0.0639 0.0246  -0.0333 16  SER A OG  
129  O OG  B SER A 15  ? 0.4393 0.4481 0.4312 -0.0633 0.0257  -0.0405 16  SER A OG  
130  O OG  C SER A 15  ? 0.3647 0.3531 0.3445 -0.0632 0.0222  -0.0395 16  SER A OG  
131  N N   . ASP A 16  ? 0.3254 0.3066 0.3063 -0.0437 0.0088  -0.0298 17  ASP A N   
132  C CA  . ASP A 16  ? 0.3422 0.3116 0.3199 -0.0384 0.0046  -0.0296 17  ASP A CA  
133  C C   . ASP A 16  ? 0.3489 0.3260 0.3334 -0.0312 0.0005  -0.0268 17  ASP A C   
134  O O   . ASP A 16  ? 0.3490 0.3159 0.3307 -0.0262 -0.0037 -0.0261 17  ASP A O   
135  C CB  . ASP A 16  ? 0.3604 0.3349 0.3421 -0.0398 0.0053  -0.0350 17  ASP A CB  
136  C CG  . ASP A 16  ? 0.5200 0.4823 0.4934 -0.0476 0.0097  -0.0391 17  ASP A CG  
137  O OD1 . ASP A 16  ? 0.5367 0.4837 0.4991 -0.0524 0.0127  -0.0376 17  ASP A OD1 
138  O OD2 . ASP A 16  ? 0.5113 0.4782 0.4878 -0.0501 0.0112  -0.0446 17  ASP A OD2 
139  N N   . VAL A 17  ? 0.2809 0.2750 0.2733 -0.0308 0.0015  -0.0258 18  VAL A N   
140  C CA  . VAL A 17  ? 0.2691 0.2678 0.2655 -0.0263 -0.0002 -0.0236 18  VAL A CA  
141  C C   . VAL A 17  ? 0.3062 0.2956 0.2981 -0.0250 -0.0014 -0.0204 18  VAL A C   
142  O O   . VAL A 17  ? 0.2953 0.2812 0.2880 -0.0216 -0.0046 -0.0208 18  VAL A O   
143  C CB  . VAL A 17  ? 0.2859 0.2980 0.2859 -0.0263 0.0014  -0.0219 18  VAL A CB  
144  C CG1 . VAL A 17  ? 0.2762 0.2878 0.2767 -0.0238 0.0017  -0.0192 18  VAL A CG1 
145  C CG2 . VAL A 17  ? 0.2770 0.2972 0.2784 -0.0276 0.0019  -0.0253 18  VAL A CG2 
146  N N   . LEU A 18  ? 0.2825 0.2692 0.2702 -0.0281 0.0013  -0.0185 19  LEU A N   
147  C CA  . LEU A 18  ? 0.2905 0.2682 0.2721 -0.0280 0.0012  -0.0160 19  LEU A CA  
148  C C   . LEU A 18  ? 0.3412 0.3011 0.3115 -0.0271 -0.0030 -0.0158 19  LEU A C   
149  O O   . LEU A 18  ? 0.3060 0.2609 0.2732 -0.0241 -0.0068 -0.0148 19  LEU A O   
150  C CB  . LEU A 18  ? 0.3020 0.2817 0.2823 -0.0323 0.0064  -0.0158 19  LEU A CB  
151  C CG  . LEU A 18  ? 0.3434 0.3170 0.3190 -0.0324 0.0079  -0.0139 19  LEU A CG  
152  C CD1 . LEU A 18  ? 0.3364 0.3178 0.3193 -0.0279 0.0072  -0.0123 19  LEU A CD1 
153  C CD2 . LEU A 18  ? 0.4057 0.3806 0.3802 -0.0377 0.0144  -0.0161 19  LEU A CD2 
154  N N   . LEU A 19  ? 0.3320 0.2816 0.2956 -0.0291 -0.0029 -0.0172 20  LEU A N   
155  C CA  . LEU A 19  ? 0.3611 0.2890 0.3106 -0.0266 -0.0080 -0.0165 20  LEU A CA  
156  C C   . LEU A 19  ? 0.3632 0.2954 0.3209 -0.0175 -0.0159 -0.0184 20  LEU A C   
157  O O   . LEU A 19  ? 0.3562 0.2783 0.3065 -0.0127 -0.0227 -0.0173 20  LEU A O   
158  C CB  . LEU A 19  ? 0.3953 0.3107 0.3370 -0.0307 -0.0051 -0.0184 20  LEU A CB  
159  C CG  . LEU A 19  ? 0.5248 0.4110 0.4471 -0.0275 -0.0102 -0.0168 20  LEU A CG  
160  C CD1 . LEU A 19  ? 0.5749 0.4395 0.4746 -0.0329 -0.0083 -0.0125 20  LEU A CD1 
161  C CD2 . LEU A 19  ? 0.5855 0.4604 0.5027 -0.0312 -0.0067 -0.0199 20  LEU A CD2 
162  N N   . ASN A 20  ? 0.3025 0.2516 0.2757 -0.0157 -0.0150 -0.0222 21  ASN A N   
163  C CA  . ASN A 20  ? 0.2997 0.2576 0.2844 -0.0088 -0.0204 -0.0267 21  ASN A CA  
164  C C   . ASN A 20  ? 0.3242 0.2919 0.3146 -0.0080 -0.0217 -0.0266 21  ASN A C   
165  O O   . ASN A 20  ? 0.3125 0.2821 0.3077 -0.0022 -0.0283 -0.0304 21  ASN A O   
166  C CB  . ASN A 20  ? 0.3052 0.2772 0.3024 -0.0094 -0.0168 -0.0317 21  ASN A CB  
167  C CG  . ASN A 20  ? 0.4448 0.4050 0.4378 -0.0078 -0.0179 -0.0345 21  ASN A CG  
168  O OD1 . ASN A 20  ? 0.4093 0.3496 0.3910 -0.0037 -0.0230 -0.0332 21  ASN A OD1 
169  N ND2 . ASN A 20  ? 0.3432 0.3126 0.3423 -0.0112 -0.0131 -0.0382 21  ASN A ND2 
170  N N   . LEU A 21  ? 0.2922 0.2666 0.2830 -0.0133 -0.0156 -0.0233 22  LEU A N   
171  C CA  . LEU A 21  ? 0.2901 0.2701 0.2838 -0.0139 -0.0154 -0.0232 22  LEU A CA  
172  C C   . LEU A 21  ? 0.3249 0.2919 0.3073 -0.0120 -0.0211 -0.0218 22  LEU A C   
173  O O   . LEU A 21  ? 0.3036 0.2749 0.2897 -0.0097 -0.0257 -0.0250 22  LEU A O   
174  C CB  . LEU A 21  ? 0.2812 0.2655 0.2744 -0.0185 -0.0081 -0.0195 22  LEU A CB  
175  C CG  . LEU A 21  ? 0.3073 0.3027 0.3078 -0.0199 -0.0036 -0.0202 22  LEU A CG  
176  C CD1 . LEU A 21  ? 0.2982 0.2946 0.2959 -0.0217 0.0012  -0.0158 22  LEU A CD1 
177  C CD2 . LEU A 21  ? 0.3288 0.3330 0.3378 -0.0200 -0.0031 -0.0254 22  LEU A CD2 
178  N N   . ASN A 22  ? 0.3032 0.2539 0.2704 -0.0141 -0.0207 -0.0176 23  ASN A N   
179  C CA  . ASN A 22  ? 0.3186 0.2528 0.2693 -0.0130 -0.0261 -0.0156 23  ASN A CA  
180  C C   . ASN A 22  ? 0.3752 0.3025 0.3235 -0.0041 -0.0379 -0.0183 23  ASN A C   
181  O O   . ASN A 22  ? 0.3803 0.3033 0.3220 -0.0005 -0.0456 -0.0190 23  ASN A O   
182  C CB  . ASN A 22  ? 0.3406 0.2567 0.2729 -0.0192 -0.0212 -0.0114 23  ASN A CB  
183  C CG  . ASN A 22  ? 0.4461 0.3449 0.3581 -0.0209 -0.0240 -0.0088 23  ASN A CG  
184  O OD1 . ASN A 22  ? 0.4242 0.3293 0.3384 -0.0205 -0.0258 -0.0099 23  ASN A OD1 
185  N ND2 . ASN A 22  ? 0.4723 0.3474 0.3622 -0.0239 -0.0239 -0.0058 23  ASN A ND2 
186  N N   . ARG A 23  ? 0.3399 0.2672 0.2944 0.0004  -0.0399 -0.0208 24  ARG A N   
187  C CA  . ARG A 23  ? 0.3514 0.2740 0.3075 0.0113  -0.0515 -0.0248 24  ARG A CA  
188  C C   . ARG A 23  ? 0.3819 0.3286 0.3589 0.0156  -0.0560 -0.0325 24  ARG A C   
189  O O   . ARG A 23  ? 0.3800 0.3252 0.3560 0.0237  -0.0674 -0.0358 24  ARG A O   
190  C CB  . ARG A 23  ? 0.3481 0.2679 0.3096 0.0143  -0.0503 -0.0275 24  ARG A CB  
191  C CG  . ARG A 23  ? 0.4475 0.3385 0.3855 0.0113  -0.0483 -0.0217 24  ARG A CG  
192  C CD  . ARG A 23  ? 0.4867 0.3790 0.4322 0.0102  -0.0431 -0.0250 24  ARG A CD  
193  N NE  . ARG A 23  ? 0.5798 0.4427 0.5023 0.0063  -0.0404 -0.0210 24  ARG A NE  
194  C CZ  . ARG A 23  ? 0.8424 0.7007 0.7656 0.0027  -0.0346 -0.0236 24  ARG A CZ  
195  N NH1 . ARG A 23  ? 0.6457 0.5278 0.5908 0.0026  -0.0310 -0.0296 24  ARG A NH1 
196  N NH2 . ARG A 23  ? 0.7195 0.5483 0.6198 -0.0022 -0.0314 -0.0206 24  ARG A NH2 
197  N N   . LEU A 24  ? 0.3289 0.2968 0.3231 0.0093  -0.0469 -0.0357 25  LEU A N   
198  C CA  . LEU A 24  ? 0.3006 0.2904 0.3132 0.0100  -0.0482 -0.0439 25  LEU A CA  
199  C C   . LEU A 24  ? 0.3633 0.3510 0.3681 0.0081  -0.0517 -0.0428 25  LEU A C   
200  O O   . LEU A 24  ? 0.3681 0.3667 0.3818 0.0128  -0.0601 -0.0503 25  LEU A O   
201  C CB  . LEU A 24  ? 0.2810 0.2866 0.3060 0.0018  -0.0362 -0.0459 25  LEU A CB  
202  C CG  . LEU A 24  ? 0.3288 0.3401 0.3623 0.0020  -0.0317 -0.0488 25  LEU A CG  
203  C CD1 . LEU A 24  ? 0.3213 0.3446 0.3609 -0.0068 -0.0203 -0.0495 25  LEU A CD1 
204  C CD2 . LEU A 24  ? 0.3417 0.3631 0.3907 0.0105  -0.0388 -0.0594 25  LEU A CD2 
205  N N   . ARG A 25  ? 0.3261 0.3012 0.3151 0.0013  -0.0457 -0.0348 26  ARG A N   
206  C CA  . ARG A 25  ? 0.3378 0.3085 0.3168 -0.0013 -0.0482 -0.0340 26  ARG A CA  
207  C C   . ARG A 25  ? 0.4160 0.3743 0.3814 0.0070  -0.0627 -0.0345 26  ARG A C   
208  O O   . ARG A 25  ? 0.4109 0.3779 0.3796 0.0089  -0.0700 -0.0401 26  ARG A O   
209  C CB  . ARG A 25  ? 0.3631 0.3210 0.3273 -0.0091 -0.0388 -0.0264 26  ARG A CB  
210  C CG  . ARG A 25  ? 0.4234 0.3768 0.3771 -0.0127 -0.0401 -0.0268 26  ARG A CG  
211  C CD  . ARG A 25  ? 0.4524 0.3962 0.3954 -0.0202 -0.0296 -0.0216 26  ARG A CD  
212  N NE  . ARG A 25  ? 0.4623 0.3881 0.3881 -0.0213 -0.0284 -0.0160 26  ARG A NE  
213  C CZ  . ARG A 25  ? 0.6452 0.5541 0.5499 -0.0258 -0.0271 -0.0133 26  ARG A CZ  
214  N NH1 . ARG A 25  ? 0.5766 0.4841 0.4742 -0.0282 -0.0287 -0.0155 26  ARG A NH1 
215  N NH2 . ARG A 25  ? 0.4527 0.3452 0.3420 -0.0290 -0.0236 -0.0094 26  ARG A NH2 
216  N N   A SER A 26  ? 0.4033 0.3400 0.3517 0.0114  -0.0669 -0.0289 27  SER A N   
217  N N   B SER A 26  ? 0.4014 0.3380 0.3498 0.0114  -0.0670 -0.0289 27  SER A N   
218  N N   C SER A 26  ? 0.3989 0.3356 0.3474 0.0115  -0.0670 -0.0289 27  SER A N   
219  C CA  A SER A 26  ? 0.4386 0.3557 0.3675 0.0204  -0.0813 -0.0273 27  SER A CA  
220  C CA  B SER A 26  ? 0.4354 0.3524 0.3640 0.0203  -0.0813 -0.0272 27  SER A CA  
221  C CA  C SER A 26  ? 0.4316 0.3482 0.3601 0.0204  -0.0813 -0.0271 27  SER A CA  
222  C C   A SER A 26  ? 0.4959 0.4304 0.4430 0.0324  -0.0951 -0.0370 27  SER A C   
223  C C   B SER A 26  ? 0.4963 0.4290 0.4422 0.0330  -0.0956 -0.0366 27  SER A C   
224  C C   C SER A 26  ? 0.4932 0.4255 0.4388 0.0330  -0.0956 -0.0365 27  SER A C   
225  O O   A SER A 26  ? 0.5128 0.4444 0.4511 0.0385  -0.1079 -0.0392 27  SER A O   
226  O O   B SER A 26  ? 0.5159 0.4420 0.4506 0.0405  -0.1095 -0.0380 27  SER A O   
227  O O   C SER A 26  ? 0.5118 0.4367 0.4456 0.0407  -0.1096 -0.0376 27  SER A O   
228  C CB  A SER A 26  ? 0.5006 0.3913 0.4114 0.0229  -0.0814 -0.0209 27  SER A CB  
229  C CB  B SER A 26  ? 0.4961 0.3838 0.4024 0.0213  -0.0806 -0.0197 27  SER A CB  
230  C CB  C SER A 26  ? 0.4903 0.3787 0.3979 0.0215  -0.0803 -0.0199 27  SER A CB  
231  O OG  A SER A 26  ? 0.6092 0.4806 0.4984 0.0121  -0.0711 -0.0132 27  SER A OG  
232  O OG  B SER A 26  ? 0.5721 0.4649 0.4931 0.0265  -0.0801 -0.0227 27  SER A OG  
233  O OG  C SER A 26  ? 0.6099 0.4722 0.4923 0.0302  -0.0941 -0.0167 27  SER A OG  
234  N N   . ARG A 27  ? 0.4323 0.3868 0.4056 0.0353  -0.0922 -0.0441 28  ARG A N   
235  C CA  . ARG A 27  ? 0.4382 0.4137 0.4345 0.0466  -0.1034 -0.0561 28  ARG A CA  
236  C C   . ARG A 27  ? 0.4570 0.4647 0.4778 0.0406  -0.0997 -0.0668 28  ARG A C   
237  O O   . ARG A 27  ? 0.4450 0.4764 0.4894 0.0476  -0.1070 -0.0796 28  ARG A O   
238  C CB  . ARG A 27  ? 0.4599 0.4382 0.4699 0.0520  -0.1010 -0.0595 28  ARG A CB  
239  C CG  . ARG A 27  ? 0.5961 0.5396 0.5801 0.0572  -0.1044 -0.0499 28  ARG A CG  
240  C CD  . ARG A 27  ? 0.6744 0.6195 0.6708 0.0601  -0.0995 -0.0534 28  ARG A CD  
241  N NE  . ARG A 27  ? 0.8983 0.8593 0.9170 0.0745  -0.1107 -0.0657 28  ARG A NE  
242  C CZ  . ARG A 27  ? 1.1112 1.0935 1.1560 0.0751  -0.1046 -0.0758 28  ARG A CZ  
243  N NH1 . ARG A 27  ? 0.9926 0.9911 1.0596 0.0888  -0.1149 -0.0887 28  ARG A NH1 
244  N NH2 . ARG A 27  ? 0.9362 0.9247 0.9852 0.0623  -0.0886 -0.0738 28  ARG A NH2 
245  N N   . ASP A 28  ? 0.3863 0.3942 0.4010 0.0275  -0.0882 -0.0625 29  ASP A N   
246  C CA  . ASP A 28  ? 0.3843 0.4161 0.4165 0.0188  -0.0817 -0.0712 29  ASP A CA  
247  C C   . ASP A 28  ? 0.4155 0.4713 0.4751 0.0154  -0.0726 -0.0809 29  ASP A C   
248  O O   . ASP A 28  ? 0.4120 0.4926 0.4925 0.0128  -0.0723 -0.0939 29  ASP A O   
249  C CB  . ASP A 28  ? 0.4213 0.4639 0.4559 0.0236  -0.0956 -0.0797 29  ASP A CB  
250  C CG  . ASP A 28  ? 0.5148 0.5738 0.5585 0.0113  -0.0871 -0.0865 29  ASP A CG  
251  O OD1 . ASP A 28  ? 0.5139 0.5627 0.5482 0.0002  -0.0729 -0.0792 29  ASP A OD1 
252  O OD2 . ASP A 28  ? 0.5602 0.6423 0.6211 0.0130  -0.0947 -0.0999 29  ASP A OD2 
253  N N   . ILE A 29  ? 0.3437 0.3923 0.4023 0.0145  -0.0647 -0.0756 30  ILE A N   
254  C CA  . ILE A 29  ? 0.3164 0.3838 0.3958 0.0105  -0.0554 -0.0839 30  ILE A CA  
255  C C   . ILE A 29  ? 0.3517 0.4193 0.4279 -0.0033 -0.0393 -0.0800 30  ILE A C   
256  O O   . ILE A 29  ? 0.3230 0.3727 0.3820 -0.0068 -0.0337 -0.0680 30  ILE A O   
257  C CB  . ILE A 29  ? 0.3553 0.4162 0.4360 0.0178  -0.0567 -0.0826 30  ILE A CB  
258  C CG1 . ILE A 29  ? 0.3758 0.4357 0.4612 0.0337  -0.0736 -0.0882 30  ILE A CG1 
259  C CG2 . ILE A 29  ? 0.3425 0.4214 0.4413 0.0113  -0.0448 -0.0908 30  ILE A CG2 
260  C CD1 . ILE A 29  ? 0.4267 0.4687 0.5043 0.0412  -0.0754 -0.0835 30  ILE A CD1 
261  N N   A LEU A 30  ? 0.3090 0.3963 0.4015 -0.0113 -0.0317 -0.0909 31  LEU A N   
262  N N   B LEU A 30  ? 0.3157 0.4031 0.4083 -0.0113 -0.0318 -0.0909 31  LEU A N   
263  C CA  A LEU A 30  ? 0.3037 0.3890 0.3918 -0.0246 -0.0161 -0.0886 31  LEU A CA  
264  C CA  B LEU A 30  ? 0.3140 0.3998 0.4025 -0.0246 -0.0162 -0.0889 31  LEU A CA  
265  C C   A LEU A 30  ? 0.3449 0.4132 0.4146 -0.0297 -0.0128 -0.0787 31  LEU A C   
266  C C   B LEU A 30  ? 0.3507 0.4191 0.4206 -0.0297 -0.0128 -0.0787 31  LEU A C   
267  O O   A LEU A 30  ? 0.3206 0.3793 0.3810 -0.0374 -0.0015 -0.0728 31  LEU A O   
268  O O   B LEU A 30  ? 0.3296 0.3884 0.3901 -0.0374 -0.0015 -0.0728 31  LEU A O   
269  C CB  A LEU A 30  ? 0.3065 0.3860 0.3903 -0.0269 -0.0074 -0.0835 31  LEU A CB  
270  C CB  B LEU A 30  ? 0.3191 0.4000 0.4042 -0.0272 -0.0073 -0.0844 31  LEU A CB  
271  C CG  A LEU A 30  ? 0.3675 0.4650 0.4697 -0.0267 -0.0046 -0.0955 31  LEU A CG  
272  C CG  B LEU A 30  ? 0.3864 0.4863 0.4885 -0.0336 0.0013  -0.0976 31  LEU A CG  
273  C CD1 A LEU A 30  ? 0.3593 0.4506 0.4528 -0.0348 0.0079  -0.0913 31  LEU A CD1 
274  C CD1 B LEU A 30  ? 0.3871 0.4950 0.5007 -0.0253 -0.0034 -0.1029 31  LEU A CD1 
275  C CD2 A LEU A 30  ? 0.3996 0.5215 0.5234 -0.0319 -0.0021 -0.1126 31  LEU A CD2 
276  C CD2 B LEU A 30  ? 0.4218 0.5127 0.5115 -0.0459 0.0164  -0.0930 31  LEU A CD2 
277  N N   . THR A 31  ? 0.3112 0.3752 0.3751 -0.0252 -0.0227 -0.0776 32  THR A N   
278  C CA  . THR A 31  ? 0.3176 0.3674 0.3658 -0.0305 -0.0190 -0.0708 32  THR A CA  
279  C C   . THR A 31  ? 0.3879 0.4487 0.4451 -0.0416 -0.0098 -0.0805 32  THR A C   
280  O O   . THR A 31  ? 0.3716 0.4536 0.4471 -0.0430 -0.0121 -0.0939 32  THR A O   
281  C CB  . THR A 31  ? 0.4082 0.4504 0.4459 -0.0243 -0.0313 -0.0687 32  THR A CB  
282  O OG1 . THR A 31  ? 0.3928 0.4535 0.4450 -0.0196 -0.0421 -0.0808 32  THR A OG1 
283  C CG2 . THR A 31  ? 0.3848 0.4096 0.4079 -0.0164 -0.0371 -0.0582 32  THR A CG2 
284  N N   . ASP A 32  ? 0.3495 0.3963 0.3950 -0.0496 0.0016  -0.0745 33  ASP A N   
285  C CA  . ASP A 32  ? 0.3480 0.3988 0.3975 -0.0618 0.0131  -0.0825 33  ASP A CA  
286  C C   . ASP A 32  ? 0.3728 0.4106 0.4104 -0.0677 0.0173  -0.0807 33  ASP A C   
287  O O   . ASP A 32  ? 0.3779 0.4115 0.4136 -0.0787 0.0289  -0.0852 33  ASP A O   
288  C CB  . ASP A 32  ? 0.3650 0.4077 0.4096 -0.0671 0.0255  -0.0782 33  ASP A CB  
289  C CG  . ASP A 32  ? 0.5049 0.5264 0.5322 -0.0619 0.0271  -0.0627 33  ASP A CG  
290  O OD1 . ASP A 32  ? 0.4638 0.4755 0.4828 -0.0566 0.0220  -0.0559 33  ASP A OD1 
291  O OD2 . ASP A 32  ? 0.6111 0.6268 0.6332 -0.0634 0.0334  -0.0585 33  ASP A OD2 
292  N N   . VAL A 33  ? 0.3172 0.3464 0.3450 -0.0613 0.0090  -0.0746 34  VAL A N   
293  C CA  . VAL A 33  ? 0.3194 0.3368 0.3360 -0.0669 0.0130  -0.0743 34  VAL A CA  
294  C C   . VAL A 33  ? 0.3668 0.3834 0.3764 -0.0611 0.0009  -0.0735 34  VAL A C   
295  O O   . VAL A 33  ? 0.3653 0.3800 0.3713 -0.0519 -0.0084 -0.0676 34  VAL A O   
296  C CB  . VAL A 33  ? 0.3637 0.3578 0.3658 -0.0685 0.0244  -0.0635 34  VAL A CB  
297  C CG1 . VAL A 33  ? 0.3470 0.3310 0.3402 -0.0590 0.0197  -0.0521 34  VAL A CG1 
298  C CG2 . VAL A 33  ? 0.3736 0.3556 0.3671 -0.0768 0.0326  -0.0667 34  VAL A CG2 
299  N N   A VAL A 34  ? 0.3366 0.3518 0.3413 -0.0675 0.0017  -0.0795 35  VAL A N   
300  N N   B VAL A 34  ? 0.3382 0.3537 0.3430 -0.0674 0.0015  -0.0795 35  VAL A N   
301  C CA  A VAL A 34  ? 0.3369 0.3471 0.3290 -0.0645 -0.0079 -0.0786 35  VAL A CA  
302  C CA  B VAL A 34  ? 0.3403 0.3502 0.3323 -0.0639 -0.0082 -0.0781 35  VAL A CA  
303  C C   A VAL A 34  ? 0.3894 0.3789 0.3661 -0.0698 0.0030  -0.0732 35  VAL A C   
304  C C   B VAL A 34  ? 0.3941 0.3843 0.3707 -0.0698 0.0023  -0.0737 35  VAL A C   
305  O O   A VAL A 34  ? 0.3897 0.3752 0.3679 -0.0785 0.0143  -0.0775 35  VAL A O   
306  O O   B VAL A 34  ? 0.3969 0.3840 0.3751 -0.0788 0.0130  -0.0787 35  VAL A O   
307  C CB  A VAL A 34  ? 0.3850 0.4136 0.3845 -0.0672 -0.0177 -0.0923 35  VAL A CB  
308  C CB  B VAL A 34  ? 0.3908 0.4193 0.3895 -0.0634 -0.0216 -0.0902 35  VAL A CB  
309  C CG1 A VAL A 34  ? 0.3936 0.4130 0.3742 -0.0649 -0.0276 -0.0907 35  VAL A CG1 
310  C CG1 B VAL A 34  ? 0.3951 0.4344 0.4021 -0.0756 -0.0146 -0.1034 35  VAL A CG1 
311  C CG2 A VAL A 34  ? 0.3776 0.4290 0.3960 -0.0601 -0.0288 -0.0995 35  VAL A CG2 
312  C CG2 B VAL A 34  ? 0.4023 0.4200 0.3813 -0.0578 -0.0336 -0.0858 35  VAL A CG2 
313  N N   . ILE A 35  ? 0.3519 0.3276 0.3138 -0.0651 0.0005  -0.0647 36  ILE A N   
314  C CA  . ILE A 35  ? 0.3563 0.3147 0.3052 -0.0691 0.0102  -0.0614 36  ILE A CA  
315  C C   . ILE A 35  ? 0.4245 0.3808 0.3597 -0.0723 0.0033  -0.0664 36  ILE A C   
316  O O   . ILE A 35  ? 0.4150 0.3705 0.3405 -0.0671 -0.0080 -0.0636 36  ILE A O   
317  C CB  . ILE A 35  ? 0.3799 0.3265 0.3230 -0.0633 0.0142  -0.0508 36  ILE A CB  
318  C CG1 . ILE A 35  ? 0.3676 0.3179 0.3226 -0.0588 0.0177  -0.0457 36  ILE A CG1 
319  C CG2 . ILE A 35  ? 0.4053 0.3373 0.3390 -0.0669 0.0247  -0.0501 36  ILE A CG2 
320  C CD1 . ILE A 35  ? 0.3736 0.3216 0.3353 -0.0633 0.0281  -0.0480 36  ILE A CD1 
321  N N   . VAL A 36  ? 0.3844 0.3377 0.3165 -0.0811 0.0102  -0.0738 37  VAL A N   
322  C CA  . VAL A 36  ? 0.3953 0.3470 0.3130 -0.0858 0.0044  -0.0800 37  VAL A CA  
323  C C   . VAL A 36  ? 0.4602 0.3921 0.3612 -0.0888 0.0141  -0.0760 37  VAL A C   
324  O O   . VAL A 36  ? 0.4464 0.3692 0.3509 -0.0922 0.0279  -0.0762 37  VAL A O   
325  C CB  . VAL A 36  ? 0.4469 0.4110 0.3728 -0.0952 0.0052  -0.0936 37  VAL A CB  
326  C CG1 . VAL A 36  ? 0.4648 0.4278 0.3742 -0.1004 -0.0017 -0.1007 37  VAL A CG1 
327  C CG2 . VAL A 36  ? 0.4402 0.4277 0.3861 -0.0927 -0.0035 -0.0999 37  VAL A CG2 
328  N N   . VAL A 37  ? 0.4385 0.3624 0.3203 -0.0873 0.0071  -0.0729 38  VAL A N   
329  C CA  . VAL A 37  ? 0.4531 0.3597 0.3180 -0.0912 0.0166  -0.0706 38  VAL A CA  
330  C C   . VAL A 37  ? 0.5443 0.4463 0.3868 -0.0972 0.0090  -0.0763 38  VAL A C   
331  O O   . VAL A 37  ? 0.5318 0.4311 0.3588 -0.0934 -0.0040 -0.0727 38  VAL A O   
332  C CB  . VAL A 37  ? 0.4999 0.3990 0.3608 -0.0851 0.0179  -0.0607 38  VAL A CB  
333  C CG1 . VAL A 37  ? 0.5086 0.3939 0.3585 -0.0900 0.0310  -0.0609 38  VAL A CG1 
334  C CG2 . VAL A 37  ? 0.4741 0.3817 0.3569 -0.0780 0.0203  -0.0554 38  VAL A CG2 
335  N N   A SER A 38  ? 0.5368 0.4330 0.3722 -0.1065 0.0180  -0.0843 39  SER A N   
336  N N   B SER A 38  ? 0.5085 0.4130 0.3527 -0.1056 0.0145  -0.0863 39  SER A N   
337  C CA  A SER A 38  ? 0.5703 0.4611 0.3812 -0.1136 0.0116  -0.0905 39  SER A CA  
338  C CA  B SER A 38  ? 0.5225 0.4273 0.3504 -0.1133 0.0085  -0.0955 39  SER A CA  
339  C C   A SER A 38  ? 0.6260 0.5288 0.4316 -0.1088 -0.0099 -0.0921 39  SER A C   
340  C C   B SER A 38  ? 0.5492 0.4699 0.3776 -0.1082 -0.0122 -0.0981 39  SER A C   
341  O O   A SER A 38  ? 0.6347 0.5272 0.4145 -0.1072 -0.0208 -0.0886 39  SER A O   
342  O O   B SER A 38  ? 0.5126 0.4519 0.3642 -0.1064 -0.0153 -0.1030 39  SER A O   
343  C CB  A SER A 38  ? 0.6532 0.5242 0.4387 -0.1167 0.0177  -0.0860 39  SER A CB  
344  C CB  B SER A 38  ? 0.5981 0.4835 0.3981 -0.1188 0.0140  -0.0943 39  SER A CB  
345  O OG  A SER A 38  ? 0.7801 0.6428 0.5712 -0.1210 0.0368  -0.0880 39  SER A OG  
346  O OG  B SER A 38  ? 0.6839 0.5603 0.4899 -0.1241 0.0331  -0.0972 39  SER A OG  
347  N N   A ARG A 39  ? 0.5704 0.4941 0.4006 -0.1060 -0.0159 -0.0975 40  ARG A N   
348  N N   B ARG A 39  ? 0.5280 0.4411 0.3313 -0.1052 -0.0261 -0.0951 40  ARG A N   
349  C CA  A ARG A 39  ? 0.5743 0.5162 0.4096 -0.0996 -0.0360 -0.1018 40  ARG A CA  
350  C CA  B ARG A 39  ? 0.5385 0.4663 0.3427 -0.0974 -0.0479 -0.0979 40  ARG A CA  
351  C C   A ARG A 39  ? 0.6223 0.5600 0.4517 -0.0865 -0.0493 -0.0909 40  ARG A C   
352  C C   B ARG A 39  ? 0.6029 0.5376 0.4236 -0.0846 -0.0552 -0.0899 40  ARG A C   
353  O O   A ARG A 39  ? 0.6513 0.5959 0.4742 -0.0792 -0.0687 -0.0929 40  ARG A O   
354  O O   B ARG A 39  ? 0.6165 0.5734 0.4584 -0.0788 -0.0660 -0.0960 40  ARG A O   
355  C CB  A ARG A 39  ? 0.6020 0.5479 0.4197 -0.1053 -0.0474 -0.1121 40  ARG A CB  
356  C CB  B ARG A 39  ? 0.5531 0.4670 0.3207 -0.0974 -0.0623 -0.0974 40  ARG A CB  
357  C CG  A ARG A 39  ? 0.7360 0.6930 0.5654 -0.1180 -0.0378 -0.1264 40  ARG A CG  
358  C CG  B ARG A 39  ? 0.6666 0.5817 0.4213 -0.1097 -0.0599 -0.1092 40  ARG A CG  
359  C CD  A ARG A 39  ? 0.8149 0.7854 0.6340 -0.1212 -0.0543 -0.1385 40  ARG A CD  
360  C CD  B ARG A 39  ? 0.6573 0.5607 0.3745 -0.1088 -0.0777 -0.1094 40  ARG A CD  
361  N NE  A ARG A 39  ? 0.9015 0.8787 0.7260 -0.1360 -0.0435 -0.1530 40  ARG A NE  
362  N NE  B ARG A 39  ? 0.7087 0.6125 0.4117 -0.1218 -0.0744 -0.1212 40  ARG A NE  
363  C CZ  A ARG A 39  ? 1.0762 1.0361 0.8781 -0.1466 -0.0340 -0.1561 40  ARG A CZ  
364  C CZ  B ARG A 39  ? 0.8868 0.8141 0.6007 -0.1244 -0.0854 -0.1353 40  ARG A CZ  
365  N NH1 A ARG A 39  ? 0.8987 0.8344 0.6711 -0.1448 -0.0331 -0.1460 40  ARG A NH1 
366  N NH1 B ARG A 39  ? 0.7346 0.6891 0.4761 -0.1148 -0.1000 -0.1402 40  ARG A NH1 
367  N NH2 A ARG A 39  ? 0.9138 0.8797 0.7219 -0.1603 -0.0240 -0.1703 40  ARG A NH2 
368  N NH2 B ARG A 39  ? 0.7635 0.6890 0.4621 -0.1375 -0.0811 -0.1461 40  ARG A NH2 
369  N N   A GLU A 40  ? 0.5341 0.4601 0.3658 -0.0831 -0.0395 -0.0803 41  GLU A N   
370  N N   B GLU A 40  ? 0.5293 0.4472 0.3434 -0.0814 -0.0473 -0.0781 41  GLU A N   
371  C CA  A GLU A 40  ? 0.5216 0.4426 0.3505 -0.0722 -0.0486 -0.0705 41  GLU A CA  
372  C CA  B GLU A 40  ? 0.5059 0.4265 0.3315 -0.0704 -0.0531 -0.0702 41  GLU A CA  
373  C C   A GLU A 40  ? 0.5094 0.4460 0.3701 -0.0683 -0.0423 -0.0700 41  GLU A C   
374  C C   B GLU A 40  ? 0.5013 0.4405 0.3614 -0.0687 -0.0450 -0.0723 41  GLU A C   
375  O O   A GLU A 40  ? 0.4695 0.4060 0.3421 -0.0737 -0.0265 -0.0701 41  GLU A O   
376  O O   B GLU A 40  ? 0.4642 0.4056 0.3358 -0.0761 -0.0300 -0.0755 41  GLU A O   
377  C CB  A GLU A 40  ? 0.5557 0.4509 0.3598 -0.0739 -0.0412 -0.0603 41  GLU A CB  
378  C CB  B GLU A 40  ? 0.5352 0.4316 0.3402 -0.0695 -0.0470 -0.0584 41  GLU A CB  
379  C CG  A GLU A 40  ? 0.7616 0.6376 0.5286 -0.0786 -0.0474 -0.0603 41  GLU A CG  
380  C CG  B GLU A 40  ? 0.7582 0.6315 0.5254 -0.0757 -0.0483 -0.0567 41  GLU A CG  
381  C CD  A GLU A 40  ? 1.2223 1.0784 0.9616 -0.0717 -0.0603 -0.0513 41  GLU A CD  
382  C CD  B GLU A 40  ? 1.2439 1.0975 0.9804 -0.0692 -0.0637 -0.0494 41  GLU A CD  
383  O OE1 A GLU A 40  ? 1.2716 1.1037 0.9844 -0.0777 -0.0519 -0.0453 41  GLU A OE1 
384  O OE1 B GLU A 40  ? 1.2825 1.1449 1.0241 -0.0581 -0.0819 -0.0500 41  GLU A OE1 
385  O OE2 A GLU A 40  ? 1.2346 1.0982 0.9781 -0.0605 -0.0783 -0.0510 41  GLU A OE2 
386  O OE2 B GLU A 40  ? 1.2787 1.1068 0.9846 -0.0753 -0.0572 -0.0437 41  GLU A OE2 
387  N N   . GLN A 41  ? 0.4530 0.4027 0.3269 -0.0586 -0.0549 -0.0702 42  GLN A N   
388  C CA  . GLN A 41  ? 0.4261 0.3924 0.3291 -0.0562 -0.0494 -0.0718 42  GLN A CA  
389  C C   . GLN A 41  ? 0.4721 0.4310 0.3762 -0.0480 -0.0500 -0.0616 42  GLN A C   
390  O O   . GLN A 41  ? 0.4879 0.4376 0.3777 -0.0402 -0.0623 -0.0571 42  GLN A O   
391  C CB  . GLN A 41  ? 0.4442 0.4365 0.3671 -0.0532 -0.0613 -0.0838 42  GLN A CB  
392  C CG  . GLN A 41  ? 0.6124 0.6164 0.5397 -0.0639 -0.0582 -0.0964 42  GLN A CG  
393  C CD  . GLN A 41  ? 0.8421 0.8765 0.7942 -0.0630 -0.0672 -0.1111 42  GLN A CD  
394  O OE1 . GLN A 41  ? 0.7344 0.7841 0.7059 -0.0551 -0.0730 -0.1130 42  GLN A OE1 
395  N NE2 . GLN A 41  ? 0.8851 0.9307 0.8385 -0.0721 -0.0678 -0.1235 42  GLN A NE2 
396  N N   . PHE A 42  ? 0.3793 0.3404 0.2983 -0.0496 -0.0371 -0.0582 43  PHE A N   
397  C CA  . PHE A 42  ? 0.3817 0.3377 0.3033 -0.0431 -0.0363 -0.0497 43  PHE A CA  
398  C C   . PHE A 42  ? 0.4150 0.3880 0.3615 -0.0415 -0.0325 -0.0528 43  PHE A C   
399  O O   . PHE A 42  ? 0.4120 0.3883 0.3677 -0.0477 -0.0207 -0.0546 43  PHE A O   
400  C CB  . PHE A 42  ? 0.4058 0.3456 0.3168 -0.0470 -0.0236 -0.0419 43  PHE A CB  
401  C CG  . PHE A 42  ? 0.4488 0.3707 0.3339 -0.0512 -0.0236 -0.0399 43  PHE A CG  
402  C CD1 . PHE A 42  ? 0.4844 0.4033 0.3629 -0.0591 -0.0169 -0.0449 43  PHE A CD1 
403  C CD2 . PHE A 42  ? 0.4941 0.3999 0.3591 -0.0485 -0.0289 -0.0336 43  PHE A CD2 
404  C CE1 . PHE A 42  ? 0.5247 0.4268 0.3775 -0.0643 -0.0160 -0.0440 43  PHE A CE1 
405  C CE2 . PHE A 42  ? 0.5471 0.4338 0.3843 -0.0544 -0.0275 -0.0321 43  PHE A CE2 
406  C CZ  . PHE A 42  ? 0.5214 0.4074 0.3530 -0.0623 -0.0210 -0.0375 43  PHE A CZ  
407  N N   . ARG A 43  ? 0.3648 0.3463 0.3205 -0.0333 -0.0419 -0.0533 44  ARG A N   
408  C CA  . ARG A 43  ? 0.3437 0.3414 0.3220 -0.0327 -0.0375 -0.0571 44  ARG A CA  
409  C C   . ARG A 43  ? 0.3905 0.3786 0.3672 -0.0314 -0.0294 -0.0477 44  ARG A C   
410  O O   . ARG A 43  ? 0.3852 0.3595 0.3484 -0.0275 -0.0323 -0.0404 44  ARG A O   
411  C CB  . ARG A 43  ? 0.3563 0.3703 0.3484 -0.0243 -0.0508 -0.0647 44  ARG A CB  
412  C CG  . ARG A 43  ? 0.4617 0.4919 0.4605 -0.0249 -0.0605 -0.0769 44  ARG A CG  
413  C CD  . ARG A 43  ? 0.5844 0.6412 0.6094 -0.0196 -0.0677 -0.0893 44  ARG A CD  
414  N NE  . ARG A 43  ? 0.7327 0.7989 0.7747 -0.0259 -0.0534 -0.0914 44  ARG A NE  
415  C CZ  . ARG A 43  ? 0.8742 0.9553 0.9307 -0.0368 -0.0428 -0.1012 44  ARG A CZ  
416  N NH1 . ARG A 43  ? 0.7706 0.8637 0.8316 -0.0427 -0.0453 -0.1119 44  ARG A NH1 
417  N NH2 . ARG A 43  ? 0.6366 0.7202 0.7019 -0.0427 -0.0296 -0.1012 44  ARG A NH2 
418  N N   . ALA A 44  ? 0.3311 0.3254 0.3194 -0.0353 -0.0189 -0.0481 45  ALA A N   
419  C CA  . ALA A 44  ? 0.3313 0.3186 0.3182 -0.0337 -0.0124 -0.0400 45  ALA A CA  
420  C C   . ALA A 44  ? 0.3416 0.3390 0.3418 -0.0360 -0.0056 -0.0425 45  ALA A C   
421  O O   . ALA A 44  ? 0.3210 0.3302 0.3318 -0.0401 -0.0043 -0.0511 45  ALA A O   
422  C CB  . ALA A 44  ? 0.3515 0.3250 0.3268 -0.0370 -0.0042 -0.0339 45  ALA A CB  
423  N N   . HIS A 45  ? 0.2961 0.2889 0.2948 -0.0343 -0.0009 -0.0359 46  HIS A N   
424  C CA  . HIS A 45  ? 0.2822 0.2796 0.2872 -0.0369 0.0062  -0.0364 46  HIS A CA  
425  C C   . HIS A 45  ? 0.3395 0.3245 0.3356 -0.0401 0.0152  -0.0310 46  HIS A C   
426  O O   . HIS A 45  ? 0.3331 0.3097 0.3224 -0.0367 0.0155  -0.0246 46  HIS A O   
427  C CB  . HIS A 45  ? 0.2725 0.2726 0.2798 -0.0322 0.0040  -0.0330 46  HIS A CB  
428  C CG  . HIS A 45  ? 0.3114 0.3194 0.3258 -0.0272 -0.0052 -0.0377 46  HIS A CG  
429  N ND1 . HIS A 45  ? 0.3386 0.3383 0.3453 -0.0220 -0.0124 -0.0339 46  HIS A ND1 
430  C CD2 . HIS A 45  ? 0.3112 0.3333 0.3391 -0.0265 -0.0079 -0.0467 46  HIS A CD2 
431  C CE1 . HIS A 45  ? 0.3256 0.3319 0.3396 -0.0168 -0.0204 -0.0394 46  HIS A CE1 
432  N NE2 . HIS A 45  ? 0.3104 0.3324 0.3395 -0.0187 -0.0182 -0.0478 46  HIS A NE2 
433  N N   . LYS A 46  ? 0.3182 0.3012 0.3143 -0.0465 0.0228  -0.0343 47  LYS A N   
434  C CA  . LYS A 46  ? 0.3200 0.2870 0.3056 -0.0483 0.0312  -0.0292 47  LYS A CA  
435  C C   . LYS A 46  ? 0.3574 0.3185 0.3377 -0.0417 0.0311  -0.0204 47  LYS A C   
436  O O   . LYS A 46  ? 0.3408 0.2918 0.3152 -0.0379 0.0326  -0.0156 47  LYS A O   
437  C CB  . LYS A 46  ? 0.3504 0.3132 0.3338 -0.0572 0.0404  -0.0336 47  LYS A CB  
438  C CG  . LYS A 46  ? 0.3498 0.3168 0.3375 -0.0653 0.0428  -0.0433 47  LYS A CG  
439  C CD  . LYS A 46  ? 0.3394 0.3022 0.3247 -0.0765 0.0539  -0.0492 47  LYS A CD  
440  C CE  . LYS A 46  ? 0.4002 0.3736 0.3942 -0.0856 0.0555  -0.0619 47  LYS A CE  
441  N NZ  . LYS A 46  ? 0.4425 0.4127 0.4347 -0.0994 0.0683  -0.0698 47  LYS A NZ  
442  N N   . THR A 47  ? 0.2992 0.2680 0.2827 -0.0402 0.0290  -0.0196 48  THR A N   
443  C CA  . THR A 47  ? 0.2996 0.2646 0.2778 -0.0344 0.0281  -0.0124 48  THR A CA  
444  C C   . THR A 47  ? 0.3087 0.2766 0.2896 -0.0283 0.0229  -0.0094 48  THR A C   
445  O O   . THR A 47  ? 0.3031 0.2665 0.2805 -0.0233 0.0232  -0.0048 48  THR A O   
446  C CB  . THR A 47  ? 0.3925 0.3648 0.3719 -0.0354 0.0276  -0.0131 48  THR A CB  
447  O OG1 . THR A 47  ? 0.3887 0.3745 0.3794 -0.0353 0.0224  -0.0186 48  THR A OG1 
448  C CG2 . THR A 47  ? 0.4234 0.3889 0.3954 -0.0429 0.0356  -0.0152 48  THR A CG2 
449  N N   . VAL A 48  ? 0.2716 0.2462 0.2578 -0.0286 0.0182  -0.0126 49  VAL A N   
450  C CA  . VAL A 48  ? 0.2773 0.2524 0.2634 -0.0254 0.0153  -0.0107 49  VAL A CA  
451  C C   . VAL A 48  ? 0.3124 0.2793 0.2945 -0.0254 0.0192  -0.0100 49  VAL A C   
452  O O   . VAL A 48  ? 0.2953 0.2622 0.2780 -0.0223 0.0205  -0.0083 49  VAL A O   
453  C CB  . VAL A 48  ? 0.3126 0.2906 0.2996 -0.0261 0.0095  -0.0135 49  VAL A CB  
454  C CG1 . VAL A 48  ? 0.3124 0.2861 0.2946 -0.0257 0.0090  -0.0119 49  VAL A CG1 
455  C CG2 . VAL A 48  ? 0.3030 0.2885 0.2952 -0.0248 0.0060  -0.0150 49  VAL A CG2 
456  N N   . LEU A 49  ? 0.2858 0.2473 0.2652 -0.0294 0.0214  -0.0131 50  LEU A N   
457  C CA  . LEU A 49  ? 0.2913 0.2436 0.2663 -0.0301 0.0263  -0.0136 50  LEU A CA  
458  C C   . LEU A 49  ? 0.3195 0.2651 0.2937 -0.0251 0.0308  -0.0099 50  LEU A C   
459  O O   . LEU A 49  ? 0.3080 0.2513 0.2832 -0.0214 0.0330  -0.0097 50  LEU A O   
460  C CB  . LEU A 49  ? 0.2936 0.2415 0.2657 -0.0362 0.0284  -0.0184 50  LEU A CB  
461  C CG  . LEU A 49  ? 0.3267 0.2810 0.2989 -0.0395 0.0219  -0.0231 50  LEU A CG  
462  C CD1 . LEU A 49  ? 0.3248 0.2778 0.2960 -0.0459 0.0242  -0.0296 50  LEU A CD1 
463  C CD2 . LEU A 49  ? 0.3571 0.3079 0.3224 -0.0387 0.0192  -0.0221 50  LEU A CD2 
464  N N   . MET A 50  ? 0.2899 0.2316 0.2612 -0.0247 0.0321  -0.0074 51  MET A N   
465  C CA  . MET A 50  ? 0.3088 0.2401 0.2749 -0.0183 0.0345  -0.0027 51  MET A CA  
466  C C   . MET A 50  ? 0.3553 0.2965 0.3272 -0.0103 0.0295  -0.0001 51  MET A C   
467  O O   . MET A 50  ? 0.3635 0.3007 0.3362 -0.0028 0.0298  0.0011  51  MET A O   
468  C CB  . MET A 50  ? 0.3393 0.2620 0.2963 -0.0211 0.0368  -0.0001 51  MET A CB  
469  C CG  . MET A 50  ? 0.3833 0.2958 0.3348 -0.0303 0.0437  -0.0042 51  MET A CG  
470  S SD  . MET A 50  ? 0.4464 0.3546 0.3892 -0.0371 0.0476  -0.0037 51  MET A SD  
471  C CE  . MET A 50  ? 0.4178 0.2980 0.3405 -0.0313 0.0516  0.0046  51  MET A CE  
472  N N   . ALA A 51  ? 0.3050 0.2597 0.2821 -0.0116 0.0249  -0.0006 52  ALA A N   
473  C CA  . ALA A 51  ? 0.3040 0.2706 0.2874 -0.0061 0.0205  0.0001  52  ALA A CA  
474  C C   . ALA A 51  ? 0.3355 0.3084 0.3269 -0.0046 0.0217  -0.0037 52  ALA A C   
475  O O   . ALA A 51  ? 0.3447 0.3278 0.3436 0.0009  0.0195  -0.0048 52  ALA A O   
476  C CB  . ALA A 51  ? 0.2981 0.2752 0.2841 -0.0098 0.0168  -0.0009 52  ALA A CB  
477  N N   . CYS A 52  ? 0.3028 0.2707 0.2926 -0.0101 0.0254  -0.0067 53  CYS A N   
478  C CA  . CYS A 52  ? 0.3042 0.2760 0.2983 -0.0118 0.0286  -0.0112 53  CYS A CA  
479  C C   . CYS A 52  ? 0.3476 0.3116 0.3418 -0.0095 0.0342  -0.0137 53  CYS A C   
480  O O   . CYS A 52  ? 0.3452 0.3147 0.3450 -0.0101 0.0381  -0.0187 53  CYS A O   
481  C CB  . CYS A 52  ? 0.3127 0.2825 0.3006 -0.0201 0.0283  -0.0129 53  CYS A CB  
482  S SG  . CYS A 52  ? 0.3519 0.3287 0.3399 -0.0221 0.0223  -0.0115 53  CYS A SG  
483  N N   . SER A 53  ? 0.3102 0.2607 0.2976 -0.0090 0.0361  -0.0116 54  SER A N   
484  C CA  . SER A 53  ? 0.2964 0.2361 0.2818 -0.0086 0.0425  -0.0147 54  SER A CA  
485  C C   . SER A 53  ? 0.3774 0.3027 0.3586 -0.0015 0.0439  -0.0115 54  SER A C   
486  O O   . SER A 53  ? 0.3579 0.2740 0.3304 -0.0039 0.0432  -0.0074 54  SER A O   
487  C CB  . SER A 53  ? 0.3204 0.2536 0.2972 -0.0187 0.0447  -0.0173 54  SER A CB  
488  O OG  . SER A 53  ? 0.3836 0.3027 0.3546 -0.0208 0.0506  -0.0197 54  SER A OG  
489  N N   . GLY A 54  ? 0.3628 0.2845 0.3491 0.0068  0.0468  -0.0139 55  GLY A N   
490  C CA  . GLY A 54  ? 0.3706 0.2729 0.3499 0.0151  0.0482  -0.0107 55  GLY A CA  
491  C C   . GLY A 54  ? 0.4155 0.2973 0.3817 0.0066  0.0551  -0.0111 55  GLY A C   
492  O O   . GLY A 54  ? 0.4216 0.2841 0.3753 0.0078  0.0564  -0.0064 55  GLY A O   
493  N N   . LEU A 55  ? 0.3816 0.2669 0.3486 -0.0035 0.0597  -0.0172 56  LEU A N   
494  C CA  . LEU A 55  ? 0.3843 0.2541 0.3406 -0.0132 0.0659  -0.0198 56  LEU A CA  
495  C C   . LEU A 55  ? 0.4025 0.2726 0.3523 -0.0209 0.0634  -0.0167 56  LEU A C   
496  O O   . LEU A 55  ? 0.4120 0.2646 0.3517 -0.0241 0.0681  -0.0156 56  LEU A O   
497  C CB  . LEU A 55  ? 0.3837 0.2588 0.3407 -0.0220 0.0696  -0.0274 56  LEU A CB  
498  C CG  . LEU A 55  ? 0.4502 0.3107 0.3970 -0.0321 0.0760  -0.0321 56  LEU A CG  
499  C CD1 . LEU A 55  ? 0.4831 0.3206 0.4250 -0.0273 0.0845  -0.0337 56  LEU A CD1 
500  C CD2 . LEU A 55  ? 0.4427 0.3115 0.3874 -0.0417 0.0763  -0.0388 56  LEU A CD2 
501  N N   . PHE A 56  ? 0.3473 0.2362 0.3029 -0.0239 0.0567  -0.0161 57  PHE A N   
502  C CA  . PHE A 56  ? 0.3427 0.2352 0.2956 -0.0305 0.0545  -0.0152 57  PHE A CA  
503  C C   . PHE A 56  ? 0.3979 0.2817 0.3450 -0.0261 0.0545  -0.0090 57  PHE A C   
504  O O   . PHE A 56  ? 0.4036 0.2805 0.3439 -0.0332 0.0580  -0.0095 57  PHE A O   
505  C CB  . PHE A 56  ? 0.3405 0.2525 0.3004 -0.0332 0.0473  -0.0166 57  PHE A CB  
506  C CG  . PHE A 56  ? 0.3513 0.2669 0.3103 -0.0397 0.0467  -0.0226 57  PHE A CG  
507  C CD1 . PHE A 56  ? 0.3838 0.2950 0.3390 -0.0480 0.0497  -0.0283 57  PHE A CD1 
508  C CD2 . PHE A 56  ? 0.3528 0.2758 0.3130 -0.0385 0.0430  -0.0230 57  PHE A CD2 
509  C CE1 . PHE A 56  ? 0.3902 0.3050 0.3424 -0.0534 0.0474  -0.0340 57  PHE A CE1 
510  C CE2 . PHE A 56  ? 0.3901 0.3132 0.3443 -0.0446 0.0415  -0.0277 57  PHE A CE2 
511  C CZ  . PHE A 56  ? 0.3662 0.2856 0.3164 -0.0513 0.0430  -0.0330 57  PHE A CZ  
512  N N   . TYR A 57  ? 0.3744 0.2585 0.3233 -0.0149 0.0509  -0.0040 58  TYR A N   
513  C CA  . TYR A 57  ? 0.3961 0.2686 0.3349 -0.0095 0.0497  0.0027  58  TYR A CA  
514  C C   . TYR A 57  ? 0.4636 0.3068 0.3859 -0.0117 0.0577  0.0042  58  TYR A C   
515  O O   . TYR A 57  ? 0.4427 0.2735 0.3518 -0.0175 0.0611  0.0068  58  TYR A O   
516  C CB  . TYR A 57  ? 0.4220 0.3011 0.3665 0.0043  0.0429  0.0064  58  TYR A CB  
517  C CG  . TYR A 57  ? 0.4844 0.3481 0.4146 0.0120  0.0400  0.0139  58  TYR A CG  
518  C CD1 . TYR A 57  ? 0.5068 0.3747 0.4304 0.0083  0.0369  0.0174  58  TYR A CD1 
519  C CD2 . TYR A 57  ? 0.5471 0.3906 0.4688 0.0237  0.0397  0.0173  58  TYR A CD2 
520  C CE1 . TYR A 57  ? 0.5486 0.3998 0.4544 0.0147  0.0341  0.0248  58  TYR A CE1 
521  C CE2 . TYR A 57  ? 0.5979 0.4234 0.5018 0.0319  0.0355  0.0253  58  TYR A CE2 
522  C CZ  . TYR A 57  ? 0.6942 0.5234 0.5890 0.0268  0.0327  0.0292  58  TYR A CZ  
523  O OH  . TYR A 57  ? 0.8064 0.6155 0.6795 0.0345  0.0283  0.0374  58  TYR A OH  
524  N N   A SER A 58  ? 0.4389 0.2698 0.3609 -0.0082 0.0621  0.0016  59  SER A N   
525  N N   B SER A 58  ? 0.4431 0.2742 0.3651 -0.0081 0.0620  0.0016  59  SER A N   
526  C CA  A SER A 58  ? 0.4671 0.2668 0.3726 -0.0103 0.0708  0.0021  59  SER A CA  
527  C CA  B SER A 58  ? 0.4735 0.2735 0.3793 -0.0102 0.0707  0.0020  59  SER A CA  
528  C C   A SER A 58  ? 0.5348 0.3301 0.4343 -0.0278 0.0789  -0.0035 59  SER A C   
529  C C   B SER A 58  ? 0.5338 0.3298 0.4335 -0.0277 0.0786  -0.0034 59  SER A C   
530  O O   A SER A 58  ? 0.5621 0.3340 0.4443 -0.0337 0.0858  -0.0015 59  SER A O   
531  O O   B SER A 58  ? 0.5556 0.3295 0.4383 -0.0335 0.0850  -0.0010 59  SER A O   
532  C CB  A SER A 58  ? 0.4961 0.2876 0.4062 -0.0030 0.0738  -0.0017 59  SER A CB  
533  C CB  B SER A 58  ? 0.5140 0.3069 0.4250 -0.0038 0.0740  -0.0022 59  SER A CB  
534  O OG  A SER A 58  ? 0.5108 0.3053 0.4270 0.0141  0.0668  0.0021  59  SER A OG  
535  O OG  B SER A 58  ? 0.6156 0.3753 0.5096 -0.0055 0.0828  -0.0021 59  SER A OG  
536  N N   . ILE A 59  ? 0.4676 0.2855 0.3807 -0.0362 0.0778  -0.0111 60  ILE A N   
537  C CA  . ILE A 59  ? 0.4556 0.2771 0.3681 -0.0520 0.0832  -0.0189 60  ILE A CA  
538  C C   . ILE A 59  ? 0.4923 0.3182 0.4017 -0.0587 0.0836  -0.0179 60  ILE A C   
539  O O   . ILE A 59  ? 0.5175 0.3286 0.4162 -0.0699 0.0929  -0.0213 60  ILE A O   
540  C CB  . ILE A 59  ? 0.4599 0.3061 0.3867 -0.0566 0.0783  -0.0265 60  ILE A CB  
541  C CG1 . ILE A 59  ? 0.4708 0.3095 0.3971 -0.0547 0.0816  -0.0302 60  ILE A CG1 
542  C CG2 . ILE A 59  ? 0.4257 0.2836 0.3562 -0.0706 0.0799  -0.0355 60  ILE A CG2 
543  C CD1 . ILE A 59  ? 0.4979 0.3587 0.4337 -0.0565 0.0749  -0.0349 60  ILE A CD1 
544  N N   . PHE A 60  ? 0.4167 0.2623 0.3349 -0.0533 0.0750  -0.0144 61  PHE A N   
545  C CA  . PHE A 60  ? 0.4184 0.2713 0.3358 -0.0606 0.0761  -0.0156 61  PHE A CA  
546  C C   . PHE A 60  ? 0.4896 0.3199 0.3877 -0.0585 0.0800  -0.0075 61  PHE A C   
547  O O   . PHE A 60  ? 0.4926 0.3256 0.3868 -0.0668 0.0835  -0.0094 61  PHE A O   
548  C CB  . PHE A 60  ? 0.4063 0.2890 0.3407 -0.0579 0.0662  -0.0175 61  PHE A CB  
549  C CG  . PHE A 60  ? 0.4023 0.3024 0.3501 -0.0611 0.0622  -0.0254 61  PHE A CG  
550  C CD1 . PHE A 60  ? 0.4435 0.3478 0.3945 -0.0726 0.0667  -0.0354 61  PHE A CD1 
551  C CD2 . PHE A 60  ? 0.4063 0.3175 0.3615 -0.0532 0.0539  -0.0234 61  PHE A CD2 
552  C CE1 . PHE A 60  ? 0.4391 0.3587 0.3997 -0.0744 0.0609  -0.0425 61  PHE A CE1 
553  C CE2 . PHE A 60  ? 0.4375 0.3604 0.3994 -0.0561 0.0495  -0.0296 61  PHE A CE2 
554  C CZ  . PHE A 60  ? 0.4150 0.3419 0.3790 -0.0657 0.0520  -0.0387 61  PHE A CZ  
555  N N   . THR A 61  ? 0.4794 0.2859 0.3638 -0.0479 0.0798  0.0006  62  THR A N   
556  C CA  . THR A 61  ? 0.5077 0.2859 0.3674 -0.0460 0.0833  0.0089  62  THR A CA  
557  C C   . THR A 61  ? 0.6187 0.3629 0.4581 -0.0556 0.0964  0.0072  62  THR A C   
558  O O   . THR A 61  ? 0.6402 0.3530 0.4530 -0.0573 0.1020  0.0135  62  THR A O   
559  C CB  . THR A 61  ? 0.5913 0.3626 0.4456 -0.0274 0.0735  0.0188  62  THR A CB  
560  O OG1 . THR A 61  ? 0.5571 0.3251 0.4193 -0.0176 0.0717  0.0179  62  THR A OG1 
561  C CG2 . THR A 61  ? 0.5248 0.3256 0.3934 -0.0214 0.0627  0.0203  62  THR A CG2 
562  N N   . ASP A 62  ? 0.5703 0.3191 0.4201 -0.0633 0.1016  -0.0017 63  ASP A N   
563  C CA  . ASP A 62  ? 0.5993 0.3176 0.4316 -0.0748 0.1153  -0.0055 63  ASP A CA  
564  C C   . ASP A 62  ? 0.6796 0.4026 0.5085 -0.0946 0.1250  -0.0133 63  ASP A C   
565  O O   . ASP A 62  ? 0.6354 0.3932 0.4868 -0.1016 0.1220  -0.0226 63  ASP A O   
566  C CB  . ASP A 62  ? 0.6108 0.3344 0.4555 -0.0769 0.1175  -0.0138 63  ASP A CB  
567  C CG  . ASP A 62  ? 0.8196 0.5146 0.6480 -0.0919 0.1326  -0.0202 63  ASP A CG  
568  O OD1 . ASP A 62  ? 0.9056 0.5628 0.7133 -0.0862 0.1380  -0.0144 63  ASP A OD1 
569  O OD2 . ASP A 62  ? 0.8312 0.5409 0.6669 -0.1095 0.1391  -0.0315 63  ASP A OD2 
570  N N   . GLN A 63  ? 0.7162 0.4032 0.5166 -0.1037 0.1370  -0.0104 64  GLN A N   
571  C CA  . GLN A 63  ? 0.7369 0.4245 0.5308 -0.1244 0.1492  -0.0185 64  GLN A CA  
572  C C   . GLN A 63  ? 0.7757 0.4905 0.5924 -0.1413 0.1555  -0.0361 64  GLN A C   
573  O O   . GLN A 63  ? 0.7927 0.5308 0.6207 -0.1539 0.1593  -0.0457 64  GLN A O   
574  C CB  . GLN A 63  ? 0.8128 0.4489 0.5665 -0.1326 0.1631  -0.0123 64  GLN A CB  
575  C CG  . GLN A 63  ? 1.0768 0.6912 0.8057 -0.1198 0.1566  0.0032  64  GLN A CG  
576  N N   . LEU A 64  ? 0.6911 0.4047 0.5153 -0.1415 0.1563  -0.0416 65  LEU A N   
577  C CA  . LEU A 64  ? 0.6609 0.4026 0.5067 -0.1564 0.1599  -0.0589 65  LEU A CA  
578  C C   . LEU A 64  ? 0.6708 0.4564 0.5474 -0.1466 0.1437  -0.0627 65  LEU A C   
579  O O   . LEU A 64  ? 0.6756 0.4939 0.5729 -0.1559 0.1420  -0.0757 65  LEU A O   
580  C CB  . LEU A 64  ? 0.6817 0.4001 0.5183 -0.1635 0.1692  -0.0645 65  LEU A CB  
581  C CG  . LEU A 64  ? 0.7904 0.4707 0.6009 -0.1821 0.1890  -0.0689 65  LEU A CG  
582  C CD1 . LEU A 64  ? 0.8069 0.4660 0.6107 -0.1865 0.1963  -0.0743 65  LEU A CD1 
583  C CD2 . LEU A 64  ? 0.8431 0.5462 0.6641 -0.2049 0.1990  -0.0850 65  LEU A CD2 
584  N N   . LYS A 65  ? 0.5802 0.3654 0.4592 -0.1285 0.1324  -0.0527 66  LYS A N   
585  C CA  . LYS A 65  ? 0.5381 0.3580 0.4406 -0.1201 0.1184  -0.0555 66  LYS A CA  
586  C C   . LYS A 65  ? 0.5850 0.4315 0.5010 -0.1140 0.1083  -0.0530 66  LYS A C   
587  O O   . LYS A 65  ? 0.5417 0.4180 0.4769 -0.1123 0.0987  -0.0591 66  LYS A O   
588  C CB  . LYS A 65  ? 0.5568 0.3673 0.4572 -0.1056 0.1123  -0.0479 66  LYS A CB  
589  C CG  . LYS A 65  ? 0.5535 0.3421 0.4445 -0.1112 0.1213  -0.0528 66  LYS A CG  
590  C CD  . LYS A 65  ? 0.5270 0.3128 0.4203 -0.0969 0.1152  -0.0477 66  LYS A CD  
591  C CE  . LYS A 65  ? 0.5913 0.3479 0.4719 -0.0998 0.1256  -0.0508 66  LYS A CE  
592  N NZ  . LYS A 65  ? 0.6619 0.3804 0.5220 -0.0939 0.1329  -0.0418 66  LYS A NZ  
593  N N   . CYS A 66  ? 0.5901 0.4241 0.4942 -0.1109 0.1104  -0.0444 67  CYS A N   
594  C CA  . CYS A 66  ? 0.5848 0.4415 0.4998 -0.1058 0.1022  -0.0423 67  CYS A CA  
595  C C   . CYS A 66  ? 0.6340 0.5216 0.5691 -0.1168 0.1024  -0.0567 67  CYS A C   
596  O O   . CYS A 66  ? 0.6141 0.5263 0.5645 -0.1107 0.0929  -0.0577 67  CYS A O   
597  C CB  . CYS A 66  ? 0.6181 0.4532 0.5127 -0.1040 0.1066  -0.0326 67  CYS A CB  
598  S SG  . CYS A 66  ? 0.7123 0.5251 0.5870 -0.1249 0.1254  -0.0390 67  CYS A SG  
599  N N   . ASN A 67  ? 0.5971 0.4830 0.5323 -0.1328 0.1133  -0.0689 68  ASN A N   
600  C CA  . ASN A 67  ? 0.5900 0.5062 0.5460 -0.1448 0.1151  -0.0858 68  ASN A CA  
601  C C   . ASN A 67  ? 0.6001 0.5418 0.5761 -0.1442 0.1059  -0.0966 68  ASN A C   
602  O O   . ASN A 67  ? 0.5776 0.5484 0.5739 -0.1519 0.1045  -0.1120 68  ASN A O   
603  C CB  . ASN A 67  ? 0.6285 0.5299 0.5731 -0.1650 0.1338  -0.0949 68  ASN A CB  
604  C CG  . ASN A 67  ? 0.8350 0.7167 0.7603 -0.1677 0.1422  -0.0869 68  ASN A CG  
605  O OD1 . ASN A 67  ? 0.8493 0.6970 0.7484 -0.1783 0.1568  -0.0839 68  ASN A OD1 
606  N ND2 . ASN A 67  ? 0.6864 0.5859 0.6210 -0.1580 0.1332  -0.0828 68  ASN A ND2 
607  N N   . LEU A 68  ? 0.5439 0.4760 0.5144 -0.1350 0.0991  -0.0896 69  LEU A N   
608  C CA  . LEU A 68  ? 0.5232 0.4759 0.5073 -0.1344 0.0897  -0.0987 69  LEU A CA  
609  C C   . LEU A 68  ? 0.5162 0.4949 0.5159 -0.1214 0.0727  -0.0973 69  LEU A C   
610  O O   . LEU A 68  ? 0.4900 0.4624 0.4851 -0.1099 0.0677  -0.0850 69  LEU A O   
611  C CB  . LEU A 68  ? 0.5357 0.4663 0.5055 -0.1305 0.0903  -0.0921 69  LEU A CB  
612  C CG  . LEU A 68  ? 0.6162 0.5178 0.5695 -0.1425 0.1065  -0.0945 69  LEU A CG  
613  C CD1 . LEU A 68  ? 0.6260 0.5072 0.5673 -0.1357 0.1062  -0.0880 69  LEU A CD1 
614  C CD2 . LEU A 68  ? 0.6303 0.5462 0.5927 -0.1608 0.1136  -0.1132 69  LEU A CD2 
615  N N   . SER A 69  ? 0.4547 0.4613 0.4718 -0.1232 0.0636  -0.1104 70  SER A N   
616  C CA  A SER A 69  ? 0.4330 0.4616 0.4630 -0.1105 0.0463  -0.1104 70  SER A CA  
617  C CA  B SER A 69  ? 0.4380 0.4661 0.4677 -0.1103 0.0463  -0.1100 70  SER A CA  
618  C C   . SER A 69  ? 0.4571 0.4802 0.4781 -0.1030 0.0357  -0.1056 70  SER A C   
619  O O   . SER A 69  ? 0.4082 0.4391 0.4314 -0.0915 0.0218  -0.1015 70  SER A O   
620  C CB  A SER A 69  ? 0.4721 0.5341 0.5259 -0.1150 0.0410  -0.1284 70  SER A CB  
621  C CB  B SER A 69  ? 0.4864 0.5479 0.5400 -0.1142 0.0410  -0.1273 70  SER A CB  
622  O OG  A SER A 69  ? 0.5399 0.6089 0.6027 -0.1226 0.0517  -0.1340 70  SER A OG  
623  O OG  B SER A 69  ? 0.5812 0.6542 0.6408 -0.1244 0.0417  -0.1417 70  SER A OG  
624  N N   . VAL A 70  ? 0.4189 0.4264 0.4279 -0.1104 0.0430  -0.1066 71  VAL A N   
625  C CA  . VAL A 70  ? 0.4108 0.4106 0.4084 -0.1063 0.0361  -0.1035 71  VAL A CA  
626  C C   . VAL A 70  ? 0.4484 0.4188 0.4288 -0.1078 0.0481  -0.0945 71  VAL A C   
627  O O   . VAL A 70  ? 0.4444 0.4014 0.4205 -0.1176 0.0616  -0.0978 71  VAL A O   
628  C CB  . VAL A 70  ? 0.4683 0.4848 0.4713 -0.1144 0.0307  -0.1189 71  VAL A CB  
629  C CG1 . VAL A 70  ? 0.4738 0.4805 0.4610 -0.1109 0.0237  -0.1156 71  VAL A CG1 
630  C CG2 . VAL A 70  ? 0.4591 0.5078 0.4826 -0.1111 0.0176  -0.1299 71  VAL A CG2 
631  N N   . ILE A 71  ? 0.3828 0.3423 0.3531 -0.0984 0.0435  -0.0843 72  ILE A N   
632  C CA  . ILE A 71  ? 0.3907 0.3259 0.3476 -0.0974 0.0529  -0.0774 72  ILE A CA  
633  C C   . ILE A 71  ? 0.4345 0.3676 0.3821 -0.0972 0.0481  -0.0794 72  ILE A C   
634  O O   . ILE A 71  ? 0.4185 0.3599 0.3643 -0.0910 0.0368  -0.0764 72  ILE A O   
635  C CB  . ILE A 71  ? 0.4159 0.3408 0.3709 -0.0869 0.0545  -0.0643 72  ILE A CB  
636  C CG1 . ILE A 71  ? 0.4322 0.3564 0.3919 -0.0879 0.0596  -0.0620 72  ILE A CG1 
637  C CG2 . ILE A 71  ? 0.4519 0.3556 0.3966 -0.0833 0.0623  -0.0589 72  ILE A CG2 
638  C CD1 . ILE A 71  ? 0.5052 0.4112 0.4577 -0.0977 0.0737  -0.0655 72  ILE A CD1 
639  N N   . ASN A 72  ? 0.4034 0.3230 0.3425 -0.1047 0.0573  -0.0846 73  ASN A N   
640  C CA  . ASN A 72  ? 0.4123 0.3278 0.3399 -0.1064 0.0549  -0.0875 73  ASN A CA  
641  C C   . ASN A 72  ? 0.4500 0.3464 0.3697 -0.1008 0.0631  -0.0800 73  ASN A C   
642  O O   . ASN A 72  ? 0.4372 0.3172 0.3559 -0.1016 0.0749  -0.0794 73  ASN A O   
643  C CB  . ASN A 72  ? 0.4632 0.3783 0.3873 -0.1193 0.0598  -0.1006 73  ASN A CB  
644  C CG  . ASN A 72  ? 0.6770 0.6153 0.6123 -0.1256 0.0518  -0.1112 73  ASN A CG  
645  O OD1 . ASN A 72  ? 0.5716 0.5274 0.5089 -0.1216 0.0370  -0.1132 73  ASN A OD1 
646  N ND2 . ASN A 72  ? 0.6604 0.5988 0.6029 -0.1356 0.0616  -0.1191 73  ASN A ND2 
647  N N   . LEU A 73  ? 0.3912 0.2888 0.3046 -0.0953 0.0573  -0.0754 74  LEU A N   
648  C CA  . LEU A 73  ? 0.3977 0.2818 0.3067 -0.0907 0.0656  -0.0711 74  LEU A CA  
649  C C   . LEU A 73  ? 0.4517 0.3245 0.3496 -0.0983 0.0737  -0.0792 74  LEU A C   
650  O O   . LEU A 73  ? 0.4623 0.3391 0.3525 -0.1071 0.0700  -0.0871 74  LEU A O   
651  C CB  . LEU A 73  ? 0.3982 0.2874 0.3047 -0.0841 0.0591  -0.0642 74  LEU A CB  
652  C CG  . LEU A 73  ? 0.4336 0.3332 0.3506 -0.0762 0.0516  -0.0563 74  LEU A CG  
653  C CD1 . LEU A 73  ? 0.4312 0.3314 0.3452 -0.0710 0.0495  -0.0505 74  LEU A CD1 
654  C CD2 . LEU A 73  ? 0.4464 0.3430 0.3747 -0.0721 0.0574  -0.0530 74  LEU A CD2 
655  N N   . ASP A 74  ? 0.4173 0.2773 0.3149 -0.0945 0.0840  -0.0782 75  ASP A N   
656  C CA  . ASP A 74  ? 0.4493 0.2969 0.3375 -0.1009 0.0941  -0.0866 75  ASP A CA  
657  C C   . ASP A 74  ? 0.5311 0.3842 0.4038 -0.1082 0.0881  -0.0907 75  ASP A C   
658  O O   . ASP A 74  ? 0.5140 0.3740 0.3835 -0.1044 0.0809  -0.0849 75  ASP A O   
659  C CB  . ASP A 74  ? 0.4712 0.3092 0.3655 -0.0923 0.1040  -0.0848 75  ASP A CB  
660  C CG  . ASP A 74  ? 0.6301 0.4544 0.5176 -0.0973 0.1163  -0.0945 75  ASP A CG  
661  O OD1 . ASP A 74  ? 0.6467 0.4733 0.5223 -0.1049 0.1169  -0.1000 75  ASP A OD1 
662  O OD2 . ASP A 74  ? 0.6629 0.4723 0.5552 -0.0933 0.1256  -0.0965 75  ASP A OD2 
663  N N   . PRO A 75  ? 0.5476 0.3962 0.4081 -0.1190 0.0906  -0.1006 76  PRO A N   
664  C CA  . PRO A 75  ? 0.5557 0.4074 0.3967 -0.1257 0.0831  -0.1037 76  PRO A CA  
665  C C   . PRO A 75  ? 0.6043 0.4491 0.4340 -0.1250 0.0880  -0.1017 76  PRO A C   
666  O O   . PRO A 75  ? 0.6223 0.4672 0.4329 -0.1291 0.0801  -0.1009 76  PRO A O   
667  C CB  . PRO A 75  ? 0.6006 0.4474 0.4316 -0.1377 0.0873  -0.1161 76  PRO A CB  
668  C CG  . PRO A 75  ? 0.6665 0.5017 0.5098 -0.1375 0.1019  -0.1196 76  PRO A CG  
669  C CD  . PRO A 75  ? 0.5843 0.4233 0.4456 -0.1265 0.0998  -0.1095 76  PRO A CD  
670  N N   . GLU A 76  ? 0.5570 0.3961 0.3979 -0.1198 0.1005  -0.1012 77  GLU A N   
671  C CA  . GLU A 76  ? 0.5720 0.4080 0.4058 -0.1203 0.1072  -0.1015 77  GLU A CA  
672  C C   . GLU A 76  ? 0.5692 0.4137 0.4056 -0.1140 0.0984  -0.0914 77  GLU A C   
673  O O   . GLU A 76  ? 0.5569 0.3991 0.3833 -0.1171 0.1023  -0.0915 77  GLU A O   
674  C CB  . GLU A 76  ? 0.6020 0.4326 0.4508 -0.1156 0.1229  -0.1067 77  GLU A CB  
675  C CG  . GLU A 76  ? 0.8708 0.6891 0.7113 -0.1239 0.1347  -0.1188 77  GLU A CG  
676  C CD  . GLU A 76  ? 1.3076 1.1212 1.1275 -0.1350 0.1417  -0.1265 77  GLU A CD  
677  O OE1 . GLU A 76  ? 1.3372 1.1525 1.1633 -0.1330 0.1516  -0.1294 77  GLU A OE1 
678  O OE2 . GLU A 76  ? 1.3183 1.1273 1.1155 -0.1462 0.1372  -0.1303 77  GLU A OE2 
679  N N   . ILE A 77  ? 0.4944 0.3479 0.3430 -0.1065 0.0877  -0.0837 78  ILE A N   
680  C CA  . ILE A 77  ? 0.4714 0.3320 0.3228 -0.1006 0.0796  -0.0748 78  ILE A CA  
681  C C   . ILE A 77  ? 0.5428 0.4000 0.3703 -0.1060 0.0685  -0.0724 78  ILE A C   
682  O O   . ILE A 77  ? 0.5338 0.3922 0.3527 -0.1085 0.0584  -0.0740 78  ILE A O   
683  C CB  . ILE A 77  ? 0.4831 0.3537 0.3552 -0.0908 0.0733  -0.0680 78  ILE A CB  
684  C CG1 . ILE A 77  ? 0.4916 0.3606 0.3823 -0.0842 0.0836  -0.0690 78  ILE A CG1 
685  C CG2 . ILE A 77  ? 0.4258 0.3033 0.2996 -0.0856 0.0649  -0.0598 78  ILE A CG2 
686  C CD1 . ILE A 77  ? 0.5530 0.4226 0.4515 -0.0801 0.0938  -0.0710 78  ILE A CD1 
687  N N   . ASN A 78  ? 0.5417 0.3942 0.3585 -0.1074 0.0702  -0.0691 79  ASN A N   
688  C CA  . ASN A 78  ? 0.5605 0.4032 0.3496 -0.1118 0.0608  -0.0653 79  ASN A CA  
689  C C   . ASN A 78  ? 0.5464 0.3955 0.3417 -0.1029 0.0459  -0.0567 79  ASN A C   
690  O O   . ASN A 78  ? 0.5064 0.3632 0.3200 -0.0967 0.0480  -0.0523 79  ASN A O   
691  C CB  . ASN A 78  ? 0.6256 0.4579 0.4002 -0.1189 0.0723  -0.0663 79  ASN A CB  
692  C CG  . ASN A 78  ? 0.8518 0.6678 0.5938 -0.1236 0.0642  -0.0607 79  ASN A CG  
693  O OD1 . ASN A 78  ? 0.6952 0.5095 0.4374 -0.1207 0.0622  -0.0544 79  ASN A OD1 
694  N ND2 . ASN A 78  ? 0.7764 0.5782 0.4876 -0.1307 0.0591  -0.0627 79  ASN A ND2 
695  N N   . PRO A 79  ? 0.5200 0.3669 0.3006 -0.1017 0.0303  -0.0550 80  PRO A N   
696  C CA  . PRO A 79  ? 0.5116 0.3651 0.3001 -0.0921 0.0163  -0.0482 80  PRO A CA  
697  C C   . PRO A 79  ? 0.5596 0.4029 0.3386 -0.0904 0.0167  -0.0407 80  PRO A C   
698  O O   . PRO A 79  ? 0.5414 0.3936 0.3380 -0.0828 0.0130  -0.0362 80  PRO A O   
699  C CB  . PRO A 79  ? 0.5568 0.4081 0.3277 -0.0913 -0.0003 -0.0500 80  PRO A CB  
700  C CG  . PRO A 79  ? 0.6197 0.4709 0.3844 -0.1000 0.0054  -0.0590 80  PRO A CG  
701  C CD  . PRO A 79  ? 0.5668 0.4068 0.3247 -0.1079 0.0237  -0.0603 80  PRO A CD  
702  N N   . GLU A 80  ? 0.5364 0.3603 0.2869 -0.0989 0.0226  -0.0401 81  GLU A N   
703  C CA  . GLU A 80  ? 0.5399 0.3521 0.2798 -0.0996 0.0250  -0.0340 81  GLU A CA  
704  C C   . GLU A 80  ? 0.5439 0.3712 0.3135 -0.0983 0.0378  -0.0352 81  GLU A C   
705  O O   . GLU A 80  ? 0.5149 0.3459 0.2942 -0.0929 0.0344  -0.0304 81  GLU A O   
706  C CB  . GLU A 80  ? 0.5981 0.3839 0.2982 -0.1115 0.0309  -0.0340 81  GLU A CB  
707  C CG  . GLU A 80  ? 0.7463 0.5161 0.4314 -0.1134 0.0325  -0.0277 81  GLU A CG  
708  C CD  . GLU A 80  ? 1.1278 0.8695 0.7735 -0.1280 0.0431  -0.0281 81  GLU A CD  
709  O OE1 . GLU A 80  ? 1.0830 0.8011 0.7019 -0.1294 0.0387  -0.0212 81  GLU A OE1 
710  O OE2 . GLU A 80  ? 1.0718 0.8132 0.7120 -0.1385 0.0567  -0.0357 81  GLU A OE2 
711  N N   . GLY A 81  ? 0.5134 0.3499 0.2978 -0.1020 0.0513  -0.0423 82  GLY A N   
712  C CA  . GLY A 81  ? 0.4917 0.3444 0.3057 -0.0983 0.0614  -0.0444 82  GLY A CA  
713  C C   . GLY A 81  ? 0.4884 0.3563 0.3274 -0.0867 0.0523  -0.0398 82  GLY A C   
714  O O   . GLY A 81  ? 0.4529 0.3295 0.3068 -0.0824 0.0532  -0.0371 82  GLY A O   
715  N N   . PHE A 82  ? 0.4320 0.3036 0.2748 -0.0827 0.0437  -0.0396 83  PHE A N   
716  C CA  . PHE A 82  ? 0.4030 0.2880 0.2671 -0.0735 0.0364  -0.0362 83  PHE A CA  
717  C C   . PHE A 82  ? 0.4307 0.3145 0.2907 -0.0693 0.0261  -0.0301 83  PHE A C   
718  O O   . PHE A 82  ? 0.4046 0.2985 0.2818 -0.0636 0.0254  -0.0272 83  PHE A O   
719  C CB  . PHE A 82  ? 0.4179 0.3075 0.2860 -0.0726 0.0304  -0.0393 83  PHE A CB  
720  C CG  . PHE A 82  ? 0.4100 0.3128 0.3000 -0.0654 0.0266  -0.0371 83  PHE A CG  
721  C CD1 . PHE A 82  ? 0.4351 0.3432 0.3424 -0.0623 0.0351  -0.0371 83  PHE A CD1 
722  C CD2 . PHE A 82  ? 0.4145 0.3234 0.3065 -0.0612 0.0144  -0.0352 83  PHE A CD2 
723  C CE1 . PHE A 82  ? 0.4326 0.3498 0.3552 -0.0569 0.0322  -0.0345 83  PHE A CE1 
724  C CE2 . PHE A 82  ? 0.4235 0.3446 0.3347 -0.0561 0.0126  -0.0341 83  PHE A CE2 
725  C CZ  . PHE A 82  ? 0.4078 0.3319 0.3324 -0.0548 0.0219  -0.0333 83  PHE A CZ  
726  N N   . CYS A 83  ? 0.4469 0.3172 0.2829 -0.0714 0.0172  -0.0282 84  CYS A N   
727  C CA  . CYS A 83  ? 0.4789 0.3432 0.3073 -0.0664 0.0066  -0.0226 84  CYS A CA  
728  C C   . CYS A 83  ? 0.4852 0.3469 0.3163 -0.0682 0.0148  -0.0198 84  CYS A C   
729  O O   . CYS A 83  ? 0.4525 0.3211 0.2962 -0.0622 0.0105  -0.0167 84  CYS A O   
730  C CB  . CYS A 83  ? 0.5467 0.3908 0.3426 -0.0683 -0.0033 -0.0209 84  CYS A CB  
731  S SG  . CYS A 83  ? 0.6306 0.4627 0.4148 -0.0594 -0.0187 -0.0141 84  CYS A SG  
732  N N   . ILE A 84  ? 0.4553 0.3089 0.2757 -0.0774 0.0273  -0.0223 85  ILE A N   
733  C CA  . ILE A 84  ? 0.4324 0.2862 0.2564 -0.0817 0.0369  -0.0225 85  ILE A CA  
734  C C   . ILE A 84  ? 0.4285 0.3064 0.2866 -0.0747 0.0396  -0.0238 85  ILE A C   
735  O O   . ILE A 84  ? 0.3929 0.2754 0.2589 -0.0729 0.0390  -0.0219 85  ILE A O   
736  C CB  . ILE A 84  ? 0.4817 0.3262 0.2911 -0.0941 0.0516  -0.0281 85  ILE A CB  
737  C CG1 . ILE A 84  ? 0.5201 0.3344 0.2876 -0.1026 0.0491  -0.0251 85  ILE A CG1 
738  C CG2 . ILE A 84  ? 0.4669 0.3234 0.2930 -0.0985 0.0642  -0.0328 85  ILE A CG2 
739  C CD1 . ILE A 84  ? 0.6089 0.4139 0.3591 -0.1150 0.0622  -0.0316 85  ILE A CD1 
740  N N   . LEU A 85  ? 0.3788 0.2695 0.2543 -0.0710 0.0422  -0.0269 86  LEU A N   
741  C CA  . LEU A 85  ? 0.3640 0.2734 0.2670 -0.0635 0.0437  -0.0272 86  LEU A CA  
742  C C   . LEU A 85  ? 0.3942 0.3097 0.3059 -0.0559 0.0332  -0.0223 86  LEU A C   
743  O O   . LEU A 85  ? 0.3549 0.2813 0.2812 -0.0516 0.0329  -0.0210 86  LEU A O   
744  C CB  . LEU A 85  ? 0.3729 0.2884 0.2878 -0.0615 0.0502  -0.0316 86  LEU A CB  
745  C CG  . LEU A 85  ? 0.4550 0.3710 0.3705 -0.0672 0.0629  -0.0387 86  LEU A CG  
746  C CD1 . LEU A 85  ? 0.4740 0.3913 0.3977 -0.0646 0.0683  -0.0431 86  LEU A CD1 
747  C CD2 . LEU A 85  ? 0.4691 0.3997 0.4020 -0.0650 0.0675  -0.0412 86  LEU A CD2 
748  N N   . LEU A 86  ? 0.3712 0.2810 0.2743 -0.0545 0.0244  -0.0209 87  LEU A N   
749  C CA  . LEU A 86  ? 0.3544 0.2714 0.2666 -0.0480 0.0149  -0.0183 87  LEU A CA  
750  C C   . LEU A 86  ? 0.3969 0.3096 0.3042 -0.0468 0.0111  -0.0150 87  LEU A C   
751  O O   . LEU A 86  ? 0.3707 0.2934 0.2919 -0.0424 0.0093  -0.0138 87  LEU A O   
752  C CB  . LEU A 86  ? 0.3567 0.2712 0.2621 -0.0471 0.0059  -0.0199 87  LEU A CB  
753  C CG  . LEU A 86  ? 0.4113 0.3369 0.3299 -0.0408 -0.0028 -0.0202 87  LEU A CG  
754  C CD1 . LEU A 86  ? 0.3909 0.3297 0.3293 -0.0393 0.0032  -0.0210 87  LEU A CD1 
755  C CD2 . LEU A 86  ? 0.4588 0.3852 0.3722 -0.0398 -0.0128 -0.0242 87  LEU A CD2 
756  N N   . ASP A 87  ? 0.3909 0.2863 0.2762 -0.0518 0.0108  -0.0139 88  ASP A N   
757  C CA  . ASP A 87  ? 0.3918 0.2780 0.2688 -0.0524 0.0092  -0.0111 88  ASP A CA  
758  C C   . ASP A 87  ? 0.4153 0.3140 0.3083 -0.0545 0.0182  -0.0128 88  ASP A C   
759  O O   . ASP A 87  ? 0.4073 0.3101 0.3075 -0.0515 0.0153  -0.0116 88  ASP A O   
760  C CB  . ASP A 87  ? 0.4508 0.3113 0.2964 -0.0597 0.0103  -0.0096 88  ASP A CB  
761  C CG  . ASP A 87  ? 0.6322 0.4772 0.4579 -0.0550 -0.0030 -0.0068 88  ASP A CG  
762  O OD1 . ASP A 87  ? 0.6301 0.4862 0.4696 -0.0457 -0.0136 -0.0069 88  ASP A OD1 
763  O OD2 . ASP A 87  ? 0.6775 0.4994 0.4732 -0.0608 -0.0031 -0.0052 88  ASP A OD2 
764  N N   . PHE A 88  ? 0.3688 0.2748 0.2684 -0.0592 0.0286  -0.0168 89  PHE A N   
765  C CA  . PHE A 88  ? 0.3431 0.2657 0.2614 -0.0597 0.0358  -0.0202 89  PHE A CA  
766  C C   . PHE A 88  ? 0.3488 0.2884 0.2879 -0.0505 0.0303  -0.0184 89  PHE A C   
767  O O   . PHE A 88  ? 0.3149 0.2641 0.2638 -0.0493 0.0302  -0.0190 89  PHE A O   
768  C CB  . PHE A 88  ? 0.3487 0.2783 0.2736 -0.0636 0.0463  -0.0263 89  PHE A CB  
769  C CG  . PHE A 88  ? 0.3391 0.2905 0.2879 -0.0604 0.0508  -0.0308 89  PHE A CG  
770  C CD1 . PHE A 88  ? 0.3613 0.3188 0.3133 -0.0664 0.0557  -0.0351 89  PHE A CD1 
771  C CD2 . PHE A 88  ? 0.3515 0.3164 0.3185 -0.0508 0.0488  -0.0307 89  PHE A CD2 
772  C CE1 . PHE A 88  ? 0.3446 0.3255 0.3202 -0.0624 0.0576  -0.0404 89  PHE A CE1 
773  C CE2 . PHE A 88  ? 0.3720 0.3563 0.3594 -0.0455 0.0499  -0.0344 89  PHE A CE2 
774  C CZ  . PHE A 88  ? 0.3452 0.3396 0.3382 -0.0510 0.0536  -0.0397 89  PHE A CZ  
775  N N   . MET A 89  ? 0.2995 0.2420 0.2440 -0.0451 0.0267  -0.0170 90  MET A N   
776  C CA  . MET A 89  ? 0.2853 0.2400 0.2449 -0.0379 0.0229  -0.0151 90  MET A CA  
777  C C   . MET A 89  ? 0.3367 0.2925 0.2965 -0.0361 0.0166  -0.0131 90  MET A C   
778  O O   . MET A 89  ? 0.3205 0.2872 0.2910 -0.0333 0.0163  -0.0129 90  MET A O   
779  C CB  . MET A 89  ? 0.2941 0.2469 0.2543 -0.0353 0.0206  -0.0144 90  MET A CB  
780  C CG  . MET A 89  ? 0.3194 0.2707 0.2810 -0.0359 0.0272  -0.0167 90  MET A CG  
781  S SD  . MET A 89  ? 0.3629 0.3111 0.3251 -0.0347 0.0255  -0.0167 90  MET A SD  
782  C CE  . MET A 89  ? 0.3587 0.2993 0.3173 -0.0373 0.0340  -0.0205 90  MET A CE  
783  N N   . TYR A 90  ? 0.3000 0.2437 0.2472 -0.0372 0.0112  -0.0120 91  TYR A N   
784  C CA  . TYR A 90  ? 0.3010 0.2437 0.2485 -0.0342 0.0048  -0.0111 91  TYR A CA  
785  C C   . TYR A 90  ? 0.3664 0.3007 0.3057 -0.0381 0.0067  -0.0110 91  TYR A C   
786  O O   . TYR A 90  ? 0.3468 0.2790 0.2866 -0.0354 0.0022  -0.0108 91  TYR A O   
787  C CB  . TYR A 90  ? 0.3234 0.2578 0.2631 -0.0309 -0.0037 -0.0109 91  TYR A CB  
788  C CG  . TYR A 90  ? 0.3237 0.2707 0.2765 -0.0273 -0.0063 -0.0130 91  TYR A CG  
789  C CD1 . TYR A 90  ? 0.3347 0.2830 0.2875 -0.0294 -0.0036 -0.0143 91  TYR A CD1 
790  C CD2 . TYR A 90  ? 0.3319 0.2887 0.2963 -0.0232 -0.0101 -0.0149 91  TYR A CD2 
791  C CE1 . TYR A 90  ? 0.3229 0.2810 0.2862 -0.0283 -0.0044 -0.0173 91  TYR A CE1 
792  C CE2 . TYR A 90  ? 0.3318 0.2996 0.3071 -0.0221 -0.0108 -0.0184 91  TYR A CE2 
793  C CZ  . TYR A 90  ? 0.3576 0.3256 0.3320 -0.0252 -0.0076 -0.0195 91  TYR A CZ  
794  O OH  . TYR A 90  ? 0.3455 0.3231 0.3295 -0.0262 -0.0068 -0.0240 91  TYR A OH  
795  N N   . THR A 91  ? 0.3324 0.2611 0.2639 -0.0454 0.0142  -0.0124 92  THR A N   
796  C CA  . THR A 91  ? 0.3516 0.2695 0.2726 -0.0517 0.0177  -0.0135 92  THR A CA  
797  C C   . THR A 91  ? 0.3723 0.3029 0.3029 -0.0588 0.0277  -0.0187 92  THR A C   
798  O O   . THR A 91  ? 0.3673 0.2924 0.2925 -0.0652 0.0315  -0.0211 92  THR A O   
799  C CB  . THR A 91  ? 0.4423 0.3321 0.3349 -0.0570 0.0175  -0.0112 92  THR A CB  
800  O OG1 . THR A 91  ? 0.4357 0.3242 0.3226 -0.0634 0.0250  -0.0132 92  THR A OG1 
801  C CG2 . THR A 91  ? 0.4597 0.3366 0.3416 -0.0489 0.0053  -0.0072 92  THR A CG2 
802  N N   . SER A 92  ? 0.3112 0.2568 0.2544 -0.0582 0.0324  -0.0216 93  SER A N   
803  C CA  . SER A 92  ? 0.2982 0.2589 0.2532 -0.0638 0.0417  -0.0288 93  SER A CA  
804  C C   . SER A 92  ? 0.3659 0.3115 0.3036 -0.0760 0.0516  -0.0327 93  SER A C   
805  O O   . SER A 92  ? 0.3628 0.3216 0.3107 -0.0822 0.0608  -0.0408 93  SER A O   
806  C CB  . SER A 92  ? 0.3121 0.2865 0.2786 -0.0654 0.0420  -0.0326 93  SER A CB  
807  O OG  . SER A 92  ? 0.3935 0.3778 0.3704 -0.0560 0.0335  -0.0290 93  SER A OG  
808  N N   A ARG A 93  ? 0.3587 0.2773 0.2702 -0.0792 0.0493  -0.0276 94  ARG A N   
809  N N   B ARG A 93  ? 0.3487 0.2671 0.2599 -0.0795 0.0495  -0.0277 94  ARG A N   
810  C CA  A ARG A 93  ? 0.3860 0.2840 0.2735 -0.0918 0.0585  -0.0299 94  ARG A CA  
811  C CA  B ARG A 93  ? 0.3723 0.2706 0.2601 -0.0922 0.0590  -0.0302 94  ARG A CA  
812  C C   A ARG A 93  ? 0.4354 0.3288 0.3158 -0.0917 0.0602  -0.0298 94  ARG A C   
813  C C   B ARG A 93  ? 0.4315 0.3236 0.3104 -0.0922 0.0603  -0.0297 94  ARG A C   
814  O O   A ARG A 93  ? 0.4236 0.3115 0.2995 -0.0836 0.0506  -0.0242 94  ARG A O   
815  O O   B ARG A 93  ? 0.4245 0.3091 0.2969 -0.0845 0.0505  -0.0238 94  ARG A O   
816  C CB  A ARG A 93  ? 0.4386 0.3044 0.2957 -0.0954 0.0543  -0.0240 94  ARG A CB  
817  C CB  B ARG A 93  ? 0.4035 0.2705 0.2615 -0.0976 0.0567  -0.0254 94  ARG A CB  
818  C CG  A ARG A 93  ? 0.5103 0.3763 0.3716 -0.0963 0.0534  -0.0246 94  ARG A CG  
819  C CG  B ARG A 93  ? 0.4268 0.2978 0.2912 -0.1025 0.0604  -0.0290 94  ARG A CG  
820  C CD  A ARG A 93  ? 0.6374 0.4704 0.4709 -0.0941 0.0454  -0.0174 94  ARG A CD  
821  C CD  B ARG A 93  ? 0.5905 0.4300 0.4287 -0.1033 0.0553  -0.0231 94  ARG A CD  
822  N NE  A ARG A 93  ? 0.7229 0.5216 0.5197 -0.1049 0.0511  -0.0155 94  ARG A NE  
823  N NE  B ARG A 93  ? 0.6602 0.5055 0.5070 -0.1082 0.0594  -0.0276 94  ARG A NE  
824  C CZ  A ARG A 93  ? 0.8898 0.6694 0.6676 -0.1194 0.0627  -0.0187 94  ARG A CZ  
825  C CZ  B ARG A 93  ? 0.8434 0.6597 0.6657 -0.1170 0.0635  -0.0271 94  ARG A CZ  
826  N NH1 A ARG A 93  ? 0.7228 0.4676 0.4628 -0.1296 0.0681  -0.0162 94  ARG A NH1 
827  N NH1 B ARG A 93  ? 0.7060 0.5303 0.5386 -0.1220 0.0678  -0.0325 94  ARG A NH1 
828  N NH2 A ARG A 93  ? 0.7064 0.5005 0.5012 -0.1248 0.0693  -0.0250 94  ARG A NH2 
829  N NH2 B ARG A 93  ? 0.6905 0.4678 0.4757 -0.1209 0.0632  -0.0211 94  ARG A NH2 
830  N N   . LEU A 94  ? 0.3938 0.2909 0.2741 -0.1016 0.0731  -0.0376 95  LEU A N   
831  C CA  . LEU A 94  ? 0.3948 0.2879 0.2683 -0.1035 0.0773  -0.0395 95  LEU A CA  
832  C C   . LEU A 94  ? 0.4939 0.3587 0.3323 -0.1184 0.0860  -0.0407 95  LEU A C   
833  O O   . LEU A 94  ? 0.4912 0.3555 0.3263 -0.1313 0.0992  -0.0481 95  LEU A O   
834  C CB  . LEU A 94  ? 0.3778 0.2993 0.2815 -0.1014 0.0855  -0.0490 95  LEU A CB  
835  C CG  . LEU A 94  ? 0.4348 0.3548 0.3366 -0.1015 0.0904  -0.0524 95  LEU A CG  
836  C CD1 . LEU A 94  ? 0.4194 0.3368 0.3226 -0.0896 0.0783  -0.0447 95  LEU A CD1 
837  C CD2 . LEU A 94  ? 0.4343 0.3798 0.3643 -0.1005 0.1006  -0.0640 95  LEU A CD2 
838  N N   . ASN A 95  ? 0.5053 0.3466 0.3166 -0.1174 0.0788  -0.0341 96  ASN A N   
839  C CA  . ASN A 95  ? 0.5478 0.3568 0.3185 -0.1306 0.0849  -0.0333 96  ASN A CA  
840  C C   . ASN A 95  ? 0.5957 0.4107 0.3667 -0.1393 0.0982  -0.0422 96  ASN A C   
841  O O   . ASN A 95  ? 0.5964 0.4024 0.3538 -0.1377 0.0941  -0.0403 96  ASN A O   
842  C CB  . ASN A 95  ? 0.6131 0.3955 0.3543 -0.1238 0.0688  -0.0228 96  ASN A CB  
843  C CG  . ASN A 95  ? 0.8676 0.6116 0.5604 -0.1361 0.0725  -0.0202 96  ASN A CG  
844  O OD1 . ASN A 95  ? 0.7651 0.4951 0.4407 -0.1515 0.0874  -0.0245 96  ASN A OD1 
845  N ND2 . ASN A 95  ? 0.7758 0.5018 0.4443 -0.1305 0.0595  -0.0140 96  ASN A ND2 
846  N N   . LEU A 96  ? 0.5448 0.3783 0.3352 -0.1477 0.1137  -0.0532 97  LEU A N   
847  C CA  . LEU A 96  ? 0.5505 0.3947 0.3482 -0.1550 0.1278  -0.0643 97  LEU A CA  
848  C C   . LEU A 96  ? 0.6318 0.4487 0.3917 -0.1752 0.1423  -0.0686 97  LEU A C   
849  O O   . LEU A 96  ? 0.6193 0.4276 0.3688 -0.1871 0.1511  -0.0713 97  LEU A O   
850  C CB  . LEU A 96  ? 0.5341 0.4160 0.3761 -0.1515 0.1356  -0.0756 97  LEU A CB  
851  C CG  . LEU A 96  ? 0.5967 0.5002 0.4626 -0.1498 0.1454  -0.0873 97  LEU A CG  
852  C CD1 . LEU A 96  ? 0.5906 0.4917 0.4584 -0.1368 0.1348  -0.0810 97  LEU A CD1 
853  C CD2 . LEU A 96  ? 0.5807 0.5213 0.4901 -0.1432 0.1490  -0.0975 97  LEU A CD2 
854  N N   . ARG A 97  ? 0.6006 0.4012 0.3364 -0.1805 0.1451  -0.0691 98  ARG A N   
855  C CA  . ARG A 97  ? 0.6562 0.4258 0.3485 -0.2008 0.1589  -0.0724 98  ARG A CA  
856  C C   . ARG A 97  ? 0.6852 0.4637 0.3814 -0.2082 0.1728  -0.0843 98  ARG A C   
857  O O   . ARG A 97  ? 0.6438 0.4423 0.3657 -0.1955 0.1668  -0.0859 98  ARG A O   
858  C CB  . ARG A 97  ? 0.6958 0.4238 0.3385 -0.2001 0.1446  -0.0580 98  ARG A CB  
859  C CG  . ARG A 97  ? 0.8011 0.5166 0.4377 -0.1912 0.1298  -0.0463 98  ARG A CG  
860  C CD  . ARG A 97  ? 1.0728 0.7508 0.6655 -0.1859 0.1123  -0.0327 98  ARG A CD  
861  N NE  . ARG A 97  ? 1.3552 0.9922 0.8930 -0.2032 0.1212  -0.0319 98  ARG A NE  
862  C CZ  . ARG A 97  ? 1.6341 1.2369 1.1354 -0.2167 0.1293  -0.0291 98  ARG A CZ  
863  N NH1 . ARG A 97  ? 1.5151 1.0781 0.9629 -0.2331 0.1379  -0.0281 98  ARG A NH1 
864  N NH2 . ARG A 97  ? 1.4997 1.1058 1.0156 -0.2147 0.1295  -0.0276 98  ARG A NH2 
865  N N   . GLU A 98  ? 0.6717 0.4337 0.3409 -0.2294 0.1923  -0.0934 99  GLU A N   
866  C CA  . GLU A 98  ? 0.6783 0.4471 0.3488 -0.2381 0.2073  -0.1063 99  GLU A CA  
867  C C   . GLU A 98  ? 0.7499 0.5081 0.4060 -0.2286 0.1940  -0.0991 99  GLU A C   
868  O O   . GLU A 98  ? 0.7314 0.5104 0.4129 -0.2235 0.1984  -0.1080 99  GLU A O   
869  C CB  . GLU A 98  ? 0.7481 0.4897 0.3770 -0.2649 0.2289  -0.1143 99  GLU A CB  
870  C CG  . GLU A 98  ? 0.9111 0.6650 0.5471 -0.2763 0.2489  -0.1317 99  GLU A CG  
871  C CD  . GLU A 98  ? 1.3758 1.0998 0.9657 -0.3045 0.2712  -0.1398 99  GLU A CD  
872  O OE1 . GLU A 98  ? 1.3842 1.0629 0.9169 -0.3136 0.2658  -0.1270 99  GLU A OE1 
873  O OE2 . GLU A 98  ? 1.4139 1.1590 1.0239 -0.3175 0.2942  -0.1596 99  GLU A OE2 
874  N N   . GLY A 99  ? 0.7444 0.4710 0.3612 -0.2257 0.1773  -0.0842 100 GLY A N   
875  C CA  . GLY A 99  ? 0.7573 0.4731 0.3569 -0.2181 0.1631  -0.0779 100 GLY A CA  
876  C C   . GLY A 99  ? 0.7480 0.4905 0.3870 -0.1968 0.1467  -0.0740 100 GLY A C   
877  O O   . GLY A 99  ? 0.7468 0.4873 0.3797 -0.1919 0.1383  -0.0728 100 GLY A O   
878  N N   . ASN A 100 ? 0.6601 0.4274 0.3385 -0.1851 0.1427  -0.0725 101 ASN A N   
879  C CA  . ASN A 100 ? 0.6113 0.4004 0.3229 -0.1665 0.1284  -0.0685 101 ASN A CA  
880  C C   . ASN A 100 ? 0.6251 0.4485 0.3862 -0.1583 0.1362  -0.0772 101 ASN A C   
881  O O   . ASN A 100 ? 0.5838 0.4223 0.3697 -0.1441 0.1265  -0.0745 101 ASN A O   
882  C CB  . ASN A 100 ? 0.5770 0.3601 0.2853 -0.1553 0.1092  -0.0554 101 ASN A CB  
883  C CG  . ASN A 100 ? 0.6704 0.4620 0.3948 -0.1543 0.1117  -0.0540 101 ASN A CG  
884  O OD1 . ASN A 100 ? 0.5500 0.3652 0.3054 -0.1551 0.1232  -0.0626 101 ASN A OD1 
885  N ND2 . ASN A 100 ? 0.6009 0.3748 0.3063 -0.1514 0.0999  -0.0439 101 ASN A ND2 
886  N N   . ILE A 101 ? 0.5788 0.4142 0.3535 -0.1668 0.1529  -0.0879 102 ILE A N   
887  C CA  . ILE A 101 ? 0.5479 0.4169 0.3698 -0.1572 0.1582  -0.0964 102 ILE A CA  
888  C C   . ILE A 101 ? 0.5619 0.4435 0.4059 -0.1468 0.1583  -0.1014 102 ILE A C   
889  O O   . ILE A 101 ? 0.5136 0.4142 0.3893 -0.1312 0.1509  -0.0996 102 ILE A O   
890  C CB  . ILE A 101 ? 0.5965 0.4792 0.4304 -0.1692 0.1767  -0.1102 102 ILE A CB  
891  C CG1 . ILE A 101 ? 0.5783 0.4984 0.4631 -0.1556 0.1773  -0.1183 102 ILE A CG1 
892  C CG2 . ILE A 101 ? 0.5898 0.4617 0.4034 -0.1870 0.1958  -0.1226 102 ILE A CG2 
893  C CD1 . ILE A 101 ? 0.5667 0.5053 0.4682 -0.1636 0.1876  -0.1282 102 ILE A CD1 
894  N N   . MET A 102 ? 0.5509 0.4195 0.3758 -0.1555 0.1666  -0.1075 103 MET A N   
895  C CA  . MET A 102 ? 0.5539 0.4307 0.3973 -0.1467 0.1679  -0.1129 103 MET A CA  
896  C C   . MET A 102 ? 0.5750 0.4483 0.4208 -0.1336 0.1501  -0.1012 103 MET A C   
897  O O   . MET A 102 ? 0.5393 0.4262 0.4136 -0.1204 0.1477  -0.1023 103 MET A O   
898  C CB  . MET A 102 ? 0.6211 0.4843 0.4424 -0.1603 0.1816  -0.1232 103 MET A CB  
899  C CG  . MET A 102 ? 0.7073 0.5773 0.5309 -0.1743 0.2027  -0.1383 103 MET A CG  
900  S SD  . MET A 102 ? 0.7568 0.6656 0.6365 -0.1630 0.2115  -0.1515 103 MET A SD  
901  C CE  . MET A 102 ? 0.7113 0.6278 0.6157 -0.1497 0.2147  -0.1604 103 MET A CE  
902  N N   . ALA A 103 ? 0.5522 0.4071 0.3682 -0.1368 0.1376  -0.0905 104 ALA A N   
903  C CA  . ALA A 103 ? 0.5436 0.3977 0.3627 -0.1259 0.1210  -0.0811 104 ALA A CA  
904  C C   . ALA A 103 ? 0.5405 0.4111 0.3875 -0.1127 0.1125  -0.0744 104 ALA A C   
905  O O   . ALA A 103 ? 0.4995 0.3782 0.3654 -0.1019 0.1065  -0.0720 104 ALA A O   
906  C CB  . ALA A 103 ? 0.5830 0.4170 0.3663 -0.1314 0.1090  -0.0731 104 ALA A CB  
907  N N   . VAL A 104 ? 0.4737 0.3475 0.3210 -0.1147 0.1128  -0.0719 105 VAL A N   
908  C CA  . VAL A 104 ? 0.4368 0.3263 0.3084 -0.1035 0.1052  -0.0665 105 VAL A CA  
909  C C   . VAL A 104 ? 0.4531 0.3631 0.3590 -0.0934 0.1105  -0.0727 105 VAL A C   
910  O O   . VAL A 104 ? 0.4199 0.3371 0.3416 -0.0815 0.1016  -0.0671 105 VAL A O   
911  C CB  . VAL A 104 ? 0.4795 0.3672 0.3435 -0.1093 0.1055  -0.0639 105 VAL A CB  
912  C CG1 . VAL A 104 ? 0.4438 0.3507 0.3353 -0.0983 0.0992  -0.0606 105 VAL A CG1 
913  C CG2 . VAL A 104 ? 0.4963 0.3601 0.3258 -0.1144 0.0959  -0.0552 105 VAL A CG2 
914  N N   A MET A 105 ? 0.4304 0.3488 0.3467 -0.0978 0.1247  -0.0845 106 MET A N   
915  N N   B MET A 105 ? 0.4359 0.3543 0.3522 -0.0977 0.1247  -0.0845 106 MET A N   
916  C CA  A MET A 105 ? 0.4244 0.3618 0.3735 -0.0859 0.1287  -0.0915 106 MET A CA  
917  C CA  B MET A 105 ? 0.4313 0.3687 0.3804 -0.0860 0.1288  -0.0916 106 MET A CA  
918  C C   A MET A 105 ? 0.4785 0.4087 0.4315 -0.0767 0.1251  -0.0894 106 MET A C   
919  C C   B MET A 105 ? 0.4818 0.4121 0.4348 -0.0767 0.1252  -0.0895 106 MET A C   
920  O O   A MET A 105 ? 0.4590 0.3973 0.4319 -0.0627 0.1194  -0.0865 106 MET A O   
921  O O   B MET A 105 ? 0.4625 0.4009 0.4353 -0.0627 0.1192  -0.0864 106 MET A O   
922  C CB  A MET A 105 ? 0.4639 0.4127 0.4244 -0.0925 0.1451  -0.1070 106 MET A CB  
923  C CB  B MET A 105 ? 0.4748 0.4236 0.4352 -0.0927 0.1454  -0.1072 106 MET A CB  
924  C CG  A MET A 105 ? 0.4981 0.4691 0.4953 -0.0773 0.1469  -0.1149 106 MET A CG  
925  C CG  B MET A 105 ? 0.5143 0.4854 0.5114 -0.0776 0.1472  -0.1152 106 MET A CG  
926  S SD  A MET A 105 ? 0.5665 0.5595 0.5848 -0.0842 0.1654  -0.1358 106 MET A SD  
927  S SD  B MET A 105 ? 0.5890 0.5786 0.6051 -0.0844 0.1668  -0.1367 106 MET A SD  
928  C CE  A MET A 105 ? 0.5488 0.5245 0.5526 -0.0916 0.1787  -0.1450 106 MET A CE  
929  C CE  B MET A 105 ? 0.5428 0.5453 0.5931 -0.0614 0.1639  -0.1423 106 MET A CE  
930  N N   . ALA A 106 ? 0.4581 0.3715 0.3899 -0.0851 0.1289  -0.0913 107 ALA A N   
931  C CA  . ALA A 106 ? 0.4543 0.3583 0.3867 -0.0795 0.1272  -0.0908 107 ALA A CA  
932  C C   . ALA A 106 ? 0.4486 0.3499 0.3810 -0.0719 0.1130  -0.0789 107 ALA A C   
933  O O   . ALA A 106 ? 0.4221 0.3230 0.3677 -0.0617 0.1111  -0.0773 107 ALA A O   
934  C CB  . ALA A 106 ? 0.4854 0.3734 0.3927 -0.0923 0.1331  -0.0958 107 ALA A CB  
935  N N   . THR A 107 ? 0.4029 0.3018 0.3206 -0.0766 0.1035  -0.0712 108 THR A N   
936  C CA  . THR A 107 ? 0.4007 0.2999 0.3201 -0.0704 0.0908  -0.0617 108 THR A CA  
937  C C   . THR A 107 ? 0.4260 0.3384 0.3680 -0.0585 0.0874  -0.0577 108 THR A C   
938  O O   . THR A 107 ? 0.3992 0.3104 0.3483 -0.0511 0.0826  -0.0533 108 THR A O   
939  C CB  . THR A 107 ? 0.4792 0.3727 0.3784 -0.0768 0.0812  -0.0559 108 THR A CB  
940  O OG1 . THR A 107 ? 0.4927 0.3734 0.3683 -0.0874 0.0840  -0.0600 108 THR A OG1 
941  C CG2 . THR A 107 ? 0.4508 0.3459 0.3526 -0.0715 0.0691  -0.0492 108 THR A CG2 
942  N N   . ALA A 108 ? 0.3820 0.3062 0.3338 -0.0577 0.0904  -0.0600 109 ALA A N   
943  C CA  . ALA A 108 ? 0.3562 0.2950 0.3290 -0.0465 0.0863  -0.0574 109 ALA A CA  
944  C C   . ALA A 108 ? 0.3861 0.3265 0.3751 -0.0350 0.0894  -0.0607 109 ALA A C   
945  O O   . ALA A 108 ? 0.3542 0.2965 0.3517 -0.0245 0.0827  -0.0550 109 ALA A O   
946  C CB  . ALA A 108 ? 0.3556 0.3086 0.3360 -0.0501 0.0901  -0.0621 109 ALA A CB  
947  N N   . MET A 109 ? 0.3703 0.3068 0.3610 -0.0369 0.0997  -0.0699 110 MET A N   
948  C CA  . MET A 109 ? 0.3763 0.3100 0.3806 -0.0245 0.1025  -0.0733 110 MET A CA  
949  C C   . MET A 109 ? 0.4199 0.3348 0.4136 -0.0214 0.0978  -0.0656 110 MET A C   
950  O O   . MET A 109 ? 0.4217 0.3327 0.4225 -0.0092 0.0936  -0.0612 110 MET A O   
951  C CB  . MET A 109 ? 0.4232 0.3555 0.4308 -0.0283 0.1155  -0.0861 110 MET A CB  
952  C CG  . MET A 109 ? 0.4806 0.4348 0.5067 -0.0278 0.1218  -0.0965 110 MET A CG  
953  S SD  . MET A 109 ? 0.5807 0.5334 0.6069 -0.0372 0.1397  -0.1133 110 MET A SD  
954  C CE  . MET A 109 ? 0.5575 0.5022 0.6003 -0.0186 0.1410  -0.1175 110 MET A CE  
955  N N   . TYR A 110 ? 0.4018 0.3052 0.3771 -0.0330 0.0983  -0.0643 111 TYR A N   
956  C CA  . TYR A 110 ? 0.4046 0.2926 0.3695 -0.0343 0.0954  -0.0596 111 TYR A CA  
957  C C   . TYR A 110 ? 0.4205 0.3124 0.3872 -0.0294 0.0852  -0.0496 111 TYR A C   
958  O O   . TYR A 110 ? 0.4070 0.2882 0.3734 -0.0235 0.0841  -0.0455 111 TYR A O   
959  C CB  . TYR A 110 ? 0.4207 0.3025 0.3678 -0.0485 0.0964  -0.0624 111 TYR A CB  
960  C CG  . TYR A 110 ? 0.4256 0.2978 0.3637 -0.0526 0.0924  -0.0594 111 TYR A CG  
961  C CD1 . TYR A 110 ? 0.4579 0.3145 0.3935 -0.0528 0.0991  -0.0631 111 TYR A CD1 
962  C CD2 . TYR A 110 ? 0.4257 0.3045 0.3581 -0.0570 0.0827  -0.0546 111 TYR A CD2 
963  C CE1 . TYR A 110 ? 0.4271 0.2763 0.3552 -0.0590 0.0971  -0.0623 111 TYR A CE1 
964  C CE2 . TYR A 110 ? 0.4289 0.3031 0.3561 -0.0619 0.0798  -0.0546 111 TYR A CE2 
965  C CZ  . TYR A 110 ? 0.4556 0.3157 0.3808 -0.0639 0.0875  -0.0588 111 TYR A CZ  
966  O OH  . TYR A 110 ? 0.4497 0.3070 0.3705 -0.0712 0.0861  -0.0609 111 TYR A OH  
967  N N   . LEU A 111 ? 0.3712 0.2762 0.3383 -0.0320 0.0786  -0.0460 112 LEU A N   
968  C CA  . LEU A 111 ? 0.3464 0.2564 0.3154 -0.0283 0.0697  -0.0379 112 LEU A CA  
969  C C   . LEU A 111 ? 0.3805 0.2971 0.3625 -0.0158 0.0671  -0.0348 112 LEU A C   
970  O O   . LEU A 111 ? 0.3715 0.2895 0.3535 -0.0121 0.0606  -0.0282 112 LEU A O   
971  C CB  . LEU A 111 ? 0.3287 0.2481 0.2928 -0.0349 0.0637  -0.0359 112 LEU A CB  
972  C CG  . LEU A 111 ? 0.3776 0.2905 0.3265 -0.0450 0.0616  -0.0374 112 LEU A CG  
973  C CD1 . LEU A 111 ? 0.3671 0.2859 0.3100 -0.0482 0.0541  -0.0342 112 LEU A CD1 
974  C CD2 . LEU A 111 ? 0.3949 0.3015 0.3412 -0.0463 0.0593  -0.0363 112 LEU A CD2 
975  N N   . GLN A 112 ? 0.3622 0.2844 0.3556 -0.0093 0.0717  -0.0405 113 GLN A N   
976  C CA  . GLN A 112 ? 0.3626 0.2943 0.3704 0.0044  0.0677  -0.0395 113 GLN A CA  
977  C C   . GLN A 112 ? 0.3852 0.3351 0.3987 0.0035  0.0607  -0.0365 113 GLN A C   
978  O O   . GLN A 112 ? 0.3648 0.3154 0.3772 0.0088  0.0532  -0.0296 113 GLN A O   
979  C CB  . GLN A 112 ? 0.3845 0.2986 0.3868 0.0145  0.0647  -0.0330 113 GLN A CB  
980  C CG  . GLN A 112 ? 0.4584 0.3509 0.4539 0.0152  0.0726  -0.0364 113 GLN A CG  
981  C CD  . GLN A 112 ? 0.6004 0.4696 0.5826 0.0200  0.0708  -0.0286 113 GLN A CD  
982  O OE1 . GLN A 112 ? 0.4940 0.3627 0.4751 0.0286  0.0635  -0.0216 113 GLN A OE1 
983  N NE2 . GLN A 112 ? 0.5561 0.4042 0.5259 0.0130  0.0780  -0.0301 113 GLN A NE2 
984  N N   . MET A 113 ? 0.3466 0.3087 0.3634 -0.0048 0.0642  -0.0423 114 MET A N   
985  C CA  . MET A 113 ? 0.3362 0.3139 0.3573 -0.0084 0.0601  -0.0416 114 MET A CA  
986  C C   . MET A 113 ? 0.4044 0.4007 0.4434 -0.0064 0.0654  -0.0521 114 MET A C   
987  O O   . MET A 113 ? 0.3876 0.3866 0.4246 -0.0169 0.0738  -0.0593 114 MET A O   
988  C CB  . MET A 113 ? 0.3505 0.3207 0.3552 -0.0218 0.0608  -0.0398 114 MET A CB  
989  C CG  . MET A 113 ? 0.3750 0.3322 0.3669 -0.0229 0.0549  -0.0320 114 MET A CG  
990  S SD  . MET A 113 ? 0.4136 0.3619 0.3869 -0.0352 0.0532  -0.0309 114 MET A SD  
991  C CE  . MET A 113 ? 0.3628 0.3220 0.3391 -0.0362 0.0480  -0.0283 114 MET A CE  
992  N N   . GLU A 114 ? 0.3894 0.3973 0.4451 0.0076  0.0610  -0.0538 115 GLU A N   
993  C CA  . GLU A 114 ? 0.4031 0.4325 0.4816 0.0133  0.0648  -0.0660 115 GLU A CA  
994  C C   . GLU A 114 ? 0.4088 0.4588 0.4959 0.0021  0.0695  -0.0744 115 GLU A C   
995  O O   . GLU A 114 ? 0.4014 0.4634 0.5007 -0.0021 0.0792  -0.0869 115 GLU A O   
996  C CB  . GLU A 114 ? 0.4366 0.4752 0.5298 0.0324  0.0550  -0.0650 115 GLU A CB  
997  C CG  . GLU A 114 ? 0.6237 0.6380 0.7069 0.0437  0.0525  -0.0581 115 GLU A CG  
998  N N   . HIS A 115 ? 0.3523 0.4058 0.4331 -0.0036 0.0640  -0.0689 116 HIS A N   
999  C CA  . HIS A 115 ? 0.3675 0.4368 0.4539 -0.0158 0.0697  -0.0772 116 HIS A CA  
1000 C C   . HIS A 115 ? 0.4021 0.4569 0.4711 -0.0328 0.0815  -0.0803 116 HIS A C   
1001 O O   . HIS A 115 ? 0.4076 0.4745 0.4842 -0.0424 0.0920  -0.0921 116 HIS A O   
1002 C CB  . HIS A 115 ? 0.3860 0.4599 0.4688 -0.0176 0.0615  -0.0711 116 HIS A CB  
1003 C CG  . HIS A 115 ? 0.4354 0.5270 0.5348 -0.0028 0.0506  -0.0706 116 HIS A CG  
1004 N ND1 . HIS A 115 ? 0.4652 0.5850 0.5906 0.0039  0.0505  -0.0830 116 HIS A ND1 
1005 C CD2 . HIS A 115 ? 0.4594 0.5445 0.5515 0.0056  0.0395  -0.0600 116 HIS A CD2 
1006 C CE1 . HIS A 115 ? 0.4571 0.5850 0.5884 0.0175  0.0378  -0.0784 116 HIS A CE1 
1007 N NE2 . HIS A 115 ? 0.4609 0.5671 0.5711 0.0182  0.0316  -0.0643 116 HIS A NE2 
1008 N N   . VAL A 116 ? 0.3378 0.3671 0.3834 -0.0365 0.0802  -0.0707 117 VAL A N   
1009 C CA  . VAL A 116 ? 0.3462 0.3585 0.3708 -0.0511 0.0893  -0.0725 117 VAL A CA  
1010 C C   . VAL A 116 ? 0.4056 0.4219 0.4384 -0.0525 0.1008  -0.0839 117 VAL A C   
1011 O O   . VAL A 116 ? 0.3862 0.4026 0.4131 -0.0659 0.1126  -0.0927 117 VAL A O   
1012 C CB  . VAL A 116 ? 0.3867 0.3745 0.3864 -0.0532 0.0830  -0.0611 117 VAL A CB  
1013 C CG1 . VAL A 116 ? 0.3997 0.3695 0.3757 -0.0670 0.0911  -0.0635 117 VAL A CG1 
1014 C CG2 . VAL A 116 ? 0.3718 0.3569 0.3647 -0.0527 0.0730  -0.0522 117 VAL A CG2 
1015 N N   . VAL A 117 ? 0.3669 0.3844 0.4118 -0.0392 0.0984  -0.0842 118 VAL A N   
1016 C CA  . VAL A 117 ? 0.3665 0.3879 0.4222 -0.0379 0.1091  -0.0960 118 VAL A CA  
1017 C C   . VAL A 117 ? 0.4344 0.4832 0.5139 -0.0405 0.1178  -0.1115 118 VAL A C   
1018 O O   . VAL A 117 ? 0.4314 0.4815 0.5093 -0.0520 0.1317  -0.1229 118 VAL A O   
1019 C CB  . VAL A 117 ? 0.3989 0.4155 0.4646 -0.0207 0.1041  -0.0936 118 VAL A CB  
1020 C CG1 . VAL A 117 ? 0.4015 0.4224 0.4804 -0.0183 0.1157  -0.1074 118 VAL A CG1 
1021 C CG2 . VAL A 117 ? 0.4027 0.3934 0.4453 -0.0215 0.0984  -0.0810 118 VAL A CG2 
1022 N N   A ASP A 118 ? 0.3995 0.4714 0.5018 -0.0299 0.1098  -0.1132 119 ASP A N   
1023 N N   B ASP A 118 ? 0.3896 0.4605 0.4892 -0.0321 0.1099  -0.1124 119 ASP A N   
1024 C CA  A ASP A 118 ? 0.4019 0.5060 0.5325 -0.0307 0.1159  -0.1296 119 ASP A CA  
1025 C CA  B ASP A 118 ? 0.3856 0.4879 0.5117 -0.0342 0.1161  -0.1282 119 ASP A CA  
1026 C C   A ASP A 118 ? 0.4603 0.5672 0.5816 -0.0533 0.1297  -0.1383 119 ASP A C   
1027 C C   B ASP A 118 ? 0.4202 0.5215 0.5334 -0.0574 0.1296  -0.1354 119 ASP A C   
1028 O O   A ASP A 118 ? 0.4646 0.5905 0.6031 -0.0599 0.1427  -0.1555 119 ASP A O   
1029 O O   B ASP A 118 ? 0.4112 0.5266 0.5368 -0.0656 0.1437  -0.1517 119 ASP A O   
1030 C CB  A ASP A 118 ? 0.4158 0.5418 0.5666 -0.0167 0.1021  -0.1278 119 ASP A CB  
1031 C CB  B ASP A 118 ? 0.4001 0.5233 0.5448 -0.0215 0.1023  -0.1257 119 ASP A CB  
1032 C CG  A ASP A 118 ? 0.5696 0.7004 0.7371 0.0071  0.0912  -0.1260 119 ASP A CG  
1033 C CG  B ASP A 118 ? 0.5570 0.7180 0.7341 -0.0212 0.1064  -0.1438 119 ASP A CG  
1034 O OD1 A ASP A 118 ? 0.6103 0.7440 0.7908 0.0145  0.0971  -0.1353 119 ASP A OD1 
1035 O OD1 B ASP A 118 ? 0.5876 0.7660 0.7883 -0.0138 0.1120  -0.1579 119 ASP A OD1 
1036 O OD2 A ASP A 118 ? 0.6368 0.7669 0.8028 0.0186  0.0769  -0.1155 119 ASP A OD2 
1037 O OD2 B ASP A 118 ? 0.6061 0.7804 0.7861 -0.0283 0.1039  -0.1451 119 ASP A OD2 
1038 N N   A THR A 119 ? 0.4178 0.5045 0.5111 -0.0652 0.1273  -0.1269 120 THR A N   
1039 N N   B THR A 119 ? 0.3712 0.4540 0.4582 -0.0681 0.1261  -0.1240 120 THR A N   
1040 C CA  A THR A 119 ? 0.4287 0.5087 0.5046 -0.0871 0.1393  -0.1319 120 THR A CA  
1041 C CA  B THR A 119 ? 0.3862 0.4611 0.4550 -0.0901 0.1387  -0.1293 120 THR A CA  
1042 C C   A THR A 119 ? 0.4812 0.5398 0.5337 -0.1007 0.1526  -0.1352 120 THR A C   
1043 C C   B THR A 119 ? 0.4615 0.5146 0.5068 -0.1031 0.1518  -0.1324 120 THR A C   
1044 O O   A THR A 119 ? 0.4871 0.5511 0.5384 -0.1168 0.1685  -0.1485 120 THR A O   
1045 O O   B THR A 119 ? 0.4646 0.5175 0.5021 -0.1210 0.1670  -0.1432 120 THR A O   
1046 C CB  A THR A 119 ? 0.5372 0.6005 0.5913 -0.0913 0.1301  -0.1181 120 THR A CB  
1047 C CB  B THR A 119 ? 0.4104 0.4687 0.4567 -0.0966 0.1312  -0.1168 120 THR A CB  
1048 O OG1 A THR A 119 ? 0.5165 0.6014 0.5939 -0.0774 0.1180  -0.1163 120 THR A OG1 
1049 O OG1 B THR A 119 ? 0.4397 0.4961 0.4755 -0.1166 0.1445  -0.1255 120 THR A OG1 
1050 C CG2 A THR A 119 ? 0.5429 0.5985 0.5797 -0.1125 0.1415  -0.1232 120 THR A CG2 
1051 C CG2 B THR A 119 ? 0.3452 0.3692 0.3584 -0.0965 0.1237  -0.1006 120 THR A CG2 
1052 N N   . CYS A 120 ? 0.4314 0.4657 0.4641 -0.0956 0.1467  -0.1239 121 CYS A N   
1053 C CA  . CYS A 120 ? 0.4551 0.4683 0.4638 -0.1072 0.1577  -0.1267 121 CYS A CA  
1054 C C   . CYS A 120 ? 0.5186 0.5521 0.5509 -0.1089 0.1728  -0.1458 121 CYS A C   
1055 O O   . CYS A 120 ? 0.5366 0.5649 0.5555 -0.1271 0.1890  -0.1561 121 CYS A O   
1056 C CB  . CYS A 120 ? 0.4542 0.4466 0.4480 -0.0981 0.1477  -0.1146 121 CYS A CB  
1057 S SG  . CYS A 120 ? 0.5012 0.4674 0.4625 -0.1001 0.1328  -0.0954 121 CYS A SG  
1058 N N   . ARG A 121 ? 0.4657 0.5229 0.5335 -0.0900 0.1677  -0.1513 122 ARG A N   
1059 C CA  . ARG A 121 ? 0.4799 0.5617 0.5782 -0.0866 0.1796  -0.1711 122 ARG A CA  
1060 C C   . ARG A 121 ? 0.5374 0.6424 0.6484 -0.1026 0.1939  -0.1880 122 ARG A C   
1061 O O   . ARG A 121 ? 0.5412 0.6518 0.6551 -0.1149 0.2119  -0.2042 122 ARG A O   
1062 C CB  . ARG A 121 ? 0.4902 0.5929 0.6232 -0.0609 0.1673  -0.1720 122 ARG A CB  
1063 C CG  . ARG A 121 ? 0.6848 0.7659 0.8096 -0.0467 0.1597  -0.1619 122 ARG A CG  
1064 C CD  . ARG A 121 ? 0.8627 0.9613 1.0206 -0.0267 0.1590  -0.1731 122 ARG A CD  
1065 N NE  . ARG A 121 ? 0.9643 1.0595 1.1290 -0.0048 0.1409  -0.1605 122 ARG A NE  
1066 C CZ  . ARG A 121 ? 1.0903 1.1584 1.2395 0.0044  0.1347  -0.1487 122 ARG A CZ  
1067 N NH1 . ARG A 121 ? 0.8308 0.8752 0.9588 -0.0058 0.1440  -0.1483 122 ARG A NH1 
1068 N NH2 . ARG A 121 ? 0.9478 1.0114 1.1006 0.0226  0.1195  -0.1377 122 ARG A NH2 
1069 N N   . LYS A 122 ? 0.4896 0.6073 0.6072 -0.1038 0.1870  -0.1850 123 LYS A N   
1070 C CA  . LYS A 122 ? 0.4920 0.6322 0.6220 -0.1201 0.2001  -0.2011 123 LYS A CA  
1071 C C   . LYS A 122 ? 0.5521 0.6651 0.6434 -0.1479 0.2170  -0.2022 123 LYS A C   
1072 O O   . LYS A 122 ? 0.5392 0.6661 0.6384 -0.1642 0.2362  -0.2212 123 LYS A O   
1073 C CB  . LYS A 122 ? 0.5067 0.6637 0.6498 -0.1148 0.1875  -0.1964 123 LYS A CB  
1074 C CG  . LYS A 122 ? 0.7219 0.9131 0.9069 -0.0899 0.1737  -0.2012 123 LYS A CG  
1075 C CD  . LYS A 122 ? 0.8487 1.0602 1.0470 -0.0878 0.1634  -0.2003 123 LYS A CD  
1076 C CE  . LYS A 122 ? 0.9476 1.1754 1.1686 -0.0608 0.1426  -0.1938 123 LYS A CE  
1077 N NZ  . LYS A 122 ? 1.0280 1.2899 1.2896 -0.0442 0.1421  -0.2111 123 LYS A NZ  
1078 N N   . PHE A 123 ? 0.5258 0.5995 0.5743 -0.1531 0.2097  -0.1825 124 PHE A N   
1079 C CA  . PHE A 123 ? 0.5584 0.5986 0.5622 -0.1772 0.2223  -0.1801 124 PHE A CA  
1080 C C   . PHE A 123 ? 0.6276 0.6577 0.6192 -0.1868 0.2378  -0.1898 124 PHE A C   
1081 O O   . PHE A 123 ? 0.6389 0.6585 0.6096 -0.2097 0.2567  -0.2000 124 PHE A O   
1082 C CB  . PHE A 123 ? 0.5887 0.5921 0.5538 -0.1754 0.2070  -0.1570 124 PHE A CB  
1083 C CG  . PHE A 123 ? 0.6153 0.6143 0.5729 -0.1795 0.2007  -0.1497 124 PHE A CG  
1084 C CD1 . PHE A 123 ? 0.6312 0.6629 0.6257 -0.1686 0.1934  -0.1539 124 PHE A CD1 
1085 C CD2 . PHE A 123 ? 0.6729 0.6332 0.5851 -0.1926 0.2004  -0.1382 124 PHE A CD2 
1086 C CE1 . PHE A 123 ? 0.6334 0.6605 0.6205 -0.1732 0.1883  -0.1482 124 PHE A CE1 
1087 C CE2 . PHE A 123 ? 0.6962 0.6499 0.6012 -0.1956 0.1948  -0.1318 124 PHE A CE2 
1088 C CZ  . PHE A 123 ? 0.6370 0.6246 0.5799 -0.1867 0.1896  -0.1373 124 PHE A CZ  
1089 N N   . ILE A 124 ? 0.5665 0.5995 0.5707 -0.1703 0.2313  -0.1881 125 ILE A N   
1090 C CA  . ILE A 124 ? 0.5949 0.6207 0.5915 -0.1773 0.2456  -0.1987 125 ILE A CA  
1091 C C   . ILE A 124 ? 0.6628 0.7232 0.6947 -0.1838 0.2652  -0.2250 125 ILE A C   
1092 O O   . ILE A 124 ? 0.6828 0.7349 0.6977 -0.2039 0.2854  -0.2377 125 ILE A O   
1093 C CB  . ILE A 124 ? 0.6213 0.6389 0.6215 -0.1581 0.2333  -0.1899 125 ILE A CB  
1094 C CG1 . ILE A 124 ? 0.6301 0.6111 0.5883 -0.1593 0.2196  -0.1684 125 ILE A CG1 
1095 C CG2 . ILE A 124 ? 0.6575 0.6768 0.6628 -0.1618 0.2491  -0.2055 125 ILE A CG2 
1096 C CD1 . ILE A 124 ? 0.6865 0.6636 0.6530 -0.1388 0.2029  -0.1567 125 ILE A CD1 
1097 N N   . LYS A 125 ? 0.6188 0.7183 0.6990 -0.1672 0.2589  -0.2338 126 LYS A N   
1098 C CA  . LYS A 125 ? 0.6292 0.7696 0.7519 -0.1691 0.2742  -0.2606 126 LYS A CA  
1099 C C   . LYS A 125 ? 0.7041 0.8497 0.8168 -0.1978 0.2941  -0.2744 126 LYS A C   
1100 O O   . LYS A 125 ? 0.7081 0.8729 0.8366 -0.2108 0.3153  -0.2977 126 LYS A O   
1101 C CB  . LYS A 125 ? 0.6418 0.8208 0.8141 -0.1431 0.2583  -0.2643 126 LYS A CB  
1102 C CG  . LYS A 125 ? 0.8503 1.0729 1.0726 -0.1358 0.2691  -0.2918 126 LYS A CG  
1103 C CD  . LYS A 125 ? 0.9818 1.2444 1.2494 -0.1140 0.2530  -0.2967 126 LYS A CD  
1104 C CE  . LYS A 125 ? 1.1383 1.4493 1.4581 -0.1083 0.2637  -0.3270 126 LYS A CE  
1105 N NZ  . LYS A 125 ? 1.2406 1.5926 1.6023 -0.0894 0.2474  -0.3330 126 LYS A NZ  
1106 N N   . ALA A 126 ? 0.6662 0.7925 0.7510 -0.2083 0.2885  -0.2605 127 ALA A N   
1107 C CA  . ALA A 126 ? 0.6904 0.8131 0.7582 -0.2369 0.3072  -0.2709 127 ALA A CA  
1108 C C   . ALA A 126 ? 0.7987 0.8841 0.8182 -0.2629 0.3275  -0.2731 127 ALA A C   
1109 O O   . ALA A 126 ? 0.8120 0.9015 0.8256 -0.2881 0.3506  -0.2905 127 ALA A O   
1110 C CB  . ALA A 126 ? 0.6888 0.7942 0.7357 -0.2389 0.2942  -0.2534 127 ALA A CB  
1111 N N   . SER A 127 ? 0.8016 0.8508 0.7857 -0.2576 0.3192  -0.2561 128 SER A N   
1112 C CA  . SER A 127 ? 0.8664 0.8764 0.7994 -0.2799 0.3346  -0.2554 128 SER A CA  
1113 C C   . SER A 127 ? 0.9584 0.9832 0.9065 -0.2853 0.3538  -0.2766 128 SER A C   
1114 O O   . SER A 127 ? 1.0075 1.0056 0.9160 -0.3089 0.3723  -0.2820 128 SER A O   
1115 C CB  . SER A 127 ? 0.9407 0.9067 0.8282 -0.2723 0.3157  -0.2288 128 SER A CB  
1116 O OG  . SER A 127 ? 1.1040 1.0392 0.9533 -0.2819 0.3091  -0.2132 128 SER A OG  
1117 N N   . GLU A 128 ? 0.8858 0.9508 0.8886 -0.2636 0.3497  -0.2888 129 GLU A N   
1118 C CA  . GLU A 128 ? 1.2008 1.2823 1.2237 -0.2654 0.3671  -0.3103 129 GLU A CA  
1119 C C   . GLU A 128 ? 1.7173 1.8317 1.7663 -0.2855 0.3941  -0.3405 129 GLU A C   
1120 O O   . GLU A 128 ? 1.3220 1.4177 1.3367 -0.3144 0.4115  -0.3445 129 GLU A O   
1121 C CB  . GLU A 128 ? 1.1856 1.2909 1.2524 -0.2330 0.3516  -0.3106 129 GLU A CB  
1122 C CG  . GLU A 128 ? 1.2795 1.4353 1.4083 -0.2137 0.3449  -0.3238 129 GLU A CG  
1123 C CD  . GLU A 128 ? 1.5266 1.6987 1.6921 -0.1797 0.3261  -0.3200 129 GLU A CD  
1124 O OE1 . GLU A 128 ? 1.4679 1.6094 1.6096 -0.1688 0.3133  -0.3014 129 GLU A OE1 
1125 O OE2 . GLU A 128 ? 1.4165 1.6315 1.6341 -0.1639 0.3237  -0.3360 129 GLU A OE2 
1129 N N   A TRP B 2   ? 0.2654 0.4981 0.3482 -0.0533 -0.0132 -0.0920 1   TRP D N   
1130 N N   B TRP B 2   ? 0.2710 0.5037 0.3539 -0.0532 -0.0132 -0.0920 1   TRP D N   
1131 C CA  A TRP B 2   ? 0.2586 0.4922 0.3426 -0.0530 -0.0123 -0.0926 1   TRP D CA  
1132 C CA  B TRP B 2   ? 0.2659 0.4995 0.3500 -0.0530 -0.0123 -0.0926 1   TRP D CA  
1133 C C   A TRP B 2   ? 0.3140 0.5474 0.3991 -0.0535 -0.0118 -0.0922 1   TRP D C   
1134 C C   B TRP B 2   ? 0.3077 0.5411 0.3928 -0.0535 -0.0118 -0.0922 1   TRP D C   
1135 O O   A TRP B 2   ? 0.3158 0.5482 0.4006 -0.0536 -0.0122 -0.0919 1   TRP D O   
1136 O O   B TRP B 2   ? 0.3025 0.5349 0.3872 -0.0538 -0.0121 -0.0919 1   TRP D O   
1137 C CB  A TRP B 2   ? 0.2476 0.4811 0.3320 -0.0524 -0.0129 -0.0934 1   TRP D CB  
1138 C CB  B TRP B 2   ? 0.2526 0.4860 0.3371 -0.0525 -0.0129 -0.0933 1   TRP D CB  
1139 C CG  A TRP B 2   ? 0.2542 0.4879 0.3385 -0.0520 -0.0132 -0.0947 1   TRP D CG  
1140 C CG  B TRP B 2   ? 0.2655 0.4986 0.3507 -0.0526 -0.0135 -0.0930 1   TRP D CG  
1141 C CD1 A TRP B 2   ? 0.2881 0.5213 0.3730 -0.0516 -0.0145 -0.0950 1   TRP D CD1 
1142 C CD1 B TRP B 2   ? 0.3041 0.5368 0.3902 -0.0526 -0.0142 -0.0932 1   TRP D CD1 
1143 C CD2 A TRP B 2   ? 0.2491 0.4835 0.3330 -0.0519 -0.0121 -0.0963 1   TRP D CD2 
1144 C CD2 B TRP B 2   ? 0.2634 0.4969 0.3490 -0.0530 -0.0133 -0.0926 1   TRP D CD2 
1145 N NE1 A TRP B 2   ? 0.2747 0.5085 0.3600 -0.0512 -0.0145 -0.0969 1   TRP D NE1 
1146 N NE1 B TRP B 2   ? 0.2977 0.5309 0.3849 -0.0529 -0.0140 -0.0932 1   TRP D NE1 
1147 C CE2 A TRP B 2   ? 0.2915 0.5260 0.3759 -0.0514 -0.0128 -0.0979 1   TRP D CE2 
1148 C CE2 B TRP B 2   ? 0.3147 0.5484 0.4012 -0.0532 -0.0135 -0.0928 1   TRP D CE2 
1149 C CE3 A TRP B 2   ? 0.2546 0.4893 0.3381 -0.0521 -0.0106 -0.0965 1   TRP D CE3 
1150 C CE3 B TRP B 2   ? 0.2773 0.5110 0.3630 -0.0531 -0.0131 -0.0921 1   TRP D CE3 
1151 C CZ2 A TRP B 2   ? 0.2733 0.5083 0.3574 -0.0512 -0.0117 -0.1003 1   TRP D CZ2 
1152 C CZ2 B TRP B 2   ? 0.3034 0.5381 0.3905 -0.0536 -0.0134 -0.0927 1   TRP D CZ2 
1153 C CZ3 A TRP B 2   ? 0.2647 0.4997 0.3476 -0.0520 -0.0095 -0.0985 1   TRP D CZ3 
1154 C CZ3 B TRP B 2   ? 0.2984 0.5326 0.3849 -0.0534 -0.0136 -0.0917 1   TRP D CZ3 
1155 C CH2 A TRP B 2   ? 0.2752 0.5105 0.3582 -0.0516 -0.0098 -0.1006 1   TRP D CH2 
1156 C CH2 B TRP B 2   ? 0.3049 0.5397 0.3917 -0.0537 -0.0137 -0.0920 1   TRP D CH2 
1157 N N   . VAL B 3   ? 0.2543 0.4884 0.3410 -0.0537 -0.0110 -0.0924 2   VAL D N   
1158 C CA  . VAL B 3   ? 0.2453 0.4794 0.3343 -0.0540 -0.0109 -0.0924 2   VAL D CA  
1159 C C   . VAL B 3   ? 0.2709 0.5053 0.3616 -0.0535 -0.0112 -0.0919 2   VAL D C   
1160 O O   . VAL B 3   ? 0.2477 0.4822 0.3376 -0.0533 -0.0109 -0.0918 2   VAL D O   
1161 C CB  . VAL B 3   ? 0.2826 0.5173 0.3736 -0.0555 -0.0095 -0.0933 2   VAL D CB  
1162 C CG1 . VAL B 3   ? 0.2892 0.5231 0.3774 -0.0567 -0.0093 -0.0935 2   VAL D CG1 
1163 C CG2 . VAL B 3   ? 0.2721 0.5086 0.3651 -0.0560 -0.0080 -0.0939 2   VAL D CG2 
1164 N N   . ILE B 4   ? 0.2405 0.4746 0.3335 -0.0535 -0.0119 -0.0917 3   ILE D N   
1165 C CA  . ILE B 4   ? 0.2450 0.4790 0.3403 -0.0532 -0.0128 -0.0908 3   ILE D CA  
1166 C C   . ILE B 4   ? 0.2800 0.5148 0.3799 -0.0538 -0.0114 -0.0916 3   ILE D C   
1167 O O   . ILE B 4   ? 0.2636 0.4988 0.3665 -0.0546 -0.0109 -0.0930 3   ILE D O   
1168 C CB  . ILE B 4   ? 0.2699 0.5036 0.3665 -0.0530 -0.0145 -0.0903 3   ILE D CB  
1169 C CG1 . ILE B 4   ? 0.2583 0.4922 0.3513 -0.0530 -0.0152 -0.0900 3   ILE D CG1 
1170 C CG2 . ILE B 4   ? 0.2812 0.5144 0.3803 -0.0527 -0.0161 -0.0888 3   ILE D CG2 
1171 C CD1 . ILE B 4   ? 0.2991 0.5328 0.3884 -0.0535 -0.0155 -0.0892 3   ILE D CD1 
1172 N N   . PRO B 5   ? 0.2750 0.5103 0.3756 -0.0537 -0.0104 -0.0914 4   PRO D N   
1173 C CA  . PRO B 5   ? 0.2812 0.5181 0.3873 -0.0546 -0.0085 -0.0927 4   PRO D CA  
1174 C C   . PRO B 5   ? 0.3454 0.5820 0.4580 -0.0547 -0.0096 -0.0926 4   PRO D C   
1175 O O   . PRO B 5   ? 0.3365 0.5715 0.4488 -0.0537 -0.0119 -0.0907 4   PRO D O   
1176 C CB  . PRO B 5   ? 0.3037 0.5412 0.4087 -0.0543 -0.0070 -0.0925 4   PRO D CB  
1177 C CG  . PRO B 5   ? 0.3469 0.5822 0.4473 -0.0534 -0.0088 -0.0909 4   PRO D CG  
1178 C CD  . PRO B 5   ? 0.2927 0.5272 0.3897 -0.0532 -0.0105 -0.0906 4   PRO D CD  
1179 N N   . ALA B 6   ? 0.3157 0.5542 0.4348 -0.0561 -0.0078 -0.0947 5   ALA D N   
# 
