data_7GUF
# 
_entry.id   7GUF 
# 
_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   7GUF         pdb_00007guf 10.2210/pdb7guf/pdb 
WWPDB D_1001406650 ?            ?                   
# 
_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                        7GUF 
_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 15  HOH HOH A . 
F 6 HOH 3   303 84  HOH HOH A . 
F 6 HOH 4   304 88  HOH HOH A . 
F 6 HOH 5   305 114 HOH HOH A . 
F 6 HOH 6   306 166 HOH HOH A . 
F 6 HOH 7   307 81  HOH HOH A . 
F 6 HOH 8   308 159 HOH HOH A . 
F 6 HOH 9   309 149 HOH HOH A . 
F 6 HOH 10  310 92  HOH HOH A . 
F 6 HOH 11  311 189 HOH HOH A . 
F 6 HOH 12  312 130 HOH HOH A . 
F 6 HOH 13  313 23  HOH HOH A . 
F 6 HOH 14  314 187 HOH HOH A . 
F 6 HOH 15  315 83  HOH HOH A . 
F 6 HOH 16  316 85  HOH HOH A . 
F 6 HOH 17  317 87  HOH HOH A . 
F 6 HOH 18  318 32  HOH HOH A . 
F 6 HOH 19  319 44  HOH HOH A . 
F 6 HOH 20  320 5   HOH HOH A . 
F 6 HOH 21  321 24  HOH HOH A . 
F 6 HOH 22  322 230 HOH HOH A . 
F 6 HOH 23  323 113 HOH HOH A . 
F 6 HOH 24  324 103 HOH HOH A . 
F 6 HOH 25  325 14  HOH HOH A . 
F 6 HOH 26  326 196 HOH HOH A . 
F 6 HOH 27  327 3   HOH HOH A . 
F 6 HOH 28  328 143 HOH HOH A . 
F 6 HOH 29  329 109 HOH HOH A . 
F 6 HOH 30  330 165 HOH HOH A . 
F 6 HOH 31  331 135 HOH HOH A . 
F 6 HOH 32  332 63  HOH HOH A . 
F 6 HOH 33  333 50  HOH HOH A . 
F 6 HOH 34  334 13  HOH HOH A . 
F 6 HOH 35  335 33  HOH HOH A . 
F 6 HOH 36  336 97  HOH HOH A . 
F 6 HOH 37  337 134 HOH HOH A . 
F 6 HOH 38  338 100 HOH HOH A . 
F 6 HOH 39  339 112 HOH HOH A . 
F 6 HOH 40  340 11  HOH HOH A . 
F 6 HOH 41  341 117 HOH HOH A . 
F 6 HOH 42  342 213 HOH HOH A . 
F 6 HOH 43  343 94  HOH HOH A . 
F 6 HOH 44  344 184 HOH HOH A . 
F 6 HOH 45  345 35  HOH HOH A . 
F 6 HOH 46  346 141 HOH HOH A . 
F 6 HOH 47  347 136 HOH HOH A . 
F 6 HOH 48  348 18  HOH HOH A . 
F 6 HOH 49  349 90  HOH HOH A . 
F 6 HOH 50  350 180 HOH HOH A . 
F 6 HOH 51  351 51  HOH HOH A . 
F 6 HOH 52  352 110 HOH HOH A . 
F 6 HOH 53  353 86  HOH HOH A . 
F 6 HOH 54  354 119 HOH HOH A . 
F 6 HOH 55  355 116 HOH HOH A . 
F 6 HOH 56  356 123 HOH HOH A . 
F 6 HOH 57  357 115 HOH HOH A . 
F 6 HOH 58  358 121 HOH HOH A . 
F 6 HOH 59  359 26  HOH HOH A . 
F 6 HOH 60  360 246 HOH HOH A . 
F 6 HOH 61  361 74  HOH HOH A . 
F 6 HOH 62  362 102 HOH HOH A . 
F 6 HOH 63  363 192 HOH HOH A . 
F 6 HOH 64  364 89  HOH HOH A . 
F 6 HOH 65  365 95  HOH HOH A . 
F 6 HOH 66  366 49  HOH HOH A . 
F 6 HOH 67  367 231 HOH HOH A . 
F 6 HOH 68  368 25  HOH HOH A . 
F 6 HOH 69  369 147 HOH HOH A . 
F 6 HOH 70  370 150 HOH HOH A . 
F 6 HOH 71  371 151 HOH HOH A . 
F 6 HOH 72  372 101 HOH HOH A . 
F 6 HOH 73  373 164 HOH HOH A . 
F 6 HOH 74  374 6   HOH HOH A . 
F 6 HOH 75  375 62  HOH HOH A . 
F 6 HOH 76  376 20  HOH HOH A . 
F 6 HOH 77  377 66  HOH HOH A . 
F 6 HOH 78  378 168 HOH HOH A . 
F 6 HOH 79  379 28  HOH HOH A . 
F 6 HOH 80  380 29  HOH HOH A . 
F 6 HOH 81  381 105 HOH HOH A . 
F 6 HOH 82  382 178 HOH HOH A . 
F 6 HOH 83  383 244 HOH HOH A . 
F 6 HOH 84  384 238 HOH HOH A . 
F 6 HOH 85  385 22  HOH HOH A . 
F 6 HOH 86  386 107 HOH HOH A . 
F 6 HOH 87  387 57  HOH HOH A . 
F 6 HOH 88  388 10  HOH HOH A . 
F 6 HOH 89  389 99  HOH HOH A . 
F 6 HOH 90  390 21  HOH HOH A . 
F 6 HOH 91  391 82  HOH HOH A . 
F 6 HOH 92  392 60  HOH HOH A . 
F 6 HOH 93  393 40  HOH HOH A . 
F 6 HOH 94  394 104 HOH HOH A . 
F 6 HOH 95  395 39  HOH HOH A . 
F 6 HOH 96  396 203 HOH HOH A . 
F 6 HOH 97  397 93  HOH HOH A . 
F 6 HOH 98  398 193 HOH HOH A . 
F 6 HOH 99  399 56  HOH HOH A . 
F 6 HOH 100 400 36  HOH HOH A . 
F 6 HOH 101 401 27  HOH HOH A . 
F 6 HOH 102 402 242 HOH HOH A . 
F 6 HOH 103 403 53  HOH HOH A . 
F 6 HOH 104 404 75  HOH HOH A . 
F 6 HOH 105 405 17  HOH HOH A . 
F 6 HOH 106 406 38  HOH HOH A . 
F 6 HOH 107 407 30  HOH HOH A . 
F 6 HOH 108 408 37  HOH HOH A . 
F 6 HOH 109 409 239 HOH HOH A . 
F 6 HOH 110 410 171 HOH HOH A . 
F 6 HOH 111 411 167 HOH HOH A . 
F 6 HOH 112 412 52  HOH HOH A . 
F 6 HOH 113 413 45  HOH HOH A . 
F 6 HOH 114 414 209 HOH HOH A . 
F 6 HOH 115 415 96  HOH HOH A . 
F 6 HOH 116 416 79  HOH HOH A . 
F 6 HOH 117 417 237 HOH HOH A . 
F 6 HOH 118 418 54  HOH HOH A . 
F 6 HOH 119 419 69  HOH HOH A . 
F 6 HOH 120 420 186 HOH HOH A . 
F 6 HOH 121 421 176 HOH HOH A . 
F 6 HOH 122 422 145 HOH HOH A . 
F 6 HOH 123 423 55  HOH HOH A . 
F 6 HOH 124 424 200 HOH HOH A . 
F 6 HOH 125 425 241 HOH HOH A . 
F 6 HOH 126 426 31  HOH HOH A . 
F 6 HOH 127 427 148 HOH HOH A . 
F 6 HOH 128 428 146 HOH HOH A . 
F 6 HOH 129 429 153 HOH HOH A . 
F 6 HOH 130 430 98  HOH HOH A . 
F 6 HOH 131 431 139 HOH HOH A . 
F 6 HOH 132 432 43  HOH HOH A . 
F 6 HOH 133 433 185 HOH HOH A . 
F 6 HOH 134 434 106 HOH HOH A . 
F 6 HOH 135 435 191 HOH HOH A . 
F 6 HOH 136 436 158 HOH HOH A . 
F 6 HOH 137 437 188 HOH HOH A . 
F 6 HOH 138 438 232 HOH HOH A . 
F 6 HOH 139 439 76  HOH HOH A . 
F 6 HOH 140 440 80  HOH HOH A . 
F 6 HOH 141 441 204 HOH HOH A . 
F 6 HOH 142 442 111 HOH HOH A . 
F 6 HOH 143 443 137 HOH HOH A . 
F 6 HOH 144 444 108 HOH HOH A . 
F 6 HOH 145 445 140 HOH HOH A . 
F 6 HOH 146 446 206 HOH HOH A . 
F 6 HOH 147 447 247 HOH HOH A . 
F 6 HOH 148 448 169 HOH HOH A . 
F 6 HOH 149 449 221 HOH HOH A . 
F 6 HOH 150 450 212 HOH HOH A . 
F 6 HOH 151 451 70  HOH HOH A . 
F 6 HOH 152 452 161 HOH HOH A . 
F 6 HOH 153 453 228 HOH HOH A . 
F 6 HOH 154 454 243 HOH HOH A . 
F 6 HOH 155 455 131 HOH HOH A . 
F 6 HOH 156 456 215 HOH HOH A . 
F 6 HOH 157 457 183 HOH HOH A . 
F 6 HOH 158 458 142 HOH HOH A . 
F 6 HOH 159 459 73  HOH HOH A . 
F 6 HOH 160 460 59  HOH HOH A . 
F 6 HOH 161 461 170 HOH HOH A . 
F 6 HOH 162 462 245 HOH HOH A . 
F 6 HOH 163 463 65  HOH HOH A . 
F 6 HOH 164 464 179 HOH HOH A . 
F 6 HOH 165 465 175 HOH HOH A . 
F 6 HOH 166 466 181 HOH HOH A . 
F 6 HOH 167 467 152 HOH HOH A . 
F 6 HOH 168 468 195 HOH HOH A . 
F 6 HOH 169 469 61  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 47  HOH HOH D . 
G 6 HOH 4   204 58  HOH HOH D . 
G 6 HOH 5   205 68  HOH HOH D . 
G 6 HOH 6   206 240 HOH HOH D . 
G 6 HOH 7   207 220 HOH HOH D . 
G 6 HOH 8   208 210 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 64  ? CD  ? A GLN 63  CD  
2  1 Y 1 A GLN 64  ? OE1 ? A GLN 63  OE1 
3  1 Y 1 A GLN 64  ? NE2 ? A GLN 63  NE2 
4  1 Y 1 A GLU 115 ? CD  ? A GLU 114 CD  
5  1 Y 1 A GLU 115 ? OE1 ? A GLU 114 OE1 
6  1 Y 1 A GLU 115 ? OE2 ? A GLU 114 OE2 
7  1 Y 1 D ALA 5   ? CA  ? B ALA 6   CA  
8  1 Y 1 D ALA 5   ? C   ? B ALA 6   C   
9  1 Y 1 D ALA 5   ? O   ? B ALA 6   O   
10 1 Y 1 D ALA 5   ? CB  ? B ALA 6   CB  
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
4 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com phasing           
http://www.globalphasing.com/buster/                ?   ? 
5 PDB_EXTRACT 3.24   'Sep. 1, 2017' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.entry_id           7GUF 
_cell.length_a           67.540 
_cell.length_b           67.540 
_cell.length_c           166.120 
_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                         7GUF 
_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          7GUF 
_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   65.93 
_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                     7GUF 
_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                   21679 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.085 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.200 
_reflns.B_iso_Wilson_estimate        26.890 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.091 
_reflns.pdbx_Rpim_I_all              0.030 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     196984 
_reflns.pdbx_scaling_rejects         825 
_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  ? 11591 1244 ? 0.594 ? ? ? 9.300 ? 3.400  ? ? ? ? ? ? 100.000 0.629 0.203 0.943 ? 
1 2 9.000 33.860 ? 1540  226  ? 0.071 ? ? ? 6.800 ? 22.600 ? ? ? ? ? ? 98.700  0.076 0.028 0.998 ? 
# 
_refine.entry_id                                 7GUF 
_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                    100.0000 
_refine.ls_number_reflns_obs                     21623 
_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                       0.2020 
_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                               32.0400 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.6743 
_refine.aniso_B[2][2]                            -0.6743 
_refine.aniso_B[3][3]                            1.3486 
_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               0.9570 
_refine.correlation_coeff_Fo_to_Fc_free          0.9480 
_refine.overall_SU_R_Cruickshank_DPI             0.0940 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0910 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1080 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.1000 
_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                                119.750 
_refine.B_iso_min                                14.520 
_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                        7GUF 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.220 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.8000 
_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           26.88 
_refine_hist.pdbx_B_iso_mean_solvent          48.39 
_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      1651 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1236 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1693 0.920  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.470  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    16.330 ? ?      ?            
# 
_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               99.9600 
_refine_ls_shell.number_reflns_R_work             2688 
_refine_ls_shell.R_factor_all                     0.2540 
_refine_ls_shell.R_factor_R_work                  0.2544 
_refine_ls_shell.R_factor_R_free                  0.2458 
_refine_ls_shell.percent_reflns_R_free            4.6100 
_refine_ls_shell.number_reflns_R_free             130 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2818 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUF 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 1 at 4.53 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUF 
_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 7GUF       7GUF   ? 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 7GUF A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUF D 1 ? 6   ? 7GUF   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 7GUF GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUF PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUF 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)' 6370  ? 
1 MORE         -68   ? 
1 'SSA (A^2)'  13250 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z          1.0000000000 0.0000000000 0.0000000000 0.0000000000  0.0000000000 
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 12_545 x,x-y-1,-z+1/6 0.5000000000 0.8660254038 0.0000000000 33.7700000000 0.8660254038 
-0.5000000000 0.0000000000 -58.4913557716 0.0000000000 0.0000000000 -1.0000000000 27.6866666667 
# 
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 ? ? ? ? ? ? ? 1.329 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 ACE B 1 ? TRP B 2 A ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
2 ACE B 1 ? TRP B 2 B ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 40 ? ALA A 44 ? GLU A 41 ALA A 45 
AA1 2 VAL A 33 ? VAL A 37 ? VAL A 34 VAL A 38 
AA1 3 VAL A 70 ? ASN A 72 ? VAL A 71 ASN A 73 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 40 ? O GLU A 41 N VAL A 37 ? N VAL A 38 
AA1 2 3 N VAL A 36 ? N VAL A 37 O ILE A 71 ? O ILE A 72 
# 
_pdbx_entry_details.entry_id                   7GUF 
_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 36.79 48.55   
2 1 SER A 39  ? B 62.33 -108.37 
3 1 SER A 93  ? ? 75.99 -1.48   
4 1 GLN A 113 ? ? 63.44 61.83   
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             VAL 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              38 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   11.18 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 330 ? F HOH . 
2 1 A HOH 373 ? F HOH . 
3 1 A HOH 448 ? F HOH . 
4 1 A HOH 464 ? F HOH . 
5 1 A HOH 465 ? F HOH . 
6 1 A HOH 468 ? 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 0.0061  -0.0517 -0.0681 -0.0391 0.0250  -0.0166 0.9550 1.8089  2.1518 
0.4103 -0.2856 1.1752 0.1387 -0.0889 -0.0498 -0.0522 0.0873 0.0740 0.2552  0.0165 -0.0502 
'X-RAY DIFFRACTION' 2 ? refined 18.9623 -32.3913 1.8231  -0.0922 0.1169  -0.0465 -0.0526 -0.0153 -0.0760 0.6527 -0.0059 0.0000 
0.1833 -0.0428 0.0985 0.0130 0.0024  -0.0154 -0.0061 0.0215 0.0370 -0.0028 0.0120 -0.0012 
# 
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                    7GUF 
_atom_sites.fract_transf_matrix[1][1]   0.014806 
_atom_sites.fract_transf_matrix[1][2]   0.008548 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017097 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006020 
_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   ? 17.561 -21.094 -4.899 1.00 62.20  ? 6   ASP A N   1 
ATOM   2    C  CA  . ASP A 1 5   ? 18.402 -22.028 -5.652 1.00 61.24  ? 6   ASP A CA  1 
ATOM   3    C  C   . ASP A 1 5   ? 17.881 -23.480 -5.540 1.00 61.24  ? 6   ASP A C   1 
ATOM   4    O  O   . ASP A 1 5   ? 16.799 -23.712 -4.989 1.00 62.07  ? 6   ASP A O   1 
ATOM   5    C  CB  . ASP A 1 5   ? 19.872 -21.930 -5.169 1.00 62.00  ? 6   ASP A CB  1 
ATOM   6    C  CG  . ASP A 1 5   ? 20.910 -22.037 -6.278 1.00 75.62  ? 6   ASP A CG  1 
ATOM   7    O  OD1 . ASP A 1 5   ? 20.951 -23.092 -6.960 1.00 76.22  ? 6   ASP A OD1 1 
ATOM   8    O  OD2 . ASP A 1 5   ? 21.693 -21.077 -6.453 1.00 82.61  ? 6   ASP A OD2 1 
ATOM   9    N  N   . SER A 1 6   ? 18.650 -24.444 -6.079 1.00 52.51  ? 7   SER A N   1 
ATOM   10   C  CA  . SER A 1 6   ? 18.353 -25.874 -6.045 1.00 49.87  ? 7   SER A CA  1 
ATOM   11   C  C   . SER A 1 6   ? 19.354 -26.619 -5.103 1.00 45.55  ? 7   SER A C   1 
ATOM   12   O  O   . SER A 1 6   ? 19.653 -27.797 -5.316 1.00 45.12  ? 7   SER A O   1 
ATOM   13   C  CB  . SER A 1 6   ? 18.400 -26.445 -7.457 1.00 55.65  ? 7   SER A CB  1 
ATOM   14   O  OG  . SER A 1 6   ? 19.680 -26.270 -8.044 1.00 67.59  ? 7   SER A OG  1 
ATOM   15   N  N   . CYS A 1 7   ? 19.848 -25.935 -4.055 1.00 35.76  ? 8   CYS A N   1 
ATOM   16   C  CA  . CYS A 1 7   ? 20.799 -26.536 -3.112 1.00 32.12  ? 8   CYS A CA  1 
ATOM   17   C  C   . CYS A 1 7   ? 20.171 -27.699 -2.319 1.00 32.91  ? 8   CYS A C   1 
ATOM   18   O  O   . CYS A 1 7   ? 18.957 -27.738 -2.130 1.00 32.89  ? 8   CYS A O   1 
ATOM   19   C  CB  . CYS A 1 7   ? 21.324 -25.471 -2.146 1.00 32.56  ? 8   CYS A CB  1 
ATOM   20   S  SG  . CYS A 1 7   ? 22.434 -24.239 -2.891 1.00 37.18  ? 8   CYS A SG  1 
ATOM   21   N  N   . ILE A 1 8   ? 21.004 -28.607 -1.813 1.00 25.19  ? 9   ILE A N   1 
ATOM   22   C  CA  . ILE A 1 8   ? 20.626 -29.597 -0.803 1.00 22.49  ? 9   ILE A CA  1 
ATOM   23   C  C   . ILE A 1 8   ? 21.241 -29.059 0.492  1.00 24.25  ? 9   ILE A C   1 
ATOM   24   O  O   . ILE A 1 8   ? 22.189 -28.272 0.438  1.00 23.51  ? 9   ILE A O   1 
ATOM   25   C  CB  . ILE A 1 8   ? 20.991 -31.072 -1.114 1.00 25.54  ? 9   ILE A CB  1 
ATOM   26   C  CG1 . ILE A 1 8   ? 22.514 -31.246 -1.380 1.00 25.39  ? 9   ILE A CG1 1 
ATOM   27   C  CG2 . ILE A 1 8   ? 20.140 -31.592 -2.284 1.00 26.43  ? 9   ILE A CG2 1 
ATOM   28   C  CD1 . ILE A 1 8   ? 23.030 -32.693 -1.538 1.00 29.81  ? 9   ILE A CD1 1 
ATOM   29   N  N   A GLN A 1 9   ? 20.760 -29.497 1.653  0.57 19.57  ? 10  GLN A N   1 
ATOM   30   N  N   B GLN A 1 9   ? 20.663 -29.427 1.636  0.43 19.51  ? 10  GLN A N   1 
ATOM   31   C  CA  A GLN A 1 9   ? 21.291 -28.985 2.918  0.57 18.82  ? 10  GLN A CA  1 
ATOM   32   C  CA  B GLN A 1 9   ? 21.095 -28.950 2.948  0.43 18.46  ? 10  GLN A CA  1 
ATOM   33   C  C   A GLN A 1 9   ? 21.602 -30.114 3.896  0.57 22.64  ? 10  GLN A C   1 
ATOM   34   C  C   B GLN A 1 9   ? 21.567 -30.102 3.822  0.43 21.03  ? 10  GLN A C   1 
ATOM   35   O  O   A GLN A 1 9   ? 20.777 -31.011 4.078  0.57 22.69  ? 10  GLN A O   1 
ATOM   36   O  O   B GLN A 1 9   ? 20.961 -31.173 3.818  0.43 20.76  ? 10  GLN A O   1 
ATOM   37   C  CB  A GLN A 1 9   ? 20.282 -27.981 3.531  0.57 20.36  ? 10  GLN A CB  1 
ATOM   38   C  CB  B GLN A 1 9   ? 19.927 -28.193 3.632  0.43 19.79  ? 10  GLN A CB  1 
ATOM   39   C  CG  A GLN A 1 9   ? 20.696 -27.388 4.881  0.57 20.41  ? 10  GLN A CG  1 
ATOM   40   C  CG  B GLN A 1 9   ? 20.126 -27.902 5.141  0.43 27.28  ? 10  GLN A CG  1 
ATOM   41   C  CD  A GLN A 1 9   ? 19.549 -26.680 5.559  0.57 47.00  ? 10  GLN A CD  1 
ATOM   42   C  CD  B GLN A 1 9   ? 20.098 -26.443 5.523  0.43 36.09  ? 10  GLN A CD  1 
ATOM   43   O  OE1 A GLN A 1 9   ? 18.568 -27.290 5.997  0.57 38.99  ? 10  GLN A OE1 1 
ATOM   44   O  OE1 B GLN A 1 9   ? 19.787 -25.549 4.718  0.43 24.83  ? 10  GLN A OE1 1 
ATOM   45   N  NE2 A GLN A 1 9   ? 19.649 -25.367 5.665  0.57 50.36  ? 10  GLN A NE2 1 
ATOM   46   N  NE2 B GLN A 1 9   ? 20.424 -26.174 6.783  0.43 25.36  ? 10  GLN A NE2 1 
ATOM   47   N  N   A PHE A 1 10  ? 22.778 -30.055 4.541  0.78 20.28  ? 11  PHE A N   1 
ATOM   48   N  N   B PHE A 1 10  ? 22.627 -29.863 4.595  0.22 17.68  ? 11  PHE A N   1 
ATOM   49   C  CA  A PHE A 1 10  ? 23.163 -31.052 5.541  0.78 19.77  ? 11  PHE A CA  1 
ATOM   50   C  CA  B PHE A 1 10  ? 23.143 -30.831 5.549  0.22 17.39  ? 11  PHE A CA  1 
ATOM   51   C  C   A PHE A 1 10  ? 22.688 -30.544 6.905  0.78 21.68  ? 11  PHE A C   1 
ATOM   52   C  C   B PHE A 1 10  ? 22.604 -30.396 6.894  0.22 20.85  ? 11  PHE A C   1 
ATOM   53   O  O   A PHE A 1 10  ? 23.251 -29.587 7.454  0.78 20.58  ? 11  PHE A O   1 
ATOM   54   O  O   B PHE A 1 10  ? 23.007 -29.343 7.408  0.22 19.65  ? 11  PHE A O   1 
ATOM   55   C  CB  A PHE A 1 10  ? 24.686 -31.352 5.500  0.78 20.88  ? 11  PHE A CB  1 
ATOM   56   C  CB  B PHE A 1 10  ? 24.678 -30.880 5.491  0.22 18.55  ? 11  PHE A CB  1 
ATOM   57   C  CG  A PHE A 1 10  ? 25.071 -32.548 6.344  0.78 21.69  ? 11  PHE A CG  1 
ATOM   58   C  CG  B PHE A 1 10  ? 25.152 -31.820 4.409  0.22 20.65  ? 11  PHE A CG  1 
ATOM   59   C  CD1 A PHE A 1 10  ? 24.674 -33.835 5.986  0.78 24.87  ? 11  PHE A CD1 1 
ATOM   60   C  CD1 B PHE A 1 10  ? 25.055 -31.468 3.066  0.22 24.22  ? 11  PHE A CD1 1 
ATOM   61   C  CD2 A PHE A 1 10  ? 25.818 -32.387 7.507  0.78 23.61  ? 11  PHE A CD2 1 
ATOM   62   C  CD2 B PHE A 1 10  ? 25.634 -33.082 4.725  0.22 23.93  ? 11  PHE A CD2 1 
ATOM   63   C  CE1 A PHE A 1 10  ? 25.008 -34.939 6.786  0.78 26.05  ? 11  PHE A CE1 1 
ATOM   64   C  CE1 B PHE A 1 10  ? 25.473 -32.345 2.065  0.22 25.59  ? 11  PHE A CE1 1 
ATOM   65   C  CE2 A PHE A 1 10  ? 26.149 -33.485 8.306  0.78 25.37  ? 11  PHE A CE2 1 
ATOM   66   C  CE2 B PHE A 1 10  ? 26.036 -33.964 3.720  0.22 27.42  ? 11  PHE A CE2 1 
ATOM   67   C  CZ  A PHE A 1 10  ? 25.747 -34.753 7.942  0.78 23.39  ? 11  PHE A CZ  1 
ATOM   68   C  CZ  B PHE A 1 10  ? 25.969 -33.583 2.401  0.22 25.40  ? 11  PHE A CZ  1 
ATOM   69   N  N   . THR A 1 11  ? 21.607 -31.144 7.410  1.00 18.32  ? 12  THR A N   1 
ATOM   70   C  CA  . THR A 1 11  ? 20.927 -30.769 8.670  1.00 18.71  ? 12  THR A CA  1 
ATOM   71   C  C   . THR A 1 11  ? 21.878 -30.518 9.874  1.00 21.87  ? 12  THR A C   1 
ATOM   72   O  O   . THR A 1 11  ? 21.742 -29.495 10.564 1.00 20.49  ? 12  THR A O   1 
ATOM   73   C  CB  . THR A 1 11  ? 19.861 -31.824 9.016  1.00 25.31  ? 12  THR A CB  1 
ATOM   74   O  OG1 . THR A 1 11  ? 18.921 -31.906 7.928  1.00 25.87  ? 12  THR A OG1 1 
ATOM   75   C  CG2 . THR A 1 11  ? 19.105 -31.493 10.317 1.00 31.04  ? 12  THR A CG2 1 
ATOM   76   N  N   A ARG A 1 12  ? 22.823 -31.440 10.102 0.50 19.49  ? 13  ARG A N   1 
ATOM   77   N  N   B ARG A 1 12  ? 22.816 -31.443 10.114 0.50 19.78  ? 13  ARG A N   1 
ATOM   78   C  CA  A ARG A 1 12  ? 23.746 -31.368 11.247 0.50 19.29  ? 13  ARG A CA  1 
ATOM   79   C  CA  B ARG A 1 12  ? 23.736 -31.359 11.261 0.50 19.70  ? 13  ARG A CA  1 
ATOM   80   C  C   A ARG A 1 12  ? 24.990 -30.486 11.042 0.50 21.17  ? 13  ARG A C   1 
ATOM   81   C  C   B ARG A 1 12  ? 24.973 -30.462 11.057 0.50 21.26  ? 13  ARG A C   1 
ATOM   82   O  O   A ARG A 1 12  ? 25.810 -30.395 11.962 0.50 19.60  ? 13  ARG A O   1 
ATOM   83   O  O   B ARG A 1 12  ? 25.774 -30.341 11.991 0.50 19.61  ? 13  ARG A O   1 
ATOM   84   C  CB  A ARG A 1 12  ? 24.179 -32.792 11.669 0.50 22.93  ? 13  ARG A CB  1 
ATOM   85   C  CB  B ARG A 1 12  ? 24.181 -32.774 11.673 0.50 24.21  ? 13  ARG A CB  1 
ATOM   86   C  CG  A ARG A 1 12  ? 23.048 -33.694 12.192 0.50 29.16  ? 13  ARG A CG  1 
ATOM   87   C  CG  B ARG A 1 12  ? 23.193 -33.505 12.587 0.50 35.18  ? 13  ARG A CG  1 
ATOM   88   C  CD  A ARG A 1 12  ? 22.486 -33.243 13.532 0.50 40.32  ? 13  ARG A CD  1 
ATOM   89   C  CD  B ARG A 1 12  ? 22.919 -34.939 12.164 0.50 43.57  ? 13  ARG A CD  1 
ATOM   90   N  NE  A ARG A 1 12  ? 23.435 -33.417 14.635 0.50 48.94  ? 13  ARG A NE  1 
ATOM   91   N  NE  B ARG A 1 12  ? 24.134 -35.723 11.917 0.50 45.79  ? 13  ARG A NE  1 
ATOM   92   C  CZ  A ARG A 1 12  ? 23.387 -32.746 15.783 0.50 56.00  ? 13  ARG A CZ  1 
ATOM   93   C  CZ  B ARG A 1 12  ? 24.339 -36.462 10.830 0.50 55.13  ? 13  ARG A CZ  1 
ATOM   94   N  NH1 A ARG A 1 12  ? 22.451 -31.826 15.984 0.50 37.08  ? 13  ARG A NH1 1 
ATOM   95   N  NH1 B ARG A 1 12  ? 25.465 -37.149 10.689 0.50 47.53  ? 13  ARG A NH1 1 
ATOM   96   N  NH2 A ARG A 1 12  ? 24.278 -32.983 16.733 0.50 43.99  ? 13  ARG A NH2 1 
ATOM   97   N  NH2 B ARG A 1 12  ? 23.413 -36.531 9.881  0.50 31.83  ? 13  ARG A NH2 1 
ATOM   98   N  N   . HIS A 1 13  ? 25.144 -29.852 9.864  1.00 17.56  ? 14  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 13  ? 26.353 -29.054 9.554  1.00 17.33  ? 14  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 13  ? 26.643 -27.947 10.565 1.00 19.73  ? 14  HIS A C   1 
ATOM   101  O  O   . HIS A 1 13  ? 27.779 -27.862 11.054 1.00 18.75  ? 14  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 13  ? 26.328 -28.476 8.126  1.00 17.48  ? 14  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 13  ? 27.602 -27.736 7.806  1.00 18.79  ? 14  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 13  ? 28.779 -28.413 7.593  1.00 19.30  ? 14  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 13  ? 27.835 -26.408 7.686  1.00 19.45  ? 14  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 13  ? 29.697 -27.492 7.350  1.00 18.81  ? 14  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 13  ? 29.172 -26.268 7.376  1.00 18.51  ? 14  HIS A NE2 1 
ATOM   108  N  N   . ALA A 1 14  ? 25.653 -27.078 10.837 1.00 16.89  ? 15  ALA A N   1 
ATOM   109  C  CA  . ALA A 1 14  ? 25.869 -25.948 11.763 1.00 16.52  ? 15  ALA A CA  1 
ATOM   110  C  C   . ALA A 1 14  ? 26.275 -26.431 13.164 1.00 18.68  ? 15  ALA A C   1 
ATOM   111  O  O   . ALA A 1 14  ? 27.176 -25.842 13.765 1.00 16.99  ? 15  ALA A O   1 
ATOM   112  C  CB  . ALA A 1 14  ? 24.630 -25.052 11.824 1.00 17.86  ? 15  ALA A CB  1 
ATOM   113  N  N   A SER A 1 15  ? 25.619 -27.488 13.667 0.38 16.72  ? 16  SER A N   1 
ATOM   114  N  N   B SER A 1 15  ? 25.625 -27.495 13.670 0.33 16.73  ? 16  SER A N   1 
ATOM   115  N  N   C SER A 1 15  ? 25.618 -27.492 13.679 0.29 16.62  ? 16  SER A N   1 
ATOM   116  C  CA  A SER A 1 15  ? 25.915 -28.062 14.978 0.38 16.81  ? 16  SER A CA  1 
ATOM   117  C  CA  B SER A 1 15  ? 25.924 -28.073 14.984 0.33 16.87  ? 16  SER A CA  1 
ATOM   118  C  CA  C SER A 1 15  ? 25.928 -28.050 14.999 0.29 16.72  ? 16  SER A CA  1 
ATOM   119  C  C   A SER A 1 15  ? 27.331 -28.651 15.014 0.38 20.59  ? 16  SER A C   1 
ATOM   120  C  C   B SER A 1 15  ? 27.334 -28.660 15.020 0.33 20.82  ? 16  SER A C   1 
ATOM   121  C  C   C SER A 1 15  ? 27.326 -28.682 15.035 0.29 20.93  ? 16  SER A C   1 
ATOM   122  O  O   A SER A 1 15  ? 28.049 -28.432 15.992 0.38 18.15  ? 16  SER A O   1 
ATOM   123  O  O   B SER A 1 15  ? 28.050 -28.454 16.002 0.33 18.76  ? 16  SER A O   1 
ATOM   124  O  O   C SER A 1 15  ? 28.035 -28.516 16.029 0.29 19.19  ? 16  SER A O   1 
ATOM   125  C  CB  A SER A 1 15  ? 24.872 -29.117 15.346 0.38 20.31  ? 16  SER A CB  1 
ATOM   126  C  CB  B SER A 1 15  ? 24.897 -29.144 15.347 0.33 20.49  ? 16  SER A CB  1 
ATOM   127  C  CB  C SER A 1 15  ? 24.851 -29.036 15.452 0.29 20.19  ? 16  SER A CB  1 
ATOM   128  O  OG  A SER A 1 15  ? 25.141 -29.674 16.621 0.38 22.76  ? 16  SER A OG  1 
ATOM   129  O  OG  B SER A 1 15  ? 23.594 -28.593 15.396 0.33 23.73  ? 16  SER A OG  1 
ATOM   130  O  OG  C SER A 1 15  ? 24.761 -30.170 14.605 0.29 23.86  ? 16  SER A OG  1 
ATOM   131  N  N   . ASP A 1 16  ? 27.735 -29.366 13.941 1.00 18.91  ? 17  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 16  ? 29.072 -29.981 13.823 1.00 19.59  ? 17  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 16  ? 30.128 -28.880 13.780 1.00 19.45  ? 17  ASP A C   1 
ATOM   134  O  O   . ASP A 1 16  ? 31.194 -29.035 14.377 1.00 19.38  ? 17  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 16  ? 29.162 -30.847 12.555 1.00 20.78  ? 17  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 16  ? 28.399 -32.166 12.633 1.00 28.82  ? 17  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 16  ? 27.884 -32.498 13.731 1.00 28.63  ? 17  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 16  ? 28.302 -32.853 11.598 1.00 28.93  ? 17  ASP A OD2 1 
ATOM   139  N  N   . VAL A 1 17  ? 29.837 -27.769 13.061 1.00 15.21  ? 18  VAL A N   1 
ATOM   140  C  CA  . VAL A 1 17  ? 30.774 -26.635 13.024 1.00 14.91  ? 18  VAL A CA  1 
ATOM   141  C  C   . VAL A 1 17  ? 30.967 -26.077 14.442 1.00 18.00  ? 18  VAL A C   1 
ATOM   142  O  O   . VAL A 1 17  ? 32.094 -25.863 14.877 1.00 16.71  ? 18  VAL A O   1 
ATOM   143  C  CB  . VAL A 1 17  ? 30.299 -25.518 12.049 1.00 16.97  ? 18  VAL A CB  1 
ATOM   144  C  CG1 . VAL A 1 17  ? 31.073 -24.214 12.268 1.00 17.01  ? 18  VAL A CG1 1 
ATOM   145  C  CG2 . VAL A 1 17  ? 30.390 -25.981 10.595 1.00 16.53  ? 18  VAL A CG2 1 
ATOM   146  N  N   . LEU A 1 18  ? 29.867 -25.846 15.160 1.00 15.96  ? 19  LEU A N   1 
ATOM   147  C  CA  . LEU A 1 18  ? 29.968 -25.263 16.495 1.00 16.36  ? 19  LEU A CA  1 
ATOM   148  C  C   . LEU A 1 18  ? 30.712 -26.201 17.450 1.00 19.55  ? 19  LEU A C   1 
ATOM   149  O  O   . LEU A 1 18  ? 31.560 -25.731 18.230 1.00 16.89  ? 19  LEU A O   1 
ATOM   150  C  CB  . LEU A 1 18  ? 28.580 -24.895 17.045 1.00 17.20  ? 19  LEU A CB  1 
ATOM   151  C  CG  . LEU A 1 18  ? 28.612 -23.936 18.273 1.00 20.09  ? 19  LEU A CG  1 
ATOM   152  C  CD1 . LEU A 1 18  ? 29.171 -22.542 17.904 1.00 19.99  ? 19  LEU A CD1 1 
ATOM   153  C  CD2 . LEU A 1 18  ? 27.215 -23.793 18.865 1.00 24.07  ? 19  LEU A CD2 1 
ATOM   154  N  N   . LEU A 1 19  ? 30.440 -27.518 17.347 1.00 17.80  ? 20  LEU A N   1 
ATOM   155  C  CA  . LEU A 1 19  ? 31.124 -28.540 18.161 1.00 18.99  ? 20  LEU A CA  1 
ATOM   156  C  C   . LEU A 1 19  ? 32.640 -28.478 17.913 1.00 19.48  ? 20  LEU A C   1 
ATOM   157  O  O   . LEU A 1 19  ? 33.424 -28.465 18.877 1.00 18.41  ? 20  LEU A O   1 
ATOM   158  C  CB  . LEU A 1 19  ? 30.579 -29.937 17.822 1.00 20.90  ? 20  LEU A CB  1 
ATOM   159  C  CG  . LEU A 1 19  ? 31.201 -31.093 18.582 1.00 29.38  ? 20  LEU A CG  1 
ATOM   160  C  CD1 . LEU A 1 19  ? 30.742 -31.079 20.046 1.00 31.90  ? 20  LEU A CD1 1 
ATOM   161  C  CD2 . LEU A 1 19  ? 30.810 -32.414 17.938 1.00 34.09  ? 20  LEU A CD2 1 
ATOM   162  N  N   . ASN A 1 20  ? 33.051 -28.370 16.633 1.00 16.67  ? 21  ASN A N   1 
ATOM   163  C  CA  . ASN A 1 20  ? 34.470 -28.257 16.290 1.00 16.63  ? 21  ASN A CA  1 
ATOM   164  C  C   . ASN A 1 20  ? 35.091 -26.942 16.784 1.00 18.63  ? 21  ASN A C   1 
ATOM   165  O  O   . ASN A 1 20  ? 36.241 -26.945 17.226 1.00 18.63  ? 21  ASN A O   1 
ATOM   166  C  CB  . ASN A 1 20  ? 34.684 -28.476 14.800 1.00 17.70  ? 21  ASN A CB  1 
ATOM   167  C  CG  . ASN A 1 20  ? 34.621 -29.946 14.446 1.00 28.81  ? 21  ASN A CG  1 
ATOM   168  O  OD1 . ASN A 1 20  ? 34.811 -30.815 15.302 1.00 24.14  ? 21  ASN A OD1 1 
ATOM   169  N  ND2 . ASN A 1 20  ? 34.326 -30.263 13.195 1.00 21.30  ? 21  ASN A ND2 1 
ATOM   170  N  N   . LEU A 1 21  ? 34.341 -25.822 16.698 1.00 16.20  ? 22  LEU A N   1 
ATOM   171  C  CA  . LEU A 1 21  ? 34.809 -24.531 17.235 1.00 15.82  ? 22  LEU A CA  1 
ATOM   172  C  C   . LEU A 1 21  ? 35.023 -24.677 18.744 1.00 17.94  ? 22  LEU A C   1 
ATOM   173  O  O   . LEU A 1 21  ? 36.011 -24.161 19.281 1.00 16.24  ? 22  LEU A O   1 
ATOM   174  C  CB  . LEU A 1 21  ? 33.810 -23.380 16.939 1.00 15.41  ? 22  LEU A CB  1 
ATOM   175  C  CG  . LEU A 1 21  ? 33.721 -23.010 15.430 1.00 18.00  ? 22  LEU A CG  1 
ATOM   176  C  CD1 . LEU A 1 21  ? 32.638 -21.943 15.200 1.00 18.10  ? 22  LEU A CD1 1 
ATOM   177  C  CD2 . LEU A 1 21  ? 35.085 -22.532 14.864 1.00 21.09  ? 22  LEU A CD2 1 
ATOM   178  N  N   . ASN A 1 22  ? 34.090 -25.365 19.446 1.00 16.02  ? 23  ASN A N   1 
ATOM   179  C  CA  . ASN A 1 22  ? 34.278 -25.571 20.892 1.00 16.48  ? 23  ASN A CA  1 
ATOM   180  C  C   . ASN A 1 22  ? 35.510 -26.472 21.190 1.00 20.88  ? 23  ASN A C   1 
ATOM   181  O  O   . ASN A 1 22  ? 36.222 -26.229 22.166 1.00 21.19  ? 23  ASN A O   1 
ATOM   182  C  CB  . ASN A 1 22  ? 33.020 -26.136 21.536 1.00 18.23  ? 23  ASN A CB  1 
ATOM   183  C  CG  . ASN A 1 22  ? 33.052 -26.009 23.046 1.00 24.84  ? 23  ASN A CG  1 
ATOM   184  O  OD1 . ASN A 1 22  ? 33.554 -25.033 23.601 1.00 22.75  ? 23  ASN A OD1 1 
ATOM   185  N  ND2 . ASN A 1 22  ? 32.498 -26.982 23.718 1.00 26.43  ? 23  ASN A ND2 1 
ATOM   186  N  N   . ARG A 1 23  ? 35.784 -27.488 20.334 1.00 18.41  ? 24  ARG A N   1 
ATOM   187  C  CA  . ARG A 1 23  ? 36.978 -28.340 20.500 1.00 19.51  ? 24  ARG A CA  1 
ATOM   188  C  C   . ARG A 1 23  ? 38.246 -27.496 20.335 1.00 23.60  ? 24  ARG A C   1 
ATOM   189  O  O   . ARG A 1 23  ? 39.192 -27.679 21.088 1.00 23.18  ? 24  ARG A O   1 
ATOM   190  C  CB  . ARG A 1 23  ? 37.000 -29.487 19.480 1.00 18.68  ? 24  ARG A CB  1 
ATOM   191  C  CG  . ARG A 1 23  ? 35.994 -30.582 19.800 1.00 25.03  ? 24  ARG A CG  1 
ATOM   192  C  CD  . ARG A 1 23  ? 35.722 -31.446 18.580 1.00 28.88  ? 24  ARG A CD  1 
ATOM   193  N  NE  . ARG A 1 23  ? 34.884 -32.591 18.923 1.00 36.17  ? 24  ARG A NE  1 
ATOM   194  C  CZ  . ARG A 1 23  ? 34.378 -33.452 18.046 1.00 54.43  ? 24  ARG A CZ  1 
ATOM   195  N  NH1 . ARG A 1 23  ? 34.571 -33.275 16.741 1.00 40.71  ? 24  ARG A NH1 1 
ATOM   196  N  NH2 . ARG A 1 23  ? 33.662 -34.486 18.462 1.00 42.47  ? 24  ARG A NH2 1 
ATOM   197  N  N   . LEU A 1 24  ? 38.250 -26.539 19.376 1.00 19.98  ? 25  LEU A N   1 
ATOM   198  C  CA  . LEU A 1 24  ? 39.399 -25.650 19.213 1.00 18.48  ? 25  LEU A CA  1 
ATOM   199  C  C   . LEU A 1 24  ? 39.554 -24.774 20.460 1.00 21.95  ? 25  LEU A C   1 
ATOM   200  O  O   . LEU A 1 24  ? 40.681 -24.616 20.960 1.00 22.42  ? 25  LEU A O   1 
ATOM   201  C  CB  . LEU A 1 24  ? 39.229 -24.758 17.995 1.00 17.73  ? 25  LEU A CB  1 
ATOM   202  C  CG  . LEU A 1 24  ? 39.201 -25.463 16.619 1.00 21.06  ? 25  LEU A CG  1 
ATOM   203  C  CD1 . LEU A 1 24  ? 39.056 -24.409 15.508 1.00 21.37  ? 25  LEU A CD1 1 
ATOM   204  C  CD2 . LEU A 1 24  ? 40.474 -26.328 16.396 1.00 23.27  ? 25  LEU A CD2 1 
ATOM   205  N  N   . ARG A 1 25  ? 38.427 -24.251 20.991 1.00 18.43  ? 26  ARG A N   1 
ATOM   206  C  CA  . ARG A 1 25  ? 38.489 -23.454 22.231 1.00 19.10  ? 26  ARG A CA  1 
ATOM   207  C  C   . ARG A 1 25  ? 39.120 -24.279 23.399 1.00 24.46  ? 26  ARG A C   1 
ATOM   208  O  O   . ARG A 1 25  ? 40.012 -23.761 24.106 1.00 24.45  ? 26  ARG A O   1 
ATOM   209  C  CB  . ARG A 1 25  ? 37.089 -22.959 22.644 1.00 19.63  ? 26  ARG A CB  1 
ATOM   210  C  CG  . ARG A 1 25  ? 37.197 -22.032 23.868 1.00 24.66  ? 26  ARG A CG  1 
ATOM   211  C  CD  . ARG A 1 25  ? 35.887 -21.412 24.247 1.00 26.96  ? 26  ARG A CD  1 
ATOM   212  N  NE  . ARG A 1 25  ? 34.877 -22.399 24.624 1.00 24.87  ? 26  ARG A NE  1 
ATOM   213  C  CZ  . ARG A 1 25  ? 34.264 -22.439 25.803 1.00 36.72  ? 26  ARG A CZ  1 
ATOM   214  N  NH1 . ARG A 1 25  ? 34.632 -21.614 26.782 1.00 31.34  ? 26  ARG A NH1 1 
ATOM   215  N  NH2 . ARG A 1 25  ? 33.310 -23.328 26.028 1.00 26.58  ? 26  ARG A NH2 1 
ATOM   216  N  N   A SER A 1 26  ? 38.635 -25.515 23.602 0.40 22.89  ? 27  SER A N   1 
ATOM   217  N  N   B SER A 1 26  ? 38.639 -25.520 23.613 0.35 22.65  ? 27  SER A N   1 
ATOM   218  N  N   C SER A 1 26  ? 38.640 -25.526 23.602 0.25 22.24  ? 27  SER A N   1 
ATOM   219  C  CA  A SER A 1 26  ? 39.110 -26.425 24.650 0.40 24.42  ? 27  SER A CA  1 
ATOM   220  C  CA  B SER A 1 26  ? 39.114 -26.403 24.690 0.35 24.06  ? 27  SER A CA  1 
ATOM   221  C  CA  C SER A 1 26  ? 39.092 -26.451 24.656 0.25 23.52  ? 27  SER A CA  1 
ATOM   222  C  C   A SER A 1 26  ? 40.622 -26.591 24.580 0.40 28.98  ? 27  SER A C   1 
ATOM   223  C  C   B SER A 1 26  ? 40.609 -26.718 24.589 0.35 29.15  ? 27  SER A C   1 
ATOM   224  C  C   C SER A 1 26  ? 40.591 -26.751 24.578 0.25 28.85  ? 27  SER A C   1 
ATOM   225  O  O   A SER A 1 26  ? 41.302 -26.510 25.605 0.40 29.38  ? 27  SER A O   1 
ATOM   226  O  O   B SER A 1 26  ? 41.265 -26.899 25.616 0.35 29.92  ? 27  SER A O   1 
ATOM   227  O  O   C SER A 1 26  ? 41.226 -26.969 25.611 0.25 29.56  ? 27  SER A O   1 
ATOM   228  C  CB  A SER A 1 26  ? 38.462 -27.798 24.492 0.40 28.68  ? 27  SER A CB  1 
ATOM   229  C  CB  B SER A 1 26  ? 38.292 -27.687 24.747 0.35 27.68  ? 27  SER A CB  1 
ATOM   230  C  CB  C SER A 1 26  ? 38.294 -27.751 24.603 0.25 26.83  ? 27  SER A CB  1 
ATOM   231  O  OG  A SER A 1 26  ? 37.102 -27.804 24.887 0.40 36.52  ? 27  SER A OG  1 
ATOM   232  O  OG  B SER A 1 26  ? 38.558 -28.550 23.654 0.35 33.66  ? 27  SER A OG  1 
ATOM   233  O  OG  C SER A 1 26  ? 38.745 -28.693 25.565 0.25 33.65  ? 27  SER A OG  1 
ATOM   234  N  N   . ARG A 1 27  ? 41.142 -26.781 23.356 1.00 25.28  ? 28  ARG A N   1 
ATOM   235  C  CA  . ARG A 1 27  ? 42.565 -27.043 23.103 1.00 26.89  ? 28  ARG A CA  1 
ATOM   236  C  C   . ARG A 1 27  ? 43.385 -25.764 22.917 1.00 29.42  ? 28  ARG A C   1 
ATOM   237  O  O   . ARG A 1 27  ? 44.600 -25.836 22.679 1.00 30.38  ? 28  ARG A O   1 
ATOM   238  C  CB  . ARG A 1 27  ? 42.694 -27.997 21.921 1.00 29.01  ? 28  ARG A CB  1 
ATOM   239  C  CG  . ARG A 1 27  ? 41.950 -29.312 22.163 1.00 39.30  ? 28  ARG A CG  1 
ATOM   240  C  CD  . ARG A 1 27  ? 41.951 -30.183 20.936 1.00 44.77  ? 28  ARG A CD  1 
ATOM   241  N  NE  . ARG A 1 27  ? 43.279 -30.751 20.710 1.00 61.50  ? 28  ARG A NE  1 
ATOM   242  C  CZ  . ARG A 1 27  ? 43.811 -30.937 19.510 1.00 78.37  ? 28  ARG A CZ  1 
ATOM   243  N  NH1 . ARG A 1 27  ? 45.023 -31.460 19.389 1.00 68.75  ? 28  ARG A NH1 1 
ATOM   244  N  NH2 . ARG A 1 27  ? 43.139 -30.598 18.423 1.00 64.01  ? 28  ARG A NH2 1 
ATOM   245  N  N   . ASP A 1 28  ? 42.731 -24.596 23.079 1.00 24.15  ? 29  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 28  ? 43.327 -23.260 22.942 1.00 24.49  ? 29  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 28  ? 43.944 -23.074 21.534 1.00 28.70  ? 29  ASP A C   1 
ATOM   248  O  O   . ASP A 1 28  ? 45.018 -22.486 21.377 1.00 29.46  ? 29  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 28  ? 44.361 -22.984 24.071 1.00 27.76  ? 29  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 28  ? 44.680 -21.518 24.240 1.00 34.31  ? 29  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 28  ? 43.769 -20.679 24.019 1.00 32.74  ? 29  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 28  ? 45.833 -21.203 24.590 1.00 38.95  ? 29  ASP A OD2 1 
ATOM   253  N  N   . ILE A 1 29  ? 43.268 -23.609 20.517 1.00 23.11  ? 30  ILE A N   1 
ATOM   254  C  CA  . ILE A 1 29  ? 43.763 -23.524 19.143 1.00 22.41  ? 30  ILE A CA  1 
ATOM   255  C  C   . ILE A 1 29  ? 43.165 -22.329 18.433 1.00 25.48  ? 30  ILE A C   1 
ATOM   256  O  O   . ILE A 1 29  ? 41.928 -22.208 18.333 1.00 22.46  ? 30  ILE A O   1 
ATOM   257  C  CB  . ILE A 1 29  ? 43.522 -24.838 18.351 1.00 24.78  ? 30  ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 29  ? 44.317 -26.030 18.970 1.00 26.30  ? 30  ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 29  ? 43.883 -24.658 16.850 1.00 23.93  ? 30  ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 29  ? 43.826 -27.401 18.444 1.00 27.87  ? 30  ILE A CD1 1 
ATOM   261  N  N   A LEU A 1 30  ? 44.044 -21.447 17.924 0.54 22.97  ? 31  LEU A N   1 
ATOM   262  N  N   B LEU A 1 30  ? 44.050 -21.450 17.922 0.46 23.78  ? 31  LEU A N   1 
ATOM   263  C  CA  A LEU A 1 30  ? 43.685 -20.248 17.159 0.54 22.23  ? 31  LEU A CA  1 
ATOM   264  C  CA  B LEU A 1 30  ? 43.725 -20.236 17.167 0.46 23.53  ? 31  LEU A CA  1 
ATOM   265  C  C   A LEU A 1 30  ? 42.799 -19.242 17.913 0.54 23.93  ? 31  LEU A C   1 
ATOM   266  C  C   B LEU A 1 30  ? 42.815 -19.241 17.910 0.46 24.72  ? 31  LEU A C   1 
ATOM   267  O  O   A LEU A 1 30  ? 42.194 -18.374 17.285 0.54 22.22  ? 31  LEU A O   1 
ATOM   268  O  O   B LEU A 1 30  ? 42.209 -18.377 17.275 0.46 23.15  ? 31  LEU A O   1 
ATOM   269  C  CB  A LEU A 1 30  ? 43.063 -20.607 15.802 0.54 21.98  ? 31  LEU A CB  1 
ATOM   270  C  CB  B LEU A 1 30  ? 43.170 -20.558 15.781 0.46 23.77  ? 31  LEU A CB  1 
ATOM   271  C  CG  A LEU A 1 30  ? 44.001 -21.234 14.740 0.54 26.93  ? 31  LEU A CG  1 
ATOM   272  C  CG  B LEU A 1 30  ? 44.213 -20.424 14.674 0.46 29.73  ? 31  LEU A CG  1 
ATOM   273  C  CD1 A LEU A 1 30  ? 43.489 -20.941 13.380 0.54 25.02  ? 31  LEU A CD1 1 
ATOM   274  C  CD1 B LEU A 1 30  ? 44.547 -21.771 14.060 0.46 30.57  ? 31  LEU A CD1 1 
ATOM   275  C  CD2 A LEU A 1 30  ? 45.430 -20.703 14.831 0.54 30.36  ? 31  LEU A CD2 1 
ATOM   276  C  CD2 B LEU A 1 30  ? 43.768 -19.432 13.633 0.46 30.58  ? 31  LEU A CD2 1 
ATOM   277  N  N   . THR A 1 31  ? 42.802 -19.298 19.255 1.00 21.15  ? 32  THR A N   1 
ATOM   278  C  CA  . THR A 1 31  ? 42.095 -18.304 20.082 1.00 20.48  ? 32  THR A CA  1 
ATOM   279  C  C   . THR A 1 31  ? 42.922 -17.015 19.877 1.00 26.29  ? 32  THR A C   1 
ATOM   280  O  O   . THR A 1 31  ? 44.149 -17.080 19.712 1.00 26.96  ? 32  THR A O   1 
ATOM   281  C  CB  . THR A 1 31  ? 42.059 -18.718 21.549 1.00 26.64  ? 32  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 31  ? 43.379 -19.091 21.921 1.00 28.72  ? 32  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 31  ? 41.078 -19.887 21.800 1.00 24.31  ? 32  THR A CG2 1 
ATOM   284  N  N   . ASP A 1 32  ? 42.249 -15.881 19.748 1.00 22.68  ? 33  ASP A N   1 
ATOM   285  C  CA  . ASP A 1 32  ? 42.899 -14.631 19.386 1.00 22.95  ? 33  ASP A CA  1 
ATOM   286  C  C   . ASP A 1 32  ? 42.561 -13.477 20.296 1.00 24.88  ? 33  ASP A C   1 
ATOM   287  O  O   . ASP A 1 32  ? 42.885 -12.324 19.994 1.00 25.19  ? 33  ASP A O   1 
ATOM   288  C  CB  . ASP A 1 32  ? 42.559 -14.304 17.924 1.00 23.75  ? 33  ASP A CB  1 
ATOM   289  C  CG  . ASP A 1 32  ? 41.070 -14.298 17.608 1.00 29.97  ? 33  ASP A CG  1 
ATOM   290  O  OD1 . ASP A 1 32  ? 40.251 -14.340 18.560 1.00 25.46  ? 33  ASP A OD1 1 
ATOM   291  O  OD2 . ASP A 1 32  ? 40.724 -14.282 16.421 1.00 36.08  ? 33  ASP A OD2 1 
ATOM   292  N  N   . VAL A 1 33  ? 41.905 -13.772 21.415 1.00 20.70  ? 34  VAL A N   1 
ATOM   293  C  CA  . VAL A 1 33  ? 41.580 -12.729 22.395 1.00 19.98  ? 34  VAL A CA  1 
ATOM   294  C  C   . VAL A 1 33  ? 41.416 -13.330 23.778 1.00 23.39  ? 34  VAL A C   1 
ATOM   295  O  O   . VAL A 1 33  ? 41.030 -14.508 23.913 1.00 23.15  ? 34  VAL A O   1 
ATOM   296  C  CB  . VAL A 1 33  ? 40.299 -11.908 21.966 1.00 22.91  ? 34  VAL A CB  1 
ATOM   297  C  CG1 . VAL A 1 33  ? 38.995 -12.704 22.141 1.00 21.36  ? 34  VAL A CG1 1 
ATOM   298  C  CG2 . VAL A 1 33  ? 40.213 -10.550 22.695 1.00 22.99  ? 34  VAL A CG2 1 
ATOM   299  N  N   A VAL A 1 34  ? 41.698 -12.513 24.802 0.53 20.51  ? 35  VAL A N   1 
ATOM   300  N  N   B VAL A 1 34  ? 41.706 -12.528 24.809 0.47 20.93  ? 35  VAL A N   1 
ATOM   301  C  CA  A VAL A 1 34  ? 41.468 -12.825 26.206 0.53 20.04  ? 35  VAL A CA  1 
ATOM   302  C  CA  B VAL A 1 34  ? 41.434 -12.892 26.189 0.47 20.70  ? 35  VAL A CA  1 
ATOM   303  C  C   A VAL A 1 34  ? 40.403 -11.833 26.677 0.53 23.75  ? 35  VAL A C   1 
ATOM   304  C  C   B VAL A 1 34  ? 40.457 -11.857 26.764 0.47 24.25  ? 35  VAL A C   1 
ATOM   305  O  O   A VAL A 1 34  ? 40.547 -10.626 26.460 0.53 23.79  ? 35  VAL A O   1 
ATOM   306  O  O   B VAL A 1 34  ? 40.682 -10.650 26.647 0.47 24.49  ? 35  VAL A O   1 
ATOM   307  C  CB  A VAL A 1 34  ? 42.753 -12.709 27.073 0.53 24.46  ? 35  VAL A CB  1 
ATOM   308  C  CB  B VAL A 1 34  ? 42.675 -13.190 27.077 0.47 25.53  ? 35  VAL A CB  1 
ATOM   309  C  CG1 A VAL A 1 34  ? 42.466 -13.014 28.547 0.53 24.55  ? 35  VAL A CG1 1 
ATOM   310  C  CG1 B VAL A 1 34  ? 43.504 -11.943 27.362 0.47 26.38  ? 35  VAL A CG1 1 
ATOM   311  C  CG2 A VAL A 1 34  ? 43.856 -13.609 26.552 0.53 24.86  ? 35  VAL A CG2 1 
ATOM   312  C  CG2 B VAL A 1 34  ? 42.263 -13.875 28.377 0.47 25.57  ? 35  VAL A CG2 1 
ATOM   313  N  N   . ILE A 1 35  ? 39.341 -12.339 27.306 1.00 19.85  ? 36  ILE A N   1 
ATOM   314  C  CA  . ILE A 1 35  ? 38.295 -11.514 27.903 1.00 19.62  ? 36  ILE A CA  1 
ATOM   315  C  C   . ILE A 1 35  ? 38.584 -11.543 29.403 1.00 24.81  ? 36  ILE A C   1 
ATOM   316  O  O   . ILE A 1 35  ? 38.588 -12.621 30.017 1.00 23.38  ? 36  ILE A O   1 
ATOM   317  C  CB  . ILE A 1 35  ? 36.857 -12.002 27.574 1.00 21.07  ? 36  ILE A CB  1 
ATOM   318  C  CG1 . ILE A 1 35  ? 36.612 -12.144 26.039 1.00 20.02  ? 36  ILE A CG1 1 
ATOM   319  C  CG2 . ILE A 1 35  ? 35.815 -11.105 28.221 1.00 22.58  ? 36  ILE A CG2 1 
ATOM   320  C  CD1 . ILE A 1 35  ? 36.953 -10.862 25.168 1.00 20.28  ? 36  ILE A CD1 1 
ATOM   321  N  N   . VAL A 1 36  ? 38.817 -10.363 29.982 1.00 22.21  ? 37  VAL A N   1 
ATOM   322  C  CA  . VAL A 1 36  ? 39.141 -10.222 31.408 1.00 23.09  ? 37  VAL A CA  1 
ATOM   323  C  C   . VAL A 1 36  ? 37.883 -9.799  32.157 1.00 27.17  ? 37  VAL A C   1 
ATOM   324  O  O   . VAL A 1 36  ? 37.274 -8.773  31.824 1.00 25.82  ? 37  VAL A O   1 
ATOM   325  C  CB  . VAL A 1 36  ? 40.336 -9.248  31.638 1.00 27.90  ? 37  VAL A CB  1 
ATOM   326  C  CG1 . VAL A 1 36  ? 40.650 -9.076  33.130 1.00 28.87  ? 37  VAL A CG1 1 
ATOM   327  C  CG2 . VAL A 1 36  ? 41.583 -9.717  30.896 1.00 28.81  ? 37  VAL A CG2 1 
ATOM   328  N  N   . VAL A 1 37  ? 37.497 -10.589 33.177 1.00 23.78  ? 38  VAL A N   1 
ATOM   329  C  CA  . VAL A 1 37  ? 36.292 -10.352 33.977 1.00 23.81  ? 38  VAL A CA  1 
ATOM   330  C  C   . VAL A 1 37  ? 36.752 -10.386 35.423 1.00 28.89  ? 38  VAL A C   1 
ATOM   331  O  O   . VAL A 1 37  ? 36.994 -11.467 35.960 1.00 26.47  ? 38  VAL A O   1 
ATOM   332  C  CB  . VAL A 1 37  ? 35.167 -11.375 33.659 1.00 27.13  ? 38  VAL A CB  1 
ATOM   333  C  CG1 . VAL A 1 37  ? 33.847 -10.959 34.301 1.00 27.12  ? 38  VAL A CG1 1 
ATOM   334  C  CG2 . VAL A 1 37  ? 34.992 -11.562 32.146 1.00 25.88  ? 38  VAL A CG2 1 
ATOM   335  N  N   A SER A 1 38  ? 36.629 -9.264  36.166 0.50 28.30  ? 39  SER A N   1 
ATOM   336  N  N   B SER A 1 38  ? 37.277 -9.190  35.795 0.50 25.54  ? 39  SER A N   1 
ATOM   337  C  CA  A SER A 1 38  ? 36.983 -9.232  37.600 0.50 29.92  ? 39  SER A CA  1 
ATOM   338  C  CA  B SER A 1 38  ? 37.945 -8.816  37.029 0.50 25.93  ? 39  SER A CA  1 
ATOM   339  C  C   A SER A 1 38  ? 38.236 -10.114 37.924 0.50 34.54  ? 39  SER A C   1 
ATOM   340  C  C   B SER A 1 38  ? 39.226 -9.643  37.193 0.50 28.50  ? 39  SER A C   1 
ATOM   341  O  O   A SER A 1 38  ? 38.186 -10.954 38.826 0.50 34.26  ? 39  SER A O   1 
ATOM   342  O  O   B SER A 1 38  ? 40.147 -9.429  36.404 0.50 27.59  ? 39  SER A O   1 
ATOM   343  C  CB  A SER A 1 38  ? 35.787 -9.645  38.466 0.50 35.34  ? 39  SER A CB  1 
ATOM   344  C  CB  B SER A 1 38  ? 36.986 -8.852  38.214 0.50 30.31  ? 39  SER A CB  1 
ATOM   345  O  OG  A SER A 1 38  ? 34.756 -8.669  38.505 0.50 46.17  ? 39  SER A OG  1 
ATOM   346  O  OG  B SER A 1 38  ? 36.028 -7.821  38.031 0.50 35.34  ? 39  SER A OG  1 
ATOM   347  N  N   A ARG A 1 39  ? 39.325 -9.950  37.127 0.50 31.05  ? 40  ARG A N   1 
ATOM   348  N  N   B ARG A 1 39  ? 39.293 -10.614 38.127 0.50 25.46  ? 40  ARG A N   1 
ATOM   349  C  CA  A ARG A 1 39  ? 40.608 -10.682 37.219 0.50 31.95  ? 40  ARG A CA  1 
ATOM   350  C  CA  B ARG A 1 39  ? 40.522 -11.404 38.247 0.50 26.18  ? 40  ARG A CA  1 
ATOM   351  C  C   A ARG A 1 39  ? 40.480 -12.224 36.983 0.50 34.23  ? 40  ARG A C   1 
ATOM   352  C  C   B ARG A 1 39  ? 40.640 -12.423 37.069 0.50 31.18  ? 40  ARG A C   1 
ATOM   353  O  O   A ARG A 1 39  ? 41.234 -13.037 37.557 0.50 34.55  ? 40  ARG A O   1 
ATOM   354  O  O   B ARG A 1 39  ? 41.644 -12.416 36.340 0.50 31.21  ? 40  ARG A O   1 
ATOM   355  C  CB  A ARG A 1 39  ? 41.371 -10.375 38.522 0.50 34.36  ? 40  ARG A CB  1 
ATOM   356  C  CB  B ARG A 1 39  ? 40.672 -12.039 39.655 0.50 27.21  ? 40  ARG A CB  1 
ATOM   357  C  CG  A ARG A 1 39  ? 41.919 -8.956  38.629 0.50 45.60  ? 40  ARG A CG  1 
ATOM   358  C  CG  B ARG A 1 39  ? 40.953 -10.995 40.753 0.50 33.76  ? 40  ARG A CG  1 
ATOM   359  C  CD  A ARG A 1 39  ? 43.033 -8.905  39.657 0.50 51.31  ? 40  ARG A CD  1 
ATOM   360  C  CD  B ARG A 1 39  ? 41.316 -11.597 42.104 0.50 33.90  ? 40  ARG A CD  1 
ATOM   361  N  NE  A ARG A 1 39  ? 43.391 -7.540  40.044 0.50 57.77  ? 40  ARG A NE  1 
ATOM   362  N  NE  B ARG A 1 39  ? 41.491 -10.577 43.143 0.50 34.00  ? 40  ARG A NE  1 
ATOM   363  C  CZ  A ARG A 1 39  ? 42.812 -6.861  41.031 0.50 68.99  ? 40  ARG A CZ  1 
ATOM   364  C  CZ  B ARG A 1 39  ? 42.658 -10.043 43.500 0.50 49.87  ? 40  ARG A CZ  1 
ATOM   365  N  NH1 A ARG A 1 39  ? 41.815 -7.401  41.723 0.50 54.40  ? 40  ARG A NH1 1 
ATOM   366  N  NH1 B ARG A 1 39  ? 43.778 -10.404 42.887 0.50 37.38  ? 40  ARG A NH1 1 
ATOM   367  N  NH2 A ARG A 1 39  ? 43.212 -5.630  41.322 0.50 54.74  ? 40  ARG A NH2 1 
ATOM   368  N  NH2 B ARG A 1 39  ? 42.712 -9.136  44.463 0.50 42.79  ? 40  ARG A NH2 1 
ATOM   369  N  N   A GLU A 1 40  ? 39.526 -12.607 36.134 0.50 27.02  ? 41  GLU A N   1 
ATOM   370  N  N   B GLU A 1 40  ? 39.560 -13.172 36.807 0.50 25.33  ? 41  GLU A N   1 
ATOM   371  C  CA  A GLU A 1 40  ? 39.327 -13.980 35.667 0.50 26.40  ? 41  GLU A CA  1 
ATOM   372  C  CA  B GLU A 1 40  ? 39.500 -14.237 35.800 0.50 24.03  ? 41  GLU A CA  1 
ATOM   373  C  C   A GLU A 1 40  ? 39.463 -13.858 34.160 0.50 28.23  ? 41  GLU A C   1 
ATOM   374  C  C   B GLU A 1 40  ? 39.742 -13.790 34.352 0.50 26.13  ? 41  GLU A C   1 
ATOM   375  O  O   A GLU A 1 40  ? 38.889 -12.940 33.570 0.50 25.87  ? 41  GLU A O   1 
ATOM   376  O  O   B GLU A 1 40  ? 39.444 -12.660 33.976 0.50 22.79  ? 41  GLU A O   1 
ATOM   377  C  CB  A GLU A 1 40  ? 37.963 -14.553 36.086 0.50 27.63  ? 41  GLU A CB  1 
ATOM   378  C  CB  B GLU A 1 40  ? 38.174 -15.014 35.900 0.50 24.98  ? 41  GLU A CB  1 
ATOM   379  C  CG  A GLU A 1 40  ? 37.861 -14.777 37.589 0.50 39.84  ? 41  GLU A CG  1 
ATOM   380  C  CG  B GLU A 1 40  ? 37.683 -15.177 37.334 0.50 39.50  ? 41  GLU A CG  1 
ATOM   381  C  CD  A GLU A 1 40  ? 37.827 -16.226 38.031 0.50 73.72  ? 41  GLU A CD  1 
ATOM   382  C  CD  B GLU A 1 40  ? 37.861 -16.524 38.007 0.50 75.48  ? 41  GLU A CD  1 
ATOM   383  O  OE1 A GLU A 1 40  ? 36.793 -16.644 38.601 0.50 76.70  ? 41  GLU A OE1 1 
ATOM   384  O  OE1 B GLU A 1 40  ? 38.916 -17.170 37.805 0.50 76.49  ? 41  GLU A OE1 1 
ATOM   385  O  OE2 A GLU A 1 40  ? 38.832 -16.943 37.814 0.50 72.73  ? 41  GLU A OE2 1 
ATOM   386  O  OE2 B GLU A 1 40  ? 36.946 -16.922 38.764 0.50 77.01  ? 41  GLU A OE2 1 
ATOM   387  N  N   . GLN A 1 41  ? 40.274 -14.723 33.541 1.00 24.38  ? 42  GLN A N   1 
ATOM   388  C  CA  . GLN A 1 41  ? 40.591 -14.577 32.130 1.00 23.97  ? 42  GLN A CA  1 
ATOM   389  C  C   . GLN A 1 41  ? 39.984 -15.696 31.332 1.00 26.58  ? 42  GLN A C   1 
ATOM   390  O  O   . GLN A 1 41  ? 40.061 -16.851 31.750 1.00 27.22  ? 42  GLN A O   1 
ATOM   391  C  CB  . GLN A 1 41  ? 42.118 -14.574 31.956 1.00 26.85  ? 42  GLN A CB  1 
ATOM   392  C  CG  . GLN A 1 41  ? 42.777 -13.330 32.549 1.00 40.59  ? 42  GLN A CG  1 
ATOM   393  C  CD  . GLN A 1 41  ? 44.242 -13.188 32.219 1.00 59.21  ? 42  GLN A CD  1 
ATOM   394  O  OE1 . GLN A 1 41  ? 44.826 -13.945 31.430 1.00 52.02  ? 42  GLN A OE1 1 
ATOM   395  N  NE2 . GLN A 1 41  ? 44.867 -12.193 32.823 1.00 63.66  ? 42  GLN A NE2 1 
ATOM   396  N  N   . PHE A 1 42  ? 39.386 -15.358 30.177 1.00 21.07  ? 43  PHE A N   1 
ATOM   397  C  CA  . PHE A 1 42  ? 38.752 -16.347 29.301 1.00 20.96  ? 43  PHE A CA  1 
ATOM   398  C  C   . PHE A 1 42  ? 39.270 -16.180 27.895 1.00 25.11  ? 43  PHE A C   1 
ATOM   399  O  O   . PHE A 1 42  ? 39.101 -15.108 27.313 1.00 25.01  ? 43  PHE A O   1 
ATOM   400  C  CB  . PHE A 1 42  ? 37.220 -16.169 29.311 1.00 22.19  ? 43  PHE A CB  1 
ATOM   401  C  CG  . PHE A 1 42  ? 36.608 -16.275 30.686 1.00 23.75  ? 43  PHE A CG  1 
ATOM   402  C  CD1 . PHE A 1 42  ? 36.491 -15.151 31.506 1.00 25.96  ? 43  PHE A CD1 1 
ATOM   403  C  CD2 . PHE A 1 42  ? 36.136 -17.496 31.161 1.00 25.99  ? 43  PHE A CD2 1 
ATOM   404  C  CE1 . PHE A 1 42  ? 35.932 -15.250 32.782 1.00 28.06  ? 43  PHE A CE1 1 
ATOM   405  C  CE2 . PHE A 1 42  ? 35.573 -17.593 32.437 1.00 28.88  ? 43  PHE A CE2 1 
ATOM   406  C  CZ  . PHE A 1 42  ? 35.475 -16.471 33.240 1.00 26.97  ? 43  PHE A CZ  1 
ATOM   407  N  N   . ARG A 1 43  ? 39.875 -17.239 27.334 1.00 21.51  ? 44  ARG A N   1 
ATOM   408  C  CA  . ARG A 1 43  ? 40.395 -17.190 25.964 1.00 20.42  ? 44  ARG A CA  1 
ATOM   409  C  C   . ARG A 1 43  ? 39.274 -17.585 25.003 1.00 23.77  ? 44  ARG A C   1 
ATOM   410  O  O   . ARG A 1 43  ? 38.467 -18.477 25.307 1.00 22.07  ? 44  ARG A O   1 
ATOM   411  C  CB  . ARG A 1 43  ? 41.622 -18.114 25.788 1.00 22.66  ? 44  ARG A CB  1 
ATOM   412  C  CG  . ARG A 1 43  ? 42.852 -17.707 26.653 1.00 30.67  ? 44  ARG A CG  1 
ATOM   413  C  CD  . ARG A 1 43  ? 44.186 -18.149 26.033 1.00 39.00  ? 44  ARG A CD  1 
ATOM   414  N  NE  . ARG A 1 43  ? 44.237 -17.792 24.607 1.00 49.11  ? 44  ARG A NE  1 
ATOM   415  C  CZ  . ARG A 1 43  ? 44.762 -16.675 24.110 1.00 61.08  ? 44  ARG A CZ  1 
ATOM   416  N  NH1 . ARG A 1 43  ? 45.388 -15.818 24.903 1.00 52.23  ? 44  ARG A NH1 1 
ATOM   417  N  NH2 . ARG A 1 43  ? 44.706 -16.431 22.809 1.00 44.64  ? 44  ARG A NH2 1 
ATOM   418  N  N   . ALA A 1 44  ? 39.188 -16.915 23.854 1.00 20.35  ? 45  ALA A N   1 
ATOM   419  C  CA  . ALA A 1 44  ? 38.106 -17.236 22.900 1.00 19.93  ? 45  ALA A CA  1 
ATOM   420  C  C   . ALA A 1 44  ? 38.506 -16.837 21.491 1.00 20.83  ? 45  ALA A C   1 
ATOM   421  O  O   . ALA A 1 44  ? 39.606 -16.312 21.280 1.00 19.92  ? 45  ALA A O   1 
ATOM   422  C  CB  . ALA A 1 44  ? 36.818 -16.500 23.301 1.00 21.14  ? 45  ALA A CB  1 
ATOM   423  N  N   . HIS A 1 45  ? 37.598 -17.072 20.533 1.00 17.54  ? 46  HIS A N   1 
ATOM   424  C  CA  . HIS A 1 45  ? 37.766 -16.646 19.147 1.00 17.04  ? 46  HIS A CA  1 
ATOM   425  C  C   . HIS A 1 45  ? 36.865 -15.411 18.946 1.00 20.40  ? 46  HIS A C   1 
ATOM   426  O  O   . HIS A 1 45  ? 35.644 -15.467 19.204 1.00 19.10  ? 46  HIS A O   1 
ATOM   427  C  CB  . HIS A 1 45  ? 37.345 -17.768 18.183 1.00 16.38  ? 46  HIS A CB  1 
ATOM   428  C  CG  . HIS A 1 45  ? 38.090 -19.055 18.408 1.00 19.30  ? 46  HIS A CG  1 
ATOM   429  N  ND1 . HIS A 1 45  ? 37.559 -20.074 19.190 1.00 20.94  ? 46  HIS A ND1 1 
ATOM   430  C  CD2 . HIS A 1 45  ? 39.322 -19.429 17.977 1.00 19.92  ? 46  HIS A CD2 1 
ATOM   431  C  CE1 . HIS A 1 45  ? 38.477 -21.036 19.207 1.00 19.99  ? 46  HIS A CE1 1 
ATOM   432  N  NE2 . HIS A 1 45  ? 39.549 -20.702 18.473 1.00 19.99  ? 46  HIS A NE2 1 
ATOM   433  N  N   . LYS A 1 46  ? 37.467 -14.298 18.509 1.00 18.50  ? 47  LYS A N   1 
ATOM   434  C  CA  . LYS A 1 46  ? 36.720 -13.058 18.230 1.00 17.62  ? 47  LYS A CA  1 
ATOM   435  C  C   . LYS A 1 46  ? 35.498 -13.318 17.356 1.00 20.49  ? 47  LYS A C   1 
ATOM   436  O  O   . LYS A 1 46  ? 34.422 -12.826 17.683 1.00 18.46  ? 47  LYS A O   1 
ATOM   437  C  CB  . LYS A 1 46  ? 37.612 -12.036 17.520 1.00 19.70  ? 47  LYS A CB  1 
ATOM   438  C  CG  . LYS A 1 46  ? 38.656 -11.449 18.459 1.00 19.07  ? 47  LYS A CG  1 
ATOM   439  C  CD  . LYS A 1 46  ? 39.583 -10.511 17.675 1.00 20.14  ? 47  LYS A CD  1 
ATOM   440  C  CE  . LYS A 1 46  ? 40.713 -10.060 18.560 1.00 24.15  ? 47  LYS A CE  1 
ATOM   441  N  NZ  . LYS A 1 46  ? 41.652 -9.184  17.803 1.00 26.36  ? 47  LYS A NZ  1 
ATOM   442  N  N   . THR A 1 47  ? 35.641 -14.141 16.290 1.00 18.04  ? 48  THR A N   1 
ATOM   443  C  CA  . THR A 1 47  ? 34.492 -14.343 15.394 1.00 17.16  ? 48  THR A CA  1 
ATOM   444  C  C   . THR A 1 47  ? 33.316 -15.015 16.063 1.00 18.59  ? 48  THR A C   1 
ATOM   445  O  O   . THR A 1 47  ? 32.180 -14.653 15.769 1.00 17.41  ? 48  THR A O   1 
ATOM   446  C  CB  . THR A 1 47  ? 34.885 -15.049 14.112 1.00 23.31  ? 48  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 47  ? 35.497 -16.271 14.467 1.00 23.78  ? 48  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 47  ? 35.779 -14.172 13.228 1.00 25.57  ? 48  THR A CG2 1 
ATOM   449  N  N   . VAL A 1 48  ? 33.578 -15.970 16.951 1.00 15.85  ? 49  VAL A N   1 
ATOM   450  C  CA  . VAL A 1 48  ? 32.487 -16.670 17.655 1.00 15.96  ? 49  VAL A CA  1 
ATOM   451  C  C   . VAL A 1 48  ? 31.820 -15.668 18.619 1.00 18.22  ? 49  VAL A C   1 
ATOM   452  O  O   . VAL A 1 48  ? 30.576 -15.621 18.718 1.00 16.49  ? 49  VAL A O   1 
ATOM   453  C  CB  . VAL A 1 48  ? 32.995 -17.935 18.402 1.00 18.34  ? 49  VAL A CB  1 
ATOM   454  C  CG1 . VAL A 1 48  ? 31.869 -18.558 19.252 1.00 18.15  ? 49  VAL A CG1 1 
ATOM   455  C  CG2 . VAL A 1 48  ? 33.519 -18.975 17.400 1.00 17.95  ? 49  VAL A CG2 1 
ATOM   456  N  N   . LEU A 1 49  ? 32.645 -14.889 19.355 1.00 15.74  ? 50  LEU A N   1 
ATOM   457  C  CA  . LEU A 1 49  ? 32.075 -13.876 20.276 1.00 16.48  ? 50  LEU A CA  1 
ATOM   458  C  C   . LEU A 1 49  ? 31.174 -12.887 19.503 1.00 18.75  ? 50  LEU A C   1 
ATOM   459  O  O   . LEU A 1 49  ? 30.062 -12.578 19.945 1.00 16.67  ? 50  LEU A O   1 
ATOM   460  C  CB  . LEU A 1 49  ? 33.210 -13.084 20.968 1.00 16.71  ? 50  LEU A CB  1 
ATOM   461  C  CG  . LEU A 1 49  ? 34.166 -13.866 21.891 1.00 18.97  ? 50  LEU A CG  1 
ATOM   462  C  CD1 . LEU A 1 49  ? 35.196 -12.891 22.522 1.00 19.11  ? 50  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A 1 49  ? 33.390 -14.607 22.994 1.00 20.01  ? 50  LEU A CD2 1 
ATOM   464  N  N   . MET A 1 50  ? 31.629 -12.428 18.332 1.00 16.10  ? 51  MET A N   1 
ATOM   465  C  CA  . MET A 1 50  ? 30.848 -11.494 17.509 1.00 16.28  ? 51  MET A CA  1 
ATOM   466  C  C   . MET A 1 50  ? 29.553 -12.141 17.027 1.00 19.05  ? 51  MET A C   1 
ATOM   467  O  O   . MET A 1 50  ? 28.510 -11.491 17.060 1.00 18.85  ? 51  MET A O   1 
ATOM   468  C  CB  . MET A 1 50  ? 31.645 -11.001 16.295 1.00 17.75  ? 51  MET A CB  1 
ATOM   469  C  CG  . MET A 1 50  ? 32.888 -10.198 16.680 1.00 20.02  ? 51  MET A CG  1 
ATOM   470  S  SD  . MET A 1 50  ? 33.922 -10.103 15.214 1.00 24.02  ? 51  MET A SD  1 
ATOM   471  C  CE  . MET A 1 50  ? 33.158 -8.736  14.415 1.00 21.69  ? 51  MET A CE  1 
ATOM   472  N  N   . ALA A 1 51  ? 29.614 -13.422 16.631 1.00 17.37  ? 52  ALA A N   1 
ATOM   473  C  CA  . ALA A 1 51  ? 28.449 -14.152 16.109 1.00 17.56  ? 52  ALA A CA  1 
ATOM   474  C  C   . ALA A 1 51  ? 27.342 -14.325 17.178 1.00 19.99  ? 52  ALA A C   1 
ATOM   475  O  O   . ALA A 1 51  ? 26.179 -14.525 16.830 1.00 20.46  ? 52  ALA A O   1 
ATOM   476  C  CB  . ALA A 1 51  ? 28.886 -15.530 15.580 1.00 18.04  ? 52  ALA A CB  1 
ATOM   477  N  N   . CYS A 1 52  ? 27.722 -14.263 18.464 1.00 16.69  ? 53  CYS A N   1 
ATOM   478  C  CA  . CYS A 1 52  ? 26.827 -14.507 19.591 1.00 16.53  ? 53  CYS A CA  1 
ATOM   479  C  C   . CYS A 1 52  ? 26.380 -13.289 20.361 1.00 20.37  ? 53  CYS A C   1 
ATOM   480  O  O   . CYS A 1 52  ? 25.412 -13.397 21.128 1.00 19.83  ? 53  CYS A O   1 
ATOM   481  C  CB  . CYS A 1 52  ? 27.503 -15.487 20.547 1.00 16.36  ? 53  CYS A CB  1 
ATOM   482  S  SG  . CYS A 1 52  ? 27.796 -17.123 19.837 1.00 19.57  ? 53  CYS A SG  1 
ATOM   483  N  N   . SER A 1 53  ? 27.146 -12.197 20.283 1.00 17.98  ? 54  SER A N   1 
ATOM   484  C  CA  . SER A 1 53  ? 26.929 -11.052 21.166 1.00 16.45  ? 54  SER A CA  1 
ATOM   485  C  C   . SER A 1 53  ? 26.964 -9.728  20.429 1.00 21.85  ? 54  SER A C   1 
ATOM   486  O  O   . SER A 1 53  ? 27.943 -9.439  19.731 1.00 19.24  ? 54  SER A O   1 
ATOM   487  C  CB  . SER A 1 53  ? 28.025 -11.104 22.229 1.00 18.15  ? 54  SER A CB  1 
ATOM   488  O  OG  . SER A 1 53  ? 28.410 -9.848  22.775 1.00 20.90  ? 54  SER A OG  1 
ATOM   489  N  N   . GLY A 1 54  ? 25.924 -8.912  20.622 1.00 20.17  ? 55  GLY A N   1 
ATOM   490  C  CA  . GLY A 1 54  ? 25.881 -7.581  20.021 1.00 20.35  ? 55  GLY A CA  1 
ATOM   491  C  C   . GLY A 1 54  ? 27.005 -6.694  20.524 1.00 23.01  ? 55  GLY A C   1 
ATOM   492  O  O   . GLY A 1 54  ? 27.535 -5.866  19.768 1.00 22.74  ? 55  GLY A O   1 
ATOM   493  N  N   . LEU A 1 55  ? 27.412 -6.885  21.806 1.00 20.71  ? 56  LEU A N   1 
ATOM   494  C  CA  . LEU A 1 55  ? 28.509 -6.092  22.377 1.00 20.47  ? 56  LEU A CA  1 
ATOM   495  C  C   . LEU A 1 55  ? 29.832 -6.436  21.683 1.00 21.74  ? 56  LEU A C   1 
ATOM   496  O  O   . LEU A 1 55  ? 30.535 -5.519  21.243 1.00 21.51  ? 56  LEU A O   1 
ATOM   497  C  CB  . LEU A 1 55  ? 28.633 -6.281  23.905 1.00 20.49  ? 56  LEU A CB  1 
ATOM   498  C  CG  . LEU A 1 55  ? 29.662 -5.360  24.590 1.00 25.03  ? 56  LEU A CG  1 
ATOM   499  C  CD1 . LEU A 1 55  ? 29.188 -3.883  24.598 1.00 26.15  ? 56  LEU A CD1 1 
ATOM   500  C  CD2 . LEU A 1 55  ? 29.961 -5.845  26.005 1.00 24.32  ? 56  LEU A CD2 1 
ATOM   501  N  N   . PHE A 1 56  ? 30.153 -7.749  21.564 1.00 18.22  ? 57  PHE A N   1 
ATOM   502  C  CA  . PHE A 1 56  ? 31.406 -8.149  20.903 1.00 17.99  ? 57  PHE A CA  1 
ATOM   503  C  C   . PHE A 1 56  ? 31.392 -7.824  19.432 1.00 21.86  ? 57  PHE A C   1 
ATOM   504  O  O   . PHE A 1 56  ? 32.433 -7.458  18.886 1.00 20.20  ? 57  PHE A O   1 
ATOM   505  C  CB  . PHE A 1 56  ? 31.759 -9.609  21.174 1.00 18.37  ? 57  PHE A CB  1 
ATOM   506  C  CG  . PHE A 1 56  ? 32.186 -9.835  22.607 1.00 19.02  ? 57  PHE A CG  1 
ATOM   507  C  CD1 . PHE A 1 56  ? 33.265 -9.134  23.150 1.00 20.80  ? 57  PHE A CD1 1 
ATOM   508  C  CD2 . PHE A 1 56  ? 31.550 -10.794 23.398 1.00 20.05  ? 57  PHE A CD2 1 
ATOM   509  C  CE1 . PHE A 1 56  ? 33.651 -9.326  24.489 1.00 21.84  ? 57  PHE A CE1 1 
ATOM   510  C  CE2 . PHE A 1 56  ? 31.969 -11.026 24.720 1.00 22.38  ? 57  PHE A CE2 1 
ATOM   511  C  CZ  . PHE A 1 56  ? 33.007 -10.279 25.261 1.00 20.33  ? 57  PHE A CZ  1 
ATOM   512  N  N   . TYR A 1 57  ? 30.205 -7.899  18.798 1.00 19.64  ? 58  TYR A N   1 
ATOM   513  C  CA  . TYR A 1 57  ? 30.102 -7.504  17.388 1.00 20.70  ? 58  TYR A CA  1 
ATOM   514  C  C   . TYR A 1 57  ? 30.532 -6.020  17.229 1.00 25.05  ? 58  TYR A C   1 
ATOM   515  O  O   . TYR A 1 57  ? 31.323 -5.702  16.338 1.00 23.55  ? 58  TYR A O   1 
ATOM   516  C  CB  . TYR A 1 57  ? 28.669 -7.735  16.890 1.00 22.62  ? 58  TYR A CB  1 
ATOM   517  C  CG  . TYR A 1 57  ? 28.448 -7.213  15.493 1.00 26.17  ? 58  TYR A CG  1 
ATOM   518  C  CD1 . TYR A 1 57  ? 29.015 -7.850  14.392 1.00 27.72  ? 58  TYR A CD1 1 
ATOM   519  C  CD2 . TYR A 1 57  ? 27.683 -6.075  15.271 1.00 30.75  ? 58  TYR A CD2 1 
ATOM   520  C  CE1 . TYR A 1 57  ? 28.818 -7.364  13.098 1.00 29.68  ? 58  TYR A CE1 1 
ATOM   521  C  CE2 . TYR A 1 57  ? 27.481 -5.582  13.988 1.00 33.63  ? 58  TYR A CE2 1 
ATOM   522  C  CZ  . TYR A 1 57  ? 28.042 -6.235  12.908 1.00 40.51  ? 58  TYR A CZ  1 
ATOM   523  O  OH  . TYR A 1 57  ? 27.816 -5.728  11.663 1.00 47.60  ? 58  TYR A OH  1 
ATOM   524  N  N   A SER A 1 58  ? 30.008 -5.132  18.093 0.52 22.51  ? 59  SER A N   1 
ATOM   525  N  N   B SER A 1 58  ? 30.004 -5.134  18.094 0.48 22.66  ? 59  SER A N   1 
ATOM   526  C  CA  A SER A 1 58  ? 30.323 -3.702  18.093 0.52 23.60  ? 59  SER A CA  1 
ATOM   527  C  CA  B SER A 1 58  ? 30.322 -3.705  18.099 0.48 23.81  ? 59  SER A CA  1 
ATOM   528  C  C   A SER A 1 58  ? 31.809 -3.459  18.399 0.52 28.04  ? 59  SER A C   1 
ATOM   529  C  C   B SER A 1 58  ? 31.816 -3.487  18.373 0.48 27.99  ? 59  SER A C   1 
ATOM   530  O  O   A SER A 1 58  ? 32.442 -2.659  17.718 0.52 28.97  ? 59  SER A O   1 
ATOM   531  O  O   B SER A 1 58  ? 32.457 -2.732  17.648 0.48 28.74  ? 59  SER A O   1 
ATOM   532  C  CB  A SER A 1 58  ? 29.432 -2.969  19.092 0.52 26.13  ? 59  SER A CB  1 
ATOM   533  C  CB  B SER A 1 58  ? 29.477 -2.979  19.144 0.48 26.84  ? 59  SER A CB  1 
ATOM   534  O  OG  A SER A 1 58  ? 28.096 -2.923  18.618 0.52 27.46  ? 59  SER A OG  1 
ATOM   535  O  OG  B SER A 1 58  ? 29.795 -1.597  19.178 0.48 31.20  ? 59  SER A OG  1 
ATOM   536  N  N   . ILE A 1 59  ? 32.367 -4.176  19.396 1.00 24.04  ? 60  ILE A N   1 
ATOM   537  C  CA  . ILE A 1 59  ? 33.781 -4.058  19.797 1.00 22.92  ? 60  ILE A CA  1 
ATOM   538  C  C   . ILE A 1 59  ? 34.726 -4.433  18.672 1.00 25.09  ? 60  ILE A C   1 
ATOM   539  O  O   . ILE A 1 59  ? 35.623 -3.646  18.342 1.00 25.99  ? 60  ILE A O   1 
ATOM   540  C  CB  . ILE A 1 59  ? 34.104 -4.886  21.101 1.00 24.57  ? 60  ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 59  ? 33.412 -4.290  22.337 1.00 24.98  ? 60  ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 59  ? 35.639 -4.990  21.351 1.00 23.47  ? 60  ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 59  ? 33.377 -5.272  23.542 1.00 26.01  ? 60  ILE A CD1 1 
ATOM   544  N  N   . PHE A 1 60  ? 34.544 -5.624  18.085 1.00 20.45  ? 61  PHE A N   1 
ATOM   545  C  CA  . PHE A 1 60  ? 35.519 -6.073  17.099 1.00 21.56  ? 61  PHE A CA  1 
ATOM   546  C  C   . PHE A 1 60  ? 35.280 -5.538  15.685 1.00 25.98  ? 61  PHE A C   1 
ATOM   547  O  O   . PHE A 1 60  ? 36.130 -5.770  14.821 1.00 26.91  ? 61  PHE A O   1 
ATOM   548  C  CB  . PHE A 1 60  ? 35.675 -7.603  17.140 1.00 21.72  ? 61  PHE A CB  1 
ATOM   549  C  CG  . PHE A 1 60  ? 36.091 -8.105  18.514 1.00 21.84  ? 61  PHE A CG  1 
ATOM   550  C  CD1 . PHE A 1 60  ? 37.287 -7.685  19.098 1.00 24.34  ? 61  PHE A CD1 1 
ATOM   551  C  CD2 . PHE A 1 60  ? 35.280 -8.983  19.223 1.00 22.70  ? 61  PHE A CD2 1 
ATOM   552  C  CE1 . PHE A 1 60  ? 37.663 -8.139  20.372 1.00 24.97  ? 61  PHE A CE1 1 
ATOM   553  C  CE2 . PHE A 1 60  ? 35.664 -9.457  20.488 1.00 25.33  ? 61  PHE A CE2 1 
ATOM   554  C  CZ  . PHE A 1 60  ? 36.850 -9.035  21.054 1.00 22.98  ? 61  PHE A CZ  1 
ATOM   555  N  N   . THR A 1 61  ? 34.210 -4.751  15.458 1.00 23.70  ? 62  THR A N   1 
ATOM   556  C  CA  . THR A 1 61  ? 34.038 -4.049  14.168 1.00 24.05  ? 62  THR A CA  1 
ATOM   557  C  C   . THR A 1 61  ? 34.597 -2.625  14.295 1.00 30.62  ? 62  THR A C   1 
ATOM   558  O  O   . THR A 1 61  ? 34.686 -1.890  13.303 1.00 30.07  ? 62  THR A O   1 
ATOM   559  C  CB  . THR A 1 61  ? 32.613 -4.074  13.619 1.00 30.49  ? 62  THR A CB  1 
ATOM   560  O  OG1 . THR A 1 61  ? 31.725 -3.564  14.606 1.00 27.34  ? 62  THR A OG1 1 
ATOM   561  C  CG2 . THR A 1 61  ? 32.181 -5.478  13.129 1.00 27.32  ? 62  THR A CG2 1 
ATOM   562  N  N   . ASP A 1 62  ? 35.023 -2.247  15.511 1.00 27.28  ? 63  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 62  ? 35.631 -0.933  15.717 1.00 28.19  ? 63  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 62  ? 37.049 -0.997  15.166 1.00 34.11  ? 63  ASP A C   1 
ATOM   565  O  O   . ASP A 1 62  ? 37.796 -1.899  15.533 1.00 31.57  ? 63  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 62  ? 35.642 -0.553  17.201 1.00 28.69  ? 63  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 62  ? 36.384 0.741   17.413 1.00 39.48  ? 63  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 62  ? 35.770 1.804   17.231 1.00 44.43  ? 63  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 62  ? 37.606 0.686   17.685 1.00 38.91  ? 63  ASP A OD2 1 
ATOM   570  N  N   . GLN A 1 63  ? 37.432 -0.013  14.322 1.00 35.16  ? 64  GLN A N   1 
ATOM   571  C  CA  . GLN A 1 63  ? 38.732 0.011   13.657 1.00 36.81  ? 64  GLN A CA  1 
ATOM   572  C  C   . GLN A 1 63  ? 39.931 -0.043  14.606 1.00 41.67  ? 64  GLN A C   1 
ATOM   573  O  O   . GLN A 1 63  ? 40.972 -0.543  14.181 1.00 43.79  ? 64  GLN A O   1 
ATOM   574  C  CB  . GLN A 1 63  ? 38.849 1.191   12.683 1.00 40.44  ? 64  GLN A CB  1 
ATOM   575  C  CG  . GLN A 1 63  ? 38.001 1.015   11.424 1.00 56.13  ? 64  GLN A CG  1 
ATOM   576  N  N   . LEU A 1 64  ? 39.816 0.480   15.860 1.00 34.88  ? 65  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 64  ? 40.920 0.400   16.823 1.00 33.44  ? 65  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 64  ? 40.835 -0.851  17.672 1.00 36.41  ? 65  LEU A C   1 
ATOM   579  O  O   . LEU A 1 64  ? 41.859 -1.456  17.962 1.00 38.64  ? 65  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 64  ? 40.943 1.608   17.781 1.00 34.18  ? 65  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 64  ? 41.601 2.873   17.268 1.00 40.88  ? 65  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 64  ? 41.490 3.974   18.291 1.00 41.66  ? 65  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 64  ? 43.073 2.652   16.909 1.00 45.79  ? 65  LEU A CD2 1 
ATOM   584  N  N   . LYS A 1 65  ? 39.639 -1.178  18.173 1.00 29.27  ? 66  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 65  ? 39.476 -2.306  19.093 1.00 27.05  ? 66  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 65  ? 39.596 -3.669  18.427 1.00 32.21  ? 66  LYS A C   1 
ATOM   587  O  O   . LYS A 1 65  ? 39.961 -4.621  19.107 1.00 30.19  ? 66  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 65  ? 38.159 -2.218  19.889 1.00 27.68  ? 66  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 65  ? 38.047 -0.997  20.793 1.00 29.42  ? 66  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 65  ? 36.748 -1.083  21.586 1.00 26.39  ? 66  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 65  ? 36.445 0.223   22.298 1.00 31.46  ? 66  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 65  ? 35.840 1.238   21.401 1.00 30.35  ? 66  LYS A NZ  1 
ATOM   593  N  N   . CYS A 1 66  ? 39.318 -3.756  17.110 1.00 32.04  ? 67  CYS A N   1 
ATOM   594  C  CA  . CYS A 1 66  ? 39.413 -5.013  16.345 1.00 31.98  ? 67  CYS A CA  1 
ATOM   595  C  C   . CYS A 1 66  ? 40.806 -5.646  16.486 1.00 37.10  ? 67  CYS A C   1 
ATOM   596  O  O   . CYS A 1 66  ? 40.942 -6.862  16.325 1.00 37.52  ? 67  CYS A O   1 
ATOM   597  C  CB  . CYS A 1 66  ? 39.056 -4.784  14.878 1.00 33.24  ? 67  CYS A CB  1 
ATOM   598  S  SG  . CYS A 1 66  ? 40.238 -3.745  13.972 1.00 39.28  ? 67  CYS A SG  1 
ATOM   599  N  N   . ASN A 1 67  ? 41.833 -4.802  16.756 1.00 33.89  ? 68  ASN A N   1 
ATOM   600  C  CA  . ASN A 1 67  ? 43.234 -5.198  16.879 1.00 34.82  ? 68  ASN A CA  1 
ATOM   601  C  C   . ASN A 1 67  ? 43.706 -5.483  18.310 1.00 37.35  ? 68  ASN A C   1 
ATOM   602  O  O   . ASN A 1 67  ? 44.869 -5.841  18.514 1.00 36.93  ? 68  ASN A O   1 
ATOM   603  C  CB  . ASN A 1 67  ? 44.137 -4.166  16.195 1.00 37.30  ? 68  ASN A CB  1 
ATOM   604  C  CG  . ASN A 1 67  ? 43.909 -4.122  14.694 1.00 50.01  ? 68  ASN A CG  1 
ATOM   605  O  OD1 . ASN A 1 67  ? 43.869 -3.054  14.085 1.00 50.17  ? 68  ASN A OD1 1 
ATOM   606  N  ND2 . ASN A 1 67  ? 43.708 -5.279  14.064 1.00 41.13  ? 68  ASN A ND2 1 
ATOM   607  N  N   . LEU A 1 68  ? 42.815 -5.366  19.292 1.00 33.78  ? 69  LEU A N   1 
ATOM   608  C  CA  . LEU A 1 68  ? 43.203 -5.638  20.671 1.00 32.94  ? 69  LEU A CA  1 
ATOM   609  C  C   . LEU A 1 68  ? 43.187 -7.137  20.947 1.00 33.83  ? 69  LEU A C   1 
ATOM   610  O  O   . LEU A 1 68  ? 42.300 -7.830  20.440 1.00 31.15  ? 69  LEU A O   1 
ATOM   611  C  CB  . LEU A 1 68  ? 42.243 -4.924  21.643 1.00 33.20  ? 69  LEU A CB  1 
ATOM   612  C  CG  . LEU A 1 68  ? 42.274 -3.389  21.622 1.00 38.03  ? 69  LEU A CG  1 
ATOM   613  C  CD1 . LEU A 1 68  ? 41.190 -2.827  22.516 1.00 37.80  ? 69  LEU A CD1 1 
ATOM   614  C  CD2 . LEU A 1 68  ? 43.655 -2.835  22.044 1.00 39.49  ? 69  LEU A CD2 1 
ATOM   615  N  N   . SER A 1 69  ? 44.152 -7.611  21.770 1.00 30.25  ? 70  SER A N   1 
ATOM   616  C  CA  A SER A 1 69  ? 44.292 -9.013  22.180 0.42 29.22  ? 70  SER A CA  1 
ATOM   617  C  CA  B SER A 1 69  ? 44.226 -9.025  22.147 0.58 29.71  ? 70  SER A CA  1 
ATOM   618  C  C   . SER A 1 69  ? 43.645 -9.222  23.552 1.00 30.05  ? 70  SER A C   1 
ATOM   619  O  O   . SER A 1 69  ? 43.464 -10.353 23.992 1.00 26.19  ? 70  SER A O   1 
ATOM   620  C  CB  A SER A 1 69  ? 45.770 -9.393  22.252 0.42 33.22  ? 70  SER A CB  1 
ATOM   621  C  CB  B SER A 1 69  ? 45.664 -9.534  22.070 0.58 34.90  ? 70  SER A CB  1 
ATOM   622  O  OG  A SER A 1 69  ? 46.378 -9.330  20.974 0.42 37.55  ? 70  SER A OG  1 
ATOM   623  O  OG  B SER A 1 69  ? 46.503 -8.823  22.963 0.58 42.56  ? 70  SER A OG  1 
ATOM   624  N  N   . VAL A 1 70  ? 43.359 -8.113  24.263 1.00 26.82  ? 71  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 70  ? 42.757 -8.158  25.598 1.00 25.98  ? 71  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 70  ? 41.578 -7.187  25.639 1.00 27.86  ? 71  VAL A C   1 
ATOM   627  O  O   . VAL A 1 70  ? 41.723 -6.021  25.230 1.00 27.64  ? 71  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 70  ? 43.796 -7.813  26.717 1.00 31.03  ? 71  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 70  ? 43.147 -7.801  28.107 1.00 30.89  ? 71  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 70  ? 44.992 -8.766  26.691 1.00 31.85  ? 71  VAL A CG2 1 
ATOM   631  N  N   . ILE A 1 71  ? 40.427 -7.665  26.153 1.00 22.14  ? 72  ILE A N   1 
ATOM   632  C  CA  . ILE A 1 71  ? 39.223 -6.858  26.370 1.00 21.22  ? 72  ILE A CA  1 
ATOM   633  C  C   . ILE A 1 71  ? 38.832 -6.973  27.833 1.00 25.12  ? 72  ILE A C   1 
ATOM   634  O  O   . ILE A 1 71  ? 38.628 -8.085  28.332 1.00 25.21  ? 72  ILE A O   1 
ATOM   635  C  CB  . ILE A 1 71  ? 38.055 -7.205  25.398 1.00 22.53  ? 72  ILE A CB  1 
ATOM   636  C  CG1 . ILE A 1 71  ? 38.456 -7.044  23.897 1.00 23.15  ? 72  ILE A CG1 1 
ATOM   637  C  CG2 . ILE A 1 71  ? 36.768 -6.415  25.736 1.00 23.19  ? 72  ILE A CG2 1 
ATOM   638  C  CD1 . ILE A 1 71  ? 38.854 -5.614  23.404 1.00 28.01  ? 72  ILE A CD1 1 
ATOM   639  N  N   . ASN A 1 72  ? 38.721 -5.825  28.521 1.00 23.50  ? 73  ASN A N   1 
ATOM   640  C  CA  . ASN A 1 72  ? 38.332 -5.805  29.921 1.00 24.03  ? 73  ASN A CA  1 
ATOM   641  C  C   . ASN A 1 72  ? 36.854 -5.473  30.034 1.00 26.17  ? 73  ASN A C   1 
ATOM   642  O  O   . ASN A 1 72  ? 36.417 -4.399  29.589 1.00 24.11  ? 73  ASN A O   1 
ATOM   643  C  CB  . ASN A 1 72  ? 39.155 -4.761  30.705 1.00 27.02  ? 73  ASN A CB  1 
ATOM   644  C  CG  . ASN A 1 72  ? 40.631 -4.982  30.634 1.00 45.17  ? 73  ASN A CG  1 
ATOM   645  O  OD1 . ASN A 1 72  ? 41.140 -6.020  31.034 1.00 34.41  ? 73  ASN A OD1 1 
ATOM   646  N  ND2 . ASN A 1 72  ? 41.352 -4.007  30.132 1.00 41.86  ? 73  ASN A ND2 1 
ATOM   647  N  N   . LEU A 1 73  ? 36.086 -6.368  30.649 1.00 20.74  ? 74  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 73  ? 34.666 -6.109  30.835 1.00 20.28  ? 74  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 73  ? 34.428 -5.211  32.042 1.00 24.12  ? 74  LEU A C   1 
ATOM   650  O  O   . LEU A 1 73  ? 35.309 -5.055  32.903 1.00 25.13  ? 74  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 73  ? 33.832 -7.402  30.963 1.00 20.20  ? 74  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 73  ? 33.902 -8.422  29.793 1.00 23.07  ? 74  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 73  ? 32.776 -9.482  29.934 1.00 23.12  ? 74  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 73  ? 33.875 -7.729  28.411 1.00 24.19  ? 74  LEU A CD2 1 
ATOM   655  N  N   . ASP A 1 74  ? 33.231 -4.638  32.105 1.00 20.78  ? 75  ASP A N   1 
ATOM   656  C  CA  . ASP A 1 74  ? 32.808 -3.736  33.190 1.00 22.88  ? 75  ASP A CA  1 
ATOM   657  C  C   . ASP A 1 74  ? 32.980 -4.488  34.531 1.00 27.66  ? 75  ASP A C   1 
ATOM   658  O  O   . ASP A 1 74  ? 32.627 -5.669  34.610 1.00 26.48  ? 75  ASP A O   1 
ATOM   659  C  CB  . ASP A 1 74  ? 31.338 -3.330  32.975 1.00 24.69  ? 75  ASP A CB  1 
ATOM   660  C  CG  . ASP A 1 74  ? 30.803 -2.303  33.963 1.00 31.82  ? 75  ASP A CG  1 
ATOM   661  O  OD1 . ASP A 1 74  ? 30.668 -2.639  35.160 1.00 31.80  ? 75  ASP A OD1 1 
ATOM   662  O  OD2 . ASP A 1 74  ? 30.491 -1.177  33.535 1.00 34.50  ? 75  ASP A OD2 1 
ATOM   663  N  N   . PRO A 1 75  ? 33.576 -3.842  35.559 1.00 28.01  ? 76  PRO A N   1 
ATOM   664  C  CA  . PRO A 1 75  ? 33.789 -4.545  36.846 1.00 28.33  ? 76  PRO A CA  1 
ATOM   665  C  C   . PRO A 1 75  ? 32.544 -5.091  37.520 1.00 31.26  ? 76  PRO A C   1 
ATOM   666  O  O   . PRO A 1 75  ? 32.682 -5.921  38.411 1.00 32.41  ? 76  PRO A O   1 
ATOM   667  C  CB  . PRO A 1 75  ? 34.485 -3.504  37.726 1.00 31.06  ? 76  PRO A CB  1 
ATOM   668  C  CG  . PRO A 1 75  ? 34.185 -2.171  37.082 1.00 36.49  ? 76  PRO A CG  1 
ATOM   669  C  CD  . PRO A 1 75  ? 34.085 -2.452  35.612 1.00 30.49  ? 76  PRO A CD  1 
ATOM   670  N  N   . GLU A 1 76  ? 31.341 -4.658  37.113 1.00 28.11  ? 77  GLU A N   1 
ATOM   671  C  CA  . GLU A 1 76  ? 30.109 -5.182  37.710 1.00 29.52  ? 77  GLU A CA  1 
ATOM   672  C  C   . GLU A 1 76  ? 29.796 -6.590  37.163 1.00 29.37  ? 77  GLU A C   1 
ATOM   673  O  O   . GLU A 1 76  ? 28.950 -7.285  37.727 1.00 28.73  ? 77  GLU A O   1 
ATOM   674  C  CB  . GLU A 1 76  ? 28.916 -4.236  37.457 1.00 32.12  ? 77  GLU A CB  1 
ATOM   675  C  CG  . GLU A 1 76  ? 28.869 -3.036  38.389 1.00 51.98  ? 77  GLU A CG  1 
ATOM   676  C  CD  . GLU A 1 76  ? 28.343 -3.357  39.773 1.00 83.44  ? 77  GLU A CD  1 
ATOM   677  O  OE1 . GLU A 1 76  ? 27.116 -3.570  39.909 1.00 83.40  ? 77  GLU A OE1 1 
ATOM   678  O  OE2 . GLU A 1 76  ? 29.161 -3.412  40.720 1.00 83.44  ? 77  GLU A OE2 1 
ATOM   679  N  N   . ILE A 1 77  ? 30.473 -7.006  36.073 1.00 24.79  ? 78  ILE A N   1 
ATOM   680  C  CA  . ILE A 1 77  ? 30.216 -8.316  35.471 1.00 24.23  ? 78  ILE A CA  1 
ATOM   681  C  C   . ILE A 1 77  ? 30.811 -9.435  36.302 1.00 28.46  ? 78  ILE A C   1 
ATOM   682  O  O   . ILE A 1 77  ? 31.984 -9.401  36.661 1.00 27.31  ? 78  ILE A O   1 
ATOM   683  C  CB  . ILE A 1 77  ? 30.645 -8.375  33.988 1.00 25.74  ? 78  ILE A CB  1 
ATOM   684  C  CG1 . ILE A 1 77  ? 29.914 -7.271  33.160 1.00 26.61  ? 78  ILE A CG1 1 
ATOM   685  C  CG2 . ILE A 1 77  ? 30.413 -9.794  33.404 1.00 21.83  ? 78  ILE A CG2 1 
ATOM   686  C  CD1 . ILE A 1 77  ? 28.291 -7.323  33.192 1.00 33.00  ? 78  ILE A CD1 1 
ATOM   687  N  N   . ASN A 1 78  ? 29.983 -10.426 36.573 1.00 27.50  ? 79  ASN A N   1 
ATOM   688  C  CA  . ASN A 1 78  ? 30.305 -11.603 37.358 1.00 28.56  ? 79  ASN A CA  1 
ATOM   689  C  C   . ASN A 1 78  ? 31.029 -12.654 36.496 1.00 27.96  ? 79  ASN A C   1 
ATOM   690  O  O   . ASN A 1 78  ? 30.488 -13.056 35.465 1.00 26.10  ? 79  ASN A O   1 
ATOM   691  C  CB  . ASN A 1 78  ? 28.994 -12.155 37.957 1.00 32.47  ? 79  ASN A CB  1 
ATOM   692  C  CG  . ASN A 1 78  ? 29.152 -13.456 38.698 1.00 45.67  ? 79  ASN A CG  1 
ATOM   693  O  OD1 . ASN A 1 78  ? 28.831 -14.520 38.178 1.00 34.38  ? 79  ASN A OD1 1 
ATOM   694  N  ND2 . ASN A 1 78  ? 29.653 -13.394 39.924 1.00 39.69  ? 79  ASN A ND2 1 
ATOM   695  N  N   . PRO A 1 79  ? 32.239 -13.133 36.906 1.00 25.22  ? 80  PRO A N   1 
ATOM   696  C  CA  . PRO A 1 79  ? 32.951 -14.142 36.096 1.00 24.78  ? 80  PRO A CA  1 
ATOM   697  C  C   . PRO A 1 79  ? 32.163 -15.433 35.855 1.00 27.92  ? 80  PRO A C   1 
ATOM   698  O  O   . PRO A 1 79  ? 32.232 -15.968 34.748 1.00 27.41  ? 80  PRO A O   1 
ATOM   699  C  CB  . PRO A 1 79  ? 34.219 -14.411 36.910 1.00 27.96  ? 80  PRO A CB  1 
ATOM   700  C  CG  . PRO A 1 79  ? 34.418 -13.151 37.718 1.00 32.71  ? 80  PRO A CG  1 
ATOM   701  C  CD  . PRO A 1 79  ? 33.034 -12.748 38.092 1.00 28.53  ? 80  PRO A CD  1 
ATOM   702  N  N   . GLU A 1 80  ? 31.397 -15.920 36.860 1.00 25.10  ? 81  GLU A N   1 
ATOM   703  C  CA  . GLU A 1 80  ? 30.621 -17.155 36.641 1.00 24.83  ? 81  GLU A CA  1 
ATOM   704  C  C   . GLU A 1 80  ? 29.544 -16.945 35.563 1.00 25.99  ? 81  GLU A C   1 
ATOM   705  O  O   . GLU A 1 80  ? 29.429 -17.782 34.676 1.00 23.84  ? 81  GLU A O   1 
ATOM   706  C  CB  . GLU A 1 80  ? 30.008 -17.691 37.939 1.00 27.43  ? 81  GLU A CB  1 
ATOM   707  C  CG  . GLU A 1 80  ? 29.375 -19.060 37.715 1.00 34.14  ? 81  GLU A CG  1 
ATOM   708  C  CD  . GLU A 1 80  ? 28.556 -19.645 38.852 1.00 58.94  ? 81  GLU A CD  1 
ATOM   709  O  OE1 . GLU A 1 80  ? 28.632 -20.879 39.050 1.00 58.64  ? 81  GLU A OE1 1 
ATOM   710  O  OE2 . GLU A 1 80  ? 27.825 -18.886 39.528 1.00 53.43  ? 81  GLU A OE2 1 
ATOM   711  N  N   . GLY A 1 81  ? 28.815 -15.816 35.629 1.00 24.80  ? 82  GLY A N   1 
ATOM   712  C  CA  . GLY A 1 81  ? 27.802 -15.469 34.631 1.00 24.21  ? 82  GLY A CA  1 
ATOM   713  C  C   . GLY A 1 81  ? 28.420 -15.420 33.242 1.00 25.21  ? 82  GLY A C   1 
ATOM   714  O  O   . GLY A 1 81  ? 27.864 -15.968 32.274 1.00 22.30  ? 82  GLY A O   1 
ATOM   715  N  N   . PHE A 1 82  ? 29.616 -14.819 33.147 1.00 20.98  ? 83  PHE A N   1 
ATOM   716  C  CA  . PHE A 1 82  ? 30.307 -14.762 31.855 1.00 19.54  ? 83  PHE A CA  1 
ATOM   717  C  C   . PHE A 1 82  ? 30.676 -16.157 31.380 1.00 21.71  ? 83  PHE A C   1 
ATOM   718  O  O   . PHE A 1 82  ? 30.500 -16.459 30.212 1.00 20.50  ? 83  PHE A O   1 
ATOM   719  C  CB  . PHE A 1 82  ? 31.578 -13.895 31.902 1.00 20.60  ? 83  PHE A CB  1 
ATOM   720  C  CG  . PHE A 1 82  ? 32.174 -13.770 30.513 1.00 20.32  ? 83  PHE A CG  1 
ATOM   721  C  CD1 . PHE A 1 82  ? 31.609 -12.913 29.570 1.00 22.93  ? 83  PHE A CD1 1 
ATOM   722  C  CD2 . PHE A 1 82  ? 33.258 -14.553 30.130 1.00 20.87  ? 83  PHE A CD2 1 
ATOM   723  C  CE1 . PHE A 1 82  ? 32.110 -12.852 28.265 1.00 23.23  ? 83  PHE A CE1 1 
ATOM   724  C  CE2 . PHE A 1 82  ? 33.758 -14.494 28.826 1.00 22.71  ? 83  PHE A CE2 1 
ATOM   725  C  CZ  . PHE A 1 82  ? 33.173 -13.654 27.900 1.00 21.53  ? 83  PHE A CZ  1 
ATOM   726  N  N   . CYS A 1 83  ? 31.250 -16.972 32.262 1.00 21.48  ? 84  CYS A N   1 
ATOM   727  C  CA  . CYS A 1 83  ? 31.679 -18.338 31.930 1.00 22.84  ? 84  CYS A CA  1 
ATOM   728  C  C   . CYS A 1 83  ? 30.489 -19.162 31.363 1.00 24.39  ? 84  CYS A C   1 
ATOM   729  O  O   . CYS A 1 83  ? 30.627 -19.847 30.333 1.00 22.24  ? 84  CYS A O   1 
ATOM   730  C  CB  . CYS A 1 83  ? 32.287 -19.005 33.161 1.00 26.36  ? 84  CYS A CB  1 
ATOM   731  S  SG  . CYS A 1 83  ? 32.932 -20.668 32.835 1.00 32.08  ? 84  CYS A SG  1 
ATOM   732  N  N   . ILE A 1 84  ? 29.318 -19.063 32.030 1.00 21.16  ? 85  ILE A N   1 
ATOM   733  C  CA  . ILE A 1 84  ? 28.093 -19.775 31.617 1.00 20.16  ? 85  ILE A CA  1 
ATOM   734  C  C   . ILE A 1 84  ? 27.688 -19.321 30.210 1.00 21.45  ? 85  ILE A C   1 
ATOM   735  O  O   . ILE A 1 84  ? 27.311 -20.150 29.354 1.00 19.43  ? 85  ILE A O   1 
ATOM   736  C  CB  . ILE A 1 84  ? 26.969 -19.553 32.671 1.00 23.18  ? 85  ILE A CB  1 
ATOM   737  C  CG1 . ILE A 1 84  ? 27.257 -20.383 33.963 1.00 23.57  ? 85  ILE A CG1 1 
ATOM   738  C  CG2 . ILE A 1 84  ? 25.550 -19.843 32.090 1.00 22.49  ? 85  ILE A CG2 1 
ATOM   739  C  CD1 . ILE A 1 84  ? 26.507 -19.852 35.191 1.00 30.05  ? 85  ILE A CD1 1 
ATOM   740  N  N   . LEU A 1 85  ? 27.777 -18.022 29.966 1.00 18.72  ? 86  LEU A N   1 
ATOM   741  C  CA  . LEU A 1 85  ? 27.414 -17.473 28.657 1.00 18.61  ? 86  LEU A CA  1 
ATOM   742  C  C   . LEU A 1 85  ? 28.413 -17.830 27.586 1.00 20.86  ? 86  LEU A C   1 
ATOM   743  O  O   . LEU A 1 85  ? 28.006 -18.100 26.461 1.00 19.13  ? 86  LEU A O   1 
ATOM   744  C  CB  . LEU A 1 85  ? 27.154 -15.974 28.721 1.00 19.70  ? 86  LEU A CB  1 
ATOM   745  C  CG  . LEU A 1 85  ? 25.856 -15.597 29.482 1.00 25.39  ? 86  LEU A CG  1 
ATOM   746  C  CD1 . LEU A 1 85  ? 25.786 -14.128 29.705 1.00 26.66  ? 86  LEU A CD1 1 
ATOM   747  C  CD2 . LEU A 1 85  ? 24.604 -16.067 28.723 1.00 27.40  ? 86  LEU A CD2 1 
ATOM   748  N  N   . LEU A 1 86  ? 29.719 -17.841 27.925 1.00 18.69  ? 87  LEU A N   1 
ATOM   749  C  CA  . LEU A 1 86  ? 30.749 -18.241 26.958 1.00 17.83  ? 87  LEU A CA  1 
ATOM   750  C  C   . LEU A 1 86  ? 30.518 -19.712 26.566 1.00 20.50  ? 87  LEU A C   1 
ATOM   751  O  O   . LEU A 1 86  ? 30.610 -20.059 25.389 1.00 19.32  ? 87  LEU A O   1 
ATOM   752  C  CB  . LEU A 1 86  ? 32.148 -18.041 27.559 1.00 17.73  ? 87  LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 86  ? 33.323 -18.334 26.598 1.00 22.08  ? 87  LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 86  ? 33.307 -17.404 25.358 1.00 20.97  ? 87  LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 86  ? 34.673 -18.229 27.352 1.00 25.89  ? 87  LEU A CD2 1 
ATOM   756  N  N   . ASP A 1 87  ? 30.214 -20.577 27.552 1.00 19.40  ? 88  ASP A N   1 
ATOM   757  C  CA  . ASP A 1 87  ? 29.894 -21.978 27.274 1.00 18.88  ? 88  ASP A CA  1 
ATOM   758  C  C   . ASP A 1 87  ? 28.694 -22.074 26.346 1.00 21.03  ? 88  ASP A C   1 
ATOM   759  O  O   . ASP A 1 87  ? 28.737 -22.838 25.391 1.00 20.77  ? 88  ASP A O   1 
ATOM   760  C  CB  . ASP A 1 87  ? 29.593 -22.705 28.587 1.00 21.48  ? 88  ASP A CB  1 
ATOM   761  C  CG  . ASP A 1 87  ? 30.838 -23.057 29.372 1.00 33.28  ? 88  ASP A CG  1 
ATOM   762  O  OD1 . ASP A 1 87  ? 31.954 -22.970 28.795 1.00 32.77  ? 88  ASP A OD1 1 
ATOM   763  O  OD2 . ASP A 1 87  ? 30.702 -23.427 30.558 1.00 33.35  ? 88  ASP A OD2 1 
ATOM   764  N  N   . PHE A 1 88  ? 27.639 -21.284 26.605 1.00 18.95  ? 89  PHE A N   1 
ATOM   765  C  CA  . PHE A 1 88  ? 26.445 -21.233 25.748 1.00 17.49  ? 89  PHE A CA  1 
ATOM   766  C  C   . PHE A 1 88  ? 26.814 -20.841 24.309 1.00 19.15  ? 89  PHE A C   1 
ATOM   767  O  O   . PHE A 1 88  ? 26.339 -21.452 23.341 1.00 17.22  ? 89  PHE A O   1 
ATOM   768  C  CB  . PHE A 1 88  ? 25.387 -20.272 26.343 1.00 18.00  ? 89  PHE A CB  1 
ATOM   769  C  CG  . PHE A 1 88  ? 24.275 -19.992 25.366 1.00 18.18  ? 89  PHE A CG  1 
ATOM   770  C  CD1 . PHE A 1 88  ? 23.308 -20.956 25.097 1.00 20.34  ? 89  PHE A CD1 1 
ATOM   771  C  CD2 . PHE A 1 88  ? 24.273 -18.821 24.602 1.00 19.71  ? 89  PHE A CD2 1 
ATOM   772  C  CE1 . PHE A 1 88  ? 22.320 -20.729 24.145 1.00 20.19  ? 89  PHE A CE1 1 
ATOM   773  C  CE2 . PHE A 1 88  ? 23.280 -18.595 23.641 1.00 22.67  ? 89  PHE A CE2 1 
ATOM   774  C  CZ  . PHE A 1 88  ? 22.315 -19.552 23.416 1.00 21.30  ? 89  PHE A CZ  1 
ATOM   775  N  N   . MET A 1 89  ? 27.644 -19.807 24.164 1.00 15.49  ? 90  MET A N   1 
ATOM   776  C  CA  . MET A 1 89  ? 28.059 -19.367 22.816 1.00 14.52  ? 90  MET A CA  1 
ATOM   777  C  C   . MET A 1 89  ? 28.613 -20.511 21.994 1.00 18.86  ? 90  MET A C   1 
ATOM   778  O  O   . MET A 1 89  ? 28.254 -20.650 20.829 1.00 18.36  ? 90  MET A O   1 
ATOM   779  C  CB  . MET A 1 89  ? 29.143 -18.274 22.915 1.00 15.60  ? 90  MET A CB  1 
ATOM   780  C  CG  . MET A 1 89  ? 28.617 -16.983 23.497 1.00 17.52  ? 90  MET A CG  1 
ATOM   781  S  SD  . MET A 1 89  ? 29.990 -15.783 23.386 1.00 20.13  ? 90  MET A SD  1 
ATOM   782  C  CE  . MET A 1 89  ? 29.357 -14.526 24.579 1.00 20.16  ? 90  MET A CE  1 
ATOM   783  N  N   . TYR A 1 90  ? 29.467 -21.342 22.617 1.00 16.19  ? 91  TYR A N   1 
ATOM   784  C  CA  . TYR A 1 90  ? 30.150 -22.435 21.933 1.00 15.95  ? 91  TYR A CA  1 
ATOM   785  C  C   . TYR A 1 90  ? 29.396 -23.760 21.923 1.00 19.29  ? 91  TYR A C   1 
ATOM   786  O  O   . TYR A 1 90  ? 29.879 -24.704 21.293 1.00 18.46  ? 91  TYR A O   1 
ATOM   787  C  CB  . TYR A 1 90  ? 31.529 -22.649 22.565 1.00 17.06  ? 91  TYR A CB  1 
ATOM   788  C  CG  . TYR A 1 90  ? 32.590 -21.681 22.076 1.00 18.04  ? 91  TYR A CG  1 
ATOM   789  C  CD1 . TYR A 1 90  ? 32.753 -20.433 22.675 1.00 19.36  ? 91  TYR A CD1 1 
ATOM   790  C  CD2 . TYR A 1 90  ? 33.435 -22.019 21.019 1.00 18.70  ? 91  TYR A CD2 1 
ATOM   791  C  CE1 . TYR A 1 90  ? 33.739 -19.545 22.235 1.00 18.05  ? 91  TYR A CE1 1 
ATOM   792  C  CE2 . TYR A 1 90  ? 34.461 -21.165 20.611 1.00 18.85  ? 91  TYR A CE2 1 
ATOM   793  C  CZ  . TYR A 1 90  ? 34.585 -19.919 21.198 1.00 20.80  ? 91  TYR A CZ  1 
ATOM   794  O  OH  . TYR A 1 90  ? 35.606 -19.096 20.792 1.00 19.17  ? 91  TYR A OH  1 
ATOM   795  N  N   . THR A 1 91  ? 28.237 -23.865 22.617 1.00 16.29  ? 92  THR A N   1 
ATOM   796  C  CA  . THR A 1 91  ? 27.553 -25.174 22.670 1.00 17.48  ? 92  THR A CA  1 
ATOM   797  C  C   . THR A 1 91  ? 26.043 -25.156 22.415 1.00 20.26  ? 92  THR A C   1 
ATOM   798  O  O   . THR A 1 91  ? 25.464 -26.246 22.271 1.00 19.34  ? 92  THR A O   1 
ATOM   799  C  CB  . THR A 1 91  ? 27.743 -25.844 24.066 1.00 22.12  ? 92  THR A CB  1 
ATOM   800  O  OG1 . THR A 1 91  ? 27.075 -25.065 25.065 1.00 22.15  ? 92  THR A OG1 1 
ATOM   801  C  CG2 . THR A 1 91  ? 29.211 -26.062 24.453 1.00 21.80  ? 92  THR A CG2 1 
ATOM   802  N  N   . SER A 1 92  ? 25.395 -23.968 22.510 1.00 16.75  ? 93  SER A N   1 
ATOM   803  C  CA  . SER A 1 92  ? 23.915 -23.756 22.465 1.00 16.36  ? 93  SER A CA  1 
ATOM   804  C  C   . SER A 1 92  ? 23.259 -24.169 23.805 1.00 19.90  ? 93  SER A C   1 
ATOM   805  O  O   . SER A 1 92  ? 22.041 -24.052 23.935 1.00 20.18  ? 93  SER A O   1 
ATOM   806  C  CB  . SER A 1 92  ? 23.243 -24.564 21.340 1.00 18.42  ? 93  SER A CB  1 
ATOM   807  O  OG  . SER A 1 92  ? 23.873 -24.402 20.081 1.00 22.90  ? 93  SER A OG  1 
ATOM   808  N  N   A ARG A 1 93  ? 24.067 -24.629 24.782 0.60 18.01  ? 94  ARG A N   1 
ATOM   809  N  N   B ARG A 1 93  ? 24.045 -24.669 24.780 0.40 17.06  ? 94  ARG A N   1 
ATOM   810  C  CA  A ARG A 1 93  ? 23.584 -25.107 26.084 0.60 18.80  ? 94  ARG A CA  1 
ATOM   811  C  CA  B ARG A 1 93  ? 23.487 -25.105 26.066 0.40 17.46  ? 94  ARG A CA  1 
ATOM   812  C  C   A ARG A 1 93  ? 23.780 -24.042 27.146 0.60 22.08  ? 94  ARG A C   1 
ATOM   813  C  C   B ARG A 1 93  ? 23.763 -24.097 27.154 0.40 21.68  ? 94  ARG A C   1 
ATOM   814  O  O   A ARG A 1 93  ? 24.901 -23.546 27.334 0.60 20.69  ? 94  ARG A O   1 
ATOM   815  O  O   B ARG A 1 93  ? 24.909 -23.670 27.345 0.40 20.46  ? 94  ARG A O   1 
ATOM   816  C  CB  A ARG A 1 93  ? 24.317 -26.396 26.500 0.60 22.66  ? 94  ARG A CB  1 
ATOM   817  C  CB  B ARG A 1 93  ? 23.952 -26.513 26.455 0.40 18.87  ? 94  ARG A CB  1 
ATOM   818  C  CG  A ARG A 1 93  ? 24.178 -27.554 25.494 0.60 30.13  ? 94  ARG A CG  1 
ATOM   819  C  CG  B ARG A 1 93  ? 23.313 -27.588 25.581 0.40 16.45  ? 94  ARG A CG  1 
ATOM   820  C  CD  A ARG A 1 93  ? 25.121 -28.707 25.818 0.60 33.98  ? 94  ARG A CD  1 
ATOM   821  C  CD  B ARG A 1 93  ? 24.075 -28.888 25.621 0.40 29.54  ? 94  ARG A CD  1 
ATOM   822  N  NE  A ARG A 1 93  ? 24.888 -29.244 27.163 0.60 37.21  ? 94  ARG A NE  1 
ATOM   823  N  NE  B ARG A 1 93  ? 23.502 -29.876 24.706 0.40 36.27  ? 94  ARG A NE  1 
ATOM   824  C  CZ  A ARG A 1 93  ? 24.001 -30.193 27.447 0.60 49.52  ? 94  ARG A CZ  1 
ATOM   825  C  CZ  B ARG A 1 93  ? 23.343 -31.164 24.994 0.40 50.30  ? 94  ARG A CZ  1 
ATOM   826  N  NH1 A ARG A 1 93  ? 23.850 -30.614 28.694 0.60 36.43  ? 94  ARG A NH1 1 
ATOM   827  N  NH1 B ARG A 1 93  ? 22.826 -31.992 24.096 0.40 36.76  ? 94  ARG A NH1 1 
ATOM   828  N  NH2 A ARG A 1 93  ? 23.257 -30.725 26.485 0.60 38.15  ? 94  ARG A NH2 1 
ATOM   829  N  NH2 B ARG A 1 93  ? 23.699 -31.634 26.182 0.40 42.89  ? 94  ARG A NH2 1 
ATOM   830  N  N   . LEU A 1 94  ? 22.696 -23.716 27.864 1.00 19.66  ? 95  LEU A N   1 
ATOM   831  C  CA  . LEU A 1 94  ? 22.732 -22.711 28.909 1.00 19.93  ? 95  LEU A CA  1 
ATOM   832  C  C   . LEU A 1 94  ? 22.497 -23.342 30.272 1.00 25.02  ? 95  LEU A C   1 
ATOM   833  O  O   . LEU A 1 94  ? 21.435 -23.914 30.525 1.00 25.14  ? 95  LEU A O   1 
ATOM   834  C  CB  . LEU A 1 94  ? 21.693 -21.622 28.583 1.00 19.84  ? 95  LEU A CB  1 
ATOM   835  C  CG  . LEU A 1 94  ? 21.711 -20.411 29.527 1.00 23.59  ? 95  LEU A CG  1 
ATOM   836  C  CD1 . LEU A 1 94  ? 22.996 -19.572 29.309 1.00 22.56  ? 95  LEU A CD1 1 
ATOM   837  C  CD2 . LEU A 1 94  ? 20.460 -19.577 29.355 1.00 25.45  ? 95  LEU A CD2 1 
ATOM   838  N  N   . ASN A 1 95  ? 23.495 -23.230 31.164 1.00 24.62  ? 96  ASN A N   1 
ATOM   839  C  CA  . ASN A 1 95  ? 23.394 -23.801 32.516 1.00 25.49  ? 96  ASN A CA  1 
ATOM   840  C  C   . ASN A 1 95  ? 22.689 -22.792 33.436 1.00 29.71  ? 96  ASN A C   1 
ATOM   841  O  O   . ASN A 1 95  ? 23.333 -22.100 34.219 1.00 29.55  ? 96  ASN A O   1 
ATOM   842  C  CB  . ASN A 1 95  ? 24.794 -24.198 33.053 1.00 28.25  ? 96  ASN A CB  1 
ATOM   843  C  CG  . ASN A 1 95  ? 24.756 -24.815 34.451 1.00 45.84  ? 96  ASN A CG  1 
ATOM   844  O  OD1 . ASN A 1 95  ? 23.750 -25.367 34.887 1.00 39.54  ? 96  ASN A OD1 1 
ATOM   845  N  ND2 . ASN A 1 95  ? 25.843 -24.718 35.191 1.00 38.95  ? 96  ASN A ND2 1 
ATOM   846  N  N   . LEU A 1 96  ? 21.374 -22.677 33.283 1.00 26.59  ? 97  LEU A N   1 
ATOM   847  C  CA  . LEU A 1 96  ? 20.563 -21.719 34.029 1.00 28.06  ? 97  LEU A CA  1 
ATOM   848  C  C   . LEU A 1 96  ? 20.024 -22.369 35.286 1.00 32.17  ? 97  LEU A C   1 
ATOM   849  O  O   . LEU A 1 96  ? 19.382 -23.424 35.218 1.00 31.27  ? 97  LEU A O   1 
ATOM   850  C  CB  . LEU A 1 96  ? 19.443 -21.223 33.103 1.00 28.98  ? 97  LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 96  ? 18.729 -19.932 33.441 1.00 35.69  ? 97  LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 96  ? 19.730 -18.736 33.541 1.00 35.92  ? 97  LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 96  ? 17.645 -19.663 32.400 1.00 36.40  ? 97  LEU A CD2 1 
ATOM   854  N  N   . ARG A 1 97  ? 20.356 -21.776 36.454 1.00 29.88  ? 98  ARG A N   1 
ATOM   855  C  CA  . ARG A 1 97  ? 19.971 -22.302 37.770 1.00 31.84  ? 98  ARG A CA  1 
ATOM   856  C  C   . ARG A 1 97  ? 19.435 -21.185 38.649 1.00 33.56  ? 98  ARG A C   1 
ATOM   857  O  O   . ARG A 1 97  ? 19.774 -20.014 38.431 1.00 31.26  ? 98  ARG A O   1 
ATOM   858  C  CB  . ARG A 1 97  ? 21.182 -22.962 38.465 1.00 33.60  ? 98  ARG A CB  1 
ATOM   859  C  CG  . ARG A 1 97  ? 21.831 -24.104 37.660 1.00 39.79  ? 98  ARG A CG  1 
ATOM   860  C  CD  . ARG A 1 97  ? 23.071 -24.689 38.329 1.00 55.36  ? 98  ARG A CD  1 
ATOM   861  N  NE  . ARG A 1 97  ? 22.803 -25.192 39.683 1.00 71.80  ? 98  ARG A NE  1 
ATOM   862  C  CZ  . ARG A 1 97  ? 22.336 -26.406 39.967 1.00 90.85  ? 98  ARG A CZ  1 
ATOM   863  N  NH1 . ARG A 1 97  ? 22.115 -26.761 41.227 1.00 78.56  ? 98  ARG A NH1 1 
ATOM   864  N  NH2 . ARG A 1 97  ? 22.080 -27.273 38.993 1.00 79.49  ? 98  ARG A NH2 1 
ATOM   865  N  N   . GLU A 1 98  ? 18.612 -21.525 39.662 1.00 31.28  ? 99  GLU A N   1 
ATOM   866  C  CA  . GLU A 1 98  ? 18.090 -20.499 40.576 1.00 31.83  ? 99  GLU A CA  1 
ATOM   867  C  C   . GLU A 1 98  ? 19.219 -19.607 41.137 1.00 36.55  ? 99  GLU A C   1 
ATOM   868  O  O   . GLU A 1 98  ? 19.052 -18.390 41.240 1.00 35.99  ? 99  GLU A O   1 
ATOM   869  C  CB  . GLU A 1 98  ? 17.319 -21.164 41.745 1.00 35.23  ? 99  GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 98  ? 16.650 -20.173 42.680 1.00 46.13  ? 99  GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 98  ? 15.932 -20.802 43.858 1.00 78.23  ? 99  GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 98  ? 16.511 -21.703 44.509 1.00 71.70  ? 99  GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 98  ? 14.786 -20.383 44.136 1.00 82.71  ? 99  GLU A OE2 1 
ATOM   874  N  N   . GLY A 1 99  ? 20.346 -20.228 41.479 1.00 34.99  ? 100 GLY A N   1 
ATOM   875  C  CA  . GLY A 1 99  ? 21.497 -19.551 42.070 1.00 35.10  ? 100 GLY A CA  1 
ATOM   876  C  C   . GLY A 1 99  ? 22.311 -18.667 41.141 1.00 36.25  ? 100 GLY A C   1 
ATOM   877  O  O   . GLY A 1 99  ? 23.113 -17.860 41.611 1.00 35.63  ? 100 GLY A O   1 
ATOM   878  N  N   . ASN A 1 100 ? 22.108 -18.781 39.823 1.00 31.25  ? 101 ASN A N   1 
ATOM   879  C  CA  . ASN A 1 100 ? 22.897 -17.972 38.891 1.00 28.70  ? 101 ASN A CA  1 
ATOM   880  C  C   . ASN A 1 100 ? 22.069 -17.112 37.930 1.00 31.92  ? 101 ASN A C   1 
ATOM   881  O  O   . ASN A 1 100 ? 22.650 -16.307 37.196 1.00 29.89  ? 101 ASN A O   1 
ATOM   882  C  CB  . ASN A 1 100 ? 23.874 -18.881 38.111 1.00 27.87  ? 101 ASN A CB  1 
ATOM   883  C  CG  . ASN A 1 100 ? 23.218 -19.817 37.106 1.00 33.99  ? 101 ASN A CG  1 
ATOM   884  O  OD1 . ASN A 1 100 ? 22.189 -19.496 36.515 1.00 26.44  ? 101 ASN A OD1 1 
ATOM   885  N  ND2 . ASN A 1 100 ? 23.830 -20.968 36.836 1.00 28.64  ? 101 ASN A ND2 1 
ATOM   886  N  N   . ILE A 1 101 ? 20.731 -17.301 37.899 1.00 30.20  ? 102 ILE A N   1 
ATOM   887  C  CA  . ILE A 1 101 ? 19.863 -16.643 36.909 1.00 29.53  ? 102 ILE A CA  1 
ATOM   888  C  C   . ILE A 1 101 ? 19.999 -15.114 36.888 1.00 30.56  ? 102 ILE A C   1 
ATOM   889  O  O   . ILE A 1 101 ? 20.025 -14.530 35.794 1.00 27.91  ? 102 ILE A O   1 
ATOM   890  C  CB  . ILE A 1 101 ? 18.384 -17.082 36.997 1.00 33.66  ? 102 ILE A CB  1 
ATOM   891  C  CG1 . ILE A 1 101 ? 17.562 -16.492 35.814 1.00 34.15  ? 102 ILE A CG1 1 
ATOM   892  C  CG2 . ILE A 1 101 ? 17.759 -16.804 38.368 1.00 33.36  ? 102 ILE A CG2 1 
ATOM   893  C  CD1 . ILE A 1 101 ? 16.361 -17.323 35.389 1.00 34.91  ? 102 ILE A CD1 1 
ATOM   894  N  N   . MET A 1 102 ? 20.098 -14.466 38.064 1.00 29.06  ? 103 MET A N   1 
ATOM   895  C  CA  . MET A 1 102 ? 20.241 -13.013 38.098 1.00 29.44  ? 103 MET A CA  1 
ATOM   896  C  C   . MET A 1 102 ? 21.548 -12.549 37.457 1.00 30.93  ? 103 MET A C   1 
ATOM   897  O  O   . MET A 1 102 ? 21.511 -11.629 36.645 1.00 28.75  ? 103 MET A O   1 
ATOM   898  C  CB  . MET A 1 102 ? 20.073 -12.449 39.526 1.00 33.48  ? 103 MET A CB  1 
ATOM   899  C  CG  . MET A 1 102 ? 18.697 -12.722 40.132 1.00 40.03  ? 103 MET A CG  1 
ATOM   900  S  SD  . MET A 1 102 ? 17.269 -12.320 39.079 1.00 46.15  ? 103 MET A SD  1 
ATOM   901  C  CE  . MET A 1 102 ? 17.299 -10.512 39.160 1.00 43.89  ? 103 MET A CE  1 
ATOM   902  N  N   . ALA A 1 103 ? 22.690 -13.213 37.778 1.00 28.50  ? 104 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 103 ? 24.010 -12.869 37.208 1.00 28.03  ? 104 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 103 ? 24.014 -13.163 35.706 1.00 29.19  ? 104 ALA A C   1 
ATOM   905  O  O   . ALA A 1 103 ? 24.498 -12.345 34.915 1.00 26.55  ? 104 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 103 ? 25.110 -13.679 37.888 1.00 29.49  ? 104 ALA A CB  1 
ATOM   907  N  N   . VAL A 1 104 ? 23.440 -14.314 35.312 1.00 24.51  ? 105 VAL A N   1 
ATOM   908  C  CA  . VAL A 1 104 ? 23.366 -14.690 33.888 1.00 22.29  ? 105 VAL A CA  1 
ATOM   909  C  C   . VAL A 1 104 ? 22.558 -13.663 33.086 1.00 24.63  ? 105 VAL A C   1 
ATOM   910  O  O   . VAL A 1 104 ? 23.042 -13.229 32.032 1.00 23.68  ? 105 VAL A O   1 
ATOM   911  C  CB  . VAL A 1 104 ? 22.887 -16.150 33.664 1.00 25.64  ? 105 VAL A CB  1 
ATOM   912  C  CG1 . VAL A 1 104 ? 22.631 -16.441 32.179 1.00 24.01  ? 105 VAL A CG1 1 
ATOM   913  C  CG2 . VAL A 1 104 ? 23.908 -17.140 34.223 1.00 25.28  ? 105 VAL A CG2 1 
ATOM   914  N  N   A MET A 1 105 ? 21.352 -13.274 33.562 0.65 23.55  ? 106 MET A N   1 
ATOM   915  N  N   B MET A 1 105 ? 21.355 -13.276 33.564 0.35 23.72  ? 106 MET A N   1 
ATOM   916  C  CA  A MET A 1 105 ? 20.534 -12.285 32.844 0.65 24.37  ? 106 MET A CA  1 
ATOM   917  C  CA  B MET A 1 105 ? 20.525 -12.292 32.860 0.35 24.59  ? 106 MET A CA  1 
ATOM   918  C  C   A MET A 1 105 ? 21.251 -10.934 32.725 0.65 27.65  ? 106 MET A C   1 
ATOM   919  C  C   B MET A 1 105 ? 21.236 -10.941 32.732 0.35 28.16  ? 106 MET A C   1 
ATOM   920  O  O   A MET A 1 105 ? 21.251 -10.331 31.646 0.65 25.91  ? 106 MET A O   1 
ATOM   921  O  O   B MET A 1 105 ? 21.230 -10.352 31.647 0.35 26.92  ? 106 MET A O   1 
ATOM   922  C  CB  A MET A 1 105 ? 19.170 -12.091 33.509 0.65 27.97  ? 106 MET A CB  1 
ATOM   923  C  CB  B MET A 1 105 ? 19.166 -12.111 33.541 0.35 28.43  ? 106 MET A CB  1 
ATOM   924  C  CG  A MET A 1 105 ? 18.259 -11.163 32.719 0.65 31.58  ? 106 MET A CG  1 
ATOM   925  C  CG  B MET A 1 105 ? 18.221 -11.255 32.729 0.35 32.59  ? 106 MET A CG  1 
ATOM   926  S  SD  A MET A 1 105 ? 16.566 -11.209 33.330 0.65 36.63  ? 106 MET A SD  1 
ATOM   927  S  SD  B MET A 1 105 ? 16.663 -10.992 33.576 0.35 38.43  ? 106 MET A SD  1 
ATOM   928  C  CE  A MET A 1 105 ? 16.698 -10.142 34.819 0.65 34.46  ? 106 MET A CE  1 
ATOM   929  C  CE  B MET A 1 105 ? 16.159 -9.484  32.805 0.35 35.98  ? 106 MET A CE  1 
ATOM   930  N  N   . ALA A 1 106 ? 21.847 -10.460 33.832 1.00 25.67  ? 107 ALA A N   1 
ATOM   931  C  CA  . ALA A 1 106 ? 22.590 -9.176  33.849 1.00 25.48  ? 107 ALA A CA  1 
ATOM   932  C  C   . ALA A 1 106 ? 23.747 -9.210  32.843 1.00 25.81  ? 107 ALA A C   1 
ATOM   933  O  O   . ALA A 1 106 ? 23.921 -8.252  32.068 1.00 24.45  ? 107 ALA A O   1 
ATOM   934  C  CB  . ALA A 1 106 ? 23.104 -8.883  35.250 1.00 26.92  ? 107 ALA A CB  1 
ATOM   935  N  N   . THR A 1 107 ? 24.489 -10.338 32.797 1.00 22.04  ? 108 THR A N   1 
ATOM   936  C  CA  . THR A 1 107 ? 25.595 -10.508 31.853 1.00 21.10  ? 108 THR A CA  1 
ATOM   937  C  C   . THR A 1 107 ? 25.073 -10.562 30.407 1.00 24.65  ? 108 THR A C   1 
ATOM   938  O  O   . THR A 1 107 ? 25.661 -9.900  29.539 1.00 22.22  ? 108 THR A O   1 
ATOM   939  C  CB  . THR A 1 107 ? 26.512 -11.694 32.234 1.00 25.92  ? 108 THR A CB  1 
ATOM   940  O  OG1 . THR A 1 107 ? 26.797 -11.654 33.641 1.00 25.13  ? 108 THR A OG1 1 
ATOM   941  C  CG2 . THR A 1 107 ? 27.827 -11.705 31.430 1.00 25.41  ? 108 THR A CG2 1 
ATOM   942  N  N   . ALA A 1 108 ? 23.961 -11.306 30.159 1.00 22.00  ? 109 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 108 ? 23.378 -11.397 28.810 1.00 20.86  ? 109 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 108 ? 22.865 -10.023 28.341 1.00 23.31  ? 109 ALA A C   1 
ATOM   945  O  O   . ALA A 1 108 ? 23.000 -9.699  27.160 1.00 22.21  ? 109 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 108 ? 22.276 -12.459 28.762 1.00 21.57  ? 109 ALA A CB  1 
ATOM   947  N  N   . MET A 1 109 ? 22.317 -9.189  29.260 1.00 21.31  ? 110 MET A N   1 
ATOM   948  C  CA  . MET A 1 109 ? 21.873 -7.840  28.869 1.00 21.61  ? 110 MET A CA  1 
ATOM   949  C  C   . MET A 1 109 ? 23.077 -6.984  28.428 1.00 24.46  ? 110 MET A C   1 
ATOM   950  O  O   . MET A 1 109 ? 23.040 -6.340  27.375 1.00 24.29  ? 110 MET A O   1 
ATOM   951  C  CB  . MET A 1 109 ? 21.115 -7.179  30.031 1.00 25.06  ? 110 MET A CB  1 
ATOM   952  C  CG  . MET A 1 109 ? 19.733 -7.772  30.207 1.00 30.21  ? 110 MET A CG  1 
ATOM   953  S  SD  . MET A 1 109 ? 18.982 -7.198  31.740 1.00 37.47  ? 110 MET A SD  1 
ATOM   954  C  CE  . MET A 1 109 ? 18.655 -5.489  31.296 1.00 35.56  ? 110 MET A CE  1 
ATOM   955  N  N   . TYR A 1 110 ? 24.159 -7.036  29.203 1.00 22.73  ? 111 TYR A N   1 
ATOM   956  C  CA  . TYR A 1 110 ? 25.403 -6.309  28.916 1.00 22.48  ? 111 TYR A CA  1 
ATOM   957  C  C   . TYR A 1 110 ? 26.021 -6.793  27.584 1.00 24.14  ? 111 TYR A C   1 
ATOM   958  O  O   . TYR A 1 110 ? 26.442 -5.969  26.749 1.00 22.25  ? 111 TYR A O   1 
ATOM   959  C  CB  . TYR A 1 110 ? 26.384 -6.539  30.074 1.00 23.23  ? 111 TYR A CB  1 
ATOM   960  C  CG  . TYR A 1 110 ? 27.804 -6.059  29.837 1.00 23.43  ? 111 TYR A CG  1 
ATOM   961  C  CD1 . TYR A 1 110 ? 28.121 -4.702  29.894 1.00 26.34  ? 111 TYR A CD1 1 
ATOM   962  C  CD2 . TYR A 1 110 ? 28.842 -6.968  29.630 1.00 22.79  ? 111 TYR A CD2 1 
ATOM   963  C  CE1 . TYR A 1 110 ? 29.432 -4.260  29.704 1.00 23.68  ? 111 TYR A CE1 1 
ATOM   964  C  CE2 . TYR A 1 110 ? 30.160 -6.541  29.478 1.00 22.60  ? 111 TYR A CE2 1 
ATOM   965  C  CZ  . TYR A 1 110 ? 30.450 -5.185  29.535 1.00 23.30  ? 111 TYR A CZ  1 
ATOM   966  O  OH  . TYR A 1 110 ? 31.747 -4.773  29.407 1.00 22.78  ? 111 TYR A OH  1 
ATOM   967  N  N   . LEU A 1 111 ? 26.054 -8.124  27.378 1.00 20.59  ? 112 LEU A N   1 
ATOM   968  C  CA  . LEU A 1 111 ? 26.648 -8.708  26.170 1.00 18.85  ? 112 LEU A CA  1 
ATOM   969  C  C   . LEU A 1 111 ? 25.729 -8.590  24.957 1.00 22.78  ? 112 LEU A C   1 
ATOM   970  O  O   . LEU A 1 111 ? 26.171 -8.855  23.841 1.00 21.48  ? 112 LEU A O   1 
ATOM   971  C  CB  . LEU A 1 111 ? 27.025 -10.181 26.409 1.00 17.43  ? 112 LEU A CB  1 
ATOM   972  C  CG  . LEU A 1 111 ? 28.144 -10.452 27.441 1.00 20.06  ? 112 LEU A CG  1 
ATOM   973  C  CD1 . LEU A 1 111 ? 28.433 -11.980 27.522 1.00 19.39  ? 112 LEU A CD1 1 
ATOM   974  C  CD2 . LEU A 1 111 ? 29.459 -9.658  27.071 1.00 21.06  ? 112 LEU A CD2 1 
ATOM   975  N  N   . GLN A 1 112 ? 24.447 -8.235  25.183 1.00 20.90  ? 113 GLN A N   1 
ATOM   976  C  CA  . GLN A 1 112 ? 23.444 -8.094  24.117 1.00 21.47  ? 113 GLN A CA  1 
ATOM   977  C  C   . GLN A 1 112 ? 23.219 -9.450  23.444 1.00 23.19  ? 113 GLN A C   1 
ATOM   978  O  O   . GLN A 1 112 ? 23.494 -9.643  22.260 1.00 21.44  ? 113 GLN A O   1 
ATOM   979  C  CB  . GLN A 1 112 ? 23.840 -6.995  23.108 1.00 22.75  ? 113 GLN A CB  1 
ATOM   980  C  CG  . GLN A 1 112 ? 24.002 -5.598  23.748 1.00 27.62  ? 113 GLN A CG  1 
ATOM   981  C  CD  . GLN A 1 112 ? 24.715 -4.656  22.808 1.00 36.21  ? 113 GLN A CD  1 
ATOM   982  O  OE1 . GLN A 1 112 ? 24.565 -4.736  21.601 1.00 27.73  ? 113 GLN A OE1 1 
ATOM   983  N  NE2 . GLN A 1 112 ? 25.524 -3.753  23.334 1.00 32.55  ? 113 GLN A NE2 1 
ATOM   984  N  N   . MET A 1 113 ? 22.747 -10.399 24.247 1.00 20.23  ? 114 MET A N   1 
ATOM   985  C  CA  . MET A 1 113 ? 22.426 -11.768 23.807 1.00 19.38  ? 114 MET A CA  1 
ATOM   986  C  C   . MET A 1 113 ? 20.919 -11.920 24.066 1.00 25.62  ? 114 MET A C   1 
ATOM   987  O  O   . MET A 1 113 ? 20.496 -12.403 25.120 1.00 24.35  ? 114 MET A O   1 
ATOM   988  C  CB  . MET A 1 113 ? 23.276 -12.744 24.622 1.00 20.09  ? 114 MET A CB  1 
ATOM   989  C  CG  . MET A 1 113 ? 24.760 -12.628 24.286 1.00 21.32  ? 114 MET A CG  1 
ATOM   990  S  SD  . MET A 1 113 ? 25.778 -13.641 25.358 1.00 24.01  ? 114 MET A SD  1 
ATOM   991  C  CE  . MET A 1 113 ? 25.422 -15.328 24.637 1.00 21.14  ? 114 MET A CE  1 
ATOM   992  N  N   . GLU A 1 114 ? 20.113 -11.379 23.135 1.00 25.88  ? 115 GLU A N   1 
ATOM   993  C  CA  . GLU A 1 114 ? 18.656 -11.234 23.282 1.00 28.56  ? 115 GLU A CA  1 
ATOM   994  C  C   . GLU A 1 114 ? 17.901 -12.516 23.593 1.00 29.17  ? 115 GLU A C   1 
ATOM   995  O  O   . GLU A 1 114 ? 16.975 -12.467 24.401 1.00 29.19  ? 115 GLU A O   1 
ATOM   996  C  CB  . GLU A 1 114 ? 18.033 -10.545 22.060 1.00 31.84  ? 115 GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 114 ? 18.624 -9.166  21.803 1.00 45.45  ? 115 GLU A CG  1 
ATOM   998  N  N   . HIS A 1 115 ? 18.266 -13.652 22.975 1.00 24.56  ? 116 HIS A N   1 
ATOM   999  C  CA  . HIS A 1 115 ? 17.521 -14.884 23.263 1.00 26.09  ? 116 HIS A CA  1 
ATOM   1000 C  C   . HIS A 1 115 ? 17.744 -15.361 24.699 1.00 28.37  ? 116 HIS A C   1 
ATOM   1001 O  O   . HIS A 1 115 ? 16.793 -15.816 25.338 1.00 29.19  ? 116 HIS A O   1 
ATOM   1002 C  CB  . HIS A 1 115 ? 17.807 -15.982 22.243 1.00 27.79  ? 116 HIS A CB  1 
ATOM   1003 C  CG  . HIS A 1 115 ? 17.347 -15.644 20.861 1.00 32.59  ? 116 HIS A CG  1 
ATOM   1004 N  ND1 . HIS A 1 115 ? 16.010 -15.441 20.576 1.00 36.37  ? 116 HIS A ND1 1 
ATOM   1005 C  CD2 . HIS A 1 115 ? 18.058 -15.548 19.714 1.00 33.97  ? 116 HIS A CD2 1 
ATOM   1006 C  CE1 . HIS A 1 115 ? 15.954 -15.178 19.280 1.00 35.91  ? 116 HIS A CE1 1 
ATOM   1007 N  NE2 . HIS A 1 115 ? 17.158 -15.247 18.719 1.00 35.01  ? 116 HIS A NE2 1 
ATOM   1008 N  N   . VAL A 1 116 ? 18.984 -15.211 25.218 1.00 22.74  ? 117 VAL A N   1 
ATOM   1009 C  CA  . VAL A 1 116 ? 19.289 -15.552 26.613 1.00 22.52  ? 117 VAL A CA  1 
ATOM   1010 C  C   . VAL A 1 116 ? 18.504 -14.643 27.569 1.00 27.90  ? 117 VAL A C   1 
ATOM   1011 O  O   . VAL A 1 116 ? 17.883 -15.130 28.530 1.00 25.89  ? 117 VAL A O   1 
ATOM   1012 C  CB  . VAL A 1 116 ? 20.804 -15.566 26.922 1.00 24.89  ? 117 VAL A CB  1 
ATOM   1013 C  CG1 . VAL A 1 116 ? 21.046 -15.814 28.415 1.00 25.02  ? 117 VAL A CG1 1 
ATOM   1014 C  CG2 . VAL A 1 116 ? 21.509 -16.630 26.078 1.00 23.84  ? 117 VAL A CG2 1 
ATOM   1015 N  N   . VAL A 1 117 ? 18.500 -13.321 27.290 1.00 24.78  ? 118 VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 117 ? 17.754 -12.362 28.118 1.00 25.86  ? 118 VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 117 ? 16.267 -12.780 28.190 1.00 31.79  ? 118 VAL A C   1 
ATOM   1018 O  O   . VAL A 1 117 ? 15.713 -12.864 29.292 1.00 31.35  ? 118 VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 117 ? 17.934 -10.889 27.646 1.00 28.63  ? 118 VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 117 ? 17.097 -9.923  28.502 1.00 29.50  ? 118 VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 117 ? 19.408 -10.478 27.673 1.00 27.58  ? 118 VAL A CG2 1 
ATOM   1022 N  N   A ASP A 1 118 ? 15.620 -12.967 27.021 0.41 29.90  ? 119 ASP A N   1 
ATOM   1023 N  N   B ASP A 1 118 ? 15.693 -13.173 27.036 0.59 28.92  ? 119 ASP A N   1 
ATOM   1024 C  CA  A ASP A 1 118 ? 14.198 -13.324 26.891 0.41 31.48  ? 119 ASP A CA  1 
ATOM   1025 C  CA  B ASP A 1 118 ? 14.313 -13.652 26.904 0.59 29.92  ? 119 ASP A CA  1 
ATOM   1026 C  C   A ASP A 1 118 ? 13.770 -14.528 27.732 0.41 35.71  ? 119 ASP A C   1 
ATOM   1027 C  C   B ASP A 1 118 ? 14.014 -14.872 27.790 0.59 31.87  ? 119 ASP A C   1 
ATOM   1028 O  O   A ASP A 1 118 ? 12.697 -14.499 28.327 0.41 36.64  ? 119 ASP A O   1 
ATOM   1029 O  O   B ASP A 1 118 ? 13.058 -14.811 28.562 0.59 31.35  ? 119 ASP A O   1 
ATOM   1030 C  CB  A ASP A 1 118 ? 13.823 -13.536 25.411 0.41 33.49  ? 119 ASP A CB  1 
ATOM   1031 C  CB  B ASP A 1 118 ? 13.980 -13.947 25.427 0.59 31.84  ? 119 ASP A CB  1 
ATOM   1032 C  CG  A ASP A 1 118 ? 13.634 -12.260 24.612 0.41 45.55  ? 119 ASP A CG  1 
ATOM   1033 C  CG  B ASP A 1 118 ? 12.528 -14.311 25.175 0.59 44.93  ? 119 ASP A CG  1 
ATOM   1034 O  OD1 A ASP A 1 118 ? 13.087 -11.284 25.168 0.41 49.11  ? 119 ASP A OD1 1 
ATOM   1035 O  OD1 B ASP A 1 118 ? 11.642 -13.498 25.522 0.59 47.35  ? 119 ASP A OD1 1 
ATOM   1036 O  OD2 A ASP A 1 118 ? 14.023 -12.240 23.427 0.41 50.66  ? 119 ASP A OD2 1 
ATOM   1037 O  OD2 B ASP A 1 118 ? 12.279 -15.399 24.618 0.59 49.45  ? 119 ASP A OD2 1 
ATOM   1038 N  N   A THR A 1 119 ? 14.613 -15.571 27.790 0.41 31.27  ? 120 THR A N   1 
ATOM   1039 N  N   B THR A 1 119 ? 14.825 -15.962 27.713 0.59 27.21  ? 120 THR A N   1 
ATOM   1040 C  CA  A THR A 1 119 ? 14.347 -16.794 28.553 0.41 31.48  ? 120 THR A CA  1 
ATOM   1041 C  CA  B THR A 1 119 ? 14.552 -17.144 28.554 0.59 27.70  ? 120 THR A CA  1 
ATOM   1042 C  C   A THR A 1 119 ? 14.538 -16.575 30.026 0.41 33.66  ? 120 THR A C   1 
ATOM   1043 C  C   B THR A 1 119 ? 14.753 -16.860 30.057 0.59 31.50  ? 120 THR A C   1 
ATOM   1044 O  O   A THR A 1 119 ? 13.693 -17.011 30.809 0.41 34.18  ? 120 THR A O   1 
ATOM   1045 O  O   B THR A 1 119 ? 14.112 -17.517 30.877 0.59 31.43  ? 120 THR A O   1 
ATOM   1046 C  CB  A THR A 1 119 ? 15.174 -17.928 27.999 0.41 39.51  ? 120 THR A CB  1 
ATOM   1047 C  CB  B THR A 1 119 ? 15.306 -18.406 28.096 0.59 28.20  ? 120 THR A CB  1 
ATOM   1048 O  OG1 A THR A 1 119 ? 14.797 -18.008 26.644 0.41 40.49  ? 120 THR A OG1 1 
ATOM   1049 O  OG1 B THR A 1 119 ? 14.673 -19.532 28.712 0.59 29.33  ? 120 THR A OG1 1 
ATOM   1050 C  CG2 A THR A 1 119 ? 14.888 -19.255 28.680 0.41 39.44  ? 120 THR A CG2 1 
ATOM   1051 C  CG2 B THR A 1 119 ? 16.787 -18.394 28.464 0.59 22.06  ? 120 THR A CG2 1 
ATOM   1052 N  N   . CYS A 1 120 ? 15.644 -15.902 30.413 1.00 28.55  ? 121 CYS A N   1 
ATOM   1053 C  CA  . CYS A 1 120 ? 15.895 -15.549 31.823 1.00 29.03  ? 121 CYS A CA  1 
ATOM   1054 C  C   . CYS A 1 120 ? 14.679 -14.828 32.368 1.00 35.05  ? 121 CYS A C   1 
ATOM   1055 O  O   . CYS A 1 120 ? 14.203 -15.165 33.462 1.00 34.49  ? 121 CYS A O   1 
ATOM   1056 C  CB  . CYS A 1 120 ? 17.138 -14.681 31.942 1.00 27.90  ? 121 CYS A CB  1 
ATOM   1057 S  SG  . CYS A 1 120 ? 18.681 -15.593 31.764 1.00 30.19  ? 121 CYS A SG  1 
ATOM   1058 N  N   . ARG A 1 121 ? 14.140 -13.868 31.571 1.00 33.41  ? 122 ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 121 ? 12.942 -13.101 31.934 1.00 35.40  ? 122 ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 121 ? 11.753 -14.044 32.196 1.00 39.93  ? 122 ARG A C   1 
ATOM   1061 O  O   . ARG A 1 121 ? 11.022 -13.864 33.179 1.00 40.28  ? 122 ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 121 ? 12.573 -12.109 30.821 1.00 37.59  ? 122 ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 121 ? 13.445 -10.872 30.781 1.00 52.78  ? 122 ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 121 ? 12.634 -9.630  30.469 1.00 68.57  ? 122 ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 121 ? 12.997 -9.053  29.173 1.00 76.99  ? 122 ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 121 ? 13.923 -8.114  28.998 1.00 86.86  ? 122 ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 121 ? 14.602 -7.637  30.035 1.00 68.27  ? 122 ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 121 ? 14.181 -7.648  27.783 1.00 75.26  ? 122 ARG A NH2 1 
ATOM   1069 N  N   . LYS A 1 122 ? 11.580 -15.052 31.321 1.00 37.60  ? 123 LYS A N   1 
ATOM   1070 C  CA  . LYS A 1 122 ? 10.493 -16.036 31.410 1.00 38.55  ? 123 LYS A CA  1 
ATOM   1071 C  C   . LYS A 1 122 ? 10.643 -16.941 32.626 1.00 42.01  ? 123 LYS A C   1 
ATOM   1072 O  O   . LYS A 1 122 ? 9.656  -17.170 33.322 1.00 42.08  ? 123 LYS A O   1 
ATOM   1073 C  CB  . LYS A 1 122 ? 10.393 -16.872 30.115 1.00 40.12  ? 123 LYS A CB  1 
ATOM   1074 C  CG  . LYS A 1 122 ? 9.884  -16.075 28.919 1.00 57.54  ? 123 LYS A CG  1 
ATOM   1075 C  CD  . LYS A 1 122 ? 9.545  -16.973 27.732 1.00 69.01  ? 123 LYS A CD  1 
ATOM   1076 C  CE  . LYS A 1 122 ? 9.609  -16.257 26.399 1.00 79.91  ? 123 LYS A CE  1 
ATOM   1077 N  NZ  . LYS A 1 122 ? 8.624  -15.146 26.282 1.00 88.69  ? 123 LYS A NZ  1 
ATOM   1078 N  N   . PHE A 1 123 ? 11.872 -17.446 32.893 1.00 37.07  ? 124 PHE A N   1 
ATOM   1079 C  CA  . PHE A 1 123 ? 12.142 -18.310 34.050 1.00 37.50  ? 124 PHE A CA  1 
ATOM   1080 C  C   . PHE A 1 123 ? 11.944 -17.547 35.362 1.00 42.55  ? 124 PHE A C   1 
ATOM   1081 O  O   . PHE A 1 123 ? 11.394 -18.110 36.316 1.00 42.28  ? 124 PHE A O   1 
ATOM   1082 C  CB  . PHE A 1 123 ? 13.541 -18.928 33.958 1.00 37.76  ? 124 PHE A CB  1 
ATOM   1083 C  CG  . PHE A 1 123 ? 13.657 -20.218 33.165 1.00 38.93  ? 124 PHE A CG  1 
ATOM   1084 C  CD1 . PHE A 1 123 ? 13.087 -20.334 31.898 1.00 41.81  ? 124 PHE A CD1 1 
ATOM   1085 C  CD2 . PHE A 1 123 ? 14.405 -21.286 33.649 1.00 41.42  ? 124 PHE A CD2 1 
ATOM   1086 C  CE1 . PHE A 1 123 ? 13.208 -21.521 31.163 1.00 42.05  ? 124 PHE A CE1 1 
ATOM   1087 C  CE2 . PHE A 1 123 ? 14.528 -22.471 32.910 1.00 42.93  ? 124 PHE A CE2 1 
ATOM   1088 C  CZ  . PHE A 1 123 ? 13.929 -22.579 31.675 1.00 40.27  ? 124 PHE A CZ  1 
ATOM   1089 N  N   . ILE A 1 124 ? 12.329 -16.252 35.393 1.00 38.09  ? 125 ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 124 ? 12.122 -15.399 36.578 1.00 39.43  ? 125 ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 124 ? 10.620 -15.167 36.826 1.00 46.04  ? 125 ILE A C   1 
ATOM   1092 O  O   . ILE A 1 124 ? 10.165 -15.304 37.968 1.00 46.58  ? 125 ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 124 ? 12.954 -14.084 36.506 1.00 41.34  ? 125 ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 124 ? 14.447 -14.397 36.683 1.00 39.64  ? 125 ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 124 ? 12.495 -13.042 37.569 1.00 44.16  ? 125 ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 124 ? 15.375 -13.357 36.121 1.00 45.48  ? 125 ILE A CD1 1 
ATOM   1097 N  N   . LYS A 1 125 ? 9.854  -14.862 35.752 1.00 44.45  ? 126 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 125 ? 8.402  -14.618 35.814 1.00 47.34  ? 126 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 125 ? 7.626  -15.847 36.335 1.00 52.81  ? 126 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 125 ? 6.651  -15.687 37.068 1.00 53.05  ? 126 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 125 ? 7.870  -14.179 34.439 1.00 50.78  ? 126 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 125 ? 6.502  -13.504 34.487 1.00 69.77  ? 126 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 125 ? 5.893  -13.376 33.098 1.00 82.49  ? 126 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 125 ? 4.467  -12.883 33.147 1.00 96.59  ? 126 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 125 ? 3.832  -12.911 31.803 1.00 106.67 ? 126 LYS A NZ  1 
ATOM   1106 N  N   . ALA A 1 126 ? 8.083  -17.063 35.983 1.00 48.73  ? 127 ALA A N   1 
ATOM   1107 C  CA  . ALA A 1 126 ? 7.456  -18.309 36.436 1.00 50.24  ? 127 ALA A CA  1 
ATOM   1108 C  C   . ALA A 1 126 ? 7.600  -18.526 37.957 1.00 55.81  ? 127 ALA A C   1 
ATOM   1109 O  O   . ALA A 1 126 ? 6.727  -19.138 38.558 1.00 56.90  ? 127 ALA A O   1 
ATOM   1110 C  CB  . ALA A 1 126 ? 8.042  -19.490 35.673 1.00 49.38  ? 127 ALA A CB  1 
ATOM   1111 N  N   . SER A 1 127 ? 8.690  -18.027 38.570 1.00 53.39  ? 128 SER A N   1 
ATOM   1112 C  CA  . SER A 1 127 ? 8.949  -18.179 40.008 1.00 55.74  ? 128 SER A CA  1 
ATOM   1113 C  C   . SER A 1 127 ? 8.279  -17.107 40.896 1.00 62.89  ? 128 SER A C   1 
ATOM   1114 O  O   . SER A 1 127 ? 8.217  -17.293 42.116 1.00 64.82  ? 128 SER A O   1 
ATOM   1115 C  CB  . SER A 1 127 ? 10.451 -18.240 40.281 1.00 59.46  ? 128 SER A CB  1 
ATOM   1116 O  OG  . SER A 1 127 ? 10.971 -19.537 40.035 1.00 70.52  ? 128 SER A OG  1 
ATOM   1117 N  N   . GLU A 1 128 ? 7.762  -16.007 40.296 1.00 59.18  ? 129 GLU A N   1 
ATOM   1118 C  CA  . GLU A 1 128 ? 7.107  -14.929 41.048 1.00 78.94  ? 129 GLU A CA  1 
ATOM   1119 C  C   . GLU A 1 128 ? 5.651  -15.256 41.396 1.00 119.75 ? 129 GLU A C   1 
ATOM   1120 O  O   . GLU A 1 128 ? 5.366  -16.327 41.928 1.00 86.78  ? 129 GLU A O   1 
ATOM   1121 C  CB  . GLU A 1 128 ? 7.241  -13.568 40.331 1.00 79.37  ? 129 GLU A CB  1 
ATOM   1122 C  CG  . GLU A 1 128 ? 6.240  -13.312 39.212 1.00 89.49  ? 129 GLU A CG  1 
ATOM   1123 C  CD  . GLU A 1 128 ? 6.450  -12.069 38.363 1.00 109.17 ? 129 GLU A CD  1 
ATOM   1124 O  OE1 . GLU A 1 128 ? 7.557  -11.482 38.404 1.00 99.72  ? 129 GLU A OE1 1 
ATOM   1125 O  OE2 . GLU A 1 128 ? 5.500  -11.690 37.641 1.00 103.93 ? 129 GLU A OE2 1 
HETATM 1126 C  C   . ACE B 2 1   ? 21.247 -35.099 5.875  1.00 25.35  ? 0   ACE D C   1 
HETATM 1127 O  O   . ACE B 2 1   ? 21.309 -33.947 6.333  1.00 25.90  ? 0   ACE D O   1 
HETATM 1128 C  CH3 . ACE B 2 1   ? 21.436 -36.288 6.763  1.00 25.31  ? 0   ACE D CH3 1 
ATOM   1129 N  N   A TRP B 2 2   ? 20.972 -35.359 4.601  0.78 24.03  ? 1   TRP D N   1 
ATOM   1130 N  N   B TRP B 2 2   ? 21.003 -35.372 4.592  0.22 24.30  ? 1   TRP D N   1 
ATOM   1131 C  CA  A TRP B 2 2   ? 20.770 -34.308 3.614  0.78 23.05  ? 1   TRP D CA  1 
ATOM   1132 C  CA  B TRP B 2 2   ? 20.745 -34.329 3.601  0.22 23.64  ? 1   TRP D CA  1 
ATOM   1133 C  C   A TRP B 2 2   ? 19.269 -34.161 3.307  0.78 27.15  ? 1   TRP D C   1 
ATOM   1134 C  C   B TRP B 2 2   ? 19.244 -34.154 3.401  0.22 26.66  ? 1   TRP D C   1 
ATOM   1135 O  O   A TRP B 2 2   ? 18.540 -35.163 3.250  0.78 26.96  ? 1   TRP D O   1 
ATOM   1136 O  O   B TRP B 2 2   ? 18.491 -35.131 3.479  0.22 26.15  ? 1   TRP D O   1 
ATOM   1137 C  CB  A TRP B 2 2   ? 21.562 -34.642 2.337  0.78 21.94  ? 1   TRP D CB  1 
ATOM   1138 C  CB  B TRP B 2 2   ? 21.451 -34.607 2.252  0.22 22.45  ? 1   TRP D CB  1 
ATOM   1139 C  CG  A TRP B 2 2   ? 23.059 -34.610 2.523  0.78 22.20  ? 1   TRP D CG  1 
ATOM   1140 C  CG  B TRP B 2 2   ? 20.803 -35.654 1.391  0.22 23.36  ? 1   TRP D CG  1 
ATOM   1141 C  CD1 A TRP B 2 2   ? 23.854 -35.618 2.991  0.78 24.89  ? 1   TRP D CD1 1 
ATOM   1142 C  CD1 B TRP B 2 2   ? 21.111 -36.980 1.350  0.22 26.40  ? 1   TRP D CD1 1 
ATOM   1143 C  CD2 A TRP B 2 2   ? 23.926 -33.491 2.291  0.78 21.65  ? 1   TRP D CD2 1 
ATOM   1144 C  CD2 B TRP B 2 2   ? 19.757 -35.455 0.426  0.22 23.15  ? 1   TRP D CD2 1 
ATOM   1145 N  NE1 A TRP B 2 2   ? 25.167 -35.190 3.065  0.78 24.26  ? 1   TRP D NE1 1 
ATOM   1146 N  NE1 B TRP B 2 2   ? 20.290 -37.631 0.460  0.22 25.93  ? 1   TRP D NE1 1 
ATOM   1147 C  CE2 A TRP B 2 2   ? 25.247 -33.913 2.576  0.78 25.06  ? 1   TRP D CE2 1 
ATOM   1148 C  CE2 B TRP B 2 2   ? 19.461 -36.716 -0.136 0.22 27.15  ? 1   TRP D CE2 1 
ATOM   1149 C  CE3 A TRP B 2 2   ? 23.717 -32.167 1.859  0.78 21.98  ? 1   TRP D CE3 1 
ATOM   1150 C  CE3 B TRP B 2 2   ? 19.020 -34.336 0.000  0.22 24.14  ? 1   TRP D CE3 1 
ATOM   1151 C  CZ2 A TRP B 2 2   ? 26.353 -33.063 2.439  0.78 23.87  ? 1   TRP D CZ2 1 
ATOM   1152 C  CZ2 B TRP B 2 2   ? 18.475 -36.888 -1.115 0.22 26.26  ? 1   TRP D CZ2 1 
ATOM   1153 C  CZ3 A TRP B 2 2   ? 24.820 -31.341 1.688  0.78 22.81  ? 1   TRP D CZ3 1 
ATOM   1154 C  CZ3 B TRP B 2 2   ? 18.037 -34.509 -0.962 0.22 25.78  ? 1   TRP D CZ3 1 
ATOM   1155 C  CH2 A TRP B 2 2   ? 26.115 -31.788 1.983  0.78 23.68  ? 1   TRP D CH2 1 
ATOM   1156 C  CH2 B TRP B 2 2   ? 17.775 -35.771 -1.511 0.22 26.29  ? 1   TRP D CH2 1 
ATOM   1157 N  N   . VAL B 2 3   ? 18.814 -32.917 3.122  1.00 22.31  ? 2   VAL D N   1 
ATOM   1158 C  CA  . VAL B 2 3   ? 17.403 -32.580 2.871  1.00 22.02  ? 2   VAL D CA  1 
ATOM   1159 C  C   . VAL B 2 3   ? 17.266 -31.533 1.768  1.00 23.64  ? 2   VAL D C   1 
ATOM   1160 O  O   . VAL B 2 3   ? 18.231 -30.840 1.427  1.00 22.69  ? 2   VAL D O   1 
ATOM   1161 C  CB  . VAL B 2 3   ? 16.677 -32.072 4.173  1.00 25.09  ? 2   VAL D CB  1 
ATOM   1162 C  CG1 . VAL B 2 3   ? 16.696 -33.116 5.296  1.00 24.67  ? 2   VAL D CG1 1 
ATOM   1163 C  CG2 . VAL B 2 3   ? 17.245 -30.724 4.664  1.00 25.00  ? 2   VAL D CG2 1 
ATOM   1164 N  N   . ILE B 2 4   ? 16.027 -31.348 1.302  1.00 21.12  ? 3   ILE D N   1 
ATOM   1165 C  CA  . ILE B 2 4   ? 15.671 -30.257 0.407  1.00 21.26  ? 3   ILE D CA  1 
ATOM   1166 C  C   . ILE B 2 4   ? 15.284 -29.124 1.392  1.00 24.75  ? 3   ILE D C   1 
ATOM   1167 O  O   . ILE B 2 4   ? 14.260 -29.257 2.085  1.00 23.71  ? 3   ILE D O   1 
ATOM   1168 C  CB  . ILE B 2 4   ? 14.466 -30.627 -0.498 1.00 22.96  ? 3   ILE D CB  1 
ATOM   1169 C  CG1 . ILE B 2 4   ? 14.740 -31.901 -1.378 1.00 22.32  ? 3   ILE D CG1 1 
ATOM   1170 C  CG2 . ILE B 2 4   ? 14.033 -29.400 -1.348 1.00 24.18  ? 3   ILE D CG2 1 
ATOM   1171 C  CD1 . ILE B 2 4   ? 16.061 -31.836 -2.310 1.00 26.13  ? 3   ILE D CD1 1 
ATOM   1172 N  N   . PRO B 2 5   ? 16.081 -28.041 1.506  1.00 24.60  ? 4   PRO D N   1 
ATOM   1173 C  CA  . PRO B 2 5   ? 15.737 -26.979 2.472  1.00 25.29  ? 4   PRO D CA  1 
ATOM   1174 C  C   . PRO B 2 5   ? 14.475 -26.204 2.093  1.00 29.21  ? 4   PRO D C   1 
ATOM   1175 O  O   . PRO B 2 5   ? 14.209 -25.987 0.907  1.00 28.92  ? 4   PRO D O   1 
ATOM   1176 C  CB  . PRO B 2 5   ? 16.978 -26.074 2.471  1.00 26.91  ? 4   PRO D CB  1 
ATOM   1177 C  CG  . PRO B 2 5   ? 17.553 -26.252 1.066  1.00 30.44  ? 4   PRO D CG  1 
ATOM   1178 C  CD  . PRO B 2 5   ? 17.310 -27.712 0.747  1.00 25.88  ? 4   PRO D CD  1 
ATOM   1179 N  N   . ALA B 2 6   ? 13.843 -25.600 3.102  1.00 26.95  ? 5   ALA D N   1 
HETATM 1180 C  C4  . 7ZO C 3 .   ? 27.279 -10.319 11.836 1.00 25.76  ? 201 7ZO A C4  1 
HETATM 1181 C  C5  . 7ZO C 3 .   ? 25.257 -9.393  12.203 1.00 28.06  ? 201 7ZO A C5  1 
HETATM 1182 C  C6  . 7ZO C 3 .   ? 23.954 -10.759 18.108 1.00 24.01  ? 201 7ZO A C6  1 
HETATM 1183 C  C7  . 7ZO C 3 .   ? 23.461 -9.460  18.165 1.00 25.09  ? 201 7ZO A C7  1 
HETATM 1184 C  C8  . 7ZO C 3 .   ? 25.503 -10.075 16.389 1.00 21.82  ? 201 7ZO A C8  1 
HETATM 1185 C  C10 . 7ZO C 3 .   ? 26.342 -10.236 14.023 1.00 22.73  ? 201 7ZO A C10 1 
HETATM 1186 C  C1  . 7ZO C 3 .   ? 23.931 -8.471  17.306 1.00 24.12  ? 201 7ZO A C1  1 
HETATM 1187 C  C2  . 7ZO C 3 .   ? 24.943 -8.793  16.408 1.00 22.52  ? 201 7ZO A C2  1 
HETATM 1188 C  C3  . 7ZO C 3 .   ? 24.972 -11.074 17.211 1.00 21.60  ? 201 7ZO A C3  1 
HETATM 1189 C  C9  . 7ZO C 3 .   ? 27.389 -10.629 13.182 1.00 23.44  ? 201 7ZO A C9  1 
HETATM 1190 C  C11 . 7ZO C 3 .   ? 22.240 -10.596 19.729 1.00 28.80  ? 201 7ZO A C11 1 
HETATM 1191 C  C12 . 7ZO C 3 .   ? 23.215 -11.583 19.122 1.00 26.76  ? 201 7ZO A C12 1 
HETATM 1192 N  N13 . 7ZO C 3 .   ? 26.214 -9.694  11.328 1.00 27.41  ? 201 7ZO A N13 1 
HETATM 1193 N  N14 . 7ZO C 3 .   ? 25.248 -9.625  13.520 1.00 26.33  ? 201 7ZO A N14 1 
HETATM 1194 N  N15 . 7ZO C 3 .   ? 22.455 -9.389  19.139 1.00 26.36  ? 201 7ZO A N15 1 
HETATM 1195 N  N16 . 7ZO C 3 .   ? 26.355 -10.526 15.356 1.00 21.18  ? 201 7ZO A N16 1 
HETATM 1196 O  O17 . 7ZO C 3 .   ? 21.389 -10.831 20.586 1.00 28.37  ? 201 7ZO A O17 1 
HETATM 1197 CL CL1 . 7ZO C 3 .   ? 28.813 -11.405 13.768 0.99 22.19  ? 201 7ZO A CL1 1 
HETATM 1198 CL CL  . CL  D 4 .   ? 21.303 -15.255 22.534 1.00 29.54  ? 202 CL  A CL  1 
HETATM 1199 S  S   A DMS E 5 .   ? 17.590 -35.368 -1.251 0.78 39.10  ? 101 DMS D S   1 
HETATM 1200 O  O   A DMS E 5 .   ? 16.295 -35.131 -0.617 0.78 41.41  ? 101 DMS D O   1 
HETATM 1201 C  C1  A DMS E 5 .   ? 18.716 -34.461 -0.210 0.78 37.10  ? 101 DMS D C1  1 
HETATM 1202 C  C2  A DMS E 5 .   ? 18.011 -37.001 -0.769 0.78 38.84  ? 101 DMS D C2  1 
HETATM 1203 O  O   . HOH F 6 .   ? 35.628 -25.714 25.535 1.00 36.66  ? 301 HOH A O   1 
HETATM 1204 O  O   . HOH F 6 .   ? 38.366 -14.941 15.437 1.00 28.64  ? 302 HOH A O   1 
HETATM 1205 O  O   . HOH F 6 .   ? 37.931 2.404   19.680 1.00 36.72  ? 303 HOH A O   1 
HETATM 1206 O  O   . HOH F 6 .   ? 41.221 -21.655 25.177 1.00 38.31  ? 304 HOH A O   1 
HETATM 1207 O  O   . HOH F 6 .   ? 16.565 -27.538 -3.274 1.00 45.13  ? 305 HOH A O   1 
HETATM 1208 O  O   . HOH F 6 .   ? 22.751 -5.330  19.749 1.00 53.87  ? 306 HOH A O   1 
HETATM 1209 O  O   . HOH F 6 .   ? 25.826 -3.409  26.355 1.00 30.51  ? 307 HOH A O   1 
HETATM 1210 O  O   . HOH F 6 .   ? 44.468 -0.922  17.857 1.00 47.76  ? 308 HOH A O   1 
HETATM 1211 O  O   . HOH F 6 .   ? 20.807 -5.821  26.006 1.00 36.64  ? 309 HOH A O   1 
HETATM 1212 O  O   . HOH F 6 .   ? 44.959 -11.295 18.659 1.00 52.03  ? 310 HOH A O   1 
HETATM 1213 O  O   . HOH F 6 .   ? 33.270 -20.762 29.542 1.00 40.32  ? 311 HOH A O   1 
HETATM 1214 O  O   . HOH F 6 .   ? 43.589 -6.635  31.929 1.00 42.10  ? 312 HOH A O   1 
HETATM 1215 O  O   . HOH F 6 .   ? 19.889 -9.516  36.961 1.00 36.50  ? 313 HOH A O   1 
HETATM 1216 O  O   . HOH F 6 .   ? 32.470 -24.649 32.178 1.00 59.44  ? 314 HOH A O   1 
HETATM 1217 O  O   . HOH F 6 .   ? 23.484 -5.729  32.899 1.00 34.63  ? 315 HOH A O   1 
HETATM 1218 O  O   . HOH F 6 .   ? 31.780 -0.824  15.862 1.00 36.08  ? 316 HOH A O   1 
HETATM 1219 O  O   . HOH F 6 .   ? 26.765 -31.952 16.122 1.00 39.79  ? 317 HOH A O   1 
HETATM 1220 O  O   . HOH F 6 .   ? 37.592 -20.403 26.979 1.00 30.72  ? 318 HOH A O   1 
HETATM 1221 O  O   . HOH F 6 .   ? 43.481 -10.714 35.338 1.00 54.54  ? 319 HOH A O   1 
HETATM 1222 O  O   . HOH F 6 .   ? 22.946 -28.225 12.618 1.00 22.28  ? 320 HOH A O   1 
HETATM 1223 O  O   . HOH F 6 .   ? 27.257 -10.107 35.804 1.00 35.46  ? 321 HOH A O   1 
HETATM 1224 O  O   . HOH F 6 .   ? 27.237 -35.326 11.782 1.00 53.12  ? 322 HOH A O   1 
HETATM 1225 O  O   . HOH F 6 .   ? 41.647 -12.779 14.376 1.00 64.91  ? 323 HOH A O   1 
HETATM 1226 O  O   . HOH F 6 .   ? 22.604 -27.616 17.712 1.00 47.45  ? 324 HOH A O   1 
HETATM 1227 O  O   . HOH F 6 .   ? 41.295 -16.944 15.171 1.00 31.85  ? 325 HOH A O   1 
HETATM 1228 O  O   . HOH F 6 .   ? 13.456 -14.341 21.815 1.00 63.19  ? 326 HOH A O   1 
HETATM 1229 O  O   . HOH F 6 .   ? 21.894 -24.931 18.309 1.00 21.51  ? 327 HOH A O   1 
HETATM 1230 O  O   . HOH F 6 .   ? 30.254 1.497   33.934 1.00 57.14  ? 328 HOH A O   1 
HETATM 1231 O  O   . HOH F 6 .   ? 20.463 -13.381 20.390 1.00 45.77  ? 329 HOH A O   1 
HETATM 1232 O  O   . HOH F 6 .   ? 34.892 -18.849 13.843 0.50 22.00  ? 330 HOH A O   1 
HETATM 1233 O  O   . HOH F 6 .   ? 32.310 -9.010  39.647 1.00 48.71  ? 331 HOH A O   1 
HETATM 1234 O  O   . HOH F 6 .   ? 29.896 -32.042 9.546  1.00 39.79  ? 332 HOH A O   1 
HETATM 1235 O  O   . HOH F 6 .   ? 28.276 -8.839  39.858 1.00 44.44  ? 333 HOH A O   1 
HETATM 1236 O  O   . HOH F 6 .   ? 27.324 -28.121 18.627 1.00 27.14  ? 334 HOH A O   1 
HETATM 1237 O  O   . HOH F 6 .   ? 17.964 -29.372 7.652  1.00 30.12  ? 335 HOH A O   1 
HETATM 1238 O  O   . HOH F 6 .   ? 14.227 -16.860 23.397 1.00 39.16  ? 336 HOH A O   1 
HETATM 1239 O  O   . HOH F 6 .   ? 21.738 -29.558 -5.249 1.00 36.17  ? 337 HOH A O   1 
HETATM 1240 O  O   . HOH F 6 .   ? 15.394 -9.869  24.805 1.00 49.81  ? 338 HOH A O   1 
HETATM 1241 O  O   . HOH F 6 .   ? 12.652 -20.382 42.427 1.00 57.67  ? 339 HOH A O   1 
HETATM 1242 O  O   . HOH F 6 .   ? 26.099 -22.541 29.907 1.00 24.18  ? 340 HOH A O   1 
HETATM 1243 O  O   . HOH F 6 .   ? 27.199 -2.478  16.070 1.00 60.15  ? 341 HOH A O   1 
HETATM 1244 O  O   . HOH F 6 .   ? 7.074  -17.009 32.426 1.00 52.02  ? 342 HOH A O   1 
HETATM 1245 O  O   . HOH F 6 .   ? 30.376 -0.511  36.859 1.00 43.76  ? 343 HOH A O   1 
HETATM 1246 O  O   . HOH F 6 .   ? 26.411 -7.718  36.789 1.00 47.83  ? 344 HOH A O   1 
HETATM 1247 O  O   . HOH F 6 .   ? 28.195 -23.691 31.636 1.00 36.54  ? 345 HOH A O   1 
HETATM 1248 O  O   . HOH F 6 .   ? 29.493 -2.228  13.734 1.00 59.65  ? 346 HOH A O   1 
HETATM 1249 O  O   . HOH F 6 .   ? 25.700 -2.846  19.966 1.00 56.36  ? 347 HOH A O   1 
HETATM 1250 O  O   . HOH F 6 .   ? 36.793 -5.616  12.160 1.00 33.38  ? 348 HOH A O   1 
HETATM 1251 O  O   . HOH F 6 .   ? 26.764 -16.522 38.600 1.00 45.32  ? 349 HOH A O   1 
HETATM 1252 O  O   . HOH F 6 .   ? 28.999 -31.141 7.228  1.00 27.27  ? 350 HOH A O   1 
HETATM 1253 O  O   . HOH F 6 .   ? 41.322 -6.986  35.859 1.00 42.37  ? 351 HOH A O   1 
HETATM 1254 O  O   . HOH F 6 .   ? 43.887 -4.352  25.709 1.00 41.73  ? 352 HOH A O   1 
HETATM 1255 O  O   . HOH F 6 .   ? 24.864 -26.751 18.986 1.00 29.01  ? 353 HOH A O   1 
HETATM 1256 O  O   . HOH F 6 .   ? 26.065 -19.149 41.660 1.00 64.96  ? 354 HOH A O   1 
HETATM 1257 O  O   . HOH F 6 .   ? 44.420 -12.485 41.162 1.00 49.50  ? 355 HOH A O   1 
HETATM 1258 O  O   . HOH F 6 .   ? 23.250 -17.138 44.291 1.00 57.50  ? 356 HOH A O   1 
HETATM 1259 O  O   . HOH F 6 .   ? 21.475 -29.969 14.158 1.00 71.01  ? 357 HOH A O   1 
HETATM 1260 O  O   . HOH F 6 .   ? 28.433 -24.238 34.292 1.00 49.77  ? 358 HOH A O   1 
HETATM 1261 O  O   . HOH F 6 .   ? 24.009 -15.806 21.130 1.00 25.58  ? 359 HOH A O   1 
HETATM 1262 O  O   . HOH F 6 .   ? 11.247 -14.980 40.518 1.00 81.46  ? 360 HOH A O   1 
HETATM 1263 O  O   . HOH F 6 .   ? 45.921 -14.265 21.537 1.00 53.65  ? 361 HOH A O   1 
HETATM 1264 O  O   . HOH F 6 .   ? 20.827 -7.175  19.644 1.00 49.43  ? 362 HOH A O   1 
HETATM 1265 O  O   . HOH F 6 .   ? 47.160 -25.311 21.680 1.00 47.37  ? 363 HOH A O   1 
HETATM 1266 O  O   . HOH F 6 .   ? 30.693 -28.820 22.623 1.00 35.45  ? 364 HOH A O   1 
HETATM 1267 O  O   . HOH F 6 .   ? 42.358 -10.316 15.342 1.00 40.73  ? 365 HOH A O   1 
HETATM 1268 O  O   . HOH F 6 .   ? 26.036 -21.824 38.593 1.00 33.84  ? 366 HOH A O   1 
HETATM 1269 O  O   A HOH F 6 .   ? 19.061 -23.012 4.268  0.60 34.12  ? 367 HOH A O   1 
HETATM 1270 O  O   . HOH F 6 .   ? 38.986 -18.911 33.317 1.00 45.85  ? 368 HOH A O   1 
HETATM 1271 O  O   . HOH F 6 .   ? 46.282 -29.784 21.256 1.00 68.56  ? 369 HOH A O   1 
HETATM 1272 O  O   . HOH F 6 .   ? 46.092 -15.790 27.621 1.00 56.03  ? 370 HOH A O   1 
HETATM 1273 O  O   . HOH F 6 .   ? 21.411 -27.063 14.505 0.50 38.65  ? 371 HOH A O   1 
HETATM 1274 O  O   . HOH F 6 .   ? 10.830 -11.401 34.519 1.00 45.87  ? 372 HOH A O   1 
HETATM 1275 O  O   . HOH F 6 .   ? 27.596 -23.062 13.843 0.50 22.78  ? 373 HOH A O   1 
HETATM 1276 O  O   . HOH F 6 .   ? 29.312 -27.374 20.605 1.00 23.65  ? 374 HOH A O   1 
HETATM 1277 O  O   . HOH F 6 .   ? 22.200 -34.015 26.089 1.00 67.77  ? 375 HOH A O   1 
HETATM 1278 O  O   . HOH F 6 .   ? 22.641 -34.035 8.830  1.00 29.65  ? 376 HOH A O   1 
HETATM 1279 O  O   . HOH F 6 .   ? 46.847 -21.824 17.919 1.00 40.60  ? 377 HOH A O   1 
HETATM 1280 O  O   . HOH F 6 .   ? 18.025 -24.294 39.771 1.00 40.74  ? 378 HOH A O   1 
HETATM 1281 O  O   . HOH F 6 .   ? 37.377 -6.468  34.232 1.00 37.30  ? 379 HOH A O   1 
HETATM 1282 O  O   . HOH F 6 .   ? 18.041 -34.573 8.320  1.00 29.04  ? 380 HOH A O   1 
HETATM 1283 O  O   . HOH F 6 .   ? 4.284  -20.308 37.712 1.00 58.31  ? 381 HOH A O   1 
HETATM 1284 O  O   . HOH F 6 .   ? 46.259 -18.990 19.695 1.00 45.24  ? 382 HOH A O   1 
HETATM 1285 O  O   . HOH F 6 .   ? 17.484 -24.445 -2.320 1.00 58.15  ? 383 HOH A O   1 
HETATM 1286 O  O   . HOH F 6 .   ? 42.124 -6.078  11.821 1.00 58.61  ? 384 HOH A O   1 
HETATM 1287 O  O   . HOH F 6 .   ? 34.167 -7.868  35.603 1.00 29.71  ? 385 HOH A O   1 
HETATM 1288 O  O   . HOH F 6 .   ? 25.847 -4.536  17.847 1.00 45.51  ? 386 HOH A O   1 
HETATM 1289 O  O   . HOH F 6 .   ? 26.264 -7.933  9.055  1.00 44.31  ? 387 HOH A O   1 
HETATM 1290 O  O   . HOH F 6 .   ? 20.156 -15.755 40.816 1.00 31.30  ? 388 HOH A O   1 
HETATM 1291 O  O   . HOH F 6 .   ? 33.031 -29.645 21.489 1.00 39.02  ? 389 HOH A O   1 
HETATM 1292 O  O   . HOH F 6 .   ? 40.338 -19.585 28.973 1.00 31.80  ? 390 HOH A O   1 
HETATM 1293 O  O   . HOH F 6 .   ? 37.861 -16.237 12.786 1.00 41.89  ? 391 HOH A O   1 
HETATM 1294 O  O   . HOH F 6 .   ? 46.015 -8.869  43.930 1.00 45.45  ? 392 HOH A O   1 
HETATM 1295 O  O   . HOH F 6 .   ? 31.828 -31.866 14.569 1.00 39.01  ? 393 HOH A O   1 
HETATM 1296 O  O   . HOH F 6 .   ? 44.746 -8.695  17.925 1.00 54.01  ? 394 HOH A O   1 
HETATM 1297 O  O   . HOH F 6 .   ? 45.204 -12.658 23.583 1.00 42.91  ? 395 HOH A O   1 
HETATM 1298 O  O   . HOH F 6 .   ? 10.129 -11.670 39.834 1.00 58.02  ? 396 HOH A O   1 
HETATM 1299 O  O   . HOH F 6 .   ? 22.443 -10.006 14.352 1.00 37.50  ? 397 HOH A O   1 
HETATM 1300 O  O   . HOH F 6 .   ? 35.456 2.057   13.548 1.00 53.77  ? 398 HOH A O   1 
HETATM 1301 O  O   . HOH F 6 .   ? 21.005 -23.065 42.048 1.00 46.22  ? 399 HOH A O   1 
HETATM 1302 O  O   . HOH F 6 .   ? 41.165 -17.051 35.155 1.00 39.25  ? 400 HOH A O   1 
HETATM 1303 O  O   . HOH F 6 .   ? 22.829 -14.795 40.311 1.00 31.42  ? 401 HOH A O   1 
HETATM 1304 O  O   . HOH F 6 .   ? 19.699 -27.375 10.033 1.00 54.73  ? 402 HOH A O   1 
HETATM 1305 O  O   . HOH F 6 .   ? 44.533 -16.400 29.738 1.00 44.95  ? 403 HOH A O   1 
HETATM 1306 O  O   . HOH F 6 .   ? 34.791 -33.340 21.827 1.00 52.21  ? 404 HOH A O   1 
HETATM 1307 O  O   . HOH F 6 .   ? 30.306 -10.528 40.535 1.00 37.01  ? 405 HOH A O   1 
HETATM 1308 O  O   . HOH F 6 .   ? 27.064 -1.578  21.948 1.00 50.45  ? 406 HOH A O   1 
HETATM 1309 O  O   . HOH F 6 .   ? 23.580 -15.612 17.880 1.00 37.63  ? 407 HOH A O   1 
HETATM 1310 O  O   . HOH F 6 .   ? 32.151 -15.647 39.762 1.00 31.44  ? 408 HOH A O   1 
HETATM 1311 O  O   . HOH F 6 .   ? 45.420 -10.607 30.319 1.00 54.87  ? 409 HOH A O   1 
HETATM 1312 O  O   . HOH F 6 .   ? 26.009 -29.201 22.543 1.00 51.45  ? 410 HOH A O   1 
HETATM 1313 O  O   . HOH F 6 .   ? 37.062 -2.373  11.494 1.00 58.85  ? 411 HOH A O   1 
HETATM 1314 O  O   . HOH F 6 .   ? 33.683 -33.077 12.275 1.00 38.51  ? 412 HOH A O   1 
HETATM 1315 O  O   . HOH F 6 .   ? 35.165 -29.727 23.541 1.00 45.69  ? 413 HOH A O   1 
HETATM 1316 O  O   . HOH F 6 .   ? 29.594 -0.840  22.135 1.00 51.17  ? 414 HOH A O   1 
HETATM 1317 O  O   . HOH F 6 .   ? 47.027 -20.195 21.960 1.00 60.68  ? 415 HOH A O   1 
HETATM 1318 O  O   . HOH F 6 .   ? 45.741 -17.137 17.079 1.00 60.14  ? 416 HOH A O   1 
HETATM 1319 O  O   . HOH F 6 .   ? 41.950 -8.070  13.663 1.00 55.22  ? 417 HOH A O   1 
HETATM 1320 O  O   . HOH F 6 .   ? 33.528 -0.289  20.022 1.00 41.51  ? 418 HOH A O   1 
HETATM 1321 O  O   . HOH F 6 .   ? 39.911 -5.587  33.848 1.00 41.82  ? 419 HOH A O   1 
HETATM 1322 O  O   . HOH F 6 .   ? 33.941 -17.660 39.290 1.00 54.44  ? 420 HOH A O   1 
HETATM 1323 O  O   B HOH F 6 .   ? 37.129 -11.812 40.019 0.50 30.99  ? 421 HOH A O   1 
HETATM 1324 O  O   . HOH F 6 .   ? 29.730 -22.603 36.656 1.00 72.98  ? 422 HOH A O   1 
HETATM 1325 O  O   . HOH F 6 .   ? 27.270 -25.555 28.234 1.00 50.47  ? 423 HOH A O   1 
HETATM 1326 O  O   . HOH F 6 .   ? 44.196 -25.860 26.668 1.00 54.35  ? 424 HOH A O   1 
HETATM 1327 O  O   . HOH F 6 .   ? 28.953 -16.177 41.305 1.00 63.51  ? 425 HOH A O   1 
HETATM 1328 O  O   . HOH F 6 .   ? 45.727 -5.520  23.618 1.00 41.24  ? 426 HOH A O   1 
HETATM 1329 O  O   . HOH F 6 .   ? 28.431 -2.605  11.250 1.00 70.17  ? 427 HOH A O   1 
HETATM 1330 O  O   . HOH F 6 .   ? 23.401 -30.451 19.249 1.00 62.45  ? 428 HOH A O   1 
HETATM 1331 O  O   . HOH F 6 .   ? 44.791 -8.141  15.162 1.00 68.40  ? 429 HOH A O   1 
HETATM 1332 O  O   . HOH F 6 .   ? 42.789 -18.277 30.691 1.00 43.14  ? 430 HOH A O   1 
HETATM 1333 O  O   . HOH F 6 .   ? 32.052 0.136   13.328 1.00 54.44  ? 431 HOH A O   1 
HETATM 1334 O  O   . HOH F 6 .   ? 25.715 -15.840 41.016 1.00 47.55  ? 432 HOH A O   1 
HETATM 1335 O  O   . HOH F 6 .   ? 32.450 -3.989  41.170 1.00 61.81  ? 433 HOH A O   1 
HETATM 1336 O  O   . HOH F 6 .   ? 31.923 -26.247 27.023 1.00 42.92  ? 434 HOH A O   1 
HETATM 1337 O  O   . HOH F 6 .   ? 47.881 -23.521 19.788 1.00 59.17  ? 435 HOH A O   1 
HETATM 1338 O  O   . HOH F 6 .   ? 27.119 -34.578 17.915 1.00 71.33  ? 436 HOH A O   1 
HETATM 1339 O  O   . HOH F 6 .   ? 37.754 -26.964 28.469 1.00 58.37  ? 437 HOH A O   1 
HETATM 1340 O  O   . HOH F 6 .   ? 28.399 -29.231 26.867 1.00 73.46  ? 438 HOH A O   1 
HETATM 1341 O  O   . HOH F 6 .   ? 20.086 -35.294 10.171 1.00 35.97  ? 439 HOH A O   1 
HETATM 1342 O  O   . HOH F 6 .   ? 35.204 -4.139  10.569 1.00 44.08  ? 440 HOH A O   1 
HETATM 1343 O  O   . HOH F 6 .   ? 19.442 -31.769 13.966 1.00 64.47  ? 441 HOH A O   1 
HETATM 1344 O  O   . HOH F 6 .   ? 24.321 -21.457 40.963 1.00 51.50  ? 442 HOH A O   1 
HETATM 1345 O  O   . HOH F 6 .   ? 36.860 -24.405 27.560 1.00 50.74  ? 443 HOH A O   1 
HETATM 1346 O  O   . HOH F 6 .   ? 30.938 -34.429 14.802 1.00 57.70  ? 444 HOH A O   1 
HETATM 1347 O  O   . HOH F 6 .   ? 22.968 -2.702  26.128 1.00 62.04  ? 445 HOH A O   1 
HETATM 1348 O  O   . HOH F 6 .   ? 46.536 -14.667 17.843 1.00 66.16  ? 446 HOH A O   1 
HETATM 1349 O  O   . HOH F 6 .   ? 12.012 -18.569 22.343 1.00 54.59  ? 447 HOH A O   1 
HETATM 1350 O  O   . HOH F 6 .   ? 33.770 -10.944 41.530 0.50 50.78  ? 448 HOH A O   1 
HETATM 1351 O  O   . HOH F 6 .   ? 47.138 -12.958 28.421 1.00 57.15  ? 449 HOH A O   1 
HETATM 1352 O  O   . HOH F 6 .   ? 13.613 -16.085 39.724 1.00 75.27  ? 450 HOH A O   1 
HETATM 1353 O  O   . HOH F 6 .   ? 34.619 -18.906 35.939 1.00 61.44  ? 451 HOH A O   1 
HETATM 1354 O  O   . HOH F 6 .   ? 47.063 -11.901 25.414 1.00 61.27  ? 452 HOH A O   1 
HETATM 1355 O  O   A HOH F 6 .   ? 12.066 -20.666 27.784 0.78 46.01  ? 453 HOH A O   1 
HETATM 1356 O  O   . HOH F 6 .   ? 32.251 -1.074  22.277 1.00 53.53  ? 454 HOH A O   1 
HETATM 1357 O  O   . HOH F 6 .   ? 32.699 -3.225  10.020 1.00 60.16  ? 455 HOH A O   1 
HETATM 1358 O  O   . HOH F 6 .   ? 43.086 -3.085  33.750 1.00 60.63  ? 456 HOH A O   1 
HETATM 1359 O  O   . HOH F 6 .   ? 19.269 -7.564  35.222 1.00 56.47  ? 457 HOH A O   1 
HETATM 1360 O  O   . HOH F 6 .   ? 17.102 -28.069 9.846  1.00 49.83  ? 458 HOH A O   1 
HETATM 1361 O  O   . HOH F 6 .   ? 25.350 -5.749  35.214 1.00 53.40  ? 459 HOH A O   1 
HETATM 1362 O  O   . HOH F 6 .   ? 15.846 -15.499 41.141 1.00 55.99  ? 460 HOH A O   1 
HETATM 1363 O  O   . HOH F 6 .   ? 28.057 -29.787 24.233 1.00 58.01  ? 461 HOH A O   1 
HETATM 1364 O  O   . HOH F 6 .   ? 17.395 -8.106  24.800 1.00 52.50  ? 462 HOH A O   1 
HETATM 1365 O  O   . HOH F 6 .   ? 32.084 -23.805 34.750 1.00 61.01  ? 463 HOH A O   1 
HETATM 1366 O  O   . HOH F 6 .   ? 44.242 -13.451 13.843 0.50 58.94  ? 464 HOH A O   1 
HETATM 1367 O  O   . HOH F 6 .   ? 33.770 -13.960 41.530 0.50 36.04  ? 465 HOH A O   1 
HETATM 1368 O  O   . HOH F 6 .   ? 32.636 -20.426 37.023 1.00 62.55  ? 466 HOH A O   1 
HETATM 1369 O  O   . HOH F 6 .   ? 45.371 -12.774 16.242 1.00 61.13  ? 467 HOH A O   1 
HETATM 1370 O  O   . HOH F 6 .   ? 18.951 -28.054 13.843 0.50 65.69  ? 468 HOH A O   1 
HETATM 1371 O  O   . HOH F 6 .   ? 21.134 -5.643  34.690 1.00 51.56  ? 469 HOH A O   1 
HETATM 1372 O  O   . HOH F 6 .   ? 23.199 -4.532  17.173 1.00 71.69  ? 470 HOH A O   1 
HETATM 1373 O  O   . HOH F 6 .   ? 34.949 -23.652 32.766 1.00 58.62  ? 471 HOH A O   1 
HETATM 1374 O  O   . HOH F 6 .   ? 16.740 -6.702  34.629 1.00 70.48  ? 472 HOH A O   1 
HETATM 1375 O  O   . HOH F 6 .   ? 33.086 -0.633  42.912 1.00 54.88  ? 473 HOH A O   1 
HETATM 1376 O  O   . HOH G 6 .   ? 12.287 -24.277 -0.010 1.00 45.52  ? 201 HOH D O   1 
HETATM 1377 O  O   . HOH G 6 .   ? 15.018 -25.829 -1.805 1.00 40.54  ? 202 HOH D O   1 
HETATM 1378 O  O   . HOH G 6 .   ? 21.038 -38.284 4.035  1.00 43.93  ? 203 HOH D O   1 
HETATM 1379 O  O   . HOH G 6 .   ? 17.750 -36.341 6.103  1.00 37.51  ? 204 HOH D O   1 
HETATM 1380 O  O   . HOH G 6 .   ? 11.660 -23.544 3.097  1.00 47.56  ? 205 HOH D O   1 
HETATM 1381 O  O   . HOH G 6 .   ? 20.872 -39.511 -2.146 1.00 54.87  ? 206 HOH D O   1 
HETATM 1382 O  O   . HOH G 6 .   ? 18.654 -40.654 0.670  1.00 66.36  ? 207 HOH D O   1 
HETATM 1383 O  O   . HOH G 6 .   ? 10.623 -24.784 5.578  1.00 53.42  ? 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   ? 0.7702 0.9452 0.6477 0.0399  -0.1274 -0.0248 6   ASP A N   
2    C CA  . ASP A 5   ? 0.7659 0.9337 0.6271 0.0239  -0.1191 -0.0272 6   ASP A CA  
3    C C   . ASP A 5   ? 0.7478 0.9458 0.6334 0.0116  -0.1155 -0.0429 6   ASP A C   
4    O O   . ASP A 5   ? 0.7398 0.9655 0.6531 0.0151  -0.1205 -0.0521 6   ASP A O   
5    C CB  . ASP A 5   ? 0.7888 0.9269 0.6402 0.0149  -0.1019 -0.0200 6   ASP A CB  
6    C CG  . ASP A 5   ? 0.9793 1.0960 0.7980 0.0058  -0.0969 -0.0159 6   ASP A CG  
7    O OD1 . ASP A 5   ? 0.9836 1.1119 0.8003 -0.0049 -0.0951 -0.0245 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.0854 1.1733 0.8800 0.0081  -0.0935 -0.0050 6   ASP A OD2 
9    N N   . SER A 6   ? 0.6428 0.8345 0.5178 -0.0033 -0.1062 -0.0468 7   SER A N   
10   C CA  . SER A 6   ? 0.5967 0.8090 0.4891 -0.0169 -0.1003 -0.0611 7   SER A CA  
11   C C   . SER A 6   ? 0.5433 0.7409 0.4464 -0.0282 -0.0819 -0.0624 7   SER A C   
12   O O   . SER A 6   ? 0.5364 0.7363 0.4416 -0.0409 -0.0738 -0.0710 7   SER A O   
13   C CB  . SER A 6   ? 0.6759 0.8919 0.5467 -0.0243 -0.1050 -0.0659 7   SER A CB  
14   O OG  . SER A 6   ? 0.8459 1.0332 0.6889 -0.0294 -0.0969 -0.0581 7   SER A OG  
15   N N   . CYS A 7   ? 0.4224 0.6046 0.3318 -0.0227 -0.0760 -0.0542 8   CYS A N   
16   C CA  . CYS A 7   ? 0.3781 0.5460 0.2963 -0.0308 -0.0610 -0.0546 8   CYS A CA  
17   C C   . CYS A 7   ? 0.3751 0.5586 0.3169 -0.0393 -0.0555 -0.0661 8   CYS A C   
18   O O   . CYS A 7   ? 0.3621 0.5684 0.3192 -0.0372 -0.0619 -0.0727 8   CYS A O   
19   C CB  . CYS A 7   ? 0.3888 0.5397 0.3086 -0.0227 -0.0578 -0.0442 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.4666 0.5900 0.3561 -0.0178 -0.0579 -0.0311 8   CYS A SG  
21   N N   . ILE A 8   ? 0.2809 0.4510 0.2253 -0.0484 -0.0435 -0.0687 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2396 0.4134 0.2014 -0.0562 -0.0360 -0.0766 9   ILE A CA  
23   C C   . ILE A 8   ? 0.2658 0.4228 0.2327 -0.0514 -0.0303 -0.0686 9   ILE A C   
24   O O   . ILE A 8   ? 0.2650 0.4066 0.2216 -0.0455 -0.0299 -0.0594 9   ILE A O   
25   C CB  . ILE A 8   ? 0.2808 0.4493 0.2402 -0.0690 -0.0278 -0.0859 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.2911 0.4364 0.2374 -0.0697 -0.0211 -0.0814 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.2859 0.4755 0.2428 -0.0749 -0.0338 -0.0960 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3508 0.4862 0.2957 -0.0800 -0.0122 -0.0903 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2015 0.3599 0.1822 -0.0551 -0.0251 -0.0724 10  GLN A N   
30   N N   B GLN A 9   ? 0.1999 0.3601 0.1812 -0.0546 -0.0259 -0.0725 10  GLN A N   
31   C CA  A GLN A 9   ? 0.1962 0.3389 0.1800 -0.0510 -0.0204 -0.0652 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.1900 0.3357 0.1755 -0.0509 -0.0210 -0.0659 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2485 0.3769 0.2346 -0.0598 -0.0108 -0.0691 10  GLN A C   
34   C C   B GLN A 9   ? 0.2278 0.3573 0.2139 -0.0598 -0.0112 -0.0693 10  GLN A C   
35   O O   A GLN A 9   ? 0.2445 0.3807 0.2368 -0.0688 -0.0074 -0.0782 10  GLN A O   
36   O O   B GLN A 9   ? 0.2216 0.3561 0.2112 -0.0695 -0.0074 -0.0786 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2071 0.3638 0.2028 -0.0436 -0.0251 -0.0639 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.1967 0.3587 0.1965 -0.0457 -0.0247 -0.0671 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2116 0.3535 0.2103 -0.0400 -0.0201 -0.0575 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.2940 0.4432 0.2993 -0.0450 -0.0180 -0.0633 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5382 0.6959 0.5515 -0.0353 -0.0224 -0.0599 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4052 0.5536 0.4125 -0.0331 -0.0223 -0.0554 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4278 0.6001 0.4537 -0.0422 -0.0192 -0.0696 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.2603 0.4176 0.2655 -0.0239 -0.0310 -0.0523 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.5823 0.7369 0.5943 -0.0239 -0.0270 -0.0523 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.2730 0.4083 0.2823 -0.0331 -0.0163 -0.0519 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2280 0.3346 0.2082 -0.0574 -0.0066 -0.0626 11  PHE A N   
48   N N   B PHE A 10  ? 0.1937 0.3028 0.1753 -0.0564 -0.0074 -0.0621 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2280 0.3164 0.2068 -0.0633 0.0007  -0.0646 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.1971 0.2870 0.1765 -0.0619 -0.0001 -0.0635 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2513 0.3369 0.2355 -0.0620 0.0027  -0.0616 11  PHE A C   
52   C C   B PHE A 10  ? 0.2398 0.3275 0.2250 -0.0613 0.0021  -0.0613 11  PHE A C   
53   O O   A PHE A 10  ? 0.2397 0.3188 0.2233 -0.0546 0.0012  -0.0539 11  PHE A O   
54   O O   B PHE A 10  ? 0.2257 0.3096 0.2113 -0.0536 0.0002  -0.0539 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2514 0.3199 0.2221 -0.0604 0.0027  -0.0610 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2205 0.2921 0.1922 -0.0578 0.0012  -0.0587 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2700 0.3176 0.2365 -0.0650 0.0082  -0.0637 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.2496 0.3193 0.2159 -0.0621 0.0027  -0.0646 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3127 0.3564 0.2760 -0.0739 0.0122  -0.0720 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.2914 0.3746 0.2542 -0.0618 -0.0010 -0.0661 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3011 0.3312 0.2649 -0.0605 0.0090  -0.0579 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.2978 0.3508 0.2608 -0.0666 0.0077  -0.0692 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3384 0.3574 0.2938 -0.0776 0.0171  -0.0736 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3112 0.3929 0.2683 -0.0669 0.0014  -0.0726 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3336 0.3409 0.2897 -0.0634 0.0125  -0.0595 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3440 0.3950 0.3027 -0.0705 0.0099  -0.0760 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3125 0.3126 0.2636 -0.0716 0.0167  -0.0668 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3141 0.3804 0.2705 -0.0711 0.0072  -0.0780 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2048 0.2967 0.1944 -0.0705 0.0068  -0.0689 12  THR A N   
70   C CA  . THR A 11  ? 0.2080 0.3001 0.2030 -0.0722 0.0106  -0.0689 12  THR A CA  
71   C C   . THR A 11  ? 0.2591 0.3265 0.2453 -0.0686 0.0132  -0.0606 12  THR A C   
72   O O   . THR A 11  ? 0.2393 0.3095 0.2297 -0.0633 0.0124  -0.0564 12  THR A O   
73   C CB  . THR A 11  ? 0.2892 0.3855 0.2870 -0.0860 0.0180  -0.0798 12  THR A CB  
74   O OG1 . THR A 11  ? 0.2832 0.4076 0.2921 -0.0886 0.0142  -0.0886 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3598 0.4569 0.3626 -0.0901 0.0240  -0.0817 12  THR A CG2 
76   N N   A ARG A 12  ? 0.2409 0.2848 0.2149 -0.0708 0.0156  -0.0590 13  ARG A N   
77   N N   B ARG A 12  ? 0.2446 0.2884 0.2186 -0.0709 0.0157  -0.0590 13  ARG A N   
78   C CA  A ARG A 12  ? 0.2495 0.2697 0.2138 -0.0673 0.0165  -0.0522 13  ARG A CA  
79   C CA  B ARG A 12  ? 0.2546 0.2749 0.2190 -0.0673 0.0165  -0.0522 13  ARG A CA  
80   C C   A ARG A 12  ? 0.2737 0.2920 0.2387 -0.0563 0.0109  -0.0449 13  ARG A C   
81   C C   B ARG A 12  ? 0.2748 0.2932 0.2398 -0.0563 0.0109  -0.0449 13  ARG A C   
82   O O   A ARG A 12  ? 0.2616 0.2632 0.2200 -0.0529 0.0104  -0.0403 13  ARG A O   
83   O O   B ARG A 12  ? 0.2615 0.2636 0.2201 -0.0529 0.0104  -0.0401 13  ARG A O   
84   C CB  A ARG A 12  ? 0.3091 0.3029 0.2591 -0.0732 0.0204  -0.0541 13  ARG A CB  
85   C CB  B ARG A 12  ? 0.3253 0.3192 0.2754 -0.0731 0.0203  -0.0540 13  ARG A CB  
86   C CG  A ARG A 12  ? 0.3921 0.3795 0.3362 -0.0867 0.0285  -0.0608 13  ARG A CG  
87   C CG  B ARG A 12  ? 0.4707 0.4535 0.4126 -0.0852 0.0283  -0.0585 13  ARG A CG  
88   C CD  A ARG A 12  ? 0.5367 0.5183 0.4770 -0.0906 0.0330  -0.0591 13  ARG A CD  
89   C CD  B ARG A 12  ? 0.5839 0.5545 0.5172 -0.0951 0.0334  -0.0656 13  ARG A CD  
90   N NE  A ARG A 12  ? 0.6617 0.6132 0.5847 -0.0869 0.0320  -0.0516 13  ARG A NE  
91   N NE  B ARG A 12  ? 0.6232 0.5709 0.5458 -0.0894 0.0304  -0.0629 13  ARG A NE  
92   C CZ  A ARG A 12  ? 0.7548 0.6999 0.6729 -0.0862 0.0332  -0.0475 13  ARG A CZ  
93   C CZ  B ARG A 12  ? 0.7404 0.6900 0.6644 -0.0907 0.0303  -0.0683 13  ARG A CZ  
94   N NH1 A ARG A 12  ? 0.5037 0.4705 0.4347 -0.0885 0.0362  -0.0502 13  ARG A NH1 
95   N NH1 B ARG A 12  ? 0.6537 0.5825 0.5696 -0.0843 0.0278  -0.0668 13  ARG A NH1 
96   N NH2 A ARG A 12  ? 0.6179 0.5353 0.5183 -0.0827 0.0308  -0.0411 13  ARG A NH2 
97   N NH2 B ARG A 12  ? 0.4342 0.4072 0.3681 -0.0981 0.0324  -0.0761 13  ARG A NH2 
98   N N   . HIS A 13  ? 0.2207 0.2548 0.1918 -0.0516 0.0069  -0.0444 14  HIS A N   
99   C CA  . HIS A 13  ? 0.2188 0.2505 0.1892 -0.0437 0.0036  -0.0390 14  HIS A CA  
100  C C   . HIS A 13  ? 0.2504 0.2777 0.2215 -0.0389 0.0030  -0.0330 14  HIS A C   
101  O O   . HIS A 13  ? 0.2429 0.2588 0.2109 -0.0356 0.0023  -0.0304 14  HIS A O   
102  C CB  . HIS A 13  ? 0.2150 0.2618 0.1874 -0.0413 0.0006  -0.0392 14  HIS A CB  
103  C CG  . HIS A 13  ? 0.2340 0.2762 0.2038 -0.0361 -0.0003 -0.0350 14  HIS A CG  
104  N ND1 . HIS A 13  ? 0.2437 0.2777 0.2120 -0.0362 0.0011  -0.0377 14  HIS A ND1 
105  C CD2 . HIS A 13  ? 0.2419 0.2864 0.2107 -0.0314 -0.0018 -0.0297 14  HIS A CD2 
106  C CE1 . HIS A 13  ? 0.2375 0.2718 0.2054 -0.0327 0.0011  -0.0348 14  HIS A CE1 
107  N NE2 . HIS A 13  ? 0.2326 0.2714 0.1992 -0.0304 -0.0002 -0.0295 14  HIS A NE2 
108  N N   . ALA A 14  ? 0.2094 0.2469 0.1855 -0.0380 0.0030  -0.0319 15  ALA A N   
109  C CA  . ALA A 14  ? 0.2061 0.2391 0.1825 -0.0337 0.0032  -0.0269 15  ALA A CA  
110  C C   . ALA A 14  ? 0.2413 0.2573 0.2112 -0.0366 0.0058  -0.0262 15  ALA A C   
111  O O   . ALA A 14  ? 0.2237 0.2312 0.1906 -0.0329 0.0046  -0.0224 15  ALA A O   
112  C CB  . ALA A 14  ? 0.2158 0.2627 0.2000 -0.0317 0.0031  -0.0276 15  ALA A CB  
113  N N   A SER A 15  ? 0.2199 0.2297 0.1856 -0.0436 0.0092  -0.0300 16  SER A N   
114  N N   B SER A 15  ? 0.2202 0.2299 0.1858 -0.0436 0.0092  -0.0300 16  SER A N   
115  N N   C SER A 15  ? 0.2187 0.2284 0.1844 -0.0437 0.0092  -0.0300 16  SER A N   
116  C CA  A SER A 15  ? 0.2318 0.2210 0.1857 -0.0471 0.0114  -0.0288 16  SER A CA  
117  C CA  B SER A 15  ? 0.2328 0.2217 0.1865 -0.0471 0.0114  -0.0288 16  SER A CA  
118  C CA  C SER A 15  ? 0.2309 0.2198 0.1846 -0.0470 0.0114  -0.0287 16  SER A CA  
119  C C   A SER A 15  ? 0.2875 0.2610 0.2338 -0.0426 0.0070  -0.0265 16  SER A C   
120  C C   B SER A 15  ? 0.2905 0.2639 0.2368 -0.0426 0.0070  -0.0265 16  SER A C   
121  C C   C SER A 15  ? 0.2921 0.2652 0.2381 -0.0427 0.0071  -0.0266 16  SER A C   
122  O O   A SER A 15  ? 0.2632 0.2240 0.2025 -0.0397 0.0048  -0.0232 16  SER A O   
123  O O   B SER A 15  ? 0.2711 0.2316 0.2102 -0.0398 0.0049  -0.0232 16  SER A O   
124  O O   C SER A 15  ? 0.2770 0.2366 0.2154 -0.0400 0.0049  -0.0233 16  SER A O   
125  C CB  A SER A 15  ? 0.2800 0.2635 0.2281 -0.0573 0.0174  -0.0340 16  SER A CB  
126  C CB  B SER A 15  ? 0.2826 0.2656 0.2304 -0.0573 0.0173  -0.0340 16  SER A CB  
127  C CB  C SER A 15  ? 0.2786 0.2619 0.2266 -0.0573 0.0176  -0.0338 16  SER A CB  
128  O OG  A SER A 15  ? 0.3250 0.2837 0.2563 -0.0612 0.0196  -0.0319 16  SER A OG  
129  O OG  B SER A 15  ? 0.3142 0.3151 0.2723 -0.0613 0.0215  -0.0382 16  SER A OG  
130  O OG  C SER A 15  ? 0.3259 0.3080 0.2724 -0.0612 0.0181  -0.0380 16  SER A OG  
131  N N   . ASP A 16  ? 0.2645 0.2406 0.2133 -0.0416 0.0054  -0.0293 17  ASP A N   
132  C CA  . ASP A 16  ? 0.2779 0.2428 0.2236 -0.0361 0.0013  -0.0294 17  ASP A CA  
133  C C   . ASP A 16  ? 0.2711 0.2439 0.2239 -0.0292 -0.0022 -0.0269 17  ASP A C   
134  O O   . ASP A 16  ? 0.2742 0.2376 0.2246 -0.0243 -0.0063 -0.0264 17  ASP A O   
135  C CB  . ASP A 16  ? 0.2904 0.2599 0.2393 -0.0373 0.0019  -0.0345 17  ASP A CB  
136  C CG  . ASP A 16  ? 0.3996 0.3562 0.3394 -0.0447 0.0057  -0.0384 17  ASP A CG  
137  O OD1 . ASP A 16  ? 0.4060 0.3469 0.3348 -0.0492 0.0081  -0.0367 17  ASP A OD1 
138  O OD2 . ASP A 16  ? 0.3987 0.3598 0.3409 -0.0472 0.0071  -0.0434 17  ASP A OD2 
139  N N   . VAL A 17  ? 0.2092 0.1988 0.1701 -0.0289 -0.0009 -0.0258 18  VAL A N   
140  C CA  . VAL A 17  ? 0.2021 0.1969 0.1676 -0.0246 -0.0023 -0.0238 18  VAL A CA  
141  C C   . VAL A 17  ? 0.2455 0.2315 0.2069 -0.0235 -0.0034 -0.0207 18  VAL A C   
142  O O   . VAL A 17  ? 0.2298 0.2129 0.1922 -0.0201 -0.0064 -0.0212 18  VAL A O   
143  C CB  . VAL A 17  ? 0.2224 0.2306 0.1919 -0.0247 -0.0004 -0.0220 18  VAL A CB  
144  C CG1 . VAL A 17  ? 0.2223 0.2310 0.1930 -0.0223 0.0000  -0.0194 18  VAL A CG1 
145  C CG2 . VAL A 17  ? 0.2137 0.2298 0.1845 -0.0258 -0.0001 -0.0252 18  VAL A CG2 
146  N N   . LEU A 18  ? 0.2219 0.2052 0.1793 -0.0268 -0.0008 -0.0188 19  LEU A N   
147  C CA  . LEU A 18  ? 0.2316 0.2064 0.1835 -0.0269 -0.0008 -0.0163 19  LEU A CA  
148  C C   . LEU A 18  ? 0.2813 0.2390 0.2225 -0.0259 -0.0050 -0.0164 19  LEU A C   
149  O O   . LEU A 18  ? 0.2500 0.2032 0.1886 -0.0230 -0.0085 -0.0154 19  LEU A O   
150  C CB  . LEU A 18  ? 0.2423 0.2186 0.1928 -0.0314 0.0042  -0.0160 19  LEU A CB  
151  C CG  . LEU A 18  ? 0.2821 0.2526 0.2284 -0.0317 0.0058  -0.0141 19  LEU A CG  
152  C CD1 . LEU A 18  ? 0.2759 0.2543 0.2295 -0.0273 0.0054  -0.0125 19  LEU A CD1 
153  C CD2 . LEU A 18  ? 0.3323 0.3044 0.2779 -0.0370 0.0120  -0.0159 19  LEU A CD2 
154  N N   . LEU A 19  ? 0.2650 0.2122 0.1991 -0.0278 -0.0052 -0.0178 20  LEU A N   
155  C CA  . LEU A 19  ? 0.2917 0.2178 0.2121 -0.0253 -0.0104 -0.0172 20  LEU A CA  
156  C C   . LEU A 19  ? 0.2937 0.2243 0.2221 -0.0164 -0.0178 -0.0192 20  LEU A C   
157  O O   . LEU A 19  ? 0.2856 0.2066 0.2072 -0.0118 -0.0242 -0.0182 20  LEU A O   
158  C CB  . LEU A 19  ? 0.3230 0.2363 0.2349 -0.0290 -0.0082 -0.0191 20  LEU A CB  
159  C CG  . LEU A 19  ? 0.4455 0.3314 0.3395 -0.0254 -0.0138 -0.0179 20  LEU A CG  
160  C CD1 . LEU A 19  ? 0.4914 0.3565 0.3642 -0.0303 -0.0127 -0.0137 20  LEU A CD1 
161  C CD2 . LEU A 19  ? 0.5110 0.3852 0.3992 -0.0286 -0.0109 -0.0208 20  LEU A CD2 
162  N N   . ASN A 20  ? 0.2479 0.1947 0.1909 -0.0143 -0.0168 -0.0228 21  ASN A N   
163  C CA  . ASN A 20  ? 0.2408 0.1963 0.1948 -0.0074 -0.0218 -0.0271 21  ASN A CA  
164  C C   . ASN A 20  ? 0.2608 0.2263 0.2208 -0.0068 -0.0227 -0.0268 21  ASN A C   
165  O O   . ASN A 20  ? 0.2587 0.2261 0.2232 -0.0012 -0.0290 -0.0303 21  ASN A O   
166  C CB  . ASN A 20  ? 0.2459 0.2150 0.2117 -0.0077 -0.0184 -0.0318 21  ASN A CB  
167  C CG  . ASN A 20  ? 0.3920 0.3496 0.3532 -0.0059 -0.0197 -0.0348 21  ASN A CG  
168  O OD1 . ASN A 20  ? 0.3426 0.2812 0.2933 -0.0019 -0.0249 -0.0339 21  ASN A OD1 
169  N ND2 . ASN A 20  ? 0.2922 0.2584 0.2587 -0.0091 -0.0151 -0.0382 21  ASN A ND2 
170  N N   . LEU A 21  ? 0.2275 0.1997 0.1882 -0.0121 -0.0168 -0.0235 22  LEU A N   
171  C CA  . LEU A 21  ? 0.2198 0.1976 0.1835 -0.0128 -0.0163 -0.0232 22  LEU A CA  
172  C C   . LEU A 21  ? 0.2546 0.2196 0.2075 -0.0113 -0.0218 -0.0217 22  LEU A C   
173  O O   . LEU A 21  ? 0.2304 0.1997 0.1869 -0.0091 -0.0259 -0.0246 22  LEU A O   
174  C CB  . LEU A 21  ? 0.2132 0.1954 0.1768 -0.0174 -0.0092 -0.0195 22  LEU A CB  
175  C CG  . LEU A 21  ? 0.2399 0.2333 0.2106 -0.0185 -0.0049 -0.0203 22  LEU A CG  
176  C CD1 . LEU A 21  ? 0.2415 0.2362 0.2099 -0.0204 -0.0002 -0.0160 22  LEU A CD1 
177  C CD2 . LEU A 21  ? 0.2733 0.2756 0.2522 -0.0183 -0.0044 -0.0251 22  LEU A CD2 
178  N N   . ASN A 22  ? 0.2404 0.1895 0.1788 -0.0135 -0.0215 -0.0179 23  ASN A N   
179  C CA  . ASN A 22  ? 0.2568 0.1897 0.1796 -0.0128 -0.0268 -0.0160 23  ASN A CA  
180  C C   . ASN A 22  ? 0.3156 0.2419 0.2361 -0.0041 -0.0379 -0.0186 23  ASN A C   
181  O O   . ASN A 22  ? 0.3226 0.2450 0.2373 -0.0009 -0.0451 -0.0192 23  ASN A O   
182  C CB  . ASN A 22  ? 0.2907 0.2061 0.1960 -0.0189 -0.0223 -0.0121 23  ASN A CB  
183  C CG  . ASN A 22  ? 0.3863 0.2849 0.2726 -0.0208 -0.0251 -0.0097 23  ASN A CG  
184  O OD1 . ASN A 22  ? 0.3570 0.2617 0.2456 -0.0204 -0.0268 -0.0105 23  ASN A OD1 
185  N ND2 . ASN A 22  ? 0.4210 0.2970 0.2862 -0.0242 -0.0248 -0.0070 23  ASN A ND2 
186  N N   . ARG A 23  ? 0.2825 0.2085 0.2084 0.0004  -0.0400 -0.0211 24  ARG A N   
187  C CA  . ARG A 23  ? 0.2976 0.2191 0.2248 0.0109  -0.0511 -0.0250 24  ARG A CA  
188  C C   . ARG A 23  ? 0.3349 0.2797 0.2820 0.0151  -0.0551 -0.0320 24  ARG A C   
189  O O   . ARG A 23  ? 0.3303 0.2738 0.2766 0.0228  -0.0659 -0.0350 24  ARG A O   
190  C CB  . ARG A 23  ? 0.2863 0.2050 0.2183 0.0144  -0.0505 -0.0278 24  ARG A CB  
191  C CG  . ARG A 23  ? 0.3832 0.2747 0.2931 0.0111  -0.0484 -0.0227 24  ARG A CG  
192  C CD  . ARG A 23  ? 0.4294 0.3221 0.3459 0.0104  -0.0437 -0.0260 24  ARG A CD  
193  N NE  . ARG A 23  ? 0.5384 0.4028 0.4330 0.0066  -0.0417 -0.0225 24  ARG A NE  
194  C CZ  . ARG A 23  ? 0.7712 0.6311 0.6658 0.0032  -0.0362 -0.0249 24  ARG A CZ  
195  N NH1 . ARG A 23  ? 0.5831 0.4658 0.4980 0.0031  -0.0325 -0.0305 24  ARG A NH1 
196  N NH2 . ARG A 23  ? 0.6366 0.4680 0.5091 -0.0015 -0.0337 -0.0223 24  ARG A NH2 
197  N N   . LEU A 24  ? 0.2767 0.2422 0.2402 0.0095  -0.0464 -0.0349 25  LEU A N   
198  C CA  . LEU A 24  ? 0.2448 0.2316 0.2258 0.0103  -0.0475 -0.0423 25  LEU A CA  
199  C C   . LEU A 24  ? 0.2918 0.2765 0.2656 0.0081  -0.0507 -0.0410 25  LEU A C   
200  O O   . LEU A 24  ? 0.2917 0.2865 0.2737 0.0128  -0.0587 -0.0477 25  LEU A O   
201  C CB  . LEU A 24  ? 0.2263 0.2285 0.2190 0.0028  -0.0361 -0.0441 25  LEU A CB  
202  C CG  . LEU A 24  ? 0.2638 0.2717 0.2645 0.0033  -0.0319 -0.0471 25  LEU A CG  
203  C CD1 . LEU A 24  ? 0.2616 0.2818 0.2686 -0.0048 -0.0212 -0.0478 25  LEU A CD1 
204  C CD2 . LEU A 24  ? 0.2840 0.3012 0.2989 0.0119  -0.0389 -0.0570 25  LEU A CD2 
205  N N   . ARG A 25  ? 0.2562 0.2287 0.2153 0.0013  -0.0449 -0.0335 26  ARG A N   
206  C CA  . ARG A 25  ? 0.2693 0.2374 0.2189 -0.0016 -0.0470 -0.0324 26  ARG A CA  
207  C C   . ARG A 25  ? 0.3455 0.3014 0.2824 0.0061  -0.0609 -0.0329 26  ARG A C   
208  O O   . ARG A 25  ? 0.3416 0.3057 0.2815 0.0078  -0.0678 -0.0378 26  ARG A O   
209  C CB  . ARG A 25  ? 0.2850 0.2404 0.2205 -0.0092 -0.0383 -0.0252 26  ARG A CB  
210  C CG  . ARG A 25  ? 0.3528 0.3047 0.2794 -0.0132 -0.0390 -0.0255 26  ARG A CG  
211  C CD  . ARG A 25  ? 0.3885 0.3310 0.3049 -0.0205 -0.0291 -0.0206 26  ARG A CD  
212  N NE  . ARG A 25  ? 0.3733 0.2983 0.2734 -0.0217 -0.0282 -0.0157 26  ARG A NE  
213  C CZ  . ARG A 25  ? 0.5353 0.4441 0.4158 -0.0264 -0.0269 -0.0131 26  ARG A CZ  
214  N NH1 . ARG A 25  ? 0.4698 0.3771 0.3437 -0.0290 -0.0281 -0.0148 26  ARG A NH1 
215  N NH2 . ARG A 25  ? 0.4169 0.3100 0.2830 -0.0297 -0.0237 -0.0096 26  ARG A NH2 
216  N N   A SER A 26  ? 0.3378 0.2729 0.2588 0.0102  -0.0650 -0.0279 27  SER A N   
217  N N   B SER A 26  ? 0.3349 0.2699 0.2557 0.0102  -0.0651 -0.0279 27  SER A N   
218  N N   C SER A 26  ? 0.3297 0.2647 0.2506 0.0103  -0.0651 -0.0279 27  SER A N   
219  C CA  A SER A 26  ? 0.3698 0.2859 0.2724 0.0184  -0.0787 -0.0264 27  SER A CA  
220  C CA  B SER A 26  ? 0.3653 0.2813 0.2675 0.0184  -0.0788 -0.0264 27  SER A CA  
221  C CA  C SER A 26  ? 0.3586 0.2741 0.2607 0.0185  -0.0787 -0.0263 27  SER A CA  
222  C C   A SER A 26  ? 0.4161 0.3492 0.3359 0.0298  -0.0914 -0.0354 27  SER A C   
223  C C   B SER A 26  ? 0.4194 0.3505 0.3379 0.0305  -0.0921 -0.0350 27  SER A C   
224  C C   C SER A 26  ? 0.4158 0.3464 0.3340 0.0306  -0.0921 -0.0349 27  SER A C   
225  O O   A SER A 26  ? 0.4246 0.3553 0.3366 0.0349  -0.1032 -0.0372 27  SER A O   
226  O O   B SER A 26  ? 0.4349 0.3592 0.3427 0.0374  -0.1053 -0.0360 27  SER A O   
227  O O   C SER A 26  ? 0.4311 0.3540 0.3379 0.0376  -0.1054 -0.0356 27  SER A O   
228  C CB  A SER A 26  ? 0.4374 0.3288 0.3234 0.0211  -0.0792 -0.0210 27  SER A CB  
229  C CB  B SER A 26  ? 0.4276 0.3155 0.3086 0.0193  -0.0785 -0.0197 27  SER A CB  
230  C CB  C SER A 26  ? 0.4159 0.3048 0.2988 0.0196  -0.0781 -0.0200 27  SER A CB  
231  O OG  A SER A 26  ? 0.5496 0.4225 0.4157 0.0106  -0.0693 -0.0139 27  SER A OG  
232  O OG  B SER A 26  ? 0.4977 0.3897 0.3916 0.0254  -0.0790 -0.0228 27  SER A OG  
233  O OG  C SER A 26  ? 0.5178 0.3825 0.3784 0.0284  -0.0916 -0.0174 27  SER A OG  
234  N N   . ARG A 27  ? 0.3548 0.3071 0.2989 0.0331  -0.0888 -0.0421 28  ARG A N   
235  C CA  . ARG A 27  ? 0.3611 0.3336 0.3269 0.0440  -0.0993 -0.0531 28  ARG A CA  
236  C C   . ARG A 27  ? 0.3751 0.3786 0.3640 0.0385  -0.0957 -0.0628 28  ARG A C   
237  O O   . ARG A 27  ? 0.3724 0.3985 0.3835 0.0455  -0.1027 -0.0746 28  ARG A O   
238  C CB  . ARG A 27  ? 0.3828 0.3581 0.3613 0.0496  -0.0971 -0.0567 28  ARG A CB  
239  C CG  . ARG A 27  ? 0.5325 0.4744 0.4865 0.0546  -0.1007 -0.0481 28  ARG A CG  
240  C CD  . ARG A 27  ? 0.5972 0.5411 0.5629 0.0579  -0.0962 -0.0518 28  ARG A CD  
241  N NE  . ARG A 27  ? 0.7979 0.7555 0.7831 0.0723  -0.1073 -0.0629 28  ARG A NE  
242  C CZ  . ARG A 27  ? 0.9964 0.9747 1.0064 0.0740  -0.1021 -0.0727 28  ARG A CZ  
243  N NH1 . ARG A 27  ? 0.8634 0.8557 0.8930 0.0878  -0.1124 -0.0844 28  ARG A NH1 
244  N NH2 . ARG A 27  ? 0.8104 0.7962 0.8257 0.0621  -0.0869 -0.0717 28  ARG A NH2 
245  N N   . ASP A 28  ? 0.3101 0.3141 0.2935 0.0259  -0.0848 -0.0588 29  ASP A N   
246  C CA  . ASP A 28  ? 0.3012 0.3283 0.3010 0.0177  -0.0786 -0.0665 29  ASP A CA  
247  C C   . ASP A 28  ? 0.3383 0.3886 0.3637 0.0153  -0.0702 -0.0756 29  ASP A C   
248  O O   . ASP A 28  ? 0.3333 0.4076 0.3785 0.0132  -0.0701 -0.0876 29  ASP A O   
249  C CB  . ASP A 28  ? 0.3385 0.3758 0.3407 0.0220  -0.0916 -0.0742 29  ASP A CB  
250  C CG  . ASP A 28  ? 0.4132 0.4664 0.4239 0.0102  -0.0836 -0.0802 29  ASP A CG  
251  O OD1 . ASP A 28  ? 0.3994 0.4432 0.4014 -0.0005 -0.0700 -0.0735 29  ASP A OD1 
252  O OD2 . ASP A 28  ? 0.4597 0.5344 0.4857 0.0119  -0.0910 -0.0922 29  ASP A OD2 
253  N N   . ILE A 29  ? 0.2703 0.3135 0.2944 0.0147  -0.0629 -0.0709 30  ILE A N   
254  C CA  . ILE A 29  ? 0.2486 0.3103 0.2925 0.0117  -0.0544 -0.0788 30  ILE A CA  
255  C C   . ILE A 29  ? 0.2882 0.3506 0.3293 -0.0014 -0.0392 -0.0751 30  ILE A C   
256  O O   . ILE A 29  ? 0.2610 0.3063 0.2861 -0.0048 -0.0338 -0.0641 30  ILE A O   
257  C CB  . ILE A 29  ? 0.2806 0.3355 0.3253 0.0189  -0.0558 -0.0777 30  ILE A CB  
258  C CG1 . ILE A 29  ? 0.2989 0.3524 0.3478 0.0341  -0.0717 -0.0831 30  ILE A CG1 
259  C CG2 . ILE A 29  ? 0.2586 0.3307 0.3199 0.0133  -0.0445 -0.0853 30  ILE A CG2 
260  C CD1 . ILE A 29  ? 0.3269 0.3635 0.3686 0.0412  -0.0734 -0.0792 30  ILE A CD1 
261  N N   A LEU A 30  ? 0.2448 0.3266 0.3012 -0.0087 -0.0321 -0.0851 31  LEU A N   
262  N N   B LEU A 30  ? 0.2550 0.3369 0.3115 -0.0087 -0.0321 -0.0851 31  LEU A N   
263  C CA  A LEU A 30  ? 0.2372 0.3177 0.2896 -0.0212 -0.0174 -0.0828 31  LEU A CA  
264  C CA  B LEU A 30  ? 0.2534 0.3345 0.3063 -0.0212 -0.0175 -0.0832 31  LEU A CA  
265  C C   A LEU A 30  ? 0.2701 0.3342 0.3051 -0.0265 -0.0140 -0.0733 31  LEU A C   
266  C C   B LEU A 30  ? 0.2799 0.3443 0.3152 -0.0265 -0.0140 -0.0734 31  LEU A C   
267  O O   A LEU A 30  ? 0.2539 0.3098 0.2807 -0.0340 -0.0033 -0.0681 31  LEU A O   
268  O O   B LEU A 30  ? 0.2654 0.3216 0.2924 -0.0340 -0.0033 -0.0683 31  LEU A O   
269  C CB  A LEU A 30  ? 0.2370 0.3124 0.2857 -0.0230 -0.0095 -0.0784 31  LEU A CB  
270  C CB  B LEU A 30  ? 0.2587 0.3357 0.3087 -0.0234 -0.0092 -0.0795 31  LEU A CB  
271  C CG  A LEU A 30  ? 0.2880 0.3811 0.3541 -0.0223 -0.0070 -0.0900 31  LEU A CG  
272  C CG  B LEU A 30  ? 0.3225 0.4185 0.3887 -0.0291 -0.0012 -0.0918 31  LEU A CG  
273  C CD1 A LEU A 30  ? 0.2680 0.3562 0.3265 -0.0300 0.0050  -0.0864 31  LEU A CD1 
274  C CD1 B LEU A 30  ? 0.3267 0.4306 0.4041 -0.0209 -0.0057 -0.0975 31  LEU A CD1 
275  C CD2 A LEU A 30  ? 0.3170 0.4336 0.4031 -0.0268 -0.0051 -0.1055 31  LEU A CD2 
276  C CD2 B LEU A 30  ? 0.3396 0.4278 0.3945 -0.0407 0.0130  -0.0876 31  LEU A CD2 
277  N N   . THR A 31  ? 0.2384 0.2977 0.2676 -0.0227 -0.0231 -0.0720 32  THR A N   
278  C CA  . THR A 31  ? 0.2392 0.2850 0.2539 -0.0283 -0.0194 -0.0656 32  THR A CA  
279  C C   . THR A 31  ? 0.3062 0.3633 0.3293 -0.0387 -0.0108 -0.0744 32  THR A C   
280  O O   . THR A 31  ? 0.3022 0.3797 0.3424 -0.0399 -0.0127 -0.0867 32  THR A O   
281  C CB  . THR A 31  ? 0.3228 0.3614 0.3280 -0.0229 -0.0310 -0.0640 32  THR A CB  
282  O OG1 . THR A 31  ? 0.3385 0.3950 0.3578 -0.0183 -0.0412 -0.0752 32  THR A OG1 
283  C CG2 . THR A 31  ? 0.3038 0.3249 0.2949 -0.0155 -0.0367 -0.0543 32  THR A CG2 
284  N N   . ASP A 32  ? 0.2686 0.3127 0.2806 -0.0465 -0.0002 -0.0689 33  ASP A N   
285  C CA  . ASP A 32  ? 0.2694 0.3178 0.2848 -0.0579 0.0107  -0.0758 33  ASP A CA  
286  C C   . ASP A 32  ? 0.3018 0.3376 0.3058 -0.0640 0.0150  -0.0740 33  ASP A C   
287  O O   . ASP A 32  ? 0.3077 0.3400 0.3095 -0.0744 0.0259  -0.0778 33  ASP A O   
288  C CB  . ASP A 32  ? 0.2832 0.3249 0.2945 -0.0623 0.0220  -0.0719 33  ASP A CB  
289  C CG  . ASP A 32  ? 0.3740 0.3954 0.3694 -0.0576 0.0237  -0.0579 33  ASP A CG  
290  O OD1 . ASP A 32  ? 0.3228 0.3343 0.3103 -0.0531 0.0190  -0.0517 33  ASP A OD1 
291  O OD2 . ASP A 32  ? 0.4545 0.4710 0.4453 -0.0585 0.0293  -0.0539 33  ASP A OD2 
292  N N   . VAL A 33  ? 0.2548 0.2818 0.2497 -0.0585 0.0074  -0.0684 34  VAL A N   
293  C CA  . VAL A 33  ? 0.2533 0.2687 0.2373 -0.0642 0.0114  -0.0678 34  VAL A CA  
294  C C   . VAL A 33  ? 0.2993 0.3130 0.2765 -0.0590 0.0000  -0.0669 34  VAL A C   
295  O O   . VAL A 33  ? 0.2977 0.3096 0.2723 -0.0502 -0.0088 -0.0618 34  VAL A O   
296  C CB  . VAL A 33  ? 0.3022 0.2956 0.2725 -0.0655 0.0221  -0.0577 34  VAL A CB  
297  C CG1 . VAL A 33  ? 0.2883 0.2721 0.2510 -0.0566 0.0176  -0.0474 34  VAL A CG1 
298  C CG2 . VAL A 33  ? 0.3102 0.2916 0.2717 -0.0735 0.0299  -0.0600 34  VAL A CG2 
299  N N   A VAL A 34  ? 0.2651 0.2771 0.2371 -0.0653 0.0008  -0.0720 35  VAL A N   
300  N N   B VAL A 34  ? 0.2703 0.2824 0.2424 -0.0652 0.0006  -0.0720 35  VAL A N   
301  C CA  A VAL A 34  ? 0.2652 0.2711 0.2250 -0.0629 -0.0080 -0.0709 35  VAL A CA  
302  C CA  B VAL A 34  ? 0.2737 0.2794 0.2334 -0.0623 -0.0084 -0.0705 35  VAL A CA  
303  C C   A VAL A 34  ? 0.3237 0.3098 0.2690 -0.0682 0.0025  -0.0658 35  VAL A C   
304  C C   B VAL A 34  ? 0.3299 0.3166 0.2750 -0.0682 0.0017  -0.0663 35  VAL A C   
305  O O   A VAL A 34  ? 0.3249 0.3076 0.2712 -0.0764 0.0132  -0.0695 35  VAL A O   
306  O O   B VAL A 34  ? 0.3333 0.3176 0.2795 -0.0768 0.0117  -0.0709 35  VAL A O   
307  C CB  A VAL A 34  ? 0.3136 0.3362 0.2794 -0.0659 -0.0172 -0.0831 35  VAL A CB  
308  C CB  B VAL A 34  ? 0.3275 0.3500 0.2927 -0.0618 -0.0212 -0.0811 35  VAL A CB  
309  C CG1 A VAL A 34  ? 0.3241 0.3369 0.2720 -0.0637 -0.0268 -0.0811 35  VAL A CG1 
310  C CG1 B VAL A 34  ? 0.3329 0.3651 0.3042 -0.0735 -0.0151 -0.0927 35  VAL A CG1 
311  C CG2 A VAL A 34  ? 0.3050 0.3503 0.2895 -0.0595 -0.0274 -0.0905 35  VAL A CG2 
312  C CG2 B VAL A 34  ? 0.3380 0.3489 0.2847 -0.0566 -0.0325 -0.0765 35  VAL A CG2 
313  N N   . ILE A 35  ? 0.2833 0.2558 0.2151 -0.0639 0.0004  -0.0580 36  ILE A N   
314  C CA  . ILE A 35  ? 0.2901 0.2458 0.2094 -0.0680 0.0097  -0.0548 36  ILE A CA  
315  C C   . ILE A 35  ? 0.3612 0.3141 0.2674 -0.0715 0.0033  -0.0592 36  ILE A C   
316  O O   . ILE A 35  ? 0.3466 0.2981 0.2437 -0.0669 -0.0074 -0.0567 36  ILE A O   
317  C CB  . ILE A 35  ? 0.3138 0.2585 0.2283 -0.0624 0.0135  -0.0454 36  ILE A CB  
318  C CG1 . ILE A 35  ? 0.2953 0.2442 0.2214 -0.0578 0.0169  -0.0409 36  ILE A CG1 
319  C CG2 . ILE A 35  ? 0.3408 0.2712 0.2458 -0.0660 0.0234  -0.0445 36  ILE A CG2 
320  C CD1 . ILE A 35  ? 0.2971 0.2445 0.2290 -0.0623 0.0267  -0.0433 36  ILE A CD1 
321  N N   . VAL A 36  ? 0.3307 0.2802 0.2332 -0.0801 0.0101  -0.0656 37  VAL A N   
322  C CA  . VAL A 36  ? 0.3472 0.2943 0.2358 -0.0852 0.0048  -0.0711 37  VAL A CA  
323  C C   . VAL A 36  ? 0.4107 0.3385 0.2833 -0.0883 0.0140  -0.0675 37  VAL A C   
324  O O   . VAL A 36  ? 0.3955 0.3147 0.2710 -0.0914 0.0272  -0.0675 37  VAL A O   
325  C CB  . VAL A 36  ? 0.4019 0.3606 0.2975 -0.0943 0.0058  -0.0832 37  VAL A CB  
326  C CG1 . VAL A 36  ? 0.4202 0.3769 0.3000 -0.0999 -0.0004 -0.0895 37  VAL A CG1 
327  C CG2 . VAL A 36  ? 0.3995 0.3810 0.3140 -0.0916 -0.0027 -0.0891 37  VAL A CG2 
328  N N   . VAL A 37  ? 0.3763 0.2960 0.2311 -0.0873 0.0073  -0.0648 38  VAL A N   
329  C CA  . VAL A 37  ? 0.3877 0.2904 0.2265 -0.0912 0.0164  -0.0627 38  VAL A CA  
330  C C   . VAL A 37  ? 0.4609 0.3583 0.2784 -0.0976 0.0097  -0.0678 38  VAL A C   
331  O O   . VAL A 37  ? 0.4361 0.3306 0.2392 -0.0944 -0.0027 -0.0646 38  VAL A O   
332  C CB  . VAL A 37  ? 0.4332 0.3289 0.2687 -0.0854 0.0175  -0.0539 38  VAL A CB  
333  C CG1 . VAL A 37  ? 0.4410 0.3232 0.2663 -0.0902 0.0302  -0.0542 38  VAL A CG1 
334  C CG2 . VAL A 37  ? 0.4074 0.3121 0.2637 -0.0779 0.0193  -0.0492 38  VAL A CG2 
335  N N   A SER A 38  ? 0.4580 0.3490 0.2684 -0.1067 0.0189  -0.0747 39  SER A N   
336  N N   B SER A 38  ? 0.4170 0.3170 0.2364 -0.1056 0.0150  -0.0766 39  SER A N   
337  C CA  A SER A 38  ? 0.4885 0.3730 0.2754 -0.1142 0.0133  -0.0801 39  SER A CA  
338  C CA  B SER A 38  ? 0.4275 0.3267 0.2311 -0.1137 0.0099  -0.0849 39  SER A CA  
339  C C   A SER A 38  ? 0.5450 0.4405 0.3266 -0.1100 -0.0073 -0.0813 39  SER A C   
340  C C   B SER A 38  ? 0.4548 0.3692 0.2588 -0.1092 -0.0098 -0.0872 39  SER A C   
341  O O   A SER A 38  ? 0.5531 0.4382 0.3105 -0.1092 -0.0172 -0.0782 39  SER A O   
342  O O   B SER A 38  ? 0.4301 0.3626 0.2555 -0.1075 -0.0129 -0.0920 39  SER A O   
343  C CB  A SER A 38  ? 0.5712 0.4367 0.3350 -0.1174 0.0194  -0.0762 39  SER A CB  
344  C CB  B SER A 38  ? 0.4979 0.3780 0.2757 -0.1194 0.0155  -0.0839 39  SER A CB  
345  O OG  A SER A 38  ? 0.7099 0.5671 0.4774 -0.1223 0.0376  -0.0792 39  SER A OG  
346  O OG  B SER A 38  ? 0.5625 0.4338 0.3463 -0.1234 0.0338  -0.0857 39  SER A OG  
347  N N   A ARG A 39  ? 0.4866 0.4025 0.2908 -0.1068 -0.0134 -0.0859 40  ARG A N   
348  N N   B ARG A 39  ? 0.4266 0.3332 0.2077 -0.1066 -0.0230 -0.0841 40  ARG A N   
349  C CA  A ARG A 39  ? 0.4910 0.4238 0.2993 -0.1009 -0.0328 -0.0896 40  ARG A CA  
350  C CA  B ARG A 39  ? 0.4303 0.3513 0.2131 -0.0994 -0.0435 -0.0867 40  ARG A CA  
351  C C   A ARG A 39  ? 0.5233 0.4515 0.3256 -0.0885 -0.0457 -0.0798 40  ARG A C   
352  C C   B ARG A 39  ? 0.4851 0.4142 0.2856 -0.0870 -0.0496 -0.0798 40  ARG A C   
353  O O   A ARG A 39  ? 0.5299 0.4610 0.3217 -0.0824 -0.0639 -0.0807 40  ARG A O   
354  O O   B ARG A 39  ? 0.4700 0.4213 0.2944 -0.0828 -0.0559 -0.0856 40  ARG A O   
355  C CB  A ARG A 39  ? 0.5261 0.4617 0.3176 -0.1073 -0.0428 -0.0988 40  ARG A CB  
356  C CB  B ARG A 39  ? 0.4591 0.3667 0.2081 -0.0997 -0.0576 -0.0859 40  ARG A CB  
357  C CG  A ARG A 39  ? 0.6613 0.6076 0.4638 -0.1193 -0.0335 -0.1116 40  ARG A CG  
358  C CG  B ARG A 39  ? 0.5469 0.4538 0.2821 -0.1121 -0.0549 -0.0961 40  ARG A CG  
359  C CD  A ARG A 39  ? 0.7321 0.6915 0.5258 -0.1229 -0.0490 -0.1225 40  ARG A CD  
360  C CD  B ARG A 39  ? 0.5637 0.4596 0.2646 -0.1120 -0.0718 -0.0963 40  ARG A CD  
361  N NE  A ARG A 39  ? 0.8113 0.7759 0.6080 -0.1373 -0.0387 -0.1353 40  ARG A NE  
362  N NE  B ARG A 39  ? 0.5704 0.4649 0.2567 -0.1251 -0.0678 -0.1065 40  ARG A NE  
363  C CZ  A ARG A 39  ? 0.9666 0.9137 0.7410 -0.1475 -0.0300 -0.1378 40  ARG A CZ  
364  C CZ  B ARG A 39  ? 0.7619 0.6773 0.4558 -0.1282 -0.0782 -0.1189 40  ARG A CZ  
365  N NH1 A ARG A 39  ? 0.7986 0.7225 0.5461 -0.1458 -0.0292 -0.1285 40  ARG A NH1 
366  N NH1 B ARG A 39  ? 0.5867 0.5283 0.3053 -0.1189 -0.0931 -0.1236 40  ARG A NH1 
367  N NH2 A ARG A 39  ? 0.7833 0.7351 0.5615 -0.1608 -0.0205 -0.1504 40  ARG A NH2 
368  N NH2 B ARG A 39  ? 0.6787 0.5904 0.3569 -0.1413 -0.0733 -0.1282 40  ARG A NH2 
369  N N   A GLU A 40  ? 0.4327 0.3529 0.2410 -0.0846 -0.0366 -0.0710 41  GLU A N   
370  N N   B GLU A 40  ? 0.4196 0.3318 0.2110 -0.0831 -0.0447 -0.0691 41  GLU A N   
371  C CA  A GLU A 40  ? 0.4271 0.3427 0.2333 -0.0741 -0.0452 -0.0623 41  GLU A CA  
372  C CA  B GLU A 40  ? 0.3982 0.3135 0.2013 -0.0723 -0.0496 -0.0620 41  GLU A CA  
373  C C   A GLU A 40  ? 0.4351 0.3664 0.2712 -0.0697 -0.0394 -0.0620 41  GLU A C   
374  C C   B GLU A 40  ? 0.4079 0.3416 0.2433 -0.0702 -0.0421 -0.0641 41  GLU A C   
375  O O   A GLU A 40  ? 0.4014 0.3329 0.2484 -0.0747 -0.0244 -0.0623 41  GLU A O   
376  O O   B GLU A 40  ? 0.3613 0.2975 0.2071 -0.0771 -0.0281 -0.0672 41  GLU A O   
377  C CB  A GLU A 40  ? 0.4584 0.3495 0.2420 -0.0759 -0.0380 -0.0533 41  GLU A CB  
378  C CB  B GLU A 40  ? 0.4239 0.3164 0.2089 -0.0718 -0.0433 -0.0517 41  GLU A CB  
379  C CG  A GLU A 40  ? 0.6307 0.5030 0.3798 -0.0812 -0.0436 -0.0532 41  GLU A CG  
380  C CG  B GLU A 40  ? 0.6270 0.4970 0.3767 -0.0785 -0.0441 -0.0501 41  GLU A CG  
381  C CD  A GLU A 40  ? 1.0743 0.9284 0.7981 -0.0748 -0.0565 -0.0453 41  GLU A CD  
382  C CD  B GLU A 40  ? 1.0983 0.9500 0.8196 -0.0727 -0.0593 -0.0438 41  GLU A CD  
383  O OE1 A GLU A 40  ? 1.1282 0.9590 0.8270 -0.0804 -0.0492 -0.0398 41  GLU A OE1 
384  O OE1 B GLU A 40  ? 1.1062 0.9669 0.8330 -0.0623 -0.0765 -0.0444 41  GLU A OE1 
385  O OE2 A GLU A 40  ? 1.0576 0.9196 0.7861 -0.0643 -0.0736 -0.0453 41  GLU A OE2 
386  O OE2 B GLU A 40  ? 1.1354 0.9627 0.8277 -0.0788 -0.0537 -0.0388 41  GLU A OE2 
387  N N   . GLN A 41  ? 0.3779 0.3219 0.2266 -0.0603 -0.0515 -0.0623 42  GLN A N   
388  C CA  . GLN A 41  ? 0.3579 0.3186 0.2341 -0.0575 -0.0464 -0.0640 42  GLN A CA  
389  C C   . GLN A 41  ? 0.3927 0.3468 0.2704 -0.0493 -0.0473 -0.0551 42  GLN A C   
390  O O   . GLN A 41  ? 0.4080 0.3535 0.2727 -0.0421 -0.0592 -0.0512 42  GLN A O   
391  C CB  . GLN A 41  ? 0.3800 0.3655 0.2745 -0.0546 -0.0576 -0.0749 42  GLN A CB  
392  C CG  . GLN A 41  ? 0.5496 0.5454 0.4473 -0.0651 -0.0543 -0.0859 42  GLN A CG  
393  C CD  . GLN A 41  ? 0.7678 0.7929 0.6890 -0.0646 -0.0621 -0.0992 42  GLN A CD  
394  O OE1 . GLN A 41  ? 0.6660 0.7058 0.6046 -0.0562 -0.0689 -0.1011 42  GLN A OE1 
395  N NE2 . GLN A 41  ? 0.8201 0.8552 0.7433 -0.0746 -0.0604 -0.1102 42  GLN A NE2 
396  N N   . PHE A 42  ? 0.3174 0.2740 0.2090 -0.0504 -0.0350 -0.0521 43  PHE A N   
397  C CA  . PHE A 42  ? 0.3164 0.2688 0.2111 -0.0438 -0.0345 -0.0448 43  PHE A CA  
398  C C   . PHE A 42  ? 0.3556 0.3248 0.2738 -0.0418 -0.0311 -0.0477 43  PHE A C   
399  O O   . PHE A 42  ? 0.3503 0.3229 0.2769 -0.0475 -0.0198 -0.0492 43  PHE A O   
400  C CB  . PHE A 42  ? 0.3405 0.2773 0.2253 -0.0476 -0.0225 -0.0377 43  PHE A CB  
401  C CG  . PHE A 42  ? 0.3744 0.2935 0.2347 -0.0520 -0.0226 -0.0358 43  PHE A CG  
402  C CD1 . PHE A 42  ? 0.4057 0.3214 0.2593 -0.0599 -0.0161 -0.0400 43  PHE A CD1 
403  C CD2 . PHE A 42  ? 0.4140 0.3177 0.2559 -0.0495 -0.0281 -0.0302 43  PHE A CD2 
404  C CE1 . PHE A 42  ? 0.4459 0.3450 0.2752 -0.0652 -0.0152 -0.0391 43  PHE A CE1 
405  C CE2 . PHE A 42  ? 0.4655 0.3506 0.2812 -0.0554 -0.0268 -0.0287 43  PHE A CE2 
406  C CZ  . PHE A 42  ? 0.4437 0.3275 0.2535 -0.0633 -0.0204 -0.0333 43  PHE A CZ  
407  N N   . ARG A 43  ? 0.3043 0.2818 0.2313 -0.0338 -0.0402 -0.0484 44  ARG A N   
408  C CA  . ARG A 43  ? 0.2780 0.2717 0.2263 -0.0325 -0.0364 -0.0521 44  ARG A CA  
409  C C   . ARG A 43  ? 0.3236 0.3086 0.2709 -0.0310 -0.0288 -0.0438 44  ARG A C   
410  O O   . ARG A 43  ? 0.3107 0.2822 0.2455 -0.0275 -0.0316 -0.0372 44  ARG A O   
411  C CB  . ARG A 43  ? 0.2969 0.3060 0.2579 -0.0242 -0.0493 -0.0591 44  ARG A CB  
412  C CG  . ARG A 43  ? 0.3916 0.4155 0.3582 -0.0249 -0.0586 -0.0699 44  ARG A CG  
413  C CD  . ARG A 43  ? 0.4806 0.5299 0.4715 -0.0190 -0.0662 -0.0813 44  ARG A CD  
414  N NE  . ARG A 43  ? 0.5995 0.6593 0.6072 -0.0240 -0.0533 -0.0837 44  ARG A NE  
415  C CZ  . ARG A 43  ? 0.7425 0.8157 0.7626 -0.0345 -0.0425 -0.0918 44  ARG A CZ  
416  N NH1 . ARG A 43  ? 0.6268 0.7089 0.6488 -0.0413 -0.0434 -0.1002 44  ARG A NH1 
417  N NH2 . ARG A 43  ? 0.5299 0.6071 0.5592 -0.0391 -0.0308 -0.0922 44  ARG A NH2 
418  N N   . ALA A 44  ? 0.2744 0.2661 0.2328 -0.0344 -0.0189 -0.0443 45  ALA A N   
419  C CA  . ALA A 44  ? 0.2715 0.2569 0.2289 -0.0327 -0.0129 -0.0370 45  ALA A CA  
420  C C   . ALA A 44  ? 0.2753 0.2710 0.2453 -0.0345 -0.0065 -0.0395 45  ALA A C   
421  O O   . ALA A 44  ? 0.2567 0.2639 0.2364 -0.0382 -0.0053 -0.0472 45  ALA A O   
422  C CB  . ALA A 44  ? 0.2949 0.2670 0.2415 -0.0362 -0.0048 -0.0313 45  ALA A CB  
423  N N   . HIS A 45  ? 0.2353 0.2269 0.2042 -0.0328 -0.0020 -0.0336 46  HIS A N   
424  C CA  . HIS A 45  ? 0.2251 0.2219 0.2002 -0.0351 0.0048  -0.0341 46  HIS A CA  
425  C C   . HIS A 45  ? 0.2744 0.2596 0.2412 -0.0381 0.0135  -0.0289 46  HIS A C   
426  O O   . HIS A 45  ? 0.2627 0.2398 0.2233 -0.0351 0.0139  -0.0229 46  HIS A O   
427  C CB  . HIS A 45  ? 0.2151 0.2146 0.1927 -0.0304 0.0025  -0.0314 46  HIS A CB  
428  C CG  . HIS A 45  ? 0.2476 0.2542 0.2317 -0.0254 -0.0063 -0.0360 46  HIS A CG  
429  N ND1 . HIS A 45  ? 0.2737 0.2716 0.2503 -0.0207 -0.0132 -0.0325 46  HIS A ND1 
430  C CD2 . HIS A 45  ? 0.2467 0.2669 0.2433 -0.0244 -0.0090 -0.0443 46  HIS A CD2 
431  C CE1 . HIS A 45  ? 0.2574 0.2613 0.2407 -0.0155 -0.0210 -0.0377 46  HIS A CE1 
432  N NE2 . HIS A 45  ? 0.2475 0.2670 0.2451 -0.0169 -0.0189 -0.0455 46  HIS A NE2 
433  N N   . LYS A 46  ? 0.2506 0.2347 0.2174 -0.0442 0.0206  -0.0319 47  LYS A N   
434  C CA  . LYS A 46  ? 0.2478 0.2171 0.2048 -0.0460 0.0287  -0.0268 47  LYS A CA  
435  C C   . LYS A 46  ? 0.2872 0.2514 0.2399 -0.0397 0.0286  -0.0190 47  LYS A C   
436  O O   . LYS A 46  ? 0.2664 0.2212 0.2138 -0.0362 0.0300  -0.0144 47  LYS A O   
437  C CB  . LYS A 46  ? 0.2760 0.2418 0.2306 -0.0541 0.0372  -0.0308 47  LYS A CB  
438  C CG  . LYS A 46  ? 0.2654 0.2355 0.2238 -0.0617 0.0390  -0.0396 47  LYS A CG  
439  C CD  . LYS A 46  ? 0.2807 0.2479 0.2368 -0.0722 0.0493  -0.0451 47  LYS A CD  
440  C CE  . LYS A 46  ? 0.3257 0.3027 0.2892 -0.0808 0.0506  -0.0564 47  LYS A CE  
441  N NZ  . LYS A 46  ? 0.3549 0.3300 0.3167 -0.0934 0.0623  -0.0636 47  LYS A NZ  
442  N N   . THR A 47  ? 0.2525 0.2245 0.2086 -0.0381 0.0264  -0.0186 48  THR A N   
443  C CA  . THR A 47  ? 0.2440 0.2126 0.1956 -0.0327 0.0256  -0.0121 48  THR A CA  
444  C C   . THR A 47  ? 0.2606 0.2311 0.2146 -0.0272 0.0210  -0.0093 48  THR A C   
445  O O   . THR A 47  ? 0.2481 0.2145 0.1990 -0.0228 0.0215  -0.0050 48  THR A O   
446  C CB  . THR A 47  ? 0.3189 0.2949 0.2719 -0.0334 0.0250  -0.0130 48  THR A CB  
447  O OG1 . THR A 47  ? 0.3174 0.3056 0.2808 -0.0331 0.0200  -0.0183 48  THR A OG1 
448  C CG2 . THR A 47  ? 0.3516 0.3221 0.2979 -0.0403 0.0325  -0.0150 48  THR A CG2 
449  N N   . VAL A 48  ? 0.2225 0.1986 0.1812 -0.0275 0.0164  -0.0124 49  VAL A N   
450  C CA  . VAL A 48  ? 0.2241 0.1998 0.1824 -0.0248 0.0138  -0.0106 49  VAL A CA  
451  C C   . VAL A 48  ? 0.2568 0.2244 0.2111 -0.0251 0.0177  -0.0097 49  VAL A C   
452  O O   . VAL A 48  ? 0.2347 0.2020 0.1897 -0.0224 0.0191  -0.0080 49  VAL A O   
453  C CB  . VAL A 48  ? 0.2535 0.2311 0.2123 -0.0253 0.0080  -0.0133 49  VAL A CB  
454  C CG1 . VAL A 48  ? 0.2543 0.2270 0.2082 -0.0253 0.0076  -0.0117 49  VAL A CG1 
455  C CG2 . VAL A 48  ? 0.2445 0.2294 0.2082 -0.0238 0.0046  -0.0149 49  VAL A CG2 
456  N N   . LEU A 49  ? 0.2279 0.1905 0.1796 -0.0289 0.0198  -0.0123 50  LEU A N   
457  C CA  . LEU A 49  ? 0.2417 0.1954 0.1890 -0.0299 0.0246  -0.0125 50  LEU A CA  
458  C C   . LEU A 49  ? 0.2725 0.2205 0.2194 -0.0253 0.0291  -0.0090 50  LEU A C   
459  O O   . LEU A 49  ? 0.2466 0.1923 0.1944 -0.0219 0.0314  -0.0087 50  LEU A O   
460  C CB  . LEU A 49  ? 0.2471 0.1965 0.1913 -0.0356 0.0267  -0.0168 50  LEU A CB  
461  C CG  . LEU A 49  ? 0.2739 0.2288 0.2179 -0.0388 0.0204  -0.0212 50  LEU A CG  
462  C CD1 . LEU A 49  ? 0.2769 0.2301 0.2193 -0.0450 0.0228  -0.0269 50  LEU A CD1 
463  C CD2 . LEU A 49  ? 0.2907 0.2415 0.2281 -0.0381 0.0177  -0.0202 50  LEU A CD2 
464  N N   . MET A 50  ? 0.2406 0.1859 0.1853 -0.0246 0.0303  -0.0068 51  MET A N   
465  C CA  . MET A 50  ? 0.2475 0.1836 0.1876 -0.0188 0.0328  -0.0024 51  MET A CA  
466  C C   . MET A 50  ? 0.2776 0.2228 0.2234 -0.0113 0.0283  -0.0001 51  MET A C   
467  O O   . MET A 50  ? 0.2758 0.2175 0.2227 -0.0046 0.0290  0.0011  51  MET A O   
468  C CB  . MET A 50  ? 0.2714 0.2001 0.2032 -0.0212 0.0349  -0.0001 51  MET A CB  
469  C CG  . MET A 50  ? 0.3047 0.2246 0.2313 -0.0301 0.0412  -0.0040 51  MET A CG  
470  S SD  . MET A 50  ? 0.3589 0.2760 0.2778 -0.0360 0.0445  -0.0037 51  MET A SD  
471  C CE  . MET A 50  ? 0.3443 0.2352 0.2445 -0.0309 0.0487  0.0040  51  MET A CE  
472  N N   . ALA A 51  ? 0.2505 0.2084 0.2013 -0.0124 0.0237  -0.0007 52  ALA A N   
473  C CA  . ALA A 51  ? 0.2471 0.2160 0.2041 -0.0073 0.0197  -0.0001 52  ALA A CA  
474  C C   . ALA A 51  ? 0.2738 0.2478 0.2379 -0.0062 0.0211  -0.0034 52  ALA A C   
475  O O   . ALA A 51  ? 0.2742 0.2578 0.2454 -0.0013 0.0192  -0.0045 52  ALA A O   
476  C CB  . ALA A 51  ? 0.2492 0.2279 0.2085 -0.0106 0.0159  -0.0012 52  ALA A CB  
477  N N   . CYS A 52  ? 0.2345 0.2031 0.1965 -0.0115 0.0245  -0.0061 53  CYS A N   
478  C CA  . CYS A 52  ? 0.2303 0.2018 0.1958 -0.0133 0.0276  -0.0102 53  CYS A CA  
479  C C   . CYS A 52  ? 0.2814 0.2455 0.2470 -0.0114 0.0332  -0.0123 53  CYS A C   
480  O O   . CYS A 52  ? 0.2713 0.2401 0.2419 -0.0122 0.0369  -0.0169 53  CYS A O   
481  C CB  . CYS A 52  ? 0.2313 0.1999 0.1905 -0.0211 0.0268  -0.0118 53  CYS A CB  
482  S SG  . CYS A 52  ? 0.2696 0.2449 0.2290 -0.0228 0.0210  -0.0109 53  CYS A SG  
483  N N   . SER A 53  ? 0.2573 0.2092 0.2167 -0.0108 0.0351  -0.0103 54  SER A N   
484  C CA  . SER A 53  ? 0.2422 0.1836 0.1993 -0.0106 0.0413  -0.0131 54  SER A CA  
485  C C   . SER A 53  ? 0.3160 0.2447 0.2695 -0.0039 0.0429  -0.0099 54  SER A C   
486  O O   . SER A 53  ? 0.2883 0.2089 0.2338 -0.0060 0.0421  -0.0063 54  SER A O   
487  C CB  . SER A 53  ? 0.2688 0.2034 0.2174 -0.0202 0.0432  -0.0154 54  SER A CB  
488  O OG  . SER A 53  ? 0.3100 0.2312 0.2528 -0.0221 0.0489  -0.0173 54  SER A OG  
489  N N   . GLY A 54  ? 0.2943 0.2196 0.2526 0.0038  0.0459  -0.0120 55  GLY A N   
490  C CA  . GLY A 54  ? 0.3045 0.2122 0.2563 0.0116  0.0473  -0.0087 55  GLY A CA  
491  C C   . GLY A 54  ? 0.3490 0.2373 0.2880 0.0036  0.0538  -0.0090 55  GLY A C   
492  O O   . GLY A 54  ? 0.3553 0.2260 0.2827 0.0049  0.0550  -0.0046 55  GLY A O   
493  N N   . LEU A 55  ? 0.3190 0.2097 0.2582 -0.0059 0.0581  -0.0146 56  LEU A N   
494  C CA  . LEU A 55  ? 0.3246 0.2002 0.2530 -0.0150 0.0638  -0.0169 56  LEU A CA  
495  C C   . LEU A 55  ? 0.3423 0.2189 0.2649 -0.0221 0.0611  -0.0142 56  LEU A C   
496  O O   . LEU A 55  ? 0.3479 0.2086 0.2608 -0.0253 0.0655  -0.0132 56  LEU A O   
497  C CB  . LEU A 55  ? 0.3236 0.2029 0.2521 -0.0235 0.0675  -0.0239 56  LEU A CB  
498  C CG  . LEU A 55  ? 0.3892 0.2545 0.3074 -0.0330 0.0735  -0.0280 56  LEU A CG  
499  C CD1 . LEU A 55  ? 0.4121 0.2559 0.3255 -0.0284 0.0817  -0.0293 56  LEU A CD1 
500  C CD2 . LEU A 55  ? 0.3788 0.2507 0.2945 -0.0422 0.0739  -0.0342 56  LEU A CD2 
501  N N   . PHE A 56  ? 0.2899 0.1842 0.2182 -0.0247 0.0546  -0.0138 57  PHE A N   
502  C CA  . PHE A 56  ? 0.2864 0.1848 0.2124 -0.0307 0.0520  -0.0131 57  PHE A CA  
503  C C   . PHE A 56  ? 0.3393 0.2308 0.2605 -0.0263 0.0519  -0.0075 57  PHE A C   
504  O O   . PHE A 56  ? 0.3223 0.2078 0.2372 -0.0329 0.0550  -0.0080 57  PHE A O   
505  C CB  . PHE A 56  ? 0.2831 0.1993 0.2158 -0.0331 0.0450  -0.0146 57  PHE A CB  
506  C CG  . PHE A 56  ? 0.2909 0.2095 0.2221 -0.0394 0.0445  -0.0200 57  PHE A CG  
507  C CD1 . PHE A 56  ? 0.3165 0.2305 0.2435 -0.0472 0.0474  -0.0250 57  PHE A CD1 
508  C CD2 . PHE A 56  ? 0.3016 0.2264 0.2338 -0.0386 0.0410  -0.0205 57  PHE A CD2 
509  C CE1 . PHE A 56  ? 0.3299 0.2462 0.2536 -0.0527 0.0456  -0.0302 57  PHE A CE1 
510  C CE2 . PHE A 56  ? 0.3334 0.2574 0.2596 -0.0445 0.0398  -0.0247 57  PHE A CE2 
511  C CZ  . PHE A 56  ? 0.3101 0.2302 0.2320 -0.0509 0.0413  -0.0294 57  PHE A CZ  
512  N N   . TYR A 57  ? 0.3102 0.2022 0.2337 -0.0158 0.0487  -0.0029 58  TYR A N   
513  C CA  . TYR A 57  ? 0.3298 0.2120 0.2445 -0.0107 0.0475  0.0032  58  TYR A CA  
514  C C   . TYR A 57  ? 0.3993 0.2543 0.2981 -0.0128 0.0551  0.0047  58  TYR A C   
515  O O   . TYR A 57  ? 0.3881 0.2321 0.2747 -0.0180 0.0579  0.0071  58  TYR A O   
516  C CB  . TYR A 57  ? 0.3502 0.2387 0.2707 0.0022  0.0414  0.0066  58  TYR A CB  
517  C CG  . TYR A 57  ? 0.4037 0.2791 0.3117 0.0094  0.0386  0.0135  58  TYR A CG  
518  C CD1 . TYR A 57  ? 0.4237 0.3037 0.3259 0.0058  0.0357  0.0164  58  TYR A CD1 
519  C CD2 . TYR A 57  ? 0.4706 0.3272 0.3705 0.0201  0.0387  0.0169  58  TYR A CD2 
520  C CE1 . TYR A 57  ? 0.4587 0.3240 0.3449 0.0115  0.0330  0.0232  58  TYR A CE1 
521  C CE2 . TYR A 57  ? 0.5178 0.3585 0.4016 0.0275  0.0348  0.0242  58  TYR A CE2 
522  C CZ  . TYR A 57  ? 0.6061 0.4511 0.4820 0.0226  0.0320  0.0276  58  TYR A CZ  
523  O OH  . TYR A 57  ? 0.7085 0.5353 0.5646 0.0295  0.0281  0.0351  58  TYR A OH  
524  N N   A SER A 58  ? 0.3713 0.2145 0.2695 -0.0097 0.0595  0.0025  59  SER A N   
525  N N   B SER A 58  ? 0.3731 0.2164 0.2714 -0.0096 0.0595  0.0025  59  SER A N   
526  C CA  A SER A 58  ? 0.4001 0.2142 0.2825 -0.0116 0.0676  0.0032  59  SER A CA  
527  C CA  B SER A 58  ? 0.4027 0.2169 0.2852 -0.0116 0.0676  0.0031  59  SER A CA  
528  C C   A SER A 58  ? 0.4596 0.2697 0.3359 -0.0280 0.0749  -0.0020 59  SER A C   
529  C C   B SER A 58  ? 0.4588 0.2694 0.3352 -0.0280 0.0747  -0.0019 59  SER A C   
530  O O   A SER A 58  ? 0.4839 0.2729 0.3440 -0.0334 0.0811  0.0000  59  SER A O   
531  O O   B SER A 58  ? 0.4805 0.2706 0.3407 -0.0334 0.0806  0.0002  59  SER A O   
532  C CB  A SER A 58  ? 0.4334 0.2394 0.3199 -0.0050 0.0709  -0.0002 59  SER A CB  
533  C CB  B SER A 58  ? 0.4422 0.2487 0.3289 -0.0057 0.0711  -0.0005 59  SER A CB  
534  O OG  A SER A 58  ? 0.4483 0.2554 0.3399 0.0112  0.0649  0.0036  59  SER A OG  
535  O OG  B SER A 58  ? 0.5131 0.2888 0.3835 -0.0078 0.0796  -0.0004 59  SER A OG  
536  N N   . ILE A 59  ? 0.3981 0.2286 0.2866 -0.0359 0.0738  -0.0089 60  ILE A N   
537  C CA  . ILE A 59  ? 0.3833 0.2169 0.2706 -0.0507 0.0786  -0.0160 60  ILE A CA  
538  C C   . ILE A 59  ? 0.4101 0.2486 0.2947 -0.0568 0.0786  -0.0153 60  ILE A C   
539  O O   . ILE A 59  ? 0.4293 0.2545 0.3036 -0.0673 0.0871  -0.0185 60  ILE A O   
540  C CB  . ILE A 59  ? 0.3926 0.2483 0.2927 -0.0552 0.0741  -0.0230 60  ILE A CB  
541  C CG1 . ILE A 59  ? 0.4010 0.2485 0.2999 -0.0538 0.0775  -0.0262 60  ILE A CG1 
542  C CG2 . ILE A 59  ? 0.3743 0.2405 0.2770 -0.0685 0.0755  -0.0313 60  ILE A CG2 
543  C CD1 . ILE A 59  ? 0.4048 0.2713 0.3121 -0.0556 0.0716  -0.0306 60  ILE A CD1 
544  N N   . PHE A 60  ? 0.3421 0.1994 0.2356 -0.0517 0.0705  -0.0124 61  PHE A N   
545  C CA  . PHE A 60  ? 0.3538 0.2187 0.2468 -0.0585 0.0712  -0.0139 61  PHE A CA  
546  C C   . PHE A 60  ? 0.4220 0.2671 0.2978 -0.0564 0.0747  -0.0065 61  PHE A C   
547  O O   . PHE A 60  ? 0.4339 0.2823 0.3063 -0.0642 0.0778  -0.0085 61  PHE A O   
548  C CB  . PHE A 60  ? 0.3411 0.2337 0.2504 -0.0558 0.0619  -0.0159 61  PHE A CB  
549  C CG  . PHE A 60  ? 0.3335 0.2415 0.2548 -0.0586 0.0580  -0.0229 61  PHE A CG  
550  C CD1 . PHE A 60  ? 0.3630 0.2751 0.2867 -0.0694 0.0619  -0.0320 61  PHE A CD1 
551  C CD2 . PHE A 60  ? 0.3389 0.2564 0.2671 -0.0512 0.0504  -0.0209 61  PHE A CD2 
552  C CE1 . PHE A 60  ? 0.3637 0.2891 0.2959 -0.0710 0.0564  -0.0382 61  PHE A CE1 
553  C CE2 . PHE A 60  ? 0.3670 0.2946 0.3009 -0.0539 0.0462  -0.0264 61  PHE A CE2 
554  C CZ  . PHE A 60  ? 0.3355 0.2669 0.2709 -0.0629 0.0482  -0.0346 61  PHE A CZ  
555  N N   . THR A 61  ? 0.4047 0.2278 0.2681 -0.0467 0.0748  0.0011  62  THR A N   
556  C CA  . THR A 61  ? 0.4253 0.2226 0.2660 -0.0446 0.0779  0.0087  62  THR A CA  
557  C C   . THR A 61  ? 0.5255 0.2913 0.3467 -0.0536 0.0900  0.0074  62  THR A C   
558  O O   . THR A 61  ? 0.5360 0.2736 0.3327 -0.0554 0.0951  0.0131  62  THR A O   
559  C CB  . THR A 61  ? 0.5103 0.3013 0.3468 -0.0274 0.0691  0.0178  62  THR A CB  
560  O OG1 . THR A 61  ? 0.4696 0.2562 0.3128 -0.0185 0.0680  0.0173  62  THR A OG1 
561  C CG2 . THR A 61  ? 0.4561 0.2752 0.3069 -0.0216 0.0590  0.0189  62  THR A CG2 
562  N N   . ASP A 62  ? 0.4792 0.2482 0.3090 -0.0607 0.0950  -0.0006 63  ASP A N   
563  C CA  . ASP A 62  ? 0.5060 0.2464 0.3186 -0.0717 0.1076  -0.0038 63  ASP A CA  
564  C C   . ASP A 62  ? 0.5809 0.3258 0.3895 -0.0898 0.1161  -0.0107 63  ASP A C   
565  O O   . ASP A 62  ? 0.5310 0.3083 0.3603 -0.0962 0.1131  -0.0191 63  ASP A O   
566  C CB  . ASP A 62  ? 0.5074 0.2520 0.3307 -0.0744 0.1101  -0.0115 63  ASP A CB  
567  C CG  . ASP A 62  ? 0.6589 0.3758 0.4652 -0.0883 0.1241  -0.0168 63  ASP A CG  
568  O OD1 . ASP A 62  ? 0.7400 0.4216 0.5267 -0.0826 0.1290  -0.0111 63  ASP A OD1 
569  O OD2 . ASP A 62  ? 0.6455 0.3754 0.4576 -0.1049 0.1301  -0.0271 63  ASP A OD2 
570  N N   . GLN A 63  ? 0.6143 0.3258 0.3958 -0.0984 0.1271  -0.0081 64  GLN A N   
571  C CA  . GLN A 63  ? 0.6366 0.3500 0.4120 -0.1174 0.1377  -0.0154 64  GLN A CA  
572  C C   . GLN A 63  ? 0.6834 0.4212 0.4785 -0.1335 0.1437  -0.0314 64  GLN A C   
573  O O   . GLN A 63  ? 0.7004 0.4587 0.5046 -0.1457 0.1477  -0.0402 64  GLN A O   
574  C CB  . GLN A 63  ? 0.7107 0.3773 0.4484 -0.1250 0.1502  -0.0095 64  GLN A CB  
575  C CG  . GLN A 63  ? 0.9226 0.5707 0.6393 -0.1120 0.1433  0.0047  64  GLN A CG  
576  N N   . LEU A 64  ? 0.5957 0.3321 0.3975 -0.1339 0.1445  -0.0363 65  LEU A N   
577  C CA  . LEU A 64  ? 0.5626 0.3246 0.3835 -0.1481 0.1479  -0.0520 65  LEU A CA  
578  C C   . LEU A 64  ? 0.5771 0.3793 0.4269 -0.1389 0.1331  -0.0554 65  LEU A C   
579  O O   . LEU A 64  ? 0.5887 0.4217 0.4575 -0.1473 0.1312  -0.0671 65  LEU A O   
580  C CB  . LEU A 64  ? 0.5826 0.3223 0.3938 -0.1554 0.1569  -0.0570 65  LEU A CB  
581  C CG  . LEU A 64  ? 0.6874 0.3925 0.4734 -0.1733 0.1751  -0.0610 65  LEU A CG  
582  C CD1 . LEU A 64  ? 0.7073 0.3907 0.4851 -0.1785 0.1827  -0.0658 65  LEU A CD1 
583  C CD2 . LEU A 64  ? 0.7387 0.4666 0.5345 -0.1941 0.1836  -0.0756 65  LEU A CD2 
584  N N   . LYS A 65  ? 0.4861 0.2873 0.3388 -0.1223 0.1231  -0.0466 66  LYS A N   
585  C CA  . LYS A 65  ? 0.4399 0.2730 0.3149 -0.1145 0.1102  -0.0493 66  LYS A CA  
586  C C   . LYS A 65  ? 0.4922 0.3507 0.3807 -0.1084 0.1006  -0.0473 66  LYS A C   
587  O O   . LYS A 65  ? 0.4515 0.3374 0.3580 -0.1067 0.0916  -0.0528 66  LYS A O   
588  C CB  . LYS A 65  ? 0.4514 0.2754 0.3249 -0.1011 0.1048  -0.0424 66  LYS A CB  
589  C CG  . LYS A 65  ? 0.4838 0.2866 0.3475 -0.1064 0.1133  -0.0465 66  LYS A CG  
590  C CD  . LYS A 65  ? 0.4457 0.2453 0.3118 -0.0930 0.1079  -0.0415 66  LYS A CD  
591  C CE  . LYS A 65  ? 0.5227 0.2957 0.3768 -0.0960 0.1176  -0.0445 66  LYS A CE  
592  N NZ  . LYS A 65  ? 0.5267 0.2642 0.3621 -0.0900 0.1245  -0.0364 66  LYS A NZ  
593  N N   . CYS A 66  ? 0.4972 0.3449 0.3753 -0.1053 0.1024  -0.0396 67  CYS A N   
594  C CA  . CYS A 66  ? 0.4855 0.3549 0.3746 -0.1003 0.0947  -0.0381 67  CYS A CA  
595  C C   . CYS A 66  ? 0.5345 0.4329 0.4420 -0.1105 0.0946  -0.0514 67  CYS A C   
596  O O   . CYS A 66  ? 0.5271 0.4488 0.4497 -0.1047 0.0857  -0.0527 67  CYS A O   
597  C CB  . CYS A 66  ? 0.5142 0.3641 0.3848 -0.0987 0.0989  -0.0294 67  CYS A CB  
598  S SG  . CYS A 66  ? 0.6034 0.4337 0.4552 -0.1185 0.1161  -0.0355 67  CYS A SG  
599  N N   . ASN A 67  ? 0.4949 0.3914 0.4013 -0.1257 0.1049  -0.0623 68  ASN A N   
600  C CA  . ASN A 67  ? 0.4906 0.4161 0.4162 -0.1368 0.1061  -0.0778 68  ASN A CA  
601  C C   . ASN A 67  ? 0.5091 0.4574 0.4527 -0.1364 0.0976  -0.0874 68  ASN A C   
602  O O   . ASN A 67  ? 0.4884 0.4642 0.4507 -0.1435 0.0962  -0.1015 68  ASN A O   
603  C CB  . ASN A 67  ? 0.5300 0.4429 0.4445 -0.1557 0.1232  -0.0860 68  ASN A CB  
604  C CG  . ASN A 67  ? 0.7030 0.5976 0.5996 -0.1572 0.1304  -0.0783 68  ASN A CG  
605  O OD1 . ASN A 67  ? 0.7241 0.5867 0.5955 -0.1667 0.1435  -0.0749 68  ASN A OD1 
606  N ND2 . ASN A 67  ? 0.5818 0.4932 0.4879 -0.1476 0.1219  -0.0747 68  ASN A ND2 
607  N N   . LEU A 68  ? 0.4689 0.4073 0.4073 -0.1279 0.0915  -0.0807 69  LEU A N   
608  C CA  . LEU A 68  ? 0.4481 0.4048 0.3986 -0.1276 0.0829  -0.0888 69  LEU A CA  
609  C C   . LEU A 68  ? 0.4462 0.4270 0.4120 -0.1153 0.0671  -0.0877 69  LEU A C   
610  O O   . LEU A 68  ? 0.4154 0.3905 0.3778 -0.1043 0.0625  -0.0767 69  LEU A O   
611  C CB  . LEU A 68  ? 0.4631 0.3982 0.4000 -0.1245 0.0839  -0.0827 69  LEU A CB  
612  C CG  . LEU A 68  ? 0.5387 0.4469 0.4594 -0.1361 0.0991  -0.0849 69  LEU A CG  
613  C CD1 . LEU A 68  ? 0.5465 0.4342 0.4556 -0.1300 0.0993  -0.0786 69  LEU A CD1 
614  C CD2 . LEU A 68  ? 0.5500 0.4721 0.4784 -0.1534 0.1053  -0.1018 69  LEU A CD2 
615  N N   . SER A 69  ? 0.3873 0.3935 0.3687 -0.1171 0.0585  -0.0995 70  SER A N   
616  C CA  A SER A 69  ? 0.3632 0.3899 0.3573 -0.1052 0.0423  -0.0998 70  SER A CA  
617  C CA  B SER A 69  ? 0.3699 0.3955 0.3633 -0.1047 0.0424  -0.0990 70  SER A CA  
618  C C   . SER A 69  ? 0.3788 0.3987 0.3641 -0.0986 0.0329  -0.0951 70  SER A C   
619  O O   . SER A 69  ? 0.3268 0.3539 0.3146 -0.0880 0.0199  -0.0918 70  SER A O   
620  C CB  A SER A 69  ? 0.3961 0.4543 0.4119 -0.1094 0.0372  -0.1163 70  SER A CB  
621  C CB  B SER A 69  ? 0.4178 0.4751 0.4334 -0.1078 0.0370  -0.1145 70  SER A CB  
622  O OG  A SER A 69  ? 0.4452 0.5117 0.4700 -0.1161 0.0466  -0.1219 70  SER A OG  
623  O OG  B SER A 69  ? 0.5093 0.5778 0.5301 -0.1177 0.0375  -0.1275 70  SER A OG  
624  N N   . VAL A 70  ? 0.3469 0.3517 0.3204 -0.1061 0.0401  -0.0959 71  VAL A N   
625  C CA  . VAL A 70  ? 0.3425 0.3393 0.3053 -0.1026 0.0337  -0.0929 71  VAL A CA  
626  C C   . VAL A 70  ? 0.3811 0.3498 0.3275 -0.1040 0.0451  -0.0845 71  VAL A C   
627  O O   . VAL A 70  ? 0.3840 0.3404 0.3259 -0.1131 0.0578  -0.0873 71  VAL A O   
628  C CB  . VAL A 70  ? 0.4002 0.4119 0.3671 -0.1106 0.0287  -0.1066 71  VAL A CB  
629  C CG1 . VAL A 70  ? 0.4072 0.4077 0.3588 -0.1084 0.0232  -0.1034 71  VAL A CG1 
630  C CG2 . VAL A 70  ? 0.3941 0.4363 0.3799 -0.1070 0.0156  -0.1164 71  VAL A CG2 
631  N N   . ILE A 71  ? 0.3151 0.2733 0.2527 -0.0952 0.0409  -0.0752 72  ILE A N   
632  C CA  . ILE A 71  ? 0.3154 0.2504 0.2403 -0.0943 0.0500  -0.0688 72  ILE A CA  
633  C C   . ILE A 71  ? 0.3689 0.3008 0.2848 -0.0946 0.0457  -0.0704 72  ILE A C   
634  O O   . ILE A 71  ? 0.3682 0.3070 0.2827 -0.0886 0.0353  -0.0674 72  ILE A O   
635  C CB  . ILE A 71  ? 0.3355 0.2611 0.2594 -0.0843 0.0518  -0.0572 72  ILE A CB  
636  C CG1 . ILE A 71  ? 0.3416 0.2676 0.2702 -0.0850 0.0563  -0.0553 72  ILE A CG1 
637  C CG2 . ILE A 71  ? 0.3540 0.2591 0.2681 -0.0813 0.0596  -0.0523 72  ILE A CG2 
638  C CD1 . ILE A 71  ? 0.4110 0.3208 0.3324 -0.0944 0.0694  -0.0586 72  ILE A CD1 
639  N N   . ASN A 72  ? 0.3556 0.2745 0.2629 -0.1022 0.0545  -0.0752 73  ASN A N   
640  C CA  . ASN A 72  ? 0.3676 0.2816 0.2638 -0.1043 0.0525  -0.0777 73  ASN A CA  
641  C C   . ASN A 72  ? 0.4033 0.2990 0.2922 -0.0991 0.0606  -0.0711 73  ASN A C   
642  O O   . ASN A 72  ? 0.3827 0.2630 0.2703 -0.0999 0.0719  -0.0705 73  ASN A O   
643  C CB  . ASN A 72  ? 0.4074 0.3202 0.2991 -0.1170 0.0573  -0.0894 73  ASN A CB  
644  C CG  . ASN A 72  ? 0.6265 0.5612 0.5285 -0.1229 0.0499  -0.0989 73  ASN A CG  
645  O OD1 . ASN A 72  ? 0.4834 0.4351 0.3889 -0.1187 0.0358  -0.1003 73  ASN A OD1 
646  N ND2 . ASN A 72  ? 0.5831 0.5173 0.4901 -0.1328 0.0593  -0.1065 73  ASN A ND2 
647  N N   . LEU A 73  ? 0.3360 0.2324 0.2195 -0.0941 0.0552  -0.0669 74  LEU A N   
648  C CA  . LEU A 73  ? 0.3359 0.2194 0.2155 -0.0898 0.0632  -0.0631 74  LEU A CA  
649  C C   . LEU A 73  ? 0.3922 0.2639 0.2604 -0.0974 0.0711  -0.0703 74  LEU A C   
650  O O   . LEU A 73  ? 0.4066 0.2812 0.2671 -0.1061 0.0678  -0.0774 74  LEU A O   
651  C CB  . LEU A 73  ? 0.3338 0.2219 0.2120 -0.0834 0.0571  -0.0569 74  LEU A CB  
652  C CG  . LEU A 73  ? 0.3630 0.2619 0.2517 -0.0755 0.0496  -0.0499 74  LEU A CG  
653  C CD1 . LEU A 73  ? 0.3643 0.2634 0.2506 -0.0707 0.0477  -0.0448 74  LEU A CD1 
654  C CD2 . LEU A 73  ? 0.3740 0.2714 0.2735 -0.0713 0.0548  -0.0469 74  LEU A CD2 
655  N N   . ASP A 74  ? 0.3540 0.2136 0.2219 -0.0938 0.0810  -0.0694 75  ASP A N   
656  C CA  . ASP A 74  ? 0.3880 0.2349 0.2463 -0.1001 0.0909  -0.0769 75  ASP A CA  
657  C C   . ASP A 74  ? 0.4520 0.3032 0.2958 -0.1074 0.0852  -0.0806 75  ASP A C   
658  O O   . ASP A 74  ? 0.4357 0.2935 0.2771 -0.1038 0.0781  -0.0754 75  ASP A O   
659  C CB  . ASP A 74  ? 0.4120 0.2500 0.2761 -0.0918 0.1004  -0.0753 75  ASP A CB  
660  C CG  . ASP A 74  ? 0.5094 0.3333 0.3664 -0.0968 0.1125  -0.0841 75  ASP A CG  
661  O OD1 . ASP A 74  ? 0.5126 0.3374 0.3581 -0.1044 0.1134  -0.0892 75  ASP A OD1 
662  O OD2 . ASP A 74  ? 0.5466 0.3566 0.4078 -0.0927 0.1213  -0.0857 75  ASP A OD2 
663  N N   . PRO A 75  ? 0.4622 0.3082 0.2938 -0.1180 0.0876  -0.0893 76  PRO A N   
664  C CA  . PRO A 75  ? 0.4717 0.3195 0.2850 -0.1249 0.0808  -0.0923 76  PRO A CA  
665  C C   . PRO A 75  ? 0.5145 0.3553 0.3177 -0.1244 0.0858  -0.0907 76  PRO A C   
666  O O   . PRO A 75  ? 0.5354 0.3755 0.3206 -0.1290 0.0787  -0.0904 76  PRO A O   
667  C CB  . PRO A 75  ? 0.5117 0.3538 0.3148 -0.1366 0.0853  -0.1032 76  PRO A CB  
668  C CG  . PRO A 75  ? 0.5804 0.4115 0.3945 -0.1359 0.0993  -0.1062 76  PRO A CG  
669  C CD  . PRO A 75  ? 0.4968 0.3332 0.3283 -0.1249 0.0968  -0.0971 76  PRO A CD  
670  N N   . GLU A 76  ? 0.4728 0.3084 0.2868 -0.1190 0.0975  -0.0902 77  GLU A N   
671  C CA  . GLU A 76  ? 0.4939 0.3262 0.3016 -0.1196 0.1040  -0.0908 77  GLU A CA  
672  C C   . GLU A 76  ? 0.4880 0.3291 0.2987 -0.1136 0.0953  -0.0819 77  GLU A C   
673  O O   . GLU A 76  ? 0.4839 0.3224 0.2854 -0.1168 0.0990  -0.0822 77  GLU A O   
674  C CB  . GLU A 76  ? 0.5236 0.3511 0.3456 -0.1146 0.1189  -0.0954 77  GLU A CB  
675  C CG  . GLU A 76  ? 0.7823 0.5970 0.5957 -0.1226 0.1307  -0.1063 77  GLU A CG  
676  C CD  . GLU A 76  ? 1.1889 0.9986 0.9830 -0.1334 0.1371  -0.1132 77  GLU A CD  
677  O OE1 . GLU A 76  ? 1.1858 0.9972 0.9858 -0.1314 0.1463  -0.1160 77  GLU A OE1 
678  O OE2 . GLU A 76  ? 1.1978 1.0024 0.9702 -0.1444 0.1328  -0.1165 77  GLU A OE2 
679  N N   . ILE A 77  ? 0.4229 0.2733 0.2455 -0.1063 0.0850  -0.0748 78  ILE A N   
680  C CA  . ILE A 77  ? 0.4122 0.2700 0.2383 -0.1005 0.0771  -0.0669 78  ILE A CA  
681  C C   . ILE A 77  ? 0.4742 0.3286 0.2785 -0.1057 0.0664  -0.0647 78  ILE A C   
682  O O   . ILE A 77  ? 0.4622 0.3174 0.2581 -0.1083 0.0569  -0.0660 78  ILE A O   
683  C CB  . ILE A 77  ? 0.4215 0.2895 0.2671 -0.0908 0.0711  -0.0609 78  ILE A CB  
684  C CG1 . ILE A 77  ? 0.4271 0.2939 0.2899 -0.0843 0.0813  -0.0619 78  ILE A CG1 
685  C CG2 . ILE A 77  ? 0.3688 0.2439 0.2169 -0.0857 0.0630  -0.0536 78  ILE A CG2 
686  C CD1 . ILE A 77  ? 0.5052 0.3729 0.3758 -0.0803 0.0907  -0.0637 78  ILE A CD1 
687  N N   . ASN A 78  ? 0.4666 0.3167 0.2616 -0.1069 0.0677  -0.0618 79  ASN A N   
688  C CA  . ASN A 78  ? 0.4917 0.3322 0.2611 -0.1114 0.0586  -0.0584 79  ASN A CA  
689  C C   . ASN A 78  ? 0.4800 0.3271 0.2552 -0.1028 0.0441  -0.0505 79  ASN A C   
690  O O   . ASN A 78  ? 0.4482 0.3029 0.2405 -0.0966 0.0459  -0.0466 79  ASN A O   
691  C CB  . ASN A 78  ? 0.5488 0.3795 0.3053 -0.1182 0.0696  -0.0596 79  ASN A CB  
692  C CG  . ASN A 78  ? 0.7315 0.5464 0.4573 -0.1233 0.0619  -0.0548 79  ASN A CG  
693  O OD1 . ASN A 78  ? 0.5889 0.4025 0.3149 -0.1202 0.0589  -0.0490 79  ASN A OD1 
694  N ND2 . ASN A 78  ? 0.6704 0.4708 0.3669 -0.1313 0.0585  -0.0570 79  ASN A ND2 
695  N N   . PRO A 79  ? 0.4506 0.2954 0.2122 -0.1019 0.0293  -0.0489 80  PRO A N   
696  C CA  . PRO A 79  ? 0.4404 0.2918 0.2092 -0.0927 0.0157  -0.0429 80  PRO A CA  
697  C C   . PRO A 79  ? 0.4861 0.3282 0.2467 -0.0909 0.0157  -0.0363 80  PRO A C   
698  O O   . PRO A 79  ? 0.4708 0.3222 0.2485 -0.0833 0.0121  -0.0324 80  PRO A O   
699  C CB  . PRO A 79  ? 0.4875 0.3359 0.2389 -0.0926 0.0002  -0.0443 80  PRO A CB  
700  C CG  . PRO A 79  ? 0.5490 0.3978 0.2959 -0.1010 0.0062  -0.0525 80  PRO A CG  
701  C CD  . PRO A 79  ? 0.5017 0.3397 0.2425 -0.1084 0.0235  -0.0538 80  PRO A CD  
702  N N   . GLU A 80  ? 0.4656 0.2888 0.1994 -0.0993 0.0211  -0.0358 81  GLU A N   
703  C CA  . GLU A 80  ? 0.4688 0.2813 0.1932 -0.0998 0.0230  -0.0305 81  GLU A CA  
704  C C   . GLU A 80  ? 0.4691 0.2966 0.2217 -0.0980 0.0351  -0.0317 81  GLU A C   
705  O O   . GLU A 80  ? 0.4375 0.2689 0.1993 -0.0926 0.0316  -0.0274 81  GLU A O   
706  C CB  . GLU A 80  ? 0.5226 0.3097 0.2099 -0.1114 0.0284  -0.0304 81  GLU A CB  
707  C CG  . GLU A 80  ? 0.6167 0.3894 0.2909 -0.1130 0.0295  -0.0250 81  GLU A CG  
708  C CD  . GLU A 80  ? 0.9522 0.6979 0.5894 -0.1271 0.0389  -0.0253 81  GLU A CD  
709  O OE1 . GLU A 80  ? 0.9649 0.6877 0.5756 -0.1280 0.0329  -0.0189 81  GLU A OE1 
710  O OE2 . GLU A 80  ? 0.8836 0.6294 0.5171 -0.1375 0.0531  -0.0324 81  GLU A OE2 
711  N N   . GLY A 81  ? 0.4467 0.2827 0.2129 -0.1015 0.0482  -0.0381 82  GLY A N   
712  C CA  . GLY A 81  ? 0.4248 0.2765 0.2187 -0.0978 0.0580  -0.0402 82  GLY A CA  
713  C C   . GLY A 81  ? 0.4245 0.2913 0.2421 -0.0864 0.0496  -0.0360 82  GLY A C   
714  O O   . GLY A 81  ? 0.3799 0.2555 0.2118 -0.0820 0.0502  -0.0337 82  GLY A O   
715  N N   . PHE A 82  ? 0.3687 0.2389 0.1896 -0.0826 0.0416  -0.0357 83  PHE A N   
716  C CA  . PHE A 82  ? 0.3392 0.2228 0.1803 -0.0736 0.0347  -0.0326 83  PHE A CA  
717  C C   . PHE A 82  ? 0.3682 0.2510 0.2057 -0.0695 0.0247  -0.0272 83  PHE A C   
718  O O   . PHE A 82  ? 0.3442 0.2369 0.1979 -0.0637 0.0239  -0.0247 83  PHE A O   
719  C CB  . PHE A 82  ? 0.3501 0.2380 0.1948 -0.0728 0.0294  -0.0352 83  PHE A CB  
720  C CG  . PHE A 82  ? 0.3352 0.2364 0.2004 -0.0655 0.0255  -0.0331 83  PHE A CG  
721  C CD1 . PHE A 82  ? 0.3610 0.2678 0.2426 -0.0622 0.0336  -0.0331 83  PHE A CD1 
722  C CD2 . PHE A 82  ? 0.3396 0.2467 0.2066 -0.0614 0.0137  -0.0315 83  PHE A CD2 
723  C CE1 . PHE A 82  ? 0.3568 0.2730 0.2529 -0.0567 0.0307  -0.0307 83  PHE A CE1 
724  C CE2 . PHE A 82  ? 0.3528 0.2721 0.2379 -0.0560 0.0118  -0.0305 83  PHE A CE2 
725  C CZ  . PHE A 82  ? 0.3325 0.2553 0.2304 -0.0545 0.0206  -0.0298 83  PHE A CZ  
726  N N   . CYS A 83  ? 0.3772 0.2468 0.1923 -0.0717 0.0161  -0.0255 84  CYS A N   
727  C CA  . CYS A 83  ? 0.3984 0.2626 0.2067 -0.0668 0.0056  -0.0205 84  CYS A CA  
728  C C   . CYS A 83  ? 0.4181 0.2798 0.2287 -0.0683 0.0129  -0.0181 84  CYS A C   
729  O O   . CYS A 83  ? 0.3847 0.2532 0.2071 -0.0623 0.0086  -0.0155 84  CYS A O   
730  C CB  . CYS A 83  ? 0.4595 0.3045 0.2377 -0.0689 -0.0041 -0.0190 84  CYS A CB  
731  S SG  . CYS A 83  ? 0.5394 0.3730 0.3066 -0.0604 -0.0188 -0.0129 84  CYS A SG  
732  N N   . ILE A 84  ? 0.3831 0.2370 0.1838 -0.0772 0.0247  -0.0205 85  ILE A N   
733  C CA  . ILE A 84  ? 0.3695 0.2234 0.1732 -0.0811 0.0334  -0.0208 85  ILE A CA  
734  C C   . ILE A 84  ? 0.3675 0.2446 0.2031 -0.0742 0.0361  -0.0219 85  ILE A C   
735  O O   . ILE A 84  ? 0.3377 0.2195 0.1809 -0.0722 0.0354  -0.0204 85  ILE A O   
736  C CB  . ILE A 84  ? 0.4154 0.2602 0.2052 -0.0931 0.0471  -0.0259 85  ILE A CB  
737  C CG1 . ILE A 84  ? 0.4431 0.2589 0.1936 -0.1014 0.0442  -0.0232 85  ILE A CG1 
738  C CG2 . ILE A 84  ? 0.3977 0.2538 0.2029 -0.0971 0.0590  -0.0303 85  ILE A CG2 
739  C CD1 . ILE A 84  ? 0.5342 0.3401 0.2676 -0.1139 0.0570  -0.0291 85  ILE A CD1 
740  N N   . LEU A 85  ? 0.3234 0.2127 0.1753 -0.0706 0.0389  -0.0246 86  LEU A N   
741  C CA  . LEU A 85  ? 0.3072 0.2148 0.1850 -0.0633 0.0407  -0.0249 86  LEU A CA  
742  C C   . LEU A 85  ? 0.3309 0.2447 0.2170 -0.0558 0.0306  -0.0205 86  LEU A C   
743  O O   . LEU A 85  ? 0.3007 0.2252 0.2008 -0.0515 0.0305  -0.0194 86  LEU A O   
744  C CB  . LEU A 85  ? 0.3153 0.2289 0.2044 -0.0615 0.0472  -0.0287 86  LEU A CB  
745  C CG  . LEU A 85  ? 0.3874 0.3009 0.2765 -0.0672 0.0594  -0.0352 86  LEU A CG  
746  C CD1 . LEU A 85  ? 0.4005 0.3152 0.2973 -0.0648 0.0650  -0.0392 86  LEU A CD1 
747  C CD2 . LEU A 85  ? 0.4029 0.3302 0.3079 -0.0654 0.0639  -0.0377 86  LEU A CD2 
748  N N   . LEU A 86  ? 0.3078 0.2163 0.1860 -0.0544 0.0222  -0.0191 87  LEU A N   
749  C CA  . LEU A 86  ? 0.2915 0.2074 0.1787 -0.0479 0.0133  -0.0169 87  LEU A CA  
750  C C   . LEU A 86  ? 0.3281 0.2399 0.2107 -0.0467 0.0093  -0.0141 87  LEU A C   
751  O O   . LEU A 86  ? 0.3057 0.2272 0.2012 -0.0421 0.0073  -0.0131 87  LEU A O   
752  C CB  . LEU A 86  ? 0.2931 0.2066 0.1739 -0.0471 0.0048  -0.0183 87  LEU A CB  
753  C CG  . LEU A 86  ? 0.3403 0.2649 0.2337 -0.0408 -0.0034 -0.0187 87  LEU A CG  
754  C CD1 . LEU A 86  ? 0.3156 0.2534 0.2277 -0.0391 0.0024  -0.0194 87  LEU A CD1 
755  C CD2 . LEU A 86  ? 0.3901 0.3152 0.2785 -0.0400 -0.0128 -0.0222 87  LEU A CD2 
756  N N   . ASP A 87  ? 0.3269 0.2217 0.1886 -0.0516 0.0088  -0.0131 88  ASP A N   
757  C CA  . ASP A 87  ? 0.3259 0.2118 0.1796 -0.0520 0.0068  -0.0108 88  ASP A CA  
758  C C   . ASP A 87  ? 0.3442 0.2420 0.2128 -0.0540 0.0153  -0.0124 88  ASP A C   
759  O O   . ASP A 87  ? 0.3371 0.2394 0.2128 -0.0507 0.0124  -0.0114 88  ASP A O   
760  C CB  . ASP A 87  ? 0.3769 0.2382 0.2011 -0.0594 0.0077  -0.0095 88  ASP A CB  
761  C CG  . ASP A 87  ? 0.5374 0.3839 0.3431 -0.0551 -0.0049 -0.0069 88  ASP A CG  
762  O OD1 . ASP A 87  ? 0.5229 0.3805 0.3419 -0.0461 -0.0147 -0.0071 88  ASP A OD1 
763  O OD2 . ASP A 87  ? 0.5550 0.3793 0.3327 -0.0609 -0.0053 -0.0053 88  ASP A OD2 
764  N N   . PHE A 88  ? 0.3137 0.2183 0.1882 -0.0586 0.0252  -0.0159 89  PHE A N   
765  C CA  . PHE A 88  ? 0.2841 0.2045 0.1761 -0.0591 0.0321  -0.0190 89  PHE A CA  
766  C C   . PHE A 88  ? 0.2930 0.2300 0.2048 -0.0500 0.0273  -0.0174 89  PHE A C   
767  O O   . PHE A 88  ? 0.2626 0.2086 0.1833 -0.0489 0.0270  -0.0180 89  PHE A O   
768  C CB  . PHE A 88  ? 0.2865 0.2131 0.1841 -0.0632 0.0425  -0.0244 89  PHE A CB  
769  C CG  . PHE A 88  ? 0.2745 0.2219 0.1946 -0.0601 0.0469  -0.0285 89  PHE A CG  
770  C CD1 . PHE A 88  ? 0.2991 0.2520 0.2219 -0.0658 0.0512  -0.0324 89  PHE A CD1 
771  C CD2 . PHE A 88  ? 0.2835 0.2442 0.2211 -0.0510 0.0453  -0.0283 89  PHE A CD2 
772  C CE1 . PHE A 88  ? 0.2824 0.2575 0.2272 -0.0621 0.0532  -0.0371 89  PHE A CE1 
773  C CE2 . PHE A 88  ? 0.3083 0.2877 0.2651 -0.0460 0.0467  -0.0315 89  PHE A CE2 
774  C CZ  . PHE A 88  ? 0.2863 0.2749 0.2480 -0.0512 0.0499  -0.0363 89  PHE A CZ  
775  N N   . MET A 89  ? 0.2436 0.1839 0.1608 -0.0449 0.0242  -0.0160 90  MET A N   
776  C CA  . MET A 89  ? 0.2224 0.1750 0.1542 -0.0379 0.0208  -0.0144 90  MET A CA  
777  C C   . MET A 89  ? 0.2770 0.2307 0.2091 -0.0359 0.0147  -0.0127 90  MET A C   
778  O O   . MET A 89  ? 0.2636 0.2280 0.2059 -0.0331 0.0144  -0.0126 90  MET A O   
779  C CB  . MET A 89  ? 0.2363 0.1875 0.1689 -0.0353 0.0188  -0.0136 90  MET A CB  
780  C CG  . MET A 89  ? 0.2607 0.2104 0.1946 -0.0362 0.0255  -0.0156 90  MET A CG  
781  S SD  . MET A 89  ? 0.2944 0.2417 0.2289 -0.0349 0.0239  -0.0154 90  MET A SD  
782  C CE  . MET A 89  ? 0.2989 0.2381 0.2289 -0.0382 0.0323  -0.0189 90  MET A CE  
783  N N   . TYR A 90  ? 0.2510 0.1930 0.1712 -0.0369 0.0092  -0.0118 91  TYR A N   
784  C CA  . TYR A 90  ? 0.2481 0.1893 0.1685 -0.0337 0.0029  -0.0112 91  TYR A CA  
785  C C   . TYR A 90  ? 0.2960 0.2287 0.2082 -0.0374 0.0043  -0.0113 91  TYR A C   
786  O O   . TYR A 90  ? 0.2861 0.2168 0.1986 -0.0346 -0.0001 -0.0113 91  TYR A O   
787  C CB  . TYR A 90  ? 0.2673 0.2006 0.1804 -0.0305 -0.0053 -0.0111 91  TYR A CB  
788  C CG  . TYR A 90  ? 0.2713 0.2171 0.1969 -0.0269 -0.0075 -0.0130 91  TYR A CG  
789  C CD1 . TYR A 90  ? 0.2876 0.2347 0.2134 -0.0290 -0.0046 -0.0139 91  TYR A CD1 
790  C CD2 . TYR A 90  ? 0.2729 0.2283 0.2095 -0.0226 -0.0111 -0.0149 91  TYR A CD2 
791  C CE1 . TYR A 90  ? 0.2644 0.2213 0.2001 -0.0279 -0.0051 -0.0166 91  TYR A CE1 
792  C CE2 . TYR A 90  ? 0.2676 0.2339 0.2146 -0.0214 -0.0116 -0.0181 91  TYR A CE2 
793  C CZ  . TYR A 90  ? 0.2924 0.2591 0.2387 -0.0246 -0.0083 -0.0188 91  TYR A CZ  
794  O OH  . TYR A 90  ? 0.2656 0.2419 0.2210 -0.0254 -0.0074 -0.0229 91  TYR A OH  
795  N N   . THR A 91  ? 0.2624 0.1895 0.1671 -0.0446 0.0114  -0.0125 92  THR A N   
796  C CA  . THR A 91  ? 0.2845 0.2009 0.1789 -0.0506 0.0142  -0.0136 92  THR A CA  
797  C C   . THR A 91  ? 0.3130 0.2409 0.2157 -0.0575 0.0237  -0.0182 92  THR A C   
798  O O   . THR A 91  ? 0.3056 0.2273 0.2021 -0.0638 0.0270  -0.0205 92  THR A O   
799  C CB  . THR A 91  ? 0.3611 0.2507 0.2288 -0.0558 0.0137  -0.0116 92  THR A CB  
800  O OG1 . THR A 91  ? 0.3638 0.2519 0.2260 -0.0622 0.0209  -0.0133 92  THR A OG1 
801  C CG2 . THR A 91  ? 0.3644 0.2417 0.2221 -0.0481 0.0023  -0.0080 92  THR A CG2 
802  N N   . SER A 92  ? 0.2596 0.2022 0.1747 -0.0570 0.0284  -0.0206 93  SER A N   
803  C CA  . SER A 92  ? 0.2462 0.2032 0.1723 -0.0624 0.0372  -0.0271 93  SER A CA  
804  C C   . SER A 92  ? 0.3013 0.2437 0.2110 -0.0742 0.0462  -0.0307 93  SER A C   
805  O O   . SER A 92  ? 0.2977 0.2523 0.2166 -0.0804 0.0550  -0.0380 93  SER A O   
806  C CB  . SER A 92  ? 0.2643 0.2345 0.2011 -0.0639 0.0375  -0.0308 93  SER A CB  
807  O OG  . SER A 92  ? 0.3144 0.2945 0.2614 -0.0549 0.0297  -0.0276 93  SER A OG  
808  N N   A ARG A 93  ? 0.2941 0.2109 0.1793 -0.0771 0.0437  -0.0261 94  ARG A N   
809  N N   B ARG A 93  ? 0.2823 0.1988 0.1672 -0.0774 0.0439  -0.0262 94  ARG A N   
810  C CA  A ARG A 93  ? 0.3187 0.2150 0.1807 -0.0893 0.0518  -0.0281 94  ARG A CA  
811  C CA  B ARG A 93  ? 0.3011 0.1985 0.1640 -0.0898 0.0526  -0.0287 94  ARG A CA  
812  C C   A ARG A 93  ? 0.3636 0.2558 0.2194 -0.0896 0.0539  -0.0281 94  ARG A C   
813  C C   B ARG A 93  ? 0.3591 0.2506 0.2141 -0.0900 0.0541  -0.0281 94  ARG A C   
814  O O   A ARG A 93  ? 0.3493 0.2360 0.2008 -0.0820 0.0452  -0.0229 94  ARG A O   
815  O O   B ARG A 93  ? 0.3475 0.2326 0.1973 -0.0825 0.0450  -0.0227 94  ARG A O   
816  C CB  A ARG A 93  ? 0.3873 0.2530 0.2206 -0.0919 0.0466  -0.0226 94  ARG A CB  
817  C CB  B ARG A 93  ? 0.3382 0.2059 0.1730 -0.0949 0.0498  -0.0245 94  ARG A CB  
818  C CG  A ARG A 93  ? 0.4809 0.3463 0.3176 -0.0923 0.0452  -0.0231 94  ARG A CG  
819  C CG  B ARG A 93  ? 0.3047 0.1758 0.1444 -0.0997 0.0533  -0.0280 94  ARG A CG  
820  C CD  A ARG A 93  ? 0.5492 0.3829 0.3590 -0.0905 0.0375  -0.0168 94  ARG A CD  
821  C CD  B ARG A 93  ? 0.4882 0.3301 0.3040 -0.0993 0.0471  -0.0224 94  ARG A CD  
822  N NE  A ARG A 93  ? 0.6122 0.4137 0.3878 -0.1012 0.0427  -0.0153 94  ARG A NE  
823  N NE  B ARG A 93  ? 0.5703 0.4157 0.3919 -0.1042 0.0508  -0.0265 94  ARG A NE  
824  C CZ  A ARG A 93  ? 0.7799 0.5640 0.5378 -0.1151 0.0533  -0.0186 94  ARG A CZ  
825  C CZ  B ARG A 93  ? 0.7658 0.5827 0.5626 -0.1132 0.0546  -0.0263 94  ARG A CZ  
826  N NH1 A ARG A 93  ? 0.6366 0.3882 0.3594 -0.1254 0.0584  -0.0166 94  ARG A NH1 
827  N NH1 B ARG A 93  ? 0.5901 0.4123 0.3942 -0.1181 0.0585  -0.0311 94  ARG A NH1 
828  N NH2 A ARG A 93  ? 0.6258 0.4240 0.3996 -0.1198 0.0592  -0.0243 94  ARG A NH2 
829  N NH2 B ARG A 93  ? 0.6954 0.4764 0.4578 -0.1176 0.0546  -0.0212 94  ARG A NH2 
830  N N   . LEU A 94  ? 0.3322 0.2275 0.1874 -0.0993 0.0662  -0.0352 95  LEU A N   
831  C CA  . LEU A 94  ? 0.3389 0.2303 0.1881 -0.1013 0.0704  -0.0369 95  LEU A CA  
832  C C   . LEU A 94  ? 0.4233 0.2877 0.2395 -0.1155 0.0781  -0.0380 95  LEU A C   
833  O O   . LEU A 94  ? 0.4268 0.2899 0.2387 -0.1278 0.0900  -0.0446 95  LEU A O   
834  C CB  . LEU A 94  ? 0.3190 0.2378 0.1969 -0.0991 0.0785  -0.0454 95  LEU A CB  
835  C CG  . LEU A 94  ? 0.3677 0.2848 0.2438 -0.0995 0.0835  -0.0483 95  LEU A CG  
836  C CD1 . LEU A 94  ? 0.3552 0.2696 0.2325 -0.0882 0.0724  -0.0411 95  LEU A CD1 
837  C CD2 . LEU A 94  ? 0.3746 0.3157 0.2769 -0.0987 0.0935  -0.0588 95  LEU A CD2 
838  N N   . ASN A 95  ? 0.4338 0.2764 0.2254 -0.1145 0.0714  -0.0320 96  ASN A N   
839  C CA  . ASN A 95  ? 0.4676 0.2796 0.2212 -0.1275 0.0769  -0.0315 96  ASN A CA  
840  C C   . ASN A 95  ? 0.5190 0.3366 0.2732 -0.1359 0.0896  -0.0395 96  ASN A C   
841  O O   . ASN A 95  ? 0.5240 0.3330 0.2658 -0.1345 0.0860  -0.0378 96  ASN A O   
842  C CB  . ASN A 95  ? 0.5206 0.3068 0.2461 -0.1214 0.0617  -0.0218 96  ASN A CB  
843  C CG  . ASN A 95  ? 0.7706 0.5204 0.4509 -0.1338 0.0652  -0.0198 96  ASN A CG  
844  O OD1 . ASN A 95  ? 0.7001 0.4375 0.3648 -0.1485 0.0790  -0.0241 96  ASN A OD1 
845  N ND2 . ASN A 95  ? 0.6969 0.4288 0.3542 -0.1287 0.0529  -0.0138 96  ASN A ND2 
846  N N   . LEU A 96  ? 0.4680 0.3027 0.2395 -0.1439 0.1042  -0.0497 97  LEU A N   
847  C CA  . LEU A 96  ? 0.4810 0.3257 0.2594 -0.1511 0.1180  -0.0599 97  LEU A CA  
848  C C   . LEU A 96  ? 0.5536 0.3722 0.2964 -0.1707 0.1312  -0.0639 97  LEU A C   
849  O O   . LEU A 96  ? 0.5484 0.3588 0.2810 -0.1819 0.1388  -0.0665 97  LEU A O   
850  C CB  . LEU A 96  ? 0.4667 0.3475 0.2868 -0.1471 0.1253  -0.0700 97  LEU A CB  
851  C CG  . LEU A 96  ? 0.5378 0.4385 0.3798 -0.1459 0.1353  -0.0807 97  LEU A CG  
852  C CD1 . LEU A 96  ? 0.5406 0.4391 0.3850 -0.1336 0.1259  -0.0748 97  LEU A CD1 
853  C CD2 . LEU A 96  ? 0.5215 0.4575 0.4041 -0.1396 0.1391  -0.0901 97  LEU A CD2 
854  N N   . ARG A 97  ? 0.5375 0.3401 0.2576 -0.1758 0.1338  -0.0642 98  ARG A N   
855  C CA  . ARG A 97  ? 0.5859 0.3588 0.2650 -0.1951 0.1461  -0.0672 98  ARG A CA  
856  C C   . ARG A 97  ? 0.6036 0.3849 0.2866 -0.2023 0.1595  -0.0781 98  ARG A C   
857  O O   . ARG A 97  ? 0.5602 0.3603 0.2674 -0.1902 0.1546  -0.0794 98  ARG A O   
858  C CB  . ARG A 97  ? 0.6364 0.3703 0.2697 -0.1946 0.1320  -0.0540 98  ARG A CB  
859  C CG  . ARG A 97  ? 0.7209 0.4429 0.3481 -0.1860 0.1177  -0.0432 98  ARG A CG  
860  C CD  . ARG A 97  ? 0.9442 0.6299 0.5294 -0.1818 0.1014  -0.0309 98  ARG A CD  
861  N NE  . ARG A 97  ? 1.1823 0.8294 0.7165 -0.1991 0.1100  -0.0306 98  ARG A NE  
862  C CZ  . ARG A 97  ? 1.4453 1.0609 0.9459 -0.2121 0.1172  -0.0285 98  ARG A CZ  
863  N NH1 . ARG A 97  ? 1.3185 0.8968 0.7695 -0.2285 0.1255  -0.0280 98  ARG A NH1 
864  N NH2 . ARG A 97  ? 1.2956 0.9148 0.8098 -0.2097 0.1168  -0.0271 98  ARG A NH2 
865  N N   . GLU A 98  ? 0.5884 0.3540 0.2460 -0.2226 0.1775  -0.0865 99  GLU A N   
866  C CA  . GLU A 98  ? 0.5927 0.3648 0.2519 -0.2308 0.1920  -0.0983 99  GLU A CA  
867  C C   . GLU A 98  ? 0.6605 0.4220 0.3063 -0.2221 0.1799  -0.0916 99  GLU A C   
868  O O   . GLU A 98  ? 0.6392 0.4198 0.3084 -0.2172 0.1847  -0.0995 99  GLU A O   
869  C CB  . GLU A 98  ? 0.6573 0.4037 0.2775 -0.2564 0.2117  -0.1060 99  GLU A CB  
870  C CG  . GLU A 98  ? 0.7915 0.5463 0.4147 -0.2670 0.2297  -0.1208 99  GLU A CG  
871  C CD  . GLU A 98  ? 1.2209 0.9489 0.8026 -0.2941 0.2506  -0.1290 99  GLU A CD  
872  O OE1 . GLU A 98  ? 1.1702 0.8555 0.6985 -0.3036 0.2456  -0.1177 99  GLU A OE1 
873  O OE2 . GLU A 98  ? 1.2639 1.0129 0.8658 -0.3058 0.2721  -0.1473 99  GLU A OE2 
874  N N   . GLY A 99  ? 0.6630 0.3944 0.2720 -0.2199 0.1642  -0.0780 100 GLY A N   
875  C CA  . GLY A 99  ? 0.6737 0.3938 0.2660 -0.2131 0.1513  -0.0720 100 GLY A CA  
876  C C   . GLY A 99  ? 0.6677 0.4131 0.2967 -0.1929 0.1366  -0.0683 100 GLY A C   
877  O O   . GLY A 99  ? 0.6626 0.4055 0.2856 -0.1888 0.1295  -0.0673 100 GLY A O   
878  N N   . ASN A 100 ? 0.5839 0.3533 0.2500 -0.1812 0.1327  -0.0669 101 ASN A N   
879  C CA  . ASN A 100 ? 0.5343 0.3245 0.2317 -0.1633 0.1197  -0.0630 101 ASN A CA  
880  C C   . ASN A 100 ? 0.5489 0.3716 0.2923 -0.1552 0.1274  -0.0709 101 ASN A C   
881  O O   . ASN A 100 ? 0.5107 0.3478 0.2774 -0.1417 0.1188  -0.0683 101 ASN A O   
882  C CB  . ASN A 100 ? 0.5268 0.3113 0.2208 -0.1527 0.1013  -0.0509 101 ASN A CB  
883  C CG  . ASN A 100 ? 0.5962 0.3895 0.3057 -0.1513 0.1032  -0.0498 101 ASN A CG  
884  O OD1 . ASN A 100 ? 0.4833 0.2993 0.2221 -0.1515 0.1139  -0.0577 101 ASN A OD1 
885  N ND2 . ASN A 100 ? 0.5398 0.3167 0.2319 -0.1486 0.0919  -0.0407 101 ASN A ND2 
886  N N   . ILE A 101 ? 0.5190 0.3532 0.2751 -0.1632 0.1431  -0.0808 102 ILE A N   
887  C CA  . ILE A 101 ? 0.4851 0.3514 0.2854 -0.1537 0.1482  -0.0885 102 ILE A CA  
888  C C   . ILE A 101 ? 0.4874 0.3655 0.3084 -0.1438 0.1491  -0.0930 102 ILE A C   
889  O O   . ILE A 101 ? 0.4376 0.3342 0.2887 -0.1289 0.1426  -0.0913 102 ILE A O   
890  C CB  . ILE A 101 ? 0.5292 0.4088 0.3410 -0.1648 0.1653  -0.1013 102 ILE A CB  
891  C CG1 . ILE A 101 ? 0.5076 0.4230 0.3671 -0.1513 0.1660  -0.1083 102 ILE A CG1 
892  C CG2 . ILE A 101 ? 0.5352 0.4044 0.3281 -0.1816 0.1831  -0.1127 102 ILE A CG2 
893  C CD1 . ILE A 101 ? 0.5058 0.4393 0.3813 -0.1586 0.1753  -0.1176 102 ILE A CD1 
894  N N   . MET A 102 ? 0.4787 0.3439 0.2815 -0.1523 0.1570  -0.0984 103 MET A N   
895  C CA  . MET A 102 ? 0.4754 0.3480 0.2953 -0.1440 0.1589  -0.1033 103 MET A CA  
896  C C   . MET A 102 ? 0.4944 0.3640 0.3168 -0.1314 0.1424  -0.0923 103 MET A C   
897  O O   . MET A 102 ? 0.4533 0.3363 0.3026 -0.1186 0.1404  -0.0931 103 MET A O   
898  C CB  . MET A 102 ? 0.5384 0.3971 0.3367 -0.1573 0.1719  -0.1126 103 MET A CB  
899  C CG  . MET A 102 ? 0.6185 0.4836 0.4189 -0.1704 0.1915  -0.1266 103 MET A CG  
900  S SD  . MET A 102 ? 0.6660 0.5682 0.5191 -0.1592 0.2001  -0.1387 103 MET A SD  
901  C CE  . MET A 102 ? 0.6281 0.5365 0.5031 -0.1466 0.2036  -0.1463 103 MET A CE  
902  N N   . ALA A 103 ? 0.4787 0.3308 0.2733 -0.1346 0.1303  -0.0825 104 ALA A N   
903  C CA  . ALA A 103 ? 0.4721 0.3235 0.2695 -0.1244 0.1149  -0.0738 104 ALA A CA  
904  C C   . ALA A 103 ? 0.4726 0.3402 0.2962 -0.1115 0.1068  -0.0678 104 ALA A C   
905  O O   . ALA A 103 ? 0.4303 0.3062 0.2721 -0.1011 0.1017  -0.0656 104 ALA A O   
906  C CB  . ALA A 103 ? 0.5081 0.3403 0.2721 -0.1299 0.1031  -0.0665 104 ALA A CB  
907  N N   . VAL A 104 ? 0.4122 0.2830 0.2362 -0.1135 0.1068  -0.0657 105 VAL A N   
908  C CA  . VAL A 104 ? 0.3710 0.2575 0.2183 -0.1025 0.0996  -0.0608 105 VAL A CA  
909  C C   . VAL A 104 ? 0.3834 0.2897 0.2629 -0.0928 0.1051  -0.0664 105 VAL A C   
910  O O   . VAL A 104 ? 0.3637 0.2775 0.2584 -0.0812 0.0969  -0.0612 105 VAL A O   
911  C CB  . VAL A 104 ? 0.4165 0.3012 0.2564 -0.1079 0.0993  -0.0586 105 VAL A CB  
912  C CG1 . VAL A 104 ? 0.3808 0.2845 0.2469 -0.0974 0.0937  -0.0558 105 VAL A CG1 
913  C CG2 . VAL A 104 ? 0.4302 0.2923 0.2382 -0.1127 0.0895  -0.0505 105 VAL A CG2 
914  N N   A MET A 105 ? 0.3639 0.2780 0.2530 -0.0969 0.1187  -0.0773 106 MET A N   
915  N N   B MET A 105 ? 0.3660 0.2800 0.2551 -0.0969 0.1187  -0.0773 106 MET A N   
916  C CA  A MET A 105 ? 0.3578 0.2902 0.2779 -0.0853 0.1227  -0.0834 106 MET A CA  
917  C CA  B MET A 105 ? 0.3607 0.2931 0.2806 -0.0855 0.1229  -0.0835 106 MET A CA  
918  C C   A MET A 105 ? 0.4005 0.3261 0.3239 -0.0766 0.1197  -0.0813 106 MET A C   
919  C C   B MET A 105 ? 0.4069 0.3326 0.3303 -0.0767 0.1198  -0.0814 106 MET A C   
920  O O   A MET A 105 ? 0.3698 0.3032 0.3116 -0.0632 0.1142  -0.0782 106 MET A O   
921  O O   B MET A 105 ? 0.3824 0.3162 0.3244 -0.0633 0.1143  -0.0783 106 MET A O   
922  C CB  A MET A 105 ? 0.3963 0.3394 0.3271 -0.0915 0.1383  -0.0977 106 MET A CB  
923  C CB  B MET A 105 ? 0.4024 0.3452 0.3326 -0.0919 0.1385  -0.0978 106 MET A CB  
924  C CG  A MET A 105 ? 0.4236 0.3877 0.3886 -0.0769 0.1403  -0.1048 106 MET A CG  
925  C CG  B MET A 105 ? 0.4363 0.4009 0.4010 -0.0776 0.1406  -0.1050 106 MET A CG  
926  S SD  A MET A 105 ? 0.4741 0.4589 0.4586 -0.0836 0.1578  -0.1240 106 MET A SD  
927  S SD  B MET A 105 ? 0.4995 0.4802 0.4805 -0.0845 0.1595  -0.1247 106 MET A SD  
928  C CE  A MET A 105 ? 0.4576 0.4249 0.4269 -0.0917 0.1713  -0.1327 106 MET A CE  
929  C CE  B MET A 105 ? 0.4529 0.4472 0.4669 -0.0625 0.1573  -0.1297 106 MET A CE  
930  N N   . ALA A 106 ? 0.3875 0.2968 0.2910 -0.0849 0.1236  -0.0832 107 ALA A N   
931  C CA  . ALA A 106 ? 0.3881 0.2883 0.2917 -0.0796 0.1223  -0.0825 107 ALA A CA  
932  C C   . ALA A 106 ? 0.3929 0.2912 0.2968 -0.0722 0.1088  -0.0715 107 ALA A C   
933  O O   . ALA A 106 ? 0.3715 0.2698 0.2878 -0.0623 0.1072  -0.0699 107 ALA A O   
934  C CB  . ALA A 106 ? 0.4200 0.3039 0.2990 -0.0922 0.1277  -0.0868 107 ALA A CB  
935  N N   . THR A 107 ? 0.3503 0.2464 0.2407 -0.0767 0.0995  -0.0644 108 THR A N   
936  C CA  . THR A 107 ? 0.3376 0.2345 0.2297 -0.0706 0.0873  -0.0557 108 THR A CA  
937  C C   . THR A 107 ? 0.3710 0.2811 0.2847 -0.0591 0.0841  -0.0521 108 THR A C   
938  O O   . THR A 107 ? 0.3381 0.2476 0.2586 -0.0519 0.0798  -0.0481 108 THR A O   
939  C CB  . THR A 107 ? 0.4069 0.2980 0.2800 -0.0768 0.0778  -0.0505 108 THR A CB  
940  O OG1 . THR A 107 ? 0.4087 0.2868 0.2594 -0.0872 0.0806  -0.0543 108 THR A OG1 
941  C CG2 . THR A 107 ? 0.3987 0.2919 0.2747 -0.0715 0.0663  -0.0443 108 THR A CG2 
942  N N   . ALA A 108 ? 0.3304 0.2519 0.2535 -0.0583 0.0868  -0.0543 109 ALA A N   
943  C CA  . ALA A 108 ? 0.3045 0.2404 0.2476 -0.0475 0.0829  -0.0519 109 ALA A CA  
944  C C   . ALA A 108 ? 0.3299 0.2676 0.2882 -0.0366 0.0864  -0.0549 109 ALA A C   
945  O O   . ALA A 108 ? 0.3122 0.2528 0.2791 -0.0264 0.0801  -0.0496 109 ALA A O   
946  C CB  . ALA A 108 ? 0.3067 0.2559 0.2569 -0.0508 0.0859  -0.0560 109 ALA A CB  
947  N N   . MET A 109 ? 0.3056 0.2391 0.2651 -0.0384 0.0964  -0.0632 110 MET A N   
948  C CA  . MET A 109 ? 0.3060 0.2370 0.2781 -0.0267 0.0995  -0.0661 110 MET A CA  
949  C C   . MET A 109 ? 0.3513 0.2649 0.3131 -0.0239 0.0951  -0.0589 110 MET A C   
950  O O   . MET A 109 ? 0.3480 0.2585 0.3165 -0.0123 0.0910  -0.0545 110 MET A O   
951  C CB  . MET A 109 ? 0.3495 0.2784 0.3243 -0.0304 0.1121  -0.0778 110 MET A CB  
952  C CG  . MET A 109 ? 0.4023 0.3518 0.3938 -0.0306 0.1180  -0.0873 110 MET A CG  
953  S SD  . MET A 109 ? 0.4952 0.4423 0.4862 -0.0395 0.1349  -0.1026 110 MET A SD  
954  C CE  . MET A 109 ? 0.4677 0.4086 0.4750 -0.0215 0.1366  -0.1063 110 MET A CE  
955  N N   . TYR A 110 ? 0.3390 0.2412 0.2832 -0.0350 0.0955  -0.0579 111 TYR A N   
956  C CA  . TYR A 110 ? 0.3439 0.2319 0.2783 -0.0360 0.0926  -0.0533 111 TYR A CA  
957  C C   . TYR A 110 ? 0.3626 0.2552 0.2994 -0.0310 0.0827  -0.0442 111 TYR A C   
958  O O   . TYR A 110 ? 0.3421 0.2250 0.2783 -0.0256 0.0817  -0.0403 111 TYR A O   
959  C CB  . TYR A 110 ? 0.3614 0.2428 0.2785 -0.0496 0.0932  -0.0557 111 TYR A CB  
960  C CG  . TYR A 110 ? 0.3697 0.2423 0.2782 -0.0534 0.0892  -0.0528 111 TYR A CG  
961  C CD1 . TYR A 110 ? 0.4124 0.2702 0.3179 -0.0537 0.0957  -0.0559 111 TYR A CD1 
962  C CD2 . TYR A 110 ? 0.3612 0.2402 0.2645 -0.0576 0.0798  -0.0484 111 TYR A CD2 
963  C CE1 . TYR A 110 ? 0.3835 0.2346 0.2816 -0.0597 0.0937  -0.0551 111 TYR A CE1 
964  C CE2 . TYR A 110 ? 0.3618 0.2369 0.2600 -0.0623 0.0769  -0.0484 111 TYR A CE2 
965  C CZ  . TYR A 110 ? 0.3760 0.2377 0.2715 -0.0643 0.0843  -0.0521 111 TYR A CZ  
966  O OH  . TYR A 110 ? 0.3718 0.2310 0.2629 -0.0711 0.0828  -0.0539 111 TYR A OH  
967  N N   . LEU A 111 ? 0.3132 0.2184 0.2509 -0.0334 0.0763  -0.0411 112 LEU A N   
968  C CA  . LEU A 111 ? 0.2886 0.1993 0.2285 -0.0298 0.0675  -0.0337 112 LEU A CA  
969  C C   . LEU A 111 ? 0.3317 0.2495 0.2843 -0.0179 0.0652  -0.0309 112 LEU A C   
970  O O   . LEU A 111 ? 0.3145 0.2344 0.2674 -0.0143 0.0589  -0.0249 112 LEU A O   
971  C CB  . LEU A 111 ? 0.2694 0.1884 0.2046 -0.0360 0.0615  -0.0320 112 LEU A CB  
972  C CG  . LEU A 111 ? 0.3097 0.2220 0.2303 -0.0457 0.0595  -0.0334 112 LEU A CG  
973  C CD1 . LEU A 111 ? 0.3012 0.2190 0.2165 -0.0487 0.0519  -0.0307 112 LEU A CD1 
974  C CD2 . LEU A 111 ? 0.3252 0.2319 0.2432 -0.0469 0.0574  -0.0324 112 LEU A CD2 
975  N N   . GLN A 112 ? 0.3027 0.2256 0.2660 -0.0119 0.0698  -0.0361 113 GLN A N   
976  C CA  . GLN A 112 ? 0.3021 0.2346 0.2792 0.0010  0.0662  -0.0350 113 GLN A CA  
977  C C   . GLN A 112 ? 0.3161 0.2660 0.2989 0.0001  0.0594  -0.0326 113 GLN A C   
978  O O   . GLN A 112 ? 0.2935 0.2452 0.2761 0.0053  0.0523  -0.0263 113 GLN A O   
979  C CB  . GLN A 112 ? 0.3251 0.2421 0.2971 0.0104  0.0633  -0.0288 113 GLN A CB  
980  C CG  . GLN A 112 ? 0.3959 0.2923 0.3613 0.0114  0.0711  -0.0318 113 GLN A CG  
981  C CD  . GLN A 112 ? 0.5159 0.3911 0.4689 0.0159  0.0694  -0.0246 113 GLN A CD  
982  O OE1 . GLN A 112 ? 0.4084 0.2841 0.3611 0.0243  0.0625  -0.0183 113 GLN A OE1 
983  N NE2 . GLN A 112 ? 0.4803 0.3354 0.4210 0.0093  0.0761  -0.0258 113 GLN A NE2 
984  N N   . MET A 113 ? 0.2744 0.2347 0.2597 -0.0080 0.0627  -0.0379 114 MET A N   
985  C CA  . MET A 113 ? 0.2572 0.2322 0.2468 -0.0112 0.0585  -0.0374 114 MET A CA  
986  C C   . MET A 113 ? 0.3249 0.3173 0.3312 -0.0094 0.0636  -0.0470 114 MET A C   
987  O O   . MET A 113 ? 0.3088 0.3034 0.3131 -0.0193 0.0713  -0.0537 114 MET A O   
988  C CB  . MET A 113 ? 0.2740 0.2413 0.2479 -0.0238 0.0588  -0.0359 114 MET A CB  
989  C CG  . MET A 113 ? 0.2973 0.2531 0.2597 -0.0246 0.0529  -0.0288 114 MET A CG  
990  S SD  . MET A 113 ? 0.3404 0.2869 0.2849 -0.0362 0.0510  -0.0279 114 MET A SD  
991  C CE  . MET A 113 ? 0.2999 0.2564 0.2470 -0.0373 0.0458  -0.0259 114 MET A CE  
992  N N   . GLU A 114 ? 0.3190 0.3230 0.3413 0.0037  0.0597  -0.0483 115 GLU A N   
993  C CA  . GLU A 114 ? 0.3392 0.3633 0.3827 0.0089  0.0636  -0.0593 115 GLU A CA  
994  C C   . GLU A 114 ? 0.3381 0.3810 0.3893 -0.0017 0.0677  -0.0671 115 GLU A C   
995  O O   . GLU A 114 ? 0.3310 0.3848 0.3933 -0.0058 0.0770  -0.0786 115 GLU A O   
996  C CB  . GLU A 114 ? 0.3729 0.4064 0.4306 0.0268  0.0548  -0.0583 115 GLU A CB  
997  C CG  . GLU A 114 ? 0.5561 0.5668 0.6042 0.0373  0.0527  -0.0515 115 GLU A CG  
998  N N   . HIS A 115 ? 0.2807 0.3267 0.3259 -0.0071 0.0621  -0.0621 116 HIS A N   
999  C CA  . HIS A 115 ? 0.2933 0.3542 0.3438 -0.0185 0.0672  -0.0700 116 HIS A CA  
1000 C C   . HIS A 115 ? 0.3325 0.3791 0.3663 -0.0345 0.0781  -0.0731 116 HIS A C   
1001 O O   . HIS A 115 ? 0.3370 0.3946 0.3775 -0.0438 0.0878  -0.0840 116 HIS A O   
1002 C CB  . HIS A 115 ? 0.3142 0.3801 0.3617 -0.0203 0.0593  -0.0648 116 HIS A CB  
1003 C CG  . HIS A 115 ? 0.3640 0.4469 0.4272 -0.0064 0.0493  -0.0640 116 HIS A CG  
1004 N ND1 . HIS A 115 ? 0.3951 0.5044 0.4825 0.0001  0.0493  -0.0750 116 HIS A ND1 
1005 C CD2 . HIS A 115 ? 0.3857 0.4628 0.4423 0.0014  0.0389  -0.0541 116 HIS A CD2 
1006 C CE1 . HIS A 115 ? 0.3847 0.5020 0.4779 0.0128  0.0376  -0.0705 116 HIS A CE1 
1007 N NE2 . HIS A 115 ? 0.3864 0.4838 0.4601 0.0132  0.0317  -0.0578 116 HIS A NE2 
1008 N N   . VAL A 116 ? 0.2766 0.2990 0.2883 -0.0380 0.0766  -0.0643 117 VAL A N   
1009 C CA  . VAL A 116 ? 0.2861 0.2917 0.2778 -0.0518 0.0849  -0.0661 117 VAL A CA  
1010 C C   . VAL A 116 ? 0.3507 0.3596 0.3497 -0.0534 0.0962  -0.0765 117 VAL A C   
1011 O O   . VAL A 116 ? 0.3272 0.3361 0.3206 -0.0661 0.1071  -0.0848 117 VAL A O   
1012 C CB  . VAL A 116 ? 0.3316 0.3140 0.3001 -0.0537 0.0787  -0.0556 117 VAL A CB  
1013 C CG1 . VAL A 116 ? 0.3467 0.3113 0.2927 -0.0667 0.0860  -0.0579 117 VAL A CG1 
1014 C CG2 . VAL A 116 ? 0.3211 0.3013 0.2833 -0.0533 0.0692  -0.0477 117 VAL A CG2 
1015 N N   . VAL A 117 ? 0.3067 0.3172 0.3174 -0.0408 0.0944  -0.0766 118 VAL A N   
1016 C CA  . VAL A 117 ? 0.3162 0.3299 0.3363 -0.0400 0.1050  -0.0873 118 VAL A CA  
1017 C C   . VAL A 117 ? 0.3755 0.4150 0.4176 -0.0428 0.1132  -0.1015 118 VAL A C   
1018 O O   . VAL A 117 ? 0.3706 0.4105 0.4101 -0.0544 0.1263  -0.1119 118 VAL A O   
1019 C CB  . VAL A 117 ? 0.3497 0.3589 0.3791 -0.0240 0.1011  -0.0851 118 VAL A CB  
1020 C CG1 . VAL A 117 ? 0.3558 0.3684 0.3968 -0.0222 0.1126  -0.0977 118 VAL A CG1 
1021 C CG2 . VAL A 117 ? 0.3518 0.3366 0.3596 -0.0247 0.0956  -0.0735 118 VAL A CG2 
1022 N N   A ASP A 118 ? 0.3366 0.3984 0.4008 -0.0323 0.1058  -0.1030 119 ASP A N   
1023 N N   B ASP A 118 ? 0.3256 0.3863 0.3870 -0.0345 0.1057  -0.1022 119 ASP A N   
1024 C CA  A ASP A 118 ? 0.3378 0.4301 0.4283 -0.0331 0.1115  -0.1180 119 ASP A CA  
1025 C CA  B ASP A 118 ? 0.3202 0.4105 0.4060 -0.0368 0.1114  -0.1166 119 ASP A CA  
1026 C C   A ASP A 118 ? 0.3937 0.4882 0.4750 -0.0545 0.1237  -0.1260 119 ASP A C   
1027 C C   B ASP A 118 ? 0.3498 0.4384 0.4227 -0.0587 0.1234  -0.1232 119 ASP A C   
1028 O O   A ASP A 118 ? 0.3943 0.5065 0.4914 -0.0609 0.1360  -0.1419 119 ASP A O   
1029 O O   B ASP A 118 ? 0.3353 0.4366 0.4191 -0.0668 0.1369  -0.1380 119 ASP A O   
1030 C CB  A ASP A 118 ? 0.3500 0.4632 0.4594 -0.0199 0.0984  -0.1158 119 ASP A CB  
1031 C CB  B ASP A 118 ? 0.3318 0.4425 0.4354 -0.0247 0.0986  -0.1141 119 ASP A CB  
1032 C CG  A ASP A 118 ? 0.4955 0.6140 0.6211 0.0025  0.0888  -0.1141 119 ASP A CG  
1033 C CG  B ASP A 118 ? 0.4758 0.6222 0.6093 -0.0248 0.1026  -0.1306 119 ASP A CG  
1034 O OD1 A ASP A 118 ? 0.5354 0.6572 0.6736 0.0093  0.0950  -0.1229 119 ASP A OD1 
1035 O OD1 B ASP A 118 ? 0.4934 0.6563 0.6493 -0.0177 0.1081  -0.1434 119 ASP A OD1 
1036 O OD2 A ASP A 118 ? 0.5612 0.6786 0.6851 0.0133  0.0755  -0.1040 119 ASP A OD2 
1037 O OD2 B ASP A 118 ? 0.5280 0.6868 0.6640 -0.0319 0.1002  -0.1319 119 ASP A OD2 
1038 N N   A THR A 119 ? 0.3525 0.4279 0.4076 -0.0656 0.1209  -0.1157 120 THR A N   
1039 N N   B THR A 119 ? 0.3048 0.3759 0.3532 -0.0686 0.1194  -0.1128 120 THR A N   
1040 C CA  A THR A 119 ? 0.3630 0.4317 0.4015 -0.0864 0.1316  -0.1206 120 THR A CA  
1041 C CA  B THR A 119 ? 0.3194 0.3826 0.3504 -0.0895 0.1308  -0.1179 120 THR A CA  
1042 C C   A THR A 119 ? 0.4051 0.4528 0.4212 -0.0992 0.1439  -0.1235 120 THR A C   
1043 C C   B THR A 119 ? 0.3823 0.4240 0.3906 -0.1019 0.1429  -0.1207 120 THR A C   
1044 O O   A THR A 119 ? 0.4104 0.4631 0.4253 -0.1144 0.1587  -0.1360 120 THR A O   
1045 O O   B THR A 119 ? 0.3850 0.4250 0.3843 -0.1191 0.1566  -0.1302 120 THR A O   
1046 C CB  A THR A 119 ? 0.4761 0.5301 0.4950 -0.0904 0.1226  -0.1084 120 THR A CB  
1047 C CB  B THR A 119 ? 0.3379 0.3856 0.3479 -0.0956 0.1233  -0.1068 120 THR A CB  
1048 O OG1 A THR A 119 ? 0.4728 0.5503 0.5154 -0.0789 0.1130  -0.1087 120 THR A OG1 
1049 O OG1 B THR A 119 ? 0.3571 0.4017 0.3557 -0.1150 0.1355  -0.1148 120 THR A OG1 
1050 C CG2 A THR A 119 ? 0.4857 0.5284 0.4844 -0.1111 0.1330  -0.1124 120 THR A CG2 
1051 C CG2 B THR A 119 ? 0.2808 0.2966 0.2608 -0.0948 0.1156  -0.0918 120 THR A CG2 
1052 N N   . CYS A 120 ? 0.3543 0.3788 0.3518 -0.0944 0.1384  -0.1130 121 CYS A N   
1053 C CA  . CYS A 120 ? 0.3747 0.3787 0.3495 -0.1056 0.1487  -0.1157 121 CYS A CA  
1054 C C   . CYS A 120 ? 0.4374 0.4604 0.4340 -0.1074 0.1634  -0.1332 121 CYS A C   
1055 O O   . CYS A 120 ? 0.4370 0.4537 0.4199 -0.1245 0.1782  -0.1425 121 CYS A O   
1056 C CB  . CYS A 120 ? 0.3714 0.3561 0.3328 -0.0969 0.1397  -0.1046 121 CYS A CB  
1057 S SG  . CYS A 120 ? 0.4191 0.3785 0.3496 -0.0990 0.1255  -0.0873 121 CYS A SG  
1058 N N   . ARG A 121 ? 0.3977 0.4439 0.4279 -0.0896 0.1591  -0.1382 122 ARG A N   
1059 C CA  . ARG A 121 ? 0.4061 0.4749 0.4640 -0.0868 0.1711  -0.1562 122 ARG A CA  
1060 C C   . ARG A 121 ? 0.4524 0.5429 0.5219 -0.1019 0.1842  -0.1718 122 ARG A C   
1061 O O   . ARG A 121 ? 0.4539 0.5500 0.5265 -0.1134 0.2011  -0.1871 122 ARG A O   
1062 C CB  . ARG A 121 ? 0.4161 0.5052 0.5070 -0.0625 0.1604  -0.1572 122 ARG A CB  
1063 C CG  . ARG A 121 ? 0.6179 0.6865 0.7010 -0.0491 0.1536  -0.1476 122 ARG A CG  
1064 C CD  . ARG A 121 ? 0.8023 0.8872 0.9160 -0.0305 0.1539  -0.1577 122 ARG A CD  
1065 N NE  . ARG A 121 ? 0.9065 0.9902 1.0284 -0.0095 0.1372  -0.1464 122 ARG A NE  
1066 C CZ  . ARG A 121 ? 1.0447 1.1033 1.1524 -0.0004 0.1310  -0.1352 122 ARG A CZ  
1067 N NH1 . ARG A 121 ? 0.8241 0.8590 0.9109 -0.0098 0.1393  -0.1342 122 ARG A NH1 
1068 N NH2 . ARG A 121 ? 0.8970 0.9532 1.0095 0.0171  0.1170  -0.1254 122 ARG A NH2 
1069 N N   . LYS A 122 ? 0.4170 0.5194 0.4921 -0.1033 0.1775  -0.1689 123 LYS A N   
1070 C CA  . LYS A 122 ? 0.4181 0.5418 0.5046 -0.1187 0.1892  -0.1838 123 LYS A CA  
1071 C C   . LYS A 122 ? 0.4831 0.5804 0.5327 -0.1448 0.2043  -0.1849 123 LYS A C   
1072 O O   . LYS A 122 ? 0.4775 0.5875 0.5339 -0.1604 0.2223  -0.2024 123 LYS A O   
1073 C CB  . LYS A 122 ? 0.4287 0.5684 0.5273 -0.1136 0.1771  -0.1792 123 LYS A CB  
1074 C CG  . LYS A 122 ? 0.6257 0.7974 0.7633 -0.0897 0.1643  -0.1827 123 LYS A CG  
1075 C CD  . LYS A 122 ? 0.7594 0.9520 0.9107 -0.0881 0.1550  -0.1828 123 LYS A CD  
1076 C CE  . LYS A 122 ? 0.8849 1.0934 1.0579 -0.0627 0.1360  -0.1765 123 LYS A CE  
1077 N NZ  . LYS A 122 ? 0.9741 1.2122 1.1835 -0.0462 0.1358  -0.1908 123 LYS A NZ  
1078 N N   . PHE A 123 ? 0.4461 0.5064 0.4560 -0.1497 0.1969  -0.1669 124 PHE A N   
1079 C CA  . PHE A 123 ? 0.4763 0.5046 0.4441 -0.1726 0.2083  -0.1651 124 PHE A CA  
1080 C C   . PHE A 123 ? 0.5471 0.5658 0.5038 -0.1815 0.2230  -0.1741 124 PHE A C   
1081 O O   . PHE A 123 ? 0.5532 0.5624 0.4908 -0.2033 0.2405  -0.1840 124 PHE A O   
1082 C CB  . PHE A 123 ? 0.5033 0.4966 0.4349 -0.1711 0.1938  -0.1441 124 PHE A CB  
1083 C CG  . PHE A 123 ? 0.5214 0.5113 0.4466 -0.1746 0.1871  -0.1376 124 PHE A CG  
1084 C CD1 . PHE A 123 ? 0.5355 0.5574 0.4957 -0.1646 0.1811  -0.1419 124 PHE A CD1 
1085 C CD2 . PHE A 123 ? 0.5793 0.5324 0.4621 -0.1862 0.1853  -0.1265 124 PHE A CD2 
1086 C CE1 . PHE A 123 ? 0.5421 0.5601 0.4957 -0.1686 0.1756  -0.1367 124 PHE A CE1 
1087 C CE2 . PHE A 123 ? 0.6024 0.5500 0.4789 -0.1888 0.1796  -0.1209 124 PHE A CE2 
1088 C CZ  . PHE A 123 ? 0.5458 0.5263 0.4580 -0.1808 0.1754  -0.1264 124 PHE A CZ  
1089 N N   . ILE A 124 ? 0.4859 0.5069 0.4544 -0.1658 0.2172  -0.1721 125 ILE A N   
1090 C CA  . ILE A 124 ? 0.5077 0.5215 0.4689 -0.1727 0.2312  -0.1821 125 ILE A CA  
1091 C C   . ILE A 124 ? 0.5698 0.6162 0.5634 -0.1791 0.2498  -0.2062 125 ILE A C   
1092 O O   . ILE A 124 ? 0.5851 0.6230 0.5618 -0.1987 0.2687  -0.2178 125 ILE A O   
1093 C CB  . ILE A 124 ? 0.5333 0.5393 0.4981 -0.1547 0.2205  -0.1740 125 ILE A CB  
1094 C CG1 . ILE A 124 ? 0.5361 0.5076 0.4623 -0.1554 0.2070  -0.1542 125 ILE A CG1 
1095 C CG2 . ILE A 124 ? 0.5679 0.5742 0.5358 -0.1591 0.2362  -0.1885 125 ILE A CG2 
1096 C CD1 . ILE A 124 ? 0.6086 0.5766 0.5428 -0.1363 0.1924  -0.1438 125 ILE A CD1 
1097 N N   . LYS A 125 ? 0.5219 0.6059 0.5611 -0.1631 0.2444  -0.2143 126 LYS A N   
1098 C CA  . LYS A 125 ? 0.5325 0.6552 0.6110 -0.1653 0.2593  -0.2390 126 LYS A CA  
1099 C C   . LYS A 125 ? 0.6039 0.7309 0.6718 -0.1927 0.2775  -0.2518 126 LYS A C   
1100 O O   . LYS A 125 ? 0.5968 0.7408 0.6780 -0.2055 0.2976  -0.2730 126 LYS A O   
1101 C CB  . LYS A 125 ? 0.5480 0.7080 0.6735 -0.1409 0.2451  -0.2424 126 LYS A CB  
1102 C CG  . LYS A 125 ? 0.7591 0.9608 0.9311 -0.1346 0.2562  -0.2679 126 LYS A CG  
1103 C CD  . LYS A 125 ? 0.8931 1.1328 1.1081 -0.1130 0.2409  -0.2717 126 LYS A CD  
1104 C CE  . LYS A 125 ? 1.0403 1.3259 1.3039 -0.1075 0.2513  -0.2994 126 LYS A CE  
1105 N NZ  . LYS A 125 ? 1.1418 1.4659 1.4453 -0.0879 0.2353  -0.3039 126 LYS A NZ  
1106 N N   . ALA A 126 ? 0.5665 0.6760 0.6091 -0.2024 0.2714  -0.2393 127 ALA A N   
1107 C CA  . ALA A 126 ? 0.5924 0.6983 0.6183 -0.2297 0.2883  -0.2490 127 ALA A CA  
1108 C C   . ALA A 126 ? 0.6897 0.7603 0.6705 -0.2544 0.3071  -0.2515 127 ALA A C   
1109 O O   . ALA A 126 ? 0.7036 0.7789 0.6794 -0.2780 0.3283  -0.2679 127 ALA A O   
1110 C CB  . ALA A 126 ? 0.5934 0.6831 0.5996 -0.2317 0.2755  -0.2330 127 ALA A CB  
1111 N N   . SER A 127 ? 0.6817 0.7174 0.6293 -0.2498 0.2996  -0.2360 128 SER A N   
1112 C CA  . SER A 127 ? 0.7396 0.7386 0.6397 -0.2715 0.3144  -0.2362 128 SER A CA  
1113 C C   . SER A 127 ? 0.8204 0.8337 0.7356 -0.2756 0.3322  -0.2555 128 SER A C   
1114 O O   . SER A 127 ? 0.8655 0.8535 0.7439 -0.2977 0.3492  -0.2607 128 SER A O   
1115 C CB  . SER A 127 ? 0.8160 0.7717 0.6716 -0.2658 0.2971  -0.2117 128 SER A CB  
1116 O OG  . SER A 127 ? 0.9757 0.9049 0.7989 -0.2735 0.2894  -0.1975 128 SER A OG  
1117 N N   . GLU A 128 ? 0.7431 0.7951 0.7103 -0.2546 0.3288  -0.2664 129 GLU A N   
1118 C CA  . GLU A 128 ? 0.9816 1.0493 0.9684 -0.2553 0.3450  -0.2858 129 GLU A CA  
1119 C C   . GLU A 128 ? 1.4794 1.5790 1.4914 -0.2735 0.3700  -0.3140 129 GLU A C   
1120 O O   . GLU A 128 ? 1.0765 1.1615 1.0593 -0.3002 0.3847  -0.3180 129 GLU A O   
1121 C CB  . GLU A 128 ? 0.9665 1.0556 0.9936 -0.2241 0.3305  -0.2849 129 GLU A CB  
1122 C CG  . GLU A 128 ? 1.0585 1.1968 1.1449 -0.2061 0.3260  -0.2983 129 GLU A CG  
1123 C CD  . GLU A 128 ? 1.2918 1.4445 1.4117 -0.1736 0.3084  -0.2936 129 GLU A CD  
1124 O OE1 . GLU A 128 ? 1.1896 1.3127 1.2865 -0.1635 0.2962  -0.2758 129 GLU A OE1 
1125 O OE2 . GLU A 128 ? 1.1955 1.3890 1.3642 -0.1582 0.3065  -0.3082 129 GLU A OE2 
1129 N N   A TRP B 2   ? 0.2205 0.4304 0.2624 -0.0529 -0.0154 -0.0755 1   TRP D N   
1130 N N   B TRP B 2   ? 0.2238 0.4337 0.2657 -0.0529 -0.0154 -0.0755 1   TRP D N   
1131 C CA  A TRP B 2   ? 0.2080 0.4174 0.2503 -0.0527 -0.0153 -0.0762 1   TRP D CA  
1132 C CA  B TRP B 2   ? 0.2155 0.4248 0.2577 -0.0527 -0.0153 -0.0762 1   TRP D CA  
1133 C C   A TRP B 2   ? 0.2594 0.4686 0.3034 -0.0530 -0.0153 -0.0759 1   TRP D C   
1134 C C   B TRP B 2   ? 0.2533 0.4625 0.2973 -0.0530 -0.0153 -0.0759 1   TRP D C   
1135 O O   A TRP B 2   ? 0.2571 0.4658 0.3015 -0.0531 -0.0159 -0.0754 1   TRP D O   
1136 O O   B TRP B 2   ? 0.2468 0.4556 0.2912 -0.0532 -0.0157 -0.0754 1   TRP D O   
1137 C CB  A TRP B 2   ? 0.1946 0.4029 0.2360 -0.0522 -0.0161 -0.0766 1   TRP D CB  
1138 C CB  B TRP B 2   ? 0.2011 0.4093 0.2426 -0.0522 -0.0162 -0.0766 1   TRP D CB  
1139 C CG  A TRP B 2   ? 0.1985 0.4068 0.2383 -0.0519 -0.0160 -0.0772 1   TRP D CG  
1140 C CG  B TRP B 2   ? 0.2125 0.4202 0.2548 -0.0523 -0.0171 -0.0764 1   TRP D CG  
1141 C CD1 A TRP B 2   ? 0.2327 0.4409 0.2721 -0.0517 -0.0165 -0.0771 1   TRP D CD1 
1142 C CD1 B TRP B 2   ? 0.2510 0.4581 0.2940 -0.0523 -0.0177 -0.0765 1   TRP D CD1 
1143 C CD2 A TRP B 2   ? 0.1916 0.4003 0.2305 -0.0516 -0.0155 -0.0781 1   TRP D CD2 
1144 C CD2 B TRP B 2   ? 0.2094 0.4175 0.2528 -0.0525 -0.0174 -0.0763 1   TRP D CD2 
1145 N NE1 A TRP B 2   ? 0.2252 0.4336 0.2630 -0.0514 -0.0162 -0.0779 1   TRP D NE1 
1146 N NE1 B TRP B 2   ? 0.2446 0.4518 0.2890 -0.0525 -0.0182 -0.0768 1   TRP D NE1 
1147 C CE2 A TRP B 2   ? 0.2355 0.4441 0.2728 -0.0514 -0.0156 -0.0787 1   TRP D CE2 
1148 C CE2 B TRP B 2   ? 0.2598 0.4678 0.3041 -0.0526 -0.0180 -0.0767 1   TRP D CE2 
1149 C CE3 A TRP B 2   ? 0.1954 0.4045 0.2351 -0.0516 -0.0149 -0.0782 1   TRP D CE3 
1150 C CE3 B TRP B 2   ? 0.2214 0.4301 0.2657 -0.0526 -0.0172 -0.0759 1   TRP D CE3 
1151 C CZ2 A TRP B 2   ? 0.2206 0.4295 0.2566 -0.0511 -0.0150 -0.0797 1   TRP D CZ2 
1152 C CZ2 B TRP B 2   ? 0.2477 0.4567 0.2932 -0.0529 -0.0184 -0.0769 1   TRP D CZ2 
1153 C CZ3 A TRP B 2   ? 0.2062 0.4155 0.2451 -0.0514 -0.0144 -0.0790 1   TRP D CZ3 
1154 C CZ3 B TRP B 2   ? 0.2417 0.4511 0.2869 -0.0528 -0.0177 -0.0755 1   TRP D CZ3 
1155 C CH2 A TRP B 2   ? 0.2180 0.4272 0.2547 -0.0511 -0.0144 -0.0799 1   TRP D CH2 
1156 C CH2 B TRP B 2   ? 0.2478 0.4576 0.2933 -0.0530 -0.0183 -0.0762 1   TRP D CH2 
1157 N N   . VAL B 3   ? 0.1975 0.4072 0.2430 -0.0530 -0.0148 -0.0763 2   VAL D N   
1158 C CA  . VAL B 3   ? 0.1931 0.4027 0.2407 -0.0533 -0.0148 -0.0760 2   VAL D CA  
1159 C C   . VAL B 3   ? 0.2131 0.4227 0.2623 -0.0530 -0.0150 -0.0756 2   VAL D C   
1160 O O   . VAL B 3   ? 0.2011 0.4109 0.2502 -0.0527 -0.0149 -0.0757 2   VAL D O   
1161 C CB  . VAL B 3   ? 0.2309 0.4421 0.2804 -0.0540 -0.0137 -0.0768 2   VAL D CB  
1162 C CG1 . VAL B 3   ? 0.2258 0.4379 0.2737 -0.0546 -0.0136 -0.0766 2   VAL D CG1 
1163 C CG2 . VAL B 3   ? 0.2286 0.4412 0.2800 -0.0541 -0.0125 -0.0780 2   VAL D CG2 
1164 N N   . ILE B 4   ? 0.1805 0.3901 0.2317 -0.0531 -0.0154 -0.0750 3   ILE D N   
1165 C CA  . ILE B 4   ? 0.1813 0.3914 0.2351 -0.0529 -0.0156 -0.0741 3   ILE D CA  
1166 C C   . ILE B 4   ? 0.2241 0.4346 0.2817 -0.0532 -0.0144 -0.0749 3   ILE D C   
1167 O O   . ILE B 4   ? 0.2103 0.4211 0.2694 -0.0536 -0.0141 -0.0757 3   ILE D O   
1168 C CB  . ILE B 4   ? 0.2024 0.4129 0.2570 -0.0530 -0.0166 -0.0730 3   ILE D CB  
1169 C CG1 . ILE B 4   ? 0.1951 0.4060 0.2468 -0.0531 -0.0175 -0.0730 3   ILE D CG1 
1170 C CG2 . ILE B 4   ? 0.2164 0.4279 0.2745 -0.0530 -0.0169 -0.0714 3   ILE D CG2 
1171 C CD1 . ILE B 4   ? 0.2437 0.4555 0.2935 -0.0530 -0.0180 -0.0727 3   ILE D CD1 
1172 N N   . PRO B 5   ? 0.2213 0.4323 0.2809 -0.0530 -0.0137 -0.0752 4   PRO D N   
1173 C CA  . PRO B 5   ? 0.2282 0.4402 0.2925 -0.0534 -0.0123 -0.0767 4   PRO D CA  
1174 C C   . PRO B 5   ? 0.2760 0.4881 0.3456 -0.0535 -0.0125 -0.0760 4   PRO D C   
1175 O O   . PRO B 5   ? 0.2722 0.4839 0.3426 -0.0532 -0.0137 -0.0737 4   PRO D O   
1176 C CB  . PRO B 5   ? 0.2483 0.4607 0.3136 -0.0531 -0.0115 -0.0771 4   PRO D CB  
1177 C CG  . PRO B 5   ? 0.2941 0.5055 0.3569 -0.0526 -0.0128 -0.0749 4   PRO D CG  
1178 C CD  . PRO B 5   ? 0.2382 0.4490 0.2963 -0.0526 -0.0140 -0.0745 4   PRO D CD  
1179 N N   . ALA B 6   ? 0.2456 0.4589 0.3195 -0.0542 -0.0113 -0.0780 5   ALA D N   
# 
