data_7GUH
# 
_entry.id   7GUH 
# 
_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   7GUH         pdb_00007guh 10.2210/pdb7guh/pdb 
WWPDB D_1001406652 ?            ?                   
# 
_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                        7GUH 
_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   302 166 HOH HOH A . 
F 6 HOH 3   303 81  HOH HOH A . 
F 6 HOH 4   304 15  HOH HOH A . 
F 6 HOH 5   305 88  HOH HOH A . 
F 6 HOH 6   306 84  HOH HOH A . 
F 6 HOH 7   307 159 HOH HOH A . 
F 6 HOH 8   308 32  HOH HOH A . 
F 6 HOH 9   309 92  HOH HOH A . 
F 6 HOH 10  310 130 HOH HOH A . 
F 6 HOH 11  311 114 HOH HOH A . 
F 6 HOH 12  312 230 HOH HOH A . 
F 6 HOH 13  313 33  HOH HOH A . 
F 6 HOH 14  314 189 HOH HOH A . 
F 6 HOH 15  315 149 HOH HOH A . 
F 6 HOH 16  316 63  HOH HOH A . 
F 6 HOH 17  317 187 HOH HOH A . 
F 6 HOH 18  318 5   HOH HOH A . 
F 6 HOH 19  319 14  HOH HOH A . 
F 6 HOH 20  320 103 HOH HOH A . 
F 6 HOH 21  321 85  HOH HOH A . 
F 6 HOH 22  322 23  HOH HOH A . 
F 6 HOH 23  323 196 HOH HOH A . 
F 6 HOH 24  324 87  HOH HOH A . 
F 6 HOH 25  325 113 HOH HOH A . 
F 6 HOH 26  326 135 HOH HOH A . 
F 6 HOH 27  327 35  HOH HOH A . 
F 6 HOH 28  328 83  HOH HOH A . 
F 6 HOH 29  329 24  HOH HOH A . 
F 6 HOH 30  330 97  HOH HOH A . 
F 6 HOH 31  331 143 HOH HOH A . 
F 6 HOH 32  332 13  HOH HOH A . 
F 6 HOH 33  333 109 HOH HOH A . 
F 6 HOH 34  334 90  HOH HOH A . 
F 6 HOH 35  335 141 HOH HOH A . 
F 6 HOH 36  336 112 HOH HOH A . 
F 6 HOH 37  337 151 HOH HOH A . 
F 6 HOH 38  338 94  HOH HOH A . 
F 6 HOH 39  339 213 HOH HOH A . 
F 6 HOH 40  340 165 HOH HOH A . 
F 6 HOH 41  341 134 HOH HOH A . 
F 6 HOH 42  342 3   HOH HOH A . 
F 6 HOH 43  343 49  HOH HOH A . 
F 6 HOH 44  344 100 HOH HOH A . 
F 6 HOH 45  345 50  HOH HOH A . 
F 6 HOH 46  346 117 HOH HOH A . 
F 6 HOH 47  347 136 HOH HOH A . 
F 6 HOH 48  348 51  HOH HOH A . 
F 6 HOH 49  349 18  HOH HOH A . 
F 6 HOH 50  350 105 HOH HOH A . 
F 6 HOH 51  351 86  HOH HOH A . 
F 6 HOH 52  352 102 HOH HOH A . 
F 6 HOH 53  353 184 HOH HOH A . 
F 6 HOH 54  354 115 HOH HOH A . 
F 6 HOH 55  355 116 HOH HOH A . 
F 6 HOH 56  356 180 HOH HOH A . 
F 6 HOH 57  357 26  HOH HOH A . 
F 6 HOH 58  358 44  HOH HOH A . 
F 6 HOH 59  359 110 HOH HOH A . 
F 6 HOH 60  360 74  HOH HOH A . 
F 6 HOH 61  361 11  HOH HOH A . 
F 6 HOH 62  362 123 HOH HOH A . 
F 6 HOH 63  363 231 HOH HOH A . 
F 6 HOH 64  364 95  HOH HOH A . 
F 6 HOH 65  365 66  HOH HOH A . 
F 6 HOH 66  366 62  HOH HOH A . 
F 6 HOH 67  367 101 HOH HOH A . 
F 6 HOH 68  368 6   HOH HOH A . 
F 6 HOH 69  369 150 HOH HOH A . 
F 6 HOH 70  370 147 HOH HOH A . 
F 6 HOH 71  371 121 HOH HOH A . 
F 6 HOH 72  372 89  HOH HOH A . 
F 6 HOH 73  373 60  HOH HOH A . 
F 6 HOH 74  374 178 HOH HOH A . 
F 6 HOH 75  375 119 HOH HOH A . 
F 6 HOH 76  376 10  HOH HOH A . 
F 6 HOH 77  377 22  HOH HOH A . 
F 6 HOH 78  378 25  HOH HOH A . 
F 6 HOH 79  379 168 HOH HOH A . 
F 6 HOH 80  380 107 HOH HOH A . 
F 6 HOH 81  381 246 HOH HOH A . 
F 6 HOH 82  382 104 HOH HOH A . 
F 6 HOH 83  383 28  HOH HOH A . 
F 6 HOH 84  384 20  HOH HOH A . 
F 6 HOH 85  385 192 HOH HOH A . 
F 6 HOH 86  386 40  HOH HOH A . 
F 6 HOH 87  387 29  HOH HOH A . 
F 6 HOH 88  388 164 HOH HOH A . 
F 6 HOH 89  389 244 HOH HOH A . 
F 6 HOH 90  390 39  HOH HOH A . 
F 6 HOH 91  391 21  HOH HOH A . 
F 6 HOH 92  392 99  HOH HOH A . 
F 6 HOH 93  393 57  HOH HOH A . 
F 6 HOH 94  394 93  HOH HOH A . 
F 6 HOH 95  395 238 HOH HOH A . 
F 6 HOH 96  396 203 HOH HOH A . 
F 6 HOH 97  397 82  HOH HOH A . 
F 6 HOH 98  398 30  HOH HOH A . 
F 6 HOH 99  399 36  HOH HOH A . 
F 6 HOH 100 400 56  HOH HOH A . 
F 6 HOH 101 401 38  HOH HOH A . 
F 6 HOH 102 402 239 HOH HOH A . 
F 6 HOH 103 403 242 HOH HOH A . 
F 6 HOH 104 404 27  HOH HOH A . 
F 6 HOH 105 405 167 HOH HOH A . 
F 6 HOH 106 406 53  HOH HOH A . 
F 6 HOH 107 407 193 HOH HOH A . 
F 6 HOH 108 408 52  HOH HOH A . 
F 6 HOH 109 409 153 HOH HOH A . 
F 6 HOH 110 410 37  HOH HOH A . 
F 6 HOH 111 411 96  HOH HOH A . 
F 6 HOH 112 412 75  HOH HOH A . 
F 6 HOH 113 413 45  HOH HOH A . 
F 6 HOH 114 414 237 HOH HOH A . 
F 6 HOH 115 415 17  HOH HOH A . 
F 6 HOH 116 416 171 HOH HOH A . 
F 6 HOH 117 417 69  HOH HOH A . 
F 6 HOH 118 418 186 HOH HOH A . 
F 6 HOH 119 419 79  HOH HOH A . 
F 6 HOH 120 420 176 HOH HOH A . 
F 6 HOH 121 421 200 HOH HOH A . 
F 6 HOH 122 422 241 HOH HOH A . 
F 6 HOH 123 423 146 HOH HOH A . 
F 6 HOH 124 424 55  HOH HOH A . 
F 6 HOH 125 425 209 HOH HOH A . 
F 6 HOH 126 426 54  HOH HOH A . 
F 6 HOH 127 427 145 HOH HOH A . 
F 6 HOH 128 428 31  HOH HOH A . 
F 6 HOH 129 429 148 HOH HOH A . 
F 6 HOH 130 430 98  HOH HOH A . 
F 6 HOH 131 431 106 HOH HOH A . 
F 6 HOH 132 432 43  HOH HOH A . 
F 6 HOH 133 433 139 HOH HOH A . 
F 6 HOH 134 434 191 HOH HOH A . 
F 6 HOH 135 435 185 HOH HOH A . 
F 6 HOH 136 436 232 HOH HOH A . 
F 6 HOH 137 437 188 HOH HOH A . 
F 6 HOH 138 438 158 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 146 446 221 HOH HOH A . 
F 6 HOH 147 447 247 HOH HOH A . 
F 6 HOH 148 448 206 HOH HOH A . 
F 6 HOH 149 449 70  HOH HOH A . 
F 6 HOH 150 450 169 HOH HOH A . 
F 6 HOH 151 451 161 HOH HOH A . 
F 6 HOH 152 452 212 HOH HOH A . 
F 6 HOH 153 453 243 HOH HOH A . 
F 6 HOH 154 454 215 HOH HOH A . 
F 6 HOH 155 455 131 HOH HOH A . 
F 6 HOH 156 456 183 HOH HOH A . 
F 6 HOH 157 457 228 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 161 461 179 HOH HOH A . 
F 6 HOH 162 462 245 HOH HOH A . 
F 6 HOH 163 463 175 HOH HOH A . 
F 6 HOH 164 464 65  HOH HOH A . 
F 6 HOH 165 465 170 HOH HOH A . 
F 6 HOH 166 466 195 HOH HOH A . 
F 6 HOH 167 467 152 HOH HOH A . 
F 6 HOH 168 468 208 HOH HOH A . 
F 6 HOH 169 469 181 HOH HOH A . 
F 6 HOH 170 470 61  HOH HOH A . 
F 6 HOH 171 471 233 HOH HOH A . 
F 6 HOH 172 472 225 HOH HOH A . 
F 6 HOH 173 473 144 HOH HOH A . 
G 6 HOH 1   201 77  HOH HOH D . 
G 6 HOH 2   202 71  HOH HOH D . 
G 6 HOH 3   203 47  HOH HOH D . 
G 6 HOH 4   204 68  HOH HOH D . 
G 6 HOH 5   205 58  HOH HOH D . 
G 6 HOH 6   206 240 HOH HOH D . 
G 6 HOH 7   207 220 HOH HOH D . 
G 6 HOH 8   208 210 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 64  ? CD  ? A GLN 63  CD  
2  1 Y 1 A GLN 64  ? OE1 ? A GLN 63  OE1 
3  1 Y 1 A GLN 64  ? NE2 ? A GLN 63  NE2 
4  1 Y 1 A GLU 115 ? CD  ? A GLU 114 CD  
5  1 Y 1 A GLU 115 ? OE1 ? A GLU 114 OE1 
6  1 Y 1 A GLU 115 ? OE2 ? A GLU 114 OE2 
7  1 Y 1 D ALA 5   ? CA  ? B ALA 6   CA  
8  1 Y 1 D ALA 5   ? C   ? B ALA 6   C   
9  1 Y 1 D ALA 5   ? O   ? B ALA 6   O   
10 1 Y 1 D ALA 5   ? CB  ? B ALA 6   CB  
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
4 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com phasing           
http://www.globalphasing.com/buster/                ?   ? 
5 PDB_EXTRACT 3.24   'Sep. 1, 2017' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.entry_id           7GUH 
_cell.length_a           67.550 
_cell.length_b           67.550 
_cell.length_c           166.220 
_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                         7GUH 
_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          7GUH 
_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   65.96 
_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                     7GUH 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.880 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   21692 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.074 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.100 
_reflns.B_iso_Wilson_estimate        28.590 
_reflns.pdbx_redundancy              9.000 
_reflns.pdbx_Rrim_I_all              0.079 
_reflns.pdbx_Rpim_I_all              0.026 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     196311 
_reflns.pdbx_scaling_rejects         989 
_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  ? 11566 1241 ? 0.864 ? ? ? 9.300 ? 2.600  ? ? ? ? ? ? 100.000 0.914 0.295 0.874 ? 
1 2 9.000 33.880 ? 1518  227  ? 0.044 ? ? ? 6.700 ? 29.800 ? ? ? ? ? ? 98.700  0.048 0.018 0.999 ? 
# 
_refine.entry_id                                 7GUH 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.8000 
_refine.ls_d_res_low                             33.8800 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    100.0000 
_refine.ls_number_reflns_obs                     21639 
_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                          0.1790 
_refine.ls_R_factor_R_work                       0.1780 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2010 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.2000 
_refine.ls_number_reflns_R_free                  1126 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               33.7500 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -1.6611 
_refine.aniso_B[2][2]                            -1.6611 
_refine.aniso_B[3][3]                            3.3221 
_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               0.9580 
_refine.correlation_coeff_Fo_to_Fc_free          0.9480 
_refine.overall_SU_R_Cruickshank_DPI             0.0930 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0910 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1070 
_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                                126.470 
_refine.B_iso_min                                15.260 
_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                        7GUH 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.190 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.8000 
_refine_hist.d_res_low                        33.8800 
_refine_hist.pdbx_number_atoms_ligand         23 
_refine_hist.number_atoms_solvent             181 
_refine_hist.number_atoms_total               1230 
_refine_hist.pdbx_number_residues_total       130 
_refine_hist.pdbx_B_iso_mean_ligand           29.00 
_refine_hist.pdbx_B_iso_mean_solvent          51.06 
_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      1653 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1236 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1693 0.910  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.390  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    16.020 ? ?      ?            
# 
_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             2684 
_refine_ls_shell.R_factor_all                     0.2537 
_refine_ls_shell.R_factor_R_work                  0.2522 
_refine_ls_shell.R_factor_R_free                  0.2850 
_refine_ls_shell.percent_reflns_R_free            4.6500 
_refine_ls_shell.number_reflns_R_free             131 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2815 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUH 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 1 at 7.55 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUH 
_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 7GUH       7GUH   ? 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 7GUH A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUH D 1 ? 6   ? 7GUH   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 7GUH GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUH PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUH GLY A 3 ? UNP P41182 ? ? 'expression tag' 4 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6360  ? 
1 MORE         -68   ? 
1 'SSA (A^2)'  13260 ? 
# 
_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 33.7750000000 0.8660254038 
-0.5000000000 0.0000000000 -58.5000160256 0.0000000000 0.0000000000 -1.0000000000 27.7033333333 
# 
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 ? ? ? ? ? ? ? 1.327 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 ACE B 1 ? TRP B 2 A ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
2 ACE B 1 ? TRP B 2 B ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 40 ? ALA A 44 ? GLU A 41 ALA A 45 
AA1 2 VAL A 33 ? VAL A 37 ? VAL A 34 VAL A 38 
AA1 3 VAL A 70 ? ASN A 72 ? VAL A 71 ASN A 73 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 40 ? O GLU A 41 N VAL A 37 ? N VAL A 38 
AA1 2 3 N VAL A 36 ? N VAL A 37 O ILE A 71 ? O ILE A 72 
# 
_pdbx_entry_details.entry_id                   7GUH 
_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 37.01 49.00   
2 1 SER A 39  ? B 61.98 -107.76 
3 1 SER A 93  ? ? 76.20 -1.96   
4 1 GLN A 113 ? ? 62.74 63.17   
# 
_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   11.25 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 340 ? F HOH . 
2 1 A HOH 388 ? F HOH . 
3 1 A HOH 450 ? F HOH . 
4 1 A HOH 461 ? F HOH . 
5 1 A HOH 463 ? F HOH . 
6 1 A HOH 466 ? 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 -0.0129 -0.0743 -0.0284 -0.0408 0.0231  -0.0149 1.0356 1.7440 2.1581 
0.4500 -0.3056 1.1688 0.1455 -0.0972 -0.0483 -0.0485 0.0952 0.0723 0.2548  0.0081  -0.0501 
'X-RAY DIFFRACTION' 2 ? refined 18.9623 -32.3913 1.8231  -0.1399 0.0868  -0.0218 -0.0550 -0.0089 -0.0770 0.8383 0.0548 0.0000 
0.2895 0.1058  1.0758 0.0234 0.0055  -0.0289 -0.0060 0.0176 0.0559 -0.0227 -0.0171 0.0126  
# 
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                    7GUH 
_atom_sites.fract_transf_matrix[1][1]   0.014804 
_atom_sites.fract_transf_matrix[1][2]   0.008547 
_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]   0.017094 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006016 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASP A 1 5   ? 17.525 -21.142 -4.954 1.00 65.11  ? 6   ASP A N   1 
ATOM   2    C  CA  . ASP A 1 5   ? 18.393 -22.068 -5.685 1.00 64.05  ? 6   ASP A CA  1 
ATOM   3    C  C   . ASP A 1 5   ? 17.892 -23.526 -5.571 1.00 63.98  ? 6   ASP A C   1 
ATOM   4    O  O   . ASP A 1 5   ? 16.819 -23.774 -5.010 1.00 64.83  ? 6   ASP A O   1 
ATOM   5    C  CB  . ASP A 1 5   ? 19.851 -21.943 -5.180 1.00 64.77  ? 6   ASP A CB  1 
ATOM   6    C  CG  . ASP A 1 5   ? 20.907 -22.038 -6.274 1.00 78.49  ? 6   ASP A CG  1 
ATOM   7    O  OD1 . ASP A 1 5   ? 20.975 -23.096 -6.949 1.00 79.06  ? 6   ASP A OD1 1 
ATOM   8    O  OD2 . ASP A 1 5   ? 21.675 -21.065 -6.444 1.00 85.27  ? 6   ASP A OD2 1 
ATOM   9    N  N   . SER A 1 6   ? 18.666 -24.479 -6.127 1.00 55.34  ? 7   SER A N   1 
ATOM   10   C  CA  . SER A 1 6   ? 18.377 -25.911 -6.095 1.00 52.66  ? 7   SER A CA  1 
ATOM   11   C  C   . SER A 1 6   ? 19.371 -26.655 -5.147 1.00 48.20  ? 7   SER A C   1 
ATOM   12   O  O   . SER A 1 6   ? 19.673 -27.833 -5.357 1.00 47.65  ? 7   SER A O   1 
ATOM   13   C  CB  . SER A 1 6   ? 18.430 -26.483 -7.508 1.00 58.41  ? 7   SER A CB  1 
ATOM   14   O  OG  . SER A 1 6   ? 19.701 -26.284 -8.106 1.00 70.48  ? 7   SER A OG  1 
ATOM   15   N  N   . CYS A 1 7   ? 19.854 -25.965 -4.097 1.00 38.16  ? 8   CYS A N   1 
ATOM   16   C  CA  . CYS A 1 7   ? 20.799 -26.538 -3.126 1.00 34.84  ? 8   CYS A CA  1 
ATOM   17   C  C   . CYS A 1 7   ? 20.174 -27.704 -2.320 1.00 34.83  ? 8   CYS A C   1 
ATOM   18   O  O   . CYS A 1 7   ? 18.952 -27.770 -2.160 1.00 35.32  ? 8   CYS A O   1 
ATOM   19   C  CB  . CYS A 1 7   ? 21.296 -25.445 -2.176 1.00 35.43  ? 8   CYS A CB  1 
ATOM   20   S  SG  . CYS A 1 7   ? 22.451 -24.247 -2.913 1.00 40.41  ? 8   CYS A SG  1 
ATOM   21   N  N   . ILE A 1 8   ? 21.012 -28.614 -1.821 1.00 26.49  ? 9   ILE A N   1 
ATOM   22   C  CA  . ILE A 1 8   ? 20.651 -29.616 -0.818 1.00 23.75  ? 9   ILE A CA  1 
ATOM   23   C  C   . ILE A 1 8   ? 21.260 -29.069 0.483  1.00 25.49  ? 9   ILE A C   1 
ATOM   24   O  O   . ILE A 1 8   ? 22.203 -28.270 0.437  1.00 24.29  ? 9   ILE A O   1 
ATOM   25   C  CB  . ILE A 1 8   ? 21.026 -31.089 -1.132 1.00 26.42  ? 9   ILE A CB  1 
ATOM   26   C  CG1 . ILE A 1 8   ? 22.564 -31.259 -1.379 1.00 26.29  ? 9   ILE A CG1 1 
ATOM   27   C  CG2 . ILE A 1 8   ? 20.182 -31.615 -2.313 1.00 27.94  ? 9   ILE A CG2 1 
ATOM   28   C  CD1 . ILE A 1 8   ? 23.051 -32.713 -1.563 1.00 30.19  ? 9   ILE A CD1 1 
ATOM   29   N  N   A GLN A 1 9   ? 20.780 -29.512 1.638  0.57 21.40  ? 10  GLN A N   1 
ATOM   30   N  N   B GLN A 1 9   ? 20.685 -29.449 1.622  0.43 21.46  ? 10  GLN A N   1 
ATOM   31   C  CA  A GLN A 1 9   ? 21.293 -28.988 2.902  0.57 20.67  ? 10  GLN A CA  1 
ATOM   32   C  CA  B GLN A 1 9   ? 21.114 -28.970 2.929  0.43 20.41  ? 10  GLN A CA  1 
ATOM   33   C  C   A GLN A 1 9   ? 21.617 -30.107 3.886  0.57 23.89  ? 10  GLN A C   1 
ATOM   34   C  C   B GLN A 1 9   ? 21.547 -30.117 3.824  0.43 22.71  ? 10  GLN A C   1 
ATOM   35   O  O   A GLN A 1 9   ? 20.807 -31.015 4.062  0.57 23.87  ? 10  GLN A O   1 
ATOM   36   O  O   B GLN A 1 9   ? 20.897 -31.161 3.853  0.43 22.92  ? 10  GLN A O   1 
ATOM   37   C  CB  A GLN A 1 9   ? 20.257 -27.999 3.502  0.57 22.17  ? 10  GLN A CB  1 
ATOM   38   C  CB  B GLN A 1 9   ? 19.974 -28.157 3.598  0.43 21.64  ? 10  GLN A CB  1 
ATOM   39   C  CG  A GLN A 1 9   ? 20.633 -27.407 4.863  0.57 23.94  ? 10  GLN A CG  1 
ATOM   40   C  CG  B GLN A 1 9   ? 20.178 -27.889 5.107  0.43 27.40  ? 10  GLN A CG  1 
ATOM   41   C  CD  A GLN A 1 9   ? 19.453 -26.710 5.496  0.57 48.42  ? 10  GLN A CD  1 
ATOM   42   C  CD  B GLN A 1 9   ? 20.088 -26.445 5.533  0.43 39.52  ? 10  GLN A CD  1 
ATOM   43   O  OE1 A GLN A 1 9   ? 18.486 -27.336 5.946  0.57 38.56  ? 10  GLN A OE1 1 
ATOM   44   O  OE1 B GLN A 1 9   ? 19.799 -25.531 4.742  0.43 29.57  ? 10  GLN A OE1 1 
ATOM   45   N  NE2 A GLN A 1 9   ? 19.500 -25.393 5.535  0.57 50.97  ? 10  GLN A NE2 1 
ATOM   46   N  NE2 B GLN A 1 9   ? 20.335 -26.212 6.816  0.43 29.74  ? 10  GLN A NE2 1 
ATOM   47   N  N   A PHE A 1 10  ? 22.784 -30.029 4.549  0.78 21.87  ? 11  PHE A N   1 
ATOM   48   N  N   B PHE A 1 10  ? 22.623 -29.898 4.581  0.22 19.23  ? 11  PHE A N   1 
ATOM   49   C  CA  A PHE A 1 10  ? 23.147 -31.037 5.547  0.78 21.30  ? 11  PHE A CA  1 
ATOM   50   C  CA  B PHE A 1 10  ? 23.121 -30.860 5.550  0.22 18.67  ? 11  PHE A CA  1 
ATOM   51   C  C   A PHE A 1 10  ? 22.676 -30.541 6.913  0.78 22.61  ? 11  PHE A C   1 
ATOM   52   C  C   B PHE A 1 10  ? 22.585 -30.403 6.888  0.22 21.82  ? 11  PHE A C   1 
ATOM   53   O  O   A PHE A 1 10  ? 23.239 -29.586 7.464  0.78 20.66  ? 11  PHE A O   1 
ATOM   54   O  O   B PHE A 1 10  ? 22.989 -29.342 7.384  0.22 20.41  ? 11  PHE A O   1 
ATOM   55   C  CB  A PHE A 1 10  ? 24.667 -31.359 5.503  0.78 22.11  ? 11  PHE A CB  1 
ATOM   56   C  CB  B PHE A 1 10  ? 24.657 -30.912 5.504  0.22 19.63  ? 11  PHE A CB  1 
ATOM   57   C  CG  A PHE A 1 10  ? 25.058 -32.552 6.349  0.78 23.00  ? 11  PHE A CG  1 
ATOM   58   C  CG  B PHE A 1 10  ? 25.174 -31.791 4.389  0.22 21.44  ? 11  PHE A CG  1 
ATOM   59   C  CD1 A PHE A 1 10  ? 24.645 -33.839 6.005  0.78 26.34  ? 11  PHE A CD1 1 
ATOM   60   C  CD1 B PHE A 1 10  ? 24.912 -31.485 3.057  0.22 24.74  ? 11  PHE A CD1 1 
ATOM   61   C  CD2 A PHE A 1 10  ? 25.840 -32.390 7.490  0.78 24.07  ? 11  PHE A CD2 1 
ATOM   62   C  CD2 B PHE A 1 10  ? 25.923 -32.924 4.669  0.22 24.13  ? 11  PHE A CD2 1 
ATOM   63   C  CE1 A PHE A 1 10  ? 24.992 -34.942 6.804  0.78 27.17  ? 11  PHE A CE1 1 
ATOM   64   C  CE1 B PHE A 1 10  ? 25.383 -32.302 2.029  0.22 26.05  ? 11  PHE A CE1 1 
ATOM   65   C  CE2 A PHE A 1 10  ? 26.174 -33.487 8.291  0.78 25.87  ? 11  PHE A CE2 1 
ATOM   66   C  CE2 B PHE A 1 10  ? 26.387 -33.743 3.638  0.22 27.52  ? 11  PHE A CE2 1 
ATOM   67   C  CZ  A PHE A 1 10  ? 25.745 -34.752 7.950  0.78 24.26  ? 11  PHE A CZ  1 
ATOM   68   C  CZ  B PHE A 1 10  ? 26.125 -33.420 2.328  0.22 25.60  ? 11  PHE A CZ  1 
ATOM   69   N  N   . THR A 1 11  ? 21.595 -31.144 7.424  1.00 19.02  ? 12  THR A N   1 
ATOM   70   C  CA  . THR A 1 11  ? 20.932 -30.753 8.684  1.00 20.17  ? 12  THR A CA  1 
ATOM   71   C  C   . THR A 1 11  ? 21.879 -30.515 9.886  1.00 23.80  ? 12  THR A C   1 
ATOM   72   O  O   . THR A 1 11  ? 21.755 -29.486 10.572 1.00 22.31  ? 12  THR A O   1 
ATOM   73   C  CB  . THR A 1 11  ? 19.864 -31.797 9.032  1.00 27.96  ? 12  THR A CB  1 
ATOM   74   O  OG1 . THR A 1 11  ? 18.951 -31.881 7.929  1.00 29.69  ? 12  THR A OG1 1 
ATOM   75   C  CG2 . THR A 1 11  ? 19.092 -31.443 10.320 1.00 32.18  ? 12  THR A CG2 1 
ATOM   76   N  N   A ARG A 1 12  ? 22.811 -31.450 10.118 0.50 20.67  ? 13  ARG A N   1 
ATOM   77   N  N   B ARG A 1 12  ? 22.806 -31.452 10.130 0.50 21.06  ? 13  ARG A N   1 
ATOM   78   C  CA  A ARG A 1 12  ? 23.734 -31.388 11.262 0.50 20.56  ? 13  ARG A CA  1 
ATOM   79   C  CA  B ARG A 1 12  ? 23.730 -31.376 11.272 0.50 21.09  ? 13  ARG A CA  1 
ATOM   80   C  C   A ARG A 1 12  ? 24.981 -30.499 11.063 0.50 22.68  ? 13  ARG A C   1 
ATOM   81   C  C   B ARG A 1 12  ? 24.968 -30.475 11.074 0.50 22.82  ? 13  ARG A C   1 
ATOM   82   O  O   A ARG A 1 12  ? 25.787 -30.385 11.993 0.50 21.58  ? 13  ARG A O   1 
ATOM   83   O  O   B ARG A 1 12  ? 25.760 -30.336 12.015 0.50 21.61  ? 13  ARG A O   1 
ATOM   84   C  CB  A ARG A 1 12  ? 24.165 -32.815 11.672 0.50 23.12  ? 13  ARG A CB  1 
ATOM   85   C  CB  B ARG A 1 12  ? 24.178 -32.792 11.667 0.50 24.75  ? 13  ARG A CB  1 
ATOM   86   C  CG  A ARG A 1 12  ? 23.035 -33.719 12.201 0.50 30.09  ? 13  ARG A CG  1 
ATOM   87   C  CG  B ARG A 1 12  ? 23.218 -33.504 12.620 0.50 37.00  ? 13  ARG A CG  1 
ATOM   88   C  CD  A ARG A 1 12  ? 22.474 -33.265 13.541 0.50 42.38  ? 13  ARG A CD  1 
ATOM   89   C  CD  B ARG A 1 12  ? 22.950 -34.949 12.245 0.50 44.32  ? 13  ARG A CD  1 
ATOM   90   N  NE  A ARG A 1 12  ? 23.444 -33.378 14.636 0.50 49.74  ? 13  ARG A NE  1 
ATOM   91   N  NE  B ARG A 1 12  ? 24.164 -35.730 11.989 0.50 46.63  ? 13  ARG A NE  1 
ATOM   92   C  CZ  A ARG A 1 12  ? 23.368 -32.702 15.778 0.50 57.08  ? 13  ARG A CZ  1 
ATOM   93   C  CZ  B ARG A 1 12  ? 24.368 -36.453 10.891 0.50 56.74  ? 13  ARG A CZ  1 
ATOM   94   N  NH1 A ARG A 1 12  ? 22.382 -31.837 15.984 0.50 38.94  ? 13  ARG A NH1 1 
ATOM   95   N  NH1 B ARG A 1 12  ? 25.492 -37.140 10.741 0.50 50.51  ? 13  ARG A NH1 1 
ATOM   96   N  NH2 A ARG A 1 12  ? 24.282 -32.879 16.721 0.50 44.68  ? 13  ARG A NH2 1 
ATOM   97   N  NH2 B ARG A 1 12  ? 23.443 -36.505 9.940  0.50 31.70  ? 13  ARG A NH2 1 
ATOM   98   N  N   . HIS A 1 13  ? 25.148 -29.881 9.874  1.00 18.60  ? 14  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 13  ? 26.355 -29.068 9.562  1.00 17.63  ? 14  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 13  ? 26.641 -27.952 10.568 1.00 20.94  ? 14  HIS A C   1 
ATOM   101  O  O   . HIS A 1 13  ? 27.771 -27.871 11.067 1.00 19.47  ? 14  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 13  ? 26.327 -28.494 8.127  1.00 17.59  ? 14  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 13  ? 27.602 -27.748 7.809  1.00 18.95  ? 14  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 13  ? 28.783 -28.419 7.619  1.00 19.28  ? 14  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 13  ? 27.822 -26.420 7.679  1.00 19.85  ? 14  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 13  ? 29.700 -27.494 7.361  1.00 18.44  ? 14  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 13  ? 29.173 -26.267 7.406  1.00 18.48  ? 14  HIS A NE2 1 
ATOM   108  N  N   . ALA A 1 14  ? 25.646 -27.087 10.843 1.00 17.75  ? 15  ALA A N   1 
ATOM   109  C  CA  . ALA A 1 14  ? 25.870 -25.956 11.772 1.00 18.10  ? 15  ALA A CA  1 
ATOM   110  C  C   . ALA A 1 14  ? 26.269 -26.431 13.178 1.00 20.38  ? 15  ALA A C   1 
ATOM   111  O  O   . ALA A 1 14  ? 27.168 -25.847 13.770 1.00 18.98  ? 15  ALA A O   1 
ATOM   112  C  CB  . ALA A 1 14  ? 24.634 -25.061 11.836 1.00 19.11  ? 15  ALA A CB  1 
ATOM   113  N  N   A SER A 1 15  ? 25.607 -27.482 13.689 0.38 18.19  ? 16  SER A N   1 
ATOM   114  N  N   B SER A 1 15  ? 25.610 -27.488 13.690 0.33 18.39  ? 16  SER A N   1 
ATOM   115  N  N   C SER A 1 15  ? 25.606 -27.484 13.701 0.29 18.09  ? 16  SER A N   1 
ATOM   116  C  CA  A SER A 1 15  ? 25.901 -28.047 15.006 0.38 18.38  ? 16  SER A CA  1 
ATOM   117  C  CA  B SER A 1 15  ? 25.898 -28.063 15.007 0.33 18.69  ? 16  SER A CA  1 
ATOM   118  C  CA  C SER A 1 15  ? 25.917 -28.031 15.027 0.29 18.21  ? 16  SER A CA  1 
ATOM   119  C  C   A SER A 1 15  ? 27.317 -28.640 15.024 0.38 22.30  ? 16  SER A C   1 
ATOM   120  C  C   B SER A 1 15  ? 27.306 -28.665 15.034 0.33 22.68  ? 16  SER A C   1 
ATOM   121  C  C   C SER A 1 15  ? 27.311 -28.671 15.045 0.29 22.58  ? 16  SER A C   1 
ATOM   122  O  O   A SER A 1 15  ? 28.043 -28.445 16.004 0.38 19.77  ? 16  SER A O   1 
ATOM   123  O  O   B SER A 1 15  ? 28.018 -28.497 16.028 0.33 20.61  ? 16  SER A O   1 
ATOM   124  O  O   C SER A 1 15  ? 28.024 -28.528 16.041 0.29 20.76  ? 16  SER A O   1 
ATOM   125  C  CB  A SER A 1 15  ? 24.872 -29.112 15.372 0.38 21.44  ? 16  SER A CB  1 
ATOM   126  C  CB  B SER A 1 15  ? 24.862 -29.125 15.368 0.33 22.17  ? 16  SER A CB  1 
ATOM   127  C  CB  C SER A 1 15  ? 24.847 -29.021 15.483 0.29 21.21  ? 16  SER A CB  1 
ATOM   128  O  OG  A SER A 1 15  ? 25.153 -29.654 16.651 0.38 24.21  ? 16  SER A OG  1 
ATOM   129  O  OG  B SER A 1 15  ? 23.561 -28.564 15.406 0.33 26.94  ? 16  SER A OG  1 
ATOM   130  O  OG  C SER A 1 15  ? 24.773 -30.154 14.634 0.29 24.37  ? 16  SER A OG  1 
ATOM   131  N  N   . ASP A 1 16  ? 27.714 -29.331 13.934 1.00 20.61  ? 17  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 16  ? 29.047 -29.959 13.806 1.00 21.01  ? 17  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 16  ? 30.121 -28.872 13.778 1.00 21.07  ? 17  ASP A C   1 
ATOM   134  O  O   . ASP A 1 16  ? 31.170 -29.049 14.390 1.00 20.69  ? 17  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 16  ? 29.146 -30.840 12.545 1.00 22.99  ? 17  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 16  ? 28.389 -32.167 12.615 1.00 31.86  ? 17  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 16  ? 27.870 -32.507 13.709 1.00 32.22  ? 17  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 16  ? 28.305 -32.858 11.574 1.00 31.51  ? 17  ASP A OD2 1 
ATOM   139  N  N   . VAL A 1 17  ? 29.859 -27.759 13.049 1.00 16.28  ? 18  VAL A N   1 
ATOM   140  C  CA  . VAL A 1 17  ? 30.803 -26.620 13.015 1.00 15.55  ? 18  VAL A CA  1 
ATOM   141  C  C   . VAL A 1 17  ? 31.002 -26.083 14.450 1.00 19.17  ? 18  VAL A C   1 
ATOM   142  O  O   . VAL A 1 17  ? 32.128 -25.867 14.887 1.00 17.54  ? 18  VAL A O   1 
ATOM   143  C  CB  . VAL A 1 17  ? 30.320 -25.495 12.061 1.00 18.06  ? 18  VAL A CB  1 
ATOM   144  C  CG1 . VAL A 1 17  ? 31.101 -24.183 12.293 1.00 17.61  ? 18  VAL A CG1 1 
ATOM   145  C  CG2 . VAL A 1 17  ? 30.432 -25.942 10.597 1.00 17.90  ? 18  VAL A CG2 1 
ATOM   146  N  N   . LEU A 1 18  ? 29.904 -25.832 15.161 1.00 17.11  ? 19  LEU A N   1 
ATOM   147  C  CA  . LEU A 1 18  ? 29.992 -25.260 16.505 1.00 17.93  ? 19  LEU A CA  1 
ATOM   148  C  C   . LEU A 1 18  ? 30.722 -26.195 17.473 1.00 20.34  ? 19  LEU A C   1 
ATOM   149  O  O   . LEU A 1 18  ? 31.559 -25.727 18.255 1.00 18.45  ? 19  LEU A O   1 
ATOM   150  C  CB  . LEU A 1 18  ? 28.602 -24.877 17.035 1.00 18.80  ? 19  LEU A CB  1 
ATOM   151  C  CG  . LEU A 1 18  ? 28.620 -23.975 18.293 1.00 21.82  ? 19  LEU A CG  1 
ATOM   152  C  CD1 . LEU A 1 18  ? 29.159 -22.591 17.970 1.00 21.70  ? 19  LEU A CD1 1 
ATOM   153  C  CD2 . LEU A 1 18  ? 27.209 -23.850 18.873 1.00 25.94  ? 19  LEU A CD2 1 
ATOM   154  N  N   . LEU A 1 19  ? 30.444 -27.505 17.379 1.00 18.72  ? 20  LEU A N   1 
ATOM   155  C  CA  . LEU A 1 19  ? 31.115 -28.529 18.186 1.00 20.02  ? 20  LEU A CA  1 
ATOM   156  C  C   . LEU A 1 19  ? 32.627 -28.468 17.927 1.00 20.63  ? 20  LEU A C   1 
ATOM   157  O  O   . LEU A 1 19  ? 33.414 -28.448 18.884 1.00 19.30  ? 20  LEU A O   1 
ATOM   158  C  CB  . LEU A 1 19  ? 30.559 -29.910 17.828 1.00 22.21  ? 20  LEU A CB  1 
ATOM   159  C  CG  . LEU A 1 19  ? 31.181 -31.084 18.571 1.00 31.51  ? 20  LEU A CG  1 
ATOM   160  C  CD1 . LEU A 1 19  ? 30.724 -31.091 20.036 1.00 34.21  ? 20  LEU A CD1 1 
ATOM   161  C  CD2 . LEU A 1 19  ? 30.783 -32.388 17.914 1.00 36.44  ? 20  LEU A CD2 1 
ATOM   162  N  N   . ASN A 1 20  ? 33.032 -28.357 16.650 1.00 16.90  ? 21  ASN A N   1 
ATOM   163  C  CA  . ASN A 1 20  ? 34.461 -28.251 16.321 1.00 16.34  ? 21  ASN A CA  1 
ATOM   164  C  C   . ASN A 1 20  ? 35.086 -26.942 16.812 1.00 19.22  ? 21  ASN A C   1 
ATOM   165  O  O   . ASN A 1 20  ? 36.239 -26.945 17.243 1.00 18.94  ? 21  ASN A O   1 
ATOM   166  C  CB  . ASN A 1 20  ? 34.692 -28.474 14.824 1.00 16.62  ? 21  ASN A CB  1 
ATOM   167  C  CG  . ASN A 1 20  ? 34.624 -29.940 14.465 1.00 27.90  ? 21  ASN A CG  1 
ATOM   168  O  OD1 . ASN A 1 20  ? 34.782 -30.812 15.319 1.00 25.15  ? 21  ASN A OD1 1 
ATOM   169  N  ND2 . ASN A 1 20  ? 34.363 -30.248 13.205 1.00 21.84  ? 21  ASN A ND2 1 
ATOM   170  N  N   . LEU A 1 21  ? 34.345 -25.816 16.730 1.00 17.16  ? 22  LEU A N   1 
ATOM   171  C  CA  . LEU A 1 21  ? 34.852 -24.547 17.246 1.00 16.71  ? 22  LEU A CA  1 
ATOM   172  C  C   . LEU A 1 21  ? 35.066 -24.684 18.762 1.00 18.48  ? 22  LEU A C   1 
ATOM   173  O  O   . LEU A 1 21  ? 36.050 -24.166 19.291 1.00 17.24  ? 22  LEU A O   1 
ATOM   174  C  CB  . LEU A 1 21  ? 33.876 -23.390 16.937 1.00 16.47  ? 22  LEU A CB  1 
ATOM   175  C  CG  . LEU A 1 21  ? 33.771 -23.053 15.426 1.00 18.41  ? 22  LEU A CG  1 
ATOM   176  C  CD1 . LEU A 1 21  ? 32.702 -21.987 15.195 1.00 18.84  ? 22  LEU A CD1 1 
ATOM   177  C  CD2 . LEU A 1 21  ? 35.140 -22.632 14.826 1.00 21.75  ? 22  LEU A CD2 1 
ATOM   178  N  N   . ASN A 1 22  ? 34.144 -25.378 19.457 1.00 16.54  ? 23  ASN A N   1 
ATOM   179  C  CA  . ASN A 1 22  ? 34.318 -25.570 20.913 1.00 17.71  ? 23  ASN A CA  1 
ATOM   180  C  C   . ASN A 1 22  ? 35.551 -26.463 21.219 1.00 22.37  ? 23  ASN A C   1 
ATOM   181  O  O   . ASN A 1 22  ? 36.265 -26.223 22.197 1.00 22.69  ? 23  ASN A O   1 
ATOM   182  C  CB  . ASN A 1 22  ? 33.053 -26.130 21.545 1.00 20.68  ? 23  ASN A CB  1 
ATOM   183  C  CG  . ASN A 1 22  ? 33.074 -26.010 23.053 1.00 25.90  ? 23  ASN A CG  1 
ATOM   184  O  OD1 . ASN A 1 22  ? 33.564 -25.032 23.614 1.00 24.43  ? 23  ASN A OD1 1 
ATOM   185  N  ND2 . ASN A 1 22  ? 32.550 -27.005 23.713 1.00 28.55  ? 23  ASN A ND2 1 
ATOM   186  N  N   . ARG A 1 23  ? 35.812 -27.476 20.372 1.00 19.82  ? 24  ARG A N   1 
ATOM   187  C  CA  . ARG A 1 23  ? 37.007 -28.334 20.517 1.00 19.55  ? 24  ARG A CA  1 
ATOM   188  C  C   . ARG A 1 23  ? 38.276 -27.496 20.340 1.00 23.88  ? 24  ARG A C   1 
ATOM   189  O  O   . ARG A 1 23  ? 39.222 -27.683 21.087 1.00 23.68  ? 24  ARG A O   1 
ATOM   190  C  CB  . ARG A 1 23  ? 37.002 -29.480 19.497 1.00 20.58  ? 24  ARG A CB  1 
ATOM   191  C  CG  . ARG A 1 23  ? 35.973 -30.554 19.818 1.00 26.10  ? 24  ARG A CG  1 
ATOM   192  C  CD  . ARG A 1 23  ? 35.730 -31.452 18.613 1.00 30.55  ? 24  ARG A CD  1 
ATOM   193  N  NE  . ARG A 1 23  ? 34.885 -32.593 18.951 1.00 37.65  ? 24  ARG A NE  1 
ATOM   194  C  CZ  . ARG A 1 23  ? 34.403 -33.467 18.073 1.00 56.41  ? 24  ARG A CZ  1 
ATOM   195  N  NH1 . ARG A 1 23  ? 34.622 -33.304 16.771 1.00 40.52  ? 24  ARG A NH1 1 
ATOM   196  N  NH2 . ARG A 1 23  ? 33.682 -34.499 18.487 1.00 45.06  ? 24  ARG A NH2 1 
ATOM   197  N  N   . LEU A 1 24  ? 38.281 -26.541 19.384 1.00 20.66  ? 25  LEU A N   1 
ATOM   198  C  CA  . LEU A 1 24  ? 39.434 -25.650 19.207 1.00 20.25  ? 25  LEU A CA  1 
ATOM   199  C  C   . LEU A 1 24  ? 39.591 -24.789 20.467 1.00 24.59  ? 25  LEU A C   1 
ATOM   200  O  O   . LEU A 1 24  ? 40.716 -24.625 20.960 1.00 24.75  ? 25  LEU A O   1 
ATOM   201  C  CB  . LEU A 1 24  ? 39.253 -24.749 17.986 1.00 19.92  ? 25  LEU A CB  1 
ATOM   202  C  CG  . LEU A 1 24  ? 39.226 -25.447 16.607 1.00 24.04  ? 25  LEU A CG  1 
ATOM   203  C  CD1 . LEU A 1 24  ? 39.090 -24.407 15.486 1.00 24.00  ? 25  LEU A CD1 1 
ATOM   204  C  CD2 . LEU A 1 24  ? 40.473 -26.312 16.389 1.00 25.99  ? 25  LEU A CD2 1 
ATOM   205  N  N   . ARG A 1 25  ? 38.465 -24.251 21.000 1.00 20.72  ? 26  ARG A N   1 
ATOM   206  C  CA  . ARG A 1 25  ? 38.530 -23.456 22.238 1.00 21.43  ? 26  ARG A CA  1 
ATOM   207  C  C   . ARG A 1 25  ? 39.147 -24.272 23.413 1.00 26.02  ? 26  ARG A C   1 
ATOM   208  O  O   . ARG A 1 25  ? 40.037 -23.754 24.116 1.00 26.43  ? 26  ARG A O   1 
ATOM   209  C  CB  . ARG A 1 25  ? 37.135 -22.927 22.629 1.00 21.43  ? 26  ARG A CB  1 
ATOM   210  C  CG  . ARG A 1 25  ? 37.220 -22.072 23.904 1.00 27.35  ? 26  ARG A CG  1 
ATOM   211  C  CD  . ARG A 1 25  ? 35.905 -21.429 24.240 1.00 27.57  ? 26  ARG A CD  1 
ATOM   212  N  NE  . ARG A 1 25  ? 34.885 -22.401 24.621 1.00 26.83  ? 26  ARG A NE  1 
ATOM   213  C  CZ  . ARG A 1 25  ? 34.287 -22.447 25.807 1.00 37.51  ? 26  ARG A CZ  1 
ATOM   214  N  NH1 . ARG A 1 25  ? 34.666 -21.629 26.784 1.00 31.26  ? 26  ARG A NH1 1 
ATOM   215  N  NH2 . ARG A 1 25  ? 33.329 -23.333 26.038 1.00 28.98  ? 26  ARG A NH2 1 
ATOM   216  N  N   A SER A 1 26  ? 38.664 -25.504 23.627 0.40 23.81  ? 27  SER A N   1 
ATOM   217  N  N   B SER A 1 26  ? 38.666 -25.514 23.622 0.35 23.69  ? 27  SER A N   1 
ATOM   218  N  N   C SER A 1 26  ? 38.667 -25.517 23.617 0.25 23.43  ? 27  SER A N   1 
ATOM   219  C  CA  A SER A 1 26  ? 39.147 -26.391 24.692 0.40 25.49  ? 27  SER A CA  1 
ATOM   220  C  CA  B SER A 1 26  ? 39.123 -26.410 24.696 0.35 25.27  ? 27  SER A CA  1 
ATOM   221  C  CA  C SER A 1 26  ? 39.111 -26.438 24.677 0.25 24.83  ? 27  SER A CA  1 
ATOM   222  C  C   A SER A 1 26  ? 40.657 -26.568 24.613 0.40 30.17  ? 27  SER A C   1 
ATOM   223  C  C   B SER A 1 26  ? 40.617 -26.735 24.613 0.35 30.56  ? 27  SER A C   1 
ATOM   224  C  C   C SER A 1 26  ? 40.609 -26.746 24.607 0.25 30.27  ? 27  SER A C   1 
ATOM   225  O  O   A SER A 1 26  ? 41.347 -26.470 25.631 0.40 30.90  ? 27  SER A O   1 
ATOM   226  O  O   B SER A 1 26  ? 41.256 -26.941 25.648 0.35 31.85  ? 27  SER A O   1 
ATOM   227  O  O   C SER A 1 26  ? 41.237 -26.963 25.645 0.25 31.39  ? 27  SER A O   1 
ATOM   228  C  CB  A SER A 1 26  ? 38.488 -27.762 24.582 0.40 29.51  ? 27  SER A CB  1 
ATOM   229  C  CB  B SER A 1 26  ? 38.290 -27.688 24.733 0.35 28.74  ? 27  SER A CB  1 
ATOM   230  C  CB  C SER A 1 26  ? 38.308 -27.734 24.627 0.25 28.10  ? 27  SER A CB  1 
ATOM   231  O  OG  A SER A 1 26  ? 37.104 -27.710 24.876 0.40 37.63  ? 27  SER A OG  1 
ATOM   232  O  OG  B SER A 1 26  ? 38.577 -28.564 23.655 0.35 35.19  ? 27  SER A OG  1 
ATOM   233  O  OG  C SER A 1 26  ? 38.712 -28.647 25.635 0.25 35.39  ? 27  SER A OG  1 
ATOM   234  N  N   . ARG A 1 27  ? 41.169 -26.777 23.388 1.00 26.63  ? 28  ARG A N   1 
ATOM   235  C  CA  . ARG A 1 27  ? 42.594 -27.046 23.144 1.00 28.46  ? 28  ARG A CA  1 
ATOM   236  C  C   . ARG A 1 27  ? 43.402 -25.768 22.944 1.00 31.16  ? 28  ARG A C   1 
ATOM   237  O  O   . ARG A 1 27  ? 44.610 -25.834 22.697 1.00 32.12  ? 28  ARG A O   1 
ATOM   238  C  CB  . ARG A 1 27  ? 42.731 -28.009 21.968 1.00 31.22  ? 28  ARG A CB  1 
ATOM   239  C  CG  . ARG A 1 27  ? 41.971 -29.312 22.199 1.00 41.21  ? 28  ARG A CG  1 
ATOM   240  C  CD  . ARG A 1 27  ? 41.980 -30.187 20.972 1.00 49.30  ? 28  ARG A CD  1 
ATOM   241  N  NE  . ARG A 1 27  ? 43.309 -30.756 20.750 1.00 66.48  ? 28  ARG A NE  1 
ATOM   242  C  CZ  . ARG A 1 27  ? 43.847 -30.937 19.552 1.00 82.32  ? 28  ARG A CZ  1 
ATOM   243  N  NH1 . ARG A 1 27  ? 45.060 -31.457 19.434 1.00 72.27  ? 28  ARG A NH1 1 
ATOM   244  N  NH2 . ARG A 1 27  ? 43.180 -30.595 18.462 1.00 67.74  ? 28  ARG A NH2 1 
ATOM   245  N  N   . ASP A 1 28  ? 42.744 -24.604 23.100 1.00 25.47  ? 29  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 28  ? 43.342 -23.273 22.953 1.00 26.49  ? 29  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 28  ? 43.961 -23.066 21.550 1.00 31.15  ? 29  ASP A C   1 
ATOM   248  O  O   . ASP A 1 28  ? 45.016 -22.439 21.399 1.00 32.24  ? 29  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 28  ? 44.363 -22.982 24.091 1.00 29.45  ? 29  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 28  ? 44.674 -21.513 24.250 1.00 37.66  ? 29  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 28  ? 43.753 -20.684 24.048 1.00 37.39  ? 29  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 28  ? 45.835 -21.187 24.564 1.00 43.37  ? 29  ASP A OD2 1 
ATOM   253  N  N   . ILE A 1 29  ? 43.308 -23.621 20.533 1.00 24.72  ? 30  ILE A N   1 
ATOM   254  C  CA  . ILE A 1 29  ? 43.775 -23.528 19.149 1.00 24.01  ? 30  ILE A CA  1 
ATOM   255  C  C   . ILE A 1 29  ? 43.184 -22.318 18.441 1.00 25.96  ? 30  ILE A C   1 
ATOM   256  O  O   . ILE A 1 29  ? 41.955 -22.181 18.353 1.00 22.30  ? 30  ILE A O   1 
ATOM   257  C  CB  . ILE A 1 29  ? 43.527 -24.838 18.359 1.00 26.86  ? 30  ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 29  ? 44.320 -26.022 18.978 1.00 28.36  ? 30  ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 29  ? 43.862 -24.666 16.848 1.00 25.54  ? 30  ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 29  ? 43.812 -27.405 18.480 1.00 29.33  ? 30  ILE A CD1 1 
ATOM   261  N  N   A LEU A 1 30  ? 44.066 -21.434 17.936 0.54 23.93  ? 31  LEU A N   1 
ATOM   262  N  N   B LEU A 1 30  ? 44.074 -21.438 17.941 0.46 24.42  ? 31  LEU A N   1 
ATOM   263  C  CA  A LEU A 1 30  ? 43.708 -20.233 17.170 0.54 23.85  ? 31  LEU A CA  1 
ATOM   264  C  CA  B LEU A 1 30  ? 43.754 -20.224 17.186 0.46 24.61  ? 31  LEU A CA  1 
ATOM   265  C  C   A LEU A 1 30  ? 42.826 -19.233 17.925 0.54 25.80  ? 31  LEU A C   1 
ATOM   266  C  C   B LEU A 1 30  ? 42.842 -19.235 17.923 0.46 26.34  ? 31  LEU A C   1 
ATOM   267  O  O   A LEU A 1 30  ? 42.208 -18.365 17.299 0.54 23.55  ? 31  LEU A O   1 
ATOM   268  O  O   B LEU A 1 30  ? 42.221 -18.377 17.287 0.46 24.38  ? 31  LEU A O   1 
ATOM   269  C  CB  A LEU A 1 30  ? 43.086 -20.581 15.802 0.54 23.90  ? 31  LEU A CB  1 
ATOM   270  C  CB  B LEU A 1 30  ? 43.205 -20.545 15.793 0.46 24.91  ? 31  LEU A CB  1 
ATOM   271  C  CG  A LEU A 1 30  ? 44.011 -21.230 14.739 0.54 29.31  ? 31  LEU A CG  1 
ATOM   272  C  CG  B LEU A 1 30  ? 44.236 -20.365 14.685 0.46 30.79  ? 31  LEU A CG  1 
ATOM   273  C  CD1 A LEU A 1 30  ? 43.506 -20.931 13.369 0.54 27.70  ? 31  LEU A CD1 1 
ATOM   274  C  CD1 B LEU A 1 30  ? 44.677 -21.704 14.113 0.46 31.36  ? 31  LEU A CD1 1 
ATOM   275  C  CD2 A LEU A 1 30  ? 45.448 -20.729 14.823 0.54 32.20  ? 31  LEU A CD2 1 
ATOM   276  C  CD2 B LEU A 1 30  ? 43.707 -19.457 13.607 0.46 32.81  ? 31  LEU A CD2 1 
ATOM   277  N  N   . THR A 1 31  ? 42.828 -19.296 19.266 1.00 23.16  ? 32  THR A N   1 
ATOM   278  C  CA  . THR A 1 31  ? 42.106 -18.305 20.090 1.00 22.69  ? 32  THR A CA  1 
ATOM   279  C  C   . THR A 1 31  ? 42.922 -17.011 19.896 1.00 27.47  ? 32  THR A C   1 
ATOM   280  O  O   . THR A 1 31  ? 44.154 -17.061 19.744 1.00 28.09  ? 32  THR A O   1 
ATOM   281  C  CB  . THR A 1 31  ? 42.069 -18.718 21.565 1.00 28.75  ? 32  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 31  ? 43.388 -19.085 21.943 1.00 30.97  ? 32  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 31  ? 41.102 -19.888 21.813 1.00 26.69  ? 32  THR A CG2 1 
ATOM   284  N  N   . ASP A 1 32  ? 42.237 -15.893 19.736 1.00 23.91  ? 33  ASP A N   1 
ATOM   285  C  CA  . ASP A 1 32  ? 42.911 -14.640 19.399 1.00 24.22  ? 33  ASP A CA  1 
ATOM   286  C  C   . ASP A 1 32  ? 42.576 -13.486 20.307 1.00 26.27  ? 33  ASP A C   1 
ATOM   287  O  O   . ASP A 1 32  ? 42.919 -12.341 19.997 1.00 25.75  ? 33  ASP A O   1 
ATOM   288  C  CB  . ASP A 1 32  ? 42.602 -14.276 17.940 1.00 25.53  ? 33  ASP A CB  1 
ATOM   289  C  CG  . ASP A 1 32  ? 41.116 -14.306 17.585 1.00 33.88  ? 33  ASP A CG  1 
ATOM   290  O  OD1 . ASP A 1 32  ? 40.274 -14.350 18.516 1.00 30.87  ? 33  ASP A OD1 1 
ATOM   291  O  OD2 . ASP A 1 32  ? 40.800 -14.302 16.387 1.00 41.96  ? 33  ASP A OD2 1 
ATOM   292  N  N   . VAL A 1 33  ? 41.926 -13.772 21.436 1.00 22.06  ? 34  VAL A N   1 
ATOM   293  C  CA  . VAL A 1 33  ? 41.604 -12.722 22.411 1.00 21.01  ? 34  VAL A CA  1 
ATOM   294  C  C   . VAL A 1 33  ? 41.427 -13.321 23.792 1.00 24.79  ? 34  VAL A C   1 
ATOM   295  O  O   . VAL A 1 33  ? 41.019 -14.492 23.921 1.00 24.78  ? 34  VAL A O   1 
ATOM   296  C  CB  . VAL A 1 33  ? 40.330 -11.897 21.979 1.00 23.76  ? 34  VAL A CB  1 
ATOM   297  C  CG1 . VAL A 1 33  ? 39.022 -12.700 22.132 1.00 21.91  ? 34  VAL A CG1 1 
ATOM   298  C  CG2 . VAL A 1 33  ? 40.239 -10.547 22.717 1.00 24.16  ? 34  VAL A CG2 1 
ATOM   299  N  N   A VAL A 1 34  ? 41.714 -12.505 24.818 0.53 22.36  ? 35  VAL A N   1 
ATOM   300  N  N   B VAL A 1 34  ? 41.722 -12.523 24.824 0.47 22.59  ? 35  VAL A N   1 
ATOM   301  C  CA  A VAL A 1 34  ? 41.495 -12.811 26.225 0.53 22.14  ? 35  VAL A CA  1 
ATOM   302  C  CA  B VAL A 1 34  ? 41.454 -12.885 26.204 0.47 22.48  ? 35  VAL A CA  1 
ATOM   303  C  C   A VAL A 1 34  ? 40.431 -11.820 26.705 0.53 25.06  ? 35  VAL A C   1 
ATOM   304  C  C   B VAL A 1 34  ? 40.478 -11.848 26.779 0.47 25.47  ? 35  VAL A C   1 
ATOM   305  O  O   A VAL A 1 34  ? 40.580 -10.610 26.500 0.53 25.08  ? 35  VAL A O   1 
ATOM   306  O  O   B VAL A 1 34  ? 40.703 -10.640 26.657 0.47 25.72  ? 35  VAL A O   1 
ATOM   307  C  CB  A VAL A 1 34  ? 42.795 -12.695 27.072 0.53 27.08  ? 35  VAL A CB  1 
ATOM   308  C  CB  B VAL A 1 34  ? 42.701 -13.181 27.086 0.47 27.54  ? 35  VAL A CB  1 
ATOM   309  C  CG1 A VAL A 1 34  ? 42.525 -12.925 28.561 0.53 26.93  ? 35  VAL A CG1 1 
ATOM   310  C  CG1 B VAL A 1 34  ? 43.584 -11.953 27.279 0.47 28.20  ? 35  VAL A CG1 1 
ATOM   311  C  CG2 A VAL A 1 34  ? 43.861 -13.655 26.575 0.53 27.63  ? 35  VAL A CG2 1 
ATOM   312  C  CG2 B VAL A 1 34  ? 42.298 -13.774 28.432 0.47 27.74  ? 35  VAL A CG2 1 
ATOM   313  N  N   . ILE A 1 35  ? 39.359 -12.331 27.318 1.00 21.57  ? 36  ILE A N   1 
ATOM   314  C  CA  . ILE A 1 35  ? 38.315 -11.508 27.917 1.00 20.68  ? 36  ILE A CA  1 
ATOM   315  C  C   . ILE A 1 35  ? 38.602 -11.539 29.420 1.00 25.74  ? 36  ILE A C   1 
ATOM   316  O  O   . ILE A 1 35  ? 38.636 -12.624 30.024 1.00 24.91  ? 36  ILE A O   1 
ATOM   317  C  CB  . ILE A 1 35  ? 36.870 -11.998 27.604 1.00 21.88  ? 36  ILE A CB  1 
ATOM   318  C  CG1 . ILE A 1 35  ? 36.641 -12.160 26.068 1.00 21.43  ? 36  ILE A CG1 1 
ATOM   319  C  CG2 . ILE A 1 35  ? 35.847 -11.049 28.222 1.00 23.25  ? 36  ILE A CG2 1 
ATOM   320  C  CD1 . ILE A 1 35  ? 36.947 -10.897 25.185 1.00 21.93  ? 36  ILE A CD1 1 
ATOM   321  N  N   . VAL A 1 36  ? 38.827 -10.359 29.999 1.00 22.76  ? 37  VAL A N   1 
ATOM   322  C  CA  . VAL A 1 36  ? 39.144 -10.219 31.430 1.00 23.56  ? 37  VAL A CA  1 
ATOM   323  C  C   . VAL A 1 36  ? 37.880 -9.782  32.169 1.00 28.34  ? 37  VAL A C   1 
ATOM   324  O  O   . VAL A 1 36  ? 37.291 -8.732  31.852 1.00 26.85  ? 37  VAL A O   1 
ATOM   325  C  CB  . VAL A 1 36  ? 40.338 -9.245  31.668 1.00 28.13  ? 37  VAL A CB  1 
ATOM   326  C  CG1 . VAL A 1 36  ? 40.660 -9.102  33.161 1.00 28.75  ? 37  VAL A CG1 1 
ATOM   327  C  CG2 . VAL A 1 36  ? 41.582 -9.704  30.915 1.00 28.94  ? 37  VAL A CG2 1 
ATOM   328  N  N   . VAL A 1 37  ? 37.495 -10.561 33.197 1.00 25.24  ? 38  VAL A N   1 
ATOM   329  C  CA  . VAL A 1 37  ? 36.297 -10.317 34.004 1.00 24.79  ? 38  VAL A CA  1 
ATOM   330  C  C   . VAL A 1 37  ? 36.771 -10.380 35.448 1.00 30.18  ? 38  VAL A C   1 
ATOM   331  O  O   . VAL A 1 37  ? 37.015 -11.472 35.958 1.00 28.18  ? 38  VAL A O   1 
ATOM   332  C  CB  . VAL A 1 37  ? 35.185 -11.350 33.672 1.00 27.71  ? 38  VAL A CB  1 
ATOM   333  C  CG1 . VAL A 1 37  ? 33.859 -10.953 34.308 1.00 27.92  ? 38  VAL A CG1 1 
ATOM   334  C  CG2 . VAL A 1 37  ? 35.026 -11.511 32.154 1.00 26.14  ? 38  VAL A CG2 1 
ATOM   335  N  N   A SER A 1 38  ? 36.668 -9.276  36.216 0.50 30.37  ? 39  SER A N   1 
ATOM   336  N  N   B SER A 1 38  ? 37.305 -9.187  35.832 0.50 26.69  ? 39  SER A N   1 
ATOM   337  C  CA  A SER A 1 38  ? 37.036 -9.273  37.651 0.50 31.96  ? 39  SER A CA  1 
ATOM   338  C  CA  B SER A 1 38  ? 37.983 -8.815  37.062 0.50 26.92  ? 39  SER A CA  1 
ATOM   339  C  C   A SER A 1 38  ? 38.283 -10.164 37.954 0.50 36.26  ? 39  SER A C   1 
ATOM   340  C  C   B SER A 1 38  ? 39.260 -9.642  37.228 0.50 29.80  ? 39  SER A C   1 
ATOM   341  O  O   A SER A 1 38  ? 38.229 -11.028 38.834 0.50 36.24  ? 39  SER A O   1 
ATOM   342  O  O   B SER A 1 38  ? 40.194 -9.418  36.459 0.50 28.43  ? 39  SER A O   1 
ATOM   343  C  CB  A SER A 1 38  ? 35.845 -9.697  38.519 0.50 37.30  ? 39  SER A CB  1 
ATOM   344  C  CB  B SER A 1 38  ? 37.037 -8.849  38.256 0.50 31.61  ? 39  SER A CB  1 
ATOM   345  O  OG  A SER A 1 38  ? 34.786 -8.751  38.503 0.50 49.39  ? 39  SER A OG  1 
ATOM   346  O  OG  B SER A 1 38  ? 36.075 -7.819  38.097 0.50 38.19  ? 39  SER A OG  1 
ATOM   347  N  N   A ARG A 1 39  ? 39.370 -9.984  37.159 0.50 32.55  ? 40  ARG A N   1 
ATOM   348  N  N   B ARG A 1 39  ? 39.315 -10.612 38.157 0.50 27.22  ? 40  ARG A N   1 
ATOM   349  C  CA  A ARG A 1 39  ? 40.646 -10.724 37.231 0.50 33.27  ? 40  ARG A CA  1 
ATOM   350  C  CA  B ARG A 1 39  ? 40.541 -11.405 38.277 0.50 28.04  ? 40  ARG A CA  1 
ATOM   351  C  C   A ARG A 1 39  ? 40.501 -12.262 36.989 0.50 35.54  ? 40  ARG A C   1 
ATOM   352  C  C   B ARG A 1 39  ? 40.666 -12.415 37.098 0.50 32.79  ? 40  ARG A C   1 
ATOM   353  O  O   A ARG A 1 39  ? 41.251 -13.086 37.552 0.50 36.31  ? 40  ARG A O   1 
ATOM   354  O  O   B ARG A 1 39  ? 41.678 -12.408 36.379 0.50 32.99  ? 40  ARG A O   1 
ATOM   355  C  CB  A ARG A 1 39  ? 41.428 -10.428 38.526 0.50 35.18  ? 40  ARG A CB  1 
ATOM   356  C  CB  B ARG A 1 39  ? 40.683 -12.046 39.679 0.50 29.05  ? 40  ARG A CB  1 
ATOM   357  C  CG  A ARG A 1 39  ? 41.948 -9.002  38.647 0.50 45.80  ? 40  ARG A CG  1 
ATOM   358  C  CG  B ARG A 1 39  ? 40.954 -11.004 40.779 0.50 35.36  ? 40  ARG A CG  1 
ATOM   359  C  CD  A ARG A 1 39  ? 43.040 -8.932  39.698 0.50 52.48  ? 40  ARG A CD  1 
ATOM   360  C  CD  B ARG A 1 39  ? 41.328 -11.597 42.131 0.50 36.25  ? 40  ARG A CD  1 
ATOM   361  N  NE  A ARG A 1 39  ? 43.387 -7.559  40.070 0.50 58.73  ? 40  ARG A NE  1 
ATOM   362  N  NE  B ARG A 1 39  ? 41.484 -10.567 43.160 0.50 36.53  ? 40  ARG A NE  1 
ATOM   363  C  CZ  A ARG A 1 39  ? 42.805 -6.874  41.050 0.50 70.75  ? 40  ARG A CZ  1 
ATOM   364  C  CZ  B ARG A 1 39  ? 42.643 -10.022 43.526 0.50 50.79  ? 40  ARG A CZ  1 
ATOM   365  N  NH1 A ARG A 1 39  ? 41.817 -7.415  41.754 0.50 53.79  ? 40  ARG A NH1 1 
ATOM   366  N  NH1 B ARG A 1 39  ? 43.775 -10.391 42.941 0.50 36.94  ? 40  ARG A NH1 1 
ATOM   367  N  NH2 A ARG A 1 39  ? 43.196 -5.636  41.325 0.50 59.09  ? 40  ARG A NH2 1 
ATOM   368  N  NH2 B ARG A 1 39  ? 42.677 -9.099  44.475 0.50 44.21  ? 40  ARG A NH2 1 
ATOM   369  N  N   A GLU A 1 40  ? 39.536 -12.632 36.145 0.50 28.38  ? 41  GLU A N   1 
ATOM   370  N  N   B GLU A 1 40  ? 39.588 -13.171 36.832 0.50 27.32  ? 41  GLU A N   1 
ATOM   371  C  CA  A GLU A 1 40  ? 39.325 -13.998 35.672 0.50 27.39  ? 41  GLU A CA  1 
ATOM   372  C  CA  B GLU A 1 40  ? 39.529 -14.235 35.823 0.50 25.75  ? 41  GLU A CA  1 
ATOM   373  C  C   A GLU A 1 40  ? 39.468 -13.865 34.165 0.50 28.83  ? 41  GLU A C   1 
ATOM   374  C  C   B GLU A 1 40  ? 39.771 -13.783 34.371 0.50 27.45  ? 41  GLU A C   1 
ATOM   375  O  O   A GLU A 1 40  ? 38.898 -12.944 33.573 0.50 26.23  ? 41  GLU A O   1 
ATOM   376  O  O   B GLU A 1 40  ? 39.482 -12.648 33.998 0.50 24.41  ? 41  GLU A O   1 
ATOM   377  C  CB  A GLU A 1 40  ? 37.957 -14.568 36.088 0.50 28.62  ? 41  GLU A CB  1 
ATOM   378  C  CB  B GLU A 1 40  ? 38.200 -15.014 35.928 0.50 26.83  ? 41  GLU A CB  1 
ATOM   379  C  CG  A GLU A 1 40  ? 37.856 -14.799 37.590 0.50 41.47  ? 41  GLU A CG  1 
ATOM   380  C  CG  B GLU A 1 40  ? 37.726 -15.198 37.367 0.50 41.60  ? 41  GLU A CG  1 
ATOM   381  C  CD  A GLU A 1 40  ? 37.838 -16.247 38.038 0.50 75.72  ? 41  GLU A CD  1 
ATOM   382  C  CD  B GLU A 1 40  ? 37.897 -16.560 38.012 0.50 78.66  ? 41  GLU A CD  1 
ATOM   383  O  OE1 A GLU A 1 40  ? 36.810 -16.675 38.610 0.50 78.34  ? 41  GLU A OE1 1 
ATOM   384  O  OE1 B GLU A 1 40  ? 38.957 -17.198 37.816 0.50 80.38  ? 41  GLU A OE1 1 
ATOM   385  O  OE2 A GLU A 1 40  ? 38.854 -16.951 37.830 0.50 75.58  ? 41  GLU A OE2 1 
ATOM   386  O  OE2 B GLU A 1 40  ? 36.969 -16.979 38.743 0.50 80.22  ? 41  GLU A OE2 1 
ATOM   387  N  N   . GLN A 1 41  ? 40.295 -14.719 33.556 1.00 25.26  ? 42  GLN A N   1 
ATOM   388  C  CA  . GLN A 1 41  ? 40.622 -14.568 32.145 1.00 24.91  ? 42  GLN A CA  1 
ATOM   389  C  C   . GLN A 1 41  ? 40.004 -15.679 31.341 1.00 28.21  ? 42  GLN A C   1 
ATOM   390  O  O   . GLN A 1 41  ? 40.059 -16.833 31.762 1.00 28.37  ? 42  GLN A O   1 
ATOM   391  C  CB  . GLN A 1 41  ? 42.155 -14.573 31.991 1.00 27.63  ? 42  GLN A CB  1 
ATOM   392  C  CG  . GLN A 1 41  ? 42.815 -13.317 32.549 1.00 44.14  ? 42  GLN A CG  1 
ATOM   393  C  CD  . GLN A 1 41  ? 44.285 -13.197 32.229 1.00 63.02  ? 42  GLN A CD  1 
ATOM   394  O  OE1 . GLN A 1 41  ? 44.872 -13.992 31.480 1.00 56.55  ? 42  GLN A OE1 1 
ATOM   395  N  NE2 . GLN A 1 41  ? 44.910 -12.181 32.794 1.00 66.44  ? 42  GLN A NE2 1 
ATOM   396  N  N   . PHE A 1 42  ? 39.416 -15.337 30.179 1.00 22.70  ? 43  PHE A N   1 
ATOM   397  C  CA  . PHE A 1 42  ? 38.775 -16.324 29.309 1.00 22.34  ? 43  PHE A CA  1 
ATOM   398  C  C   . PHE A 1 42  ? 39.295 -16.169 27.894 1.00 26.60  ? 43  PHE A C   1 
ATOM   399  O  O   . PHE A 1 42  ? 39.148 -15.099 27.309 1.00 26.62  ? 43  PHE A O   1 
ATOM   400  C  CB  . PHE A 1 42  ? 37.244 -16.130 29.316 1.00 23.51  ? 43  PHE A CB  1 
ATOM   401  C  CG  . PHE A 1 42  ? 36.626 -16.252 30.687 1.00 25.37  ? 43  PHE A CG  1 
ATOM   402  C  CD1 . PHE A 1 42  ? 36.493 -15.138 31.512 1.00 26.56  ? 43  PHE A CD1 1 
ATOM   403  C  CD2 . PHE A 1 42  ? 36.135 -17.475 31.138 1.00 27.11  ? 43  PHE A CD2 1 
ATOM   404  C  CE1 . PHE A 1 42  ? 35.938 -15.255 32.791 1.00 28.80  ? 43  PHE A CE1 1 
ATOM   405  C  CE2 . PHE A 1 42  ? 35.569 -17.589 32.411 1.00 30.13  ? 43  PHE A CE2 1 
ATOM   406  C  CZ  . PHE A 1 42  ? 35.463 -16.477 33.227 1.00 28.26  ? 43  PHE A CZ  1 
ATOM   407  N  N   . ARG A 1 43  ? 39.902 -17.224 27.343 1.00 22.97  ? 44  ARG A N   1 
ATOM   408  C  CA  . ARG A 1 43  ? 40.408 -17.181 25.966 1.00 21.72  ? 44  ARG A CA  1 
ATOM   409  C  C   . ARG A 1 43  ? 39.273 -17.568 25.010 1.00 25.71  ? 44  ARG A C   1 
ATOM   410  O  O   . ARG A 1 43  ? 38.474 -18.463 25.310 1.00 24.66  ? 44  ARG A O   1 
ATOM   411  C  CB  . ARG A 1 43  ? 41.641 -18.103 25.796 1.00 23.74  ? 44  ARG A CB  1 
ATOM   412  C  CG  . ARG A 1 43  ? 42.867 -17.686 26.653 1.00 32.93  ? 44  ARG A CG  1 
ATOM   413  C  CD  . ARG A 1 43  ? 44.191 -18.130 26.021 1.00 41.40  ? 44  ARG A CD  1 
ATOM   414  N  NE  . ARG A 1 43  ? 44.233 -17.750 24.602 1.00 52.19  ? 44  ARG A NE  1 
ATOM   415  C  CZ  . ARG A 1 43  ? 44.794 -16.645 24.119 1.00 65.30  ? 44  ARG A CZ  1 
ATOM   416  N  NH1 . ARG A 1 43  ? 45.468 -15.831 24.918 1.00 57.82  ? 44  ARG A NH1 1 
ATOM   417  N  NH2 . ARG A 1 43  ? 44.730 -16.374 22.824 1.00 48.86  ? 44  ARG A NH2 1 
ATOM   418  N  N   . ALA A 1 44  ? 39.181 -16.905 23.854 1.00 21.62  ? 45  ALA A N   1 
ATOM   419  C  CA  . ALA A 1 44  ? 38.098 -17.220 22.910 1.00 21.02  ? 45  ALA A CA  1 
ATOM   420  C  C   . ALA A 1 44  ? 38.511 -16.817 21.511 1.00 22.27  ? 45  ALA A C   1 
ATOM   421  O  O   . ALA A 1 44  ? 39.607 -16.254 21.316 1.00 21.58  ? 45  ALA A O   1 
ATOM   422  C  CB  . ALA A 1 44  ? 36.817 -16.471 23.310 1.00 21.41  ? 45  ALA A CB  1 
ATOM   423  N  N   . HIS A 1 45  ? 37.616 -17.058 20.557 1.00 19.27  ? 46  HIS A N   1 
ATOM   424  C  CA  . HIS A 1 45  ? 37.789 -16.651 19.167 1.00 18.17  ? 46  HIS A CA  1 
ATOM   425  C  C   . HIS A 1 45  ? 36.894 -15.414 18.965 1.00 21.44  ? 46  HIS A C   1 
ATOM   426  O  O   . HIS A 1 45  ? 35.680 -15.467 19.224 1.00 20.73  ? 46  HIS A O   1 
ATOM   427  C  CB  . HIS A 1 45  ? 37.331 -17.765 18.214 1.00 17.53  ? 46  HIS A CB  1 
ATOM   428  C  CG  . HIS A 1 45  ? 38.071 -19.055 18.408 1.00 21.11  ? 46  HIS A CG  1 
ATOM   429  N  ND1 . HIS A 1 45  ? 37.538 -20.091 19.159 1.00 22.57  ? 46  HIS A ND1 1 
ATOM   430  C  CD2 . HIS A 1 45  ? 39.318 -19.408 17.997 1.00 22.29  ? 46  HIS A CD2 1 
ATOM   431  C  CE1 . HIS A 1 45  ? 38.465 -21.044 19.171 1.00 21.94  ? 46  HIS A CE1 1 
ATOM   432  N  NE2 . HIS A 1 45  ? 39.550 -20.679 18.479 1.00 21.92  ? 46  HIS A NE2 1 
ATOM   433  N  N   . LYS A 1 46  ? 37.493 -14.302 18.536 1.00 18.91  ? 47  LYS A N   1 
ATOM   434  C  CA  . LYS A 1 46  ? 36.735 -13.067 18.253 1.00 19.67  ? 47  LYS A CA  1 
ATOM   435  C  C   . LYS A 1 46  ? 35.506 -13.327 17.382 1.00 21.94  ? 47  LYS A C   1 
ATOM   436  O  O   . LYS A 1 46  ? 34.430 -12.821 17.695 1.00 19.80  ? 47  LYS A O   1 
ATOM   437  C  CB  . LYS A 1 46  ? 37.627 -12.040 17.539 1.00 22.46  ? 47  LYS A CB  1 
ATOM   438  C  CG  . LYS A 1 46  ? 38.673 -11.431 18.459 1.00 23.94  ? 47  LYS A CG  1 
ATOM   439  C  CD  . LYS A 1 46  ? 39.596 -10.524 17.665 1.00 22.83  ? 47  LYS A CD  1 
ATOM   440  C  CE  . LYS A 1 46  ? 40.754 -10.081 18.528 1.00 26.02  ? 47  LYS A CE  1 
ATOM   441  N  NZ  . LYS A 1 46  ? 41.655 -9.153  17.794 1.00 29.11  ? 47  LYS A NZ  1 
ATOM   442  N  N   . THR A 1 47  ? 35.654 -14.109 16.290 1.00 19.84  ? 48  THR A N   1 
ATOM   443  C  CA  . THR A 1 47  ? 34.505 -14.328 15.399 1.00 19.51  ? 48  THR A CA  1 
ATOM   444  C  C   . THR A 1 47  ? 33.328 -14.998 16.078 1.00 20.26  ? 48  THR A C   1 
ATOM   445  O  O   . THR A 1 47  ? 32.196 -14.603 15.805 1.00 18.59  ? 48  THR A O   1 
ATOM   446  C  CB  . THR A 1 47  ? 34.909 -15.054 14.125 1.00 24.54  ? 48  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 47  ? 35.505 -16.286 14.497 1.00 24.83  ? 48  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 47  ? 35.831 -14.185 13.247 1.00 27.66  ? 48  THR A CG2 1 
ATOM   449  N  N   . VAL A 1 48  ? 33.578 -15.967 16.967 1.00 17.65  ? 49  VAL A N   1 
ATOM   450  C  CA  . VAL A 1 48  ? 32.486 -16.659 17.682 1.00 17.46  ? 49  VAL A CA  1 
ATOM   451  C  C   . VAL A 1 48  ? 31.819 -15.653 18.645 1.00 19.86  ? 49  VAL A C   1 
ATOM   452  O  O   . VAL A 1 48  ? 30.583 -15.589 18.719 1.00 18.79  ? 49  VAL A O   1 
ATOM   453  C  CB  . VAL A 1 48  ? 32.983 -17.927 18.435 1.00 20.05  ? 49  VAL A CB  1 
ATOM   454  C  CG1 . VAL A 1 48  ? 31.845 -18.532 19.284 1.00 19.51  ? 49  VAL A CG1 1 
ATOM   455  C  CG2 . VAL A 1 48  ? 33.533 -18.962 17.442 1.00 19.75  ? 49  VAL A CG2 1 
ATOM   456  N  N   . LEU A 1 49  ? 32.645 -14.858 19.376 1.00 17.02  ? 50  LEU A N   1 
ATOM   457  C  CA  . LEU A 1 49  ? 32.095 -13.841 20.292 1.00 17.61  ? 50  LEU A CA  1 
ATOM   458  C  C   . LEU A 1 49  ? 31.197 -12.848 19.525 1.00 20.21  ? 50  LEU A C   1 
ATOM   459  O  O   . LEU A 1 49  ? 30.072 -12.574 19.950 1.00 19.04  ? 50  LEU A O   1 
ATOM   460  C  CB  . LEU A 1 49  ? 33.248 -13.074 20.980 1.00 17.50  ? 50  LEU A CB  1 
ATOM   461  C  CG  . LEU A 1 49  ? 34.177 -13.874 21.915 1.00 19.75  ? 50  LEU A CG  1 
ATOM   462  C  CD1 . LEU A 1 49  ? 35.211 -12.906 22.550 1.00 20.32  ? 50  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A 1 49  ? 33.363 -14.583 23.025 1.00 20.96  ? 50  LEU A CD2 1 
ATOM   464  N  N   . MET A 1 50  ? 31.640 -12.402 18.336 1.00 17.38  ? 51  MET A N   1 
ATOM   465  C  CA  . MET A 1 50  ? 30.857 -11.469 17.498 1.00 18.12  ? 51  MET A CA  1 
ATOM   466  C  C   . MET A 1 50  ? 29.565 -12.107 17.016 1.00 20.52  ? 51  MET A C   1 
ATOM   467  O  O   . MET A 1 50  ? 28.519 -11.461 17.055 1.00 20.39  ? 51  MET A O   1 
ATOM   468  C  CB  . MET A 1 50  ? 31.661 -10.998 16.284 1.00 20.17  ? 51  MET A CB  1 
ATOM   469  C  CG  . MET A 1 50  ? 32.894 -10.207 16.674 1.00 22.93  ? 51  MET A CG  1 
ATOM   470  S  SD  . MET A 1 50  ? 33.924 -10.103 15.213 1.00 26.31  ? 51  MET A SD  1 
ATOM   471  C  CE  . MET A 1 50  ? 33.176 -8.730  14.458 1.00 23.64  ? 51  MET A CE  1 
ATOM   472  N  N   . ALA A 1 51  ? 29.615 -13.397 16.637 1.00 17.58  ? 52  ALA A N   1 
ATOM   473  C  CA  . ALA A 1 51  ? 28.446 -14.119 16.115 1.00 17.58  ? 52  ALA A CA  1 
ATOM   474  C  C   . ALA A 1 51  ? 27.357 -14.311 17.183 1.00 21.08  ? 52  ALA A C   1 
ATOM   475  O  O   . ALA A 1 51  ? 26.187 -14.513 16.846 1.00 21.13  ? 52  ALA A O   1 
ATOM   476  C  CB  . ALA A 1 51  ? 28.889 -15.493 15.574 1.00 17.34  ? 52  ALA A CB  1 
ATOM   477  N  N   . CYS A 1 52  ? 27.750 -14.254 18.461 1.00 18.06  ? 53  CYS A N   1 
ATOM   478  C  CA  . CYS A 1 52  ? 26.850 -14.490 19.592 1.00 18.83  ? 53  CYS A CA  1 
ATOM   479  C  C   . CYS A 1 52  ? 26.395 -13.268 20.366 1.00 21.38  ? 53  CYS A C   1 
ATOM   480  O  O   . CYS A 1 52  ? 25.434 -13.389 21.133 1.00 21.06  ? 53  CYS A O   1 
ATOM   481  C  CB  . CYS A 1 52  ? 27.520 -15.465 20.546 1.00 19.13  ? 53  CYS A CB  1 
ATOM   482  S  SG  . CYS A 1 52  ? 27.807 -17.096 19.840 1.00 21.67  ? 53  CYS A SG  1 
ATOM   483  N  N   . SER A 1 53  ? 27.151 -12.163 20.296 1.00 19.23  ? 54  SER A N   1 
ATOM   484  C  CA  . SER A 1 53  ? 26.929 -11.032 21.185 1.00 18.32  ? 54  SER A CA  1 
ATOM   485  C  C   . SER A 1 53  ? 26.966 -9.713  20.436 1.00 22.95  ? 54  SER A C   1 
ATOM   486  O  O   . SER A 1 53  ? 27.949 -9.435  19.739 1.00 21.15  ? 54  SER A O   1 
ATOM   487  C  CB  . SER A 1 53  ? 28.037 -11.080 22.241 1.00 19.82  ? 54  SER A CB  1 
ATOM   488  O  OG  . SER A 1 53  ? 28.397 -9.832  22.809 1.00 22.83  ? 54  SER A OG  1 
ATOM   489  N  N   . GLY A 1 54  ? 25.925 -8.894  20.624 1.00 22.36  ? 55  GLY A N   1 
ATOM   490  C  CA  . GLY A 1 54  ? 25.873 -7.559  20.038 1.00 22.66  ? 55  GLY A CA  1 
ATOM   491  C  C   . GLY A 1 54  ? 26.999 -6.680  20.544 1.00 24.78  ? 55  GLY A C   1 
ATOM   492  O  O   . GLY A 1 54  ? 27.529 -5.851  19.792 1.00 24.21  ? 55  GLY A O   1 
ATOM   493  N  N   . LEU A 1 55  ? 27.402 -6.871  21.830 1.00 21.64  ? 56  LEU A N   1 
ATOM   494  C  CA  . LEU A 1 55  ? 28.509 -6.086  22.390 1.00 20.73  ? 56  LEU A CA  1 
ATOM   495  C  C   . LEU A 1 55  ? 29.836 -6.430  21.692 1.00 22.61  ? 56  LEU A C   1 
ATOM   496  O  O   . LEU A 1 55  ? 30.538 -5.517  21.238 1.00 21.75  ? 56  LEU A O   1 
ATOM   497  C  CB  . LEU A 1 55  ? 28.633 -6.285  23.922 1.00 20.44  ? 56  LEU A CB  1 
ATOM   498  C  CG  . LEU A 1 55  ? 29.682 -5.355  24.597 1.00 25.77  ? 56  LEU A CG  1 
ATOM   499  C  CD1 . LEU A 1 55  ? 29.235 -3.868  24.579 1.00 26.78  ? 56  LEU A CD1 1 
ATOM   500  C  CD2 . LEU A 1 55  ? 29.970 -5.812  26.006 1.00 27.24  ? 56  LEU A CD2 1 
ATOM   501  N  N   . PHE A 1 56  ? 30.161 -7.731  21.582 1.00 19.73  ? 57  PHE A N   1 
ATOM   502  C  CA  . PHE A 1 56  ? 31.416 -8.124  20.925 1.00 18.63  ? 57  PHE A CA  1 
ATOM   503  C  C   . PHE A 1 56  ? 31.398 -7.796  19.452 1.00 22.70  ? 57  PHE A C   1 
ATOM   504  O  O   . PHE A 1 56  ? 32.433 -7.431  18.910 1.00 21.44  ? 57  PHE A O   1 
ATOM   505  C  CB  . PHE A 1 56  ? 31.766 -9.590  21.189 1.00 19.24  ? 57  PHE A CB  1 
ATOM   506  C  CG  . PHE A 1 56  ? 32.212 -9.827  22.618 1.00 19.44  ? 57  PHE A CG  1 
ATOM   507  C  CD1 . PHE A 1 56  ? 33.293 -9.119  23.159 1.00 21.44  ? 57  PHE A CD1 1 
ATOM   508  C  CD2 . PHE A 1 56  ? 31.577 -10.781 23.414 1.00 20.91  ? 57  PHE A CD2 1 
ATOM   509  C  CE1 . PHE A 1 56  ? 33.682 -9.307  24.497 1.00 22.10  ? 57  PHE A CE1 1 
ATOM   510  C  CE2 . PHE A 1 56  ? 32.001 -11.009 24.738 1.00 23.27  ? 57  PHE A CE2 1 
ATOM   511  C  CZ  . PHE A 1 56  ? 33.045 -10.261 25.270 1.00 20.67  ? 57  PHE A CZ  1 
ATOM   512  N  N   . TYR A 1 57  ? 30.216 -7.870  18.814 1.00 20.42  ? 58  TYR A N   1 
ATOM   513  C  CA  . TYR A 1 57  ? 30.110 -7.482  17.402 1.00 21.04  ? 58  TYR A CA  1 
ATOM   514  C  C   . TYR A 1 57  ? 30.539 -5.996  17.252 1.00 25.17  ? 58  TYR A C   1 
ATOM   515  O  O   . TYR A 1 57  ? 31.329 -5.669  16.364 1.00 24.06  ? 58  TYR A O   1 
ATOM   516  C  CB  . TYR A 1 57  ? 28.674 -7.697  16.913 1.00 23.01  ? 58  TYR A CB  1 
ATOM   517  C  CG  . TYR A 1 57  ? 28.462 -7.195  15.509 1.00 27.00  ? 58  TYR A CG  1 
ATOM   518  C  CD1 . TYR A 1 57  ? 29.045 -7.838  14.422 1.00 27.99  ? 58  TYR A CD1 1 
ATOM   519  C  CD2 . TYR A 1 57  ? 27.708 -6.052  15.267 1.00 32.18  ? 58  TYR A CD2 1 
ATOM   520  C  CE1 . TYR A 1 57  ? 28.853 -7.372  13.119 1.00 29.88  ? 58  TYR A CE1 1 
ATOM   521  C  CE2 . TYR A 1 57  ? 27.512 -5.579  13.976 1.00 35.60  ? 58  TYR A CE2 1 
ATOM   522  C  CZ  . TYR A 1 57  ? 28.076 -6.248  12.908 1.00 42.33  ? 58  TYR A CZ  1 
ATOM   523  O  OH  . TYR A 1 57  ? 27.863 -5.759  11.654 1.00 49.34  ? 58  TYR A OH  1 
ATOM   524  N  N   A SER A 1 58  ? 30.013 -5.114  18.121 0.52 23.26  ? 59  SER A N   1 
ATOM   525  N  N   B SER A 1 58  ? 30.005 -5.120  18.116 0.48 23.42  ? 59  SER A N   1 
ATOM   526  C  CA  A SER A 1 58  ? 30.334 -3.687  18.127 0.52 24.31  ? 59  SER A CA  1 
ATOM   527  C  CA  B SER A 1 58  ? 30.335 -3.700  18.115 0.48 24.59  ? 59  SER A CA  1 
ATOM   528  C  C   A SER A 1 58  ? 31.815 -3.442  18.439 0.52 29.22  ? 59  SER A C   1 
ATOM   529  C  C   B SER A 1 58  ? 31.829 -3.497  18.385 0.48 28.98  ? 59  SER A C   1 
ATOM   530  O  O   A SER A 1 58  ? 32.436 -2.604  17.794 0.52 30.45  ? 59  SER A O   1 
ATOM   531  O  O   B SER A 1 58  ? 32.474 -2.762  17.643 0.48 29.87  ? 59  SER A O   1 
ATOM   532  C  CB  A SER A 1 58  ? 29.442 -2.947  19.120 0.52 26.61  ? 59  SER A CB  1 
ATOM   533  C  CB  B SER A 1 58  ? 29.499 -2.957  19.154 0.48 27.74  ? 59  SER A CB  1 
ATOM   534  O  OG  A SER A 1 58  ? 28.108 -2.909  18.641 0.52 27.29  ? 59  SER A OG  1 
ATOM   535  O  OG  B SER A 1 58  ? 29.818 -1.576  19.142 0.48 32.70  ? 59  SER A OG  1 
ATOM   536  N  N   . ILE A 1 59  ? 32.377 -4.179  19.417 1.00 25.17  ? 60  ILE A N   1 
ATOM   537  C  CA  . ILE A 1 59  ? 33.791 -4.059  19.817 1.00 24.65  ? 60  ILE A CA  1 
ATOM   538  C  C   . ILE A 1 59  ? 34.739 -4.432  18.681 1.00 27.04  ? 60  ILE A C   1 
ATOM   539  O  O   . ILE A 1 59  ? 35.652 -3.654  18.367 1.00 27.72  ? 60  ILE A O   1 
ATOM   540  C  CB  . ILE A 1 59  ? 34.118 -4.893  21.116 1.00 26.66  ? 60  ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 59  ? 33.407 -4.323  22.356 1.00 27.01  ? 60  ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 59  ? 35.650 -5.000  21.358 1.00 25.02  ? 60  ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 59  ? 33.398 -5.299  23.570 1.00 28.53  ? 60  ILE A CD1 1 
ATOM   544  N  N   . PHE A 1 60  ? 34.549 -5.619  18.084 1.00 23.19  ? 61  PHE A N   1 
ATOM   545  C  CA  . PHE A 1 60  ? 35.519 -6.083  17.101 1.00 23.02  ? 61  PHE A CA  1 
ATOM   546  C  C   . PHE A 1 60  ? 35.286 -5.535  15.687 1.00 27.08  ? 61  PHE A C   1 
ATOM   547  O  O   . PHE A 1 60  ? 36.126 -5.775  14.826 1.00 28.23  ? 61  PHE A O   1 
ATOM   548  C  CB  . PHE A 1 60  ? 35.644 -7.625  17.146 1.00 22.85  ? 61  PHE A CB  1 
ATOM   549  C  CG  . PHE A 1 60  ? 36.082 -8.116  18.517 1.00 23.25  ? 61  PHE A CG  1 
ATOM   550  C  CD1 . PHE A 1 60  ? 37.284 -7.684  19.081 1.00 26.32  ? 61  PHE A CD1 1 
ATOM   551  C  CD2 . PHE A 1 60  ? 35.292 -8.999  19.241 1.00 24.88  ? 61  PHE A CD2 1 
ATOM   552  C  CE1 . PHE A 1 60  ? 37.674 -8.117  20.359 1.00 27.39  ? 61  PHE A CE1 1 
ATOM   553  C  CE2 . PHE A 1 60  ? 35.691 -9.448  20.514 1.00 27.67  ? 61  PHE A CE2 1 
ATOM   554  C  CZ  . PHE A 1 60  ? 36.874 -9.003  21.063 1.00 25.84  ? 61  PHE A CZ  1 
ATOM   555  N  N   . THR A 1 61  ? 34.233 -4.721  15.463 1.00 24.62  ? 62  THR A N   1 
ATOM   556  C  CA  . THR A 1 61  ? 34.071 -4.034  14.170 1.00 25.05  ? 62  THR A CA  1 
ATOM   557  C  C   . THR A 1 61  ? 34.611 -2.607  14.294 1.00 31.92  ? 62  THR A C   1 
ATOM   558  O  O   . THR A 1 61  ? 34.674 -1.871  13.303 1.00 32.53  ? 62  THR A O   1 
ATOM   559  C  CB  . THR A 1 61  ? 32.649 -4.069  13.616 1.00 33.04  ? 62  THR A CB  1 
ATOM   560  O  OG1 . THR A 1 61  ? 31.752 -3.551  14.588 1.00 29.73  ? 62  THR A OG1 1 
ATOM   561  C  CG2 . THR A 1 61  ? 32.230 -5.464  13.127 1.00 29.08  ? 62  THR A CG2 1 
ATOM   562  N  N   . ASP A 1 62  ? 35.043 -2.230  15.507 1.00 27.54  ? 63  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 62  ? 35.641 -0.911  15.716 1.00 28.67  ? 63  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 62  ? 37.066 -0.991  15.182 1.00 36.08  ? 63  ASP A C   1 
ATOM   565  O  O   . ASP A 1 62  ? 37.796 -1.900  15.565 1.00 34.74  ? 63  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 62  ? 35.637 -0.530  17.203 1.00 28.88  ? 63  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 62  ? 36.389 0.759   17.422 1.00 42.46  ? 63  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 62  ? 35.787 1.825   17.228 1.00 47.21  ? 63  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 62  ? 37.610 0.695   17.708 1.00 43.48  ? 63  ASP A OD2 1 
ATOM   570  N  N   . GLN A 1 63  ? 37.471 -0.017  14.334 1.00 37.61  ? 64  GLN A N   1 
ATOM   571  C  CA  . GLN A 1 63  ? 38.776 0.027   13.673 1.00 38.99  ? 64  GLN A CA  1 
ATOM   572  C  C   . GLN A 1 63  ? 39.979 -0.026  14.621 1.00 43.49  ? 64  GLN A C   1 
ATOM   573  O  O   . GLN A 1 63  ? 41.028 -0.506  14.188 1.00 45.54  ? 64  GLN A O   1 
ATOM   574  C  CB  . GLN A 1 63  ? 38.882 1.230   12.723 1.00 42.60  ? 64  GLN A CB  1 
ATOM   575  C  CG  . GLN A 1 63  ? 38.030 1.080   11.463 1.00 62.33  ? 64  GLN A CG  1 
ATOM   576  N  N   . LEU A 1 64  ? 39.858 0.476   15.885 1.00 36.26  ? 65  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 64  ? 40.956 0.394   16.859 1.00 35.22  ? 65  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 64  ? 40.866 -0.852  17.721 1.00 38.05  ? 65  LEU A C   1 
ATOM   579  O  O   . LEU A 1 64  ? 41.889 -1.459  18.020 1.00 40.07  ? 65  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 64  ? 40.985 1.616   17.808 1.00 36.13  ? 65  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 64  ? 41.635 2.888   17.309 1.00 43.28  ? 65  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 64  ? 41.472 3.987   18.330 1.00 43.42  ? 65  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 64  ? 43.123 2.696   17.000 1.00 47.62  ? 65  LEU A CD2 1 
ATOM   584  N  N   . LYS A 1 65  ? 39.661 -1.187  18.207 1.00 30.46  ? 66  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 65  ? 39.495 -2.304  19.135 1.00 29.33  ? 66  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 65  ? 39.616 -3.664  18.464 1.00 34.13  ? 66  LYS A C   1 
ATOM   587  O  O   . LYS A 1 65  ? 39.976 -4.622  19.144 1.00 32.83  ? 66  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 65  ? 38.172 -2.208  19.921 1.00 30.11  ? 66  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 65  ? 38.066 -0.969  20.814 1.00 30.37  ? 66  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 65  ? 36.778 -1.057  21.626 1.00 28.49  ? 66  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 65  ? 36.471 0.261   22.314 1.00 33.09  ? 66  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 65  ? 35.902 1.268   21.391 1.00 34.14  ? 66  LYS A NZ  1 
ATOM   593  N  N   . CYS A 1 66  ? 39.347 -3.749  17.137 1.00 34.31  ? 67  CYS A N   1 
ATOM   594  C  CA  . CYS A 1 66  ? 39.446 -5.013  16.375 1.00 34.37  ? 67  CYS A CA  1 
ATOM   595  C  C   . CYS A 1 66  ? 40.839 -5.641  16.515 1.00 38.94  ? 67  CYS A C   1 
ATOM   596  O  O   . CYS A 1 66  ? 40.982 -6.855  16.348 1.00 38.94  ? 67  CYS A O   1 
ATOM   597  C  CB  . CYS A 1 66  ? 39.084 -4.798  14.905 1.00 36.05  ? 67  CYS A CB  1 
ATOM   598  S  SG  . CYS A 1 66  ? 40.256 -3.753  13.988 1.00 42.25  ? 67  CYS A SG  1 
ATOM   599  N  N   . ASN A 1 67  ? 41.861 -4.796  16.788 1.00 35.37  ? 68  ASN A N   1 
ATOM   600  C  CA  . ASN A 1 67  ? 43.258 -5.192  16.913 1.00 36.47  ? 68  ASN A CA  1 
ATOM   601  C  C   . ASN A 1 67  ? 43.729 -5.491  18.342 1.00 39.16  ? 68  ASN A C   1 
ATOM   602  O  O   . ASN A 1 67  ? 44.892 -5.858  18.537 1.00 38.52  ? 68  ASN A O   1 
ATOM   603  C  CB  . ASN A 1 67  ? 44.156 -4.144  16.244 1.00 38.03  ? 68  ASN A CB  1 
ATOM   604  C  CG  . ASN A 1 67  ? 43.972 -4.132  14.737 1.00 52.63  ? 68  ASN A CG  1 
ATOM   605  O  OD1 . ASN A 1 67  ? 43.945 -3.077  14.108 1.00 52.73  ? 68  ASN A OD1 1 
ATOM   606  N  ND2 . ASN A 1 67  ? 43.794 -5.303  14.125 1.00 43.93  ? 68  ASN A ND2 1 
ATOM   607  N  N   . LEU A 1 68  ? 42.838 -5.374  19.331 1.00 35.22  ? 69  LEU A N   1 
ATOM   608  C  CA  . LEU A 1 68  ? 43.223 -5.640  20.711 1.00 33.96  ? 69  LEU A CA  1 
ATOM   609  C  C   . LEU A 1 68  ? 43.213 -7.141  20.987 1.00 35.06  ? 69  LEU A C   1 
ATOM   610  O  O   . LEU A 1 68  ? 42.321 -7.838  20.486 1.00 32.81  ? 69  LEU A O   1 
ATOM   611  C  CB  . LEU A 1 68  ? 42.258 -4.926  21.680 1.00 33.81  ? 69  LEU A CB  1 
ATOM   612  C  CG  . LEU A 1 68  ? 42.305 -3.386  21.661 1.00 38.33  ? 69  LEU A CG  1 
ATOM   613  C  CD1 . LEU A 1 68  ? 41.231 -2.815  22.562 1.00 37.91  ? 69  LEU A CD1 1 
ATOM   614  C  CD2 . LEU A 1 68  ? 43.692 -2.856  22.076 1.00 39.19  ? 69  LEU A CD2 1 
ATOM   615  N  N   . SER A 1 69  ? 44.189 -7.618  21.795 1.00 31.29  ? 70  SER A N   1 
ATOM   616  C  CA  A SER A 1 69  ? 44.313 -9.027  22.190 0.42 30.61  ? 70  SER A CA  1 
ATOM   617  C  CA  B SER A 1 69  ? 44.263 -9.038  22.163 0.58 31.03  ? 70  SER A CA  1 
ATOM   618  C  C   . SER A 1 69  ? 43.672 -9.239  23.566 1.00 31.93  ? 70  SER A C   1 
ATOM   619  O  O   . SER A 1 69  ? 43.498 -10.369 24.006 1.00 28.46  ? 70  SER A O   1 
ATOM   620  C  CB  A SER A 1 69  ? 45.786 -9.429  22.245 0.42 34.77  ? 70  SER A CB  1 
ATOM   621  C  CB  B SER A 1 69  ? 45.704 -9.542  22.098 0.58 36.08  ? 70  SER A CB  1 
ATOM   622  O  OG  A SER A 1 69  ? 46.379 -9.371  20.959 0.42 39.42  ? 70  SER A OG  1 
ATOM   623  O  OG  B SER A 1 69  ? 46.540 -8.828  22.993 0.58 43.16  ? 70  SER A OG  1 
ATOM   624  N  N   . VAL A 1 70  ? 43.378 -8.134  24.274 1.00 28.55  ? 71  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 70  ? 42.781 -8.169  25.617 1.00 27.35  ? 71  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 70  ? 41.605 -7.198  25.666 1.00 29.19  ? 71  VAL A C   1 
ATOM   627  O  O   . VAL A 1 70  ? 41.748 -6.033  25.266 1.00 28.79  ? 71  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 70  ? 43.827 -7.832  26.729 1.00 32.96  ? 71  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 70  ? 43.192 -7.834  28.125 1.00 33.00  ? 71  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 70  ? 45.032 -8.775  26.679 1.00 33.81  ? 71  VAL A CG2 1 
ATOM   631  N  N   . ILE A 1 71  ? 40.455 -7.676  26.171 1.00 23.33  ? 72  ILE A N   1 
ATOM   632  C  CA  . ILE A 1 71  ? 39.253 -6.866  26.378 1.00 22.73  ? 72  ILE A CA  1 
ATOM   633  C  C   . ILE A 1 71  ? 38.866 -6.973  27.850 1.00 27.13  ? 72  ILE A C   1 
ATOM   634  O  O   . ILE A 1 71  ? 38.641 -8.079  28.349 1.00 26.74  ? 72  ILE A O   1 
ATOM   635  C  CB  . ILE A 1 71  ? 38.072 -7.225  25.418 1.00 24.45  ? 72  ILE A CB  1 
ATOM   636  C  CG1 . ILE A 1 71  ? 38.475 -7.091  23.909 1.00 25.36  ? 72  ILE A CG1 1 
ATOM   637  C  CG2 . ILE A 1 71  ? 36.791 -6.415  25.747 1.00 26.14  ? 72  ILE A CG2 1 
ATOM   638  C  CD1 . ILE A 1 71  ? 38.860 -5.629  23.409 1.00 28.31  ? 72  ILE A CD1 1 
ATOM   639  N  N   . ASN A 1 72  ? 38.738 -5.828  28.525 1.00 24.13  ? 73  ASN A N   1 
ATOM   640  C  CA  . ASN A 1 72  ? 38.345 -5.797  29.928 1.00 24.13  ? 73  ASN A CA  1 
ATOM   641  C  C   . ASN A 1 72  ? 36.867 -5.465  30.040 1.00 27.10  ? 73  ASN A C   1 
ATOM   642  O  O   . ASN A 1 72  ? 36.432 -4.393  29.596 1.00 26.04  ? 73  ASN A O   1 
ATOM   643  C  CB  . ASN A 1 72  ? 39.171 -4.745  30.714 1.00 28.68  ? 73  ASN A CB  1 
ATOM   644  C  CG  . ASN A 1 72  ? 40.648 -4.972  30.649 1.00 46.45  ? 73  ASN A CG  1 
ATOM   645  O  OD1 . ASN A 1 72  ? 41.150 -6.011  31.049 1.00 36.94  ? 73  ASN A OD1 1 
ATOM   646  N  ND2 . ASN A 1 72  ? 41.381 -4.001  30.149 1.00 41.05  ? 73  ASN A ND2 1 
ATOM   647  N  N   . LEU A 1 73  ? 36.099 -6.361  30.655 1.00 22.25  ? 74  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 73  ? 34.677 -6.105  30.855 1.00 22.02  ? 74  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 73  ? 34.443 -5.200  32.069 1.00 25.77  ? 74  LEU A C   1 
ATOM   650  O  O   . LEU A 1 73  ? 35.326 -5.047  32.921 1.00 25.89  ? 74  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 73  ? 33.863 -7.406  30.978 1.00 21.86  ? 74  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 73  ? 33.934 -8.402  29.797 1.00 24.32  ? 74  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 73  ? 32.805 -9.458  29.920 1.00 23.47  ? 74  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 73  ? 33.880 -7.699  28.424 1.00 23.72  ? 74  LEU A CD2 1 
ATOM   655  N  N   . ASP A 1 74  ? 33.251 -4.612  32.135 1.00 22.71  ? 75  ASP A N   1 
ATOM   656  C  CA  . ASP A 1 74  ? 32.836 -3.717  33.225 1.00 24.02  ? 75  ASP A CA  1 
ATOM   657  C  C   . ASP A 1 74  ? 33.014 -4.465  34.563 1.00 29.06  ? 75  ASP A C   1 
ATOM   658  O  O   . ASP A 1 74  ? 32.663 -5.647  34.636 1.00 27.06  ? 75  ASP A O   1 
ATOM   659  C  CB  . ASP A 1 74  ? 31.366 -3.317  33.018 1.00 25.81  ? 75  ASP A CB  1 
ATOM   660  C  CG  . ASP A 1 74  ? 30.820 -2.299  34.008 1.00 36.62  ? 75  ASP A CG  1 
ATOM   661  O  OD1 . ASP A 1 74  ? 30.682 -2.644  35.206 1.00 36.66  ? 75  ASP A OD1 1 
ATOM   662  O  OD2 . ASP A 1 74  ? 30.491 -1.181  33.581 1.00 38.19  ? 75  ASP A OD2 1 
ATOM   663  N  N   . PRO A 1 75  ? 33.602 -3.822  35.595 1.00 29.70  ? 76  PRO A N   1 
ATOM   664  C  CA  . PRO A 1 75  ? 33.804 -4.526  36.885 1.00 30.48  ? 76  PRO A CA  1 
ATOM   665  C  C   . PRO A 1 75  ? 32.553 -5.093  37.543 1.00 33.35  ? 76  PRO A C   1 
ATOM   666  O  O   . PRO A 1 75  ? 32.689 -5.951  38.407 1.00 35.01  ? 76  PRO A O   1 
ATOM   667  C  CB  . PRO A 1 75  ? 34.480 -3.481  37.778 1.00 33.35  ? 76  PRO A CB  1 
ATOM   668  C  CG  . PRO A 1 75  ? 34.200 -2.154  37.125 1.00 38.14  ? 76  PRO A CG  1 
ATOM   669  C  CD  . PRO A 1 75  ? 34.103 -2.429  35.654 1.00 31.74  ? 76  PRO A CD  1 
ATOM   670  N  N   . GLU A 1 76  ? 31.346 -4.650  37.150 1.00 29.49  ? 77  GLU A N   1 
ATOM   671  C  CA  . GLU A 1 76  ? 30.112 -5.195  37.725 1.00 31.17  ? 77  GLU A CA  1 
ATOM   672  C  C   . GLU A 1 76  ? 29.816 -6.598  37.185 1.00 31.58  ? 77  GLU A C   1 
ATOM   673  O  O   . GLU A 1 76  ? 28.979 -7.304  37.752 1.00 31.10  ? 77  GLU A O   1 
ATOM   674  C  CB  . GLU A 1 76  ? 28.910 -4.269  37.460 1.00 34.01  ? 77  GLU A CB  1 
ATOM   675  C  CG  . GLU A 1 76  ? 28.874 -3.034  38.346 1.00 54.24  ? 77  GLU A CG  1 
ATOM   676  C  CD  . GLU A 1 76  ? 28.371 -3.294  39.754 1.00 87.33  ? 77  GLU A CD  1 
ATOM   677  O  OE1 . GLU A 1 76  ? 27.144 -3.478  39.923 1.00 88.44  ? 77  GLU A OE1 1 
ATOM   678  O  OE2 . GLU A 1 76  ? 29.208 -3.325  40.686 1.00 86.51  ? 77  GLU A OE2 1 
ATOM   679  N  N   . ILE A 1 77  ? 30.476 -6.994  36.084 1.00 25.86  ? 78  ILE A N   1 
ATOM   680  C  CA  . ILE A 1 77  ? 30.221 -8.314  35.497 1.00 24.54  ? 78  ILE A CA  1 
ATOM   681  C  C   . ILE A 1 77  ? 30.826 -9.423  36.337 1.00 29.28  ? 78  ILE A C   1 
ATOM   682  O  O   . ILE A 1 77  ? 32.007 -9.395  36.669 1.00 27.70  ? 78  ILE A O   1 
ATOM   683  C  CB  . ILE A 1 77  ? 30.646 -8.373  34.011 1.00 26.54  ? 78  ILE A CB  1 
ATOM   684  C  CG1 . ILE A 1 77  ? 29.907 -7.269  33.187 1.00 27.38  ? 78  ILE A CG1 1 
ATOM   685  C  CG2 . ILE A 1 77  ? 30.434 -9.788  33.424 1.00 23.46  ? 78  ILE A CG2 1 
ATOM   686  C  CD1 . ILE A 1 77  ? 28.285 -7.325  33.230 1.00 33.48  ? 78  ILE A CD1 1 
ATOM   687  N  N   . ASN A 1 78  ? 29.998 -10.417 36.617 1.00 28.89  ? 79  ASN A N   1 
ATOM   688  C  CA  . ASN A 1 78  ? 30.312 -11.601 37.395 1.00 29.64  ? 79  ASN A CA  1 
ATOM   689  C  C   . ASN A 1 78  ? 31.044 -12.638 36.523 1.00 28.71  ? 79  ASN A C   1 
ATOM   690  O  O   . ASN A 1 78  ? 30.521 -13.014 35.473 1.00 25.51  ? 79  ASN A O   1 
ATOM   691  C  CB  . ASN A 1 78  ? 28.997 -12.175 37.958 1.00 33.60  ? 79  ASN A CB  1 
ATOM   692  C  CG  . ASN A 1 78  ? 29.167 -13.471 38.700 1.00 47.65  ? 79  ASN A CG  1 
ATOM   693  O  OD1 . ASN A 1 78  ? 28.798 -14.529 38.204 1.00 36.87  ? 79  ASN A OD1 1 
ATOM   694  N  ND2 . ASN A 1 78  ? 29.733 -13.413 39.899 1.00 42.50  ? 79  ASN A ND2 1 
ATOM   695  N  N   . PRO A 1 79  ? 32.244 -13.127 36.936 1.00 26.88  ? 80  PRO A N   1 
ATOM   696  C  CA  . PRO A 1 79  ? 32.960 -14.123 36.112 1.00 26.42  ? 80  PRO A CA  1 
ATOM   697  C  C   . PRO A 1 79  ? 32.171 -15.411 35.860 1.00 29.03  ? 80  PRO A C   1 
ATOM   698  O  O   . PRO A 1 79  ? 32.244 -15.951 34.753 1.00 27.79  ? 80  PRO A O   1 
ATOM   699  C  CB  . PRO A 1 79  ? 34.228 -14.399 36.922 1.00 29.71  ? 80  PRO A CB  1 
ATOM   700  C  CG  . PRO A 1 79  ? 34.415 -13.153 37.763 1.00 34.58  ? 80  PRO A CG  1 
ATOM   701  C  CD  . PRO A 1 79  ? 33.030 -12.757 38.134 1.00 30.38  ? 80  PRO A CD  1 
ATOM   702  N  N   . GLU A 1 80  ? 31.411 -15.895 36.859 1.00 26.19  ? 81  GLU A N   1 
ATOM   703  C  CA  . GLU A 1 80  ? 30.632 -17.129 36.655 1.00 25.85  ? 81  GLU A CA  1 
ATOM   704  C  C   . GLU A 1 80  ? 29.537 -16.936 35.576 1.00 27.61  ? 81  GLU A C   1 
ATOM   705  O  O   . GLU A 1 80  ? 29.395 -17.789 34.699 1.00 25.83  ? 81  GLU A O   1 
ATOM   706  C  CB  . GLU A 1 80  ? 30.042 -17.648 37.973 1.00 28.51  ? 81  GLU A CB  1 
ATOM   707  C  CG  . GLU A 1 80  ? 29.412 -19.025 37.783 1.00 37.79  ? 81  GLU A CG  1 
ATOM   708  C  CD  . GLU A 1 80  ? 28.544 -19.560 38.908 1.00 63.81  ? 81  GLU A CD  1 
ATOM   709  O  OE1 . GLU A 1 80  ? 28.522 -20.798 39.090 1.00 61.09  ? 81  GLU A OE1 1 
ATOM   710  O  OE2 . GLU A 1 80  ? 27.872 -18.754 39.592 1.00 59.19  ? 81  GLU A OE2 1 
ATOM   711  N  N   . GLY A 1 81  ? 28.812 -15.808 35.636 1.00 25.47  ? 82  GLY A N   1 
ATOM   712  C  CA  . GLY A 1 81  ? 27.802 -15.467 34.636 1.00 24.44  ? 82  GLY A CA  1 
ATOM   713  C  C   . GLY A 1 81  ? 28.439 -15.411 33.256 1.00 26.09  ? 82  GLY A C   1 
ATOM   714  O  O   . GLY A 1 81  ? 27.884 -15.940 32.282 1.00 24.62  ? 82  GLY A O   1 
ATOM   715  N  N   . PHE A 1 82  ? 29.638 -14.791 33.167 1.00 21.59  ? 83  PHE A N   1 
ATOM   716  C  CA  . PHE A 1 82  ? 30.330 -14.735 31.874 1.00 20.16  ? 83  PHE A CA  1 
ATOM   717  C  C   . PHE A 1 82  ? 30.685 -16.142 31.403 1.00 23.31  ? 83  PHE A C   1 
ATOM   718  O  O   . PHE A 1 82  ? 30.484 -16.454 30.241 1.00 21.30  ? 83  PHE A O   1 
ATOM   719  C  CB  . PHE A 1 82  ? 31.604 -13.861 31.919 1.00 21.29  ? 83  PHE A CB  1 
ATOM   720  C  CG  . PHE A 1 82  ? 32.195 -13.734 30.528 1.00 21.31  ? 83  PHE A CG  1 
ATOM   721  C  CD1 . PHE A 1 82  ? 31.613 -12.894 29.581 1.00 23.75  ? 83  PHE A CD1 1 
ATOM   722  C  CD2 . PHE A 1 82  ? 33.274 -14.522 30.139 1.00 21.94  ? 83  PHE A CD2 1 
ATOM   723  C  CE1 . PHE A 1 82  ? 32.111 -12.833 28.271 1.00 24.14  ? 83  PHE A CE1 1 
ATOM   724  C  CE2 . PHE A 1 82  ? 33.774 -14.456 28.838 1.00 23.28  ? 83  PHE A CE2 1 
ATOM   725  C  CZ  . PHE A 1 82  ? 33.192 -13.614 27.914 1.00 22.71  ? 83  PHE A CZ  1 
ATOM   726  N  N   . CYS A 1 83  ? 31.260 -16.955 32.282 1.00 23.65  ? 84  CYS A N   1 
ATOM   727  C  CA  . CYS A 1 83  ? 31.676 -18.326 31.954 1.00 24.96  ? 84  CYS A CA  1 
ATOM   728  C  C   . CYS A 1 83  ? 30.488 -19.147 31.392 1.00 26.18  ? 84  CYS A C   1 
ATOM   729  O  O   . CYS A 1 83  ? 30.626 -19.818 30.353 1.00 24.46  ? 84  CYS A O   1 
ATOM   730  C  CB  . CYS A 1 83  ? 32.299 -18.993 33.176 1.00 28.54  ? 84  CYS A CB  1 
ATOM   731  S  SG  . CYS A 1 83  ? 32.948 -20.655 32.847 1.00 34.27  ? 84  CYS A SG  1 
ATOM   732  N  N   . ILE A 1 84  ? 29.316 -19.035 32.049 1.00 22.60  ? 85  ILE A N   1 
ATOM   733  C  CA  . ILE A 1 84  ? 28.087 -19.740 31.629 1.00 21.16  ? 85  ILE A CA  1 
ATOM   734  C  C   . ILE A 1 84  ? 27.686 -19.280 30.217 1.00 21.39  ? 85  ILE A C   1 
ATOM   735  O  O   . ILE A 1 84  ? 27.320 -20.103 29.360 1.00 20.77  ? 85  ILE A O   1 
ATOM   736  C  CB  . ILE A 1 84  ? 26.967 -19.505 32.676 1.00 24.62  ? 85  ILE A CB  1 
ATOM   737  C  CG1 . ILE A 1 84  ? 27.259 -20.329 33.973 1.00 26.03  ? 85  ILE A CG1 1 
ATOM   738  C  CG2 . ILE A 1 84  ? 25.557 -19.827 32.105 1.00 24.35  ? 85  ILE A CG2 1 
ATOM   739  C  CD1 . ILE A 1 84  ? 26.520 -19.762 35.204 1.00 33.64  ? 85  ILE A CD1 1 
ATOM   740  N  N   . LEU A 1 85  ? 27.760 -17.977 29.977 1.00 19.51  ? 86  LEU A N   1 
ATOM   741  C  CA  . LEU A 1 85  ? 27.412 -17.444 28.657 1.00 19.10  ? 86  LEU A CA  1 
ATOM   742  C  C   . LEU A 1 85  ? 28.416 -17.804 27.594 1.00 22.15  ? 86  LEU A C   1 
ATOM   743  O  O   . LEU A 1 85  ? 28.012 -18.051 26.460 1.00 20.33  ? 86  LEU A O   1 
ATOM   744  C  CB  . LEU A 1 85  ? 27.169 -15.943 28.733 1.00 20.08  ? 86  LEU A CB  1 
ATOM   745  C  CG  . LEU A 1 85  ? 25.876 -15.568 29.496 1.00 25.96  ? 86  LEU A CG  1 
ATOM   746  C  CD1 . LEU A 1 85  ? 25.807 -14.098 29.670 1.00 26.98  ? 86  LEU A CD1 1 
ATOM   747  C  CD2 . LEU A 1 85  ? 24.616 -16.057 28.741 1.00 27.39  ? 86  LEU A CD2 1 
ATOM   748  N  N   . LEU A 1 86  ? 29.733 -17.837 27.938 1.00 19.33  ? 87  LEU A N   1 
ATOM   749  C  CA  . LEU A 1 86  ? 30.757 -18.243 26.968 1.00 18.82  ? 87  LEU A CA  1 
ATOM   750  C  C   . LEU A 1 86  ? 30.525 -19.709 26.573 1.00 21.85  ? 87  LEU A C   1 
ATOM   751  O  O   . LEU A 1 86  ? 30.593 -20.067 25.391 1.00 19.72  ? 87  LEU A O   1 
ATOM   752  C  CB  . LEU A 1 86  ? 32.161 -18.033 27.568 1.00 18.48  ? 87  LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 86  ? 33.335 -18.338 26.622 1.00 23.37  ? 87  LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 86  ? 33.318 -17.403 25.383 1.00 23.06  ? 87  LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 86  ? 34.689 -18.223 27.385 1.00 25.60  ? 87  LEU A CD2 1 
ATOM   756  N  N   . ASP A 1 87  ? 30.220 -20.554 27.561 1.00 20.43  ? 88  ASP A N   1 
ATOM   757  C  CA  . ASP A 1 87  ? 29.890 -21.946 27.295 1.00 20.11  ? 88  ASP A CA  1 
ATOM   758  C  C   . ASP A 1 87  ? 28.682 -22.046 26.360 1.00 22.49  ? 88  ASP A C   1 
ATOM   759  O  O   . ASP A 1 87  ? 28.712 -22.833 25.415 1.00 22.30  ? 88  ASP A O   1 
ATOM   760  C  CB  . ASP A 1 87  ? 29.596 -22.661 28.615 1.00 23.21  ? 88  ASP A CB  1 
ATOM   761  C  CG  . ASP A 1 87  ? 30.841 -23.036 29.398 1.00 35.64  ? 88  ASP A CG  1 
ATOM   762  O  OD1 . ASP A 1 87  ? 31.955 -22.973 28.817 1.00 35.90  ? 88  ASP A OD1 1 
ATOM   763  O  OD2 . ASP A 1 87  ? 30.706 -23.393 30.591 1.00 36.76  ? 88  ASP A OD2 1 
ATOM   764  N  N   . PHE A 1 88  ? 27.629 -21.256 26.617 1.00 19.46  ? 89  PHE A N   1 
ATOM   765  C  CA  . PHE A 1 88  ? 26.438 -21.215 25.750 1.00 18.58  ? 89  PHE A CA  1 
ATOM   766  C  C   . PHE A 1 88  ? 26.817 -20.827 24.311 1.00 19.62  ? 89  PHE A C   1 
ATOM   767  O  O   . PHE A 1 88  ? 26.338 -21.432 23.344 1.00 18.60  ? 89  PHE A O   1 
ATOM   768  C  CB  . PHE A 1 88  ? 25.377 -20.246 26.326 1.00 19.60  ? 89  PHE A CB  1 
ATOM   769  C  CG  . PHE A 1 88  ? 24.267 -19.967 25.348 1.00 19.98  ? 89  PHE A CG  1 
ATOM   770  C  CD1 . PHE A 1 88  ? 23.289 -20.928 25.087 1.00 21.40  ? 89  PHE A CD1 1 
ATOM   771  C  CD2 . PHE A 1 88  ? 24.255 -18.787 24.602 1.00 21.40  ? 89  PHE A CD2 1 
ATOM   772  C  CE1 . PHE A 1 88  ? 22.301 -20.696 24.135 1.00 21.71  ? 89  PHE A CE1 1 
ATOM   773  C  CE2 . PHE A 1 88  ? 23.264 -18.558 23.640 1.00 24.18  ? 89  PHE A CE2 1 
ATOM   774  C  CZ  . PHE A 1 88  ? 22.291 -19.508 23.418 1.00 22.47  ? 89  PHE A CZ  1 
ATOM   775  N  N   . MET A 1 89  ? 27.649 -19.789 24.160 1.00 16.23  ? 90  MET A N   1 
ATOM   776  C  CA  . MET A 1 89  ? 28.075 -19.369 22.805 1.00 15.26  ? 90  MET A CA  1 
ATOM   777  C  C   . MET A 1 89  ? 28.626 -20.514 21.995 1.00 19.36  ? 90  MET A C   1 
ATOM   778  O  O   . MET A 1 89  ? 28.287 -20.639 20.820 1.00 18.65  ? 90  MET A O   1 
ATOM   779  C  CB  . MET A 1 89  ? 29.164 -18.273 22.918 1.00 16.18  ? 90  MET A CB  1 
ATOM   780  C  CG  . MET A 1 89  ? 28.631 -16.978 23.486 1.00 18.55  ? 90  MET A CG  1 
ATOM   781  S  SD  . MET A 1 89  ? 30.000 -15.768 23.381 1.00 21.82  ? 90  MET A SD  1 
ATOM   782  C  CE  . MET A 1 89  ? 29.349 -14.443 24.526 1.00 22.01  ? 90  MET A CE  1 
ATOM   783  N  N   . TYR A 1 90  ? 29.477 -21.348 22.619 1.00 17.22  ? 91  TYR A N   1 
ATOM   784  C  CA  . TYR A 1 90  ? 30.153 -22.441 21.939 1.00 16.99  ? 91  TYR A CA  1 
ATOM   785  C  C   . TYR A 1 90  ? 29.404 -23.755 21.941 1.00 21.05  ? 91  TYR A C   1 
ATOM   786  O  O   . TYR A 1 90  ? 29.891 -24.708 21.322 1.00 19.98  ? 91  TYR A O   1 
ATOM   787  C  CB  . TYR A 1 90  ? 31.531 -22.661 22.568 1.00 18.21  ? 91  TYR A CB  1 
ATOM   788  C  CG  . TYR A 1 90  ? 32.591 -21.689 22.089 1.00 19.06  ? 91  TYR A CG  1 
ATOM   789  C  CD1 . TYR A 1 90  ? 32.743 -20.439 22.687 1.00 20.64  ? 91  TYR A CD1 1 
ATOM   790  C  CD2 . TYR A 1 90  ? 33.431 -22.014 21.023 1.00 19.71  ? 91  TYR A CD2 1 
ATOM   791  C  CE1 . TYR A 1 90  ? 33.737 -19.551 22.264 1.00 20.42  ? 91  TYR A CE1 1 
ATOM   792  C  CE2 . TYR A 1 90  ? 34.460 -21.160 20.625 1.00 19.71  ? 91  TYR A CE2 1 
ATOM   793  C  CZ  . TYR A 1 90  ? 34.582 -19.913 21.220 1.00 23.19  ? 91  TYR A CZ  1 
ATOM   794  O  OH  . TYR A 1 90  ? 35.608 -19.091 20.830 1.00 21.33  ? 91  TYR A OH  1 
ATOM   795  N  N   . THR A 1 91  ? 28.240 -23.839 22.624 1.00 17.58  ? 92  THR A N   1 
ATOM   796  C  CA  . THR A 1 91  ? 27.561 -25.145 22.693 1.00 17.85  ? 92  THR A CA  1 
ATOM   797  C  C   . THR A 1 91  ? 26.057 -25.130 22.433 1.00 20.31  ? 92  THR A C   1 
ATOM   798  O  O   . THR A 1 91  ? 25.487 -26.216 22.292 1.00 20.81  ? 92  THR A O   1 
ATOM   799  C  CB  . THR A 1 91  ? 27.758 -25.820 24.083 1.00 22.85  ? 92  THR A CB  1 
ATOM   800  O  OG1 . THR A 1 91  ? 27.101 -25.040 25.090 1.00 22.93  ? 92  THR A OG1 1 
ATOM   801  C  CG2 . THR A 1 91  ? 29.227 -26.059 24.459 1.00 23.03  ? 92  THR A CG2 1 
ATOM   802  N  N   . SER A 1 92  ? 25.412 -23.959 22.525 1.00 16.84  ? 93  SER A N   1 
ATOM   803  C  CA  . SER A 1 92  ? 23.935 -23.762 22.476 1.00 17.12  ? 93  SER A CA  1 
ATOM   804  C  C   . SER A 1 92  ? 23.276 -24.174 23.814 1.00 20.95  ? 93  SER A C   1 
ATOM   805  O  O   . SER A 1 92  ? 22.055 -24.066 23.933 1.00 21.08  ? 93  SER A O   1 
ATOM   806  C  CB  . SER A 1 92  ? 23.276 -24.580 21.354 1.00 19.64  ? 93  SER A CB  1 
ATOM   807  O  OG  . SER A 1 92  ? 23.908 -24.397 20.100 1.00 22.88  ? 93  SER A OG  1 
ATOM   808  N  N   A ARG A 1 93  ? 24.079 -24.628 24.799 0.60 19.03  ? 94  ARG A N   1 
ATOM   809  N  N   B ARG A 1 93  ? 24.057 -24.673 24.796 0.40 18.38  ? 94  ARG A N   1 
ATOM   810  C  CA  A ARG A 1 93  ? 23.592 -25.105 26.100 0.60 19.85  ? 94  ARG A CA  1 
ATOM   811  C  CA  B ARG A 1 93  ? 23.497 -25.106 26.081 0.40 18.96  ? 94  ARG A CA  1 
ATOM   812  C  C   A ARG A 1 93  ? 23.785 -24.044 27.164 0.60 24.18  ? 94  ARG A C   1 
ATOM   813  C  C   B ARG A 1 93  ? 23.771 -24.102 27.173 0.40 23.63  ? 94  ARG A C   1 
ATOM   814  O  O   A ARG A 1 93  ? 24.901 -23.542 27.342 0.60 22.34  ? 94  ARG A O   1 
ATOM   815  O  O   B ARG A 1 93  ? 24.915 -23.672 27.355 0.40 21.93  ? 94  ARG A O   1 
ATOM   816  C  CB  A ARG A 1 93  ? 24.317 -26.396 26.522 0.60 22.55  ? 94  ARG A CB  1 
ATOM   817  C  CB  B ARG A 1 93  ? 23.947 -26.521 26.472 0.40 20.28  ? 94  ARG A CB  1 
ATOM   818  C  CG  A ARG A 1 93  ? 24.171 -27.554 25.518 0.60 27.74  ? 94  ARG A CG  1 
ATOM   819  C  CG  B ARG A 1 93  ? 23.259 -27.590 25.631 0.40 20.51  ? 94  ARG A CG  1 
ATOM   820  C  CD  A ARG A 1 93  ? 25.113 -28.706 25.844 0.60 35.43  ? 94  ARG A CD  1 
ATOM   821  C  CD  B ARG A 1 93  ? 23.962 -28.923 25.697 0.40 32.79  ? 94  ARG A CD  1 
ATOM   822  N  NE  A ARG A 1 93  ? 24.889 -29.221 27.200 0.60 39.94  ? 94  ARG A NE  1 
ATOM   823  N  NE  B ARG A 1 93  ? 23.375 -29.881 24.760 0.40 38.16  ? 94  ARG A NE  1 
ATOM   824  C  CZ  A ARG A 1 93  ? 24.012 -30.172 27.507 0.60 53.30  ? 94  ARG A CZ  1 
ATOM   825  C  CZ  B ARG A 1 93  ? 23.333 -31.194 24.957 0.40 49.28  ? 94  ARG A CZ  1 
ATOM   826  N  NH1 A ARG A 1 93  ? 23.869 -30.570 28.762 0.60 41.10  ? 94  ARG A NH1 1 
ATOM   827  N  NH1 B ARG A 1 93  ? 22.786 -31.990 24.049 0.40 39.17  ? 94  ARG A NH1 1 
ATOM   828  N  NH2 A ARG A 1 93  ? 23.269 -30.731 26.559 0.60 38.79  ? 94  ARG A NH2 1 
ATOM   829  N  NH2 B ARG A 1 93  ? 23.835 -31.721 26.065 0.40 36.79  ? 94  ARG A NH2 1 
ATOM   830  N  N   . LEU A 1 94  ? 22.708 -23.724 27.889 1.00 21.39  ? 95  LEU A N   1 
ATOM   831  C  CA  . LEU A 1 94  ? 22.758 -22.715 28.935 1.00 21.67  ? 95  LEU A CA  1 
ATOM   832  C  C   . LEU A 1 94  ? 22.509 -23.340 30.298 1.00 26.72  ? 95  LEU A C   1 
ATOM   833  O  O   . LEU A 1 94  ? 21.435 -23.906 30.541 1.00 26.01  ? 95  LEU A O   1 
ATOM   834  C  CB  . LEU A 1 94  ? 21.741 -21.612 28.606 1.00 21.93  ? 95  LEU A CB  1 
ATOM   835  C  CG  . LEU A 1 94  ? 21.715 -20.412 29.560 1.00 25.74  ? 95  LEU A CG  1 
ATOM   836  C  CD1 . LEU A 1 94  ? 22.972 -19.548 29.373 1.00 24.00  ? 95  LEU A CD1 1 
ATOM   837  C  CD2 . LEU A 1 94  ? 20.443 -19.604 29.374 1.00 27.34  ? 95  LEU A CD2 1 
ATOM   838  N  N   . ASN A 1 95  ? 23.508 -23.235 31.192 1.00 25.79  ? 96  ASN A N   1 
ATOM   839  C  CA  . ASN A 1 95  ? 23.413 -23.782 32.555 1.00 27.14  ? 96  ASN A CA  1 
ATOM   840  C  C   . ASN A 1 95  ? 22.705 -22.768 33.473 1.00 31.25  ? 96  ASN A C   1 
ATOM   841  O  O   . ASN A 1 95  ? 23.348 -22.065 34.256 1.00 31.40  ? 96  ASN A O   1 
ATOM   842  C  CB  . ASN A 1 95  ? 24.808 -24.180 33.091 1.00 30.31  ? 96  ASN A CB  1 
ATOM   843  C  CG  . ASN A 1 95  ? 24.762 -24.818 34.477 1.00 47.42  ? 96  ASN A CG  1 
ATOM   844  O  OD1 . ASN A 1 95  ? 23.754 -25.387 34.898 1.00 41.73  ? 96  ASN A OD1 1 
ATOM   845  N  ND2 . ASN A 1 95  ? 25.852 -24.733 35.218 1.00 41.26  ? 96  ASN A ND2 1 
ATOM   846  N  N   . LEU A 1 96  ? 21.393 -22.645 33.304 1.00 27.80  ? 97  LEU A N   1 
ATOM   847  C  CA  . LEU A 1 96  ? 20.568 -21.691 34.045 1.00 28.81  ? 97  LEU A CA  1 
ATOM   848  C  C   . LEU A 1 96  ? 20.039 -22.340 35.305 1.00 33.47  ? 97  LEU A C   1 
ATOM   849  O  O   . LEU A 1 96  ? 19.386 -23.393 35.241 1.00 32.82  ? 97  LEU A O   1 
ATOM   850  C  CB  . LEU A 1 96  ? 19.435 -21.213 33.131 1.00 29.62  ? 97  LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 96  ? 18.722 -19.925 33.472 1.00 36.04  ? 97  LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 96  ? 19.729 -18.739 33.588 1.00 35.63  ? 97  LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 96  ? 17.652 -19.642 32.428 1.00 36.65  ? 97  LEU A CD2 1 
ATOM   854  N  N   . ARG A 1 97  ? 20.369 -21.737 36.467 1.00 30.42  ? 98  ARG A N   1 
ATOM   855  C  CA  . ARG A 1 97  ? 19.982 -22.257 37.788 1.00 32.76  ? 98  ARG A CA  1 
ATOM   856  C  C   . ARG A 1 97  ? 19.458 -21.139 38.674 1.00 34.92  ? 98  ARG A C   1 
ATOM   857  O  O   . ARG A 1 97  ? 19.821 -19.972 38.469 1.00 32.65  ? 98  ARG A O   1 
ATOM   858  C  CB  . ARG A 1 97  ? 21.181 -22.941 38.475 1.00 35.48  ? 98  ARG A CB  1 
ATOM   859  C  CG  . ARG A 1 97  ? 21.785 -24.117 37.694 1.00 42.22  ? 98  ARG A CG  1 
ATOM   860  C  CD  . ARG A 1 97  ? 23.046 -24.685 38.338 1.00 57.85  ? 98  ARG A CD  1 
ATOM   861  N  NE  . ARG A 1 97  ? 22.807 -25.206 39.690 1.00 76.39  ? 98  ARG A NE  1 
ATOM   862  C  CZ  . ARG A 1 97  ? 22.351 -26.427 39.965 1.00 96.16  ? 98  ARG A CZ  1 
ATOM   863  N  NH1 . ARG A 1 97  ? 22.156 -26.800 41.224 1.00 85.40  ? 98  ARG A NH1 1 
ATOM   864  N  NH2 . ARG A 1 97  ? 22.079 -27.280 38.984 1.00 83.91  ? 98  ARG A NH2 1 
ATOM   865  N  N   . GLU A 1 98  ? 18.623 -21.480 39.688 1.00 33.13  ? 99  GLU A N   1 
ATOM   866  C  CA  . GLU A 1 98  ? 18.103 -20.463 40.617 1.00 33.80  ? 99  GLU A CA  1 
ATOM   867  C  C   . GLU A 1 98  ? 19.238 -19.578 41.182 1.00 37.65  ? 99  GLU A C   1 
ATOM   868  O  O   . GLU A 1 98  ? 19.081 -18.360 41.280 1.00 38.00  ? 99  GLU A O   1 
ATOM   869  C  CB  . GLU A 1 98  ? 17.324 -21.134 41.774 1.00 37.27  ? 99  GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 98  ? 16.636 -20.151 42.704 1.00 48.47  ? 99  GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 98  ? 15.922 -20.781 43.885 1.00 82.02  ? 99  GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 98  ? 16.495 -21.695 44.524 1.00 78.10  ? 99  GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 98  ? 14.785 -20.348 44.179 1.00 86.16  ? 99  GLU A OE2 1 
ATOM   874  N  N   . GLY A 1 99  ? 20.366 -20.203 41.513 1.00 35.60  ? 100 GLY A N   1 
ATOM   875  C  CA  . GLY A 1 99  ? 21.521 -19.522 42.093 1.00 36.38  ? 100 GLY A CA  1 
ATOM   876  C  C   . GLY A 1 99  ? 22.324 -18.642 41.150 1.00 37.75  ? 100 GLY A C   1 
ATOM   877  O  O   . GLY A 1 99  ? 23.117 -17.817 41.610 1.00 37.63  ? 100 GLY A O   1 
ATOM   878  N  N   . ASN A 1 100 ? 22.132 -18.780 39.827 1.00 32.73  ? 101 ASN A N   1 
ATOM   879  C  CA  . ASN A 1 100 ? 22.920 -17.958 38.895 1.00 30.82  ? 101 ASN A CA  1 
ATOM   880  C  C   . ASN A 1 100 ? 22.090 -17.089 37.939 1.00 33.19  ? 101 ASN A C   1 
ATOM   881  O  O   . ASN A 1 100 ? 22.670 -16.289 37.199 1.00 31.08  ? 101 ASN A O   1 
ATOM   882  C  CB  . ASN A 1 100 ? 23.900 -18.854 38.104 1.00 30.40  ? 101 ASN A CB  1 
ATOM   883  C  CG  . ASN A 1 100 ? 23.239 -19.807 37.122 1.00 37.68  ? 101 ASN A CG  1 
ATOM   884  O  OD1 . ASN A 1 100 ? 22.190 -19.508 36.549 1.00 27.65  ? 101 ASN A OD1 1 
ATOM   885  N  ND2 . ASN A 1 100 ? 23.859 -20.958 36.866 1.00 29.92  ? 101 ASN A ND2 1 
ATOM   886  N  N   . ILE A 1 101 ? 20.754 -17.279 37.908 1.00 30.78  ? 102 ILE A N   1 
ATOM   887  C  CA  . ILE A 1 101 ? 19.877 -16.623 36.926 1.00 30.43  ? 102 ILE A CA  1 
ATOM   888  C  C   . ILE A 1 101 ? 20.006 -15.097 36.911 1.00 32.73  ? 102 ILE A C   1 
ATOM   889  O  O   . ILE A 1 101 ? 20.042 -14.505 35.821 1.00 29.73  ? 102 ILE A O   1 
ATOM   890  C  CB  . ILE A 1 101 ? 18.397 -17.072 37.028 1.00 34.63  ? 102 ILE A CB  1 
ATOM   891  C  CG1 . ILE A 1 101 ? 17.555 -16.471 35.865 1.00 35.37  ? 102 ILE A CG1 1 
ATOM   892  C  CG2 . ILE A 1 101 ? 17.782 -16.813 38.412 1.00 34.72  ? 102 ILE A CG2 1 
ATOM   893  C  CD1 . ILE A 1 101 ? 16.386 -17.307 35.408 1.00 36.95  ? 102 ILE A CD1 1 
ATOM   894  N  N   . MET A 1 102 ? 20.082 -14.456 38.087 1.00 30.84  ? 103 MET A N   1 
ATOM   895  C  CA  . MET A 1 102 ? 20.234 -13.001 38.117 1.00 31.58  ? 103 MET A CA  1 
ATOM   896  C  C   . MET A 1 102 ? 21.538 -12.540 37.475 1.00 32.89  ? 103 MET A C   1 
ATOM   897  O  O   . MET A 1 102 ? 21.500 -11.601 36.681 1.00 30.48  ? 103 MET A O   1 
ATOM   898  C  CB  . MET A 1 102 ? 20.073 -12.427 39.544 1.00 35.87  ? 103 MET A CB  1 
ATOM   899  C  CG  . MET A 1 102 ? 18.701 -12.688 40.158 1.00 42.47  ? 103 MET A CG  1 
ATOM   900  S  SD  . MET A 1 102 ? 17.276 -12.324 39.092 1.00 48.62  ? 103 MET A SD  1 
ATOM   901  C  CE  . MET A 1 102 ? 17.295 -10.513 39.127 1.00 46.13  ? 103 MET A CE  1 
ATOM   902  N  N   . ALA A 1 103 ? 22.683 -13.209 37.786 1.00 29.61  ? 104 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 103 ? 23.999 -12.853 37.215 1.00 29.11  ? 104 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 103 ? 23.994 -13.149 35.716 1.00 29.80  ? 104 ALA A C   1 
ATOM   905  O  O   . ALA A 1 103 ? 24.470 -12.332 34.926 1.00 27.76  ? 104 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 103 ? 25.108 -13.659 37.881 1.00 30.61  ? 104 ALA A CB  1 
ATOM   907  N  N   . VAL A 1 104 ? 23.436 -14.313 35.330 1.00 24.53  ? 105 VAL A N   1 
ATOM   908  C  CA  . VAL A 1 104 ? 23.357 -14.686 33.904 1.00 22.65  ? 105 VAL A CA  1 
ATOM   909  C  C   . VAL A 1 104 ? 22.549 -13.650 33.108 1.00 25.64  ? 105 VAL A C   1 
ATOM   910  O  O   . VAL A 1 104 ? 23.028 -13.220 32.049 1.00 24.64  ? 105 VAL A O   1 
ATOM   911  C  CB  . VAL A 1 104 ? 22.859 -16.139 33.692 1.00 25.91  ? 105 VAL A CB  1 
ATOM   912  C  CG1 . VAL A 1 104 ? 22.614 -16.434 32.208 1.00 24.09  ? 105 VAL A CG1 1 
ATOM   913  C  CG2 . VAL A 1 104 ? 23.867 -17.135 34.255 1.00 26.02  ? 105 VAL A CG2 1 
ATOM   914  N  N   A MET A 1 105 ? 21.354 -13.246 33.599 0.65 24.86  ? 106 MET A N   1 
ATOM   915  N  N   B MET A 1 105 ? 21.354 -13.249 33.597 0.35 24.79  ? 106 MET A N   1 
ATOM   916  C  CA  A MET A 1 105 ? 20.537 -12.261 32.881 0.65 25.84  ? 106 MET A CA  1 
ATOM   917  C  CA  B MET A 1 105 ? 20.532 -12.263 32.888 0.35 25.72  ? 106 MET A CA  1 
ATOM   918  C  C   A MET A 1 105 ? 21.254 -10.918 32.761 0.65 28.62  ? 106 MET A C   1 
ATOM   919  C  C   B MET A 1 105 ? 21.246 -10.920 32.763 0.35 29.16  ? 106 MET A C   1 
ATOM   920  O  O   A MET A 1 105 ? 21.237 -10.319 31.685 0.65 26.72  ? 106 MET A O   1 
ATOM   921  O  O   B MET A 1 105 ? 21.240 -10.333 31.680 0.35 27.82  ? 106 MET A O   1 
ATOM   922  C  CB  A MET A 1 105 ? 19.172 -12.059 33.538 0.65 29.82  ? 106 MET A CB  1 
ATOM   923  C  CB  B MET A 1 105 ? 19.163 -12.075 33.546 0.35 29.68  ? 106 MET A CB  1 
ATOM   924  C  CG  A MET A 1 105 ? 18.249 -11.178 32.710 0.65 33.95  ? 106 MET A CG  1 
ATOM   925  C  CG  B MET A 1 105 ? 18.226 -11.236 32.704 0.35 33.99  ? 106 MET A CG  1 
ATOM   926  S  SD  A MET A 1 105 ? 16.565 -11.183 33.344 0.65 39.73  ? 106 MET A SD  1 
ATOM   927  S  SD  B MET A 1 105 ? 16.629 -11.016 33.489 0.35 40.11  ? 106 MET A SD  1 
ATOM   928  C  CE  A MET A 1 105 ? 16.748 -10.121 34.830 0.65 37.79  ? 106 MET A CE  1 
ATOM   929  C  CE  B MET A 1 105 ? 16.175 -9.451  32.811 0.35 37.78  ? 106 MET A CE  1 
ATOM   930  N  N   . ALA A 1 106 ? 21.856 -10.438 33.864 1.00 26.97  ? 107 ALA A N   1 
ATOM   931  C  CA  . ALA A 1 106 ? 22.606 -9.155  33.870 1.00 26.98  ? 107 ALA A CA  1 
ATOM   932  C  C   . ALA A 1 106 ? 23.771 -9.202  32.864 1.00 27.82  ? 107 ALA A C   1 
ATOM   933  O  O   . ALA A 1 106 ? 23.968 -8.244  32.096 1.00 25.88  ? 107 ALA A O   1 
ATOM   934  C  CB  . ALA A 1 106 ? 23.122 -8.857  35.271 1.00 28.64  ? 107 ALA A CB  1 
ATOM   935  N  N   . THR A 1 107 ? 24.505 -10.336 32.827 1.00 23.60  ? 108 THR A N   1 
ATOM   936  C  CA  . THR A 1 107 ? 25.615 -10.510 31.882 1.00 22.48  ? 108 THR A CA  1 
ATOM   937  C  C   . THR A 1 107 ? 25.090 -10.550 30.436 1.00 25.91  ? 108 THR A C   1 
ATOM   938  O  O   . THR A 1 107 ? 25.675 -9.898  29.571 1.00 23.53  ? 108 THR A O   1 
ATOM   939  C  CB  . THR A 1 107 ? 26.518 -11.712 32.255 1.00 27.68  ? 108 THR A CB  1 
ATOM   940  O  OG1 . THR A 1 107 ? 26.790 -11.698 33.664 1.00 26.64  ? 108 THR A OG1 1 
ATOM   941  C  CG2 . THR A 1 107 ? 27.842 -11.717 31.478 1.00 26.42  ? 108 THR A CG2 1 
ATOM   942  N  N   . ALA A 1 108 ? 23.976 -11.280 30.182 1.00 22.18  ? 109 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 108 ? 23.391 -11.373 28.833 1.00 20.74  ? 109 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 108 ? 22.875 -10.008 28.364 1.00 23.92  ? 109 ALA A C   1 
ATOM   945  O  O   . ALA A 1 108 ? 23.009 -9.681  27.181 1.00 22.88  ? 109 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 108 ? 22.289 -12.434 28.795 1.00 21.06  ? 109 ALA A CB  1 
ATOM   947  N  N   . MET A 1 109 ? 22.335 -9.181  29.282 1.00 22.92  ? 110 MET A N   1 
ATOM   948  C  CA  . MET A 1 109 ? 21.888 -7.834  28.890 1.00 22.88  ? 110 MET A CA  1 
ATOM   949  C  C   . MET A 1 109 ? 23.079 -6.969  28.452 1.00 25.96  ? 110 MET A C   1 
ATOM   950  O  O   . MET A 1 109 ? 23.036 -6.327  27.396 1.00 25.89  ? 110 MET A O   1 
ATOM   951  C  CB  . MET A 1 109 ? 21.118 -7.171  30.047 1.00 26.31  ? 110 MET A CB  1 
ATOM   952  C  CG  . MET A 1 109 ? 19.731 -7.766  30.230 1.00 31.71  ? 110 MET A CG  1 
ATOM   953  S  SD  . MET A 1 109 ? 18.992 -7.194  31.774 1.00 39.25  ? 110 MET A SD  1 
ATOM   954  C  CE  . MET A 1 109 ? 18.713 -5.475  31.375 1.00 37.41  ? 110 MET A CE  1 
ATOM   955  N  N   . TYR A 1 110 ? 24.160 -7.024  29.224 1.00 24.59  ? 111 TYR A N   1 
ATOM   956  C  CA  . TYR A 1 110 ? 25.405 -6.295  28.946 1.00 24.13  ? 111 TYR A CA  1 
ATOM   957  C  C   . TYR A 1 110 ? 26.033 -6.782  27.609 1.00 25.48  ? 111 TYR A C   1 
ATOM   958  O  O   . TYR A 1 110 ? 26.446 -5.965  26.777 1.00 24.10  ? 111 TYR A O   1 
ATOM   959  C  CB  . TYR A 1 110 ? 26.378 -6.529  30.102 1.00 24.48  ? 111 TYR A CB  1 
ATOM   960  C  CG  . TYR A 1 110 ? 27.795 -6.051  29.859 1.00 24.20  ? 111 TYR A CG  1 
ATOM   961  C  CD1 . TYR A 1 110 ? 28.117 -4.696  29.924 1.00 26.56  ? 111 TYR A CD1 1 
ATOM   962  C  CD2 . TYR A 1 110 ? 28.831 -6.960  29.652 1.00 23.61  ? 111 TYR A CD2 1 
ATOM   963  C  CE1 . TYR A 1 110 ? 29.429 -4.255  29.724 1.00 24.17  ? 111 TYR A CE1 1 
ATOM   964  C  CE2 . TYR A 1 110 ? 30.148 -6.535  29.493 1.00 23.18  ? 111 TYR A CE2 1 
ATOM   965  C  CZ  . TYR A 1 110 ? 30.443 -5.182  29.560 1.00 25.09  ? 111 TYR A CZ  1 
ATOM   966  O  OH  . TYR A 1 110 ? 31.736 -4.779  29.421 1.00 24.86  ? 111 TYR A OH  1 
ATOM   967  N  N   . LEU A 1 111 ? 26.086 -8.109  27.402 1.00 21.20  ? 112 LEU A N   1 
ATOM   968  C  CA  . LEU A 1 111 ? 26.666 -8.685  26.193 1.00 19.80  ? 112 LEU A CA  1 
ATOM   969  C  C   . LEU A 1 111 ? 25.739 -8.548  24.985 1.00 23.73  ? 112 LEU A C   1 
ATOM   970  O  O   . LEU A 1 111 ? 26.176 -8.815  23.870 1.00 22.77  ? 112 LEU A O   1 
ATOM   971  C  CB  . LEU A 1 111 ? 27.021 -10.172 26.438 1.00 18.00  ? 112 LEU A CB  1 
ATOM   972  C  CG  . LEU A 1 111 ? 28.163 -10.442 27.457 1.00 20.88  ? 112 LEU A CG  1 
ATOM   973  C  CD1 . LEU A 1 111 ? 28.454 -11.962 27.549 1.00 21.28  ? 112 LEU A CD1 1 
ATOM   974  C  CD2 . LEU A 1 111 ? 29.468 -9.664  27.064 1.00 22.06  ? 112 LEU A CD2 1 
ATOM   975  N  N   . GLN A 1 112 ? 24.452 -8.191  25.210 1.00 21.83  ? 113 GLN A N   1 
ATOM   976  C  CA  . GLN A 1 112 ? 23.448 -8.062  24.139 1.00 22.90  ? 113 GLN A CA  1 
ATOM   977  C  C   . GLN A 1 112 ? 23.231 -9.429  23.457 1.00 24.30  ? 113 GLN A C   1 
ATOM   978  O  O   . GLN A 1 112 ? 23.536 -9.624  22.272 1.00 22.57  ? 113 GLN A O   1 
ATOM   979  C  CB  . GLN A 1 112 ? 23.833 -6.966  23.126 1.00 24.67  ? 113 GLN A CB  1 
ATOM   980  C  CG  . GLN A 1 112 ? 24.010 -5.575  23.764 1.00 27.15  ? 113 GLN A CG  1 
ATOM   981  C  CD  . GLN A 1 112 ? 24.719 -4.628  22.826 1.00 36.16  ? 113 GLN A CD  1 
ATOM   982  O  OE1 . GLN A 1 112 ? 24.584 -4.713  21.615 1.00 29.82  ? 113 GLN A OE1 1 
ATOM   983  N  NE2 . GLN A 1 112 ? 25.512 -3.723  23.361 1.00 34.34  ? 113 GLN A NE2 1 
ATOM   984  N  N   . MET A 1 113 ? 22.736 -10.383 24.249 1.00 21.30  ? 114 MET A N   1 
ATOM   985  C  CA  . MET A 1 113 ? 22.428 -11.763 23.816 1.00 21.26  ? 114 MET A CA  1 
ATOM   986  C  C   . MET A 1 113 ? 20.929 -11.915 24.070 1.00 26.96  ? 114 MET A C   1 
ATOM   987  O  O   . MET A 1 113 ? 20.490 -12.357 25.142 1.00 25.33  ? 114 MET A O   1 
ATOM   988  C  CB  . MET A 1 113 ? 23.270 -12.745 24.630 1.00 22.33  ? 114 MET A CB  1 
ATOM   989  C  CG  . MET A 1 113 ? 24.768 -12.601 24.331 1.00 23.75  ? 114 MET A CG  1 
ATOM   990  S  SD  . MET A 1 113 ? 25.795 -13.635 25.383 1.00 25.77  ? 114 MET A SD  1 
ATOM   991  C  CE  . MET A 1 113 ? 25.440 -15.312 24.639 1.00 22.77  ? 114 MET A CE  1 
ATOM   992  N  N   . GLU A 1 114 ? 20.146 -11.385 23.127 1.00 27.33  ? 115 GLU A N   1 
ATOM   993  C  CA  . GLU A 1 114 ? 18.691 -11.229 23.276 1.00 29.85  ? 115 GLU A CA  1 
ATOM   994  C  C   . GLU A 1 114 ? 17.919 -12.506 23.586 1.00 30.77  ? 115 GLU A C   1 
ATOM   995  O  O   . GLU A 1 114 ? 16.990 -12.438 24.382 1.00 29.81  ? 115 GLU A O   1 
ATOM   996  C  CB  . GLU A 1 114 ? 18.076 -10.535 22.052 1.00 33.25  ? 115 GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 114 ? 18.643 -9.141  21.822 1.00 47.23  ? 115 GLU A CG  1 
ATOM   998  N  N   . HIS A 1 115 ? 18.278 -13.651 22.984 1.00 26.49  ? 116 HIS A N   1 
ATOM   999  C  CA  . HIS A 1 115 ? 17.528 -14.881 23.265 1.00 28.35  ? 116 HIS A CA  1 
ATOM   1000 C  C   . HIS A 1 115 ? 17.739 -15.365 24.703 1.00 29.71  ? 116 HIS A C   1 
ATOM   1001 O  O   . HIS A 1 115 ? 16.787 -15.826 25.334 1.00 30.39  ? 116 HIS A O   1 
ATOM   1002 C  CB  . HIS A 1 115 ? 17.814 -15.971 22.233 1.00 29.87  ? 116 HIS A CB  1 
ATOM   1003 C  CG  . HIS A 1 115 ? 17.344 -15.622 20.858 1.00 34.84  ? 116 HIS A CG  1 
ATOM   1004 N  ND1 . HIS A 1 115 ? 16.006 -15.417 20.586 1.00 38.64  ? 116 HIS A ND1 1 
ATOM   1005 C  CD2 . HIS A 1 115 ? 18.050 -15.493 19.710 1.00 36.58  ? 116 HIS A CD2 1 
ATOM   1006 C  CE1 . HIS A 1 115 ? 15.940 -15.142 19.293 1.00 38.56  ? 116 HIS A CE1 1 
ATOM   1007 N  NE2 . HIS A 1 115 ? 17.142 -15.187 18.725 1.00 37.68  ? 116 HIS A NE2 1 
ATOM   1008 N  N   . VAL A 1 116 ? 18.971 -15.211 25.234 1.00 24.40  ? 117 VAL A N   1 
ATOM   1009 C  CA  . VAL A 1 116 ? 19.267 -15.547 26.632 1.00 24.35  ? 117 VAL A CA  1 
ATOM   1010 C  C   . VAL A 1 116 ? 18.485 -14.628 27.583 1.00 29.44  ? 117 VAL A C   1 
ATOM   1011 O  O   . VAL A 1 116 ? 17.868 -15.111 28.547 1.00 27.44  ? 117 VAL A O   1 
ATOM   1012 C  CB  . VAL A 1 116 ? 20.785 -15.553 26.937 1.00 26.02  ? 117 VAL A CB  1 
ATOM   1013 C  CG1 . VAL A 1 116 ? 21.038 -15.802 28.429 1.00 25.83  ? 117 VAL A CG1 1 
ATOM   1014 C  CG2 . VAL A 1 116 ? 21.503 -16.599 26.081 1.00 25.22  ? 117 VAL A CG2 1 
ATOM   1015 N  N   . VAL A 1 117 ? 18.497 -13.302 27.314 1.00 25.98  ? 118 VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 117 ? 17.747 -12.337 28.131 1.00 26.75  ? 118 VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 117 ? 16.261 -12.756 28.188 1.00 32.51  ? 118 VAL A C   1 
ATOM   1018 O  O   . VAL A 1 117 ? 15.706 -12.828 29.282 1.00 32.03  ? 118 VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 117 ? 17.938 -10.869 27.659 1.00 29.67  ? 118 VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 117 ? 17.104 -9.889  28.504 1.00 30.73  ? 118 VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 117 ? 19.414 -10.476 27.703 1.00 28.14  ? 118 VAL A CG2 1 
ATOM   1022 N  N   A ASP A 1 118 ? 15.621 -12.956 27.017 0.41 31.04  ? 119 ASP A N   1 
ATOM   1023 N  N   B ASP A 1 118 ? 15.694 -13.162 27.035 0.59 30.10  ? 119 ASP A N   1 
ATOM   1024 C  CA  A ASP A 1 118 ? 14.200 -13.318 26.895 0.41 32.74  ? 119 ASP A CA  1 
ATOM   1025 C  CA  B ASP A 1 118 ? 14.313 -13.648 26.903 0.59 31.05  ? 119 ASP A CA  1 
ATOM   1026 C  C   A ASP A 1 118 ? 13.781 -14.524 27.739 0.41 37.19  ? 119 ASP A C   1 
ATOM   1027 C  C   B ASP A 1 118 ? 14.003 -14.859 27.803 0.59 33.61  ? 119 ASP A C   1 
ATOM   1028 O  O   A ASP A 1 118 ? 12.713 -14.492 28.344 0.41 38.33  ? 119 ASP A O   1 
ATOM   1029 O  O   B ASP A 1 118 ? 13.051 -14.782 28.580 0.59 33.33  ? 119 ASP A O   1 
ATOM   1030 C  CB  A ASP A 1 118 ? 13.805 -13.528 25.421 0.41 34.95  ? 119 ASP A CB  1 
ATOM   1031 C  CB  B ASP A 1 118 ? 13.980 -13.951 25.428 0.59 33.32  ? 119 ASP A CB  1 
ATOM   1032 C  CG  A ASP A 1 118 ? 13.599 -12.252 24.624 0.41 47.76  ? 119 ASP A CG  1 
ATOM   1033 C  CG  B ASP A 1 118 ? 12.524 -14.288 25.157 0.59 47.56  ? 119 ASP A CG  1 
ATOM   1034 O  OD1 A ASP A 1 118 ? 13.058 -11.276 25.189 0.41 51.14  ? 119 ASP A OD1 1 
ATOM   1035 O  OD1 B ASP A 1 118 ? 11.645 -13.484 25.539 0.59 50.33  ? 119 ASP A OD1 1 
ATOM   1036 O  OD2 A ASP A 1 118 ? 13.972 -12.229 23.433 0.41 53.26  ? 119 ASP A OD2 1 
ATOM   1037 O  OD2 B ASP A 1 118 ? 12.267 -15.344 24.541 0.59 52.56  ? 119 ASP A OD2 1 
ATOM   1038 N  N   A THR A 1 119 ? 14.625 -15.567 27.797 0.41 32.37  ? 120 THR A N   1 
ATOM   1039 N  N   B THR A 1 119 ? 14.803 -15.953 27.733 0.59 28.72  ? 120 THR A N   1 
ATOM   1040 C  CA  A THR A 1 119 ? 14.354 -16.790 28.563 0.41 32.59  ? 120 THR A CA  1 
ATOM   1041 C  CA  B THR A 1 119 ? 14.526 -17.131 28.579 0.59 29.26  ? 120 THR A CA  1 
ATOM   1042 C  C   A THR A 1 119 ? 14.530 -16.565 30.038 0.41 34.99  ? 120 THR A C   1 
ATOM   1043 C  C   B THR A 1 119 ? 14.734 -16.848 30.079 0.59 32.81  ? 120 THR A C   1 
ATOM   1044 O  O   A THR A 1 119 ? 13.681 -17.001 30.813 0.41 35.55  ? 120 THR A O   1 
ATOM   1045 O  O   B THR A 1 119 ? 14.097 -17.505 30.899 0.59 32.38  ? 120 THR A O   1 
ATOM   1046 C  CB  A THR A 1 119 ? 15.206 -17.922 28.039 0.41 39.44  ? 120 THR A CB  1 
ATOM   1047 C  CB  B THR A 1 119 ? 15.280 -18.391 28.121 0.59 30.31  ? 120 THR A CB  1 
ATOM   1048 O  OG1 A THR A 1 119 ? 14.937 -17.968 26.658 0.41 38.47  ? 120 THR A OG1 1 
ATOM   1049 O  OG1 B THR A 1 119 ? 14.638 -19.519 28.723 0.59 31.79  ? 120 THR A OG1 1 
ATOM   1050 C  CG2 A THR A 1 119 ? 14.855 -19.259 28.664 0.41 39.65  ? 120 THR A CG2 1 
ATOM   1051 C  CG2 B THR A 1 119 ? 16.752 -18.383 28.515 0.59 23.08  ? 120 THR A CG2 1 
ATOM   1052 N  N   . CYS A 1 120 ? 15.636 -15.897 30.434 1.00 29.94  ? 121 CYS A N   1 
ATOM   1053 C  CA  . CYS A 1 120 ? 15.883 -15.547 31.846 1.00 30.40  ? 121 CYS A CA  1 
ATOM   1054 C  C   . CYS A 1 120 ? 14.669 -14.825 32.390 1.00 37.03  ? 121 CYS A C   1 
ATOM   1055 O  O   . CYS A 1 120 ? 14.183 -15.170 33.476 1.00 36.11  ? 121 CYS A O   1 
ATOM   1056 C  CB  . CYS A 1 120 ? 17.127 -14.677 31.960 1.00 29.24  ? 121 CYS A CB  1 
ATOM   1057 S  SG  . CYS A 1 120 ? 18.668 -15.594 31.793 1.00 31.58  ? 121 CYS A SG  1 
ATOM   1058 N  N   . ARG A 1 121 ? 14.152 -13.847 31.604 1.00 35.73  ? 122 ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 121 ? 12.952 -13.075 31.937 1.00 37.56  ? 122 ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 121 ? 11.756 -14.018 32.202 1.00 41.98  ? 122 ARG A C   1 
ATOM   1061 O  O   . ARG A 1 121 ? 11.053 -13.854 33.207 1.00 42.03  ? 122 ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 121 ? 12.610 -12.104 30.798 1.00 39.09  ? 122 ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 121 ? 13.454 -10.845 30.798 1.00 54.69  ? 122 ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 121 ? 12.625 -9.614  30.482 1.00 69.82  ? 122 ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 121 ? 12.995 -9.025  29.193 1.00 78.18  ? 122 ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 121 ? 13.917 -8.080  29.030 1.00 87.05  ? 122 ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 121 ? 14.584 -7.606  30.076 1.00 68.73  ? 122 ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 121 ? 14.182 -7.605  27.821 1.00 74.27  ? 122 ARG A NH2 1 
ATOM   1069 N  N   . LYS A 1 122 ? 11.560 -15.014 31.316 1.00 39.27  ? 123 LYS A N   1 
ATOM   1070 C  CA  . LYS A 1 122 ? 10.474 -16.003 31.409 1.00 40.62  ? 123 LYS A CA  1 
ATOM   1071 C  C   . LYS A 1 122 ? 10.635 -16.912 32.625 1.00 44.18  ? 123 LYS A C   1 
ATOM   1072 O  O   . LYS A 1 122 ? 9.650  -17.167 33.307 1.00 44.05  ? 123 LYS A O   1 
ATOM   1073 C  CB  . LYS A 1 122 ? 10.371 -16.842 30.117 1.00 42.20  ? 123 LYS A CB  1 
ATOM   1074 C  CG  . LYS A 1 122 ? 9.882  -16.048 28.911 1.00 59.68  ? 123 LYS A CG  1 
ATOM   1075 C  CD  . LYS A 1 122 ? 9.595  -16.946 27.709 1.00 70.90  ? 123 LYS A CD  1 
ATOM   1076 C  CE  . LYS A 1 122 ? 9.612  -16.209 26.387 1.00 81.21  ? 123 LYS A CE  1 
ATOM   1077 N  NZ  . LYS A 1 122 ? 8.559  -15.160 26.289 1.00 89.94  ? 123 LYS A NZ  1 
ATOM   1078 N  N   . PHE A 1 123 ? 11.870 -17.406 32.895 1.00 39.90  ? 124 PHE A N   1 
ATOM   1079 C  CA  . PHE A 1 123 ? 12.147 -18.264 34.052 1.00 40.14  ? 124 PHE A CA  1 
ATOM   1080 C  C   . PHE A 1 123 ? 11.947 -17.499 35.369 1.00 44.45  ? 124 PHE A C   1 
ATOM   1081 O  O   . PHE A 1 123 ? 11.403 -18.064 36.323 1.00 44.08  ? 124 PHE A O   1 
ATOM   1082 C  CB  . PHE A 1 123 ? 13.547 -18.884 33.956 1.00 40.33  ? 124 PHE A CB  1 
ATOM   1083 C  CG  . PHE A 1 123 ? 13.660 -20.181 33.172 1.00 41.87  ? 124 PHE A CG  1 
ATOM   1084 C  CD1 . PHE A 1 123 ? 13.094 -20.305 31.903 1.00 44.77  ? 124 PHE A CD1 1 
ATOM   1085 C  CD2 . PHE A 1 123 ? 14.396 -21.252 33.670 1.00 44.26  ? 124 PHE A CD2 1 
ATOM   1086 C  CE1 . PHE A 1 123 ? 13.219 -21.494 31.173 1.00 44.84  ? 124 PHE A CE1 1 
ATOM   1087 C  CE2 . PHE A 1 123 ? 14.524 -22.440 32.935 1.00 45.82  ? 124 PHE A CE2 1 
ATOM   1088 C  CZ  . PHE A 1 123 ? 13.937 -22.550 31.693 1.00 43.33  ? 124 PHE A CZ  1 
ATOM   1089 N  N   . ILE A 1 124 ? 12.328 -16.202 35.406 1.00 39.79  ? 125 ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 124 ? 12.117 -15.361 36.598 1.00 41.33  ? 125 ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 124 ? 10.618 -15.127 36.844 1.00 48.37  ? 125 ILE A C   1 
ATOM   1092 O  O   . ILE A 1 124 ? 10.164 -15.255 37.987 1.00 49.12  ? 125 ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 124 ? 12.953 -14.051 36.527 1.00 43.36  ? 125 ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 124 ? 14.445 -14.380 36.672 1.00 41.90  ? 125 ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 124 ? 12.522 -13.013 37.601 1.00 46.36  ? 125 ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 124 ? 15.373 -13.316 36.134 1.00 48.06  ? 125 ILE A CD1 1 
ATOM   1097 N  N   . LYS A 1 125 ? 9.853  -14.830 35.768 1.00 46.78  ? 126 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 125 ? 8.404  -14.581 35.826 1.00 49.27  ? 126 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 125 ? 7.627  -15.810 36.347 1.00 54.60  ? 126 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 125 ? 6.658  -15.648 37.089 1.00 55.20  ? 126 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 125 ? 7.877  -14.137 34.450 1.00 52.50  ? 126 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 125 ? 6.506  -13.467 34.499 1.00 70.95  ? 126 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 125 ? 5.884  -13.361 33.114 1.00 83.29  ? 126 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 125 ? 4.463  -12.855 33.166 1.00 97.13  ? 126 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 125 ? 3.808  -12.919 31.832 1.00 107.26 ? 126 LYS A NZ  1 
ATOM   1106 N  N   . ALA A 1 126 ? 8.078  -17.027 35.989 1.00 49.87  ? 127 ALA A N   1 
ATOM   1107 C  CA  . ALA A 1 126 ? 7.459  -18.278 36.436 1.00 51.34  ? 127 ALA A CA  1 
ATOM   1108 C  C   . ALA A 1 126 ? 7.598  -18.496 37.957 1.00 56.84  ? 127 ALA A C   1 
ATOM   1109 O  O   . ALA A 1 126 ? 6.726  -19.111 38.556 1.00 57.38  ? 127 ALA A O   1 
ATOM   1110 C  CB  . ALA A 1 126 ? 8.059  -19.454 35.678 1.00 50.34  ? 127 ALA A CB  1 
ATOM   1111 N  N   . SER A 1 127 ? 8.692  -18.004 38.566 1.00 54.92  ? 128 SER A N   1 
ATOM   1112 C  CA  . SER A 1 127 ? 8.967  -18.146 40.001 1.00 57.69  ? 128 SER A CA  1 
ATOM   1113 C  C   . SER A 1 127 ? 8.264  -17.097 40.891 1.00 65.56  ? 128 SER A C   1 
ATOM   1114 O  O   . SER A 1 127 ? 8.139  -17.325 42.099 1.00 67.99  ? 128 SER A O   1 
ATOM   1115 C  CB  . SER A 1 127 ? 10.472 -18.141 40.262 1.00 61.36  ? 128 SER A CB  1 
ATOM   1116 O  OG  . SER A 1 127 ? 11.047 -19.412 40.001 1.00 72.84  ? 128 SER A OG  1 
ATOM   1117 N  N   . GLU A 1 128 ? 7.790  -15.972 40.305 1.00 61.73  ? 129 GLU A N   1 
ATOM   1118 C  CA  . GLU A 1 128 ? 7.106  -14.910 41.053 1.00 84.04  ? 129 GLU A CA  1 
ATOM   1119 C  C   . GLU A 1 128 ? 5.646  -15.256 41.372 1.00 126.47 ? 129 GLU A C   1 
ATOM   1120 O  O   . GLU A 1 128 ? 5.368  -16.274 42.001 1.00 94.14  ? 129 GLU A O   1 
ATOM   1121 C  CB  . GLU A 1 128 ? 7.234  -13.544 40.344 1.00 84.52  ? 129 GLU A CB  1 
ATOM   1122 C  CG  . GLU A 1 128 ? 6.225  -13.286 39.232 1.00 94.42  ? 129 GLU A CG  1 
ATOM   1123 C  CD  . GLU A 1 128 ? 6.431  -12.049 38.375 1.00 114.63 ? 129 GLU A CD  1 
ATOM   1124 O  OE1 . GLU A 1 128 ? 7.526  -11.441 38.432 1.00 105.39 ? 129 GLU A OE1 1 
ATOM   1125 O  OE2 . GLU A 1 128 ? 5.489  -11.693 37.629 1.00 109.64 ? 129 GLU A OE2 1 
HETATM 1126 C  C   . ACE B 2 1   ? 21.224 -35.106 5.873  1.00 27.15  ? 0   ACE D C   1 
HETATM 1127 O  O   . ACE B 2 1   ? 21.273 -33.952 6.325  1.00 27.75  ? 0   ACE D O   1 
HETATM 1128 C  CH3 . ACE B 2 1   ? 21.418 -36.296 6.769  1.00 26.93  ? 0   ACE D CH3 1 
ATOM   1129 N  N   A TRP B 2 2   ? 20.967 -35.372 4.599  0.78 24.24  ? 1   TRP D N   1 
ATOM   1130 N  N   B TRP B 2 2   ? 21.002 -35.386 4.587  0.22 24.69  ? 1   TRP D N   1 
ATOM   1131 C  CA  A TRP B 2 2   ? 20.768 -34.323 3.609  0.78 23.77  ? 1   TRP D CA  1 
ATOM   1132 C  CA  B TRP B 2 2   ? 20.751 -34.351 3.582  0.22 24.15  ? 1   TRP D CA  1 
ATOM   1133 C  C   A TRP B 2 2   ? 19.275 -34.169 3.309  0.78 27.49  ? 1   TRP D C   1 
ATOM   1134 C  C   B TRP B 2 2   ? 19.253 -34.165 3.388  0.22 27.22  ? 1   TRP D C   1 
ATOM   1135 O  O   A TRP B 2 2   ? 18.537 -35.162 3.292  0.78 28.37  ? 1   TRP D O   1 
ATOM   1136 O  O   B TRP B 2 2   ? 18.497 -35.138 3.472  0.22 26.98  ? 1   TRP D O   1 
ATOM   1137 C  CB  A TRP B 2 2   ? 21.555 -34.659 2.329  0.78 22.29  ? 1   TRP D CB  1 
ATOM   1138 C  CB  B TRP B 2 2   ? 21.446 -34.658 2.231  0.22 22.82  ? 1   TRP D CB  1 
ATOM   1139 C  CG  A TRP B 2 2   ? 23.054 -34.613 2.522  0.78 22.29  ? 1   TRP D CG  1 
ATOM   1140 C  CG  B TRP B 2 2   ? 20.768 -35.689 1.373  0.22 23.66  ? 1   TRP D CG  1 
ATOM   1141 C  CD1 A TRP B 2 2   ? 23.859 -35.619 2.976  0.78 24.84  ? 1   TRP D CD1 1 
ATOM   1142 C  CD1 B TRP B 2 2   ? 21.041 -37.023 1.329  0.22 26.75  ? 1   TRP D CD1 1 
ATOM   1143 C  CD2 A TRP B 2 2   ? 23.910 -33.488 2.287  0.78 22.02  ? 1   TRP D CD2 1 
ATOM   1144 C  CD2 B TRP B 2 2   ? 19.720 -35.463 0.415  0.22 23.36  ? 1   TRP D CD2 1 
ATOM   1145 N  NE1 A TRP B 2 2   ? 25.164 -35.166 3.087  0.78 24.14  ? 1   TRP D NE1 1 
ATOM   1146 N  NE1 B TRP B 2 2   ? 20.198 -37.652 0.444  0.22 26.26  ? 1   TRP D NE1 1 
ATOM   1147 C  CE2 A TRP B 2 2   ? 25.234 -33.894 2.586  0.78 25.28  ? 1   TRP D CE2 1 
ATOM   1148 C  CE2 B TRP B 2 2   ? 19.390 -36.716 -0.147 0.22 27.39  ? 1   TRP D CE2 1 
ATOM   1149 C  CE3 A TRP B 2 2   ? 23.688 -32.166 1.862  0.78 22.69  ? 1   TRP D CE3 1 
ATOM   1150 C  CE3 B TRP B 2 2   ? 19.010 -34.325 -0.006 0.22 24.36  ? 1   TRP D CE3 1 
ATOM   1151 C  CZ2 A TRP B 2 2   ? 26.332 -33.036 2.444  0.78 24.18  ? 1   TRP D CZ2 1 
ATOM   1152 C  CZ2 B TRP B 2 2   ? 18.393 -36.862 -1.119 0.22 26.55  ? 1   TRP D CZ2 1 
ATOM   1153 C  CZ3 A TRP B 2 2   ? 24.783 -31.336 1.672  0.78 23.37  ? 1   TRP D CZ3 1 
ATOM   1154 C  CZ3 B TRP B 2 2   ? 18.010 -34.474 -0.955 0.22 26.06  ? 1   TRP D CZ3 1 
ATOM   1155 C  CH2 A TRP B 2 2   ? 26.082 -31.765 1.980  0.78 24.29  ? 1   TRP D CH2 1 
ATOM   1156 C  CH2 B TRP B 2 2   ? 17.717 -35.728 -1.509 0.22 26.51  ? 1   TRP D CH2 1 
ATOM   1157 N  N   . VAL B 2 3   ? 18.823 -32.925 3.110  1.00 23.11  ? 2   VAL D N   1 
ATOM   1158 C  CA  . VAL B 2 3   ? 17.406 -32.600 2.868  1.00 22.96  ? 2   VAL D CA  1 
ATOM   1159 C  C   . VAL B 2 3   ? 17.268 -31.536 1.766  1.00 24.61  ? 2   VAL D C   1 
ATOM   1160 O  O   . VAL B 2 3   ? 18.235 -30.840 1.428  1.00 24.03  ? 2   VAL D O   1 
ATOM   1161 C  CB  . VAL B 2 3   ? 16.664 -32.112 4.176  1.00 26.30  ? 2   VAL D CB  1 
ATOM   1162 C  CG1 . VAL B 2 3   ? 16.717 -33.147 5.311  1.00 25.72  ? 2   VAL D CG1 1 
ATOM   1163 C  CG2 . VAL B 2 3   ? 17.178 -30.740 4.656  1.00 26.14  ? 2   VAL D CG2 1 
ATOM   1164 N  N   . ILE B 2 4   ? 16.033 -31.350 1.302  1.00 22.43  ? 3   ILE D N   1 
ATOM   1165 C  CA  . ILE B 2 4   ? 15.660 -30.264 0.406  1.00 23.31  ? 3   ILE D CA  1 
ATOM   1166 C  C   . ILE B 2 4   ? 15.288 -29.125 1.393  1.00 26.93  ? 3   ILE D C   1 
ATOM   1167 O  O   . ILE B 2 4   ? 14.278 -29.244 2.096  1.00 27.48  ? 3   ILE D O   1 
ATOM   1168 C  CB  . ILE B 2 4   ? 14.453 -30.639 -0.505 1.00 25.54  ? 3   ILE D CB  1 
ATOM   1169 C  CG1 . ILE B 2 4   ? 14.736 -31.910 -1.402 1.00 24.05  ? 3   ILE D CG1 1 
ATOM   1170 C  CG2 . ILE B 2 4   ? 14.020 -29.411 -1.345 1.00 27.64  ? 3   ILE D CG2 1 
ATOM   1171 C  CD1 . ILE B 2 4   ? 16.034 -31.817 -2.364 1.00 27.58  ? 3   ILE D CD1 1 
ATOM   1172 N  N   . PRO B 2 5   ? 16.088 -28.039 1.492  1.00 25.99  ? 4   PRO D N   1 
ATOM   1173 C  CA  . PRO B 2 5   ? 15.761 -26.970 2.455  1.00 26.45  ? 4   PRO D CA  1 
ATOM   1174 C  C   . PRO B 2 5   ? 14.486 -26.204 2.097  1.00 30.86  ? 4   PRO D C   1 
ATOM   1175 O  O   . PRO B 2 5   ? 14.200 -26.011 0.914  1.00 30.02  ? 4   PRO D O   1 
ATOM   1176 C  CB  . PRO B 2 5   ? 17.000 -26.059 2.409  1.00 28.04  ? 4   PRO D CB  1 
ATOM   1177 C  CG  . PRO B 2 5   ? 17.543 -26.254 1.007  1.00 31.96  ? 4   PRO D CG  1 
ATOM   1178 C  CD  . PRO B 2 5   ? 17.318 -27.723 0.728  1.00 27.19  ? 4   PRO D CD  1 
ATOM   1179 N  N   . ALA B 2 6   ? 13.852 -25.595 3.107  1.00 28.27  ? 5   ALA D N   1 
HETATM 1180 C  C4  . 7ZO C 3 .   ? 27.271 -10.308 11.840 1.00 25.75  ? 201 7ZO A C4  1 
HETATM 1181 C  C5  . 7ZO C 3 .   ? 25.243 -9.399  12.212 1.00 27.75  ? 201 7ZO A C5  1 
HETATM 1182 C  C6  . 7ZO C 3 .   ? 23.944 -10.744 18.108 1.00 27.09  ? 201 7ZO A C6  1 
HETATM 1183 C  C7  . 7ZO C 3 .   ? 23.454 -9.443  18.161 1.00 27.66  ? 201 7ZO A C7  1 
HETATM 1184 C  C8  . 7ZO C 3 .   ? 25.506 -10.068 16.397 1.00 24.57  ? 201 7ZO A C8  1 
HETATM 1185 C  C10 . 7ZO C 3 .   ? 26.343 -10.229 14.030 1.00 23.31  ? 201 7ZO A C10 1 
HETATM 1186 C  C1  . 7ZO C 3 .   ? 23.935 -8.455  17.305 1.00 26.69  ? 201 7ZO A C1  1 
HETATM 1187 C  C2  . 7ZO C 3 .   ? 24.951 -8.782  16.414 1.00 25.44  ? 201 7ZO A C2  1 
HETATM 1188 C  C3  . 7ZO C 3 .   ? 24.966 -11.064 17.217 1.00 24.67  ? 201 7ZO A C3  1 
HETATM 1189 C  C9  . 7ZO C 3 .   ? 27.390 -10.611 13.186 1.00 23.29  ? 201 7ZO A C9  1 
HETATM 1190 C  C11 . 7ZO C 3 .   ? 22.228 -10.570 19.727 1.00 31.66  ? 201 7ZO A C11 1 
HETATM 1191 C  C12 . 7ZO C 3 .   ? 23.201 -11.563 19.125 1.00 29.51  ? 201 7ZO A C12 1 
HETATM 1192 N  N13 . 7ZO C 3 .   ? 26.197 -9.697  11.334 1.00 28.95  ? 201 7ZO A N13 1 
HETATM 1193 N  N14 . 7ZO C 3 .   ? 25.242 -9.626  13.531 1.00 25.95  ? 201 7ZO A N14 1 
HETATM 1194 N  N15 . 7ZO C 3 .   ? 22.446 -9.367  19.133 1.00 27.50  ? 201 7ZO A N15 1 
HETATM 1195 N  N16 . 7ZO C 3 .   ? 26.359 -10.516 15.360 1.00 21.70  ? 201 7ZO A N16 1 
HETATM 1196 O  O17 . 7ZO C 3 .   ? 21.380 -10.798 20.590 1.00 30.99  ? 201 7ZO A O17 1 
HETATM 1197 CL CL1 . 7ZO C 3 .   ? 28.813 -11.393 13.768 0.99 23.52  ? 201 7ZO A CL1 1 
HETATM 1198 CL CL  . CL  D 4 .   ? 21.314 -15.211 22.569 1.00 32.10  ? 202 CL  A CL  1 
HETATM 1199 S  S   A DMS E 5 .   ? 17.571 -35.342 -1.240 0.78 44.09  ? 101 DMS D S   1 
HETATM 1200 O  O   A DMS E 5 .   ? 16.296 -35.123 -0.571 0.78 45.56  ? 101 DMS D O   1 
HETATM 1201 C  C1  A DMS E 5 .   ? 18.728 -34.470 -0.210 0.78 42.68  ? 101 DMS D C1  1 
HETATM 1202 C  C2  A DMS E 5 .   ? 18.001 -36.987 -0.804 0.78 44.10  ? 101 DMS D C2  1 
HETATM 1203 O  O   . HOH F 6 .   ? 35.585 -25.673 25.567 1.00 36.32  ? 301 HOH A O   1 
HETATM 1204 O  O   . HOH F 6 .   ? 22.766 -5.307  19.785 1.00 54.52  ? 302 HOH A O   1 
HETATM 1205 O  O   . HOH F 6 .   ? 25.864 -3.412  26.372 1.00 32.37  ? 303 HOH A O   1 
HETATM 1206 O  O   . HOH F 6 .   ? 38.384 -14.915 15.474 1.00 31.22  ? 304 HOH A O   1 
HETATM 1207 O  O   . HOH F 6 .   ? 41.247 -21.640 25.178 1.00 40.77  ? 305 HOH A O   1 
HETATM 1208 O  O   . HOH F 6 .   ? 37.928 2.454   19.675 1.00 39.21  ? 306 HOH A O   1 
HETATM 1209 O  O   . HOH F 6 .   ? 44.483 -0.866  17.893 1.00 49.76  ? 307 HOH A O   1 
HETATM 1210 O  O   . HOH F 6 .   ? 37.610 -20.367 26.963 1.00 32.03  ? 308 HOH A O   1 
HETATM 1211 O  O   . HOH F 6 .   ? 44.920 -11.227 18.622 1.00 51.22  ? 309 HOH A O   1 
HETATM 1212 O  O   . HOH F 6 .   ? 43.600 -6.628  31.926 1.00 43.05  ? 310 HOH A O   1 
HETATM 1213 O  O   . HOH F 6 .   ? 16.512 -27.548 -3.246 1.00 48.95  ? 311 HOH A O   1 
HETATM 1214 O  O   . HOH F 6 .   ? 27.295 -35.336 11.784 1.00 56.29  ? 312 HOH A O   1 
HETATM 1215 O  O   . HOH F 6 .   ? 17.990 -29.385 7.655  1.00 31.14  ? 313 HOH A O   1 
HETATM 1216 O  O   . HOH F 6 .   ? 33.312 -20.773 29.566 1.00 47.31  ? 314 HOH A O   1 
HETATM 1217 O  O   . HOH F 6 .   ? 20.770 -5.851  26.012 1.00 39.57  ? 315 HOH A O   1 
HETATM 1218 O  O   . HOH F 6 .   ? 29.910 -32.080 9.550  1.00 41.84  ? 316 HOH A O   1 
HETATM 1219 O  O   . HOH F 6 .   ? 32.437 -24.678 32.215 1.00 60.16  ? 317 HOH A O   1 
HETATM 1220 O  O   . HOH F 6 .   ? 22.975 -28.242 12.634 1.00 23.34  ? 318 HOH A O   1 
HETATM 1221 O  O   . HOH F 6 .   ? 41.324 -16.915 15.199 1.00 34.41  ? 319 HOH A O   1 
HETATM 1222 O  O   . HOH F 6 .   ? 22.551 -27.601 17.724 1.00 49.76  ? 320 HOH A O   1 
HETATM 1223 O  O   . HOH F 6 .   ? 31.778 -0.824  15.865 1.00 39.40  ? 321 HOH A O   1 
HETATM 1224 O  O   . HOH F 6 .   ? 19.790 -9.525  36.982 1.00 40.76  ? 322 HOH A O   1 
HETATM 1225 O  O   . HOH F 6 .   ? 13.502 -14.344 21.808 1.00 62.06  ? 323 HOH A O   1 
HETATM 1226 O  O   . HOH F 6 .   ? 26.819 -31.950 16.144 1.00 40.77  ? 324 HOH A O   1 
HETATM 1227 O  O   . HOH F 6 .   ? 41.650 -12.781 14.310 1.00 79.96  ? 325 HOH A O   1 
HETATM 1228 O  O   . HOH F 6 .   ? 32.327 -8.868  39.639 1.00 53.58  ? 326 HOH A O   1 
HETATM 1229 O  O   . HOH F 6 .   ? 28.227 -23.687 31.651 1.00 38.98  ? 327 HOH A O   1 
HETATM 1230 O  O   . HOH F 6 .   ? 23.478 -5.696  32.894 1.00 36.55  ? 328 HOH A O   1 
HETATM 1231 O  O   . HOH F 6 .   ? 27.235 -10.116 35.830 1.00 36.69  ? 329 HOH A O   1 
HETATM 1232 O  O   . HOH F 6 .   ? 14.258 -16.809 23.406 1.00 40.64  ? 330 HOH A O   1 
HETATM 1233 O  O   . HOH F 6 .   ? 30.291 1.507   33.944 1.00 60.70  ? 331 HOH A O   1 
HETATM 1234 O  O   . HOH F 6 .   ? 27.323 -28.135 18.649 1.00 28.77  ? 332 HOH A O   1 
HETATM 1235 O  O   . HOH F 6 .   ? 20.498 -13.375 20.402 1.00 50.01  ? 333 HOH A O   1 
HETATM 1236 O  O   . HOH F 6 .   ? 26.746 -16.476 38.592 1.00 46.10  ? 334 HOH A O   1 
HETATM 1237 O  O   . HOH F 6 .   ? 29.555 -2.131  13.804 1.00 61.69  ? 335 HOH A O   1 
HETATM 1238 O  O   . HOH F 6 .   ? 12.715 -20.362 42.397 1.00 58.75  ? 336 HOH A O   1 
HETATM 1239 O  O   . HOH F 6 .   ? 21.491 -27.020 14.513 0.50 38.26  ? 337 HOH A O   1 
HETATM 1240 O  O   . HOH F 6 .   ? 30.341 -0.475  36.832 1.00 50.55  ? 338 HOH A O   1 
HETATM 1241 O  O   . HOH F 6 .   ? 7.068  -17.048 32.421 1.00 53.36  ? 339 HOH A O   1 
HETATM 1242 O  O   . HOH F 6 .   ? 34.873 -18.866 13.852 0.50 25.87  ? 340 HOH A O   1 
HETATM 1243 O  O   . HOH F 6 .   ? 21.746 -29.611 -5.230 1.00 36.35  ? 341 HOH A O   1 
HETATM 1244 O  O   . HOH F 6 .   ? 21.913 -24.930 18.308 1.00 21.69  ? 342 HOH A O   1 
HETATM 1245 O  O   . HOH F 6 .   ? 26.020 -21.795 38.618 1.00 37.11  ? 343 HOH A O   1 
HETATM 1246 O  O   . HOH F 6 .   ? 15.408 -9.915  24.849 1.00 50.15  ? 344 HOH A O   1 
HETATM 1247 O  O   . HOH F 6 .   ? 28.280 -8.845  39.904 1.00 45.54  ? 345 HOH A O   1 
HETATM 1248 O  O   . HOH F 6 .   ? 27.199 -2.462  16.096 1.00 62.18  ? 346 HOH A O   1 
HETATM 1249 O  O   . HOH F 6 .   ? 25.695 -2.762  19.929 1.00 58.99  ? 347 HOH A O   1 
HETATM 1250 O  O   . HOH F 6 .   ? 41.322 -6.985  35.891 1.00 44.24  ? 348 HOH A O   1 
HETATM 1251 O  O   . HOH F 6 .   ? 36.787 -5.609  12.158 1.00 36.20  ? 349 HOH A O   1 
HETATM 1252 O  O   . HOH F 6 .   ? 4.317  -20.226 37.802 1.00 58.96  ? 350 HOH A O   1 
HETATM 1253 O  O   . HOH F 6 .   ? 24.819 -26.778 19.013 1.00 32.83  ? 351 HOH A O   1 
HETATM 1254 O  O   . HOH F 6 .   ? 20.869 -7.162  19.729 1.00 51.86  ? 352 HOH A O   1 
HETATM 1255 O  O   . HOH F 6 .   ? 26.408 -7.701  36.783 1.00 50.59  ? 353 HOH A O   1 
HETATM 1256 O  O   . HOH F 6 .   ? 21.471 -29.932 14.172 1.00 71.29  ? 354 HOH A O   1 
HETATM 1257 O  O   . HOH F 6 .   ? 44.420 -12.456 41.189 1.00 53.27  ? 355 HOH A O   1 
HETATM 1258 O  O   . HOH F 6 .   ? 29.058 -31.164 7.247  1.00 28.18  ? 356 HOH A O   1 
HETATM 1259 O  O   . HOH F 6 .   ? 24.045 -15.803 21.181 1.00 29.13  ? 357 HOH A O   1 
HETATM 1260 O  O   . HOH F 6 .   ? 43.509 -10.576 35.353 1.00 61.85  ? 358 HOH A O   1 
HETATM 1261 O  O   . HOH F 6 .   ? 43.923 -4.360  25.754 1.00 45.45  ? 359 HOH A O   1 
HETATM 1262 O  O   . HOH F 6 .   ? 45.928 -14.216 21.525 1.00 57.43  ? 360 HOH A O   1 
HETATM 1263 O  O   . HOH F 6 .   ? 26.100 -22.552 29.909 1.00 25.70  ? 361 HOH A O   1 
HETATM 1264 O  O   . HOH F 6 .   ? 23.240 -17.155 44.326 1.00 60.69  ? 362 HOH A O   1 
HETATM 1265 O  O   A HOH F 6 .   ? 19.037 -22.948 4.249  0.60 35.56  ? 363 HOH A O   1 
HETATM 1266 O  O   . HOH F 6 .   ? 42.385 -10.355 15.371 1.00 46.28  ? 364 HOH A O   1 
HETATM 1267 O  O   . HOH F 6 .   ? 46.844 -21.845 17.823 1.00 40.48  ? 365 HOH A O   1 
HETATM 1268 O  O   . HOH F 6 .   ? 22.233 -34.016 26.212 1.00 70.99  ? 366 HOH A O   1 
HETATM 1269 O  O   . HOH F 6 .   ? 10.814 -11.338 34.424 1.00 51.29  ? 367 HOH A O   1 
HETATM 1270 O  O   . HOH F 6 .   ? 29.340 -27.372 20.633 1.00 25.39  ? 368 HOH A O   1 
HETATM 1271 O  O   . HOH F 6 .   ? 46.157 -15.847 27.639 1.00 61.72  ? 369 HOH A O   1 
HETATM 1272 O  O   . HOH F 6 .   ? 46.292 -29.763 21.307 1.00 69.79  ? 370 HOH A O   1 
HETATM 1273 O  O   . HOH F 6 .   ? 28.460 -24.209 34.312 1.00 51.69  ? 371 HOH A O   1 
HETATM 1274 O  O   . HOH F 6 .   ? 30.683 -28.809 22.619 1.00 37.48  ? 372 HOH A O   1 
HETATM 1275 O  O   . HOH F 6 .   ? 45.931 -8.895  43.973 1.00 49.83  ? 373 HOH A O   1 
HETATM 1276 O  O   . HOH F 6 .   ? 46.237 -18.963 19.706 1.00 45.93  ? 374 HOH A O   1 
HETATM 1277 O  O   . HOH F 6 .   ? 26.020 -19.136 41.689 1.00 68.41  ? 375 HOH A O   1 
HETATM 1278 O  O   . HOH F 6 .   ? 20.055 -15.747 40.813 1.00 33.59  ? 376 HOH A O   1 
HETATM 1279 O  O   . HOH F 6 .   ? 34.145 -7.864  35.622 1.00 31.36  ? 377 HOH A O   1 
HETATM 1280 O  O   . HOH F 6 .   ? 38.982 -18.912 33.357 1.00 48.58  ? 378 HOH A O   1 
HETATM 1281 O  O   . HOH F 6 .   ? 37.482 3.455   15.641 1.00 42.33  ? 379 HOH A O   1 
HETATM 1282 O  O   . HOH F 6 .   ? 25.896 -4.522  17.884 1.00 47.27  ? 380 HOH A O   1 
HETATM 1283 O  O   . HOH F 6 .   ? 11.321 -14.891 40.558 1.00 86.45  ? 381 HOH A O   1 
HETATM 1284 O  O   . HOH F 6 .   ? 44.682 -8.621  17.899 1.00 59.55  ? 382 HOH A O   1 
HETATM 1285 O  O   . HOH F 6 .   ? 37.408 -6.455  34.253 1.00 38.27  ? 383 HOH A O   1 
HETATM 1286 O  O   . HOH F 6 .   ? 22.626 -34.003 8.856  1.00 31.14  ? 384 HOH A O   1 
HETATM 1287 O  O   . HOH F 6 .   ? 47.197 -25.265 21.646 1.00 51.91  ? 385 HOH A O   1 
HETATM 1288 O  O   . HOH F 6 .   ? 31.818 -31.831 14.604 1.00 40.43  ? 386 HOH A O   1 
HETATM 1289 O  O   . HOH F 6 .   ? 18.051 -34.581 8.320  1.00 31.04  ? 387 HOH A O   1 
HETATM 1290 O  O   . HOH F 6 .   ? 27.684 -23.017 13.852 0.50 25.52  ? 388 HOH A O   1 
HETATM 1291 O  O   . HOH F 6 .   ? 17.417 -24.461 -2.272 1.00 61.63  ? 389 HOH A O   1 
HETATM 1292 O  O   . HOH F 6 .   ? 45.251 -12.648 23.617 1.00 44.38  ? 390 HOH A O   1 
HETATM 1293 O  O   . HOH F 6 .   ? 40.347 -19.573 28.999 1.00 35.12  ? 391 HOH A O   1 
HETATM 1294 O  O   . HOH F 6 .   ? 33.022 -29.647 21.505 1.00 41.82  ? 392 HOH A O   1 
HETATM 1295 O  O   . HOH F 6 .   ? 26.334 -7.869  9.071  1.00 45.52  ? 393 HOH A O   1 
HETATM 1296 O  O   . HOH F 6 .   ? 22.471 -9.993  14.350 1.00 39.64  ? 394 HOH A O   1 
HETATM 1297 O  O   . HOH F 6 .   ? 42.121 -6.093  11.836 1.00 65.12  ? 395 HOH A O   1 
HETATM 1298 O  O   . HOH F 6 .   ? 10.107 -11.655 39.846 1.00 59.06  ? 396 HOH A O   1 
HETATM 1299 O  O   . HOH F 6 .   ? 37.911 -16.248 12.764 1.00 47.01  ? 397 HOH A O   1 
HETATM 1300 O  O   . HOH F 6 .   ? 23.615 -15.630 17.817 1.00 41.67  ? 398 HOH A O   1 
HETATM 1301 O  O   . HOH F 6 .   ? 41.191 -17.044 35.176 1.00 40.60  ? 399 HOH A O   1 
HETATM 1302 O  O   . HOH F 6 .   ? 21.038 -23.047 42.069 1.00 47.18  ? 400 HOH A O   1 
HETATM 1303 O  O   . HOH F 6 .   ? 27.133 -1.670  21.939 1.00 48.71  ? 401 HOH A O   1 
HETATM 1304 O  O   . HOH F 6 .   ? 45.460 -10.583 30.336 1.00 56.80  ? 402 HOH A O   1 
HETATM 1305 O  O   . HOH F 6 .   ? 19.659 -27.411 10.095 1.00 52.51  ? 403 HOH A O   1 
HETATM 1306 O  O   . HOH F 6 .   ? 22.890 -14.806 40.334 1.00 33.43  ? 404 HOH A O   1 
HETATM 1307 O  O   . HOH F 6 .   ? 37.045 -2.303  11.470 1.00 61.49  ? 405 HOH A O   1 
HETATM 1308 O  O   . HOH F 6 .   ? 44.561 -16.449 29.737 1.00 46.74  ? 406 HOH A O   1 
HETATM 1309 O  O   . HOH F 6 .   ? 35.399 2.074   13.603 1.00 55.91  ? 407 HOH A O   1 
HETATM 1310 O  O   . HOH F 6 .   ? 33.737 -33.081 12.302 1.00 43.02  ? 408 HOH A O   1 
HETATM 1311 O  O   . HOH F 6 .   ? 44.696 -8.025  15.152 1.00 71.65  ? 409 HOH A O   1 
HETATM 1312 O  O   . HOH F 6 .   ? 32.131 -15.589 39.803 1.00 34.18  ? 410 HOH A O   1 
HETATM 1313 O  O   . HOH F 6 .   ? 47.067 -20.246 21.915 1.00 62.24  ? 411 HOH A O   1 
HETATM 1314 O  O   . HOH F 6 .   ? 34.886 -33.401 21.889 1.00 54.10  ? 412 HOH A O   1 
HETATM 1315 O  O   . HOH F 6 .   ? 35.218 -29.746 23.599 1.00 46.92  ? 413 HOH A O   1 
HETATM 1316 O  O   . HOH F 6 .   ? 41.960 -8.078  13.705 1.00 59.35  ? 414 HOH A O   1 
HETATM 1317 O  O   . HOH F 6 .   ? 30.375 -10.474 40.540 1.00 42.04  ? 415 HOH A O   1 
HETATM 1318 O  O   . HOH F 6 .   ? 26.061 -29.227 22.577 1.00 56.70  ? 416 HOH A O   1 
HETATM 1319 O  O   . HOH F 6 .   ? 39.944 -5.559  33.865 1.00 40.61  ? 417 HOH A O   1 
HETATM 1320 O  O   . HOH F 6 .   ? 33.931 -17.594 39.345 1.00 58.11  ? 418 HOH A O   1 
HETATM 1321 O  O   . HOH F 6 .   ? 45.887 -17.167 17.158 1.00 63.76  ? 419 HOH A O   1 
HETATM 1322 O  O   B HOH F 6 .   ? 37.184 -11.895 40.060 0.50 33.32  ? 420 HOH A O   1 
HETATM 1323 O  O   . HOH F 6 .   ? 44.301 -25.997 26.628 1.00 58.30  ? 421 HOH A O   1 
HETATM 1324 O  O   . HOH F 6 .   ? 28.744 -16.044 41.339 1.00 66.34  ? 422 HOH A O   1 
HETATM 1325 O  O   . HOH F 6 .   ? 23.498 -30.432 19.230 1.00 64.77  ? 423 HOH A O   1 
HETATM 1326 O  O   . HOH F 6 .   ? 27.433 -25.628 28.182 1.00 54.19  ? 424 HOH A O   1 
HETATM 1327 O  O   . HOH F 6 .   ? 29.616 -0.805  22.212 1.00 55.54  ? 425 HOH A O   1 
HETATM 1328 O  O   . HOH F 6 .   ? 33.499 -0.286  19.995 1.00 44.46  ? 426 HOH A O   1 
HETATM 1329 O  O   . HOH F 6 .   ? 29.801 -22.570 36.747 1.00 72.80  ? 427 HOH A O   1 
HETATM 1330 O  O   . HOH F 6 .   ? 45.741 -5.495  23.680 1.00 45.69  ? 428 HOH A O   1 
HETATM 1331 O  O   . HOH F 6 .   ? 28.366 -2.563  11.375 1.00 72.56  ? 429 HOH A O   1 
HETATM 1332 O  O   . HOH F 6 .   ? 42.791 -18.276 30.723 1.00 45.79  ? 430 HOH A O   1 
HETATM 1333 O  O   . HOH F 6 .   ? 31.906 -26.195 27.028 1.00 45.73  ? 431 HOH A O   1 
HETATM 1334 O  O   . HOH F 6 .   ? 25.763 -15.834 41.044 1.00 50.64  ? 432 HOH A O   1 
HETATM 1335 O  O   . HOH F 6 .   ? 31.947 0.111   13.306 1.00 57.04  ? 433 HOH A O   1 
HETATM 1336 O  O   . HOH F 6 .   ? 47.878 -23.339 19.859 1.00 63.87  ? 434 HOH A O   1 
HETATM 1337 O  O   . HOH F 6 .   ? 32.442 -4.119  41.236 1.00 62.40  ? 435 HOH A O   1 
HETATM 1338 O  O   . HOH F 6 .   ? 28.321 -29.187 26.873 1.00 78.89  ? 436 HOH A O   1 
HETATM 1339 O  O   . HOH F 6 .   ? 37.724 -26.960 28.484 1.00 61.65  ? 437 HOH A O   1 
HETATM 1340 O  O   . HOH F 6 .   ? 27.096 -34.585 17.949 1.00 71.27  ? 438 HOH A O   1 
HETATM 1341 O  O   . HOH F 6 .   ? 20.110 -35.332 10.163 1.00 37.67  ? 439 HOH A O   1 
HETATM 1342 O  O   . HOH F 6 .   ? 35.198 -4.112  10.599 1.00 46.42  ? 440 HOH A O   1 
HETATM 1343 O  O   . HOH F 6 .   ? 19.444 -31.737 13.947 1.00 69.06  ? 441 HOH A O   1 
HETATM 1344 O  O   . HOH F 6 .   ? 24.247 -21.454 41.027 1.00 56.09  ? 442 HOH A O   1 
HETATM 1345 O  O   . HOH F 6 .   ? 36.942 -24.410 27.546 1.00 54.50  ? 443 HOH A O   1 
HETATM 1346 O  O   . HOH F 6 .   ? 30.936 -34.410 14.802 1.00 60.92  ? 444 HOH A O   1 
HETATM 1347 O  O   . HOH F 6 .   ? 23.017 -2.709  26.164 1.00 62.78  ? 445 HOH A O   1 
HETATM 1348 O  O   . HOH F 6 .   ? 47.140 -13.068 28.502 1.00 60.17  ? 446 HOH A O   1 
HETATM 1349 O  O   . HOH F 6 .   ? 11.958 -18.565 22.393 1.00 57.37  ? 447 HOH A O   1 
HETATM 1350 O  O   . HOH F 6 .   ? 46.578 -14.646 17.893 1.00 67.94  ? 448 HOH A O   1 
HETATM 1351 O  O   . HOH F 6 .   ? 34.553 -18.770 36.118 1.00 61.87  ? 449 HOH A O   1 
HETATM 1352 O  O   . HOH F 6 .   ? 33.775 -10.994 41.555 0.50 52.97  ? 450 HOH A O   1 
HETATM 1353 O  O   . HOH F 6 .   ? 47.103 -11.877 25.454 1.00 63.50  ? 451 HOH A O   1 
HETATM 1354 O  O   . HOH F 6 .   ? 13.622 -16.154 39.776 1.00 78.15  ? 452 HOH A O   1 
HETATM 1355 O  O   . HOH F 6 .   ? 32.274 -1.054  22.275 1.00 58.72  ? 453 HOH A O   1 
HETATM 1356 O  O   . HOH F 6 .   ? 43.071 -3.095  33.709 1.00 61.73  ? 454 HOH A O   1 
HETATM 1357 O  O   . HOH F 6 .   ? 47.350 -28.576 17.718 1.00 62.93  ? 455 HOH A O   1 
HETATM 1358 O  O   . HOH F 6 .   ? 19.251 -7.549  35.219 1.00 59.57  ? 456 HOH A O   1 
HETATM 1359 O  O   A HOH F 6 .   ? 12.068 -20.773 27.816 0.78 48.47  ? 457 HOH A O   1 
HETATM 1360 O  O   . HOH F 6 .   ? 17.082 -28.064 9.832  1.00 51.66  ? 458 HOH A O   1 
HETATM 1361 O  O   . HOH F 6 .   ? 25.335 -5.714  35.203 1.00 56.56  ? 459 HOH A O   1 
HETATM 1362 O  O   . HOH F 6 .   ? 15.863 -15.538 41.177 1.00 59.11  ? 460 HOH A O   1 
HETATM 1363 O  O   . HOH F 6 .   ? 44.264 -13.444 13.852 0.50 60.53  ? 461 HOH A O   1 
HETATM 1364 O  O   . HOH F 6 .   ? 17.323 -8.060  24.776 1.00 57.16  ? 462 HOH A O   1 
HETATM 1365 O  O   . HOH F 6 .   ? 33.775 -13.973 41.555 0.50 37.98  ? 463 HOH A O   1 
HETATM 1366 O  O   . HOH F 6 .   ? 32.023 -23.834 34.788 1.00 66.12  ? 464 HOH A O   1 
HETATM 1367 O  O   . HOH F 6 .   ? 28.134 -29.814 24.232 1.00 64.54  ? 465 HOH A O   1 
HETATM 1368 O  O   . HOH F 6 .   ? 19.033 -28.012 13.851 0.50 67.56  ? 466 HOH A O   1 
HETATM 1369 O  O   . HOH F 6 .   ? 45.409 -12.798 16.251 1.00 63.17  ? 467 HOH A O   1 
HETATM 1370 O  O   . HOH F 6 .   ? 23.252 -4.558  17.206 1.00 71.37  ? 468 HOH A O   1 
HETATM 1371 O  O   . HOH F 6 .   ? 32.646 -20.484 37.046 1.00 72.48  ? 469 HOH A O   1 
HETATM 1372 O  O   . HOH F 6 .   ? 21.108 -5.612  34.695 1.00 56.71  ? 470 HOH A O   1 
HETATM 1373 O  O   . HOH F 6 .   ? 34.961 -23.688 32.560 1.00 62.20  ? 471 HOH A O   1 
HETATM 1374 O  O   . HOH F 6 .   ? 32.917 -0.757  42.864 1.00 56.84  ? 472 HOH A O   1 
HETATM 1375 O  O   . HOH F 6 .   ? 16.673 -6.670  34.640 1.00 74.54  ? 473 HOH A O   1 
HETATM 1376 O  O   . HOH G 6 .   ? 12.365 -24.238 -0.059 1.00 50.41  ? 201 HOH D O   1 
HETATM 1377 O  O   . HOH G 6 .   ? 15.032 -25.790 -1.788 1.00 41.16  ? 202 HOH D O   1 
HETATM 1378 O  O   . HOH G 6 .   ? 21.052 -38.268 4.037  1.00 46.78  ? 203 HOH D O   1 
HETATM 1379 O  O   . HOH G 6 .   ? 11.669 -23.516 3.036  1.00 53.02  ? 204 HOH D O   1 
HETATM 1380 O  O   . HOH G 6 .   ? 17.695 -36.356 6.117  1.00 40.32  ? 205 HOH D O   1 
HETATM 1381 O  O   . HOH G 6 .   ? 20.912 -39.457 -2.195 1.00 56.10  ? 206 HOH D O   1 
HETATM 1382 O  O   . HOH G 6 .   ? 18.648 -40.656 0.716  1.00 69.17  ? 207 HOH D O   1 
HETATM 1383 O  O   . HOH G 6 .   ? 10.677 -24.845 5.564  1.00 54.89  ? 208 HOH D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP A 5   ? 0.7688 0.9883 0.7169 0.0354  -0.1210 -0.0211 6   ASP A N   
2    C CA  . ASP A 5   ? 0.7623 0.9759 0.6953 0.0186  -0.1123 -0.0242 6   ASP A CA  
3    C C   . ASP A 5   ? 0.7437 0.9871 0.7004 0.0059  -0.1077 -0.0411 6   ASP A C   
4    O O   . ASP A 5   ? 0.7367 1.0067 0.7198 0.0095  -0.1119 -0.0504 6   ASP A O   
5    C CB  . ASP A 5   ? 0.7851 0.9668 0.7090 0.0102  -0.0962 -0.0172 6   ASP A CB  
6    C CG  . ASP A 5   ? 0.9757 1.1383 0.8685 0.0004  -0.0913 -0.0130 6   ASP A CG  
7    O OD1 . ASP A 5   ? 0.9789 1.1547 0.8705 -0.0111 -0.0887 -0.0224 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.0788 1.2127 0.9484 0.0030  -0.0888 -0.0013 6   ASP A OD2 
9    N N   . SER A 6   ? 0.6392 0.8775 0.5858 -0.0094 -0.0984 -0.0458 7   SER A N   
10   C CA  . SER A 6   ? 0.5926 0.8516 0.5565 -0.0233 -0.0918 -0.0613 7   SER A CA  
11   C C   . SER A 6   ? 0.5385 0.7799 0.5129 -0.0342 -0.0740 -0.0634 7   SER A C   
12   O O   . SER A 6   ? 0.5298 0.7740 0.5069 -0.0473 -0.0656 -0.0732 7   SER A O   
13   C CB  . SER A 6   ? 0.6695 0.9364 0.6134 -0.0317 -0.0958 -0.0666 7   SER A CB  
14   O OG  . SER A 6   ? 0.8404 1.0798 0.7578 -0.0369 -0.0886 -0.0587 7   SER A OG  
15   N N   . CYS A 7   ? 0.4156 0.6386 0.3955 -0.0279 -0.0691 -0.0548 8   CYS A N   
16   C CA  . CYS A 7   ? 0.3764 0.5821 0.3651 -0.0355 -0.0548 -0.0556 8   CYS A CA  
17   C C   . CYS A 7   ? 0.3641 0.5837 0.3757 -0.0438 -0.0487 -0.0680 8   CYS A C   
18   O O   . CYS A 7   ? 0.3579 0.6007 0.3835 -0.0418 -0.0546 -0.0747 8   CYS A O   
19   C CB  . CYS A 7   ? 0.3902 0.5764 0.3795 -0.0265 -0.0529 -0.0443 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.4718 0.6314 0.4321 -0.0222 -0.0532 -0.0306 8   CYS A SG  
21   N N   . ILE A 8   ? 0.2625 0.4672 0.2768 -0.0529 -0.0370 -0.0713 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2220 0.4280 0.2525 -0.0605 -0.0292 -0.0799 9   ILE A CA  
23   C C   . ILE A 8   ? 0.2492 0.4351 0.2840 -0.0550 -0.0245 -0.0713 9   ILE A C   
24   O O   . ILE A 8   ? 0.2425 0.4128 0.2676 -0.0490 -0.0248 -0.0616 9   ILE A O   
25   C CB  . ILE A 8   ? 0.2578 0.4592 0.2869 -0.0737 -0.0205 -0.0903 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.2678 0.4458 0.2855 -0.0745 -0.0143 -0.0859 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.2696 0.4952 0.2968 -0.0803 -0.0254 -0.1008 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3202 0.4893 0.3375 -0.0853 -0.0052 -0.0962 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.1935 0.3785 0.2409 -0.0584 -0.0194 -0.0754 10  GLN A N   
30   N N   B GLN A 9   ? 0.1935 0.3803 0.2414 -0.0579 -0.0201 -0.0755 10  GLN A N   
31   C CA  A GLN A 9   ? 0.1896 0.3563 0.2394 -0.0536 -0.0156 -0.0678 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.1849 0.3543 0.2362 -0.0536 -0.0160 -0.0685 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2352 0.3853 0.2871 -0.0622 -0.0061 -0.0722 10  GLN A C   
34   C C   B GLN A 9   ? 0.2197 0.3715 0.2718 -0.0624 -0.0064 -0.0727 10  GLN A C   
35   O O   A GLN A 9   ? 0.2305 0.3883 0.2881 -0.0712 -0.0022 -0.0818 10  GLN A O   
36   O O   B GLN A 9   ? 0.2190 0.3768 0.2752 -0.0722 -0.0021 -0.0826 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2007 0.3807 0.2611 -0.0459 -0.0205 -0.0660 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.1915 0.3757 0.2552 -0.0474 -0.0200 -0.0686 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2279 0.3908 0.2908 -0.0418 -0.0163 -0.0594 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.2683 0.4365 0.3364 -0.0464 -0.0139 -0.0647 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5282 0.7069 0.6047 -0.0368 -0.0188 -0.0617 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4215 0.5886 0.4917 -0.0345 -0.0185 -0.0563 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.3947 0.5874 0.4829 -0.0438 -0.0151 -0.0718 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.2927 0.4698 0.3610 -0.0252 -0.0271 -0.0524 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.5616 0.7382 0.6369 -0.0249 -0.0243 -0.0535 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.3016 0.4543 0.3739 -0.0345 -0.0130 -0.0534 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2192 0.3461 0.2656 -0.0595 -0.0026 -0.0655 11  PHE A N   
48   N N   B PHE A 10  ? 0.1846 0.3140 0.2321 -0.0589 -0.0033 -0.0654 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2191 0.3263 0.2642 -0.0654 0.0046  -0.0681 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.1851 0.2937 0.2307 -0.0643 0.0038  -0.0672 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2360 0.3380 0.2851 -0.0638 0.0062  -0.0648 11  PHE A C   
52   C C   B PHE A 10  ? 0.2249 0.3292 0.2749 -0.0631 0.0056  -0.0645 11  PHE A C   
53   O O   A PHE A 10  ? 0.2143 0.3085 0.2624 -0.0561 0.0041  -0.0565 11  PHE A O   
54   O O   B PHE A 10  ? 0.2087 0.3082 0.2587 -0.0551 0.0030  -0.0564 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2384 0.3254 0.2765 -0.0628 0.0063  -0.0648 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2058 0.2955 0.2445 -0.0603 0.0047  -0.0623 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2584 0.3230 0.2925 -0.0674 0.0118  -0.0679 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.2298 0.3200 0.2647 -0.0647 0.0064  -0.0686 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3026 0.3642 0.3342 -0.0765 0.0164  -0.0770 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.2666 0.3743 0.2992 -0.0654 0.0030  -0.0707 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.2796 0.3245 0.3106 -0.0624 0.0119  -0.0618 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.2710 0.3427 0.3030 -0.0677 0.0112  -0.0727 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3242 0.3597 0.3484 -0.0801 0.0213  -0.0790 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.2846 0.3927 0.3127 -0.0707 0.0056  -0.0776 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3127 0.3337 0.3365 -0.0652 0.0153  -0.0636 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3146 0.3867 0.3442 -0.0716 0.0137  -0.0799 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.2959 0.3105 0.3154 -0.0737 0.0202  -0.0717 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.2846 0.3755 0.3124 -0.0738 0.0115  -0.0826 11  PHE A CZ  
69   N N   . THR A 11  ? 0.1871 0.2948 0.2407 -0.0721 0.0107  -0.0723 12  THR A N   
70   C CA  . THR A 11  ? 0.2009 0.3068 0.2586 -0.0732 0.0140  -0.0718 12  THR A CA  
71   C C   . THR A 11  ? 0.2588 0.3379 0.3075 -0.0696 0.0160  -0.0633 12  THR A C   
72   O O   . THR A 11  ? 0.2383 0.3189 0.2903 -0.0640 0.0147  -0.0585 12  THR A O   
73   C CB  . THR A 11  ? 0.2975 0.4075 0.3574 -0.0869 0.0218  -0.0832 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3058 0.4456 0.3765 -0.0896 0.0187  -0.0921 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3498 0.4593 0.4135 -0.0905 0.0273  -0.0849 12  THR A CG2 
76   N N   A ARG A 12  ? 0.2310 0.2861 0.2684 -0.0721 0.0183  -0.0621 13  ARG A N   
77   N N   B ARG A 12  ? 0.2359 0.2910 0.2733 -0.0721 0.0184  -0.0621 13  ARG A N   
78   C CA  A ARG A 12  ? 0.2412 0.2709 0.2689 -0.0685 0.0186  -0.0551 13  ARG A CA  
79   C CA  B ARG A 12  ? 0.2479 0.2777 0.2757 -0.0685 0.0186  -0.0550 13  ARG A CA  
80   C C   A ARG A 12  ? 0.2685 0.2961 0.2972 -0.0575 0.0126  -0.0473 13  ARG A C   
81   C C   B ARG A 12  ? 0.2702 0.2980 0.2990 -0.0574 0.0126  -0.0473 13  ARG A C   
82   O O   A ARG A 12  ? 0.2627 0.2724 0.2849 -0.0540 0.0116  -0.0424 13  ARG A O   
83   O O   B ARG A 12  ? 0.2628 0.2730 0.2852 -0.0539 0.0116  -0.0422 13  ARG A O   
84   C CB  A ARG A 12  ? 0.2871 0.2900 0.3013 -0.0745 0.0226  -0.0575 13  ARG A CB  
85   C CB  B ARG A 12  ? 0.3076 0.3107 0.3219 -0.0743 0.0225  -0.0574 13  ARG A CB  
86   C CG  A ARG A 12  ? 0.3798 0.3760 0.3876 -0.0879 0.0311  -0.0647 13  ARG A CG  
87   C CG  B ARG A 12  ? 0.4700 0.4605 0.4753 -0.0860 0.0304  -0.0617 13  ARG A CG  
88   C CD  A ARG A 12  ? 0.5395 0.5283 0.5423 -0.0915 0.0351  -0.0625 13  ARG A CD  
89   C CD  B ARG A 12  ? 0.5696 0.5477 0.5666 -0.0961 0.0362  -0.0694 13  ARG A CD  
90   N NE  A ARG A 12  ? 0.6484 0.6066 0.6348 -0.0873 0.0332  -0.0545 13  ARG A NE  
91   N NE  B ARG A 12  ? 0.6094 0.5651 0.5973 -0.0905 0.0332  -0.0670 13  ARG A NE  
92   C CZ  A ARG A 12  ? 0.7456 0.6967 0.7267 -0.0867 0.0340  -0.0500 13  ARG A CZ  
93   C CZ  B ARG A 12  ? 0.7352 0.6946 0.7259 -0.0920 0.0336  -0.0729 13  ARG A CZ  
94   N NH1 A ARG A 12  ? 0.5050 0.4773 0.4974 -0.0895 0.0374  -0.0531 13  ARG A NH1 
95   N NH1 B ARG A 12  ? 0.6654 0.6042 0.6495 -0.0858 0.0311  -0.0717 13  ARG A NH1 
96   N NH2 A ARG A 12  ? 0.6031 0.5266 0.5677 -0.0827 0.0309  -0.0432 13  ARG A NH2 
97   N NH2 B ARG A 12  ? 0.4065 0.3911 0.4071 -0.0995 0.0363  -0.0810 13  ARG A NH2 
98   N N   . HIS A 13  ? 0.2089 0.2537 0.2441 -0.0530 0.0087  -0.0468 14  HIS A N   
99   C CA  . HIS A 13  ? 0.1974 0.2400 0.2324 -0.0451 0.0050  -0.0410 14  HIS A CA  
100  C C   . HIS A 13  ? 0.2413 0.2780 0.2762 -0.0400 0.0038  -0.0343 14  HIS A C   
101  O O   . HIS A 13  ? 0.2279 0.2522 0.2598 -0.0367 0.0026  -0.0315 14  HIS A O   
102  C CB  . HIS A 13  ? 0.1903 0.2501 0.2279 -0.0429 0.0021  -0.0411 14  HIS A CB  
103  C CG  . HIS A 13  ? 0.2098 0.2651 0.2453 -0.0377 0.0007  -0.0365 14  HIS A CG  
104  N ND1 . HIS A 13  ? 0.2168 0.2640 0.2516 -0.0380 0.0020  -0.0394 14  HIS A ND1 
105  C CD2 . HIS A 13  ? 0.2208 0.2785 0.2549 -0.0330 -0.0011 -0.0305 14  HIS A CD2 
106  C CE1 . HIS A 13  ? 0.2061 0.2538 0.2406 -0.0346 0.0015  -0.0361 14  HIS A CE1 
107  N NE2 . HIS A 13  ? 0.2059 0.2578 0.2384 -0.0321 0.0000  -0.0302 14  HIS A NE2 
108  N N   . ALA A 14  ? 0.1963 0.2429 0.2353 -0.0389 0.0038  -0.0329 15  ALA A N   
109  C CA  . ALA A 14  ? 0.2029 0.2434 0.2415 -0.0344 0.0035  -0.0274 15  ALA A CA  
110  C C   . ALA A 14  ? 0.2403 0.2621 0.2720 -0.0372 0.0058  -0.0266 15  ALA A C   
111  O O   . ALA A 14  ? 0.2266 0.2392 0.2553 -0.0336 0.0043  -0.0225 15  ALA A O   
112  C CB  . ALA A 14  ? 0.2087 0.2630 0.2542 -0.0322 0.0035  -0.0277 15  ALA A CB  
113  N N   A SER A 15  ? 0.2161 0.2316 0.2436 -0.0443 0.0095  -0.0309 16  SER A N   
114  N N   B SER A 15  ? 0.2186 0.2340 0.2460 -0.0443 0.0095  -0.0309 16  SER A N   
115  N N   C SER A 15  ? 0.2148 0.2302 0.2422 -0.0443 0.0095  -0.0309 16  SER A N   
116  C CA  A SER A 15  ? 0.2298 0.2234 0.2453 -0.0477 0.0114  -0.0297 16  SER A CA  
117  C CA  B SER A 15  ? 0.2337 0.2272 0.2492 -0.0478 0.0114  -0.0297 16  SER A CA  
118  C CA  C SER A 15  ? 0.2278 0.2211 0.2432 -0.0476 0.0114  -0.0296 16  SER A CA  
119  C C   A SER A 15  ? 0.2868 0.2649 0.2958 -0.0434 0.0069  -0.0274 16  SER A C   
120  C C   B SER A 15  ? 0.2916 0.2695 0.3005 -0.0435 0.0069  -0.0275 16  SER A C   
121  C C   C SER A 15  ? 0.2906 0.2682 0.2993 -0.0436 0.0069  -0.0275 16  SER A C   
122  O O   A SER A 15  ? 0.2619 0.2260 0.2635 -0.0406 0.0043  -0.0238 16  SER A O   
123  O O   B SER A 15  ? 0.2729 0.2362 0.2740 -0.0409 0.0045  -0.0239 16  SER A O   
124  O O   C SER A 15  ? 0.2751 0.2379 0.2759 -0.0410 0.0044  -0.0239 16  SER A O   
125  C CB  A SER A 15  ? 0.2724 0.2602 0.2820 -0.0579 0.0176  -0.0353 16  SER A CB  
126  C CB  B SER A 15  ? 0.2817 0.2694 0.2912 -0.0580 0.0176  -0.0353 16  SER A CB  
127  C CB  C SER A 15  ? 0.2697 0.2572 0.2791 -0.0578 0.0177  -0.0350 16  SER A CB  
128  O OG  A SER A 15  ? 0.3216 0.2837 0.3144 -0.0616 0.0194  -0.0331 16  SER A OG  
129  O OG  B SER A 15  ? 0.3329 0.3388 0.3519 -0.0617 0.0219  -0.0396 16  SER A OG  
130  O OG  C SER A 15  ? 0.3101 0.2973 0.3186 -0.0618 0.0186  -0.0396 16  SER A OG  
131  N N   . ASP A 16  ? 0.2627 0.2451 0.2754 -0.0425 0.0055  -0.0305 17  ASP A N   
132  C CA  . ASP A 16  ? 0.2722 0.2434 0.2826 -0.0373 0.0014  -0.0307 17  ASP A CA  
133  C C   . ASP A 16  ? 0.2684 0.2467 0.2855 -0.0304 -0.0026 -0.0277 17  ASP A C   
134  O O   . ASP A 16  ? 0.2678 0.2357 0.2825 -0.0256 -0.0069 -0.0270 17  ASP A O   
135  C CB  . ASP A 16  ? 0.2940 0.2709 0.3086 -0.0387 0.0024  -0.0364 17  ASP A CB  
136  C CG  . ASP A 16  ? 0.4134 0.3778 0.4194 -0.0461 0.0066  -0.0408 17  ASP A CG  
137  O OD1 . ASP A 16  ? 0.4273 0.3750 0.4218 -0.0505 0.0089  -0.0392 17  ASP A OD1 
138  O OD2 . ASP A 16  ? 0.4059 0.3760 0.4151 -0.0487 0.0084  -0.0464 17  ASP A OD2 
139  N N   . VAL A 17  ? 0.1994 0.1949 0.2242 -0.0299 -0.0014 -0.0264 18  VAL A N   
140  C CA  . VAL A 17  ? 0.1870 0.1875 0.2162 -0.0256 -0.0032 -0.0239 18  VAL A CA  
141  C C   . VAL A 17  ? 0.2380 0.2279 0.2623 -0.0244 -0.0046 -0.0205 18  VAL A C   
142  O O   . VAL A 17  ? 0.2182 0.2047 0.2435 -0.0211 -0.0079 -0.0207 18  VAL A O   
143  C CB  . VAL A 17  ? 0.2130 0.2276 0.2458 -0.0257 -0.0013 -0.0218 18  VAL A CB  
144  C CG1 . VAL A 17  ? 0.2071 0.2214 0.2407 -0.0233 -0.0012 -0.0187 18  VAL A CG1 
145  C CG2 . VAL A 17  ? 0.2069 0.2314 0.2420 -0.0270 -0.0007 -0.0254 18  VAL A CG2 
146  N N   . LEU A 18  ? 0.2145 0.2012 0.2342 -0.0275 -0.0019 -0.0185 19  LEU A N   
147  C CA  . LEU A 18  ? 0.2303 0.2071 0.2437 -0.0277 -0.0022 -0.0158 19  LEU A CA  
148  C C   . LEU A 18  ? 0.2702 0.2293 0.2732 -0.0269 -0.0065 -0.0158 19  LEU A C   
149  O O   . LEU A 18  ? 0.2490 0.2030 0.2492 -0.0242 -0.0102 -0.0145 19  LEU A O   
150  C CB  . LEU A 18  ? 0.2414 0.2196 0.2530 -0.0320 0.0029  -0.0155 19  LEU A CB  
151  C CG  . LEU A 18  ? 0.2840 0.2548 0.2903 -0.0326 0.0042  -0.0134 19  LEU A CG  
152  C CD1 . LEU A 18  ? 0.2776 0.2559 0.2908 -0.0283 0.0038  -0.0114 19  LEU A CD1 
153  C CD2 . LEU A 18  ? 0.3361 0.3082 0.3412 -0.0378 0.0105  -0.0154 19  LEU A CD2 
154  N N   . LEU A 19  ? 0.2553 0.2043 0.2517 -0.0289 -0.0065 -0.0176 20  LEU A N   
155  C CA  . LEU A 19  ? 0.2833 0.2109 0.2666 -0.0265 -0.0116 -0.0170 20  LEU A CA  
156  C C   . LEU A 19  ? 0.2866 0.2189 0.2784 -0.0178 -0.0191 -0.0187 20  LEU A C   
157  O O   . LEU A 19  ? 0.2753 0.1977 0.2604 -0.0134 -0.0257 -0.0174 20  LEU A O   
158  C CB  . LEU A 19  ? 0.3174 0.2332 0.2932 -0.0303 -0.0091 -0.0193 20  LEU A CB  
159  C CG  . LEU A 19  ? 0.4500 0.3382 0.4089 -0.0269 -0.0146 -0.0182 20  LEU A CG  
160  C CD1 . LEU A 19  ? 0.4988 0.3652 0.4359 -0.0318 -0.0138 -0.0137 20  LEU A CD1 
161  C CD2 . LEU A 19  ? 0.5176 0.3953 0.4719 -0.0301 -0.0113 -0.0216 20  LEU A CD2 
162  N N   . ASN A 20  ? 0.2287 0.1780 0.2353 -0.0158 -0.0181 -0.0225 21  ASN A N   
163  C CA  . ASN A 20  ? 0.2151 0.1730 0.2329 -0.0090 -0.0233 -0.0265 21  ASN A CA  
164  C C   . ASN A 20  ? 0.2468 0.2139 0.2697 -0.0083 -0.0246 -0.0258 21  ASN A C   
165  O O   . ASN A 20  ? 0.2411 0.2099 0.2686 -0.0029 -0.0310 -0.0290 21  ASN A O   
166  C CB  . ASN A 20  ? 0.2095 0.1822 0.2398 -0.0092 -0.0199 -0.0317 21  ASN A CB  
167  C CG  . ASN A 20  ? 0.3571 0.3190 0.3840 -0.0075 -0.0209 -0.0351 21  ASN A CG  
168  O OD1 . ASN A 20  ? 0.3324 0.2745 0.3489 -0.0037 -0.0258 -0.0341 21  ASN A OD1 
169  N ND2 . ASN A 20  ? 0.2748 0.2469 0.3080 -0.0106 -0.0161 -0.0391 21  ASN A ND2 
170  N N   . LEU A 21  ? 0.2185 0.1922 0.2415 -0.0135 -0.0187 -0.0224 22  LEU A N   
171  C CA  . LEU A 21  ? 0.2102 0.1891 0.2358 -0.0141 -0.0186 -0.0219 22  LEU A CA  
172  C C   . LEU A 21  ? 0.2408 0.2061 0.2553 -0.0127 -0.0241 -0.0202 22  LEU A C   
173  O O   . LEU A 21  ? 0.2226 0.1919 0.2405 -0.0107 -0.0283 -0.0227 22  LEU A O   
174  C CB  . LEU A 21  ? 0.2057 0.1892 0.2308 -0.0185 -0.0114 -0.0181 22  LEU A CB  
175  C CG  . LEU A 21  ? 0.2237 0.2194 0.2562 -0.0195 -0.0071 -0.0190 22  LEU A CG  
176  C CD1 . LEU A 21  ? 0.2296 0.2266 0.2595 -0.0214 -0.0023 -0.0145 22  LEU A CD1 
177  C CD2 . LEU A 21  ? 0.2602 0.2652 0.3011 -0.0194 -0.0070 -0.0237 22  LEU A CD2 
178  N N   . ASN A 22  ? 0.2264 0.1756 0.2266 -0.0148 -0.0238 -0.0165 23  ASN A N   
179  C CA  . ASN A 22  ? 0.2520 0.1844 0.2364 -0.0143 -0.0291 -0.0143 23  ASN A CA  
180  C C   . ASN A 22  ? 0.3138 0.2397 0.2965 -0.0059 -0.0403 -0.0168 23  ASN A C   
181  O O   . ASN A 22  ? 0.3212 0.2430 0.2979 -0.0029 -0.0476 -0.0170 23  ASN A O   
182  C CB  . ASN A 22  ? 0.3012 0.2162 0.2683 -0.0204 -0.0245 -0.0107 23  ASN A CB  
183  C CG  . ASN A 22  ? 0.3795 0.2773 0.3274 -0.0226 -0.0274 -0.0080 23  ASN A CG  
184  O OD1 . ASN A 22  ? 0.3583 0.2619 0.3081 -0.0225 -0.0290 -0.0086 23  ASN A OD1 
185  N ND2 . ASN A 22  ? 0.4274 0.3026 0.3548 -0.0258 -0.0274 -0.0054 23  ASN A ND2 
186  N N   . ARG A 23  ? 0.2795 0.2056 0.2681 -0.0014 -0.0422 -0.0194 24  ARG A N   
187  C CA  . ARG A 23  ? 0.2766 0.1986 0.2675 0.0090  -0.0532 -0.0232 24  ARG A CA  
188  C C   . ARG A 23  ? 0.3173 0.2625 0.3277 0.0131  -0.0573 -0.0299 24  ARG A C   
189  O O   . ARG A 23  ? 0.3155 0.2592 0.3251 0.0206  -0.0681 -0.0325 24  ARG A O   
190  C CB  . ARG A 23  ? 0.2887 0.2083 0.2851 0.0125  -0.0523 -0.0263 24  ARG A CB  
191  C CG  . ARG A 23  ? 0.3748 0.2673 0.3497 0.0090  -0.0498 -0.0213 24  ARG A CG  
192  C CD  . ARG A 23  ? 0.4281 0.3222 0.4104 0.0087  -0.0452 -0.0253 24  ARG A CD  
193  N NE  . ARG A 23  ? 0.5346 0.4005 0.4956 0.0049  -0.0428 -0.0220 24  ARG A NE  
194  C CZ  . ARG A 23  ? 0.7732 0.6351 0.7351 0.0018  -0.0373 -0.0251 24  ARG A CZ  
195  N NH1 . ARG A 23  ? 0.5572 0.4426 0.5397 0.0020  -0.0336 -0.0311 24  ARG A NH1 
196  N NH2 . ARG A 23  ? 0.6461 0.4796 0.5865 -0.0029 -0.0345 -0.0226 24  ARG A NH2 
197  N N   . LEU A 24  ? 0.2642 0.2303 0.2905 0.0076  -0.0488 -0.0329 25  LEU A N   
198  C CA  . LEU A 24  ? 0.2462 0.2336 0.2895 0.0082  -0.0499 -0.0401 25  LEU A CA  
199  C C   . LEU A 24  ? 0.3049 0.2892 0.3400 0.0060  -0.0534 -0.0383 25  LEU A C   
200  O O   . LEU A 24  ? 0.3009 0.2954 0.3440 0.0104  -0.0613 -0.0447 25  LEU A O   
201  C CB  . LEU A 24  ? 0.2331 0.2362 0.2877 0.0008  -0.0386 -0.0419 25  LEU A CB  
202  C CG  . LEU A 24  ? 0.2801 0.2899 0.3435 0.0014  -0.0344 -0.0453 25  LEU A CG  
203  C CD1 . LEU A 24  ? 0.2733 0.2959 0.3426 -0.0066 -0.0239 -0.0462 25  LEU A CD1 
204  C CD2 . LEU A 24  ? 0.2969 0.3160 0.3746 0.0097  -0.0414 -0.0551 25  LEU A CD2 
205  N N   . ARG A 25  ? 0.2650 0.2369 0.2852 -0.0008 -0.0474 -0.0309 26  ARG A N   
206  C CA  . ARG A 25  ? 0.2790 0.2461 0.2893 -0.0039 -0.0496 -0.0296 26  ARG A CA  
207  C C   . ARG A 25  ? 0.3454 0.3003 0.3430 0.0034  -0.0633 -0.0297 26  ARG A C   
208  O O   . ARG A 25  ? 0.3470 0.3100 0.3473 0.0049  -0.0701 -0.0343 26  ARG A O   
209  C CB  . ARG A 25  ? 0.2877 0.2424 0.2841 -0.0116 -0.0405 -0.0227 26  ARG A CB  
210  C CG  . ARG A 25  ? 0.3680 0.3175 0.3538 -0.0156 -0.0416 -0.0225 26  ARG A CG  
211  C CD  . ARG A 25  ? 0.3769 0.3175 0.3531 -0.0229 -0.0315 -0.0180 26  ARG A CD  
212  N NE  . ARG A 25  ? 0.3785 0.3018 0.3389 -0.0242 -0.0305 -0.0132 26  ARG A NE  
213  C CZ  . ARG A 25  ? 0.5259 0.4328 0.4666 -0.0290 -0.0293 -0.0107 26  ARG A CZ  
214  N NH1 . ARG A 25  ? 0.4495 0.3550 0.3834 -0.0320 -0.0306 -0.0123 26  ARG A NH1 
215  N NH2 . ARG A 25  ? 0.4277 0.3192 0.3543 -0.0322 -0.0261 -0.0074 26  ARG A NH2 
216  N N   A SER A 26  ? 0.3293 0.2637 0.3118 0.0075  -0.0674 -0.0248 27  SER A N   
217  N N   B SER A 26  ? 0.3278 0.2621 0.3102 0.0076  -0.0674 -0.0248 27  SER A N   
218  N N   C SER A 26  ? 0.3245 0.2588 0.3070 0.0076  -0.0674 -0.0248 27  SER A N   
219  C CA  A SER A 26  ? 0.3626 0.2785 0.3274 0.0155  -0.0810 -0.0231 27  SER A CA  
220  C CA  B SER A 26  ? 0.3602 0.2755 0.3245 0.0154  -0.0809 -0.0229 27  SER A CA  
221  C CA  C SER A 26  ? 0.3548 0.2698 0.3190 0.0155  -0.0809 -0.0228 27  SER A CA  
222  C C   A SER A 26  ? 0.4105 0.3434 0.3924 0.0267  -0.0937 -0.0316 27  SER A C   
223  C C   B SER A 26  ? 0.4169 0.3471 0.3971 0.0275  -0.0944 -0.0310 27  SER A C   
224  C C   C SER A 26  ? 0.4134 0.3433 0.3935 0.0275  -0.0943 -0.0310 27  SER A C   
225  O O   A SER A 26  ? 0.4229 0.3541 0.3972 0.0314  -0.1054 -0.0332 27  SER A O   
226  O O   B SER A 26  ? 0.4393 0.3623 0.4084 0.0342  -0.1075 -0.0314 27  SER A O   
227  O O   C SER A 26  ? 0.4339 0.3562 0.4025 0.0342  -0.1075 -0.0312 27  SER A O   
228  C CB  A SER A 26  ? 0.4274 0.3181 0.3757 0.0182  -0.0816 -0.0176 27  SER A CB  
229  C CB  B SER A 26  ? 0.4200 0.3076 0.3642 0.0163  -0.0804 -0.0164 27  SER A CB  
230  C CB  C SER A 26  ? 0.4110 0.2996 0.3569 0.0167  -0.0802 -0.0167 27  SER A CB  
231  O OG  A SER A 26  ? 0.5418 0.4160 0.4721 0.0074  -0.0709 -0.0111 27  SER A OG  
232  O OG  B SER A 26  ? 0.4959 0.3878 0.4536 0.0229  -0.0811 -0.0198 27  SER A OG  
233  O OG  C SER A 26  ? 0.5191 0.3831 0.4423 0.0247  -0.0933 -0.0135 27  SER A OG  
234  N N   . ARG A 27  ? 0.3513 0.3032 0.3575 0.0303  -0.0912 -0.0384 28  ARG A N   
235  C CA  . ARG A 27  ? 0.3606 0.3326 0.3882 0.0412  -0.1019 -0.0492 28  ARG A CA  
236  C C   . ARG A 27  ? 0.3772 0.3799 0.4267 0.0355  -0.0982 -0.0586 28  ARG A C   
237  O O   . ARG A 27  ? 0.3745 0.4001 0.4460 0.0423  -0.1050 -0.0702 28  ARG A O   
238  C CB  . ARG A 27  ? 0.3901 0.3652 0.4311 0.0472  -0.0999 -0.0531 28  ARG A CB  
239  C CG  . ARG A 27  ? 0.5353 0.4773 0.5531 0.0520  -0.1030 -0.0446 28  ARG A CG  
240  C CD  . ARG A 27  ? 0.6328 0.5772 0.6632 0.0556  -0.0985 -0.0488 28  ARG A CD  
241  N NE  . ARG A 27  ? 0.8390 0.7974 0.8895 0.0699  -0.1097 -0.0597 28  ARG A NE  
242  C CZ  . ARG A 27  ? 1.0242 1.0038 1.0998 0.0716  -0.1046 -0.0699 28  ARG A CZ  
243  N NH1 . ARG A 27  ? 0.8855 0.8793 0.9810 0.0854  -0.1149 -0.0814 28  ARG A NH1 
244  N NH2 . ARG A 27  ? 0.8352 0.8226 0.9161 0.0600  -0.0895 -0.0694 28  ARG A NH2 
245  N N   . ASP A 28  ? 0.3072 0.3101 0.3505 0.0229  -0.0873 -0.0547 29  ASP A N   
246  C CA  . ASP A 28  ? 0.3072 0.3331 0.3661 0.0146  -0.0811 -0.0624 29  ASP A CA  
247  C C   . ASP A 28  ? 0.3500 0.3994 0.4343 0.0123  -0.0729 -0.0716 29  ASP A C   
248  O O   . ASP A 28  ? 0.3496 0.4227 0.4526 0.0097  -0.0726 -0.0832 29  ASP A O   
249  C CB  . ASP A 28  ? 0.3408 0.3767 0.4013 0.0184  -0.0938 -0.0694 29  ASP A CB  
250  C CG  . ASP A 28  ? 0.4373 0.4886 0.5052 0.0064  -0.0856 -0.0753 29  ASP A CG  
251  O OD1 . ASP A 28  ? 0.4402 0.4816 0.4990 -0.0041 -0.0722 -0.0688 29  ASP A OD1 
252  O OD2 . ASP A 28  ? 0.4972 0.5706 0.5803 0.0077  -0.0926 -0.0871 29  ASP A OD2 
253  N N   . ILE A 29  ? 0.2708 0.3136 0.3548 0.0122  -0.0660 -0.0675 30  ILE A N   
254  C CA  . ILE A 29  ? 0.2492 0.3106 0.3526 0.0091  -0.0574 -0.0753 30  ILE A CA  
255  C C   . ILE A 29  ? 0.2745 0.3368 0.3749 -0.0039 -0.0423 -0.0718 30  ILE A C   
256  O O   . ILE A 29  ? 0.2390 0.2844 0.3237 -0.0073 -0.0368 -0.0611 30  ILE A O   
257  C CB  . ILE A 29  ? 0.2867 0.3419 0.3919 0.0164  -0.0588 -0.0745 30  ILE A CB  
258  C CG1 . ILE A 29  ? 0.3046 0.3585 0.4146 0.0313  -0.0745 -0.0797 30  ILE A CG1 
259  C CG2 . ILE A 29  ? 0.2587 0.3314 0.3803 0.0108  -0.0476 -0.0821 30  ILE A CG2 
260  C CD1 . ILE A 29  ? 0.3248 0.3615 0.4283 0.0387  -0.0763 -0.0760 30  ILE A CD1 
261  N N   A LEU A 30  ? 0.2376 0.3192 0.3524 -0.0113 -0.0355 -0.0816 31  LEU A N   
262  N N   B LEU A 30  ? 0.2437 0.3255 0.3587 -0.0112 -0.0356 -0.0817 31  LEU A N   
263  C CA  A LEU A 30  ? 0.2384 0.3189 0.3489 -0.0237 -0.0210 -0.0793 31  LEU A CA  
264  C CA  B LEU A 30  ? 0.2476 0.3287 0.3586 -0.0237 -0.0211 -0.0798 31  LEU A CA  
265  C C   A LEU A 30  ? 0.2746 0.3381 0.3676 -0.0289 -0.0174 -0.0698 31  LEU A C   
266  C C   B LEU A 30  ? 0.2813 0.3451 0.3745 -0.0289 -0.0175 -0.0699 31  LEU A C   
267  O O   A LEU A 30  ? 0.2516 0.3070 0.3363 -0.0362 -0.0067 -0.0645 31  LEU A O   
268  O O   B LEU A 30  ? 0.2620 0.3176 0.3469 -0.0362 -0.0068 -0.0647 31  LEU A O   
269  C CB  A LEU A 30  ? 0.2413 0.3177 0.3490 -0.0254 -0.0130 -0.0753 31  LEU A CB  
270  C CB  B LEU A 30  ? 0.2530 0.3312 0.3621 -0.0257 -0.0129 -0.0764 31  LEU A CB  
271  C CG  A LEU A 30  ? 0.2978 0.3927 0.4232 -0.0247 -0.0109 -0.0869 31  LEU A CG  
272  C CG  B LEU A 30  ? 0.3158 0.4134 0.4406 -0.0319 -0.0050 -0.0887 31  LEU A CG  
273  C CD1 A LEU A 30  ? 0.2810 0.3721 0.3994 -0.0324 0.0009  -0.0836 31  LEU A CD1 
274  C CD1 B LEU A 30  ? 0.3150 0.4231 0.4534 -0.0236 -0.0100 -0.0957 31  LEU A CD1 
275  C CD2 A LEU A 30  ? 0.3202 0.4385 0.4649 -0.0291 -0.0095 -0.1022 31  LEU A CD2 
276  C CD2 B LEU A 30  ? 0.3481 0.4376 0.4609 -0.0427 0.0086  -0.0836 31  LEU A CD2 
277  N N   . THR A 31  ? 0.2449 0.3030 0.3319 -0.0252 -0.0263 -0.0684 32  THR A N   
278  C CA  . THR A 31  ? 0.2488 0.2926 0.3207 -0.0308 -0.0224 -0.0618 32  THR A CA  
279  C C   . THR A 31  ? 0.3033 0.3580 0.3826 -0.0414 -0.0138 -0.0702 32  THR A C   
280  O O   . THR A 31  ? 0.2988 0.3739 0.3946 -0.0428 -0.0159 -0.0824 32  THR A O   
281  C CB  . THR A 31  ? 0.3312 0.3676 0.3936 -0.0257 -0.0337 -0.0601 32  THR A CB  
282  O OG1 . THR A 31  ? 0.3488 0.4031 0.4248 -0.0214 -0.0438 -0.0710 32  THR A OG1 
283  C CG2 . THR A 31  ? 0.3152 0.3344 0.3644 -0.0182 -0.0394 -0.0508 32  THR A CG2 
284  N N   . ASP A 32  ? 0.2662 0.3076 0.3345 -0.0489 -0.0031 -0.0646 33  ASP A N   
285  C CA  . ASP A 32  ? 0.2677 0.3135 0.3390 -0.0604 0.0075  -0.0716 33  ASP A CA  
286  C C   . ASP A 32  ? 0.3020 0.3346 0.3617 -0.0667 0.0121  -0.0697 33  ASP A C   
287  O O   . ASP A 32  ? 0.2972 0.3264 0.3547 -0.0771 0.0230  -0.0736 33  ASP A O   
288  C CB  . ASP A 32  ? 0.2875 0.3273 0.3552 -0.0649 0.0187  -0.0680 33  ASP A CB  
289  C CG  . ASP A 32  ? 0.4049 0.4248 0.4576 -0.0598 0.0205  -0.0540 33  ASP A CG  
290  O OD1 . ASP A 32  ? 0.3728 0.3822 0.4177 -0.0553 0.0162  -0.0478 33  ASP A OD1 
291  O OD2 . ASP A 32  ? 0.5096 0.5259 0.5587 -0.0606 0.0259  -0.0503 33  ASP A OD2 
292  N N   . VAL A 33  ? 0.2547 0.2782 0.3054 -0.0614 0.0049  -0.0644 34  VAL A N   
293  C CA  . VAL A 33  ? 0.2491 0.2604 0.2888 -0.0673 0.0093  -0.0639 34  VAL A CA  
294  C C   . VAL A 33  ? 0.2997 0.3093 0.3328 -0.0625 -0.0018 -0.0630 34  VAL A C   
295  O O   . VAL A 33  ? 0.3010 0.3088 0.3315 -0.0536 -0.0105 -0.0578 34  VAL A O   
296  C CB  . VAL A 33  ? 0.2956 0.2848 0.3223 -0.0684 0.0200  -0.0539 34  VAL A CB  
297  C CG1 . VAL A 33  ? 0.2777 0.2574 0.2974 -0.0592 0.0156  -0.0438 34  VAL A CG1 
298  C CG2 . VAL A 33  ? 0.3078 0.2845 0.3256 -0.0766 0.0282  -0.0562 34  VAL A CG2 
299  N N   A VAL A 34  ? 0.2715 0.2792 0.2990 -0.0692 -0.0007 -0.0682 35  VAL A N   
300  N N   B VAL A 34  ? 0.2743 0.2821 0.3019 -0.0691 -0.0009 -0.0682 35  VAL A N   
301  C CA  A VAL A 34  ? 0.2745 0.2766 0.2902 -0.0672 -0.0092 -0.0674 35  VAL A CA  
302  C CA  B VAL A 34  ? 0.2790 0.2807 0.2945 -0.0666 -0.0096 -0.0669 35  VAL A CA  
303  C C   A VAL A 34  ? 0.3229 0.3048 0.3244 -0.0726 0.0016  -0.0626 35  VAL A C   
304  C C   B VAL A 34  ? 0.3280 0.3105 0.3293 -0.0726 0.0008  -0.0630 35  VAL A C   
305  O O   A VAL A 34  ? 0.3242 0.3023 0.3265 -0.0808 0.0123  -0.0665 35  VAL A O   
306  O O   B VAL A 34  ? 0.3318 0.3114 0.3340 -0.0812 0.0110  -0.0676 35  VAL A O   
307  C CB  A VAL A 34  ? 0.3293 0.3487 0.3508 -0.0708 -0.0180 -0.0795 35  VAL A CB  
308  C CB  B VAL A 34  ? 0.3356 0.3547 0.3562 -0.0666 -0.0221 -0.0773 35  VAL A CB  
309  C CG1 A VAL A 34  ? 0.3364 0.3466 0.3403 -0.0697 -0.0267 -0.0780 35  VAL A CG1 
310  C CG1 B VAL A 34  ? 0.3380 0.3678 0.3655 -0.0785 -0.0155 -0.0892 35  VAL A CG1 
311  C CG2 A VAL A 34  ? 0.3231 0.3647 0.3620 -0.0637 -0.0289 -0.0861 35  VAL A CG2 
312  C CG2 B VAL A 34  ? 0.3478 0.3559 0.3502 -0.0626 -0.0326 -0.0732 35  VAL A CG2 
313  N N   . ILE A 35  ? 0.2875 0.2559 0.2760 -0.0683 -0.0005 -0.0550 36  ILE A N   
314  C CA  . ILE A 35  ? 0.2860 0.2374 0.2626 -0.0724 0.0090  -0.0521 36  ILE A CA  
315  C C   . ILE A 35  ? 0.3552 0.3043 0.3186 -0.0767 0.0030  -0.0567 36  ILE A C   
316  O O   . ILE A 35  ? 0.3476 0.2963 0.3025 -0.0722 -0.0081 -0.0543 36  ILE A O   
317  C CB  . ILE A 35  ? 0.3064 0.2466 0.2784 -0.0665 0.0125  -0.0429 36  ILE A CB  
318  C CG1 . ILE A 35  ? 0.2953 0.2397 0.2790 -0.0613 0.0155  -0.0383 36  ILE A CG1 
319  C CG2 . ILE A 35  ? 0.3314 0.2571 0.2948 -0.0704 0.0230  -0.0425 36  ILE A CG2 
320  C CD1 . ILE A 35  ? 0.3005 0.2429 0.2900 -0.0653 0.0253  -0.0402 36  ILE A CD1 
321  N N   . VAL A 36  ? 0.3198 0.2654 0.2796 -0.0856 0.0101  -0.0632 37  VAL A N   
322  C CA  . VAL A 36  ? 0.3352 0.2789 0.2812 -0.0915 0.0053  -0.0689 37  VAL A CA  
323  C C   . VAL A 36  ? 0.4070 0.3316 0.3380 -0.0947 0.0148  -0.0658 37  VAL A C   
324  O O   . VAL A 36  ? 0.3903 0.3056 0.3242 -0.0979 0.0281  -0.0664 37  VAL A O   
325  C CB  . VAL A 36  ? 0.3871 0.3425 0.3394 -0.1009 0.0066  -0.0809 37  VAL A CB  
326  C CG1 . VAL A 36  ? 0.4003 0.3549 0.3370 -0.1072 0.0006  -0.0874 37  VAL A CG1 
327  C CG2 . VAL A 36  ? 0.3838 0.3618 0.3542 -0.0981 -0.0018 -0.0862 37  VAL A CG2 
328  N N   . VAL A 37  ? 0.3761 0.2935 0.2895 -0.0943 0.0081  -0.0633 38  VAL A N   
329  C CA  . VAL A 37  ? 0.3809 0.2818 0.2791 -0.0985 0.0172  -0.0619 38  VAL A CA  
330  C C   . VAL A 37  ? 0.4575 0.3545 0.3347 -0.1057 0.0105  -0.0670 38  VAL A C   
331  O O   . VAL A 37  ? 0.4374 0.3326 0.3008 -0.1025 -0.0021 -0.0635 38  VAL A O   
332  C CB  . VAL A 37  ? 0.4212 0.3152 0.3165 -0.0921 0.0176  -0.0531 38  VAL A CB  
333  C CG1 . VAL A 37  ? 0.4316 0.3122 0.3172 -0.0969 0.0301  -0.0538 38  VAL A CG1 
334  C CG2 . VAL A 37  ? 0.3917 0.2939 0.3076 -0.0839 0.0192  -0.0482 38  VAL A CG2 
335  N N   A SER A 38  ? 0.4643 0.3552 0.3343 -0.1154 0.0198  -0.0745 39  SER A N   
336  N N   B SER A 38  ? 0.4119 0.3115 0.2908 -0.1142 0.0162  -0.0762 39  SER A N   
337  C CA  A SER A 38  ? 0.4937 0.3799 0.3407 -0.1236 0.0142  -0.0800 39  SER A CA  
338  C CA  B SER A 38  ? 0.4196 0.3200 0.2832 -0.1232 0.0115  -0.0847 39  SER A CA  
339  C C   A SER A 38  ? 0.5460 0.4442 0.3876 -0.1195 -0.0063 -0.0805 39  SER A C   
340  C C   B SER A 38  ? 0.4508 0.3671 0.3142 -0.1189 -0.0080 -0.0864 39  SER A C   
341  O O   A SER A 38  ? 0.5567 0.4457 0.3747 -0.1189 -0.0165 -0.0770 39  SER A O   
342  O O   B SER A 38  ? 0.4209 0.3548 0.3047 -0.1171 -0.0112 -0.0910 39  SER A O   
343  C CB  A SER A 38  ? 0.5749 0.4428 0.3994 -0.1271 0.0199  -0.0765 39  SER A CB  
344  C CB  B SER A 38  ? 0.4933 0.3758 0.3320 -0.1295 0.0170  -0.0843 39  SER A CB  
345  O OG  A SER A 38  ? 0.7294 0.5886 0.5587 -0.1315 0.0381  -0.0796 39  SER A OG  
346  O OG  B SER A 38  ? 0.5779 0.4505 0.4226 -0.1334 0.0355  -0.0867 39  SER A OG  
347  N N   A ARG A 39  ? 0.4851 0.4030 0.3486 -0.1161 -0.0122 -0.0847 40  ARG A N   
348  N N   B ARG A 39  ? 0.4278 0.3376 0.2687 -0.1167 -0.0212 -0.0830 40  ARG A N   
349  C CA  A ARG A 39  ? 0.4871 0.4225 0.3543 -0.1103 -0.0314 -0.0877 40  ARG A CA  
350  C CA  B ARG A 39  ? 0.4328 0.3576 0.2748 -0.1097 -0.0417 -0.0849 40  ARG A CA  
351  C C   A ARG A 39  ? 0.5194 0.4502 0.3806 -0.0975 -0.0447 -0.0773 40  ARG A C   
352  C C   B ARG A 39  ? 0.4848 0.4168 0.3443 -0.0965 -0.0483 -0.0776 40  ARG A C   
353  O O   A ARG A 39  ? 0.5314 0.4661 0.3821 -0.0917 -0.0628 -0.0776 40  ARG A O   
354  O O   B ARG A 39  ? 0.4724 0.4261 0.3547 -0.0920 -0.0546 -0.0830 40  ARG A O   
355  C CB  A ARG A 39  ? 0.5151 0.4554 0.3662 -0.1175 -0.0411 -0.0970 40  ARG A CB  
356  C CB  B ARG A 39  ? 0.4606 0.3737 0.2694 -0.1109 -0.0554 -0.0838 40  ARG A CB  
357  C CG  A ARG A 39  ? 0.6429 0.5932 0.5041 -0.1300 -0.0308 -0.1100 40  ARG A CG  
358  C CG  B ARG A 39  ? 0.5448 0.4585 0.3403 -0.1242 -0.0520 -0.0945 40  ARG A CG  
359  C CD  A ARG A 39  ? 0.7260 0.6904 0.5777 -0.1347 -0.0454 -0.1207 40  ARG A CD  
360  C CD  B ARG A 39  ? 0.5701 0.4753 0.3320 -0.1252 -0.0686 -0.0946 40  ARG A CD  
361  N NE  A ARG A 39  ? 0.8024 0.7720 0.6572 -0.1496 -0.0342 -0.1340 40  ARG A NE  
362  N NE  B ARG A 39  ? 0.5783 0.4833 0.3264 -0.1394 -0.0635 -0.1053 40  ARG A NE  
363  C CZ  A ARG A 39  ? 0.9672 0.9203 0.8008 -0.1607 -0.0249 -0.1371 40  ARG A CZ  
364  C CZ  B ARG A 39  ? 0.7495 0.6759 0.5044 -0.1432 -0.0731 -0.1176 40  ARG A CZ  
365  N NH1 A ARG A 39  ? 0.7684 0.6994 0.5762 -0.1592 -0.0244 -0.1282 40  ARG A NH1 
366  N NH1 B ARG A 39  ? 0.5579 0.5099 0.3357 -0.1335 -0.0883 -0.1215 40  ARG A NH1 
367  N NH2 A ARG A 39  ? 0.8166 0.7744 0.6542 -0.1743 -0.0145 -0.1502 40  ARG A NH2 
368  N NH2 B ARG A 39  ? 0.6719 0.5959 0.4122 -0.1574 -0.0670 -0.1274 40  ARG A NH2 
369  N N   A GLU A 40  ? 0.4297 0.3515 0.2970 -0.0930 -0.0359 -0.0686 41  GLU A N   
370  N N   B GLU A 40  ? 0.4240 0.3389 0.2749 -0.0920 -0.0440 -0.0669 41  GLU A N   
371  C CA  A GLU A 40  ? 0.4195 0.3364 0.2848 -0.0821 -0.0448 -0.0595 41  GLU A CA  
372  C CA  B GLU A 40  ? 0.3997 0.3169 0.2620 -0.0806 -0.0494 -0.0595 41  GLU A CA  
373  C C   A GLU A 40  ? 0.4231 0.3545 0.3178 -0.0770 -0.0392 -0.0593 41  GLU A C   
374  C C   B GLU A 40  ? 0.4049 0.3392 0.2988 -0.0778 -0.0419 -0.0615 41  GLU A C   
375  O O   A GLU A 40  ? 0.3867 0.3175 0.2922 -0.0817 -0.0243 -0.0599 41  GLU A O   
376  O O   B GLU A 40  ? 0.3624 0.2986 0.2666 -0.0846 -0.0278 -0.0650 41  GLU A O   
377  C CB  A GLU A 40  ? 0.4504 0.3432 0.2939 -0.0839 -0.0379 -0.0508 41  GLU A CB  
378  C CB  B GLU A 40  ? 0.4267 0.3212 0.2714 -0.0798 -0.0436 -0.0493 41  GLU A CB  
379  C CG  A GLU A 40  ? 0.6302 0.5058 0.4399 -0.0901 -0.0433 -0.0508 41  GLU A CG  
380  C CG  B GLU A 40  ? 0.6323 0.5058 0.4425 -0.0871 -0.0446 -0.0479 41  GLU A CG  
381  C CD  A GLU A 40  ? 1.0779 0.9364 0.8628 -0.0837 -0.0568 -0.0426 41  GLU A CD  
382  C CD  B GLU A 40  ? 1.1166 0.9730 0.8992 -0.0815 -0.0599 -0.0410 41  GLU A CD  
383  O OE1 A GLU A 40  ? 1.1267 0.9625 0.8872 -0.0894 -0.0498 -0.0373 41  GLU A OE1 
384  O OE1 B GLU A 40  ? 1.1335 0.9991 0.9213 -0.0710 -0.0771 -0.0411 41  GLU A OE1 
385  O OE2 A GLU A 40  ? 1.0719 0.9385 0.8613 -0.0732 -0.0738 -0.0421 41  GLU A OE2 
386  O OE2 B GLU A 40  ? 1.1535 0.9862 0.9082 -0.0877 -0.0544 -0.0361 41  GLU A OE2 
387  N N   . GLN A 41  ? 0.3695 0.3138 0.2765 -0.0674 -0.0515 -0.0592 42  GLN A N   
388  C CA  . GLN A 41  ? 0.3509 0.3108 0.2847 -0.0640 -0.0466 -0.0608 42  GLN A CA  
389  C C   . GLN A 41  ? 0.3944 0.3475 0.3301 -0.0553 -0.0477 -0.0519 42  GLN A C   
390  O O   . GLN A 41  ? 0.4034 0.3481 0.3263 -0.0483 -0.0596 -0.0476 42  GLN A O   
391  C CB  . GLN A 41  ? 0.3713 0.3561 0.3225 -0.0613 -0.0578 -0.0713 42  GLN A CB  
392  C CG  . GLN A 41  ? 0.5756 0.5712 0.5301 -0.0723 -0.0537 -0.0825 42  GLN A CG  
393  C CD  . GLN A 41  ? 0.7976 0.8224 0.7745 -0.0717 -0.0617 -0.0953 42  GLN A CD  
394  O OE1 . GLN A 41  ? 0.7053 0.7446 0.6988 -0.0625 -0.0695 -0.0967 42  GLN A OE1 
395  N NE2 . GLN A 41  ? 0.8368 0.8721 0.8158 -0.0823 -0.0591 -0.1065 42  GLN A NE2 
396  N N   . PHE A 42  ? 0.3193 0.2742 0.2690 -0.0558 -0.0358 -0.0491 43  PHE A N   
397  C CA  . PHE A 42  ? 0.3152 0.2655 0.2681 -0.0488 -0.0356 -0.0417 43  PHE A CA  
398  C C   . PHE A 42  ? 0.3559 0.3226 0.3320 -0.0462 -0.0324 -0.0444 43  PHE A C   
399  O O   . PHE A 42  ? 0.3524 0.3222 0.3367 -0.0517 -0.0212 -0.0462 43  PHE A O   
400  C CB  . PHE A 42  ? 0.3385 0.2730 0.2819 -0.0523 -0.0236 -0.0351 43  PHE A CB  
401  C CG  . PHE A 42  ? 0.3757 0.2931 0.2951 -0.0571 -0.0237 -0.0333 43  PHE A CG  
402  C CD1 . PHE A 42  ? 0.3943 0.3082 0.3068 -0.0654 -0.0169 -0.0377 43  PHE A CD1 
403  C CD2 . PHE A 42  ? 0.4085 0.3112 0.3103 -0.0546 -0.0292 -0.0276 43  PHE A CD2 
404  C CE1 . PHE A 42  ? 0.4359 0.3338 0.3245 -0.0711 -0.0161 -0.0370 43  PHE A CE1 
405  C CE2 . PHE A 42  ? 0.4613 0.3460 0.3374 -0.0610 -0.0280 -0.0262 43  PHE A CE2 
406  C CZ  . PHE A 42  ? 0.4402 0.3235 0.3101 -0.0693 -0.0214 -0.0311 43  PHE A CZ  
407  N N   . ARG A 43  ? 0.3043 0.2795 0.2890 -0.0380 -0.0417 -0.0450 44  ARG A N   
408  C CA  . ARG A 43  ? 0.2762 0.2671 0.2819 -0.0363 -0.0380 -0.0484 44  ARG A CA  
409  C C   . ARG A 43  ? 0.3300 0.3120 0.3348 -0.0344 -0.0305 -0.0403 44  ARG A C   
410  O O   . ARG A 43  ? 0.3251 0.2939 0.3181 -0.0308 -0.0334 -0.0339 44  ARG A O   
411  C CB  . ARG A 43  ? 0.2923 0.2990 0.3105 -0.0282 -0.0511 -0.0551 44  ARG A CB  
412  C CG  . ARG A 43  ? 0.4021 0.4237 0.4253 -0.0294 -0.0600 -0.0656 44  ARG A CG  
413  C CD  . ARG A 43  ? 0.4929 0.5401 0.5400 -0.0236 -0.0675 -0.0766 44  ARG A CD  
414  N NE  . ARG A 43  ? 0.6208 0.6779 0.6842 -0.0283 -0.0547 -0.0791 44  ARG A NE  
415  C CZ  . ARG A 43  ? 0.7783 0.8491 0.8538 -0.0387 -0.0444 -0.0875 44  ARG A CZ  
416  N NH1 . ARG A 43  ? 0.6798 0.7601 0.7570 -0.0455 -0.0456 -0.0961 44  ARG A NH1 
417  N NH2 . ARG A 43  ? 0.5659 0.6403 0.6502 -0.0431 -0.0328 -0.0879 44  ARG A NH2 
418  N N   . ALA A 44  ? 0.2723 0.2608 0.2882 -0.0375 -0.0208 -0.0408 45  ALA A N   
419  C CA  . ALA A 44  ? 0.2671 0.2494 0.2823 -0.0354 -0.0149 -0.0337 45  ALA A CA  
420  C C   . ALA A 44  ? 0.2752 0.2679 0.3029 -0.0369 -0.0088 -0.0361 45  ALA A C   
421  O O   . ALA A 44  ? 0.2597 0.2637 0.2965 -0.0410 -0.0075 -0.0437 45  ALA A O   
422  C CB  . ALA A 44  ? 0.2801 0.2487 0.2847 -0.0388 -0.0066 -0.0283 45  ALA A CB  
423  N N   . HIS A 45  ? 0.2387 0.2278 0.2658 -0.0349 -0.0045 -0.0304 46  HIS A N   
424  C CA  . HIS A 45  ? 0.2207 0.2155 0.2541 -0.0369 0.0020  -0.0309 46  HIS A CA  
425  C C   . HIS A 45  ? 0.2687 0.2518 0.2940 -0.0398 0.0108  -0.0256 46  HIS A C   
426  O O   . HIS A 45  ? 0.2646 0.2394 0.2838 -0.0367 0.0115  -0.0198 46  HIS A O   
427  C CB  . HIS A 45  ? 0.2106 0.2085 0.2468 -0.0320 -0.0002 -0.0281 46  HIS A CB  
428  C CG  . HIS A 45  ? 0.2512 0.2566 0.2941 -0.0272 -0.0090 -0.0328 46  HIS A CG  
429  N ND1 . HIS A 45  ? 0.2750 0.2716 0.3109 -0.0225 -0.0157 -0.0295 46  HIS A ND1 
430  C CD2 . HIS A 45  ? 0.2574 0.2768 0.3129 -0.0264 -0.0119 -0.0411 46  HIS A CD2 
431  C CE1 . HIS A 45  ? 0.2626 0.2656 0.3055 -0.0175 -0.0234 -0.0348 46  HIS A CE1 
432  N NE2 . HIS A 45  ? 0.2524 0.2712 0.3092 -0.0191 -0.0216 -0.0425 46  HIS A NE2 
433  N N   . LYS A 46  ? 0.2372 0.2191 0.2623 -0.0459 0.0179  -0.0283 47  LYS A N   
434  C CA  . LYS A 46  ? 0.2550 0.2218 0.2705 -0.0475 0.0261  -0.0231 47  LYS A CA  
435  C C   . LYS A 46  ? 0.2865 0.2489 0.2983 -0.0410 0.0260  -0.0152 47  LYS A C   
436  O O   . LYS A 46  ? 0.2644 0.2171 0.2710 -0.0373 0.0277  -0.0107 47  LYS A O   
437  C CB  . LYS A 46  ? 0.2922 0.2558 0.3052 -0.0556 0.0344  -0.0267 47  LYS A CB  
438  C CG  . LYS A 46  ? 0.3089 0.2758 0.3250 -0.0636 0.0365  -0.0354 47  LYS A CG  
439  C CD  . LYS A 46  ? 0.2963 0.2609 0.3101 -0.0739 0.0463  -0.0405 47  LYS A CD  
440  C CE  . LYS A 46  ? 0.3313 0.3053 0.3519 -0.0830 0.0479  -0.0520 47  LYS A CE  
441  N NZ  . LYS A 46  ? 0.3724 0.3435 0.3901 -0.0957 0.0596  -0.0586 47  LYS A NZ  
442  N N   . THR A 47  ? 0.2559 0.2268 0.2712 -0.0394 0.0239  -0.0148 48  THR A N   
443  C CA  . THR A 47  ? 0.2538 0.2224 0.2652 -0.0337 0.0231  -0.0083 48  THR A CA  
444  C C   . THR A 47  ? 0.2619 0.2321 0.2757 -0.0281 0.0187  -0.0059 48  THR A C   
445  O O   . THR A 47  ? 0.2432 0.2091 0.2540 -0.0236 0.0195  -0.0015 48  THR A O   
446  C CB  . THR A 47  ? 0.3138 0.2913 0.3273 -0.0345 0.0222  -0.0094 48  THR A CB  
447  O OG1 . THR A 47  ? 0.3100 0.2996 0.3337 -0.0341 0.0170  -0.0149 48  THR A OG1 
448  C CG2 . THR A 47  ? 0.3570 0.3298 0.3641 -0.0415 0.0294  -0.0112 48  THR A CG2 
449  N N   . VAL A 48  ? 0.2258 0.2011 0.2440 -0.0285 0.0141  -0.0092 49  VAL A N   
450  C CA  . VAL A 48  ? 0.2238 0.1983 0.2415 -0.0258 0.0116  -0.0077 49  VAL A CA  
451  C C   . VAL A 48  ? 0.2585 0.2241 0.2721 -0.0261 0.0158  -0.0069 49  VAL A C   
452  O O   . VAL A 48  ? 0.2448 0.2101 0.2590 -0.0231 0.0173  -0.0052 49  VAL A O   
453  C CB  . VAL A 48  ? 0.2559 0.2321 0.2739 -0.0265 0.0059  -0.0107 49  VAL A CB  
454  C CG1 . VAL A 48  ? 0.2524 0.2235 0.2656 -0.0264 0.0056  -0.0094 49  VAL A CG1 
455  C CG2 . VAL A 48  ? 0.2475 0.2319 0.2710 -0.0249 0.0023  -0.0125 49  VAL A CG2 
456  N N   . LEU A 49  ? 0.2254 0.1853 0.2361 -0.0301 0.0179  -0.0094 50  LEU A N   
457  C CA  . LEU A 49  ? 0.2375 0.1877 0.2437 -0.0312 0.0229  -0.0097 50  LEU A CA  
458  C C   . LEU A 49  ? 0.2724 0.2170 0.2784 -0.0263 0.0275  -0.0060 50  LEU A C   
459  O O   . LEU A 49  ? 0.2580 0.2003 0.2651 -0.0228 0.0298  -0.0057 50  LEU A O   
460  C CB  . LEU A 49  ? 0.2388 0.1845 0.2418 -0.0373 0.0248  -0.0139 50  LEU A CB  
461  C CG  . LEU A 49  ? 0.2657 0.2167 0.2680 -0.0406 0.0184  -0.0183 50  LEU A CG  
462  C CD1 . LEU A 49  ? 0.2742 0.2232 0.2747 -0.0472 0.0209  -0.0239 50  LEU A CD1 
463  C CD2 . LEU A 49  ? 0.2847 0.2313 0.2804 -0.0402 0.0160  -0.0176 50  LEU A CD2 
464  N N   . MET A 50  ? 0.2380 0.1805 0.2421 -0.0255 0.0285  -0.0033 51  MET A N   
465  C CA  . MET A 50  ? 0.2517 0.1853 0.2516 -0.0193 0.0311  0.0015  51  MET A CA  
466  C C   . MET A 50  ? 0.2768 0.2202 0.2826 -0.0116 0.0267  0.0037  51  MET A C   
467  O O   . MET A 50  ? 0.2760 0.2156 0.2830 -0.0047 0.0276  0.0050  51  MET A O   
468  C CB  . MET A 50  ? 0.2823 0.2095 0.2744 -0.0217 0.0330  0.0042  51  MET A CB  
469  C CG  . MET A 50  ? 0.3221 0.2401 0.3090 -0.0307 0.0391  0.0004  51  MET A CG  
470  S SD  . MET A 50  ? 0.3680 0.2841 0.3474 -0.0366 0.0421  0.0012  51  MET A SD  
471  C CE  . MET A 50  ? 0.3487 0.2391 0.3105 -0.0315 0.0465  0.0093  51  MET A CE  
472  N N   . ALA A 51  ? 0.2335 0.1902 0.2442 -0.0127 0.0221  0.0028  52  ALA A N   
473  C CA  . ALA A 51  ? 0.2275 0.1960 0.2444 -0.0074 0.0182  0.0033  52  ALA A CA  
474  C C   . ALA A 51  ? 0.2680 0.2410 0.2918 -0.0063 0.0197  -0.0004 52  ALA A C   
475  O O   . ALA A 51  ? 0.2630 0.2460 0.2938 -0.0013 0.0180  -0.0015 52  ALA A O   
476  C CB  . ALA A 51  ? 0.2201 0.1992 0.2395 -0.0108 0.0143  0.0019  52  ALA A CB  
477  N N   . CYS A 52  ? 0.2328 0.1994 0.2541 -0.0118 0.0230  -0.0033 53  CYS A N   
478  C CA  . CYS A 52  ? 0.2407 0.2095 0.2651 -0.0137 0.0261  -0.0077 53  CYS A CA  
479  C C   . CYS A 52  ? 0.2756 0.2363 0.3003 -0.0118 0.0318  -0.0098 53  CYS A C   
480  O O   . CYS A 52  ? 0.2685 0.2336 0.2979 -0.0127 0.0355  -0.0147 53  CYS A O   
481  C CB  . CYS A 52  ? 0.2477 0.2134 0.2657 -0.0217 0.0252  -0.0097 53  CYS A CB  
482  S SG  . CYS A 52  ? 0.2772 0.2505 0.2955 -0.0233 0.0193  -0.0089 53  CYS A SG  
483  N N   . SER A 53  ? 0.2547 0.2027 0.2734 -0.0112 0.0339  -0.0076 54  SER A N   
484  C CA  . SER A 53  ? 0.2474 0.1844 0.2642 -0.0112 0.0402  -0.0105 54  SER A CA  
485  C C   . SER A 53  ? 0.3113 0.2355 0.3250 -0.0043 0.0420  -0.0068 54  SER A C   
486  O O   . SER A 53  ? 0.2938 0.2103 0.2996 -0.0064 0.0410  -0.0029 54  SER A O   
487  C CB  . SER A 53  ? 0.2719 0.2016 0.2798 -0.0212 0.0421  -0.0130 54  SER A CB  
488  O OG  . SER A 53  ? 0.3164 0.2321 0.3189 -0.0233 0.0480  -0.0150 54  SER A OG  
489  N N   . GLY A 54  ? 0.3034 0.2240 0.3222 0.0036  0.0451  -0.0089 55  GLY A N   
490  C CA  . GLY A 54  ? 0.3151 0.2179 0.3280 0.0116  0.0468  -0.0052 55  GLY A CA  
491  C C   . GLY A 54  ? 0.3527 0.2356 0.3532 0.0033  0.0533  -0.0055 55  GLY A C   
492  O O   . GLY A 54  ? 0.3550 0.2204 0.3444 0.0047  0.0546  -0.0006 55  GLY A O   
493  N N   . LEU A 55  ? 0.3124 0.1971 0.3128 -0.0066 0.0576  -0.0117 56  LEU A N   
494  C CA  . LEU A 55  ? 0.3095 0.1788 0.2992 -0.0160 0.0634  -0.0139 56  LEU A CA  
495  C C   . LEU A 55  ? 0.3351 0.2056 0.3186 -0.0232 0.0604  -0.0109 56  LEU A C   
496  O O   . LEU A 55  ? 0.3326 0.1871 0.3067 -0.0264 0.0649  -0.0095 56  LEU A O   
497  C CB  . LEU A 55  ? 0.3048 0.1776 0.2944 -0.0251 0.0671  -0.0215 56  LEU A CB  
498  C CG  . LEU A 55  ? 0.3806 0.2387 0.3600 -0.0350 0.0734  -0.0258 56  LEU A CG  
499  C CD1 . LEU A 55  ? 0.4022 0.2380 0.3773 -0.0304 0.0820  -0.0269 56  LEU A CD1 
500  C CD2 . LEU A 55  ? 0.3980 0.2625 0.3746 -0.0447 0.0740  -0.0325 56  LEU A CD2 
501  N N   . PHE A 56  ? 0.2909 0.1794 0.2795 -0.0259 0.0538  -0.0106 57  PHE A N   
502  C CA  . PHE A 56  ? 0.2763 0.1692 0.2623 -0.0319 0.0511  -0.0097 57  PHE A CA  
503  C C   . PHE A 56  ? 0.3314 0.2180 0.3131 -0.0272 0.0508  -0.0035 57  PHE A C   
504  O O   . PHE A 56  ? 0.3196 0.2004 0.2948 -0.0338 0.0537  -0.0037 57  PHE A O   
505  C CB  . PHE A 56  ? 0.2758 0.1870 0.2680 -0.0344 0.0437  -0.0114 57  PHE A CB  
506  C CG  . PHE A 56  ? 0.2783 0.1916 0.2688 -0.0413 0.0433  -0.0171 57  PHE A CG  
507  C CD1 . PHE A 56  ? 0.3068 0.2152 0.2928 -0.0494 0.0464  -0.0222 57  PHE A CD1 
508  C CD2 . PHE A 56  ? 0.2945 0.2142 0.2858 -0.0405 0.0398  -0.0180 57  PHE A CD2 
509  C CE1 . PHE A 56  ? 0.3156 0.2261 0.2981 -0.0554 0.0447  -0.0277 57  PHE A CE1 
510  C CE2 . PHE A 56  ? 0.3268 0.2454 0.3118 -0.0470 0.0385  -0.0226 57  PHE A CE2 
511  C CZ  . PHE A 56  ? 0.2966 0.2113 0.2774 -0.0537 0.0403  -0.0272 57  PHE A CZ  
512  N N   . TYR A 57  ? 0.3014 0.1889 0.2856 -0.0164 0.0477  0.0012  58  TYR A N   
513  C CA  . TYR A 57  ? 0.3149 0.1936 0.2909 -0.0110 0.0463  0.0079  58  TYR A CA  
514  C C   . TYR A 57  ? 0.3815 0.2326 0.3423 -0.0131 0.0541  0.0098  58  TYR A C   
515  O O   . TYR A 57  ? 0.3751 0.2155 0.3237 -0.0182 0.0568  0.0127  58  TYR A O   
516  C CB  . TYR A 57  ? 0.3356 0.2209 0.3177 0.0022  0.0405  0.0113  58  TYR A CB  
517  C CG  . TYR A 57  ? 0.3940 0.2676 0.3643 0.0095  0.0377  0.0189  58  TYR A CG  
518  C CD1 . TYR A 57  ? 0.4065 0.2859 0.3712 0.0057  0.0345  0.0220  58  TYR A CD1 
519  C CD2 . TYR A 57  ? 0.4685 0.3230 0.4312 0.0204  0.0380  0.0228  58  TYR A CD2 
520  C CE1 . TYR A 57  ? 0.4397 0.3062 0.3894 0.0115  0.0318  0.0293  58  TYR A CE1 
521  C CE2 . TYR A 57  ? 0.5217 0.3618 0.4692 0.0279  0.0341  0.0309  58  TYR A CE2 
522  C CZ  . TYR A 57  ? 0.6075 0.4535 0.5474 0.0228  0.0310  0.0343  58  TYR A CZ  
523  O OH  . TYR A 57  ? 0.7079 0.5377 0.6291 0.0296  0.0271  0.0425  58  TYR A OH  
524  N N   A SER A 58  ? 0.3616 0.2001 0.3221 -0.0100 0.0588  0.0074  59  SER A N   
525  N N   B SER A 58  ? 0.3635 0.2021 0.3241 -0.0099 0.0587  0.0074  59  SER A N   
526  C CA  A SER A 58  ? 0.3897 0.1988 0.3352 -0.0120 0.0671  0.0083  59  SER A CA  
527  C CA  B SER A 58  ? 0.3932 0.2024 0.3387 -0.0120 0.0670  0.0083  59  SER A CA  
528  C C   A SER A 58  ? 0.4555 0.2602 0.3944 -0.0286 0.0742  0.0031  59  SER A C   
529  C C   B SER A 58  ? 0.4522 0.2577 0.3912 -0.0286 0.0739  0.0033  59  SER A C   
530  O O   A SER A 58  ? 0.4836 0.2666 0.4066 -0.0340 0.0806  0.0054  59  SER A O   
531  O O   B SER A 58  ? 0.4752 0.2609 0.3987 -0.0340 0.0796  0.0059  59  SER A O   
532  C CB  A SER A 58  ? 0.4204 0.2204 0.3703 -0.0054 0.0708  0.0046  59  SER A CB  
533  C CB  B SER A 58  ? 0.4346 0.2348 0.3844 -0.0062 0.0710  0.0044  59  SER A CB  
534  O OG  A SER A 58  ? 0.4267 0.2281 0.3821 0.0111  0.0649  0.0087  59  SER A OG  
535  O OG  B SER A 58  ? 0.5132 0.2819 0.4472 -0.0082 0.0797  0.0050  59  SER A OG  
536  N N   . ILE A 59  ? 0.3936 0.2186 0.3440 -0.0369 0.0730  -0.0043 60  ILE A N   
537  C CA  . ILE A 59  ? 0.3867 0.2145 0.3352 -0.0520 0.0777  -0.0115 60  ILE A CA  
538  C C   . ILE A 59  ? 0.4162 0.2495 0.3617 -0.0580 0.0774  -0.0103 60  ILE A C   
539  O O   . ILE A 59  ? 0.4325 0.2528 0.3680 -0.0687 0.0857  -0.0133 60  ILE A O   
540  C CB  . ILE A 59  ? 0.4009 0.2504 0.3615 -0.0569 0.0733  -0.0191 60  ILE A CB  
541  C CG1 . ILE A 59  ? 0.4084 0.2496 0.3684 -0.0555 0.0769  -0.0226 60  ILE A CG1 
542  C CG2 . ILE A 59  ? 0.3760 0.2360 0.3385 -0.0704 0.0746  -0.0273 60  ILE A CG2 
543  C CD1 . ILE A 59  ? 0.4187 0.2789 0.3864 -0.0580 0.0711  -0.0277 60  ILE A CD1 
544  N N   . PHE A 60  ? 0.3582 0.2108 0.3123 -0.0527 0.0690  -0.0073 61  PHE A N   
545  C CA  . PHE A 60  ? 0.3532 0.2146 0.3068 -0.0594 0.0691  -0.0085 61  PHE A CA  
546  C C   . PHE A 60  ? 0.4166 0.2589 0.3535 -0.0572 0.0726  -0.0006 61  PHE A C   
547  O O   . PHE A 60  ? 0.4309 0.2773 0.3643 -0.0648 0.0752  -0.0023 61  PHE A O   
548  C CB  . PHE A 60  ? 0.3365 0.2259 0.3058 -0.0566 0.0595  -0.0107 61  PHE A CB  
549  C CG  . PHE A 60  ? 0.3330 0.2370 0.3135 -0.0599 0.0559  -0.0182 61  PHE A CG  
550  C CD1 . PHE A 60  ? 0.3701 0.2775 0.3523 -0.0710 0.0599  -0.0273 61  PHE A CD1 
551  C CD2 . PHE A 60  ? 0.3481 0.2617 0.3356 -0.0526 0.0484  -0.0168 61  PHE A CD2 
552  C CE1 . PHE A 60  ? 0.3768 0.2969 0.3669 -0.0731 0.0548  -0.0339 61  PHE A CE1 
553  C CE2 . PHE A 60  ? 0.3786 0.3016 0.3712 -0.0558 0.0445  -0.0227 61  PHE A CE2 
554  C CZ  . PHE A 60  ? 0.3541 0.2802 0.3475 -0.0652 0.0468  -0.0308 61  PHE A CZ  
555  N N   . THR A 61  ? 0.3969 0.2166 0.3219 -0.0474 0.0731  0.0072  62  THR A N   
556  C CA  . THR A 61  ? 0.4176 0.2130 0.3210 -0.0453 0.0761  0.0154  62  THR A CA  
557  C C   . THR A 61  ? 0.5219 0.2849 0.4061 -0.0541 0.0881  0.0146  62  THR A C   
558  O O   . THR A 61  ? 0.5466 0.2821 0.4071 -0.0554 0.0930  0.0211  62  THR A O   
559  C CB  . THR A 61  ? 0.5219 0.3118 0.4218 -0.0278 0.0675  0.0248  62  THR A CB  
560  O OG1 . THR A 61  ? 0.4796 0.2637 0.3862 -0.0187 0.0667  0.0242  62  THR A OG1 
561  C CG2 . THR A 61  ? 0.4574 0.2762 0.3713 -0.0221 0.0572  0.0257  62  THR A CG2 
562  N N   . ASP A 62  ? 0.4631 0.2281 0.3554 -0.0615 0.0934  0.0062  63  ASP A N   
563  C CA  . ASP A 62  ? 0.4928 0.2283 0.3681 -0.0724 0.1062  0.0032  63  ASP A CA  
564  C C   . ASP A 62  ? 0.5862 0.3274 0.4574 -0.0908 0.1141  -0.0037 63  ASP A C   
565  O O   . ASP A 62  ? 0.5518 0.3254 0.4428 -0.0971 0.1108  -0.0124 63  ASP A O   
566  C CB  . ASP A 62  ? 0.4910 0.2295 0.3768 -0.0752 0.1091  -0.0050 63  ASP A CB  
567  C CG  . ASP A 62  ? 0.6779 0.3883 0.5471 -0.0894 0.1233  -0.0102 63  ASP A CG  
568  O OD1 . ASP A 62  ? 0.7562 0.4308 0.6066 -0.0837 0.1286  -0.0042 63  ASP A OD1 
569  O OD2 . ASP A 62  ? 0.6848 0.4083 0.5591 -0.1062 0.1291  -0.0208 63  ASP A OD2 
570  N N   . GLN A 63  ? 0.6252 0.3338 0.4701 -0.0996 0.1251  -0.0006 64  GLN A N   
571  C CA  . GLN A 63  ? 0.6442 0.3548 0.4822 -0.1188 0.1353  -0.0078 64  GLN A CA  
572  C C   . GLN A 63  ? 0.6874 0.4214 0.5438 -0.1353 0.1414  -0.0242 64  GLN A C   
573  O O   . GLN A 63  ? 0.7039 0.4584 0.5681 -0.1479 0.1452  -0.0330 64  GLN A O   
574  C CB  . GLN A 63  ? 0.7179 0.3818 0.5191 -0.1263 0.1477  -0.0011 64  GLN A CB  
575  C CG  . GLN A 63  ? 0.9803 0.6264 0.7614 -0.1130 0.1408  0.0139  64  GLN A CG  
576  N N   . LEU A 64  ? 0.5941 0.3261 0.4574 -0.1357 0.1426  -0.0295 65  LEU A N   
577  C CA  . LEU A 64  ? 0.5667 0.3236 0.4479 -0.1502 0.1460  -0.0457 65  LEU A CA  
578  C C   . LEU A 64  ? 0.5798 0.3768 0.4891 -0.1410 0.1313  -0.0496 65  LEU A C   
579  O O   . LEU A 64  ? 0.5890 0.4169 0.5164 -0.1496 0.1291  -0.0615 65  LEU A O   
580  C CB  . LEU A 64  ? 0.5894 0.3226 0.4609 -0.1579 0.1558  -0.0509 65  LEU A CB  
581  C CG  . LEU A 64  ? 0.6997 0.3982 0.5465 -0.1756 0.1739  -0.0545 65  LEU A CG  
582  C CD1 . LEU A 64  ? 0.7120 0.3870 0.5507 -0.1803 0.1820  -0.0591 65  LEU A CD1 
583  C CD2 . LEU A 64  ? 0.7441 0.4657 0.5995 -0.1970 0.1822  -0.0694 65  LEU A CD2 
584  N N   . LYS A 65  ? 0.4830 0.2787 0.3958 -0.1242 0.1215  -0.0409 66  LYS A N   
585  C CA  . LYS A 65  ? 0.4510 0.2781 0.3852 -0.1166 0.1088  -0.0441 66  LYS A CA  
586  C C   . LYS A 65  ? 0.4987 0.3520 0.4460 -0.1104 0.0988  -0.0420 66  LYS A C   
587  O O   . LYS A 65  ? 0.4675 0.3481 0.4320 -0.1088 0.0897  -0.0479 66  LYS A O   
588  C CB  . LYS A 65  ? 0.4645 0.2819 0.3978 -0.1032 0.1039  -0.0374 66  LYS A CB  
589  C CG  . LYS A 65  ? 0.4785 0.2733 0.4021 -0.1089 0.1132  -0.0418 66  LYS A CG  
590  C CD  . LYS A 65  ? 0.4547 0.2464 0.3815 -0.0956 0.1081  -0.0374 66  LYS A CD  
591  C CE  . LYS A 65  ? 0.5261 0.2900 0.4414 -0.0987 0.1185  -0.0405 66  LYS A CE  
592  N NZ  . LYS A 65  ? 0.5570 0.2856 0.4546 -0.0928 0.1255  -0.0320 66  LYS A NZ  
593  N N   . CYS A 66  ? 0.5076 0.3510 0.4451 -0.1071 0.1002  -0.0340 67  CYS A N   
594  C CA  . CYS A 66  ? 0.4972 0.3632 0.4454 -0.1020 0.0921  -0.0324 67  CYS A CA  
595  C C   . CYS A 66  ? 0.5397 0.4347 0.5052 -0.1125 0.0917  -0.0459 67  CYS A C   
596  O O   . CYS A 66  ? 0.5268 0.4457 0.5072 -0.1067 0.0827  -0.0474 67  CYS A O   
597  C CB  . CYS A 66  ? 0.5303 0.3783 0.4611 -0.1001 0.0958  -0.0233 67  CYS A CB  
598  S SG  . CYS A 66  ? 0.6216 0.4503 0.5334 -0.1198 0.1126  -0.0288 67  CYS A SG  
599  N N   . ASN A 67  ? 0.4957 0.3884 0.4597 -0.1278 0.1019  -0.0566 68  ASN A N   
600  C CA  . ASN A 67  ? 0.4940 0.4156 0.4759 -0.1391 0.1029  -0.0721 68  ASN A CA  
601  C C   . ASN A 67  ? 0.5150 0.4589 0.5142 -0.1389 0.0947  -0.0821 68  ASN A C   
602  O O   . ASN A 67  ? 0.4918 0.4633 0.5086 -0.1461 0.0931  -0.0961 68  ASN A O   
603  C CB  . ASN A 67  ? 0.5219 0.4308 0.4923 -0.1580 0.1198  -0.0799 68  ASN A CB  
604  C CG  . ASN A 67  ? 0.7174 0.6106 0.6716 -0.1595 0.1264  -0.0724 68  ASN A CG  
605  O OD1 . ASN A 67  ? 0.7372 0.5992 0.6671 -0.1691 0.1394  -0.0687 68  ASN A OD1 
606  N ND2 . ASN A 67  ? 0.5976 0.5093 0.5623 -0.1499 0.1174  -0.0692 68  ASN A ND2 
607  N N   . LEU A 68  ? 0.4701 0.4036 0.4645 -0.1305 0.0891  -0.0756 69  LEU A N   
608  C CA  . LEU A 68  ? 0.4444 0.3957 0.4502 -0.1306 0.0809  -0.0841 69  LEU A CA  
609  C C   . LEU A 68  ? 0.4452 0.4210 0.4661 -0.1184 0.0649  -0.0832 69  LEU A C   
610  O O   . LEU A 68  ? 0.4194 0.3898 0.4375 -0.1070 0.0601  -0.0722 69  LEU A O   
611  C CB  . LEU A 68  ? 0.4543 0.3834 0.4471 -0.1276 0.0825  -0.0783 69  LEU A CB  
612  C CG  . LEU A 68  ? 0.5258 0.4277 0.5028 -0.1395 0.0980  -0.0805 69  LEU A CG  
613  C CD1 . LEU A 68  ? 0.5311 0.4119 0.4973 -0.1337 0.0989  -0.0747 69  LEU A CD1 
614  C CD2 . LEU A 68  ? 0.5296 0.4457 0.5137 -0.1570 0.1041  -0.0975 69  LEU A CD2 
615  N N   . SER A 69  ? 0.3839 0.3853 0.4197 -0.1205 0.0565  -0.0952 70  SER A N   
616  C CA  A SER A 69  ? 0.3643 0.3863 0.4124 -0.1086 0.0403  -0.0953 70  SER A CA  
617  C CA  B SER A 69  ? 0.3700 0.3912 0.4176 -0.1082 0.0404  -0.0946 70  SER A CA  
618  C C   . SER A 69  ? 0.3861 0.4013 0.4258 -0.1024 0.0312  -0.0909 70  SER A C   
619  O O   . SER A 69  ? 0.3388 0.3615 0.3811 -0.0919 0.0182  -0.0877 70  SER A O   
620  C CB  A SER A 69  ? 0.3995 0.4533 0.4684 -0.1129 0.0349  -0.1115 70  SER A CB  
621  C CB  B SER A 69  ? 0.4162 0.4694 0.4851 -0.1116 0.0348  -0.1100 70  SER A CB  
622  O OG  A SER A 69  ? 0.4527 0.5148 0.5301 -0.1191 0.0438  -0.1166 70  SER A OG  
623  O OG  B SER A 69  ? 0.5009 0.5649 0.5742 -0.1218 0.0356  -0.1230 70  SER A OG  
624  N N   . VAL A 70  ? 0.3524 0.3519 0.3803 -0.1100 0.0389  -0.0918 71  VAL A N   
625  C CA  . VAL A 70  ? 0.3432 0.3349 0.3609 -0.1070 0.0329  -0.0892 71  VAL A CA  
626  C C   . VAL A 70  ? 0.3812 0.3445 0.3834 -0.1083 0.0446  -0.0811 71  VAL A C   
627  O O   . VAL A 70  ? 0.3819 0.3324 0.3795 -0.1174 0.0574  -0.0838 71  VAL A O   
628  C CB  . VAL A 70  ? 0.4080 0.4150 0.4293 -0.1156 0.0284  -0.1030 71  VAL A CB  
629  C CG1 . VAL A 70  ? 0.4169 0.4133 0.4235 -0.1138 0.0232  -0.1003 71  VAL A CG1 
630  C CG2 . VAL A 70  ? 0.4025 0.4404 0.4419 -0.1122 0.0153  -0.1125 71  VAL A CG2 
631  N N   . ILE A 71  ? 0.3133 0.2660 0.3072 -0.0995 0.0404  -0.0721 72  ILE A N   
632  C CA  . ILE A 71  ? 0.3175 0.2466 0.2996 -0.0985 0.0498  -0.0659 72  ILE A CA  
633  C C   . ILE A 71  ? 0.3771 0.3033 0.3503 -0.0994 0.0459  -0.0680 72  ILE A C   
634  O O   . ILE A 71  ? 0.3703 0.3037 0.3421 -0.0935 0.0355  -0.0651 72  ILE A O   
635  C CB  . ILE A 71  ? 0.3426 0.2623 0.3242 -0.0879 0.0511  -0.0542 72  ILE A CB  
636  C CG1 . ILE A 71  ? 0.3523 0.2728 0.3386 -0.0879 0.0551  -0.0519 72  ILE A CG1 
637  C CG2 . ILE A 71  ? 0.3741 0.2727 0.3465 -0.0849 0.0593  -0.0497 72  ILE A CG2 
638  C CD1 . ILE A 71  ? 0.3977 0.3011 0.3768 -0.0974 0.0686  -0.0549 72  ILE A CD1 
639  N N   . ASN A 72  ? 0.3463 0.2593 0.3114 -0.1073 0.0552  -0.0730 73  ASN A N   
640  C CA  . ASN A 72  ? 0.3513 0.2597 0.3057 -0.1100 0.0537  -0.0760 73  ASN A CA  
641  C C   . ASN A 72  ? 0.3973 0.2872 0.3453 -0.1046 0.0617  -0.0698 73  ASN A C   
642  O O   . ASN A 72  ? 0.3894 0.2633 0.3365 -0.1051 0.0732  -0.0693 73  ASN A O   
643  C CB  . ASN A 72  ? 0.4109 0.3182 0.3606 -0.1233 0.0592  -0.0880 73  ASN A CB  
644  C CG  . ASN A 72  ? 0.6255 0.5549 0.5845 -0.1294 0.0517  -0.0971 73  ASN A CG  
645  O OD1 . ASN A 72  ? 0.4981 0.4452 0.4602 -0.1254 0.0375  -0.0983 73  ASN A OD1 
646  N ND2 . ASN A 72  ? 0.5558 0.4845 0.5195 -0.1394 0.0613  -0.1047 73  ASN A ND2 
647  N N   . LEU A 73  ? 0.3371 0.2282 0.2800 -0.0996 0.0562  -0.0658 74  LEU A N   
648  C CA  . LEU A 73  ? 0.3398 0.2177 0.2792 -0.0953 0.0641  -0.0624 74  LEU A CA  
649  C C   . LEU A 73  ? 0.3946 0.2610 0.3233 -0.1036 0.0725  -0.0703 74  LEU A C   
650  O O   . LEU A 73  ? 0.3975 0.2676 0.3185 -0.1129 0.0696  -0.0775 74  LEU A O   
651  C CB  . LEU A 73  ? 0.3364 0.2196 0.2745 -0.0887 0.0574  -0.0563 74  LEU A CB  
652  C CG  . LEU A 73  ? 0.3608 0.2545 0.3089 -0.0803 0.0496  -0.0488 74  LEU A CG  
653  C CD1 . LEU A 73  ? 0.3505 0.2448 0.2966 -0.0751 0.0475  -0.0439 74  LEU A CD1 
654  C CD2 . LEU A 73  ? 0.3504 0.2416 0.3092 -0.0755 0.0550  -0.0455 74  LEU A CD2 
655  N N   . ASP A 74  ? 0.3600 0.2139 0.2891 -0.1000 0.0826  -0.0699 75  ASP A N   
656  C CA  . ASP A 74  ? 0.3837 0.2251 0.3038 -0.1069 0.0929  -0.0781 75  ASP A CA  
657  C C   . ASP A 74  ? 0.4505 0.2975 0.3562 -0.1149 0.0871  -0.0820 75  ASP A C   
658  O O   . ASP A 74  ? 0.4236 0.2778 0.3267 -0.1112 0.0795  -0.0767 75  ASP A O   
659  C CB  . ASP A 74  ? 0.4073 0.2394 0.3339 -0.0983 0.1023  -0.0767 75  ASP A CB  
660  C CG  . ASP A 74  ? 0.5509 0.3692 0.4714 -0.1037 0.1148  -0.0862 75  ASP A CG  
661  O OD1 . ASP A 74  ? 0.5544 0.3747 0.4637 -0.1120 0.1157  -0.0918 75  ASP A OD1 
662  O OD2 . ASP A 74  ? 0.5739 0.3778 0.4995 -0.0993 0.1240  -0.0879 75  ASP A OD2 
663  N N   . PRO A 75  ? 0.4640 0.3066 0.3580 -0.1263 0.0902  -0.0912 76  PRO A N   
664  C CA  . PRO A 75  ? 0.4788 0.3247 0.3546 -0.1340 0.0834  -0.0945 76  PRO A CA  
665  C C   . PRO A 75  ? 0.5203 0.3601 0.3868 -0.1334 0.0878  -0.0931 76  PRO A C   
666  O O   . PRO A 75  ? 0.5471 0.3875 0.3958 -0.1383 0.0804  -0.0926 76  PRO A O   
667  C CB  . PRO A 75  ? 0.5202 0.3608 0.3862 -0.1465 0.0888  -0.1059 76  PRO A CB  
668  C CG  . PRO A 75  ? 0.5810 0.4096 0.4585 -0.1454 0.1030  -0.1090 76  PRO A CG  
669  C CD  . PRO A 75  ? 0.4930 0.3256 0.3873 -0.1335 0.1000  -0.0993 76  PRO A CD  
670  N N   . GLU A 76  ? 0.4699 0.3035 0.3473 -0.1277 0.0996  -0.0930 77  GLU A N   
671  C CA  . GLU A 76  ? 0.4938 0.3249 0.3656 -0.1282 0.1054  -0.0938 77  GLU A CA  
672  C C   . GLU A 76  ? 0.4955 0.3352 0.3693 -0.1218 0.0960  -0.0844 77  GLU A C   
673  O O   . GLU A 76  ? 0.4930 0.3308 0.3577 -0.1251 0.0991  -0.0850 77  GLU A O   
674  C CB  . GLU A 76  ? 0.5267 0.3523 0.4135 -0.1228 0.1203  -0.0987 77  GLU A CB  
675  C CG  . GLU A 76  ? 0.7892 0.6025 0.6693 -0.1311 0.1327  -0.1102 77  GLU A CG  
676  C CD  . GLU A 76  ? 1.2159 1.0252 1.0772 -0.1430 0.1394  -0.1183 77  GLU A CD  
677  O OE1 . GLU A 76  ? 1.2275 1.0383 1.0946 -0.1410 0.1484  -0.1218 77  GLU A OE1 
678  O OE2 . GLU A 76  ? 1.2136 1.0192 1.0540 -0.1548 0.1355  -0.1219 77  GLU A OE2 
679  N N   . ILE A 77  ? 0.4163 0.2646 0.3016 -0.1137 0.0858  -0.0768 78  ILE A N   
680  C CA  . ILE A 77  ? 0.3964 0.2518 0.2842 -0.1076 0.0773  -0.0684 78  ILE A CA  
681  C C   . ILE A 77  ? 0.4645 0.3177 0.3303 -0.1134 0.0664  -0.0661 78  ILE A C   
682  O O   . ILE A 77  ? 0.4467 0.3014 0.3045 -0.1163 0.0571  -0.0671 78  ILE A O   
683  C CB  . ILE A 77  ? 0.4123 0.2770 0.3192 -0.0971 0.0713  -0.0618 78  ILE A CB  
684  C CG1 . ILE A 77  ? 0.4178 0.2803 0.3421 -0.0901 0.0816  -0.0629 78  ILE A CG1 
685  C CG2 . ILE A 77  ? 0.3703 0.2421 0.2790 -0.0915 0.0626  -0.0541 78  ILE A CG2 
686  C CD1 . ILE A 77  ? 0.4923 0.3554 0.4244 -0.0858 0.0908  -0.0650 78  ILE A CD1 
687  N N   . ASN A 78  ? 0.4640 0.3134 0.3204 -0.1146 0.0672  -0.0633 79  ASN A N   
688  C CA  . ASN A 78  ? 0.4847 0.3258 0.3158 -0.1194 0.0579  -0.0596 79  ASN A CA  
689  C C   . ASN A 78  ? 0.4690 0.3164 0.3056 -0.1103 0.0432  -0.0511 79  ASN A C   
690  O O   . ASN A 78  ? 0.4204 0.2748 0.2741 -0.1032 0.0447  -0.0471 79  ASN A O   
691  C CB  . ASN A 78  ? 0.5419 0.3740 0.3609 -0.1260 0.0682  -0.0610 79  ASN A CB  
692  C CG  . ASN A 78  ? 0.7348 0.5523 0.5232 -0.1315 0.0602  -0.0559 79  ASN A CG  
693  O OD1 . ASN A 78  ? 0.5990 0.4148 0.3871 -0.1283 0.0573  -0.0501 79  ASN A OD1 
694  N ND2 . ASN A 78  ? 0.6832 0.4882 0.4435 -0.1399 0.0561  -0.0580 79  ASN A ND2 
695  N N   . PRO A 79  ? 0.4509 0.2967 0.2737 -0.1098 0.0286  -0.0491 80  PRO A N   
696  C CA  . PRO A 79  ? 0.4405 0.2928 0.2704 -0.1001 0.0149  -0.0424 80  PRO A CA  
697  C C   . PRO A 79  ? 0.4792 0.3225 0.3013 -0.0979 0.0144  -0.0357 80  PRO A C   
698  O O   . PRO A 79  ? 0.4551 0.3068 0.2938 -0.0895 0.0106  -0.0315 80  PRO A O   
699  C CB  . PRO A 79  ? 0.4885 0.3390 0.3013 -0.1006 -0.0004 -0.0434 80  PRO A CB  
700  C CG  . PRO A 79  ? 0.5518 0.4026 0.3595 -0.1099 0.0061  -0.0520 80  PRO A CG  
701  C CD  . PRO A 79  ? 0.5040 0.3441 0.3061 -0.1173 0.0232  -0.0539 80  PRO A CD  
702  N N   . GLU A 80  ? 0.4578 0.2834 0.2539 -0.1065 0.0195  -0.0355 81  GLU A N   
703  C CA  . GLU A 80  ? 0.4603 0.2751 0.2467 -0.1068 0.0209  -0.0301 81  GLU A CA  
704  C C   . GLU A 80  ? 0.4690 0.2973 0.2828 -0.1043 0.0330  -0.0316 81  GLU A C   
705  O O   . GLU A 80  ? 0.4426 0.2740 0.2650 -0.0986 0.0294  -0.0270 81  GLU A O   
706  C CB  . GLU A 80  ? 0.5143 0.3050 0.2640 -0.1191 0.0258  -0.0303 81  GLU A CB  
707  C CG  . GLU A 80  ? 0.6414 0.4172 0.3771 -0.1205 0.0264  -0.0247 81  GLU A CG  
708  C CD  . GLU A 80  ? 0.9910 0.7420 0.6914 -0.1353 0.0362  -0.0256 81  GLU A CD  
709  O OE1 . GLU A 80  ? 0.9724 0.7014 0.6473 -0.1369 0.0311  -0.0191 81  GLU A OE1 
710  O OE2 . GLU A 80  ? 0.9332 0.6851 0.6305 -0.1457 0.0498  -0.0333 81  GLU A OE2 
711  N N   . GLY A 81  ? 0.4346 0.2710 0.2620 -0.1078 0.0461  -0.0384 82  GLY A N   
712  C CA  . GLY A 81  ? 0.4077 0.2587 0.2623 -0.1033 0.0557  -0.0407 82  GLY A CA  
713  C C   . GLY A 81  ? 0.4161 0.2813 0.2939 -0.0913 0.0473  -0.0360 82  GLY A C   
714  O O   . GLY A 81  ? 0.3901 0.2635 0.2818 -0.0863 0.0479  -0.0337 82  GLY A O   
715  N N   . PHE A 82  ? 0.3570 0.2254 0.2380 -0.0878 0.0399  -0.0356 83  PHE A N   
716  C CA  . PHE A 82  ? 0.3280 0.2091 0.2289 -0.0783 0.0330  -0.0321 83  PHE A CA  
717  C C   . PHE A 82  ? 0.3695 0.2498 0.2665 -0.0740 0.0228  -0.0263 83  PHE A C   
718  O O   . PHE A 82  ? 0.3356 0.2254 0.2485 -0.0678 0.0221  -0.0237 83  PHE A O   
719  C CB  . PHE A 82  ? 0.3397 0.2250 0.2442 -0.0778 0.0281  -0.0345 83  PHE A CB  
720  C CG  . PHE A 82  ? 0.3290 0.2269 0.2536 -0.0699 0.0243  -0.0321 83  PHE A CG  
721  C CD1 . PHE A 82  ? 0.3530 0.2557 0.2938 -0.0662 0.0325  -0.0320 83  PHE A CD1 
722  C CD2 . PHE A 82  ? 0.3345 0.2385 0.2608 -0.0658 0.0125  -0.0300 83  PHE A CD2 
723  C CE1 . PHE A 82  ? 0.3500 0.2618 0.3052 -0.0602 0.0295  -0.0292 83  PHE A CE1 
724  C CE2 . PHE A 82  ? 0.3416 0.2573 0.2856 -0.0601 0.0106  -0.0287 83  PHE A CE2 
725  C CZ  . PHE A 82  ? 0.3292 0.2479 0.2858 -0.0581 0.0195  -0.0280 83  PHE A CZ  
726  N N   . CYS A 83  ? 0.3852 0.2533 0.2602 -0.0767 0.0142  -0.0245 84  CYS A N   
727  C CA  . CYS A 83  ? 0.4057 0.2686 0.2739 -0.0716 0.0036  -0.0191 84  CYS A CA  
728  C C   . CYS A 83  ? 0.4213 0.2816 0.2918 -0.0727 0.0106  -0.0169 84  CYS A C   
729  O O   . CYS A 83  ? 0.3933 0.2602 0.2757 -0.0662 0.0064  -0.0141 84  CYS A O   
730  C CB  . CYS A 83  ? 0.4669 0.3118 0.3057 -0.0743 -0.0063 -0.0173 84  CYS A CB  
731  S SG  . CYS A 83  ? 0.5466 0.3807 0.3750 -0.0656 -0.0212 -0.0108 84  CYS A SG  
732  N N   . ILE A 84  ? 0.3817 0.2345 0.2425 -0.0817 0.0223  -0.0197 85  ILE A N   
733  C CA  . ILE A 84  ? 0.3624 0.2154 0.2264 -0.0851 0.0307  -0.0203 85  ILE A CA  
734  C C   . ILE A 84  ? 0.3473 0.2227 0.2427 -0.0775 0.0335  -0.0214 85  ILE A C   
735  O O   . ILE A 84  ? 0.3353 0.2154 0.2382 -0.0751 0.0327  -0.0198 85  ILE A O   
736  C CB  . ILE A 84  ? 0.4135 0.2580 0.2640 -0.0973 0.0442  -0.0259 85  ILE A CB  
737  C CG1 . ILE A 84  ? 0.4535 0.2702 0.2653 -0.1062 0.0410  -0.0231 85  ILE A CG1 
738  C CG2 . ILE A 84  ? 0.4018 0.2568 0.2665 -0.1009 0.0557  -0.0304 85  ILE A CG2 
739  C CD1 . ILE A 84  ? 0.5582 0.3662 0.3538 -0.1191 0.0537  -0.0295 85  ILE A CD1 
740  N N   . LEU A 85  ? 0.3142 0.2013 0.2257 -0.0739 0.0367  -0.0242 86  LEU A N   
741  C CA  . LEU A 85  ? 0.2947 0.1993 0.2317 -0.0660 0.0384  -0.0243 86  LEU A CA  
742  C C   . LEU A 85  ? 0.3286 0.2393 0.2737 -0.0584 0.0284  -0.0196 86  LEU A C   
743  O O   . LEU A 85  ? 0.2972 0.2187 0.2563 -0.0536 0.0284  -0.0185 86  LEU A O   
744  C CB  . LEU A 85  ? 0.3017 0.2117 0.2497 -0.0642 0.0451  -0.0282 86  LEU A CB  
745  C CG  . LEU A 85  ? 0.3762 0.2859 0.3241 -0.0701 0.0571  -0.0351 86  LEU A CG  
746  C CD1 . LEU A 85  ? 0.3859 0.2969 0.3423 -0.0674 0.0628  -0.0391 86  LEU A CD1 
747  C CD2 . LEU A 85  ? 0.3847 0.3081 0.3479 -0.0679 0.0615  -0.0378 86  LEU A CD2 
748  N N   . LEU A 86  ? 0.2973 0.2028 0.2345 -0.0573 0.0199  -0.0179 87  LEU A N   
749  C CA  . LEU A 86  ? 0.2854 0.1982 0.2315 -0.0506 0.0111  -0.0153 87  LEU A CA  
750  C C   . LEU A 86  ? 0.3265 0.2356 0.2683 -0.0492 0.0070  -0.0126 87  LEU A C   
751  O O   . LEU A 86  ? 0.2920 0.2108 0.2466 -0.0443 0.0052  -0.0115 87  LEU A O   
752  C CB  . LEU A 86  ? 0.2839 0.1945 0.2238 -0.0502 0.0028  -0.0165 87  LEU A CB  
753  C CG  . LEU A 86  ? 0.3380 0.2596 0.2902 -0.0438 -0.0055 -0.0165 87  LEU A CG  
754  C CD1 . LEU A 86  ? 0.3237 0.2580 0.2944 -0.0417 0.0004  -0.0172 87  LEU A CD1 
755  C CD2 . LEU A 86  ? 0.3678 0.2900 0.3148 -0.0435 -0.0148 -0.0198 87  LEU A CD2 
756  N N   . ASP A 87  ? 0.3207 0.2134 0.2421 -0.0544 0.0064  -0.0117 88  ASP A N   
757  C CA  . ASP A 87  ? 0.3223 0.2062 0.2357 -0.0547 0.0044  -0.0094 88  ASP A CA  
758  C C   . ASP A 87  ? 0.3434 0.2394 0.2716 -0.0562 0.0129  -0.0114 88  ASP A C   
759  O O   . ASP A 87  ? 0.3374 0.2376 0.2724 -0.0528 0.0102  -0.0104 88  ASP A O   
760  C CB  . ASP A 87  ? 0.3792 0.2391 0.2636 -0.0624 0.0051  -0.0082 88  ASP A CB  
761  C CG  . ASP A 87  ? 0.5475 0.3929 0.4138 -0.0586 -0.0075 -0.0052 88  ASP A CG  
762  O OD1 . ASP A 87  ? 0.5428 0.3990 0.4222 -0.0495 -0.0172 -0.0051 88  ASP A OD1 
763  O OD2 . ASP A 87  ? 0.5780 0.4019 0.4166 -0.0648 -0.0080 -0.0036 88  ASP A OD2 
764  N N   . PHE A 88  ? 0.3010 0.2034 0.2348 -0.0607 0.0229  -0.0151 89  PHE A N   
765  C CA  . PHE A 88  ? 0.2791 0.1972 0.2299 -0.0607 0.0298  -0.0184 89  PHE A CA  
766  C C   . PHE A 88  ? 0.2801 0.2148 0.2507 -0.0514 0.0250  -0.0166 89  PHE A C   
767  O O   . PHE A 88  ? 0.2611 0.2052 0.2405 -0.0499 0.0249  -0.0172 89  PHE A O   
768  C CB  . PHE A 88  ? 0.2879 0.2123 0.2444 -0.0647 0.0400  -0.0240 89  PHE A CB  
769  C CG  . PHE A 88  ? 0.2785 0.2236 0.2570 -0.0612 0.0445  -0.0282 89  PHE A CG  
770  C CD1 . PHE A 88  ? 0.2938 0.2448 0.2746 -0.0667 0.0488  -0.0324 89  PHE A CD1 
771  C CD2 . PHE A 88  ? 0.2865 0.2445 0.2822 -0.0519 0.0433  -0.0278 89  PHE A CD2 
772  C CE1 . PHE A 88  ? 0.2830 0.2564 0.2855 -0.0626 0.0510  -0.0371 89  PHE A CE1 
773  C CE2 . PHE A 88  ? 0.3091 0.2860 0.3237 -0.0466 0.0447  -0.0310 89  PHE A CE2 
774  C CZ  . PHE A 88  ? 0.2827 0.2692 0.3019 -0.0516 0.0480  -0.0361 89  PHE A CZ  
775  N N   . MET A 89  ? 0.2343 0.1721 0.2104 -0.0463 0.0220  -0.0149 90  MET A N   
776  C CA  . MET A 89  ? 0.2131 0.1632 0.2037 -0.0390 0.0186  -0.0130 90  MET A CA  
777  C C   . MET A 89  ? 0.2643 0.2160 0.2554 -0.0370 0.0126  -0.0114 90  MET A C   
778  O O   . MET A 89  ? 0.2481 0.2111 0.2496 -0.0338 0.0124  -0.0112 90  MET A O   
779  C CB  . MET A 89  ? 0.2250 0.1733 0.2163 -0.0367 0.0168  -0.0120 90  MET A CB  
780  C CG  . MET A 89  ? 0.2552 0.2016 0.2479 -0.0376 0.0235  -0.0139 90  MET A CG  
781  S SD  . MET A 89  ? 0.2973 0.2410 0.2906 -0.0365 0.0221  -0.0135 90  MET A SD  
782  C CE  . MET A 89  ? 0.3039 0.2391 0.2933 -0.0397 0.0309  -0.0171 90  MET A CE  
783  N N   . TYR A 90  ? 0.2449 0.1850 0.2243 -0.0382 0.0071  -0.0105 91  TYR A N   
784  C CA  . TYR A 90  ? 0.2420 0.1816 0.2221 -0.0350 0.0009  -0.0098 91  TYR A CA  
785  C C   . TYR A 90  ? 0.2988 0.2302 0.2709 -0.0387 0.0023  -0.0102 91  TYR A C   
786  O O   . TYR A 90  ? 0.2856 0.2153 0.2584 -0.0359 -0.0021 -0.0102 91  TYR A O   
787  C CB  . TYR A 90  ? 0.2625 0.1940 0.2354 -0.0321 -0.0074 -0.0094 91  TYR A CB  
788  C CG  . TYR A 90  ? 0.2651 0.2089 0.2503 -0.0286 -0.0096 -0.0111 91  TYR A CG  
789  C CD1 . TYR A 90  ? 0.2848 0.2296 0.2698 -0.0309 -0.0067 -0.0118 91  TYR A CD1 
790  C CD2 . TYR A 90  ? 0.2661 0.2201 0.2627 -0.0242 -0.0132 -0.0129 91  TYR A CD2 
791  C CE1 . TYR A 90  ? 0.2756 0.2299 0.2703 -0.0298 -0.0073 -0.0143 91  TYR A CE1 
792  C CE2 . TYR A 90  ? 0.2592 0.2240 0.2658 -0.0231 -0.0138 -0.0158 91  TYR A CE2 
793  C CZ  . TYR A 90  ? 0.3036 0.2683 0.3090 -0.0264 -0.0105 -0.0163 91  TYR A CZ  
794  O OH  . TYR A 90  ? 0.2741 0.2481 0.2882 -0.0273 -0.0098 -0.0202 91  TYR A OH  
795  N N   . THR A 91  ? 0.2590 0.1851 0.2237 -0.0458 0.0094  -0.0116 92  THR A N   
796  C CA  . THR A 91  ? 0.2693 0.1850 0.2238 -0.0517 0.0122  -0.0129 92  THR A CA  
797  C C   . THR A 91  ? 0.2942 0.2213 0.2563 -0.0584 0.0217  -0.0179 92  THR A C   
798  O O   . THR A 91  ? 0.3045 0.2256 0.2605 -0.0645 0.0250  -0.0203 92  THR A O   
799  C CB  . THR A 91  ? 0.3505 0.2391 0.2785 -0.0572 0.0114  -0.0109 92  THR A CB  
800  O OG1 . THR A 91  ? 0.3542 0.2409 0.2761 -0.0636 0.0183  -0.0126 92  THR A OG1 
801  C CG2 . THR A 91  ? 0.3600 0.2363 0.2786 -0.0497 -0.0001 -0.0069 92  THR A CG2 
802  N N   . SER A 92  ? 0.2416 0.1828 0.2154 -0.0578 0.0263  -0.0203 93  SER A N   
803  C CA  . SER A 92  ? 0.2369 0.1925 0.2210 -0.0630 0.0351  -0.0269 93  SER A CA  
804  C C   . SER A 92  ? 0.2960 0.2367 0.2634 -0.0750 0.0438  -0.0307 93  SER A C   
805  O O   . SER A 92  ? 0.2906 0.2436 0.2666 -0.0811 0.0526  -0.0383 93  SER A O   
806  C CB  . SER A 92  ? 0.2608 0.2300 0.2552 -0.0643 0.0357  -0.0307 93  SER A CB  
807  O OG  . SER A 92  ? 0.2948 0.2745 0.2999 -0.0552 0.0282  -0.0274 93  SER A OG  
808  N N   A ARG A 93  ? 0.2881 0.2033 0.2316 -0.0782 0.0412  -0.0261 94  ARG A N   
809  N N   B ARG A 93  ? 0.2801 0.1950 0.2233 -0.0785 0.0413  -0.0262 94  ARG A N   
810  C CA  A ARG A 93  ? 0.3130 0.2078 0.2332 -0.0906 0.0490  -0.0282 94  ARG A CA  
811  C CA  B ARG A 93  ? 0.3011 0.1970 0.2222 -0.0911 0.0497  -0.0288 94  ARG A CA  
812  C C   A ARG A 93  ? 0.3716 0.2619 0.2854 -0.0913 0.0509  -0.0281 94  ARG A C   
813  C C   B ARG A 93  ? 0.3650 0.2546 0.2781 -0.0917 0.0510  -0.0281 94  ARG A C   
814  O O   A ARG A 93  ? 0.3513 0.2362 0.2615 -0.0839 0.0422  -0.0227 94  ARG A O   
815  O O   B ARG A 93  ? 0.3471 0.2304 0.2556 -0.0844 0.0420  -0.0225 94  ARG A O   
816  C CB  A ARG A 93  ? 0.3667 0.2312 0.2590 -0.0935 0.0437  -0.0226 94  ARG A CB  
817  C CB  B ARG A 93  ? 0.3368 0.2033 0.2303 -0.0965 0.0470  -0.0246 94  ARG A CB  
818  C CG  A ARG A 93  ? 0.4312 0.2958 0.3271 -0.0937 0.0426  -0.0233 94  ARG A CG  
819  C CG  B ARG A 93  ? 0.3369 0.2071 0.2352 -0.1015 0.0511  -0.0286 94  ARG A CG  
820  C CD  A ARG A 93  ? 0.5478 0.3808 0.4178 -0.0921 0.0349  -0.0168 94  ARG A CD  
821  C CD  B ARG A 93  ? 0.5101 0.3509 0.3848 -0.1020 0.0456  -0.0232 94  ARG A CD  
822  N NE  A ARG A 93  ? 0.6268 0.4280 0.4629 -0.1030 0.0398  -0.0152 94  ARG A NE  
823  N NE  B ARG A 93  ? 0.5743 0.4200 0.4557 -0.1066 0.0497  -0.0278 94  ARG A NE  
824  C CZ  A ARG A 93  ? 0.8080 0.5915 0.6259 -0.1169 0.0501  -0.0186 94  ARG A CZ  
825  C CZ  B ARG A 93  ? 0.7324 0.5498 0.5902 -0.1143 0.0523  -0.0271 94  ARG A CZ  
826  N NH1 A ARG A 93  ? 0.6756 0.4273 0.4589 -0.1274 0.0547  -0.0164 94  ARG A NH1 
827  N NH1 B ARG A 93  ? 0.5994 0.4235 0.4653 -0.1191 0.0567  -0.0325 94  ARG A NH1 
828  N NH2 A ARG A 93  ? 0.6148 0.4116 0.4475 -0.1215 0.0563  -0.0246 94  ARG A NH2 
829  N NH2 B ARG A 93  ? 0.5977 0.3783 0.4218 -0.1174 0.0503  -0.0211 94  ARG A NH2 
830  N N   . LEU A 94  ? 0.3356 0.2288 0.2483 -0.1011 0.0629  -0.0354 95  LEU A N   
831  C CA  . LEU A 94  ? 0.3426 0.2316 0.2490 -0.1034 0.0669  -0.0371 95  LEU A CA  
832  C C   . LEU A 94  ? 0.4261 0.2890 0.3002 -0.1181 0.0742  -0.0384 95  LEU A C   
833  O O   . LEU A 94  ? 0.4188 0.2809 0.2885 -0.1303 0.0860  -0.0454 95  LEU A O   
834  C CB  . LEU A 94  ? 0.3276 0.2436 0.2622 -0.1008 0.0748  -0.0456 95  LEU A CB  
835  C CG  . LEU A 94  ? 0.3769 0.2913 0.3099 -0.1019 0.0802  -0.0490 95  LEU A CG  
836  C CD1 . LEU A 94  ? 0.3551 0.2667 0.2899 -0.0909 0.0697  -0.0418 95  LEU A CD1 
837  C CD2 . LEU A 94  ? 0.3805 0.3189 0.3393 -0.1010 0.0903  -0.0599 95  LEU A CD2 
838  N N   . ASN A 95  ? 0.4295 0.2709 0.2794 -0.1176 0.0674  -0.0322 96  ASN A N   
839  C CA  . ASN A 95  ? 0.4690 0.2807 0.2815 -0.1310 0.0725  -0.0318 96  ASN A CA  
840  C C   . ASN A 95  ? 0.5190 0.3365 0.3320 -0.1397 0.0851  -0.0402 96  ASN A C   
841  O O   . ASN A 95  ? 0.5274 0.3369 0.3286 -0.1388 0.0816  -0.0384 96  ASN A O   
842  C CB  . ASN A 95  ? 0.5266 0.3131 0.3120 -0.1254 0.0575  -0.0217 96  ASN A CB  
843  C CG  . ASN A 95  ? 0.7700 0.5210 0.5108 -0.1383 0.0605  -0.0195 96  ASN A CG  
844  O OD1 . ASN A 95  ? 0.7071 0.4461 0.4323 -0.1530 0.0740  -0.0240 96  ASN A OD1 
845  N ND2 . ASN A 95  ? 0.7053 0.4389 0.4235 -0.1338 0.0483  -0.0131 96  ASN A ND2 
846  N N   . LEU A 96  ? 0.4639 0.2986 0.2940 -0.1473 0.0994  -0.0507 97  LEU A N   
847  C CA  . LEU A 96  ? 0.4710 0.3158 0.3078 -0.1548 0.1131  -0.0614 97  LEU A CA  
848  C C   . LEU A 96  ? 0.5501 0.3699 0.3516 -0.1747 0.1256  -0.0656 97  LEU A C   
849  O O   . LEU A 96  ? 0.5481 0.3599 0.3390 -0.1859 0.1330  -0.0683 97  LEU A O   
850  C CB  . LEU A 96  ? 0.4560 0.3360 0.3333 -0.1506 0.1208  -0.0719 97  LEU A CB  
851  C CG  . LEU A 96  ? 0.5237 0.4233 0.4225 -0.1495 0.1307  -0.0829 97  LEU A CG  
852  C CD1 . LEU A 96  ? 0.5186 0.4153 0.4199 -0.1375 0.1217  -0.0769 97  LEU A CD1 
853  C CD2 . LEU A 96  ? 0.5066 0.4409 0.4452 -0.1423 0.1346  -0.0923 97  LEU A CD2 
854  N N   . ARG A 97  ? 0.5237 0.3285 0.3034 -0.1805 0.1281  -0.0661 98  ARG A N   
855  C CA  . ARG A 97  ? 0.5762 0.3528 0.3156 -0.2004 0.1398  -0.0693 98  ARG A CA  
856  C C   . ARG A 97  ? 0.5996 0.3847 0.3427 -0.2080 0.1530  -0.0806 98  ARG A C   
857  O O   . ARG A 97  ? 0.5571 0.3598 0.3236 -0.1960 0.1483  -0.0818 98  ARG A O   
858  C CB  . ARG A 97  ? 0.6383 0.3768 0.3329 -0.2006 0.1260  -0.0556 98  ARG A CB  
859  C CG  . ARG A 97  ? 0.7304 0.4559 0.4180 -0.1924 0.1124  -0.0445 98  ARG A CG  
860  C CD  . ARG A 97  ? 0.9532 0.6440 0.6007 -0.1882 0.0959  -0.0315 98  ARG A CD  
861  N NE  . ARG A 97  ? 1.2173 0.8707 0.8143 -0.2059 0.1035  -0.0309 98  ARG A NE  
862  C CZ  . ARG A 97  ? 1.4892 1.1116 1.0529 -0.2187 0.1101  -0.0285 98  ARG A CZ  
863  N NH1 . ARG A 97  ? 1.3814 0.9676 0.8958 -0.2356 0.1174  -0.0276 98  ARG A NH1 
864  N NH2 . ARG A 97  ? 1.3283 0.9540 0.9057 -0.2158 0.1100  -0.0273 98  ARG A NH2 
865  N N   . GLU A 98  ? 0.5900 0.3607 0.3081 -0.2289 0.1705  -0.0895 99  GLU A N   
866  C CA  . GLU A 98  ? 0.5959 0.3731 0.3151 -0.2378 0.1849  -0.1019 99  GLU A CA  
867  C C   . GLU A 98  ? 0.6523 0.4193 0.3588 -0.2298 0.1732  -0.0951 99  GLU A C   
868  O O   . GLU A 98  ? 0.6427 0.4285 0.3727 -0.2250 0.1781  -0.1033 99  GLU A O   
869  C CB  . GLU A 98  ? 0.6606 0.4140 0.3415 -0.2639 0.2038  -0.1099 99  GLU A CB  
870  C CG  . GLU A 98  ? 0.7981 0.5609 0.4825 -0.2752 0.2218  -0.1256 99  GLU A CG  
871  C CD  . GLU A 98  ? 1.2452 0.9828 0.8883 -0.3030 0.2418  -0.1340 99  GLU A CD  
872  O OE1 . GLU A 98  ? 1.2267 0.9232 0.8176 -0.3129 0.2365  -0.1223 99  GLU A OE1 
873  O OE2 . GLU A 98  ? 1.2843 1.0428 0.9467 -0.3147 0.2628  -0.1529 99  GLU A OE2 
874  N N   . GLY A 99  ? 0.6480 0.3859 0.3188 -0.2278 0.1576  -0.0808 100 GLY A N   
875  C CA  . GLY A 99  ? 0.6664 0.3942 0.3218 -0.2216 0.1449  -0.0747 100 GLY A CA  
876  C C   . GLY A 99  ? 0.6634 0.4152 0.3556 -0.2009 0.1311  -0.0709 100 GLY A C   
877  O O   . GLY A 99  ? 0.6640 0.4144 0.3515 -0.1972 0.1246  -0.0701 100 GLY A O   
878  N N   . ASN A 100 ? 0.5806 0.3544 0.3084 -0.1883 0.1271  -0.0691 101 ASN A N   
879  C CA  . ASN A 100 ? 0.5394 0.3330 0.2985 -0.1700 0.1148  -0.0651 101 ASN A CA  
880  C C   . ASN A 100 ? 0.5441 0.3688 0.3484 -0.1613 0.1228  -0.0733 101 ASN A C   
881  O O   . ASN A 100 ? 0.5051 0.3433 0.3326 -0.1475 0.1146  -0.0705 101 ASN A O   
882  C CB  . ASN A 100 ? 0.5370 0.3250 0.2932 -0.1589 0.0966  -0.0523 101 ASN A CB  
883  C CG  . ASN A 100 ? 0.6220 0.4174 0.3921 -0.1571 0.0984  -0.0511 101 ASN A CG  
884  O OD1 . ASN A 100 ? 0.4786 0.2955 0.2766 -0.1572 0.1094  -0.0593 101 ASN A OD1 
885  N ND2 . ASN A 100 ? 0.5351 0.3140 0.2877 -0.1542 0.0870  -0.0415 101 ASN A ND2 
886  N N   . ILE A 101 ? 0.5057 0.3417 0.3221 -0.1690 0.1380  -0.0836 102 ILE A N   
887  C CA  . ILE A 101 ? 0.4767 0.3434 0.3363 -0.1590 0.1435  -0.0915 102 ILE A CA  
888  C C   . ILE A 101 ? 0.4951 0.3730 0.3757 -0.1494 0.1449  -0.0963 102 ILE A C   
889  O O   . ILE A 101 ? 0.4413 0.3367 0.3517 -0.1338 0.1388  -0.0944 102 ILE A O   
890  C CB  . ILE A 101 ? 0.5219 0.4017 0.3920 -0.1701 0.1601  -0.1046 102 ILE A CB  
891  C CG1 . ILE A 101 ? 0.5043 0.4186 0.4212 -0.1561 0.1615  -0.1120 102 ILE A CG1 
892  C CG2 . ILE A 101 ? 0.5328 0.4027 0.3836 -0.1878 0.1775  -0.1165 102 ILE A CG2 
893  C CD1 . ILE A 101 ? 0.5133 0.4456 0.4452 -0.1625 0.1698  -0.1208 102 ILE A CD1 
894  N N   . MET A 102 ? 0.4808 0.3469 0.3442 -0.1587 0.1531  -0.1023 103 MET A N   
895  C CA  . MET A 102 ? 0.4820 0.3551 0.3630 -0.1505 0.1553  -0.1074 103 MET A CA  
896  C C   . MET A 102 ? 0.4988 0.3683 0.3826 -0.1377 0.1394  -0.0959 103 MET A C   
897  O O   . MET A 102 ? 0.4553 0.3370 0.3657 -0.1246 0.1380  -0.0968 103 MET A O   
898  C CB  . MET A 102 ? 0.5474 0.4078 0.4078 -0.1646 0.1682  -0.1174 103 MET A CB  
899  C CG  . MET A 102 ? 0.6281 0.4953 0.4903 -0.1779 0.1873  -0.1320 103 MET A CG  
900  S SD  . MET A 102 ? 0.6770 0.5798 0.5906 -0.1658 0.1955  -0.1440 103 MET A SD  
901  C CE  . MET A 102 ? 0.6353 0.5444 0.5728 -0.1528 0.1994  -0.1518 103 MET A CE  
902  N N   . ALA A 103 ? 0.4720 0.3247 0.3283 -0.1412 0.1272  -0.0857 104 ALA A N   
903  C CA  . ALA A 103 ? 0.4651 0.3167 0.3244 -0.1309 0.1124  -0.0766 104 ALA A CA  
904  C C   . ALA A 103 ? 0.4603 0.3270 0.3451 -0.1172 0.1045  -0.0701 104 ALA A C   
905  O O   . ALA A 103 ? 0.4259 0.3000 0.3289 -0.1065 0.0999  -0.0678 104 ALA A O   
906  C CB  . ALA A 103 ? 0.5010 0.3347 0.3276 -0.1367 0.1005  -0.0688 104 ALA A CB  
907  N N   . VAL A 104 ? 0.3927 0.2624 0.2769 -0.1188 0.1039  -0.0678 105 VAL A N   
908  C CA  . VAL A 104 ? 0.3563 0.2408 0.2633 -0.1071 0.0968  -0.0625 105 VAL A CA  
909  C C   . VAL A 104 ? 0.3773 0.2806 0.3162 -0.0969 0.1026  -0.0682 105 VAL A C   
910  O O   . VAL A 104 ? 0.3572 0.2675 0.3114 -0.0849 0.0947  -0.0627 105 VAL A O   
911  C CB  . VAL A 104 ? 0.4007 0.2838 0.3000 -0.1124 0.0964  -0.0603 105 VAL A CB  
912  C CG1 . VAL A 104 ? 0.3632 0.2643 0.2878 -0.1011 0.0908  -0.0571 105 VAL A CG1 
913  C CG2 . VAL A 104 ? 0.4199 0.2811 0.2875 -0.1177 0.0866  -0.0520 105 VAL A CG2 
914  N N   A MET A 105 ? 0.3618 0.2727 0.3101 -0.1011 0.1161  -0.0796 106 MET A N   
915  N N   B MET A 105 ? 0.3608 0.2718 0.3092 -0.1011 0.1161  -0.0796 106 MET A N   
916  C CA  A MET A 105 ? 0.3581 0.2867 0.3372 -0.0891 0.1203  -0.0858 106 MET A CA  
917  C CA  B MET A 105 ? 0.3566 0.2851 0.3356 -0.0892 0.1204  -0.0859 106 MET A CA  
918  C C   A MET A 105 ? 0.3945 0.3156 0.3774 -0.0805 0.1177  -0.0836 106 MET A C   
919  C C   B MET A 105 ? 0.4012 0.3225 0.3843 -0.0805 0.1178  -0.0836 106 MET A C   
920  O O   A MET A 105 ? 0.3617 0.2902 0.3632 -0.0667 0.1127  -0.0803 106 MET A O   
921  O O   B MET A 105 ? 0.3757 0.3043 0.3771 -0.0667 0.1125  -0.0801 106 MET A O   
922  C CB  A MET A 105 ? 0.4012 0.3407 0.3910 -0.0952 0.1355  -0.1007 106 MET A CB  
923  C CB  B MET A 105 ? 0.3996 0.3390 0.3892 -0.0954 0.1356  -0.1007 106 MET A CB  
924  C CG  A MET A 105 ? 0.4353 0.3954 0.4594 -0.0800 0.1375  -0.1075 106 MET A CG  
925  C CG  B MET A 105 ? 0.4356 0.3962 0.4597 -0.0803 0.1376  -0.1075 106 MET A CG  
926  S SD  A MET A 105 ? 0.4952 0.4760 0.5383 -0.0866 0.1548  -0.1275 106 MET A SD  
927  S SD  B MET A 105 ? 0.5015 0.4796 0.5429 -0.0870 0.1558  -0.1279 106 MET A SD  
928  C CE  A MET A 105 ? 0.4817 0.4445 0.5097 -0.0957 0.1679  -0.1363 106 MET A CE  
929  C CE  B MET A 105 ? 0.4578 0.4468 0.5308 -0.0652 0.1547  -0.1329 106 MET A CE  
930  N N   . ALA A 106 ? 0.3852 0.2905 0.3489 -0.0894 0.1217  -0.0858 107 ALA A N   
931  C CA  . ALA A 106 ? 0.3883 0.2841 0.3528 -0.0843 0.1209  -0.0850 107 ALA A CA  
932  C C   . ALA A 106 ? 0.3996 0.2932 0.3642 -0.0766 0.1075  -0.0733 107 ALA A C   
933  O O   . ALA A 106 ? 0.3712 0.2638 0.3481 -0.0665 0.1061  -0.0713 107 ALA A O   
934  C CB  . ALA A 106 ? 0.4223 0.3028 0.3632 -0.0977 0.1263  -0.0898 107 ALA A CB  
935  N N   . THR A 107 ? 0.3514 0.2431 0.3020 -0.0812 0.0980  -0.0660 108 THR A N   
936  C CA  . THR A 107 ? 0.3365 0.2289 0.2887 -0.0749 0.0860  -0.0567 108 THR A CA  
937  C C   . THR A 107 ? 0.3688 0.2737 0.3422 -0.0626 0.0828  -0.0527 108 THR A C   
938  O O   . THR A 107 ? 0.3367 0.2405 0.3168 -0.0552 0.0787  -0.0483 108 THR A O   
939  C CB  . THR A 107 ? 0.4105 0.2978 0.3435 -0.0813 0.0762  -0.0512 108 THR A CB  
940  O OG1 . THR A 107 ? 0.4088 0.2840 0.3196 -0.0925 0.0790  -0.0553 108 THR A OG1 
941  C CG2 . THR A 107 ? 0.3932 0.2822 0.3286 -0.0760 0.0650  -0.0446 108 THR A CG2 
942  N N   . ALA A 108 ? 0.3145 0.2309 0.2971 -0.0614 0.0853  -0.0551 109 ALA A N   
943  C CA  . ALA A 108 ? 0.2851 0.2156 0.2872 -0.0499 0.0814  -0.0523 109 ALA A CA  
944  C C   . ALA A 108 ? 0.3197 0.2515 0.3375 -0.0388 0.0852  -0.0551 109 ALA A C   
945  O O   . ALA A 108 ? 0.3029 0.2373 0.3293 -0.0281 0.0790  -0.0494 109 ALA A O   
946  C CB  . ALA A 108 ? 0.2825 0.2265 0.2912 -0.0531 0.0841  -0.0566 109 ALA A CB  
947  N N   . MET A 109 ? 0.3081 0.2354 0.3274 -0.0410 0.0952  -0.0639 110 MET A N   
948  C CA  . MET A 109 ? 0.3042 0.2285 0.3367 -0.0290 0.0987  -0.0667 110 MET A CA  
949  C C   . MET A 109 ? 0.3523 0.2589 0.3751 -0.0262 0.0947  -0.0592 110 MET A C   
950  O O   . MET A 109 ? 0.3502 0.2536 0.3801 -0.0141 0.0908  -0.0543 110 MET A O   
951  C CB  . MET A 109 ? 0.3472 0.2696 0.3829 -0.0330 0.1113  -0.0792 110 MET A CB  
952  C CG  . MET A 109 ? 0.4033 0.3465 0.4552 -0.0331 0.1169  -0.0890 110 MET A CG  
953  S SD  . MET A 109 ? 0.4996 0.4404 0.5512 -0.0428 0.1339  -0.1051 110 MET A SD  
954  C CE  . MET A 109 ? 0.4737 0.4064 0.5413 -0.0252 0.1363  -0.1086 110 MET A CE  
955  N N   . TYR A 110 ? 0.3445 0.2400 0.3499 -0.0378 0.0951  -0.0584 111 TYR A N   
956  C CA  . TYR A 110 ? 0.3467 0.2277 0.3425 -0.0390 0.0926  -0.0536 111 TYR A CA  
957  C C   . TYR A 110 ? 0.3616 0.2471 0.3593 -0.0335 0.0825  -0.0437 111 TYR A C   
958  O O   . TYR A 110 ? 0.3475 0.2232 0.3451 -0.0279 0.0817  -0.0395 111 TYR A O   
959  C CB  . TYR A 110 ? 0.3589 0.2338 0.3375 -0.0533 0.0932  -0.0563 111 TYR A CB  
960  C CG  . TYR A 110 ? 0.3612 0.2272 0.3313 -0.0571 0.0894  -0.0530 111 TYR A CG  
961  C CD1 . TYR A 110 ? 0.3969 0.2477 0.3646 -0.0576 0.0964  -0.0562 111 TYR A CD1 
962  C CD2 . TYR A 110 ? 0.3533 0.2261 0.3177 -0.0614 0.0798  -0.0484 111 TYR A CD2 
963  C CE1 . TYR A 110 ? 0.3713 0.2153 0.3316 -0.0637 0.0945  -0.0551 111 TYR A CE1 
964  C CE2 . TYR A 110 ? 0.3510 0.2197 0.3102 -0.0662 0.0771  -0.0480 111 TYR A CE2 
965  C CZ  . TYR A 110 ? 0.3805 0.2354 0.3374 -0.0685 0.0850  -0.0519 111 TYR A CZ  
966  O OH  . TYR A 110 ? 0.3799 0.2324 0.3323 -0.0753 0.0836  -0.0533 111 TYR A OH  
967  N N   . LEU A 111 ? 0.3031 0.2015 0.3009 -0.0359 0.0757  -0.0405 112 LEU A N   
968  C CA  . LEU A 111 ? 0.2828 0.1869 0.2826 -0.0318 0.0669  -0.0326 112 LEU A CA  
969  C C   . LEU A 111 ? 0.3260 0.2371 0.3386 -0.0194 0.0647  -0.0295 112 LEU A C   
970  O O   . LEU A 111 ? 0.3128 0.2264 0.3258 -0.0155 0.0584  -0.0231 112 LEU A O   
971  C CB  . LEU A 111 ? 0.2586 0.1718 0.2534 -0.0382 0.0605  -0.0311 112 LEU A CB  
972  C CG  . LEU A 111 ? 0.3021 0.2088 0.2823 -0.0484 0.0584  -0.0326 112 LEU A CG  
973  C CD1 . LEU A 111 ? 0.3072 0.2198 0.2815 -0.0515 0.0506  -0.0298 112 LEU A CD1 
974  C CD2 . LEU A 111 ? 0.3198 0.2208 0.2976 -0.0495 0.0565  -0.0311 112 LEU A CD2 
975  N N   . GLN A 112 ? 0.2965 0.2127 0.3200 -0.0131 0.0694  -0.0349 113 GLN A N   
976  C CA  . GLN A 112 ? 0.3023 0.2282 0.3397 0.0003  0.0657  -0.0334 113 GLN A CA  
977  C C   . GLN A 112 ? 0.3123 0.2564 0.3547 -0.0005 0.0587  -0.0308 113 GLN A C   
978  O O   . GLN A 112 ? 0.2898 0.2360 0.3317 0.0049  0.0515  -0.0240 113 GLN A O   
979  C CB  . GLN A 112 ? 0.3313 0.2418 0.3643 0.0100  0.0631  -0.0266 113 GLN A CB  
980  C CG  . GLN A 112 ? 0.3717 0.2609 0.3988 0.0106  0.0711  -0.0297 113 GLN A CG  
981  C CD  . GLN A 112 ? 0.4969 0.3648 0.5123 0.0154  0.0696  -0.0219 113 GLN A CD  
982  O OE1 . GLN A 112 ? 0.4164 0.2852 0.4314 0.0240  0.0627  -0.0150 113 GLN A OE1 
983  N NE2 . GLN A 112 ? 0.4846 0.3319 0.4882 0.0086  0.0766  -0.0233 113 GLN A NE2 
984  N N   . MET A 113 ? 0.2699 0.2248 0.3146 -0.0086 0.0617  -0.0367 114 MET A N   
985  C CA  . MET A 113 ? 0.2632 0.2333 0.3114 -0.0117 0.0573  -0.0362 114 MET A CA  
986  C C   . MET A 113 ? 0.3241 0.3116 0.3885 -0.0098 0.0623  -0.0460 114 MET A C   
987  O O   . MET A 113 ? 0.3035 0.2930 0.3658 -0.0198 0.0700  -0.0533 114 MET A O   
988  C CB  . MET A 113 ? 0.2844 0.2470 0.3168 -0.0247 0.0573  -0.0350 114 MET A CB  
989  C CG  . MET A 113 ? 0.3103 0.2609 0.3312 -0.0257 0.0516  -0.0276 114 MET A CG  
990  S SD  . MET A 113 ? 0.3449 0.2866 0.3478 -0.0378 0.0494  -0.0269 114 MET A SD  
991  C CE  . MET A 113 ? 0.3025 0.2549 0.3079 -0.0385 0.0439  -0.0248 114 MET A CE  
992  N N   . GLU A 114 ? 0.3198 0.3189 0.3999 0.0036  0.0585  -0.0468 115 GLU A N   
993  C CA  . GLU A 114 ? 0.3381 0.3570 0.4390 0.0091  0.0625  -0.0579 115 GLU A CA  
994  C C   . GLU A 114 ? 0.3410 0.3793 0.4489 -0.0014 0.0663  -0.0662 115 GLU A C   
995  O O   . GLU A 114 ? 0.3216 0.3706 0.4405 -0.0052 0.0753  -0.0780 115 GLU A O   
996  C CB  . GLU A 114 ? 0.3733 0.4017 0.4884 0.0274  0.0540  -0.0561 115 GLU A CB  
997  C CG  . GLU A 114 ? 0.5609 0.5662 0.6676 0.0378  0.0524  -0.0493 115 GLU A CG  
998  N N   . HIS A 115 ? 0.2877 0.3297 0.3893 -0.0069 0.0609  -0.0612 116 HIS A N   
999  C CA  . HIS A 115 ? 0.3046 0.3618 0.4107 -0.0182 0.0657  -0.0695 116 HIS A CA  
1000 C C   . HIS A 115 ? 0.3321 0.3749 0.4217 -0.0347 0.0762  -0.0731 116 HIS A C   
1001 O O   . HIS A 115 ? 0.3350 0.3890 0.4307 -0.0439 0.0856  -0.0844 116 HIS A O   
1002 C CB  . HIS A 115 ? 0.3229 0.3859 0.4260 -0.0197 0.0578  -0.0641 116 HIS A CB  
1003 C CG  . HIS A 115 ? 0.3747 0.4554 0.4937 -0.0054 0.0482  -0.0629 116 HIS A CG  
1004 N ND1 . HIS A 115 ? 0.4060 0.5134 0.5486 0.0012  0.0486  -0.0739 116 HIS A ND1 
1005 C CD2 . HIS A 115 ? 0.4004 0.4759 0.5135 0.0028  0.0381  -0.0527 116 HIS A CD2 
1006 C CE1 . HIS A 115 ? 0.4001 0.5163 0.5489 0.0143  0.0372  -0.0690 116 HIS A CE1 
1007 N NE2 . HIS A 115 ? 0.4016 0.4982 0.5318 0.0148  0.0313  -0.0560 116 HIS A NE2 
1008 N N   . VAL A 116 ? 0.2801 0.2986 0.3482 -0.0385 0.0747  -0.0645 117 VAL A N   
1009 C CA  . VAL A 116 ? 0.2917 0.2935 0.3401 -0.0528 0.0828  -0.0667 117 VAL A CA  
1010 C C   . VAL A 116 ? 0.3527 0.3575 0.4086 -0.0544 0.0939  -0.0774 117 VAL A C   
1011 O O   . VAL A 116 ? 0.3292 0.3341 0.3792 -0.0674 0.1045  -0.0862 117 VAL A O   
1012 C CB  . VAL A 116 ? 0.3281 0.3066 0.3540 -0.0549 0.0766  -0.0561 117 VAL A CB  
1013 C CG1 . VAL A 116 ? 0.3390 0.2998 0.3425 -0.0685 0.0835  -0.0586 117 VAL A CG1 
1014 C CG2 . VAL A 116 ? 0.3207 0.2973 0.3404 -0.0542 0.0669  -0.0478 117 VAL A CG2 
1015 N N   . VAL A 117 ? 0.3047 0.3103 0.3723 -0.0418 0.0925  -0.0773 118 VAL A N   
1016 C CA  . VAL A 117 ? 0.3100 0.3187 0.3875 -0.0411 0.1030  -0.0884 118 VAL A CA  
1017 C C   . VAL A 117 ? 0.3672 0.4019 0.4660 -0.0435 0.1108  -0.1028 118 VAL A C   
1018 O O   . VAL A 117 ? 0.3618 0.3972 0.4581 -0.0552 0.1235  -0.1137 118 VAL A O   
1019 C CB  . VAL A 117 ? 0.3456 0.3490 0.4328 -0.0250 0.0994  -0.0858 118 VAL A CB  
1020 C CG1 . VAL A 117 ? 0.3539 0.3604 0.4531 -0.0231 0.1108  -0.0987 118 VAL A CG1 
1021 C CG2 . VAL A 117 ? 0.3414 0.3203 0.4074 -0.0263 0.0942  -0.0741 118 VAL A CG2 
1022 N N   A ASP A 118 ? 0.3342 0.3911 0.4542 -0.0326 0.1035  -0.1039 119 ASP A N   
1023 N N   B ASP A 118 ? 0.3235 0.3795 0.4407 -0.0348 0.1035  -0.1031 119 ASP A N   
1024 C CA  A ASP A 118 ? 0.3370 0.4245 0.4823 -0.0332 0.1092  -0.1190 119 ASP A CA  
1025 C CA  B ASP A 118 ? 0.3178 0.4036 0.4584 -0.0369 0.1091  -0.1176 119 ASP A CA  
1026 C C   A ASP A 118 ? 0.3959 0.4859 0.5311 -0.0549 0.1209  -0.1274 119 ASP A C   
1027 C C   B ASP A 118 ? 0.3551 0.4396 0.4823 -0.0591 0.1207  -0.1248 119 ASP A C   
1028 O O   A ASP A 118 ? 0.3996 0.5069 0.5497 -0.0614 0.1330  -0.1436 119 ASP A O   
1029 O O   B ASP A 118 ? 0.3439 0.4410 0.4815 -0.0672 0.1339  -0.1401 119 ASP A O   
1030 C CB  A ASP A 118 ? 0.3515 0.4607 0.5156 -0.0196 0.0966  -0.1166 119 ASP A CB  
1031 C CB  B ASP A 118 ? 0.3339 0.4404 0.4918 -0.0245 0.0966  -0.1147 119 ASP A CB  
1032 C CG  A ASP A 118 ? 0.5062 0.6208 0.6874 0.0032  0.0876  -0.1145 119 ASP A CG  
1033 C CG  B ASP A 118 ? 0.4925 0.6351 0.6796 -0.0238 0.1004  -0.1312 119 ASP A CG  
1034 O OD1 A ASP A 118 ? 0.5440 0.6613 0.7379 0.0098  0.0938  -0.1235 119 ASP A OD1 
1035 O OD1 B ASP A 118 ? 0.5151 0.6734 0.7239 -0.0170 0.1063  -0.1441 119 ASP A OD1 
1036 O OD2 A ASP A 118 ? 0.5764 0.6907 0.7566 0.0144  0.0745  -0.1041 119 ASP A OD2 
1037 O OD2 B ASP A 118 ? 0.5503 0.7066 0.7401 -0.0296 0.0973  -0.1324 119 ASP A OD2 
1038 N N   A THR A 119 ? 0.3500 0.4210 0.4590 -0.0662 0.1179  -0.1171 120 THR A N   
1039 N N   B THR A 119 ? 0.3069 0.3744 0.4098 -0.0693 0.1167  -0.1146 120 THR A N   
1040 C CA  A THR A 119 ? 0.3604 0.4254 0.4525 -0.0871 0.1282  -0.1224 120 THR A CA  
1041 C CA  B THR A 119 ? 0.3223 0.3822 0.4072 -0.0905 0.1277  -0.1201 120 THR A CA  
1042 C C   A THR A 119 ? 0.4049 0.4493 0.4754 -0.1005 0.1402  -0.1259 120 THR A C   
1043 C C   B THR A 119 ? 0.3818 0.4203 0.4446 -0.1033 0.1393  -0.1233 120 THR A C   
1044 O O   A THR A 119 ? 0.4106 0.4605 0.4796 -0.1158 0.1545  -0.1388 120 THR A O   
1045 O O   B THR A 119 ? 0.3799 0.4171 0.4332 -0.1208 0.1526  -0.1331 120 THR A O   
1046 C CB  A THR A 119 ? 0.4590 0.5086 0.5308 -0.0913 0.1194  -0.1098 120 THR A CB  
1047 C CB  B THR A 119 ? 0.3475 0.3924 0.4117 -0.0965 0.1202  -0.1088 120 THR A CB  
1048 O OG1 A THR A 119 ? 0.4322 0.5036 0.5260 -0.0785 0.1093  -0.1084 120 THR A OG1 
1049 O OG1 B THR A 119 ? 0.3708 0.4134 0.4235 -0.1159 0.1319  -0.1173 120 THR A OG1 
1050 C CG2 A THR A 119 ? 0.4709 0.5117 0.5240 -0.1119 0.1293  -0.1147 120 THR A CG2 
1051 C CG2 B THR A 119 ? 0.2764 0.2891 0.3112 -0.0964 0.1128  -0.0938 120 THR A CG2 
1052 N N   . CYS A 120 ? 0.3547 0.3755 0.4073 -0.0962 0.1350  -0.1154 121 CYS A N   
1053 C CA  . CYS A 120 ? 0.3746 0.3753 0.4052 -0.1081 0.1450  -0.1185 121 CYS A CA  
1054 C C   . CYS A 120 ? 0.4451 0.4648 0.4972 -0.1099 0.1594  -0.1364 121 CYS A C   
1055 O O   . CYS A 120 ? 0.4397 0.4540 0.4783 -0.1274 0.1739  -0.1463 121 CYS A O   
1056 C CB  . CYS A 120 ? 0.3705 0.3518 0.3887 -0.0996 0.1363  -0.1073 121 CYS A CB  
1057 S SG  . CYS A 120 ? 0.4187 0.3749 0.4063 -0.1020 0.1222  -0.0895 121 CYS A SG  
1058 N N   . ARG A 121 ? 0.4101 0.4519 0.4954 -0.0916 0.1555  -0.1411 122 ARG A N   
1059 C CA  . ARG A 121 ? 0.4165 0.4809 0.5296 -0.0884 0.1671  -0.1594 122 ARG A CA  
1060 C C   . ARG A 121 ? 0.4615 0.5482 0.5851 -0.1034 0.1798  -0.1754 122 ARG A C   
1061 O O   . ARG A 121 ? 0.4600 0.5515 0.5854 -0.1156 0.1963  -0.1909 122 ARG A O   
1062 C CB  . ARG A 121 ? 0.4185 0.5024 0.5642 -0.0635 0.1566  -0.1595 122 ARG A CB  
1063 C CG  . ARG A 121 ? 0.6252 0.6882 0.7645 -0.0505 0.1508  -0.1503 122 ARG A CG  
1064 C CD  . ARG A 121 ? 0.8010 0.8803 0.9716 -0.0316 0.1516  -0.1606 122 ARG A CD  
1065 N NE  . ARG A 121 ? 0.9048 0.9822 1.0836 -0.0102 0.1354  -0.1485 122 ARG A NE  
1066 C CZ  . ARG A 121 ? 1.0299 1.0818 1.1957 -0.0012 0.1298  -0.1372 122 ARG A CZ  
1067 N NH1 . ARG A 121 ? 0.8124 0.8408 0.9584 -0.0112 0.1382  -0.1369 122 ARG A NH1 
1068 N NH2 . ARG A 121 ? 0.8673 0.9163 1.0381 0.0167  0.1161  -0.1266 122 ARG A NH2 
1069 N N   . LYS A 122 ? 0.4211 0.5205 0.5504 -0.1041 0.1731  -0.1725 123 LYS A N   
1070 C CA  . LYS A 122 ? 0.4277 0.5487 0.5670 -0.1195 0.1845  -0.1876 123 LYS A CA  
1071 C C   . LYS A 122 ? 0.4938 0.5888 0.5960 -0.1462 0.1988  -0.1889 123 LYS A C   
1072 O O   . LYS A 122 ? 0.4858 0.5939 0.5941 -0.1619 0.2162  -0.2068 123 LYS A O   
1073 C CB  . LYS A 122 ? 0.4386 0.5756 0.5893 -0.1139 0.1727  -0.1826 123 LYS A CB  
1074 C CG  . LYS A 122 ? 0.6369 0.8051 0.8257 -0.0894 0.1603  -0.1854 123 LYS A CG  
1075 C CD  . LYS A 122 ? 0.7683 0.9565 0.9690 -0.0871 0.1508  -0.1843 123 LYS A CD  
1076 C CE  . LYS A 122 ? 0.8856 1.0907 1.1094 -0.0612 0.1328  -0.1781 123 LYS A CE  
1077 N NZ  . LYS A 122 ? 0.9736 1.2096 1.2342 -0.0456 0.1335  -0.1934 123 LYS A NZ  
1078 N N   . PHE A 123 ? 0.4648 0.5230 0.5282 -0.1512 0.1915  -0.1707 124 PHE A N   
1079 C CA  . PHE A 123 ? 0.4921 0.5192 0.5139 -0.1747 0.2022  -0.1691 124 PHE A CA  
1080 C C   . PHE A 123 ? 0.5533 0.5712 0.5644 -0.1842 0.2165  -0.1787 124 PHE A C   
1081 O O   . PHE A 123 ? 0.5580 0.5671 0.5498 -0.2063 0.2333  -0.1889 124 PHE A O   
1082 C CB  . PHE A 123 ? 0.5179 0.5103 0.5043 -0.1733 0.1878  -0.1476 124 PHE A CB  
1083 C CG  . PHE A 123 ? 0.5409 0.5298 0.5201 -0.1767 0.1813  -0.1409 124 PHE A CG  
1084 C CD1 . PHE A 123 ? 0.5559 0.5761 0.5691 -0.1661 0.1756  -0.1450 124 PHE A CD1 
1085 C CD2 . PHE A 123 ? 0.5971 0.5499 0.5345 -0.1888 0.1795  -0.1298 124 PHE A CD2 
1086 C CE1 . PHE A 123 ? 0.5604 0.5767 0.5665 -0.1698 0.1702  -0.1395 124 PHE A CE1 
1087 C CE2 . PHE A 123 ? 0.6211 0.5681 0.5517 -0.1911 0.1738  -0.1239 124 PHE A CE2 
1088 C CZ  . PHE A 123 ? 0.5673 0.5465 0.5326 -0.1824 0.1699  -0.1292 124 PHE A CZ  
1089 N N   . ILE A 124 ? 0.4894 0.5093 0.5131 -0.1687 0.2113  -0.1768 125 ILE A N   
1090 C CA  . ILE A 124 ? 0.5135 0.5266 0.5304 -0.1764 0.2252  -0.1875 125 ILE A CA  
1091 C C   . ILE A 124 ? 0.5813 0.6269 0.6297 -0.1826 0.2434  -0.2120 125 ILE A C   
1092 O O   . ILE A 124 ? 0.5988 0.6369 0.6307 -0.2027 0.2616  -0.2243 125 ILE A O   
1093 C CB  . ILE A 124 ? 0.5405 0.5451 0.5619 -0.1586 0.2151  -0.1793 125 ILE A CB  
1094 C CG1 . ILE A 124 ? 0.5456 0.5166 0.5297 -0.1595 0.2015  -0.1589 125 ILE A CG1 
1095 C CG2 . ILE A 124 ? 0.5775 0.5821 0.6018 -0.1638 0.2305  -0.1941 125 ILE A CG2 
1096 C CD1 . ILE A 124 ? 0.6224 0.5888 0.6150 -0.1403 0.1878  -0.1484 125 ILE A CD1 
1097 N N   . LYS A 125 ? 0.5341 0.6163 0.6271 -0.1660 0.2383  -0.2199 126 LYS A N   
1098 C CA  . LYS A 125 ? 0.5401 0.6608 0.6713 -0.1679 0.2528  -0.2449 126 LYS A CA  
1099 C C   . LYS A 125 ? 0.6095 0.7354 0.7294 -0.1953 0.2702  -0.2579 126 LYS A C   
1100 O O   . LYS A 125 ? 0.6074 0.7503 0.7397 -0.2084 0.2899  -0.2797 126 LYS A O   
1101 C CB  . LYS A 125 ? 0.5535 0.7104 0.7309 -0.1426 0.2391  -0.2477 126 LYS A CB  
1102 C CG  . LYS A 125 ? 0.7580 0.9565 0.9813 -0.1362 0.2501  -0.2735 126 LYS A CG  
1103 C CD  . LYS A 125 ? 0.8879 1.1239 1.1531 -0.1142 0.2356  -0.2770 126 LYS A CD  
1104 C CE  . LYS A 125 ? 1.0319 1.3135 1.3449 -0.1083 0.2458  -0.3049 126 LYS A CE  
1105 N NZ  . LYS A 125 ? 1.1345 1.4548 1.4862 -0.0887 0.2307  -0.3092 126 LYS A NZ  
1106 N N   . ALA A 126 ? 0.5639 0.6728 0.6583 -0.2048 0.2640  -0.2451 127 ALA A N   
1107 C CA  . ALA A 126 ? 0.5893 0.6952 0.6661 -0.2321 0.2800  -0.2549 127 ALA A CA  
1108 C C   . ALA A 126 ? 0.6850 0.7570 0.7177 -0.2576 0.2981  -0.2579 127 ALA A C   
1109 O O   . ALA A 126 ? 0.6921 0.7693 0.7189 -0.2815 0.3186  -0.2747 127 ALA A O   
1110 C CB  . ALA A 126 ? 0.5890 0.6782 0.6455 -0.2337 0.2674  -0.2382 127 ALA A CB  
1111 N N   . SER A 127 ? 0.6828 0.7203 0.6836 -0.2537 0.2908  -0.2424 128 SER A N   
1112 C CA  . SER A 127 ? 0.7453 0.7473 0.6996 -0.2759 0.3046  -0.2427 128 SER A CA  
1113 C C   . SER A 127 ? 0.8346 0.8519 0.8046 -0.2811 0.3227  -0.2632 128 SER A C   
1114 O O   . SER A 127 ? 0.8846 0.8793 0.8195 -0.3047 0.3398  -0.2697 128 SER A O   
1115 C CB  . SER A 127 ? 0.8194 0.7796 0.7324 -0.2697 0.2875  -0.2180 128 SER A CB  
1116 O OG  . SER A 127 ? 0.9845 0.9182 0.8649 -0.2765 0.2788  -0.2025 128 SER A OG  
1117 N N   . GLU A 128 ? 0.7570 0.8108 0.7778 -0.2593 0.3194  -0.2736 129 GLU A N   
1118 C CA  . GLU A 128 ? 1.0272 1.0976 1.0685 -0.2607 0.3357  -0.2942 129 GLU A CA  
1119 C C   . GLU A 128 ? 1.5454 1.6486 1.6111 -0.2786 0.3596  -0.3228 129 GLU A C   
1120 O O   . GLU A 128 ? 1.1514 1.2395 1.1859 -0.3064 0.3747  -0.3274 129 GLU A O   
1121 C CB  . GLU A 128 ? 1.0129 1.1035 1.0950 -0.2292 0.3222  -0.2934 129 GLU A CB  
1122 C CG  . GLU A 128 ? 1.1028 1.2416 1.2429 -0.2105 0.3182  -0.3068 129 GLU A CG  
1123 C CD  . GLU A 128 ? 1.3430 1.4952 1.5173 -0.1775 0.3014  -0.3018 129 GLU A CD  
1124 O OE1 . GLU A 128 ? 1.2430 1.3656 1.3959 -0.1677 0.2900  -0.2841 129 GLU A OE1 
1125 O OE2 . GLU A 128 ? 1.2506 1.4426 1.4725 -0.1615 0.2993  -0.3159 129 GLU A OE2 
1129 N N   A TRP B 2   ? 0.1929 0.4211 0.3070 -0.0549 -0.0112 -0.0777 1   TRP D N   
1130 N N   B TRP B 2   ? 0.1987 0.4268 0.3127 -0.0549 -0.0113 -0.0777 1   TRP D N   
1131 C CA  A TRP B 2   ? 0.1864 0.4151 0.3016 -0.0550 -0.0098 -0.0785 1   TRP D CA  
1132 C CA  B TRP B 2   ? 0.1912 0.4198 0.3064 -0.0550 -0.0099 -0.0784 1   TRP D CA  
1133 C C   A TRP B 2   ? 0.2330 0.4611 0.3507 -0.0553 -0.0095 -0.0768 1   TRP D C   
1134 C C   B TRP B 2   ? 0.2295 0.4576 0.3472 -0.0553 -0.0094 -0.0768 1   TRP D C   
1135 O O   A TRP B 2   ? 0.2438 0.4713 0.3629 -0.0552 -0.0104 -0.0760 1   TRP D O   
1136 O O   B TRP B 2   ? 0.2262 0.4537 0.3451 -0.0554 -0.0102 -0.0759 1   TRP D O   
1137 C CB  A TRP B 2   ? 0.1676 0.3965 0.2826 -0.0550 -0.0117 -0.0805 1   TRP D CB  
1138 C CB  B TRP B 2   ? 0.1743 0.4031 0.2895 -0.0550 -0.0117 -0.0803 1   TRP D CB  
1139 C CG  A TRP B 2   ? 0.1683 0.3976 0.2809 -0.0551 -0.0120 -0.0846 1   TRP D CG  
1140 C CG  B TRP B 2   ? 0.1834 0.4134 0.3023 -0.0549 -0.0138 -0.0793 1   TRP D CG  
1141 C CD1 A TRP B 2   ? 0.2006 0.4300 0.3133 -0.0545 -0.0147 -0.0869 1   TRP D CD1 
1142 C CD1 B TRP B 2   ? 0.2209 0.4523 0.3431 -0.0547 -0.0164 -0.0800 1   TRP D CD1 
1143 C CD2 A TRP B 2   ? 0.1657 0.3952 0.2758 -0.0556 -0.0094 -0.0879 1   TRP D CD2 
1144 C CD2 B TRP B 2   ? 0.1786 0.4094 0.2996 -0.0545 -0.0135 -0.0782 1   TRP D CD2 
1145 N NE1 A TRP B 2   ? 0.1924 0.4223 0.3026 -0.0543 -0.0141 -0.0924 1   TRP D NE1 
1146 N NE1 B TRP B 2   ? 0.2121 0.4463 0.3395 -0.0542 -0.0169 -0.0795 1   TRP D NE1 
1147 C CE2 A TRP B 2   ? 0.2072 0.4374 0.3157 -0.0553 -0.0104 -0.0934 1   TRP D CE2 
1148 C CE2 B TRP B 2   ? 0.2269 0.4609 0.3531 -0.0539 -0.0151 -0.0786 1   TRP D CE2 
1149 C CE3 A TRP B 2   ? 0.1748 0.4034 0.2839 -0.0564 -0.0064 -0.0872 1   TRP D CE3 
1150 C CE3 B TRP B 2   ? 0.1923 0.4214 0.3120 -0.0542 -0.0123 -0.0772 1   TRP D CE3 
1151 C CZ2 A TRP B 2   ? 0.1943 0.4247 0.3000 -0.0558 -0.0077 -0.0990 1   TRP D CZ2 
1152 C CZ2 B TRP B 2   ? 0.2140 0.4507 0.3439 -0.0527 -0.0148 -0.0786 1   TRP D CZ2 
1153 C CZ3 A TRP B 2   ? 0.1845 0.4128 0.2907 -0.0572 -0.0038 -0.0915 1   TRP D CZ3 
1154 C CZ3 B TRP B 2   ? 0.2126 0.4428 0.3347 -0.0530 -0.0129 -0.0769 1   TRP D CZ3 
1155 C CH2 A TRP B 2   ? 0.1963 0.4258 0.3008 -0.0569 -0.0039 -0.0978 1   TRP D CH2 
1156 C CH2 B TRP B 2   ? 0.2153 0.4497 0.3423 -0.0521 -0.0138 -0.0778 1   TRP D CH2 
1157 N N   . VAL B 3   ? 0.1770 0.4051 0.2959 -0.0554 -0.0082 -0.0771 2   VAL D N   
1158 C CA  . VAL B 3   ? 0.1745 0.4018 0.2962 -0.0554 -0.0086 -0.0773 2   VAL D CA  
1159 C C   . VAL B 3   ? 0.1960 0.4213 0.3177 -0.0546 -0.0094 -0.0771 2   VAL D C   
1160 O O   . VAL B 3   ? 0.1897 0.4143 0.3092 -0.0549 -0.0087 -0.0767 2   VAL D O   
1161 C CB  . VAL B 3   ? 0.2148 0.4447 0.3397 -0.0573 -0.0073 -0.0788 2   VAL D CB  
1162 C CG1 . VAL B 3   ? 0.2077 0.4389 0.3308 -0.0589 -0.0066 -0.0783 2   VAL D CG1 
1163 C CG2 . VAL B 3   ? 0.2107 0.4437 0.3386 -0.0579 -0.0059 -0.0798 2   VAL D CG2 
1164 N N   . ILE B 4   ? 0.1681 0.3920 0.2921 -0.0537 -0.0107 -0.0779 3   ILE D N   
1165 C CA  . ILE B 4   ? 0.1803 0.4010 0.3042 -0.0527 -0.0124 -0.0775 3   ILE D CA  
1166 C C   . ILE B 4   ? 0.2242 0.4458 0.3532 -0.0540 -0.0122 -0.0794 3   ILE D C   
1167 O O   . ILE B 4   ? 0.2290 0.4526 0.3625 -0.0547 -0.0127 -0.0826 3   ILE D O   
1168 C CB  . ILE B 4   ? 0.2088 0.4280 0.3335 -0.0504 -0.0146 -0.0787 3   ILE D CB  
1169 C CG1 . ILE B 4   ? 0.1895 0.4114 0.3127 -0.0493 -0.0143 -0.0779 3   ILE D CG1 
1170 C CG2 . ILE B 4   ? 0.2371 0.4518 0.3612 -0.0492 -0.0174 -0.0781 3   ILE D CG2 
1171 C CD1 . ILE B 4   ? 0.2354 0.4581 0.3545 -0.0505 -0.0146 -0.0752 3   ILE D CD1 
1172 N N   . PRO B 5   ? 0.2121 0.4336 0.3418 -0.0547 -0.0112 -0.0783 4   PRO D N   
1173 C CA  . PRO B 5   ? 0.2141 0.4392 0.3519 -0.0560 -0.0109 -0.0808 4   PRO D CA  
1174 C C   . PRO B 5   ? 0.2690 0.4914 0.4121 -0.0554 -0.0149 -0.0831 4   PRO D C   
1175 O O   . PRO B 5   ? 0.2619 0.4778 0.4009 -0.0535 -0.0177 -0.0811 4   PRO D O   
1176 C CB  . PRO B 5   ? 0.2342 0.4594 0.3716 -0.0562 -0.0083 -0.0794 4   PRO D CB  
1177 C CG  . PRO B 5   ? 0.2892 0.5076 0.4174 -0.0555 -0.0092 -0.0761 4   PRO D CG  
1178 C CD  . PRO B 5   ? 0.2300 0.4489 0.3541 -0.0548 -0.0101 -0.0759 4   PRO D CD  
1179 N N   . ALA B 6   ? 0.2309 0.4590 0.3841 -0.0573 -0.0155 -0.0876 5   ALA D N   
# 
