data_7GUL
# 
_entry.id   7GUL 
# 
_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   7GUL         pdb_00007gul 10.2210/pdb7gul/pdb 
WWPDB D_1001406656 ?            ?                   
# 
_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                        7GUL 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-09 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              Rob.vanMontfort@icr.ac.uk 
_pdbx_contact_author.name_first         Rob 
_pdbx_contact_author.name_last          'van Montfort' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rodrigues, M.J.'      1 0000-0003-1243-903X 
'Le Bihan, Y.V.'       2 0000-0002-6850-9706 
'van Montfort, R.L.M.' 3 0000-0002-5688-3450 
# 
_citation.id                        primary 
_citation.title                     
'Specific radiation damage to halogenated inhibitors and ligands in protein-ligand crystal structures.' 
_citation.journal_abbrev            J.Appl.Crystallogr. 
_citation.journal_volume            57 
_citation.page_first                1951 
_citation.page_last                 1965 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39628887 
_citation.pdbx_database_id_DOI      10.1107/S1600576724010549 
_citation.journal_id_ASTM           JACGAR 
_citation.country                   DK 
_citation.journal_id_ISSN           0021-8898 
_citation.journal_id_CSD            0228 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rodrigues, M.J.'      1 0000-0003-1243-903X 
primary 'Cabry, M.'            2 0000-0002-9070-5498 
primary 'Collie, G.'           3 0000-0002-0406-922X 
primary 'Carter, M.'           4 ?                   
primary 'McAndrew, C.'         5 0000-0002-1366-088X 
primary 'Owen, R.L.'           6 0000-0002-2104-7057 
primary 'Bellenie, B.R.'       7 0000-0001-9987-3079 
primary 'Le Bihan, Y.V.'       8 0000-0002-6850-9706 
primary 'van Montfort, R.L.M.' 9 0000-0002-5688-3450 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'B-cell lymphoma 6 protein'                                   14536.915 1   ? ? ? ? 
2 polymer     syn 'WVIP tetrapeptide'                                           610.744   1   ? ? ? ? 
3 non-polymer syn '5-[(5-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' 260.679   1   ? ? ? ? 
4 non-polymer nat 'CHLORIDE ION'                                                35.453    1   ? ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                          78.133    1   ? ? ? ? 
6 water       nat water                                                         18.015    181 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'BCL-6,B-cell lymphoma 5 protein,BCL-5,Protein LAZ-3,Zinc finger and BTB domain-containing protein 27,Zinc finger protein 51' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
A ? 
2 'polypeptide(L)' no yes '(ACE)WVIPA' XWVIPA D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '5-[(5-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' 7ZO 
4 'CHLORIDE ION'                                                CL  
5 'DIMETHYL SULFOXIDE'                                          DMS 
6 water                                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   ALA n 
1 5   ASP n 
1 6   SER n 
1 7   CYS n 
1 8   ILE n 
1 9   GLN n 
1 10  PHE n 
1 11  THR n 
1 12  ARG n 
1 13  HIS n 
1 14  ALA n 
1 15  SER n 
1 16  ASP n 
1 17  VAL n 
1 18  LEU n 
1 19  LEU n 
1 20  ASN n 
1 21  LEU n 
1 22  ASN n 
1 23  ARG n 
1 24  LEU n 
1 25  ARG n 
1 26  SER n 
1 27  ARG n 
1 28  ASP n 
1 29  ILE n 
1 30  LEU n 
1 31  THR n 
1 32  ASP n 
1 33  VAL n 
1 34  VAL n 
1 35  ILE n 
1 36  VAL n 
1 37  VAL n 
1 38  SER n 
1 39  ARG n 
1 40  GLU n 
1 41  GLN n 
1 42  PHE n 
1 43  ARG n 
1 44  ALA n 
1 45  HIS n 
1 46  LYS n 
1 47  THR n 
1 48  VAL n 
1 49  LEU n 
1 50  MET n 
1 51  ALA n 
1 52  CYS n 
1 53  SER n 
1 54  GLY n 
1 55  LEU n 
1 56  PHE n 
1 57  TYR n 
1 58  SER n 
1 59  ILE n 
1 60  PHE n 
1 61  THR n 
1 62  ASP n 
1 63  GLN n 
1 64  LEU n 
1 65  LYS n 
1 66  CYS n 
1 67  ASN n 
1 68  LEU n 
1 69  SER n 
1 70  VAL n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ASP n 
1 75  PRO n 
1 76  GLU n 
1 77  ILE n 
1 78  ASN n 
1 79  PRO n 
1 80  GLU n 
1 81  GLY n 
1 82  PHE n 
1 83  CYS n 
1 84  ILE n 
1 85  LEU n 
1 86  LEU n 
1 87  ASP n 
1 88  PHE n 
1 89  MET n 
1 90  TYR n 
1 91  THR n 
1 92  SER n 
1 93  ARG n 
1 94  LEU n 
1 95  ASN n 
1 96  LEU n 
1 97  ARG n 
1 98  GLU n 
1 99  GLY n 
1 100 ASN n 
1 101 ILE n 
1 102 MET n 
1 103 ALA n 
1 104 VAL n 
1 105 MET n 
1 106 ALA n 
1 107 THR n 
1 108 ALA n 
1 109 MET n 
1 110 TYR n 
1 111 LEU n 
1 112 GLN n 
1 113 MET n 
1 114 GLU n 
1 115 HIS n 
1 116 VAL n 
1 117 VAL n 
1 118 ASP n 
1 119 THR n 
1 120 CYS n 
1 121 ARG n 
1 122 LYS n 
1 123 PHE n 
1 124 ILE n 
1 125 LYS n 
1 126 ALA n 
1 127 SER n 
1 128 GLU n 
2 1   ACE n 
2 2   TRP n 
2 3   VAL n 
2 4   ILE n 
2 5   PRO n 
2 6   ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   128 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'BCL6, BCL5, LAZ3, ZBTB27, ZNF51' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               BL21-AI 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               pET48b 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1 6 'synthetic construct' ? 32630 ? 
3 2 sample ? ? 'synthetic construct' ? 32630 ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
7ZO non-polymer         . '5-[(5-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' ? 'C12 H9 Cl N4 O' 260.679 
ACE non-polymer         . 'ACETYL GROUP'                                                ? 'C2 H4 O'        44.053  
ALA 'L-peptide linking' y ALANINE                                                       ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                      ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                    ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                               ? 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'                                                ? 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE                                                      ? 'C3 H7 N O2 S'   121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                          ? 'C2 H6 O S'      78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                     ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                               ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                       ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                                     ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                         ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                    ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                       ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                        ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                    ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                 ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                                       ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                        ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                                     ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                    ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                      ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                        ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   2   ?   ?   ?   A . n 
A 1 2   PRO 2   3   ?   ?   ?   A . n 
A 1 3   GLY 3   4   ?   ?   ?   A . n 
A 1 4   ALA 4   5   ?   ?   ?   A . n 
A 1 5   ASP 5   6   6   ASP ASP A . n 
A 1 6   SER 6   7   7   SER SER A . n 
A 1 7   CYS 7   8   8   CYS CYS A . n 
A 1 8   ILE 8   9   9   ILE ILE A . n 
A 1 9   GLN 9   10  10  GLN GLN A . n 
A 1 10  PHE 10  11  11  PHE PHE A . n 
A 1 11  THR 11  12  12  THR THR A . n 
A 1 12  ARG 12  13  13  ARG ARG A . n 
A 1 13  HIS 13  14  14  HIS HIS A . n 
A 1 14  ALA 14  15  15  ALA ALA A . n 
A 1 15  SER 15  16  16  SER SER A . n 
A 1 16  ASP 16  17  17  ASP ASP A . n 
A 1 17  VAL 17  18  18  VAL VAL A . n 
A 1 18  LEU 18  19  19  LEU LEU A . n 
A 1 19  LEU 19  20  20  LEU LEU A . n 
A 1 20  ASN 20  21  21  ASN ASN A . n 
A 1 21  LEU 21  22  22  LEU LEU A . n 
A 1 22  ASN 22  23  23  ASN ASN A . n 
A 1 23  ARG 23  24  24  ARG ARG A . n 
A 1 24  LEU 24  25  25  LEU LEU A . n 
A 1 25  ARG 25  26  26  ARG ARG A . n 
A 1 26  SER 26  27  27  SER SER A . n 
A 1 27  ARG 27  28  28  ARG ARG A . n 
A 1 28  ASP 28  29  29  ASP ASP A . n 
A 1 29  ILE 29  30  30  ILE ILE A . n 
A 1 30  LEU 30  31  31  LEU LEU A . n 
A 1 31  THR 31  32  32  THR THR A . n 
A 1 32  ASP 32  33  33  ASP ASP A . n 
A 1 33  VAL 33  34  34  VAL VAL A . n 
A 1 34  VAL 34  35  35  VAL VAL A . n 
A 1 35  ILE 35  36  36  ILE ILE A . n 
A 1 36  VAL 36  37  37  VAL VAL A . n 
A 1 37  VAL 37  38  38  VAL VAL A . n 
A 1 38  SER 38  39  39  SER SER A . n 
A 1 39  ARG 39  40  40  ARG ARG A . n 
A 1 40  GLU 40  41  41  GLU GLU A . n 
A 1 41  GLN 41  42  42  GLN GLN A . n 
A 1 42  PHE 42  43  43  PHE PHE A . n 
A 1 43  ARG 43  44  44  ARG ARG A . n 
A 1 44  ALA 44  45  45  ALA ALA A . n 
A 1 45  HIS 45  46  46  HIS HIS A . n 
A 1 46  LYS 46  47  47  LYS LYS A . n 
A 1 47  THR 47  48  48  THR THR A . n 
A 1 48  VAL 48  49  49  VAL VAL A . n 
A 1 49  LEU 49  50  50  LEU LEU A . n 
A 1 50  MET 50  51  51  MET MET A . n 
A 1 51  ALA 51  52  52  ALA ALA A . n 
A 1 52  CYS 52  53  53  CYS CYS A . n 
A 1 53  SER 53  54  54  SER SER A . n 
A 1 54  GLY 54  55  55  GLY GLY A . n 
A 1 55  LEU 55  56  56  LEU LEU A . n 
A 1 56  PHE 56  57  57  PHE PHE A . n 
A 1 57  TYR 57  58  58  TYR TYR A . n 
A 1 58  SER 58  59  59  SER SER A . n 
A 1 59  ILE 59  60  60  ILE ILE A . n 
A 1 60  PHE 60  61  61  PHE PHE A . n 
A 1 61  THR 61  62  62  THR THR A . n 
A 1 62  ASP 62  63  63  ASP ASP A . n 
A 1 63  GLN 63  64  64  GLN GLN A . n 
A 1 64  LEU 64  65  65  LEU LEU A . n 
A 1 65  LYS 65  66  66  LYS LYS A . n 
A 1 66  CYS 66  67  67  CYS CYS A . n 
A 1 67  ASN 67  68  68  ASN ASN A . n 
A 1 68  LEU 68  69  69  LEU LEU A . n 
A 1 69  SER 69  70  70  SER SER A . n 
A 1 70  VAL 70  71  71  VAL VAL A . n 
A 1 71  ILE 71  72  72  ILE ILE A . n 
A 1 72  ASN 72  73  73  ASN ASN A . n 
A 1 73  LEU 73  74  74  LEU LEU A . n 
A 1 74  ASP 74  75  75  ASP ASP A . n 
A 1 75  PRO 75  76  76  PRO PRO A . n 
A 1 76  GLU 76  77  77  GLU GLU A . n 
A 1 77  ILE 77  78  78  ILE ILE A . n 
A 1 78  ASN 78  79  79  ASN ASN A . n 
A 1 79  PRO 79  80  80  PRO PRO A . n 
A 1 80  GLU 80  81  81  GLU GLU A . n 
A 1 81  GLY 81  82  82  GLY GLY A . n 
A 1 82  PHE 82  83  83  PHE PHE A . n 
A 1 83  CYS 83  84  84  CYS CYS A . n 
A 1 84  ILE 84  85  85  ILE ILE A . n 
A 1 85  LEU 85  86  86  LEU LEU A . n 
A 1 86  LEU 86  87  87  LEU LEU A . n 
A 1 87  ASP 87  88  88  ASP ASP A . n 
A 1 88  PHE 88  89  89  PHE PHE A . n 
A 1 89  MET 89  90  90  MET MET A . n 
A 1 90  TYR 90  91  91  TYR TYR A . n 
A 1 91  THR 91  92  92  THR THR A . n 
A 1 92  SER 92  93  93  SER SER A . n 
A 1 93  ARG 93  94  94  ARG ARG A . n 
A 1 94  LEU 94  95  95  LEU LEU A . n 
A 1 95  ASN 95  96  96  ASN ASN A . n 
A 1 96  LEU 96  97  97  LEU LEU A . n 
A 1 97  ARG 97  98  98  ARG ARG A . n 
A 1 98  GLU 98  99  99  GLU GLU A . n 
A 1 99  GLY 99  100 100 GLY GLY A . n 
A 1 100 ASN 100 101 101 ASN ASN A . n 
A 1 101 ILE 101 102 102 ILE ILE A . n 
A 1 102 MET 102 103 103 MET MET A . n 
A 1 103 ALA 103 104 104 ALA ALA A . n 
A 1 104 VAL 104 105 105 VAL VAL A . n 
A 1 105 MET 105 106 106 MET MET A . n 
A 1 106 ALA 106 107 107 ALA ALA A . n 
A 1 107 THR 107 108 108 THR THR A . n 
A 1 108 ALA 108 109 109 ALA ALA A . n 
A 1 109 MET 109 110 110 MET MET A . n 
A 1 110 TYR 110 111 111 TYR TYR A . n 
A 1 111 LEU 111 112 112 LEU LEU A . n 
A 1 112 GLN 112 113 113 GLN GLN A . n 
A 1 113 MET 113 114 114 MET MET A . n 
A 1 114 GLU 114 115 115 GLU GLU A . n 
A 1 115 HIS 115 116 116 HIS HIS A . n 
A 1 116 VAL 116 117 117 VAL VAL A . n 
A 1 117 VAL 117 118 118 VAL VAL A . n 
A 1 118 ASP 118 119 119 ASP ASP A . n 
A 1 119 THR 119 120 120 THR THR A . n 
A 1 120 CYS 120 121 121 CYS CYS A . n 
A 1 121 ARG 121 122 122 ARG ARG A . n 
A 1 122 LYS 122 123 123 LYS LYS A . n 
A 1 123 PHE 123 124 124 PHE PHE A . n 
A 1 124 ILE 124 125 125 ILE ILE A . n 
A 1 125 LYS 125 126 126 LYS LYS A . n 
A 1 126 ALA 126 127 127 ALA ALA A . n 
A 1 127 SER 127 128 128 SER SER A . n 
A 1 128 GLU 128 129 129 GLU GLU A . n 
B 2 1   ACE 1   0   0   ACE ACE D . n 
B 2 2   TRP 2   1   1   TRP TRP D . n 
B 2 3   VAL 3   2   2   VAL VAL D . n 
B 2 4   ILE 4   3   3   ILE ILE D . n 
B 2 5   PRO 5   4   4   PRO PRO D . n 
B 2 6   ALA 6   5   5   ALA ALA D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 7ZO 1   201 1   7ZO 375 A . 
D 4 CL  1   202 1   CL  CL  A . 
E 5 DMS 1   101 1   DMS DMS D . 
F 6 HOH 1   301 42  HOH HOH A . 
F 6 HOH 2   302 81  HOH HOH A . 
F 6 HOH 3   303 88  HOH HOH A . 
F 6 HOH 4   304 15  HOH HOH A . 
F 6 HOH 5   305 32  HOH HOH A . 
F 6 HOH 6   306 84  HOH HOH A . 
F 6 HOH 7   307 166 HOH HOH A . 
F 6 HOH 8   308 92  HOH HOH A . 
F 6 HOH 9   309 33  HOH HOH A . 
F 6 HOH 10  310 130 HOH HOH A . 
F 6 HOH 11  311 159 HOH HOH A . 
F 6 HOH 12  312 230 HOH HOH A . 
F 6 HOH 13  313 114 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 23  HOH HOH A . 
F 6 HOH 18  318 143 HOH HOH A . 
F 6 HOH 19  319 87  HOH HOH A . 
F 6 HOH 20  320 5   HOH HOH A . 
F 6 HOH 21  321 85  HOH HOH A . 
F 6 HOH 22  322 83  HOH HOH A . 
F 6 HOH 23  323 14  HOH HOH A . 
F 6 HOH 24  324 103 HOH HOH A . 
F 6 HOH 25  325 196 HOH HOH A . 
F 6 HOH 26  326 187 HOH HOH A . 
F 6 HOH 27  327 97  HOH HOH A . 
F 6 HOH 28  328 24  HOH HOH A . 
F 6 HOH 29  329 135 HOH HOH A . 
F 6 HOH 30  330 113 HOH HOH A . 
F 6 HOH 31  331 35  HOH HOH A . 
F 6 HOH 32  332 165 HOH HOH A . 
F 6 HOH 33  333 105 HOH HOH A . 
F 6 HOH 34  334 134 HOH HOH A . 
F 6 HOH 35  335 213 HOH HOH A . 
F 6 HOH 36  336 141 HOH HOH A . 
F 6 HOH 37  337 50  HOH HOH A . 
F 6 HOH 38  338 94  HOH HOH A . 
F 6 HOH 39  339 13  HOH HOH A . 
F 6 HOH 40  340 112 HOH HOH A . 
F 6 HOH 41  341 90  HOH HOH A . 
F 6 HOH 42  342 184 HOH HOH A . 
F 6 HOH 43  343 49  HOH HOH A . 
F 6 HOH 44  344 136 HOH HOH A . 
F 6 HOH 45  345 110 HOH HOH A . 
F 6 HOH 46  346 117 HOH HOH A . 
F 6 HOH 47  347 51  HOH HOH A . 
F 6 HOH 48  348 151 HOH HOH A . 
F 6 HOH 49  349 100 HOH HOH A . 
F 6 HOH 50  350 109 HOH HOH A . 
F 6 HOH 51  351 3   HOH HOH A . 
F 6 HOH 52  352 86  HOH HOH A . 
F 6 HOH 53  353 26  HOH HOH A . 
F 6 HOH 54  354 116 HOH HOH A . 
F 6 HOH 55  355 102 HOH HOH A . 
F 6 HOH 56  356 18  HOH HOH A . 
F 6 HOH 57  357 115 HOH HOH A . 
F 6 HOH 58  358 74  HOH HOH A . 
F 6 HOH 59  359 180 HOH HOH A . 
F 6 HOH 60  360 6   HOH HOH A . 
F 6 HOH 61  361 11  HOH HOH A . 
F 6 HOH 62  362 121 HOH HOH A . 
F 6 HOH 63  363 168 HOH HOH A . 
F 6 HOH 64  364 150 HOH HOH A . 
F 6 HOH 65  365 231 HOH HOH A . 
F 6 HOH 66  366 101 HOH HOH A . 
F 6 HOH 67  367 62  HOH HOH A . 
F 6 HOH 68  368 25  HOH HOH A . 
F 6 HOH 69  369 147 HOH HOH A . 
F 6 HOH 70  370 95  HOH HOH A . 
F 6 HOH 71  371 244 HOH HOH A . 
F 6 HOH 72  372 66  HOH HOH A . 
F 6 HOH 73  373 89  HOH HOH A . 
F 6 HOH 74  374 28  HOH HOH A . 
F 6 HOH 75  375 104 HOH HOH A . 
F 6 HOH 76  376 123 HOH HOH A . 
F 6 HOH 77  377 178 HOH HOH A . 
F 6 HOH 78  378 119 HOH HOH A . 
F 6 HOH 79  379 22  HOH HOH A . 
F 6 HOH 80  380 107 HOH HOH A . 
F 6 HOH 81  381 20  HOH HOH A . 
F 6 HOH 82  382 40  HOH HOH A . 
F 6 HOH 83  383 10  HOH HOH A . 
F 6 HOH 84  384 44  HOH HOH A . 
F 6 HOH 85  385 164 HOH HOH A . 
F 6 HOH 86  386 57  HOH HOH A . 
F 6 HOH 87  387 238 HOH HOH A . 
F 6 HOH 88  388 29  HOH HOH A . 
F 6 HOH 89  389 39  HOH HOH A . 
F 6 HOH 90  390 192 HOH HOH A . 
F 6 HOH 91  391 38  HOH HOH A . 
F 6 HOH 92  392 60  HOH HOH A . 
F 6 HOH 93  393 21  HOH HOH A . 
F 6 HOH 94  394 246 HOH HOH A . 
F 6 HOH 95  395 99  HOH HOH A . 
F 6 HOH 96  396 30  HOH HOH A . 
F 6 HOH 97  397 52  HOH HOH A . 
F 6 HOH 98  398 27  HOH HOH A . 
F 6 HOH 99  399 203 HOH HOH A . 
F 6 HOH 100 400 36  HOH HOH A . 
F 6 HOH 101 401 56  HOH HOH A . 
F 6 HOH 102 402 242 HOH HOH A . 
F 6 HOH 103 403 82  HOH HOH A . 
F 6 HOH 104 404 193 HOH HOH A . 
F 6 HOH 105 405 239 HOH HOH A . 
F 6 HOH 106 406 93  HOH HOH A . 
F 6 HOH 107 407 96  HOH HOH A . 
F 6 HOH 108 408 75  HOH HOH A . 
F 6 HOH 109 409 37  HOH HOH A . 
F 6 HOH 110 410 237 HOH HOH A . 
F 6 HOH 111 411 53  HOH HOH A . 
F 6 HOH 112 412 45  HOH HOH A . 
F 6 HOH 113 413 17  HOH HOH A . 
F 6 HOH 114 414 176 HOH HOH A . 
F 6 HOH 115 415 209 HOH HOH A . 
F 6 HOH 116 416 79  HOH HOH A . 
F 6 HOH 117 417 69  HOH HOH A . 
F 6 HOH 118 418 167 HOH HOH A . 
F 6 HOH 119 419 186 HOH HOH A . 
F 6 HOH 120 420 55  HOH HOH A . 
F 6 HOH 121 421 153 HOH HOH A . 
F 6 HOH 122 422 200 HOH HOH A . 
F 6 HOH 123 423 54  HOH HOH A . 
F 6 HOH 124 424 146 HOH HOH A . 
F 6 HOH 125 425 171 HOH HOH A . 
F 6 HOH 126 426 148 HOH HOH A . 
F 6 HOH 127 427 241 HOH HOH A . 
F 6 HOH 128 428 145 HOH HOH A . 
F 6 HOH 129 429 98  HOH HOH A . 
F 6 HOH 130 430 31  HOH HOH A . 
F 6 HOH 131 431 106 HOH HOH A . 
F 6 HOH 132 432 43  HOH HOH A . 
F 6 HOH 133 433 185 HOH HOH A . 
F 6 HOH 134 434 188 HOH HOH A . 
F 6 HOH 135 435 191 HOH HOH A . 
F 6 HOH 136 436 139 HOH HOH A . 
F 6 HOH 137 437 80  HOH HOH A . 
F 6 HOH 138 438 232 HOH HOH A . 
F 6 HOH 139 439 158 HOH HOH A . 
F 6 HOH 140 440 76  HOH HOH A . 
F 6 HOH 141 441 204 HOH HOH A . 
F 6 HOH 142 442 111 HOH HOH A . 
F 6 HOH 143 443 140 HOH HOH A . 
F 6 HOH 144 444 137 HOH HOH A . 
F 6 HOH 145 445 108 HOH HOH A . 
F 6 HOH 146 446 221 HOH HOH A . 
F 6 HOH 147 447 169 HOH HOH A . 
F 6 HOH 148 448 243 HOH HOH A . 
F 6 HOH 149 449 206 HOH HOH A . 
F 6 HOH 150 450 247 HOH HOH A . 
F 6 HOH 151 451 70  HOH HOH A . 
F 6 HOH 152 452 161 HOH HOH A . 
F 6 HOH 153 453 131 HOH HOH A . 
F 6 HOH 154 454 212 HOH HOH A . 
F 6 HOH 155 455 228 HOH HOH A . 
F 6 HOH 156 456 215 HOH HOH A . 
F 6 HOH 157 457 183 HOH HOH A . 
F 6 HOH 158 458 142 HOH HOH A . 
F 6 HOH 159 459 73  HOH HOH A . 
F 6 HOH 160 460 245 HOH HOH A . 
F 6 HOH 161 461 59  HOH HOH A . 
F 6 HOH 162 462 179 HOH HOH A . 
F 6 HOH 163 463 175 HOH HOH A . 
F 6 HOH 164 464 65  HOH HOH A . 
F 6 HOH 165 465 152 HOH HOH A . 
F 6 HOH 166 466 195 HOH HOH A . 
F 6 HOH 167 467 208 HOH HOH A . 
F 6 HOH 168 468 181 HOH HOH A . 
F 6 HOH 169 469 170 HOH HOH A . 
F 6 HOH 170 470 233 HOH HOH A . 
F 6 HOH 171 471 61  HOH HOH A . 
F 6 HOH 172 472 144 HOH HOH A . 
F 6 HOH 173 473 225 HOH HOH A . 
G 6 HOH 1   201 77  HOH HOH D . 
G 6 HOH 2   202 71  HOH HOH D . 
G 6 HOH 3   203 47  HOH HOH D . 
G 6 HOH 4   204 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           7GUL 
_cell.length_a           67.580 
_cell.length_b           67.580 
_cell.length_c           166.330 
_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                         7GUL 
_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          7GUL 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.62 
_exptl_crystal.density_percent_sol   66.01 
_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                     7GUL 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.900 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   21722 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.082 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.300 
_reflns.B_iso_Wilson_estimate        31.290 
_reflns.pdbx_redundancy              9.000 
_reflns.pdbx_Rrim_I_all              0.087 
_reflns.pdbx_Rpim_I_all              0.029 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     195962 
_reflns.pdbx_scaling_rejects         805 
_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  ? 11580 1246 ? 1.487 ? ? ? 9.300 ? 1.500  ? ? ? ? ? ? 100.000 1.573 0.507 0.697 ? 
1 2 9.000 33.900 ? 1510  226  ? 0.037 ? ? ? 6.700 ? 33.000 ? ? ? ? ? ? 98.700  0.040 0.015 0.999 ? 
# 
_refine.entry_id                                 7GUL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.8000 
_refine.ls_d_res_low                             33.9000 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.9000 
_refine.ls_number_reflns_obs                     21664 
_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                          0.1800 
_refine.ls_R_factor_R_work                       0.1790 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2040 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.2000 
_refine.ls_number_reflns_R_free                  1127 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               36.9900 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -1.3551 
_refine.aniso_B[2][2]                            -1.3551 
_refine.aniso_B[3][3]                            2.7101 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9610 
_refine.correlation_coeff_Fo_to_Fc_free          0.9510 
_refine.overall_SU_R_Cruickshank_DPI             0.0940 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0920 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1080 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.1010 
_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                                136.190 
_refine.B_iso_min                                17.300 
_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                        7GUL 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.220 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.8000 
_refine_hist.d_res_low                        33.9000 
_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           32.19 
_refine_hist.pdbx_B_iso_mean_solvent          55.24 
_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      1635 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1236 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1693 0.900  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.340  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    16.330 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       1.8000 
_refine_ls_shell.d_res_low                        1.8900 
_refine_ls_shell.pdbx_total_number_of_bins_used   11 
_refine_ls_shell.percent_reflns_obs               99.8600 
_refine_ls_shell.number_reflns_R_work             2679 
_refine_ls_shell.R_factor_all                     0.2748 
_refine_ls_shell.R_factor_R_work                  0.2748 
_refine_ls_shell.R_factor_R_free                  0.2762 
_refine_ls_shell.percent_reflns_R_free            4.6600 
_refine_ls_shell.number_reflns_R_free             131 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2810 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUL 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 1 at 13.59 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUL 
_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 7GUL       7GUL   ? 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 7GUL A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUL D 1 ? 6   ? 7GUL   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 7GUL GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUL PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUL GLY A 3 ? UNP P41182 ? ? 'expression tag' 4 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6370  ? 
1 MORE         -68   ? 
1 'SSA (A^2)'  13280 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z          1.0000000000 0.0000000000 0.0000000000 0.0000000000  0.0000000000 
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 12_545 x,x-y-1,-z+1/6 0.5000000000 0.8660254038 0.0000000000 33.7900000000 0.8660254038 
-0.5000000000 0.0000000000 -58.5259967878 0.0000000000 0.0000000000 -1.0000000000 27.7216666667 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ARG A 12  ? ARG A 27  ? ARG A 13  ARG A 28  1 ? 16 
HELX_P HELX_P2 AA2 HIS A 45  ? SER A 53  ? HIS A 46  SER A 54  1 ? 9  
HELX_P HELX_P3 AA3 SER A 53  ? THR A 61  ? SER A 54  THR A 62  1 ? 9  
HELX_P HELX_P4 AA4 LEU A 64  ? LEU A 68  ? LEU A 65  LEU A 69  5 ? 5  
HELX_P HELX_P5 AA5 ASN A 78  ? SER A 92  ? ASN A 79  SER A 93  1 ? 15 
HELX_P HELX_P6 AA6 ASN A 100 ? GLN A 112 ? ASN A 101 GLN A 113 1 ? 13 
HELX_P HELX_P7 AA7 MET A 113 ? GLU A 128 ? MET A 114 GLU A 129 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N A ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 ACE B 1 ? TRP B 2 A ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
2 ACE B 1 ? TRP B 2 B ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 40 ? ALA A 44 ? GLU A 41 ALA A 45 
AA1 2 VAL A 33 ? VAL A 37 ? VAL A 34 VAL A 38 
AA1 3 VAL A 70 ? ASN A 72 ? VAL A 71 ASN A 73 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 40 ? O GLU A 41 N VAL A 37 ? N VAL A 38 
AA1 2 3 N VAL A 36 ? N VAL A 37 O ILE A 71 ? O ILE A 72 
# 
_pdbx_entry_details.entry_id                   7GUL 
_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 37.95   48.06   
2 1 SER A 39  ? B 62.04   -107.51 
3 1 SER A 93  ? ? 76.78   -0.14   
4 1 SER A 93  ? ? 76.78   -2.96   
5 1 GLN A 113 ? ? 62.41   62.86   
6 1 MET A 114 ? ? -118.50 79.16   
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             VAL 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              38 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   10.89 
# 
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 332 ? F HOH . 
2 1 A HOH 385 ? F HOH . 
3 1 A HOH 447 ? F HOH . 
4 1 A HOH 462 ? 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 -0.0144 -0.0767 -0.0215 -0.0430 0.0247  -0.0158 1.0856 1.8063 2.2111 
0.4618 -0.2704 1.1993 0.1479 -0.0986 -0.0493 -0.0506 0.1025 0.0748 0.2571  0.0079  -0.0547 
'X-RAY DIFFRACTION' 2 ? refined 18.9623 -32.3913 1.8231  -0.1484 0.0949  -0.0214 -0.0550 -0.0116 -0.0806 0.7064 0.1529 0.0000 
0.3364 -0.1510 0.8841 0.0280 0.0133  -0.0412 0.0009  0.0139 0.0639 -0.0305 -0.0214 0.0055  
# 
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                    7GUL 
_atom_sites.fract_transf_matrix[1][1]   0.014797 
_atom_sites.fract_transf_matrix[1][2]   0.008543 
_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]   0.017086 
_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]   0.006012 
_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   ? 17.526 -21.135 -4.991 1.00 68.77  ? 6   ASP A N   1 
ATOM   2    C  CA  . ASP A 1 5   ? 18.400 -22.062 -5.714 1.00 67.62  ? 6   ASP A CA  1 
ATOM   3    C  C   . ASP A 1 5   ? 17.901 -23.525 -5.604 1.00 67.43  ? 6   ASP A C   1 
ATOM   4    O  O   . ASP A 1 5   ? 16.816 -23.773 -5.066 1.00 68.19  ? 6   ASP A O   1 
ATOM   5    C  CB  . ASP A 1 5   ? 19.855 -21.930 -5.203 1.00 68.29  ? 6   ASP A CB  1 
ATOM   6    C  CG  . ASP A 1 5   ? 20.913 -22.022 -6.293 1.00 82.17  ? 6   ASP A CG  1 
ATOM   7    O  OD1 . ASP A 1 5   ? 20.990 -23.082 -6.964 1.00 82.71  ? 6   ASP A OD1 1 
ATOM   8    O  OD2 . ASP A 1 5   ? 21.675 -21.044 -6.465 1.00 89.19  ? 6   ASP A OD2 1 
ATOM   9    N  N   . SER A 1 6   ? 18.690 -24.480 -6.135 1.00 58.76  ? 7   SER A N   1 
ATOM   10   C  CA  . SER A 1 6   ? 18.398 -25.912 -6.105 1.00 56.08  ? 7   SER A CA  1 
ATOM   11   C  C   . SER A 1 6   ? 19.390 -26.671 -5.166 1.00 51.58  ? 7   SER A C   1 
ATOM   12   O  O   . SER A 1 6   ? 19.689 -27.848 -5.386 1.00 50.70  ? 7   SER A O   1 
ATOM   13   C  CB  . SER A 1 6   ? 18.434 -26.478 -7.520 1.00 61.67  ? 7   SER A CB  1 
ATOM   14   O  OG  . SER A 1 6   ? 19.701 -26.286 -8.129 1.00 73.86  ? 7   SER A OG  1 
ATOM   15   N  N   . CYS A 1 7   ? 19.874 -25.993 -4.111 1.00 41.99  ? 8   CYS A N   1 
ATOM   16   C  CA  . CYS A 1 7   ? 20.814 -26.570 -3.140 1.00 38.74  ? 8   CYS A CA  1 
ATOM   17   C  C   . CYS A 1 7   ? 20.197 -27.739 -2.337 1.00 38.32  ? 8   CYS A C   1 
ATOM   18   O  O   . CYS A 1 7   ? 18.977 -27.817 -2.187 1.00 38.43  ? 8   CYS A O   1 
ATOM   19   C  CB  . CYS A 1 7   ? 21.306 -25.480 -2.186 1.00 39.54  ? 8   CYS A CB  1 
ATOM   20   S  SG  . CYS A 1 7   ? 22.432 -24.260 -2.929 1.00 44.65  ? 8   CYS A SG  1 
ATOM   21   N  N   . ILE A 1 8   ? 21.042 -28.635 -1.817 1.00 29.10  ? 9   ILE A N   1 
ATOM   22   C  CA  . ILE A 1 8   ? 20.657 -29.631 -0.816 1.00 26.42  ? 9   ILE A CA  1 
ATOM   23   C  C   . ILE A 1 8   ? 21.264 -29.084 0.484  1.00 28.14  ? 9   ILE A C   1 
ATOM   24   O  O   . ILE A 1 8   ? 22.199 -28.275 0.431  1.00 27.15  ? 9   ILE A O   1 
ATOM   25   C  CB  . ILE A 1 8   ? 21.021 -31.110 -1.122 1.00 29.10  ? 9   ILE A CB  1 
ATOM   26   C  CG1 . ILE A 1 8   ? 22.556 -31.292 -1.351 1.00 28.87  ? 9   ILE A CG1 1 
ATOM   27   C  CG2 . ILE A 1 8   ? 20.176 -31.638 -2.302 1.00 31.42  ? 9   ILE A CG2 1 
ATOM   28   C  CD1 . ILE A 1 8   ? 23.039 -32.755 -1.544 1.00 33.09  ? 9   ILE A CD1 1 
ATOM   29   N  N   A GLN A 1 9   ? 20.790 -29.529 1.641  0.57 24.19  ? 10  GLN A N   1 
ATOM   30   N  N   B GLN A 1 9   ? 20.685 -29.457 1.625  0.43 24.16  ? 10  GLN A N   1 
ATOM   31   C  CA  A GLN A 1 9   ? 21.313 -29.002 2.900  0.57 23.11  ? 10  GLN A CA  1 
ATOM   32   C  CA  B GLN A 1 9   ? 21.107 -28.978 2.937  0.43 22.88  ? 10  GLN A CA  1 
ATOM   33   C  C   A GLN A 1 9   ? 21.633 -30.116 3.889  0.57 26.41  ? 10  GLN A C   1 
ATOM   34   C  C   B GLN A 1 9   ? 21.554 -30.128 3.824  0.43 25.00  ? 10  GLN A C   1 
ATOM   35   O  O   A GLN A 1 9   ? 20.821 -31.022 4.066  0.57 25.86  ? 10  GLN A O   1 
ATOM   36   O  O   B GLN A 1 9   ? 20.919 -31.181 3.835  0.43 24.71  ? 10  GLN A O   1 
ATOM   37   C  CB  A GLN A 1 9   ? 20.294 -27.998 3.493  0.57 24.57  ? 10  GLN A CB  1 
ATOM   38   C  CB  B GLN A 1 9   ? 19.952 -28.190 3.607  0.43 24.30  ? 10  GLN A CB  1 
ATOM   39   C  CG  A GLN A 1 9   ? 20.657 -27.405 4.856  0.57 25.02  ? 10  GLN A CG  1 
ATOM   40   C  CG  B GLN A 1 9   ? 20.132 -27.929 5.123  0.43 30.28  ? 10  GLN A CG  1 
ATOM   41   C  CD  A GLN A 1 9   ? 19.466 -26.715 5.480  0.57 51.11  ? 10  GLN A CD  1 
ATOM   42   C  CD  B GLN A 1 9   ? 20.093 -26.480 5.538  0.43 42.12  ? 10  GLN A CD  1 
ATOM   43   O  OE1 A GLN A 1 9   ? 18.486 -27.344 5.897  0.57 41.71  ? 10  GLN A OE1 1 
ATOM   44   O  OE1 B GLN A 1 9   ? 19.796 -25.569 4.747  0.43 32.47  ? 10  GLN A OE1 1 
ATOM   45   N  NE2 A GLN A 1 9   ? 19.522 -25.399 5.554  0.57 53.10  ? 10  GLN A NE2 1 
ATOM   46   N  NE2 B GLN A 1 9   ? 20.387 -26.238 6.811  0.43 32.01  ? 10  GLN A NE2 1 
ATOM   47   N  N   A PHE A 1 10  ? 22.802 -30.041 4.548  0.78 24.51  ? 11  PHE A N   1 
ATOM   48   N  N   B PHE A 1 10  ? 22.626 -29.905 4.589  0.22 21.45  ? 11  PHE A N   1 
ATOM   49   C  CA  A PHE A 1 10  ? 23.168 -31.040 5.555  0.78 23.85  ? 11  PHE A CA  1 
ATOM   50   C  CA  B PHE A 1 10  ? 23.133 -30.873 5.550  0.22 20.75  ? 11  PHE A CA  1 
ATOM   51   C  C   A PHE A 1 10  ? 22.684 -30.545 6.920  0.78 25.05  ? 11  PHE A C   1 
ATOM   52   C  C   B PHE A 1 10  ? 22.607 -30.425 6.896  0.22 24.31  ? 11  PHE A C   1 
ATOM   53   O  O   A PHE A 1 10  ? 23.244 -29.592 7.481  0.78 23.11  ? 11  PHE A O   1 
ATOM   54   O  O   B PHE A 1 10  ? 23.035 -29.383 7.408  0.22 23.07  ? 11  PHE A O   1 
ATOM   55   C  CB  A PHE A 1 10  ? 24.693 -31.349 5.529  0.78 24.79  ? 11  PHE A CB  1 
ATOM   56   C  CB  B PHE A 1 10  ? 24.669 -30.922 5.495  0.22 21.56  ? 11  PHE A CB  1 
ATOM   57   C  CG  A PHE A 1 10  ? 25.078 -32.556 6.360  0.78 25.87  ? 11  PHE A CG  1 
ATOM   58   C  CG  B PHE A 1 10  ? 25.182 -31.811 4.387  0.22 23.22  ? 11  PHE A CG  1 
ATOM   59   C  CD1 A PHE A 1 10  ? 24.648 -33.835 6.009  0.78 29.50  ? 11  PHE A CD1 1 
ATOM   60   C  CD1 B PHE A 1 10  ? 24.911 -31.521 3.053  0.22 26.46  ? 11  PHE A CD1 1 
ATOM   61   C  CD2 A PHE A 1 10  ? 25.882 -32.416 7.490  0.78 27.18  ? 11  PHE A CD2 1 
ATOM   62   C  CD2 B PHE A 1 10  ? 25.940 -32.938 4.675  0.22 25.71  ? 11  PHE A CD2 1 
ATOM   63   C  CE1 A PHE A 1 10  ? 24.992 -34.950 6.794  0.78 30.73  ? 11  PHE A CE1 1 
ATOM   64   C  CE1 B PHE A 1 10  ? 25.379 -32.347 2.031  0.22 27.65  ? 11  PHE A CE1 1 
ATOM   65   C  CE2 A PHE A 1 10  ? 26.215 -33.524 8.277  0.78 29.01  ? 11  PHE A CE2 1 
ATOM   66   C  CE2 B PHE A 1 10  ? 26.406 -33.763 3.649  0.22 28.99  ? 11  PHE A CE2 1 
ATOM   67   C  CZ  A PHE A 1 10  ? 25.764 -34.780 7.932  0.78 27.65  ? 11  PHE A CZ  1 
ATOM   68   C  CZ  B PHE A 1 10  ? 26.130 -33.457 2.337  0.22 27.08  ? 11  PHE A CZ  1 
ATOM   69   N  N   . THR A 1 11  ? 21.604 -31.155 7.424  1.00 21.80  ? 12  THR A N   1 
ATOM   70   C  CA  . THR A 1 11  ? 20.943 -30.767 8.685  1.00 22.69  ? 12  THR A CA  1 
ATOM   71   C  C   . THR A 1 11  ? 21.900 -30.537 9.885  1.00 26.37  ? 12  THR A C   1 
ATOM   72   O  O   . THR A 1 11  ? 21.779 -29.508 10.564 1.00 24.88  ? 12  THR A O   1 
ATOM   73   C  CB  . THR A 1 11  ? 19.861 -31.797 9.029  1.00 31.15  ? 12  THR A CB  1 
ATOM   74   O  OG1 . THR A 1 11  ? 18.945 -31.857 7.927  1.00 32.10  ? 12  THR A OG1 1 
ATOM   75   C  CG2 . THR A 1 11  ? 19.099 -31.444 10.320 1.00 35.37  ? 12  THR A CG2 1 
ATOM   76   N  N   A ARG A 1 12  ? 22.839 -31.470 10.116 0.50 23.55  ? 13  ARG A N   1 
ATOM   77   N  N   B ARG A 1 12  ? 22.835 -31.472 10.126 0.50 23.82  ? 13  ARG A N   1 
ATOM   78   C  CA  A ARG A 1 12  ? 23.757 -31.405 11.264 0.50 23.58  ? 13  ARG A CA  1 
ATOM   79   C  CA  B ARG A 1 12  ? 23.762 -31.400 11.268 0.50 23.95  ? 13  ARG A CA  1 
ATOM   80   C  C   A ARG A 1 12  ? 25.005 -30.522 11.066 0.50 25.36  ? 13  ARG A C   1 
ATOM   81   C  C   B ARG A 1 12  ? 24.993 -30.499 11.076 0.50 25.45  ? 13  ARG A C   1 
ATOM   82   O  O   A ARG A 1 12  ? 25.811 -30.408 11.999 0.50 23.89  ? 13  ARG A O   1 
ATOM   83   O  O   B ARG A 1 12  ? 25.785 -30.363 12.017 0.50 23.87  ? 13  ARG A O   1 
ATOM   84   C  CB  A ARG A 1 12  ? 24.183 -32.828 11.694 0.50 26.66  ? 13  ARG A CB  1 
ATOM   85   C  CB  B ARG A 1 12  ? 24.219 -32.814 11.663 0.50 27.76  ? 13  ARG A CB  1 
ATOM   86   C  CG  A ARG A 1 12  ? 23.038 -33.733 12.194 0.50 34.71  ? 13  ARG A CG  1 
ATOM   87   C  CG  B ARG A 1 12  ? 23.257 -33.535 12.608 0.50 39.63  ? 13  ARG A CG  1 
ATOM   88   C  CD  A ARG A 1 12  ? 22.461 -33.298 13.534 0.50 46.10  ? 13  ARG A CD  1 
ATOM   89   C  CD  B ARG A 1 12  ? 22.980 -34.973 12.212 0.50 46.51  ? 13  ARG A CD  1 
ATOM   90   N  NE  A ARG A 1 12  ? 23.416 -33.449 14.637 0.50 52.68  ? 13  ARG A NE  1 
ATOM   91   N  NE  B ARG A 1 12  ? 24.193 -35.754 11.945 0.50 50.35  ? 13  ARG A NE  1 
ATOM   92   C  CZ  A ARG A 1 12  ? 23.387 -32.739 15.761 0.50 59.96  ? 13  ARG A CZ  1 
ATOM   93   C  CZ  B ARG A 1 12  ? 24.384 -36.485 10.850 0.50 60.49  ? 13  ARG A CZ  1 
ATOM   94   N  NH1 A ARG A 1 12  ? 22.463 -31.802 15.941 0.50 38.88  ? 13  ARG A NH1 1 
ATOM   95   N  NH1 B ARG A 1 12  ? 25.510 -37.168 10.689 0.50 54.28  ? 13  ARG A NH1 1 
ATOM   96   N  NH2 A ARG A 1 12  ? 24.285 -32.954 16.711 0.50 49.69  ? 13  ARG A NH2 1 
ATOM   97   N  NH2 B ARG A 1 12  ? 23.449 -36.544 9.910  0.50 36.69  ? 13  ARG A NH2 1 
ATOM   98   N  N   . HIS A 1 13  ? 25.167 -29.901 9.880  1.00 20.94  ? 14  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 13  ? 26.371 -29.085 9.569  1.00 19.65  ? 14  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 13  ? 26.655 -27.972 10.580 1.00 22.79  ? 14  HIS A C   1 
ATOM   101  O  O   . HIS A 1 13  ? 27.786 -27.900 11.075 1.00 21.51  ? 14  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 13  ? 26.346 -28.510 8.139  1.00 19.65  ? 14  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 13  ? 27.618 -27.760 7.825  1.00 21.23  ? 14  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 13  ? 28.802 -28.426 7.636  1.00 21.83  ? 14  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 13  ? 27.832 -26.430 7.694  1.00 21.85  ? 14  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 13  ? 29.713 -27.496 7.371  1.00 20.66  ? 14  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 13  ? 29.180 -26.271 7.421  1.00 20.94  ? 14  HIS A NE2 1 
ATOM   108  N  N   . ALA A 1 14  ? 25.668 -27.095 10.852 1.00 19.89  ? 15  ALA A N   1 
ATOM   109  C  CA  . ALA A 1 14  ? 25.884 -25.964 11.787 1.00 20.28  ? 15  ALA A CA  1 
ATOM   110  C  C   . ALA A 1 14  ? 26.290 -26.436 13.195 1.00 22.34  ? 15  ALA A C   1 
ATOM   111  O  O   . ALA A 1 14  ? 27.191 -25.852 13.789 1.00 20.75  ? 15  ALA A O   1 
ATOM   112  C  CB  . ALA A 1 14  ? 24.637 -25.079 11.847 1.00 21.46  ? 15  ALA A CB  1 
ATOM   113  N  N   A SER A 1 15  ? 25.640 -27.495 13.698 0.38 20.86  ? 16  SER A N   1 
ATOM   114  N  N   B SER A 1 15  ? 25.644 -27.502 13.701 0.33 20.96  ? 16  SER A N   1 
ATOM   115  N  N   C SER A 1 15  ? 25.641 -27.499 13.711 0.29 20.57  ? 16  SER A N   1 
ATOM   116  C  CA  A SER A 1 15  ? 25.932 -28.067 15.011 0.38 21.19  ? 16  SER A CA  1 
ATOM   117  C  CA  B SER A 1 15  ? 25.931 -28.078 15.016 0.33 21.39  ? 16  SER A CA  1 
ATOM   118  C  CA  C SER A 1 15  ? 25.948 -28.053 15.033 0.29 20.79  ? 16  SER A CA  1 
ATOM   119  C  C   A SER A 1 15  ? 27.344 -28.654 15.032 0.38 25.08  ? 16  SER A C   1 
ATOM   120  C  C   B SER A 1 15  ? 27.334 -28.683 15.046 0.33 25.40  ? 16  SER A C   1 
ATOM   121  C  C   C SER A 1 15  ? 27.341 -28.687 15.054 0.29 25.22  ? 16  SER A C   1 
ATOM   122  O  O   A SER A 1 15  ? 28.069 -28.439 16.008 0.38 22.93  ? 16  SER A O   1 
ATOM   123  O  O   B SER A 1 15  ? 28.043 -28.513 16.041 0.33 23.69  ? 16  SER A O   1 
ATOM   124  O  O   C SER A 1 15  ? 28.051 -28.541 16.051 0.29 23.70  ? 16  SER A O   1 
ATOM   125  C  CB  A SER A 1 15  ? 24.904 -29.138 15.367 0.38 24.77  ? 16  SER A CB  1 
ATOM   126  C  CB  B SER A 1 15  ? 24.891 -29.134 15.381 0.33 25.28  ? 16  SER A CB  1 
ATOM   127  C  CB  C SER A 1 15  ? 24.885 -29.059 15.468 0.29 24.04  ? 16  SER A CB  1 
ATOM   128  O  OG  A SER A 1 15  ? 25.186 -29.705 16.634 0.38 28.89  ? 16  SER A OG  1 
ATOM   129  O  OG  B SER A 1 15  ? 23.589 -28.573 15.409 0.33 30.96  ? 16  SER A OG  1 
ATOM   130  O  OG  C SER A 1 15  ? 24.848 -30.188 14.611 0.29 27.61  ? 16  SER A OG  1 
ATOM   131  N  N   . ASP A 1 16  ? 27.741 -29.361 13.950 1.00 23.09  ? 17  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 16  ? 29.077 -29.986 13.820 1.00 23.22  ? 17  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 16  ? 30.148 -28.891 13.788 1.00 23.44  ? 17  ASP A C   1 
ATOM   134  O  O   . ASP A 1 16  ? 31.197 -29.054 14.409 1.00 23.18  ? 17  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 16  ? 29.174 -30.859 12.550 1.00 25.07  ? 17  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 16  ? 28.409 -32.183 12.621 1.00 36.58  ? 17  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 16  ? 27.870 -32.507 13.707 1.00 36.90  ? 17  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 16  ? 28.339 -32.887 11.583 1.00 37.83  ? 17  ASP A OD2 1 
ATOM   139  N  N   . VAL A 1 17  ? 29.884 -27.783 13.053 1.00 18.56  ? 18  VAL A N   1 
ATOM   140  C  CA  . VAL A 1 17  ? 30.825 -26.642 13.022 1.00 17.97  ? 18  VAL A CA  1 
ATOM   141  C  C   . VAL A 1 17  ? 31.027 -26.101 14.458 1.00 21.18  ? 18  VAL A C   1 
ATOM   142  O  O   . VAL A 1 17  ? 32.153 -25.890 14.900 1.00 19.82  ? 18  VAL A O   1 
ATOM   143  C  CB  . VAL A 1 17  ? 30.347 -25.516 12.066 1.00 20.54  ? 18  VAL A CB  1 
ATOM   144  C  CG1 . VAL A 1 17  ? 31.127 -24.210 12.307 1.00 20.01  ? 18  VAL A CG1 1 
ATOM   145  C  CG2 . VAL A 1 17  ? 30.458 -25.955 10.602 1.00 20.47  ? 18  VAL A CG2 1 
ATOM   146  N  N   . LEU A 1 18  ? 29.932 -25.839 15.162 1.00 19.25  ? 19  LEU A N   1 
ATOM   147  C  CA  . LEU A 1 18  ? 30.014 -25.271 16.511 1.00 19.87  ? 19  LEU A CA  1 
ATOM   148  C  C   . LEU A 1 18  ? 30.740 -26.213 17.486 1.00 22.48  ? 19  LEU A C   1 
ATOM   149  O  O   . LEU A 1 18  ? 31.574 -25.747 18.267 1.00 20.75  ? 19  LEU A O   1 
ATOM   150  C  CB  . LEU A 1 18  ? 28.628 -24.887 17.032 1.00 21.06  ? 19  LEU A CB  1 
ATOM   151  C  CG  . LEU A 1 18  ? 28.643 -23.980 18.287 1.00 24.60  ? 19  LEU A CG  1 
ATOM   152  C  CD1 . LEU A 1 18  ? 29.183 -22.590 17.953 1.00 24.39  ? 19  LEU A CD1 1 
ATOM   153  C  CD2 . LEU A 1 18  ? 27.231 -23.840 18.848 1.00 28.78  ? 19  LEU A CD2 1 
ATOM   154  N  N   . LEU A 1 19  ? 30.461 -27.525 17.398 1.00 20.87  ? 20  LEU A N   1 
ATOM   155  C  CA  . LEU A 1 19  ? 31.148 -28.541 18.210 1.00 22.33  ? 20  LEU A CA  1 
ATOM   156  C  C   . LEU A 1 19  ? 32.663 -28.469 17.946 1.00 23.29  ? 20  LEU A C   1 
ATOM   157  O  O   . LEU A 1 19  ? 33.452 -28.457 18.901 1.00 21.92  ? 20  LEU A O   1 
ATOM   158  C  CB  . LEU A 1 19  ? 30.618 -29.930 17.848 1.00 24.22  ? 20  LEU A CB  1 
ATOM   159  C  CG  . LEU A 1 19  ? 31.203 -31.092 18.636 1.00 33.69  ? 20  LEU A CG  1 
ATOM   160  C  CD1 . LEU A 1 19  ? 30.692 -31.074 20.088 1.00 36.32  ? 20  LEU A CD1 1 
ATOM   161  C  CD2 . LEU A 1 19  ? 30.806 -32.406 17.996 1.00 38.62  ? 20  LEU A CD2 1 
ATOM   162  N  N   . ASN A 1 20  ? 33.064 -28.365 16.671 1.00 19.74  ? 21  ASN A N   1 
ATOM   163  C  CA  . ASN A 1 20  ? 34.497 -28.261 16.344 1.00 19.15  ? 21  ASN A CA  1 
ATOM   164  C  C   . ASN A 1 20  ? 35.122 -26.958 16.827 1.00 21.78  ? 21  ASN A C   1 
ATOM   165  O  O   . ASN A 1 20  ? 36.281 -26.955 17.248 1.00 20.96  ? 21  ASN A O   1 
ATOM   166  C  CB  . ASN A 1 20  ? 34.731 -28.493 14.846 1.00 20.84  ? 21  ASN A CB  1 
ATOM   167  C  CG  . ASN A 1 20  ? 34.657 -29.960 14.491 1.00 31.12  ? 21  ASN A CG  1 
ATOM   168  O  OD1 . ASN A 1 20  ? 34.813 -30.824 15.348 1.00 27.91  ? 21  ASN A OD1 1 
ATOM   169  N  ND2 . ASN A 1 20  ? 34.400 -30.281 13.228 1.00 24.86  ? 21  ASN A ND2 1 
ATOM   170  N  N   . LEU A 1 21  ? 34.373 -25.839 16.754 1.00 19.06  ? 22  LEU A N   1 
ATOM   171  C  CA  . LEU A 1 21  ? 34.885 -24.565 17.259 1.00 18.92  ? 22  LEU A CA  1 
ATOM   172  C  C   . LEU A 1 21  ? 35.096 -24.688 18.778 1.00 21.10  ? 22  LEU A C   1 
ATOM   173  O  O   . LEU A 1 21  ? 36.086 -24.181 19.307 1.00 19.75  ? 22  LEU A O   1 
ATOM   174  C  CB  . LEU A 1 21  ? 33.900 -23.419 16.937 1.00 18.36  ? 22  LEU A CB  1 
ATOM   175  C  CG  . LEU A 1 21  ? 33.781 -23.072 15.422 1.00 20.94  ? 22  LEU A CG  1 
ATOM   176  C  CD1 . LEU A 1 21  ? 32.740 -21.976 15.212 1.00 21.24  ? 22  LEU A CD1 1 
ATOM   177  C  CD2 . LEU A 1 21  ? 35.137 -22.623 14.835 1.00 25.36  ? 22  LEU A CD2 1 
ATOM   178  N  N   . ASN A 1 22  ? 34.167 -25.368 19.475 1.00 19.02  ? 23  ASN A N   1 
ATOM   179  C  CA  . ASN A 1 22  ? 34.337 -25.565 20.931 1.00 19.95  ? 23  ASN A CA  1 
ATOM   180  C  C   . ASN A 1 22  ? 35.571 -26.467 21.232 1.00 24.34  ? 23  ASN A C   1 
ATOM   181  O  O   . ASN A 1 22  ? 36.267 -26.243 22.226 1.00 25.07  ? 23  ASN A O   1 
ATOM   182  C  CB  . ASN A 1 22  ? 33.071 -26.145 21.558 1.00 21.63  ? 23  ASN A CB  1 
ATOM   183  C  CG  . ASN A 1 22  ? 33.091 -26.027 23.069 1.00 27.49  ? 23  ASN A CG  1 
ATOM   184  O  OD1 . ASN A 1 22  ? 33.562 -25.040 23.633 1.00 26.59  ? 23  ASN A OD1 1 
ATOM   185  N  ND2 . ASN A 1 22  ? 32.594 -27.027 23.735 1.00 29.94  ? 23  ASN A ND2 1 
ATOM   186  N  N   . ARG A 1 23  ? 35.838 -27.482 20.378 1.00 21.75  ? 24  ARG A N   1 
ATOM   187  C  CA  . ARG A 1 23  ? 37.024 -28.351 20.539 1.00 22.14  ? 24  ARG A CA  1 
ATOM   188  C  C   . ARG A 1 23  ? 38.297 -27.516 20.366 1.00 26.35  ? 24  ARG A C   1 
ATOM   189  O  O   . ARG A 1 23  ? 39.235 -27.699 21.122 1.00 26.56  ? 24  ARG A O   1 
ATOM   190  C  CB  . ARG A 1 23  ? 37.029 -29.497 19.522 1.00 22.77  ? 24  ARG A CB  1 
ATOM   191  C  CG  . ARG A 1 23  ? 36.020 -30.590 19.860 1.00 28.55  ? 24  ARG A CG  1 
ATOM   192  C  CD  . ARG A 1 23  ? 35.763 -31.473 18.652 1.00 33.42  ? 24  ARG A CD  1 
ATOM   193  N  NE  . ARG A 1 23  ? 34.910 -32.607 18.989 1.00 40.27  ? 24  ARG A NE  1 
ATOM   194  C  CZ  . ARG A 1 23  ? 34.423 -33.472 18.107 1.00 59.11  ? 24  ARG A CZ  1 
ATOM   195  N  NH1 . ARG A 1 23  ? 34.645 -33.303 16.806 1.00 42.36  ? 24  ARG A NH1 1 
ATOM   196  N  NH2 . ARG A 1 23  ? 33.696 -34.503 18.514 1.00 48.28  ? 24  ARG A NH2 1 
ATOM   197  N  N   . LEU A 1 24  ? 38.313 -26.570 19.403 1.00 23.01  ? 25  LEU A N   1 
ATOM   198  C  CA  . LEU A 1 24  ? 39.455 -25.666 19.226 1.00 22.22  ? 25  LEU A CA  1 
ATOM   199  C  C   . LEU A 1 24  ? 39.616 -24.790 20.481 1.00 27.50  ? 25  LEU A C   1 
ATOM   200  O  O   . LEU A 1 24  ? 40.742 -24.618 20.972 1.00 27.45  ? 25  LEU A O   1 
ATOM   201  C  CB  . LEU A 1 24  ? 39.271 -24.781 17.994 1.00 21.85  ? 25  LEU A CB  1 
ATOM   202  C  CG  . LEU A 1 24  ? 39.260 -25.482 16.609 1.00 26.31  ? 25  LEU A CG  1 
ATOM   203  C  CD1 . LEU A 1 24  ? 39.137 -24.434 15.493 1.00 26.23  ? 25  LEU A CD1 1 
ATOM   204  C  CD2 . LEU A 1 24  ? 40.525 -26.313 16.396 1.00 27.32  ? 25  LEU A CD2 1 
ATOM   205  N  N   . ARG A 1 25  ? 38.495 -24.250 21.020 1.00 23.63  ? 26  ARG A N   1 
ATOM   206  C  CA  . ARG A 1 25  ? 38.569 -23.458 22.258 1.00 24.42  ? 26  ARG A CA  1 
ATOM   207  C  C   . ARG A 1 25  ? 39.185 -24.268 23.433 1.00 29.12  ? 26  ARG A C   1 
ATOM   208  O  O   . ARG A 1 25  ? 40.069 -23.747 24.130 1.00 29.39  ? 26  ARG A O   1 
ATOM   209  C  CB  . ARG A 1 25  ? 37.179 -22.924 22.652 1.00 24.32  ? 26  ARG A CB  1 
ATOM   210  C  CG  . ARG A 1 25  ? 37.249 -22.072 23.927 1.00 29.75  ? 26  ARG A CG  1 
ATOM   211  C  CD  . ARG A 1 25  ? 35.925 -21.443 24.244 1.00 30.06  ? 26  ARG A CD  1 
ATOM   212  N  NE  . ARG A 1 25  ? 34.922 -22.426 24.642 1.00 30.15  ? 26  ARG A NE  1 
ATOM   213  C  CZ  . ARG A 1 25  ? 34.339 -22.472 25.834 1.00 44.01  ? 26  ARG A CZ  1 
ATOM   214  N  NH1 . ARG A 1 25  ? 34.720 -21.641 26.801 1.00 34.35  ? 26  ARG A NH1 1 
ATOM   215  N  NH2 . ARG A 1 25  ? 33.397 -23.368 26.081 1.00 32.58  ? 26  ARG A NH2 1 
ATOM   216  N  N   A SER A 1 26  ? 38.714 -25.508 23.645 0.40 27.18  ? 27  SER A N   1 
ATOM   217  N  N   B SER A 1 26  ? 38.714 -25.511 23.647 0.35 26.81  ? 27  SER A N   1 
ATOM   218  N  N   C SER A 1 26  ? 38.714 -25.515 23.642 0.25 26.75  ? 27  SER A N   1 
ATOM   219  C  CA  A SER A 1 26  ? 39.193 -26.396 24.711 0.40 28.99  ? 27  SER A CA  1 
ATOM   220  C  CA  B SER A 1 26  ? 39.181 -26.393 24.726 0.35 28.41  ? 27  SER A CA  1 
ATOM   221  C  CA  C SER A 1 26  ? 39.169 -26.422 24.707 0.25 28.28  ? 27  SER A CA  1 
ATOM   222  C  C   A SER A 1 26  ? 40.702 -26.595 24.629 0.40 34.36  ? 27  SER A C   1 
ATOM   223  C  C   B SER A 1 26  ? 40.680 -26.702 24.633 0.35 34.30  ? 27  SER A C   1 
ATOM   224  C  C   C SER A 1 26  ? 40.669 -26.724 24.626 0.25 34.11  ? 27  SER A C   1 
ATOM   225  O  O   A SER A 1 26  ? 41.390 -26.547 25.653 0.40 35.72  ? 27  SER A O   1 
ATOM   226  O  O   B SER A 1 26  ? 41.340 -26.846 25.665 0.35 35.88  ? 27  SER A O   1 
ATOM   227  O  O   C SER A 1 26  ? 41.314 -26.905 25.662 0.25 35.47  ? 27  SER A O   1 
ATOM   228  C  CB  A SER A 1 26  ? 38.515 -27.759 24.612 0.40 33.33  ? 27  SER A CB  1 
ATOM   229  C  CB  B SER A 1 26  ? 38.364 -27.681 24.766 0.35 31.91  ? 27  SER A CB  1 
ATOM   230  C  CB  C SER A 1 26  ? 38.369 -27.721 24.677 0.25 31.85  ? 27  SER A CB  1 
ATOM   231  O  OG  A SER A 1 26  ? 37.117 -27.672 24.818 0.40 42.42  ? 27  SER A OG  1 
ATOM   232  O  OG  B SER A 1 26  ? 38.621 -28.520 23.652 0.35 38.55  ? 27  SER A OG  1 
ATOM   233  O  OG  C SER A 1 26  ? 38.805 -28.631 25.675 0.25 40.59  ? 27  SER A OG  1 
ATOM   234  N  N   . ARG A 1 27  ? 41.214 -26.785 23.402 1.00 30.48  ? 28  ARG A N   1 
ATOM   235  C  CA  . ARG A 1 27  ? 42.638 -27.053 23.153 1.00 32.22  ? 28  ARG A CA  1 
ATOM   236  C  C   . ARG A 1 27  ? 43.444 -25.772 22.957 1.00 34.72  ? 28  ARG A C   1 
ATOM   237  O  O   . ARG A 1 27  ? 44.653 -25.835 22.722 1.00 35.91  ? 28  ARG A O   1 
ATOM   238  C  CB  . ARG A 1 27  ? 42.779 -28.020 21.981 1.00 34.53  ? 28  ARG A CB  1 
ATOM   239  C  CG  . ARG A 1 27  ? 42.007 -29.318 22.206 1.00 43.91  ? 28  ARG A CG  1 
ATOM   240  C  CD  . ARG A 1 27  ? 41.997 -30.190 20.978 1.00 52.92  ? 28  ARG A CD  1 
ATOM   241  N  NE  . ARG A 1 27  ? 43.323 -30.753 20.724 1.00 70.60  ? 28  ARG A NE  1 
ATOM   242  C  CZ  . ARG A 1 27  ? 43.839 -30.915 19.513 1.00 87.80  ? 28  ARG A CZ  1 
ATOM   243  N  NH1 . ARG A 1 27  ? 45.050 -31.432 19.366 1.00 77.86  ? 28  ARG A NH1 1 
ATOM   244  N  NH2 . ARG A 1 27  ? 43.150 -30.558 18.442 1.00 74.80  ? 28  ARG A NH2 1 
ATOM   245  N  N   . ASP A 1 28  ? 42.781 -24.611 23.098 1.00 28.28  ? 29  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 28  ? 43.377 -23.276 22.957 1.00 29.38  ? 29  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 28  ? 43.985 -23.057 21.547 1.00 34.31  ? 29  ASP A C   1 
ATOM   248  O  O   . ASP A 1 28  ? 45.039 -22.434 21.393 1.00 36.22  ? 29  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 28  ? 44.406 -22.998 24.094 1.00 32.74  ? 29  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 28  ? 44.708 -21.526 24.274 1.00 41.32  ? 29  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 28  ? 43.781 -20.701 24.075 1.00 40.27  ? 29  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 28  ? 45.868 -21.196 24.594 1.00 48.33  ? 29  ASP A OD2 1 
ATOM   253  N  N   . ILE A 1 29  ? 43.324 -23.601 20.530 1.00 27.87  ? 30  ILE A N   1 
ATOM   254  C  CA  . ILE A 1 29  ? 43.788 -23.506 19.144 1.00 26.67  ? 30  ILE A CA  1 
ATOM   255  C  C   . ILE A 1 29  ? 43.192 -22.303 18.442 1.00 29.43  ? 30  ILE A C   1 
ATOM   256  O  O   . ILE A 1 29  ? 41.961 -22.184 18.351 1.00 25.93  ? 30  ILE A O   1 
ATOM   257  C  CB  . ILE A 1 29  ? 43.546 -24.816 18.354 1.00 29.29  ? 30  ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 29  ? 44.346 -25.994 18.971 1.00 30.73  ? 30  ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 29  ? 43.881 -24.635 16.848 1.00 28.09  ? 30  ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 29  ? 43.834 -27.383 18.484 1.00 31.57  ? 30  ILE A CD1 1 
ATOM   261  N  N   A LEU A 1 30  ? 44.069 -21.414 17.931 0.54 27.40  ? 31  LEU A N   1 
ATOM   262  N  N   B LEU A 1 30  ? 44.079 -21.417 17.942 0.46 27.47  ? 31  LEU A N   1 
ATOM   263  C  CA  A LEU A 1 30  ? 43.710 -20.212 17.168 0.54 27.05  ? 31  LEU A CA  1 
ATOM   264  C  CA  B LEU A 1 30  ? 43.762 -20.203 17.188 0.46 27.22  ? 31  LEU A CA  1 
ATOM   265  C  C   A LEU A 1 30  ? 42.831 -19.216 17.933 0.54 28.89  ? 31  LEU A C   1 
ATOM   266  C  C   B LEU A 1 30  ? 42.848 -19.219 17.931 0.46 29.08  ? 31  LEU A C   1 
ATOM   267  O  O   A LEU A 1 30  ? 42.201 -18.356 17.310 0.54 27.05  ? 31  LEU A O   1 
ATOM   268  O  O   B LEU A 1 30  ? 42.215 -18.370 17.296 0.46 27.41  ? 31  LEU A O   1 
ATOM   269  C  CB  A LEU A 1 30  ? 43.080 -20.560 15.801 0.54 27.08  ? 31  LEU A CB  1 
ATOM   270  C  CB  B LEU A 1 30  ? 43.218 -20.526 15.791 0.46 27.34  ? 31  LEU A CB  1 
ATOM   271  C  CG  A LEU A 1 30  ? 43.993 -21.202 14.726 0.54 32.87  ? 31  LEU A CG  1 
ATOM   272  C  CG  B LEU A 1 30  ? 44.257 -20.370 14.684 0.46 33.09  ? 31  LEU A CG  1 
ATOM   273  C  CD1 A LEU A 1 30  ? 43.456 -20.920 13.364 0.54 31.60  ? 31  LEU A CD1 1 
ATOM   274  C  CD1 B LEU A 1 30  ? 44.630 -21.711 14.081 0.46 33.58  ? 31  LEU A CD1 1 
ATOM   275  C  CD2 A LEU A 1 30  ? 45.425 -20.677 14.775 0.54 36.64  ? 31  LEU A CD2 1 
ATOM   276  C  CD2 B LEU A 1 30  ? 43.767 -19.422 13.620 0.46 35.17  ? 31  LEU A CD2 1 
ATOM   277  N  N   . THR A 1 31  ? 42.845 -19.279 19.279 1.00 25.42  ? 32  THR A N   1 
ATOM   278  C  CA  . THR A 1 31  ? 42.126 -18.299 20.116 1.00 24.76  ? 32  THR A CA  1 
ATOM   279  C  C   . THR A 1 31  ? 42.934 -17.006 19.919 1.00 30.14  ? 32  THR A C   1 
ATOM   280  O  O   . THR A 1 31  ? 44.164 -17.057 19.778 1.00 30.86  ? 32  THR A O   1 
ATOM   281  C  CB  . THR A 1 31  ? 42.092 -18.720 21.592 1.00 30.26  ? 32  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 31  ? 43.414 -19.075 21.975 1.00 33.19  ? 32  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 31  ? 41.126 -19.888 21.838 1.00 28.94  ? 32  THR A CG2 1 
ATOM   284  N  N   . ASP A 1 32  ? 42.249 -15.887 19.744 1.00 27.36  ? 33  ASP A N   1 
ATOM   285  C  CA  . ASP A 1 32  ? 42.936 -14.641 19.405 1.00 27.92  ? 33  ASP A CA  1 
ATOM   286  C  C   . ASP A 1 32  ? 42.612 -13.494 20.330 1.00 29.58  ? 33  ASP A C   1 
ATOM   287  O  O   . ASP A 1 32  ? 42.948 -12.346 20.029 1.00 29.44  ? 33  ASP A O   1 
ATOM   288  C  CB  . ASP A 1 32  ? 42.629 -14.265 17.946 1.00 29.66  ? 33  ASP A CB  1 
ATOM   289  C  CG  . ASP A 1 32  ? 41.144 -14.289 17.575 1.00 39.05  ? 33  ASP A CG  1 
ATOM   290  O  OD1 . ASP A 1 32  ? 40.293 -14.349 18.497 1.00 35.59  ? 33  ASP A OD1 1 
ATOM   291  O  OD2 . ASP A 1 32  ? 40.837 -14.255 16.370 1.00 49.05  ? 33  ASP A OD2 1 
ATOM   292  N  N   . VAL A 1 33  ? 41.956 -13.786 21.456 1.00 24.51  ? 34  VAL A N   1 
ATOM   293  C  CA  . VAL A 1 33  ? 41.632 -12.733 22.427 1.00 23.91  ? 34  VAL A CA  1 
ATOM   294  C  C   . VAL A 1 33  ? 41.453 -13.324 23.807 1.00 27.29  ? 34  VAL A C   1 
ATOM   295  O  O   . VAL A 1 33  ? 41.037 -14.488 23.944 1.00 27.10  ? 34  VAL A O   1 
ATOM   296  C  CB  . VAL A 1 33  ? 40.365 -11.899 21.987 1.00 26.39  ? 34  VAL A CB  1 
ATOM   297  C  CG1 . VAL A 1 33  ? 39.053 -12.692 22.145 1.00 24.93  ? 34  VAL A CG1 1 
ATOM   298  C  CG2 . VAL A 1 33  ? 40.277 -10.543 22.719 1.00 26.68  ? 34  VAL A CG2 1 
ATOM   299  N  N   A VAL A 1 34  ? 41.749 -12.507 24.827 0.53 24.68  ? 35  VAL A N   1 
ATOM   300  N  N   B VAL A 1 34  ? 41.760 -12.525 24.834 0.47 25.16  ? 35  VAL A N   1 
ATOM   301  C  CA  A VAL A 1 34  ? 41.520 -12.811 26.232 0.53 24.69  ? 35  VAL A CA  1 
ATOM   302  C  CA  B VAL A 1 34  ? 41.490 -12.881 26.216 0.47 25.36  ? 35  VAL A CA  1 
ATOM   303  C  C   A VAL A 1 34  ? 40.456 -11.822 26.715 0.53 27.44  ? 35  VAL A C   1 
ATOM   304  C  C   B VAL A 1 34  ? 40.505 -11.849 26.790 0.47 27.97  ? 35  VAL A C   1 
ATOM   305  O  O   A VAL A 1 34  ? 40.607 -10.611 26.523 0.53 27.61  ? 35  VAL A O   1 
ATOM   306  O  O   B VAL A 1 34  ? 40.724 -10.640 26.671 0.47 28.23  ? 35  VAL A O   1 
ATOM   307  C  CB  A VAL A 1 34  ? 42.817 -12.703 27.082 0.53 29.53  ? 35  VAL A CB  1 
ATOM   308  C  CB  B VAL A 1 34  ? 42.747 -13.156 27.093 0.47 30.62  ? 35  VAL A CB  1 
ATOM   309  C  CG1 A VAL A 1 34  ? 42.535 -12.912 28.570 0.53 29.59  ? 35  VAL A CG1 1 
ATOM   310  C  CG1 B VAL A 1 34  ? 43.595 -11.908 27.309 0.47 31.40  ? 35  VAL A CG1 1 
ATOM   311  C  CG2 A VAL A 1 34  ? 43.871 -13.684 26.599 0.53 30.10  ? 35  VAL A CG2 1 
ATOM   312  C  CG2 B VAL A 1 34  ? 42.364 -13.784 28.428 0.47 30.91  ? 35  VAL A CG2 1 
ATOM   313  N  N   . ILE A 1 35  ? 39.389 -12.335 27.337 1.00 23.48  ? 36  ILE A N   1 
ATOM   314  C  CA  . ILE A 1 35  ? 38.346 -11.506 27.941 1.00 22.77  ? 36  ILE A CA  1 
ATOM   315  C  C   . ILE A 1 35  ? 38.630 -11.547 29.444 1.00 28.11  ? 36  ILE A C   1 
ATOM   316  O  O   . ILE A 1 35  ? 38.652 -12.629 30.043 1.00 27.43  ? 36  ILE A O   1 
ATOM   317  C  CB  . ILE A 1 35  ? 36.899 -11.984 27.621 1.00 24.23  ? 36  ILE A CB  1 
ATOM   318  C  CG1 . ILE A 1 35  ? 36.670 -12.152 26.081 1.00 24.01  ? 36  ILE A CG1 1 
ATOM   319  C  CG2 . ILE A 1 35  ? 35.877 -11.036 28.248 1.00 26.06  ? 36  ILE A CG2 1 
ATOM   320  C  CD1 . ILE A 1 35  ? 36.984 -10.895 25.193 1.00 26.06  ? 36  ILE A CD1 1 
ATOM   321  N  N   . VAL A 1 36  ? 38.862 -10.372 30.028 1.00 24.98  ? 37  VAL A N   1 
ATOM   322  C  CA  . VAL A 1 36  ? 39.174 -10.229 31.456 1.00 25.53  ? 37  VAL A CA  1 
ATOM   323  C  C   . VAL A 1 36  ? 37.911 -9.780  32.187 1.00 30.14  ? 37  VAL A C   1 
ATOM   324  O  O   . VAL A 1 36  ? 37.326 -8.733  31.856 1.00 28.48  ? 37  VAL A O   1 
ATOM   325  C  CB  . VAL A 1 36  ? 40.369 -9.254  31.681 1.00 30.16  ? 37  VAL A CB  1 
ATOM   326  C  CG1 . VAL A 1 36  ? 40.707 -9.104  33.171 1.00 31.06  ? 37  VAL A CG1 1 
ATOM   327  C  CG2 . VAL A 1 36  ? 41.604 -9.718  30.920 1.00 31.00  ? 37  VAL A CG2 1 
ATOM   328  N  N   . VAL A 1 37  ? 37.512 -10.560 33.210 1.00 27.71  ? 38  VAL A N   1 
ATOM   329  C  CA  . VAL A 1 37  ? 36.315 -10.324 34.024 1.00 27.45  ? 38  VAL A CA  1 
ATOM   330  C  C   . VAL A 1 37  ? 36.792 -10.396 35.470 1.00 32.88  ? 38  VAL A C   1 
ATOM   331  O  O   . VAL A 1 37  ? 37.031 -11.493 35.974 1.00 31.00  ? 38  VAL A O   1 
ATOM   332  C  CB  . VAL A 1 37  ? 35.195 -11.352 33.697 1.00 30.22  ? 38  VAL A CB  1 
ATOM   333  C  CG1 . VAL A 1 37  ? 33.879 -10.947 34.351 1.00 30.29  ? 38  VAL A CG1 1 
ATOM   334  C  CG2 . VAL A 1 37  ? 35.013 -11.512 32.179 1.00 28.92  ? 38  VAL A CG2 1 
ATOM   335  N  N   A SER A 1 38  ? 36.690 -9.295  36.243 0.50 32.50  ? 39  SER A N   1 
ATOM   336  N  N   B SER A 1 38  ? 37.318 -9.208  35.870 0.50 29.76  ? 39  SER A N   1 
ATOM   337  C  CA  A SER A 1 38  ? 37.057 -9.295  37.679 0.50 34.30  ? 39  SER A CA  1 
ATOM   338  C  CA  B SER A 1 38  ? 37.998 -8.831  37.101 0.50 30.49  ? 39  SER A CA  1 
ATOM   339  C  C   A SER A 1 38  ? 38.318 -10.169 37.976 0.50 38.95  ? 39  SER A C   1 
ATOM   340  C  C   B SER A 1 38  ? 39.282 -9.645  37.252 0.50 33.54  ? 39  SER A C   1 
ATOM   341  O  O   A SER A 1 38  ? 38.285 -11.023 38.865 0.50 39.23  ? 39  SER A O   1 
ATOM   342  O  O   B SER A 1 38  ? 40.202 -9.420  36.466 0.50 32.13  ? 39  SER A O   1 
ATOM   343  C  CB  A SER A 1 38  ? 35.871 -9.735  38.546 0.50 39.25  ? 39  SER A CB  1 
ATOM   344  C  CB  B SER A 1 38  ? 37.061 -8.879  38.303 0.50 34.74  ? 39  SER A CB  1 
ATOM   345  O  OG  A SER A 1 38  ? 34.782 -8.823  38.501 0.50 50.51  ? 39  SER A OG  1 
ATOM   346  O  OG  B SER A 1 38  ? 36.098 -7.845  38.173 0.50 41.71  ? 39  SER A OG  1 
ATOM   347  N  N   A ARG A 1 39  ? 39.397 -9.982  37.170 0.50 35.35  ? 40  ARG A N   1 
ATOM   348  N  N   B ARG A 1 39  ? 39.346 -10.623 38.174 0.50 30.88  ? 40  ARG A N   1 
ATOM   349  C  CA  A ARG A 1 39  ? 40.682 -10.708 37.229 0.50 36.00  ? 40  ARG A CA  1 
ATOM   350  C  CA  B ARG A 1 39  ? 40.570 -11.417 38.306 0.50 31.93  ? 40  ARG A CA  1 
ATOM   351  C  C   A ARG A 1 39  ? 40.558 -12.241 36.968 0.50 38.97  ? 40  ARG A C   1 
ATOM   352  C  C   B ARG A 1 39  ? 40.696 -12.462 37.162 0.50 36.98  ? 40  ARG A C   1 
ATOM   353  O  O   A ARG A 1 39  ? 41.358 -13.048 37.477 0.50 40.30  ? 40  ARG A O   1 
ATOM   354  O  O   B ARG A 1 39  ? 41.756 -12.553 36.522 0.50 38.04  ? 40  ARG A O   1 
ATOM   355  C  CB  A ARG A 1 39  ? 41.464 -10.425 38.527 0.50 37.77  ? 40  ARG A CB  1 
ATOM   356  C  CB  B ARG A 1 39  ? 40.709 -12.028 39.723 0.50 31.81  ? 40  ARG A CB  1 
ATOM   357  C  CG  A ARG A 1 39  ? 41.945 -8.989  38.678 0.50 48.95  ? 40  ARG A CG  1 
ATOM   358  C  CG  B ARG A 1 39  ? 41.005 -10.973 40.808 0.50 40.04  ? 40  ARG A CG  1 
ATOM   359  C  CD  A ARG A 1 39  ? 43.039 -8.912  39.723 0.50 56.50  ? 40  ARG A CD  1 
ATOM   360  C  CD  B ARG A 1 39  ? 41.345 -11.569 42.167 0.50 39.44  ? 40  ARG A CD  1 
ATOM   361  N  NE  A ARG A 1 39  ? 43.382 -7.535  40.079 0.50 63.60  ? 40  ARG A NE  1 
ATOM   362  N  NE  B ARG A 1 39  ? 41.504 -10.542 43.202 0.50 39.35  ? 40  ARG A NE  1 
ATOM   363  C  CZ  A ARG A 1 39  ? 42.821 -6.853  41.074 0.50 76.43  ? 40  ARG A CZ  1 
ATOM   364  C  CZ  B ARG A 1 39  ? 42.667 -10.013 43.580 0.50 53.00  ? 40  ARG A CZ  1 
ATOM   365  N  NH1 A ARG A 1 39  ? 41.864 -7.404  41.811 0.50 60.36  ? 40  ARG A NH1 1 
ATOM   366  N  NH1 B ARG A 1 39  ? 43.798 -10.391 42.999 0.50 40.20  ? 40  ARG A NH1 1 
ATOM   367  N  NH2 A ARG A 1 39  ? 43.203 -5.609  41.331 0.50 64.43  ? 40  ARG A NH2 1 
ATOM   368  N  NH2 B ARG A 1 39  ? 42.705 -9.097  44.534 0.50 45.01  ? 40  ARG A NH2 1 
ATOM   369  N  N   A GLU A 1 40  ? 39.555 -12.630 36.176 0.50 31.96  ? 41  GLU A N   1 
ATOM   370  N  N   B GLU A 1 40  ? 39.591 -13.151 36.836 0.50 31.09  ? 41  GLU A N   1 
ATOM   371  C  CA  A GLU A 1 40  ? 39.358 -14.001 35.704 0.50 30.90  ? 41  GLU A CA  1 
ATOM   372  C  CA  B GLU A 1 40  ? 39.550 -14.227 35.841 0.50 29.59  ? 41  GLU A CA  1 
ATOM   373  C  C   A GLU A 1 40  ? 39.493 -13.868 34.195 0.50 31.97  ? 41  GLU A C   1 
ATOM   374  C  C   B GLU A 1 40  ? 39.795 -13.786 34.385 0.50 30.95  ? 41  GLU A C   1 
ATOM   375  O  O   A GLU A 1 40  ? 38.917 -12.946 33.609 0.50 28.94  ? 41  GLU A O   1 
ATOM   376  O  O   B GLU A 1 40  ? 39.507 -12.655 34.002 0.50 27.85  ? 41  GLU A O   1 
ATOM   377  C  CB  A GLU A 1 40  ? 37.995 -14.584 36.126 0.50 32.13  ? 41  GLU A CB  1 
ATOM   378  C  CB  B GLU A 1 40  ? 38.232 -15.025 35.948 0.50 30.65  ? 41  GLU A CB  1 
ATOM   379  C  CG  A GLU A 1 40  ? 37.894 -14.804 37.630 0.50 46.13  ? 41  GLU A CG  1 
ATOM   380  C  CG  B GLU A 1 40  ? 37.750 -15.201 37.385 0.50 46.38  ? 41  GLU A CG  1 
ATOM   381  C  CD  A GLU A 1 40  ? 37.844 -16.249 38.087 0.50 80.82  ? 41  GLU A CD  1 
ATOM   382  C  CD  B GLU A 1 40  ? 37.898 -16.563 38.036 0.50 83.23  ? 41  GLU A CD  1 
ATOM   383  O  OE1 A GLU A 1 40  ? 36.806 -16.651 38.660 0.50 83.38  ? 41  GLU A OE1 1 
ATOM   384  O  OE1 B GLU A 1 40  ? 38.951 -17.216 37.850 0.50 85.42  ? 41  GLU A OE1 1 
ATOM   385  O  OE2 A GLU A 1 40  ? 38.845 -16.977 37.886 0.50 81.32  ? 41  GLU A OE2 1 
ATOM   386  O  OE2 B GLU A 1 40  ? 36.959 -16.966 38.762 0.50 84.52  ? 41  GLU A OE2 1 
ATOM   387  N  N   . GLN A 1 41  ? 40.314 -14.726 33.575 1.00 28.39  ? 42  GLN A N   1 
ATOM   388  C  CA  . GLN A 1 41  ? 40.629 -14.573 32.158 1.00 28.13  ? 42  GLN A CA  1 
ATOM   389  C  C   . GLN A 1 41  ? 40.021 -15.687 31.357 1.00 31.05  ? 42  GLN A C   1 
ATOM   390  O  O   . GLN A 1 41  ? 40.078 -16.843 31.782 1.00 31.86  ? 42  GLN A O   1 
ATOM   391  C  CB  . GLN A 1 41  ? 42.158 -14.554 31.979 1.00 31.05  ? 42  GLN A CB  1 
ATOM   392  C  CG  . GLN A 1 41  ? 42.813 -13.311 32.558 1.00 45.97  ? 42  GLN A CG  1 
ATOM   393  C  CD  . GLN A 1 41  ? 44.285 -13.186 32.248 1.00 66.31  ? 42  GLN A CD  1 
ATOM   394  O  OE1 . GLN A 1 41  ? 44.883 -13.978 31.503 1.00 60.08  ? 42  GLN A OE1 1 
ATOM   395  N  NE2 . GLN A 1 41  ? 44.901 -12.169 32.821 1.00 68.75  ? 42  GLN A NE2 1 
ATOM   396  N  N   . PHE A 1 42  ? 39.444 -15.351 30.189 1.00 24.90  ? 43  PHE A N   1 
ATOM   397  C  CA  . PHE A 1 42  ? 38.801 -16.342 29.321 1.00 24.66  ? 43  PHE A CA  1 
ATOM   398  C  C   . PHE A 1 42  ? 39.304 -16.165 27.906 1.00 29.10  ? 43  PHE A C   1 
ATOM   399  O  O   . PHE A 1 42  ? 39.130 -15.097 27.326 1.00 28.87  ? 43  PHE A O   1 
ATOM   400  C  CB  . PHE A 1 42  ? 37.270 -16.163 29.347 1.00 26.15  ? 43  PHE A CB  1 
ATOM   401  C  CG  . PHE A 1 42  ? 36.659 -16.266 30.721 1.00 28.32  ? 43  PHE A CG  1 
ATOM   402  C  CD1 . PHE A 1 42  ? 36.523 -15.139 31.528 1.00 29.96  ? 43  PHE A CD1 1 
ATOM   403  C  CD2 . PHE A 1 42  ? 36.193 -17.486 31.201 1.00 30.09  ? 43  PHE A CD2 1 
ATOM   404  C  CE1 . PHE A 1 42  ? 35.964 -15.235 32.806 1.00 31.98  ? 43  PHE A CE1 1 
ATOM   405  C  CE2 . PHE A 1 42  ? 35.632 -17.581 32.479 1.00 33.41  ? 43  PHE A CE2 1 
ATOM   406  C  CZ  . PHE A 1 42  ? 35.516 -16.455 33.272 1.00 31.30  ? 43  PHE A CZ  1 
ATOM   407  N  N   . ARG A 1 43  ? 39.933 -17.205 27.354 1.00 25.49  ? 44  ARG A N   1 
ATOM   408  C  CA  . ARG A 1 43  ? 40.436 -17.177 25.977 1.00 24.37  ? 44  ARG A CA  1 
ATOM   409  C  C   . ARG A 1 43  ? 39.296 -17.569 25.024 1.00 28.26  ? 44  ARG A C   1 
ATOM   410  O  O   . ARG A 1 43  ? 38.494 -18.462 25.326 1.00 27.59  ? 44  ARG A O   1 
ATOM   411  C  CB  . ARG A 1 43  ? 41.656 -18.115 25.817 1.00 25.99  ? 44  ARG A CB  1 
ATOM   412  C  CG  . ARG A 1 43  ? 42.887 -17.680 26.658 1.00 35.06  ? 44  ARG A CG  1 
ATOM   413  C  CD  . ARG A 1 43  ? 44.211 -18.093 26.008 1.00 46.71  ? 44  ARG A CD  1 
ATOM   414  N  NE  . ARG A 1 43  ? 44.239 -17.687 24.596 1.00 56.68  ? 44  ARG A NE  1 
ATOM   415  C  CZ  . ARG A 1 43  ? 44.831 -16.595 24.122 1.00 68.79  ? 44  ARG A CZ  1 
ATOM   416  N  NH1 . ARG A 1 43  ? 45.551 -15.822 24.921 1.00 61.13  ? 44  ARG A NH1 1 
ATOM   417  N  NH2 . ARG A 1 43  ? 44.753 -16.300 22.833 1.00 52.36  ? 44  ARG A NH2 1 
ATOM   418  N  N   . ALA A 1 44  ? 39.199 -16.900 23.869 1.00 24.28  ? 45  ALA A N   1 
ATOM   419  C  CA  . ALA A 1 44  ? 38.122 -17.212 22.920 1.00 23.92  ? 45  ALA A CA  1 
ATOM   420  C  C   . ALA A 1 44  ? 38.526 -16.805 21.520 1.00 25.09  ? 45  ALA A C   1 
ATOM   421  O  O   . ALA A 1 44  ? 39.619 -16.247 21.317 1.00 24.26  ? 45  ALA A O   1 
ATOM   422  C  CB  . ALA A 1 44  ? 36.832 -16.478 23.321 1.00 24.43  ? 45  ALA A CB  1 
ATOM   423  N  N   . HIS A 1 45  ? 37.634 -17.062 20.565 1.00 21.86  ? 46  HIS A N   1 
ATOM   424  C  CA  . HIS A 1 45  ? 37.804 -16.650 19.180 1.00 20.93  ? 46  HIS A CA  1 
ATOM   425  C  C   . HIS A 1 45  ? 36.915 -15.411 18.993 1.00 24.36  ? 46  HIS A C   1 
ATOM   426  O  O   . HIS A 1 45  ? 35.692 -15.465 19.241 1.00 22.88  ? 46  HIS A O   1 
ATOM   427  C  CB  . HIS A 1 45  ? 37.343 -17.761 18.221 1.00 20.63  ? 46  HIS A CB  1 
ATOM   428  C  CG  . HIS A 1 45  ? 38.081 -19.055 18.419 1.00 24.29  ? 46  HIS A CG  1 
ATOM   429  N  ND1 . HIS A 1 45  ? 37.546 -20.086 19.169 1.00 25.83  ? 46  HIS A ND1 1 
ATOM   430  C  CD2 . HIS A 1 45  ? 39.326 -19.411 18.010 1.00 25.54  ? 46  HIS A CD2 1 
ATOM   431  C  CE1 . HIS A 1 45  ? 38.469 -21.044 19.182 1.00 24.97  ? 46  HIS A CE1 1 
ATOM   432  N  NE2 . HIS A 1 45  ? 39.556 -20.681 18.494 1.00 25.20  ? 46  HIS A NE2 1 
ATOM   433  N  N   . LYS A 1 46  ? 37.518 -14.311 18.555 1.00 22.05  ? 47  LYS A N   1 
ATOM   434  C  CA  . LYS A 1 46  ? 36.776 -13.070 18.264 1.00 22.74  ? 47  LYS A CA  1 
ATOM   435  C  C   . LYS A 1 46  ? 35.543 -13.323 17.389 1.00 24.57  ? 47  LYS A C   1 
ATOM   436  O  O   . LYS A 1 46  ? 34.466 -12.810 17.700 1.00 22.94  ? 47  LYS A O   1 
ATOM   437  C  CB  . LYS A 1 46  ? 37.685 -12.060 17.546 1.00 25.73  ? 47  LYS A CB  1 
ATOM   438  C  CG  . LYS A 1 46  ? 38.713 -11.425 18.468 1.00 26.54  ? 47  LYS A CG  1 
ATOM   439  C  CD  . LYS A 1 46  ? 39.642 -10.507 17.675 1.00 26.74  ? 47  LYS A CD  1 
ATOM   440  C  CE  . LYS A 1 46  ? 40.789 -10.055 18.546 1.00 30.19  ? 47  LYS A CE  1 
ATOM   441  N  NZ  . LYS A 1 46  ? 41.713 -9.139  17.820 1.00 31.70  ? 47  LYS A NZ  1 
ATOM   442  N  N   . THR A 1 47  ? 35.683 -14.118 16.303 1.00 22.07  ? 48  THR A N   1 
ATOM   443  C  CA  . THR A 1 47  ? 34.534 -14.337 15.408 1.00 22.03  ? 48  THR A CA  1 
ATOM   444  C  C   . THR A 1 47  ? 33.356 -14.999 16.086 1.00 23.18  ? 48  THR A C   1 
ATOM   445  O  O   . THR A 1 47  ? 32.226 -14.598 15.821 1.00 21.54  ? 48  THR A O   1 
ATOM   446  C  CB  . THR A 1 47  ? 34.933 -15.069 14.135 1.00 26.48  ? 48  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 47  ? 35.521 -16.305 14.506 1.00 27.53  ? 48  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 47  ? 35.859 -14.205 13.255 1.00 29.75  ? 48  THR A CG2 1 
ATOM   449  N  N   . VAL A 1 48  ? 33.607 -15.962 16.976 1.00 20.34  ? 49  VAL A N   1 
ATOM   450  C  CA  . VAL A 1 48  ? 32.515 -16.649 17.694 1.00 19.77  ? 49  VAL A CA  1 
ATOM   451  C  C   . VAL A 1 48  ? 31.845 -15.650 18.660 1.00 22.65  ? 49  VAL A C   1 
ATOM   452  O  O   . VAL A 1 48  ? 30.607 -15.578 18.738 1.00 21.58  ? 49  VAL A O   1 
ATOM   453  C  CB  . VAL A 1 48  ? 33.015 -17.917 18.437 1.00 21.99  ? 49  VAL A CB  1 
ATOM   454  C  CG1 . VAL A 1 48  ? 31.885 -18.515 19.292 1.00 21.23  ? 49  VAL A CG1 1 
ATOM   455  C  CG2 . VAL A 1 48  ? 33.542 -18.955 17.438 1.00 21.67  ? 49  VAL A CG2 1 
ATOM   456  N  N   . LEU A 1 49  ? 32.676 -14.852 19.383 1.00 19.75  ? 50  LEU A N   1 
ATOM   457  C  CA  . LEU A 1 49  ? 32.131 -13.832 20.299 1.00 20.26  ? 50  LEU A CA  1 
ATOM   458  C  C   . LEU A 1 49  ? 31.229 -12.844 19.535 1.00 22.75  ? 50  LEU A C   1 
ATOM   459  O  O   . LEU A 1 49  ? 30.103 -12.579 19.963 1.00 21.69  ? 50  LEU A O   1 
ATOM   460  C  CB  . LEU A 1 49  ? 33.282 -13.068 20.979 1.00 20.18  ? 50  LEU A CB  1 
ATOM   461  C  CG  . LEU A 1 49  ? 34.194 -13.863 21.933 1.00 22.93  ? 50  LEU A CG  1 
ATOM   462  C  CD1 . LEU A 1 49  ? 35.244 -12.920 22.553 1.00 23.32  ? 50  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A 1 49  ? 33.370 -14.555 23.037 1.00 24.38  ? 50  LEU A CD2 1 
ATOM   464  N  N   . MET A 1 50  ? 31.672 -12.395 18.347 1.00 20.09  ? 51  MET A N   1 
ATOM   465  C  CA  . MET A 1 50  ? 30.885 -11.469 17.505 1.00 20.75  ? 51  MET A CA  1 
ATOM   466  C  C   . MET A 1 50  ? 29.600 -12.108 17.024 1.00 22.74  ? 51  MET A C   1 
ATOM   467  O  O   . MET A 1 50  ? 28.560 -11.457 17.043 1.00 22.64  ? 51  MET A O   1 
ATOM   468  C  CB  . MET A 1 50  ? 31.686 -11.001 16.294 1.00 22.77  ? 51  MET A CB  1 
ATOM   469  C  CG  . MET A 1 50  ? 32.907 -10.200 16.675 1.00 25.64  ? 51  MET A CG  1 
ATOM   470  S  SD  . MET A 1 50  ? 33.935 -10.075 15.213 1.00 29.98  ? 51  MET A SD  1 
ATOM   471  C  CE  . MET A 1 50  ? 33.162 -8.713  14.449 1.00 27.03  ? 51  MET A CE  1 
ATOM   472  N  N   . ALA A 1 51  ? 29.649 -13.398 16.631 1.00 19.50  ? 52  ALA A N   1 
ATOM   473  C  CA  . ALA A 1 51  ? 28.469 -14.113 16.107 1.00 20.11  ? 52  ALA A CA  1 
ATOM   474  C  C   . ALA A 1 51  ? 27.373 -14.297 17.170 1.00 24.05  ? 52  ALA A C   1 
ATOM   475  O  O   . ALA A 1 51  ? 26.208 -14.512 16.824 1.00 23.78  ? 52  ALA A O   1 
ATOM   476  C  CB  . ALA A 1 51  ? 28.905 -15.492 15.575 1.00 20.24  ? 52  ALA A CB  1 
ATOM   477  N  N   . CYS A 1 52  ? 27.758 -14.253 18.457 1.00 20.51  ? 53  CYS A N   1 
ATOM   478  C  CA  . CYS A 1 52  ? 26.861 -14.488 19.591 1.00 21.31  ? 53  CYS A CA  1 
ATOM   479  C  C   . CYS A 1 52  ? 26.416 -13.265 20.370 1.00 24.31  ? 53  CYS A C   1 
ATOM   480  O  O   . CYS A 1 52  ? 25.461 -13.377 21.147 1.00 24.24  ? 53  CYS A O   1 
ATOM   481  C  CB  . CYS A 1 52  ? 27.531 -15.465 20.544 1.00 21.93  ? 53  CYS A CB  1 
ATOM   482  S  SG  . CYS A 1 52  ? 27.828 -17.091 19.836 1.00 24.60  ? 53  CYS A SG  1 
ATOM   483  N  N   . SER A 1 53  ? 27.175 -12.166 20.295 1.00 21.92  ? 54  SER A N   1 
ATOM   484  C  CA  . SER A 1 53  ? 26.957 -11.030 21.182 1.00 21.13  ? 54  SER A CA  1 
ATOM   485  C  C   . SER A 1 53  ? 26.991 -9.706  20.445 1.00 26.22  ? 54  SER A C   1 
ATOM   486  O  O   . SER A 1 53  ? 27.971 -9.423  19.750 1.00 24.08  ? 54  SER A O   1 
ATOM   487  C  CB  . SER A 1 53  ? 28.054 -11.085 22.249 1.00 22.80  ? 54  SER A CB  1 
ATOM   488  O  OG  . SER A 1 53  ? 28.416 -9.831  22.805 1.00 26.08  ? 54  SER A OG  1 
ATOM   489  N  N   . GLY A 1 54  ? 25.946 -8.888  20.633 1.00 25.05  ? 55  GLY A N   1 
ATOM   490  C  CA  . GLY A 1 54  ? 25.890 -7.552  20.048 1.00 24.98  ? 55  GLY A CA  1 
ATOM   491  C  C   . GLY A 1 54  ? 27.007 -6.663  20.557 1.00 27.21  ? 55  GLY A C   1 
ATOM   492  O  O   . GLY A 1 54  ? 27.532 -5.829  19.806 1.00 26.34  ? 55  GLY A O   1 
ATOM   493  N  N   . LEU A 1 55  ? 27.420 -6.865  21.836 1.00 24.04  ? 56  LEU A N   1 
ATOM   494  C  CA  . LEU A 1 55  ? 28.525 -6.076  22.402 1.00 23.58  ? 56  LEU A CA  1 
ATOM   495  C  C   . LEU A 1 55  ? 29.855 -6.410  21.700 1.00 25.59  ? 56  LEU A C   1 
ATOM   496  O  O   . LEU A 1 55  ? 30.556 -5.493  21.252 1.00 24.74  ? 56  LEU A O   1 
ATOM   497  C  CB  . LEU A 1 55  ? 28.651 -6.289  23.929 1.00 22.89  ? 56  LEU A CB  1 
ATOM   498  C  CG  . LEU A 1 55  ? 29.688 -5.356  24.606 1.00 27.88  ? 56  LEU A CG  1 
ATOM   499  C  CD1 . LEU A 1 55  ? 29.215 -3.874  24.603 1.00 29.30  ? 56  LEU A CD1 1 
ATOM   500  C  CD2 . LEU A 1 55  ? 30.016 -5.835  26.005 1.00 30.42  ? 56  LEU A CD2 1 
ATOM   501  N  N   . PHE A 1 56  ? 30.188 -7.707  21.591 1.00 21.84  ? 57  PHE A N   1 
ATOM   502  C  CA  . PHE A 1 56  ? 31.441 -8.102  20.934 1.00 21.01  ? 57  PHE A CA  1 
ATOM   503  C  C   . PHE A 1 56  ? 31.419 -7.784  19.462 1.00 25.26  ? 57  PHE A C   1 
ATOM   504  O  O   . PHE A 1 56  ? 32.450 -7.427  18.916 1.00 23.99  ? 57  PHE A O   1 
ATOM   505  C  CB  . PHE A 1 56  ? 31.805 -9.566  21.200 1.00 21.68  ? 57  PHE A CB  1 
ATOM   506  C  CG  . PHE A 1 56  ? 32.245 -9.810  22.628 1.00 22.19  ? 57  PHE A CG  1 
ATOM   507  C  CD1 . PHE A 1 56  ? 33.336 -9.123  23.170 1.00 24.09  ? 57  PHE A CD1 1 
ATOM   508  C  CD2 . PHE A 1 56  ? 31.596 -10.756 23.423 1.00 23.66  ? 57  PHE A CD2 1 
ATOM   509  C  CE1 . PHE A 1 56  ? 33.719 -9.318  24.508 1.00 24.89  ? 57  PHE A CE1 1 
ATOM   510  C  CE2 . PHE A 1 56  ? 32.017 -10.992 24.743 1.00 26.06  ? 57  PHE A CE2 1 
ATOM   511  C  CZ  . PHE A 1 56  ? 33.064 -10.255 25.283 1.00 23.14  ? 57  PHE A CZ  1 
ATOM   512  N  N   . TYR A 1 57  ? 30.235 -7.852  18.828 1.00 22.59  ? 58  TYR A N   1 
ATOM   513  C  CA  . TYR A 1 57  ? 30.129 -7.467  17.420 1.00 23.11  ? 58  TYR A CA  1 
ATOM   514  C  C   . TYR A 1 57  ? 30.560 -5.986  17.266 1.00 27.97  ? 58  TYR A C   1 
ATOM   515  O  O   . TYR A 1 57  ? 31.358 -5.666  16.386 1.00 27.30  ? 58  TYR A O   1 
ATOM   516  C  CB  . TYR A 1 57  ? 28.695 -7.676  16.939 1.00 25.29  ? 58  TYR A CB  1 
ATOM   517  C  CG  . TYR A 1 57  ? 28.475 -7.179  15.534 1.00 29.40  ? 58  TYR A CG  1 
ATOM   518  C  CD1 . TYR A 1 57  ? 29.065 -7.818  14.448 1.00 30.94  ? 58  TYR A CD1 1 
ATOM   519  C  CD2 . TYR A 1 57  ? 27.701 -6.051  15.291 1.00 34.47  ? 58  TYR A CD2 1 
ATOM   520  C  CE1 . TYR A 1 57  ? 28.867 -7.356  13.145 1.00 32.84  ? 58  TYR A CE1 1 
ATOM   521  C  CE2 . TYR A 1 57  ? 27.496 -5.583  14.000 1.00 37.80  ? 58  TYR A CE2 1 
ATOM   522  C  CZ  . TYR A 1 57  ? 28.068 -6.248  12.933 1.00 44.36  ? 58  TYR A CZ  1 
ATOM   523  O  OH  . TYR A 1 57  ? 27.848 -5.761  11.679 1.00 50.31  ? 58  TYR A OH  1 
ATOM   524  N  N   A SER A 1 58  ? 30.038 -5.104  18.132 0.52 25.91  ? 59  SER A N   1 
ATOM   525  N  N   B SER A 1 58  ? 30.032 -5.109  18.130 0.48 26.10  ? 59  SER A N   1 
ATOM   526  C  CA  A SER A 1 58  ? 30.365 -3.675  18.134 0.52 26.95  ? 59  SER A CA  1 
ATOM   527  C  CA  B SER A 1 58  ? 30.358 -3.685  18.135 0.48 27.27  ? 59  SER A CA  1 
ATOM   528  C  C   A SER A 1 58  ? 31.850 -3.435  18.436 0.52 32.00  ? 59  SER A C   1 
ATOM   529  C  C   B SER A 1 58  ? 31.854 -3.468  18.407 0.48 31.94  ? 59  SER A C   1 
ATOM   530  O  O   A SER A 1 58  ? 32.478 -2.623  17.760 0.52 33.18  ? 59  SER A O   1 
ATOM   531  O  O   B SER A 1 58  ? 32.493 -2.712  17.677 0.48 32.86  ? 59  SER A O   1 
ATOM   532  C  CB  A SER A 1 58  ? 29.483 -2.934  19.135 0.52 29.74  ? 59  SER A CB  1 
ATOM   533  C  CB  B SER A 1 58  ? 29.512 -2.954  19.175 0.48 30.73  ? 59  SER A CB  1 
ATOM   534  O  OG  A SER A 1 58  ? 28.151 -2.882  18.656 0.52 31.65  ? 59  SER A OG  1 
ATOM   535  O  OG  B SER A 1 58  ? 29.861 -1.582  19.218 0.48 36.59  ? 59  SER A OG  1 
ATOM   536  N  N   . ILE A 1 59  ? 32.410 -4.160  19.427 1.00 27.97  ? 60  ILE A N   1 
ATOM   537  C  CA  . ILE A 1 59  ? 33.827 -4.048  19.827 1.00 27.66  ? 60  ILE A CA  1 
ATOM   538  C  C   . ILE A 1 59  ? 34.777 -4.426  18.689 1.00 30.61  ? 60  ILE A C   1 
ATOM   539  O  O   . ILE A 1 59  ? 35.693 -3.653  18.375 1.00 31.32  ? 60  ILE A O   1 
ATOM   540  C  CB  . ILE A 1 59  ? 34.149 -4.884  21.127 1.00 29.53  ? 60  ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 59  ? 33.428 -4.324  22.369 1.00 29.37  ? 60  ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 59  ? 35.681 -4.993  21.379 1.00 28.06  ? 60  ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 59  ? 33.425 -5.307  23.582 1.00 32.91  ? 60  ILE A CD1 1 
ATOM   544  N  N   . PHE A 1 60  ? 34.587 -5.615  18.098 1.00 26.40  ? 61  PHE A N   1 
ATOM   545  C  CA  . PHE A 1 60  ? 35.548 -6.086  17.106 1.00 26.24  ? 61  PHE A CA  1 
ATOM   546  C  C   . PHE A 1 60  ? 35.312 -5.532  15.691 1.00 29.99  ? 61  PHE A C   1 
ATOM   547  O  O   . PHE A 1 60  ? 36.162 -5.753  14.833 1.00 30.61  ? 61  PHE A O   1 
ATOM   548  C  CB  . PHE A 1 60  ? 35.660 -7.625  17.151 1.00 26.19  ? 61  PHE A CB  1 
ATOM   549  C  CG  . PHE A 1 60  ? 36.114 -8.119  18.515 1.00 26.36  ? 61  PHE A CG  1 
ATOM   550  C  CD1 . PHE A 1 60  ? 37.313 -7.674  19.075 1.00 29.31  ? 61  PHE A CD1 1 
ATOM   551  C  CD2 . PHE A 1 60  ? 35.328 -8.995  19.250 1.00 27.76  ? 61  PHE A CD2 1 
ATOM   552  C  CE1 . PHE A 1 60  ? 37.722 -8.117  20.343 1.00 29.99  ? 61  PHE A CE1 1 
ATOM   553  C  CE2 . PHE A 1 60  ? 35.742 -9.449  20.514 1.00 30.46  ? 61  PHE A CE2 1 
ATOM   554  C  CZ  . PHE A 1 60  ? 36.926 -8.998  21.057 1.00 28.63  ? 61  PHE A CZ  1 
ATOM   555  N  N   . THR A 1 61  ? 34.259 -4.717  15.469 1.00 27.40  ? 62  THR A N   1 
ATOM   556  C  CA  . THR A 1 61  ? 34.098 -4.025  14.180 1.00 28.19  ? 62  THR A CA  1 
ATOM   557  C  C   . THR A 1 61  ? 34.642 -2.602  14.307 1.00 35.27  ? 62  THR A C   1 
ATOM   558  O  O   . THR A 1 61  ? 34.715 -1.869  13.316 1.00 35.75  ? 62  THR A O   1 
ATOM   559  C  CB  . THR A 1 61  ? 32.673 -4.063  13.622 1.00 34.96  ? 62  THR A CB  1 
ATOM   560  O  OG1 . THR A 1 61  ? 31.772 -3.555  14.596 1.00 32.77  ? 62  THR A OG1 1 
ATOM   561  C  CG2 . THR A 1 61  ? 32.258 -5.460  13.124 1.00 30.49  ? 62  THR A CG2 1 
ATOM   562  N  N   . ASP A 1 62  ? 35.071 -2.222  15.521 1.00 31.37  ? 63  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 62  ? 35.675 -0.910  15.729 1.00 32.62  ? 63  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 62  ? 37.101 -0.985  15.197 1.00 39.44  ? 63  ASP A C   1 
ATOM   565  O  O   . ASP A 1 62  ? 37.834 -1.889  15.584 1.00 37.92  ? 63  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 62  ? 35.666 -0.521  17.216 1.00 33.25  ? 63  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 62  ? 36.433 0.760   17.429 1.00 46.81  ? 63  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 62  ? 35.840 1.834   17.246 1.00 51.59  ? 63  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 62  ? 37.658 0.682   17.693 1.00 48.27  ? 63  ASP A OD2 1 
ATOM   570  N  N   . GLN A 1 63  ? 37.506 -0.006  14.354 1.00 40.48  ? 64  GLN A N   1 
ATOM   571  C  CA  . GLN A 1 63  ? 38.815 0.035   13.703 1.00 42.12  ? 64  GLN A CA  1 
ATOM   572  C  C   . GLN A 1 63  ? 40.010 -0.029  14.662 1.00 46.64  ? 64  GLN A C   1 
ATOM   573  O  O   . GLN A 1 63  ? 41.045 -0.556  14.259 1.00 48.47  ? 64  GLN A O   1 
ATOM   574  C  CB  . GLN A 1 63  ? 38.936 1.240   12.760 1.00 46.01  ? 64  GLN A CB  1 
ATOM   575  C  CG  . GLN A 1 63  ? 38.102 1.100   11.489 1.00 67.20  ? 64  GLN A CG  1 
ATOM   576  N  N   . LEU A 1 64  ? 39.886 0.493   15.913 1.00 39.81  ? 65  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 64  ? 40.979 0.410   16.892 1.00 38.74  ? 65  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 64  ? 40.896 -0.845  17.746 1.00 41.61  ? 65  LEU A C   1 
ATOM   579  O  O   . LEU A 1 64  ? 41.924 -1.450  18.035 1.00 43.53  ? 65  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 64  ? 40.999 1.626   17.842 1.00 39.80  ? 65  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 64  ? 41.647 2.906   17.357 1.00 47.01  ? 65  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 64  ? 41.451 3.998   18.377 1.00 47.65  ? 65  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 64  ? 43.142 2.724   17.083 1.00 51.70  ? 65  LEU A CD2 1 
ATOM   584  N  N   . LYS A 1 65  ? 39.690 -1.193  18.228 1.00 33.95  ? 66  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 65  ? 39.529 -2.316  19.151 1.00 32.78  ? 66  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 65  ? 39.655 -3.677  18.485 1.00 37.86  ? 66  LYS A C   1 
ATOM   587  O  O   . LYS A 1 65  ? 40.008 -4.636  19.170 1.00 36.18  ? 66  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 65  ? 38.211 -2.216  19.941 1.00 33.71  ? 66  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 65  ? 38.097 -0.952  20.793 1.00 33.02  ? 66  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 65  ? 36.827 -1.035  21.629 1.00 31.07  ? 66  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 65  ? 36.529 0.273   22.329 1.00 37.44  ? 66  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 65  ? 35.898 1.265   21.432 1.00 37.53  ? 66  LYS A NZ  1 
ATOM   593  N  N   . CYS A 1 66  ? 39.391 -3.762  17.157 1.00 37.86  ? 67  CYS A N   1 
ATOM   594  C  CA  . CYS A 1 66  ? 39.486 -5.020  16.389 1.00 38.05  ? 67  CYS A CA  1 
ATOM   595  C  C   . CYS A 1 66  ? 40.877 -5.659  16.521 1.00 42.76  ? 67  CYS A C   1 
ATOM   596  O  O   . CYS A 1 66  ? 41.006 -6.872  16.347 1.00 43.01  ? 67  CYS A O   1 
ATOM   597  C  CB  . CYS A 1 66  ? 39.114 -4.802  14.922 1.00 39.89  ? 67  CYS A CB  1 
ATOM   598  S  SG  . CYS A 1 66  ? 40.292 -3.782  13.984 1.00 46.22  ? 67  CYS A SG  1 
ATOM   599  N  N   . ASN A 1 67  ? 41.905 -4.822  16.808 1.00 38.98  ? 68  ASN A N   1 
ATOM   600  C  CA  . ASN A 1 67  ? 43.311 -5.194  16.947 1.00 40.10  ? 68  ASN A CA  1 
ATOM   601  C  C   . ASN A 1 67  ? 43.775 -5.493  18.379 1.00 42.84  ? 68  ASN A C   1 
ATOM   602  O  O   . ASN A 1 67  ? 44.942 -5.840  18.585 1.00 42.16  ? 68  ASN A O   1 
ATOM   603  C  CB  . ASN A 1 67  ? 44.200 -4.117  16.303 1.00 41.62  ? 68  ASN A CB  1 
ATOM   604  C  CG  . ASN A 1 67  ? 44.028 -4.069  14.796 1.00 57.84  ? 68  ASN A CG  1 
ATOM   605  O  OD1 . ASN A 1 67  ? 44.031 -3.003  14.184 1.00 59.32  ? 68  ASN A OD1 1 
ATOM   606  N  ND2 . ASN A 1 67  ? 43.834 -5.224  14.162 1.00 46.71  ? 68  ASN A ND2 1 
ATOM   607  N  N   . LEU A 1 68  ? 42.876 -5.380  19.358 1.00 38.62  ? 69  LEU A N   1 
ATOM   608  C  CA  . LEU A 1 68  ? 43.250 -5.644  20.743 1.00 37.69  ? 69  LEU A CA  1 
ATOM   609  C  C   . LEU A 1 68  ? 43.239 -7.147  21.022 1.00 38.35  ? 69  LEU A C   1 
ATOM   610  O  O   . LEU A 1 68  ? 42.340 -7.849  20.537 1.00 35.88  ? 69  LEU A O   1 
ATOM   611  C  CB  . LEU A 1 68  ? 42.285 -4.925  21.709 1.00 37.74  ? 69  LEU A CB  1 
ATOM   612  C  CG  . LEU A 1 68  ? 42.314 -3.385  21.697 1.00 42.68  ? 69  LEU A CG  1 
ATOM   613  C  CD1 . LEU A 1 68  ? 41.260 -2.832  22.624 1.00 42.39  ? 69  LEU A CD1 1 
ATOM   614  C  CD2 . LEU A 1 68  ? 43.706 -2.833  22.079 1.00 43.97  ? 69  LEU A CD2 1 
ATOM   615  N  N   . SER A 1 69  ? 44.230 -7.620  21.813 1.00 34.44  ? 70  SER A N   1 
ATOM   616  C  CA  A SER A 1 69  ? 44.367 -9.025  22.213 0.42 33.94  ? 70  SER A CA  1 
ATOM   617  C  CA  B SER A 1 69  ? 44.319 -9.035  22.189 0.58 34.26  ? 70  SER A CA  1 
ATOM   618  C  C   . SER A 1 69  ? 43.719 -9.242  23.588 1.00 35.23  ? 70  SER A C   1 
ATOM   619  O  O   . SER A 1 69  ? 43.530 -10.376 24.021 1.00 31.87  ? 70  SER A O   1 
ATOM   620  C  CB  A SER A 1 69  ? 45.843 -9.412  22.269 0.42 38.67  ? 70  SER A CB  1 
ATOM   621  C  CB  B SER A 1 69  ? 45.767 -9.520  22.136 0.58 39.47  ? 70  SER A CB  1 
ATOM   622  O  OG  A SER A 1 69  ? 46.433 -9.376  20.980 0.42 45.54  ? 70  SER A OG  1 
ATOM   623  O  OG  B SER A 1 69  ? 46.590 -8.794  23.031 0.58 46.83  ? 70  SER A OG  1 
ATOM   624  N  N   . VAL A 1 70  ? 43.425 -8.139  24.298 1.00 31.83  ? 71  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 70  ? 42.821 -8.172  25.638 1.00 30.89  ? 71  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 70  ? 41.645 -7.197  25.691 1.00 32.51  ? 71  VAL A C   1 
ATOM   627  O  O   . VAL A 1 70  ? 41.798 -6.029  25.307 1.00 31.85  ? 71  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 70  ? 43.867 -7.838  26.745 1.00 36.84  ? 71  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 70  ? 43.241 -7.856  28.142 1.00 36.88  ? 71  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 70  ? 45.079 -8.768  26.681 1.00 37.64  ? 71  VAL A CG2 1 
ATOM   631  N  N   . ILE A 1 71  ? 40.488 -7.675  26.191 1.00 26.39  ? 72  ILE A N   1 
ATOM   632  C  CA  . ILE A 1 71  ? 39.287 -6.867  26.397 1.00 25.60  ? 72  ILE A CA  1 
ATOM   633  C  C   . ILE A 1 71  ? 38.896 -6.961  27.873 1.00 29.09  ? 72  ILE A C   1 
ATOM   634  O  O   . ILE A 1 71  ? 38.676 -8.061  28.386 1.00 28.19  ? 72  ILE A O   1 
ATOM   635  C  CB  . ILE A 1 71  ? 38.110 -7.239  25.437 1.00 27.17  ? 72  ILE A CB  1 
ATOM   636  C  CG1 . ILE A 1 71  ? 38.495 -7.102  23.920 1.00 28.37  ? 72  ILE A CG1 1 
ATOM   637  C  CG2 . ILE A 1 71  ? 36.818 -6.451  25.771 1.00 28.66  ? 72  ILE A CG2 1 
ATOM   638  C  CD1 . ILE A 1 71  ? 38.889 -5.651  23.404 1.00 32.42  ? 72  ILE A CD1 1 
ATOM   639  N  N   . ASN A 1 72  ? 38.764 -5.813  28.542 1.00 26.73  ? 73  ASN A N   1 
ATOM   640  C  CA  . ASN A 1 72  ? 38.364 -5.788  29.943 1.00 26.51  ? 73  ASN A CA  1 
ATOM   641  C  C   . ASN A 1 72  ? 36.885 -5.460  30.051 1.00 29.47  ? 73  ASN A C   1 
ATOM   642  O  O   . ASN A 1 72  ? 36.458 -4.383  29.616 1.00 28.24  ? 73  ASN A O   1 
ATOM   643  C  CB  . ASN A 1 72  ? 39.190 -4.736  30.732 1.00 30.29  ? 73  ASN A CB  1 
ATOM   644  C  CG  . ASN A 1 72  ? 40.670 -4.956  30.678 1.00 49.20  ? 73  ASN A CG  1 
ATOM   645  O  OD1 . ASN A 1 72  ? 41.181 -5.991  31.081 1.00 39.77  ? 73  ASN A OD1 1 
ATOM   646  N  ND2 . ASN A 1 72  ? 41.396 -3.980  30.188 1.00 45.71  ? 73  ASN A ND2 1 
ATOM   647  N  N   . LEU A 1 73  ? 36.109 -6.354  30.666 1.00 24.66  ? 74  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 73  ? 34.690 -6.090  30.864 1.00 24.26  ? 74  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 73  ? 34.453 -5.199  32.090 1.00 28.25  ? 74  LEU A C   1 
ATOM   650  O  O   . LEU A 1 73  ? 35.334 -5.060  32.952 1.00 28.69  ? 74  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 73  ? 33.889 -7.394  30.976 1.00 23.90  ? 74  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 73  ? 33.969 -8.384  29.794 1.00 26.85  ? 74  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 73  ? 32.853 -9.442  29.928 1.00 26.00  ? 74  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 73  ? 33.893 -7.682  28.426 1.00 26.93  ? 74  LEU A CD2 1 
ATOM   655  N  N   . ASP A 1 74  ? 33.266 -4.586  32.150 1.00 24.79  ? 75  ASP A N   1 
ATOM   656  C  CA  . ASP A 1 74  ? 32.840 -3.707  33.243 1.00 26.89  ? 75  ASP A CA  1 
ATOM   657  C  C   . ASP A 1 74  ? 33.024 -4.456  34.583 1.00 31.82  ? 75  ASP A C   1 
ATOM   658  O  O   . ASP A 1 74  ? 32.682 -5.637  34.656 1.00 29.72  ? 75  ASP A O   1 
ATOM   659  C  CB  . ASP A 1 74  ? 31.363 -3.319  33.038 1.00 28.72  ? 75  ASP A CB  1 
ATOM   660  C  CG  . ASP A 1 74  ? 30.835 -2.295  34.030 1.00 40.59  ? 75  ASP A CG  1 
ATOM   661  O  OD1 . ASP A 1 74  ? 30.671 -2.646  35.220 1.00 41.92  ? 75  ASP A OD1 1 
ATOM   662  O  OD2 . ASP A 1 74  ? 30.555 -1.161  33.613 1.00 43.38  ? 75  ASP A OD2 1 
ATOM   663  N  N   . PRO A 1 75  ? 33.602 -3.813  35.622 1.00 32.37  ? 76  PRO A N   1 
ATOM   664  C  CA  . PRO A 1 75  ? 33.815 -4.525  36.904 1.00 32.93  ? 76  PRO A CA  1 
ATOM   665  C  C   . PRO A 1 75  ? 32.574 -5.106  37.571 1.00 36.13  ? 76  PRO A C   1 
ATOM   666  O  O   . PRO A 1 75  ? 32.723 -5.991  38.407 1.00 37.37  ? 76  PRO A O   1 
ATOM   667  C  CB  . PRO A 1 75  ? 34.495 -3.484  37.801 1.00 35.99  ? 76  PRO A CB  1 
ATOM   668  C  CG  . PRO A 1 75  ? 34.218 -2.162  37.162 1.00 40.38  ? 76  PRO A CG  1 
ATOM   669  C  CD  . PRO A 1 75  ? 34.101 -2.419  35.688 1.00 34.17  ? 76  PRO A CD  1 
ATOM   670  N  N   . GLU A 1 76  ? 31.363 -4.661  37.198 1.00 32.38  ? 77  GLU A N   1 
ATOM   671  C  CA  . GLU A 1 76  ? 30.125 -5.200  37.767 1.00 34.04  ? 77  GLU A CA  1 
ATOM   672  C  C   . GLU A 1 76  ? 29.825 -6.602  37.215 1.00 34.56  ? 77  GLU A C   1 
ATOM   673  O  O   . GLU A 1 76  ? 28.973 -7.301  37.763 1.00 34.18  ? 77  GLU A O   1 
ATOM   674  C  CB  . GLU A 1 76  ? 28.933 -4.267  37.491 1.00 36.92  ? 77  GLU A CB  1 
ATOM   675  C  CG  . GLU A 1 76  ? 28.896 -3.027  38.372 1.00 57.05  ? 77  GLU A CG  1 
ATOM   676  C  CD  . GLU A 1 76  ? 28.391 -3.273  39.781 1.00 90.55  ? 77  GLU A CD  1 
ATOM   677  O  OE1 . GLU A 1 76  ? 27.163 -3.453  39.951 1.00 91.92  ? 77  GLU A OE1 1 
ATOM   678  O  OE2 . GLU A 1 76  ? 29.226 -3.297  40.715 1.00 89.60  ? 77  GLU A OE2 1 
ATOM   679  N  N   . ILE A 1 77  ? 30.493 -7.001  36.117 1.00 28.84  ? 78  ILE A N   1 
ATOM   680  C  CA  . ILE A 1 77  ? 30.243 -8.316  35.521 1.00 27.56  ? 78  ILE A CA  1 
ATOM   681  C  C   . ILE A 1 77  ? 30.837 -9.424  36.367 1.00 32.14  ? 78  ILE A C   1 
ATOM   682  O  O   . ILE A 1 77  ? 32.018 -9.406  36.698 1.00 30.54  ? 78  ILE A O   1 
ATOM   683  C  CB  . ILE A 1 77  ? 30.688 -8.388  34.030 1.00 29.60  ? 78  ILE A CB  1 
ATOM   684  C  CG1 . ILE A 1 77  ? 29.979 -7.285  33.185 1.00 30.78  ? 78  ILE A CG1 1 
ATOM   685  C  CG2 . ILE A 1 77  ? 30.475 -9.800  33.441 1.00 26.39  ? 78  ILE A CG2 1 
ATOM   686  C  CD1 . ILE A 1 77  ? 28.348 -7.312  33.223 1.00 37.34  ? 78  ILE A CD1 1 
ATOM   687  N  N   . ASN A 1 78  ? 30.006 -10.410 36.645 1.00 31.48  ? 79  ASN A N   1 
ATOM   688  C  CA  . ASN A 1 78  ? 30.325 -11.592 37.420 1.00 31.91  ? 79  ASN A CA  1 
ATOM   689  C  C   . ASN A 1 78  ? 31.060 -12.631 36.549 1.00 31.11  ? 79  ASN A C   1 
ATOM   690  O  O   . ASN A 1 78  ? 30.540 -13.014 35.498 1.00 27.77  ? 79  ASN A O   1 
ATOM   691  C  CB  . ASN A 1 78  ? 29.012 -12.161 37.992 1.00 36.33  ? 79  ASN A CB  1 
ATOM   692  C  CG  . ASN A 1 78  ? 29.187 -13.451 38.737 1.00 52.94  ? 79  ASN A CG  1 
ATOM   693  O  OD1 . ASN A 1 78  ? 28.829 -14.513 38.241 1.00 40.78  ? 79  ASN A OD1 1 
ATOM   694  N  ND2 . ASN A 1 78  ? 29.748 -13.382 39.938 1.00 46.02  ? 79  ASN A ND2 1 
ATOM   695  N  N   . PRO A 1 79  ? 32.260 -13.116 36.961 1.00 29.72  ? 80  PRO A N   1 
ATOM   696  C  CA  . PRO A 1 79  ? 32.971 -14.123 36.144 1.00 28.93  ? 80  PRO A CA  1 
ATOM   697  C  C   . PRO A 1 79  ? 32.180 -15.409 35.894 1.00 32.22  ? 80  PRO A C   1 
ATOM   698  O  O   . PRO A 1 79  ? 32.251 -15.946 34.789 1.00 30.80  ? 80  PRO A O   1 
ATOM   699  C  CB  . PRO A 1 79  ? 34.237 -14.407 36.954 1.00 32.05  ? 80  PRO A CB  1 
ATOM   700  C  CG  . PRO A 1 79  ? 34.420 -13.182 37.809 1.00 37.04  ? 80  PRO A CG  1 
ATOM   701  C  CD  . PRO A 1 79  ? 33.038 -12.765 38.170 1.00 32.66  ? 80  PRO A CD  1 
ATOM   702  N  N   . GLU A 1 80  ? 31.427 -15.900 36.892 1.00 29.68  ? 81  GLU A N   1 
ATOM   703  C  CA  . GLU A 1 80  ? 30.650 -17.134 36.682 1.00 29.22  ? 81  GLU A CA  1 
ATOM   704  C  C   . GLU A 1 80  ? 29.564 -16.937 35.602 1.00 30.50  ? 81  GLU A C   1 
ATOM   705  O  O   . GLU A 1 80  ? 29.432 -17.785 34.724 1.00 28.74  ? 81  GLU A O   1 
ATOM   706  C  CB  . GLU A 1 80  ? 30.044 -17.652 37.996 1.00 32.15  ? 81  GLU A CB  1 
ATOM   707  C  CG  . GLU A 1 80  ? 29.426 -19.036 37.813 1.00 43.57  ? 81  GLU A CG  1 
ATOM   708  C  CD  . GLU A 1 80  ? 28.565 -19.578 38.941 1.00 71.63  ? 81  GLU A CD  1 
ATOM   709  O  OE1 . GLU A 1 80  ? 28.545 -20.817 39.115 1.00 69.09  ? 81  GLU A OE1 1 
ATOM   710  O  OE2 . GLU A 1 80  ? 27.900 -18.776 39.638 1.00 66.99  ? 81  GLU A OE2 1 
ATOM   711  N  N   . GLY A 1 81  ? 28.838 -15.811 35.665 1.00 28.30  ? 82  GLY A N   1 
ATOM   712  C  CA  . GLY A 1 81  ? 27.828 -15.464 34.670 1.00 27.37  ? 82  GLY A CA  1 
ATOM   713  C  C   . GLY A 1 81  ? 28.459 -15.400 33.287 1.00 28.95  ? 82  GLY A C   1 
ATOM   714  O  O   . GLY A 1 81  ? 27.907 -15.940 32.318 1.00 27.25  ? 82  GLY A O   1 
ATOM   715  N  N   . PHE A 1 82  ? 29.658 -14.786 33.190 1.00 23.96  ? 83  PHE A N   1 
ATOM   716  C  CA  . PHE A 1 82  ? 30.344 -14.734 31.894 1.00 22.35  ? 83  PHE A CA  1 
ATOM   717  C  C   . PHE A 1 82  ? 30.706 -16.144 31.421 1.00 25.93  ? 83  PHE A C   1 
ATOM   718  O  O   . PHE A 1 82  ? 30.505 -16.456 30.258 1.00 24.10  ? 83  PHE A O   1 
ATOM   719  C  CB  . PHE A 1 82  ? 31.619 -13.867 31.938 1.00 23.87  ? 83  PHE A CB  1 
ATOM   720  C  CG  . PHE A 1 82  ? 32.211 -13.746 30.549 1.00 24.26  ? 83  PHE A CG  1 
ATOM   721  C  CD1 . PHE A 1 82  ? 31.641 -12.895 29.602 1.00 26.60  ? 83  PHE A CD1 1 
ATOM   722  C  CD2 . PHE A 1 82  ? 33.292 -14.532 30.164 1.00 24.75  ? 83  PHE A CD2 1 
ATOM   723  C  CE1 . PHE A 1 82  ? 32.148 -12.830 28.297 1.00 26.76  ? 83  PHE A CE1 1 
ATOM   724  C  CE2 . PHE A 1 82  ? 33.805 -14.458 28.868 1.00 26.38  ? 83  PHE A CE2 1 
ATOM   725  C  CZ  . PHE A 1 82  ? 33.230 -13.611 27.942 1.00 25.85  ? 83  PHE A CZ  1 
ATOM   726  N  N   . CYS A 1 83  ? 31.289 -16.956 32.300 1.00 26.15  ? 84  CYS A N   1 
ATOM   727  C  CA  . CYS A 1 83  ? 31.705 -18.328 31.978 1.00 27.62  ? 84  CYS A CA  1 
ATOM   728  C  C   . CYS A 1 83  ? 30.518 -19.148 31.408 1.00 28.52  ? 84  CYS A C   1 
ATOM   729  O  O   . CYS A 1 83  ? 30.662 -19.822 30.378 1.00 26.13  ? 84  CYS A O   1 
ATOM   730  C  CB  . CYS A 1 83  ? 32.314 -19.001 33.204 1.00 31.33  ? 84  CYS A CB  1 
ATOM   731  S  SG  . CYS A 1 83  ? 32.967 -20.659 32.872 1.00 37.31  ? 84  CYS A SG  1 
ATOM   732  N  N   . ILE A 1 84  ? 29.340 -19.035 32.058 1.00 24.92  ? 85  ILE A N   1 
ATOM   733  C  CA  . ILE A 1 84  ? 28.109 -19.734 31.640 1.00 23.67  ? 85  ILE A CA  1 
ATOM   734  C  C   . ILE A 1 84  ? 27.708 -19.274 30.226 1.00 24.25  ? 85  ILE A C   1 
ATOM   735  O  O   . ILE A 1 84  ? 27.332 -20.100 29.384 1.00 23.84  ? 85  ILE A O   1 
ATOM   736  C  CB  . ILE A 1 84  ? 26.983 -19.516 32.689 1.00 27.21  ? 85  ILE A CB  1 
ATOM   737  C  CG1 . ILE A 1 84  ? 27.262 -20.354 33.978 1.00 28.82  ? 85  ILE A CG1 1 
ATOM   738  C  CG2 . ILE A 1 84  ? 25.564 -19.798 32.114 1.00 26.57  ? 85  ILE A CG2 1 
ATOM   739  C  CD1 . ILE A 1 84  ? 26.564 -19.788 35.207 1.00 37.08  ? 85  ILE A CD1 1 
ATOM   740  N  N   . LEU A 1 85  ? 27.775 -17.971 29.978 1.00 21.84  ? 86  LEU A N   1 
ATOM   741  C  CA  . LEU A 1 85  ? 27.426 -17.429 28.661 1.00 21.31  ? 86  LEU A CA  1 
ATOM   742  C  C   . LEU A 1 85  ? 28.436 -17.795 27.599 1.00 24.62  ? 86  LEU A C   1 
ATOM   743  O  O   . LEU A 1 85  ? 28.041 -18.051 26.467 1.00 22.82  ? 86  LEU A O   1 
ATOM   744  C  CB  . LEU A 1 85  ? 27.187 -15.922 28.746 1.00 22.34  ? 86  LEU A CB  1 
ATOM   745  C  CG  . LEU A 1 85  ? 25.893 -15.551 29.504 1.00 28.10  ? 86  LEU A CG  1 
ATOM   746  C  CD1 . LEU A 1 85  ? 25.790 -14.078 29.628 1.00 29.44  ? 86  LEU A CD1 1 
ATOM   747  C  CD2 . LEU A 1 85  ? 24.645 -16.071 28.764 1.00 29.22  ? 86  LEU A CD2 1 
ATOM   748  N  N   . LEU A 1 86  ? 29.748 -17.828 27.948 1.00 21.97  ? 87  LEU A N   1 
ATOM   749  C  CA  . LEU A 1 86  ? 30.778 -18.245 26.987 1.00 21.55  ? 87  LEU A CA  1 
ATOM   750  C  C   . LEU A 1 86  ? 30.543 -19.715 26.592 1.00 24.12  ? 87  LEU A C   1 
ATOM   751  O  O   . LEU A 1 86  ? 30.617 -20.065 25.410 1.00 22.34  ? 87  LEU A O   1 
ATOM   752  C  CB  . LEU A 1 86  ? 32.183 -18.042 27.593 1.00 21.37  ? 87  LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 86  ? 33.355 -18.321 26.647 1.00 26.04  ? 87  LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 86  ? 33.319 -17.384 25.409 1.00 24.65  ? 87  LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 86  ? 34.703 -18.197 27.409 1.00 28.62  ? 87  LEU A CD2 1 
ATOM   756  N  N   . ASP A 1 87  ? 30.236 -20.565 27.578 1.00 23.36  ? 88  ASP A N   1 
ATOM   757  C  CA  . ASP A 1 87  ? 29.904 -21.960 27.317 1.00 22.82  ? 88  ASP A CA  1 
ATOM   758  C  C   . ASP A 1 87  ? 28.693 -22.058 26.379 1.00 25.37  ? 88  ASP A C   1 
ATOM   759  O  O   . ASP A 1 87  ? 28.724 -22.837 25.429 1.00 25.44  ? 88  ASP A O   1 
ATOM   760  C  CB  . ASP A 1 87  ? 29.609 -22.679 28.636 1.00 26.02  ? 88  ASP A CB  1 
ATOM   761  C  CG  . ASP A 1 87  ? 30.853 -23.047 29.427 1.00 39.59  ? 88  ASP A CG  1 
ATOM   762  O  OD1 . ASP A 1 87  ? 31.973 -22.974 28.851 1.00 40.71  ? 88  ASP A OD1 1 
ATOM   763  O  OD2 . ASP A 1 87  ? 30.711 -23.408 30.624 1.00 40.91  ? 88  ASP A OD2 1 
ATOM   764  N  N   . PHE A 1 88  ? 27.639 -21.264 26.633 1.00 21.97  ? 89  PHE A N   1 
ATOM   765  C  CA  . PHE A 1 88  ? 26.448 -21.214 25.761 1.00 20.71  ? 89  PHE A CA  1 
ATOM   766  C  C   . PHE A 1 88  ? 26.825 -20.824 24.315 1.00 21.39  ? 89  PHE A C   1 
ATOM   767  O  O   . PHE A 1 88  ? 26.337 -21.422 23.352 1.00 20.25  ? 89  PHE A O   1 
ATOM   768  C  CB  . PHE A 1 88  ? 25.387 -20.238 26.337 1.00 21.89  ? 89  PHE A CB  1 
ATOM   769  C  CG  . PHE A 1 88  ? 24.272 -19.963 25.359 1.00 22.28  ? 89  PHE A CG  1 
ATOM   770  C  CD1 . PHE A 1 88  ? 23.299 -20.930 25.096 1.00 23.43  ? 89  PHE A CD1 1 
ATOM   771  C  CD2 . PHE A 1 88  ? 24.250 -18.782 24.618 1.00 23.47  ? 89  PHE A CD2 1 
ATOM   772  C  CE1 . PHE A 1 88  ? 22.310 -20.702 24.146 1.00 23.63  ? 89  PHE A CE1 1 
ATOM   773  C  CE2 . PHE A 1 88  ? 23.268 -18.566 23.641 1.00 26.33  ? 89  PHE A CE2 1 
ATOM   774  C  CZ  . PHE A 1 88  ? 22.296 -19.517 23.422 1.00 24.61  ? 89  PHE A CZ  1 
ATOM   775  N  N   . MET A 1 89  ? 27.660 -19.785 24.160 1.00 18.05  ? 90  MET A N   1 
ATOM   776  C  CA  . MET A 1 89  ? 28.090 -19.358 22.814 1.00 17.30  ? 90  MET A CA  1 
ATOM   777  C  C   . MET A 1 89  ? 28.646 -20.510 22.008 1.00 22.19  ? 90  MET A C   1 
ATOM   778  O  O   . MET A 1 89  ? 28.326 -20.624 20.827 1.00 21.25  ? 90  MET A O   1 
ATOM   779  C  CB  . MET A 1 89  ? 29.175 -18.259 22.931 1.00 18.47  ? 90  MET A CB  1 
ATOM   780  C  CG  . MET A 1 89  ? 28.641 -16.968 23.493 1.00 21.13  ? 90  MET A CG  1 
ATOM   781  S  SD  . MET A 1 89  ? 30.012 -15.757 23.386 1.00 25.01  ? 90  MET A SD  1 
ATOM   782  C  CE  . MET A 1 89  ? 29.377 -14.450 24.551 1.00 24.97  ? 90  MET A CE  1 
ATOM   783  N  N   . TYR A 1 90  ? 29.494 -21.343 22.636 1.00 19.84  ? 91  TYR A N   1 
ATOM   784  C  CA  . TYR A 1 90  ? 30.172 -22.447 21.969 1.00 19.40  ? 91  TYR A CA  1 
ATOM   785  C  C   . TYR A 1 90  ? 29.415 -23.761 21.951 1.00 23.03  ? 91  TYR A C   1 
ATOM   786  O  O   . TYR A 1 90  ? 29.899 -24.721 21.334 1.00 22.49  ? 91  TYR A O   1 
ATOM   787  C  CB  . TYR A 1 90  ? 31.545 -22.659 22.608 1.00 20.63  ? 91  TYR A CB  1 
ATOM   788  C  CG  . TYR A 1 90  ? 32.606 -21.691 22.118 1.00 21.61  ? 91  TYR A CG  1 
ATOM   789  C  CD1 . TYR A 1 90  ? 32.752 -20.431 22.696 1.00 23.10  ? 91  TYR A CD1 1 
ATOM   790  C  CD2 . TYR A 1 90  ? 33.436 -22.021 21.045 1.00 22.13  ? 91  TYR A CD2 1 
ATOM   791  C  CE1 . TYR A 1 90  ? 33.753 -19.553 22.272 1.00 23.59  ? 91  TYR A CE1 1 
ATOM   792  C  CE2 . TYR A 1 90  ? 34.467 -21.171 20.640 1.00 22.06  ? 91  TYR A CE2 1 
ATOM   793  C  CZ  . TYR A 1 90  ? 34.594 -19.922 21.229 1.00 25.56  ? 91  TYR A CZ  1 
ATOM   794  O  OH  . TYR A 1 90  ? 35.623 -19.092 20.840 1.00 23.83  ? 91  TYR A OH  1 
ATOM   795  N  N   . THR A 1 91  ? 28.260 -23.845 22.637 1.00 19.41  ? 92  THR A N   1 
ATOM   796  C  CA  . THR A 1 91  ? 27.573 -25.147 22.708 1.00 20.06  ? 92  THR A CA  1 
ATOM   797  C  C   . THR A 1 91  ? 26.072 -25.121 22.445 1.00 23.06  ? 92  THR A C   1 
ATOM   798  O  O   . THR A 1 91  ? 25.504 -26.197 22.289 1.00 23.71  ? 92  THR A O   1 
ATOM   799  C  CB  . THR A 1 91  ? 27.777 -25.821 24.103 1.00 26.67  ? 92  THR A CB  1 
ATOM   800  O  OG1 . THR A 1 91  ? 27.117 -25.053 25.109 1.00 25.69  ? 92  THR A OG1 1 
ATOM   801  C  CG2 . THR A 1 91  ? 29.247 -26.048 24.481 1.00 26.52  ? 92  THR A CG2 1 
ATOM   802  N  N   . SER A 1 92  ? 25.421 -23.951 22.545 1.00 19.65  ? 93  SER A N   1 
ATOM   803  C  CA  . SER A 1 92  ? 23.941 -23.772 22.496 1.00 19.39  ? 93  SER A CA  1 
ATOM   804  C  C   . SER A 1 92  ? 23.277 -24.188 23.842 1.00 23.25  ? 93  SER A C   1 
ATOM   805  O  O   . SER A 1 92  ? 22.064 -24.061 23.969 1.00 23.64  ? 93  SER A O   1 
ATOM   806  C  CB  . SER A 1 92  ? 23.287 -24.577 21.362 1.00 21.90  ? 93  SER A CB  1 
ATOM   807  O  OG  . SER A 1 92  ? 23.942 -24.405 20.116 1.00 26.90  ? 93  SER A OG  1 
ATOM   808  N  N   A ARG A 1 93  ? 24.080 -24.636 24.827 0.60 21.39  ? 94  ARG A N   1 
ATOM   809  N  N   B ARG A 1 93  ? 24.057 -24.694 24.822 0.40 20.75  ? 94  ARG A N   1 
ATOM   810  C  CA  A ARG A 1 93  ? 23.593 -25.106 26.127 0.60 22.39  ? 94  ARG A CA  1 
ATOM   811  C  CA  B ARG A 1 93  ? 23.499 -25.124 26.110 0.40 21.46  ? 94  ARG A CA  1 
ATOM   812  C  C   A ARG A 1 93  ? 23.789 -24.048 27.190 0.60 26.61  ? 94  ARG A C   1 
ATOM   813  C  C   B ARG A 1 93  ? 23.775 -24.116 27.200 0.40 26.17  ? 94  ARG A C   1 
ATOM   814  O  O   A ARG A 1 93  ? 24.904 -23.538 27.364 0.60 24.67  ? 94  ARG A O   1 
ATOM   815  O  O   B ARG A 1 93  ? 24.921 -23.688 27.385 0.40 24.62  ? 94  ARG A O   1 
ATOM   816  C  CB  A ARG A 1 93  ? 24.311 -26.403 26.546 0.60 25.44  ? 94  ARG A CB  1 
ATOM   817  C  CB  B ARG A 1 93  ? 23.953 -26.540 26.503 0.40 22.87  ? 94  ARG A CB  1 
ATOM   818  C  CG  A ARG A 1 93  ? 24.163 -27.550 25.535 0.60 31.06  ? 94  ARG A CG  1 
ATOM   819  C  CG  B ARG A 1 93  ? 23.263 -27.614 25.673 0.40 23.78  ? 94  ARG A CG  1 
ATOM   820  C  CD  A ARG A 1 93  ? 25.098 -28.706 25.856 0.60 39.91  ? 94  ARG A CD  1 
ATOM   821  C  CD  B ARG A 1 93  ? 24.032 -28.916 25.647 0.40 34.81  ? 94  ARG A CD  1 
ATOM   822  N  NE  A ARG A 1 93  ? 24.832 -29.267 27.184 0.60 45.81  ? 94  ARG A NE  1 
ATOM   823  N  NE  B ARG A 1 93  ? 23.455 -29.857 24.686 0.40 41.21  ? 94  ARG A NE  1 
ATOM   824  C  CZ  A ARG A 1 93  ? 23.953 -30.234 27.427 0.60 56.91  ? 94  ARG A CZ  1 
ATOM   825  C  CZ  B ARG A 1 93  ? 23.323 -31.163 24.897 0.40 53.60  ? 94  ARG A CZ  1 
ATOM   826  N  NH1 A ARG A 1 93  ? 23.772 -30.675 28.663 0.60 43.68  ? 94  ARG A NH1 1 
ATOM   827  N  NH1 B ARG A 1 93  ? 22.793 -31.941 23.963 0.40 43.25  ? 94  ARG A NH1 1 
ATOM   828  N  NH2 A ARG A 1 93  ? 23.248 -30.766 26.435 0.60 41.91  ? 94  ARG A NH2 1 
ATOM   829  N  NH2 B ARG A 1 93  ? 23.714 -31.699 26.044 0.40 40.22  ? 94  ARG A NH2 1 
ATOM   830  N  N   . LEU A 1 94  ? 22.708 -23.717 27.902 1.00 23.98  ? 95  LEU A N   1 
ATOM   831  C  CA  . LEU A 1 94  ? 22.759 -22.713 28.949 1.00 24.15  ? 95  LEU A CA  1 
ATOM   832  C  C   . LEU A 1 94  ? 22.515 -23.345 30.314 1.00 29.42  ? 95  LEU A C   1 
ATOM   833  O  O   . LEU A 1 94  ? 21.446 -23.924 30.554 1.00 29.20  ? 95  LEU A O   1 
ATOM   834  C  CB  . LEU A 1 94  ? 21.743 -21.603 28.630 1.00 24.32  ? 95  LEU A CB  1 
ATOM   835  C  CG  . LEU A 1 94  ? 21.728 -20.395 29.576 1.00 28.36  ? 95  LEU A CG  1 
ATOM   836  C  CD1 . LEU A 1 94  ? 22.983 -19.522 29.362 1.00 26.51  ? 95  LEU A CD1 1 
ATOM   837  C  CD2 . LEU A 1 94  ? 20.463 -19.585 29.378 1.00 30.12  ? 95  LEU A CD2 1 
ATOM   838  N  N   . ASN A 1 95  ? 23.514 -23.238 31.209 1.00 27.75  ? 96  ASN A N   1 
ATOM   839  C  CA  . ASN A 1 95  ? 23.434 -23.780 32.578 1.00 29.64  ? 96  ASN A CA  1 
ATOM   840  C  C   . ASN A 1 95  ? 22.724 -22.767 33.495 1.00 33.83  ? 96  ASN A C   1 
ATOM   841  O  O   . ASN A 1 95  ? 23.364 -22.052 34.269 1.00 33.41  ? 96  ASN A O   1 
ATOM   842  C  CB  . ASN A 1 95  ? 24.841 -24.156 33.112 1.00 32.42  ? 96  ASN A CB  1 
ATOM   843  C  CG  . ASN A 1 95  ? 24.814 -24.807 34.494 1.00 50.73  ? 96  ASN A CG  1 
ATOM   844  O  OD1 . ASN A 1 95  ? 23.823 -25.403 34.913 1.00 43.85  ? 96  ASN A OD1 1 
ATOM   845  N  ND2 . ASN A 1 95  ? 25.902 -24.705 35.235 1.00 44.62  ? 96  ASN A ND2 1 
ATOM   846  N  N   . LEU A 1 96  ? 21.410 -22.658 33.336 1.00 30.47  ? 97  LEU A N   1 
ATOM   847  C  CA  . LEU A 1 96  ? 20.596 -21.693 34.072 1.00 31.87  ? 97  LEU A CA  1 
ATOM   848  C  C   . LEU A 1 96  ? 20.066 -22.335 35.335 1.00 36.54  ? 97  LEU A C   1 
ATOM   849  O  O   . LEU A 1 96  ? 19.416 -23.388 35.272 1.00 35.90  ? 97  LEU A O   1 
ATOM   850  C  CB  . LEU A 1 96  ? 19.460 -21.220 33.159 1.00 32.85  ? 97  LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 96  ? 18.748 -19.929 33.482 1.00 39.29  ? 97  LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 96  ? 19.751 -18.743 33.576 1.00 38.66  ? 97  LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 96  ? 17.673 -19.661 32.430 1.00 39.70  ? 97  LEU A CD2 1 
ATOM   854  N  N   . ARG A 1 97  ? 20.400 -21.733 36.493 1.00 33.50  ? 98  ARG A N   1 
ATOM   855  C  CA  . ARG A 1 97  ? 20.001 -22.249 37.812 1.00 35.50  ? 98  ARG A CA  1 
ATOM   856  C  C   . ARG A 1 97  ? 19.488 -21.127 38.693 1.00 38.06  ? 98  ARG A C   1 
ATOM   857  O  O   . ARG A 1 97  ? 19.867 -19.964 38.492 1.00 35.31  ? 98  ARG A O   1 
ATOM   858  C  CB  . ARG A 1 97  ? 21.184 -22.957 38.503 1.00 37.78  ? 98  ARG A CB  1 
ATOM   859  C  CG  . ARG A 1 97  ? 21.768 -24.146 37.719 1.00 46.02  ? 98  ARG A CG  1 
ATOM   860  C  CD  . ARG A 1 97  ? 23.044 -24.706 38.339 1.00 62.50  ? 98  ARG A CD  1 
ATOM   861  N  NE  . ARG A 1 97  ? 22.832 -25.220 39.698 1.00 82.30  ? 98  ARG A NE  1 
ATOM   862  C  CZ  . ARG A 1 97  ? 22.383 -26.439 39.990 1.00 101.27 ? 98  ARG A CZ  1 
ATOM   863  N  NH1 . ARG A 1 97  ? 22.215 -26.805 41.254 1.00 89.79  ? 98  ARG A NH1 1 
ATOM   864  N  NH2 . ARG A 1 97  ? 22.095 -27.299 39.020 1.00 89.62  ? 98  ARG A NH2 1 
ATOM   865  N  N   . GLU A 1 98  ? 18.647 -21.461 39.695 1.00 37.00  ? 99  GLU A N   1 
ATOM   866  C  CA  . GLU A 1 98  ? 18.121 -20.453 40.636 1.00 37.80  ? 99  GLU A CA  1 
ATOM   867  C  C   . GLU A 1 98  ? 19.252 -19.573 41.211 1.00 41.36  ? 99  GLU A C   1 
ATOM   868  O  O   . GLU A 1 98  ? 19.090 -18.353 41.316 1.00 41.48  ? 99  GLU A O   1 
ATOM   869  C  CB  . GLU A 1 98  ? 17.340 -21.138 41.783 1.00 41.54  ? 99  GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 98  ? 16.681 -20.164 42.747 1.00 54.61  ? 99  GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 98  ? 15.944 -20.804 43.908 1.00 88.36  ? 99  GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 98  ? 16.518 -21.698 44.572 1.00 85.95  ? 99  GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 98  ? 14.787 -20.398 44.161 1.00 91.94  ? 99  GLU A OE2 1 
ATOM   874  N  N   . GLY A 1 99  ? 20.387 -20.197 41.531 1.00 38.52  ? 100 GLY A N   1 
ATOM   875  C  CA  . GLY A 1 99  ? 21.540 -19.506 42.111 1.00 39.15  ? 100 GLY A CA  1 
ATOM   876  C  C   . GLY A 1 99  ? 22.349 -18.635 41.165 1.00 40.50  ? 100 GLY A C   1 
ATOM   877  O  O   . GLY A 1 99  ? 23.162 -17.828 41.619 1.00 40.38  ? 100 GLY A O   1 
ATOM   878  N  N   . ASN A 1 100 ? 22.143 -18.762 39.844 1.00 35.44  ? 101 ASN A N   1 
ATOM   879  C  CA  . ASN A 1 100 ? 22.936 -17.946 38.911 1.00 33.74  ? 101 ASN A CA  1 
ATOM   880  C  C   . ASN A 1 100 ? 22.106 -17.079 37.956 1.00 36.31  ? 101 ASN A C   1 
ATOM   881  O  O   . ASN A 1 100 ? 22.686 -16.277 37.222 1.00 33.72  ? 101 ASN A O   1 
ATOM   882  C  CB  . ASN A 1 100 ? 23.914 -18.847 38.122 1.00 33.36  ? 101 ASN A CB  1 
ATOM   883  C  CG  . ASN A 1 100 ? 23.247 -19.797 37.142 1.00 39.37  ? 101 ASN A CG  1 
ATOM   884  O  OD1 . ASN A 1 100 ? 22.190 -19.499 36.580 1.00 30.65  ? 101 ASN A OD1 1 
ATOM   885  N  ND2 . ASN A 1 100 ? 23.866 -20.948 36.878 1.00 31.78  ? 101 ASN A ND2 1 
ATOM   886  N  N   . ILE A 1 101 ? 20.769 -17.273 37.921 1.00 33.81  ? 102 ILE A N   1 
ATOM   887  C  CA  . ILE A 1 101 ? 19.888 -16.615 36.945 1.00 33.42  ? 102 ILE A CA  1 
ATOM   888  C  C   . ILE A 1 101 ? 20.015 -15.088 36.930 1.00 35.80  ? 102 ILE A C   1 
ATOM   889  O  O   . ILE A 1 101 ? 20.039 -14.504 35.836 1.00 33.20  ? 102 ILE A O   1 
ATOM   890  C  CB  . ILE A 1 101 ? 18.407 -17.065 37.049 1.00 37.95  ? 102 ILE A CB  1 
ATOM   891  C  CG1 . ILE A 1 101 ? 17.561 -16.462 35.889 1.00 38.77  ? 102 ILE A CG1 1 
ATOM   892  C  CG2 . ILE A 1 101 ? 17.791 -16.811 38.435 1.00 37.59  ? 102 ILE A CG2 1 
ATOM   893  C  CD1 . ILE A 1 101 ? 16.383 -17.313 35.434 1.00 39.73  ? 102 ILE A CD1 1 
ATOM   894  N  N   . MET A 1 102 ? 20.113 -14.443 38.103 1.00 34.11  ? 103 MET A N   1 
ATOM   895  C  CA  . MET A 1 102 ? 20.252 -12.988 38.137 1.00 34.64  ? 103 MET A CA  1 
ATOM   896  C  C   . MET A 1 102 ? 21.554 -12.522 37.499 1.00 35.92  ? 103 MET A C   1 
ATOM   897  O  O   . MET A 1 102 ? 21.517 -11.581 36.708 1.00 33.99  ? 103 MET A O   1 
ATOM   898  C  CB  . MET A 1 102 ? 20.085 -12.419 39.563 1.00 39.05  ? 103 MET A CB  1 
ATOM   899  C  CG  . MET A 1 102 ? 18.713 -12.693 40.178 1.00 46.00  ? 103 MET A CG  1 
ATOM   900  S  SD  . MET A 1 102 ? 17.279 -12.323 39.122 1.00 52.11  ? 103 MET A SD  1 
ATOM   901  C  CE  . MET A 1 102 ? 17.319 -10.501 39.141 1.00 49.55  ? 103 MET A CE  1 
ATOM   902  N  N   . ALA A 1 103 ? 22.693 -13.196 37.806 1.00 32.34  ? 104 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 103 ? 24.015 -12.854 37.241 1.00 31.93  ? 104 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 103 ? 24.017 -13.151 35.739 1.00 32.49  ? 104 ALA A C   1 
ATOM   905  O  O   . ALA A 1 103 ? 24.512 -12.343 34.952 1.00 30.63  ? 104 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 103 ? 25.110 -13.670 37.918 1.00 33.41  ? 104 ALA A CB  1 
ATOM   907  N  N   . VAL A 1 104 ? 23.437 -14.300 35.348 1.00 26.69  ? 105 VAL A N   1 
ATOM   908  C  CA  . VAL A 1 104 ? 23.363 -14.680 33.922 1.00 25.30  ? 105 VAL A CA  1 
ATOM   909  C  C   . VAL A 1 104 ? 22.552 -13.652 33.123 1.00 28.96  ? 105 VAL A C   1 
ATOM   910  O  O   . VAL A 1 104 ? 23.028 -13.219 32.066 1.00 27.68  ? 105 VAL A O   1 
ATOM   911  C  CB  . VAL A 1 104 ? 22.878 -16.136 33.714 1.00 28.89  ? 105 VAL A CB  1 
ATOM   912  C  CG1 . VAL A 1 104 ? 22.612 -16.421 32.235 1.00 27.01  ? 105 VAL A CG1 1 
ATOM   913  C  CG2 . VAL A 1 104 ? 23.903 -17.124 34.262 1.00 28.73  ? 105 VAL A CG2 1 
ATOM   914  N  N   A MET A 1 105 ? 21.362 -13.246 33.619 0.65 27.61  ? 106 MET A N   1 
ATOM   915  N  N   B MET A 1 105 ? 21.359 -13.249 33.614 0.35 27.79  ? 106 MET A N   1 
ATOM   916  C  CA  A MET A 1 105 ? 20.544 -12.261 32.902 0.65 28.75  ? 106 MET A CA  1 
ATOM   917  C  CA  B MET A 1 105 ? 20.538 -12.263 32.904 0.35 28.81  ? 106 MET A CA  1 
ATOM   918  C  C   A MET A 1 105 ? 21.260 -10.917 32.790 0.65 31.81  ? 106 MET A C   1 
ATOM   919  C  C   B MET A 1 105 ? 21.251 -10.918 32.789 0.35 32.41  ? 106 MET A C   1 
ATOM   920  O  O   A MET A 1 105 ? 21.251 -10.314 31.717 0.65 29.61  ? 106 MET A O   1 
ATOM   921  O  O   B MET A 1 105 ? 21.246 -10.323 31.711 0.35 30.96  ? 106 MET A O   1 
ATOM   922  C  CB  A MET A 1 105 ? 19.180 -12.067 33.562 0.65 32.84  ? 106 MET A CB  1 
ATOM   923  C  CB  B MET A 1 105 ? 19.165 -12.081 33.556 0.35 32.87  ? 106 MET A CB  1 
ATOM   924  C  CG  A MET A 1 105 ? 18.258 -11.169 32.750 0.65 37.26  ? 106 MET A CG  1 
ATOM   925  C  CG  B MET A 1 105 ? 18.231 -11.235 32.715 0.35 37.32  ? 106 MET A CG  1 
ATOM   926  S  SD  A MET A 1 105 ? 16.580 -11.168 33.394 0.65 43.60  ? 106 MET A SD  1 
ATOM   927  S  SD  B MET A 1 105 ? 16.628 -11.020 33.490 0.35 43.80  ? 106 MET A SD  1 
ATOM   928  C  CE  A MET A 1 105 ? 16.764 -10.070 34.858 0.65 41.61  ? 106 MET A CE  1 
ATOM   929  C  CE  B MET A 1 105 ? 16.189 -9.439  32.841 0.35 41.51  ? 106 MET A CE  1 
ATOM   930  N  N   . ALA A 1 106 ? 21.863 -10.445 33.891 1.00 30.26  ? 107 ALA A N   1 
ATOM   931  C  CA  . ALA A 1 106 ? 22.610 -9.161  33.898 1.00 29.75  ? 107 ALA A CA  1 
ATOM   932  C  C   . ALA A 1 106 ? 23.774 -9.197  32.887 1.00 29.88  ? 107 ALA A C   1 
ATOM   933  O  O   . ALA A 1 106 ? 23.963 -8.236  32.122 1.00 28.14  ? 107 ALA A O   1 
ATOM   934  C  CB  . ALA A 1 106 ? 23.123 -8.856  35.298 1.00 31.17  ? 107 ALA A CB  1 
ATOM   935  N  N   . THR A 1 107 ? 24.515 -10.326 32.840 1.00 25.16  ? 108 THR A N   1 
ATOM   936  C  CA  . THR A 1 107 ? 25.621 -10.506 31.900 1.00 24.66  ? 108 THR A CA  1 
ATOM   937  C  C   . THR A 1 107 ? 25.099 -10.536 30.451 1.00 27.86  ? 108 THR A C   1 
ATOM   938  O  O   . THR A 1 107 ? 25.690 -9.882  29.592 1.00 25.58  ? 108 THR A O   1 
ATOM   939  C  CB  . THR A 1 107 ? 26.519 -11.711 32.272 1.00 31.30  ? 108 THR A CB  1 
ATOM   940  O  OG1 . THR A 1 107 ? 26.795 -11.693 33.678 1.00 29.93  ? 108 THR A OG1 1 
ATOM   941  C  CG2 . THR A 1 107 ? 27.845 -11.722 31.492 1.00 29.28  ? 108 THR A CG2 1 
ATOM   942  N  N   . ALA A 1 108 ? 23.991 -11.276 30.182 1.00 24.83  ? 109 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 108 ? 23.404 -11.370 28.838 1.00 23.71  ? 109 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 108 ? 22.891 -9.998  28.370 1.00 26.52  ? 109 ALA A C   1 
ATOM   945  O  O   . ALA A 1 108 ? 23.025 -9.666  27.190 1.00 25.42  ? 109 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 108 ? 22.287 -12.418 28.815 1.00 24.21  ? 109 ALA A CB  1 
ATOM   947  N  N   . MET A 1 109 ? 22.358 -9.179  29.289 1.00 25.45  ? 110 MET A N   1 
ATOM   948  C  CA  . MET A 1 109 ? 21.906 -7.824  28.916 1.00 26.01  ? 110 MET A CA  1 
ATOM   949  C  C   . MET A 1 109 ? 23.097 -6.960  28.480 1.00 28.25  ? 110 MET A C   1 
ATOM   950  O  O   . MET A 1 109 ? 23.055 -6.304  27.432 1.00 28.58  ? 110 MET A O   1 
ATOM   951  C  CB  . MET A 1 109 ? 21.143 -7.166  30.076 1.00 29.77  ? 110 MET A CB  1 
ATOM   952  C  CG  . MET A 1 109 ? 19.740 -7.723  30.237 1.00 35.66  ? 110 MET A CG  1 
ATOM   953  S  SD  . MET A 1 109 ? 18.976 -7.173  31.777 1.00 43.38  ? 110 MET A SD  1 
ATOM   954  C  CE  . MET A 1 109 ? 18.710 -5.446  31.407 1.00 41.46  ? 110 MET A CE  1 
ATOM   955  N  N   . TYR A 1 110 ? 24.179 -7.029  29.242 1.00 26.86  ? 111 TYR A N   1 
ATOM   956  C  CA  . TYR A 1 110 ? 25.416 -6.293  28.962 1.00 26.60  ? 111 TYR A CA  1 
ATOM   957  C  C   . TYR A 1 110 ? 26.047 -6.770  27.619 1.00 27.55  ? 111 TYR A C   1 
ATOM   958  O  O   . TYR A 1 110 ? 26.451 -5.942  26.796 1.00 26.58  ? 111 TYR A O   1 
ATOM   959  C  CB  . TYR A 1 110 ? 26.386 -6.514  30.125 1.00 27.15  ? 111 TYR A CB  1 
ATOM   960  C  CG  . TYR A 1 110 ? 27.805 -6.038  29.890 1.00 26.72  ? 111 TYR A CG  1 
ATOM   961  C  CD1 . TYR A 1 110 ? 28.128 -4.683  29.950 1.00 29.59  ? 111 TYR A CD1 1 
ATOM   962  C  CD2 . TYR A 1 110 ? 28.840 -6.949  29.683 1.00 26.18  ? 111 TYR A CD2 1 
ATOM   963  C  CE1 . TYR A 1 110 ? 29.440 -4.244  29.749 1.00 27.03  ? 111 TYR A CE1 1 
ATOM   964  C  CE2 . TYR A 1 110 ? 30.158 -6.526  29.529 1.00 25.97  ? 111 TYR A CE2 1 
ATOM   965  C  CZ  . TYR A 1 110 ? 30.453 -5.172  29.576 1.00 27.98  ? 111 TYR A CZ  1 
ATOM   966  O  OH  . TYR A 1 110 ? 31.752 -4.767  29.445 1.00 27.29  ? 111 TYR A OH  1 
ATOM   967  N  N   . LEU A 1 111 ? 26.101 -8.096  27.398 1.00 23.55  ? 112 LEU A N   1 
ATOM   968  C  CA  . LEU A 1 111 ? 26.684 -8.689  26.196 1.00 22.51  ? 112 LEU A CA  1 
ATOM   969  C  C   . LEU A 1 111 ? 25.757 -8.550  24.983 1.00 26.20  ? 112 LEU A C   1 
ATOM   970  O  O   . LEU A 1 111 ? 26.186 -8.821  23.869 1.00 24.94  ? 112 LEU A O   1 
ATOM   971  C  CB  . LEU A 1 111 ? 27.036 -10.173 26.450 1.00 21.13  ? 112 LEU A CB  1 
ATOM   972  C  CG  . LEU A 1 111 ? 28.181 -10.445 27.466 1.00 24.24  ? 112 LEU A CG  1 
ATOM   973  C  CD1 . LEU A 1 111 ? 28.460 -11.964 27.561 1.00 24.34  ? 112 LEU A CD1 1 
ATOM   974  C  CD2 . LEU A 1 111 ? 29.491 -9.663  27.082 1.00 25.33  ? 112 LEU A CD2 1 
ATOM   975  N  N   . GLN A 1 112 ? 24.471 -8.188  25.211 1.00 24.64  ? 113 GLN A N   1 
ATOM   976  C  CA  . GLN A 1 112 ? 23.460 -8.053  24.152 1.00 25.83  ? 113 GLN A CA  1 
ATOM   977  C  C   . GLN A 1 112 ? 23.231 -9.414  23.459 1.00 27.32  ? 113 GLN A C   1 
ATOM   978  O  O   . GLN A 1 112 ? 23.542 -9.604  22.276 1.00 25.68  ? 113 GLN A O   1 
ATOM   979  C  CB  . GLN A 1 112 ? 23.843 -6.949  23.145 1.00 27.55  ? 113 GLN A CB  1 
ATOM   980  C  CG  . GLN A 1 112 ? 24.009 -5.559  23.780 1.00 29.64  ? 113 GLN A CG  1 
ATOM   981  C  CD  . GLN A 1 112 ? 24.739 -4.626  22.840 1.00 39.53  ? 113 GLN A CD  1 
ATOM   982  O  OE1 . GLN A 1 112 ? 24.623 -4.722  21.625 1.00 34.04  ? 113 GLN A OE1 1 
ATOM   983  N  NE2 . GLN A 1 112 ? 25.534 -3.732  23.379 1.00 36.42  ? 113 GLN A NE2 1 
ATOM   984  N  N   . MET A 1 113 ? 22.746 -10.377 24.248 1.00 24.24  ? 114 MET A N   1 
ATOM   985  C  CA  . MET A 1 113 ? 22.427 -11.755 23.821 1.00 23.77  ? 114 MET A CA  1 
ATOM   986  C  C   . MET A 1 113 ? 20.925 -11.899 24.075 1.00 29.66  ? 114 MET A C   1 
ATOM   987  O  O   . MET A 1 113 ? 20.492 -12.356 25.141 1.00 27.62  ? 114 MET A O   1 
ATOM   988  C  CB  . MET A 1 113 ? 23.267 -12.740 24.639 1.00 24.77  ? 114 MET A CB  1 
ATOM   989  C  CG  . MET A 1 113 ? 24.770 -12.615 24.333 1.00 26.16  ? 114 MET A CG  1 
ATOM   990  S  SD  . MET A 1 113 ? 25.800 -13.625 25.404 1.00 28.65  ? 114 MET A SD  1 
ATOM   991  C  CE  . MET A 1 113 ? 25.421 -15.306 24.728 1.00 25.48  ? 114 MET A CE  1 
ATOM   992  N  N   . GLU A 1 114 ? 20.136 -11.344 23.144 1.00 29.96  ? 115 GLU A N   1 
ATOM   993  C  CA  . GLU A 1 114 ? 18.680 -11.199 23.283 1.00 32.71  ? 115 GLU A CA  1 
ATOM   994  C  C   . GLU A 1 114 ? 17.915 -12.485 23.588 1.00 33.77  ? 115 GLU A C   1 
ATOM   995  O  O   . GLU A 1 114 ? 16.982 -12.431 24.383 1.00 33.37  ? 115 GLU A O   1 
ATOM   996  C  CB  . GLU A 1 114 ? 18.064 -10.506 22.059 1.00 36.11  ? 115 GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 114 ? 18.612 -9.105  21.833 1.00 51.02  ? 115 GLU A CG  1 
ATOM   998  N  N   . HIS A 1 115 ? 18.293 -13.627 22.993 1.00 29.08  ? 116 HIS A N   1 
ATOM   999  C  CA  . HIS A 1 115 ? 17.557 -14.864 23.269 1.00 30.92  ? 116 HIS A CA  1 
ATOM   1000 C  C   . HIS A 1 115 ? 17.773 -15.350 24.702 1.00 32.50  ? 116 HIS A C   1 
ATOM   1001 O  O   . HIS A 1 115 ? 16.823 -15.824 25.322 1.00 32.66  ? 116 HIS A O   1 
ATOM   1002 C  CB  . HIS A 1 115 ? 17.850 -15.948 22.231 1.00 32.55  ? 116 HIS A CB  1 
ATOM   1003 C  CG  . HIS A 1 115 ? 17.332 -15.616 20.870 1.00 37.46  ? 116 HIS A CG  1 
ATOM   1004 N  ND1 . HIS A 1 115 ? 15.982 -15.423 20.644 1.00 41.23  ? 116 HIS A ND1 1 
ATOM   1005 C  CD2 . HIS A 1 115 ? 17.994 -15.508 19.694 1.00 38.92  ? 116 HIS A CD2 1 
ATOM   1006 C  CE1 . HIS A 1 115 ? 15.868 -15.160 19.352 1.00 41.20  ? 116 HIS A CE1 1 
ATOM   1007 N  NE2 . HIS A 1 115 ? 17.049 -15.213 18.739 1.00 40.15  ? 116 HIS A NE2 1 
ATOM   1008 N  N   . VAL A 1 116 ? 19.003 -15.185 25.241 1.00 26.20  ? 117 VAL A N   1 
ATOM   1009 C  CA  . VAL A 1 116 ? 19.295 -15.530 26.640 1.00 26.32  ? 117 VAL A CA  1 
ATOM   1010 C  C   . VAL A 1 116 ? 18.507 -14.619 27.594 1.00 32.02  ? 117 VAL A C   1 
ATOM   1011 O  O   . VAL A 1 116 ? 17.887 -15.109 28.554 1.00 30.01  ? 117 VAL A O   1 
ATOM   1012 C  CB  . VAL A 1 116 ? 20.811 -15.550 26.959 1.00 28.40  ? 117 VAL A CB  1 
ATOM   1013 C  CG1 . VAL A 1 116 ? 21.048 -15.808 28.452 1.00 28.48  ? 117 VAL A CG1 1 
ATOM   1014 C  CG2 . VAL A 1 116 ? 21.525 -16.605 26.111 1.00 27.57  ? 117 VAL A CG2 1 
ATOM   1015 N  N   . VAL A 1 117 ? 18.513 -13.290 27.328 1.00 28.77  ? 118 VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 117 ? 17.755 -12.327 28.141 1.00 29.44  ? 118 VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 117 ? 16.268 -12.735 28.196 1.00 35.51  ? 118 VAL A C   1 
ATOM   1018 O  O   . VAL A 1 117 ? 15.699 -12.774 29.289 1.00 35.37  ? 118 VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 117 ? 17.944 -10.860 27.666 1.00 32.76  ? 118 VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 117 ? 17.093 -9.883  28.496 1.00 33.41  ? 118 VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 117 ? 19.416 -10.458 27.728 1.00 31.36  ? 118 VAL A CG2 1 
ATOM   1022 N  N   A ASP A 1 118 ? 15.634 -12.954 27.024 0.41 33.97  ? 119 ASP A N   1 
ATOM   1023 N  N   B ASP A 1 118 ? 15.701 -13.137 27.041 0.59 32.97  ? 119 ASP A N   1 
ATOM   1024 C  CA  A ASP A 1 118 ? 14.210 -13.308 26.902 0.41 35.90  ? 119 ASP A CA  1 
ATOM   1025 C  CA  B ASP A 1 118 ? 14.316 -13.604 26.903 0.59 34.30  ? 119 ASP A CA  1 
ATOM   1026 C  C   A ASP A 1 118 ? 13.788 -14.508 27.753 0.41 40.59  ? 119 ASP A C   1 
ATOM   1027 C  C   B ASP A 1 118 ? 14.001 -14.814 27.796 0.59 37.07  ? 119 ASP A C   1 
ATOM   1028 O  O   A ASP A 1 118 ? 12.724 -14.471 28.365 0.41 42.17  ? 119 ASP A O   1 
ATOM   1029 O  O   B ASP A 1 118 ? 13.039 -14.748 28.557 0.59 37.39  ? 119 ASP A O   1 
ATOM   1030 C  CB  A ASP A 1 118 ? 13.822 -13.531 25.429 0.41 38.13  ? 119 ASP A CB  1 
ATOM   1031 C  CB  B ASP A 1 118 ? 13.984 -13.908 25.429 0.59 36.57  ? 119 ASP A CB  1 
ATOM   1032 C  CG  A ASP A 1 118 ? 13.608 -12.267 24.617 0.41 51.41  ? 119 ASP A CG  1 
ATOM   1033 C  CG  B ASP A 1 118 ? 12.526 -14.253 25.168 0.59 51.99  ? 119 ASP A CG  1 
ATOM   1034 O  OD1 A ASP A 1 118 ? 13.044 -11.295 25.163 0.41 55.04  ? 119 ASP A OD1 1 
ATOM   1035 O  OD1 B ASP A 1 118 ? 11.647 -13.444 25.540 0.59 55.06  ? 119 ASP A OD1 1 
ATOM   1036 O  OD2 A ASP A 1 118 ? 13.999 -12.250 23.431 0.41 57.03  ? 119 ASP A OD2 1 
ATOM   1037 O  OD2 B ASP A 1 118 ? 12.266 -15.322 24.577 0.59 56.90  ? 119 ASP A OD2 1 
ATOM   1038 N  N   A THR A 1 119 ? 14.627 -15.552 27.805 0.41 35.83  ? 120 THR A N   1 
ATOM   1039 N  N   B THR A 1 119 ? 14.808 -15.901 27.733 0.59 32.07  ? 120 THR A N   1 
ATOM   1040 C  CA  A THR A 1 119 ? 14.360 -16.776 28.566 0.41 35.87  ? 120 THR A CA  1 
ATOM   1041 C  CA  B THR A 1 119 ? 14.521 -17.079 28.571 0.59 32.28  ? 120 THR A CA  1 
ATOM   1042 C  C   A THR A 1 119 ? 14.542 -16.565 30.046 0.41 38.17  ? 120 THR A C   1 
ATOM   1043 C  C   B THR A 1 119 ? 14.720 -16.807 30.074 0.59 35.74  ? 120 THR A C   1 
ATOM   1044 O  O   A THR A 1 119 ? 13.705 -17.026 30.824 0.41 38.67  ? 120 THR A O   1 
ATOM   1045 O  O   B THR A 1 119 ? 14.062 -17.456 30.882 0.59 35.04  ? 120 THR A O   1 
ATOM   1046 C  CB  A THR A 1 119 ? 15.192 -17.907 28.009 0.41 43.54  ? 120 THR A CB  1 
ATOM   1047 C  CB  B THR A 1 119 ? 15.270 -18.339 28.112 0.59 33.43  ? 120 THR A CB  1 
ATOM   1048 O  OG1 A THR A 1 119 ? 14.842 -17.969 26.645 0.41 43.94  ? 120 THR A OG1 1 
ATOM   1049 O  OG1 B THR A 1 119 ? 14.638 -19.462 28.732 0.59 34.10  ? 120 THR A OG1 1 
ATOM   1050 C  CG2 A THR A 1 119 ? 14.889 -19.243 28.666 0.41 43.54  ? 120 THR A CG2 1 
ATOM   1051 C  CG2 B THR A 1 119 ? 16.743 -18.329 28.487 0.59 26.30  ? 120 THR A CG2 1 
ATOM   1052 N  N   . CYS A 1 120 ? 15.634 -15.875 30.441 1.00 32.94  ? 121 CYS A N   1 
ATOM   1053 C  CA  . CYS A 1 120 ? 15.892 -15.531 31.849 1.00 33.55  ? 121 CYS A CA  1 
ATOM   1054 C  C   . CYS A 1 120 ? 14.684 -14.800 32.399 1.00 39.89  ? 121 CYS A C   1 
ATOM   1055 O  O   . CYS A 1 120 ? 14.204 -15.143 33.487 1.00 39.35  ? 121 CYS A O   1 
ATOM   1056 C  CB  . CYS A 1 120 ? 17.145 -14.674 31.965 1.00 32.35  ? 121 CYS A CB  1 
ATOM   1057 S  SG  . CYS A 1 120 ? 18.678 -15.602 31.791 1.00 34.89  ? 121 CYS A SG  1 
ATOM   1058 N  N   . ARG A 1 121 ? 14.157 -13.834 31.607 1.00 38.46  ? 122 ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 121 ? 12.956 -13.065 31.936 1.00 40.47  ? 122 ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 121 ? 11.755 -14.004 32.195 1.00 45.08  ? 122 ARG A C   1 
ATOM   1061 O  O   . ARG A 1 121 ? 11.041 -13.832 33.191 1.00 44.98  ? 122 ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 121 ? 12.621 -12.089 30.799 1.00 42.24  ? 122 ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 121 ? 13.442 -10.816 30.828 1.00 58.44  ? 122 ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 121 ? 12.606 -9.608  30.446 1.00 74.34  ? 122 ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 121 ? 13.018 -9.040  29.160 1.00 83.43  ? 122 ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 121 ? 13.933 -8.084  29.016 1.00 93.15  ? 122 ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 121 ? 14.553 -7.581  30.078 1.00 74.35  ? 122 ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 121 ? 14.239 -7.628  27.809 1.00 80.69  ? 122 ARG A NH2 1 
ATOM   1069 N  N   . LYS A 1 122 ? 11.557 -15.003 31.310 1.00 42.35  ? 123 LYS A N   1 
ATOM   1070 C  CA  . LYS A 1 122 ? 10.464 -15.980 31.407 1.00 43.88  ? 123 LYS A CA  1 
ATOM   1071 C  C   . LYS A 1 122 ? 10.615 -16.884 32.628 1.00 46.99  ? 123 LYS A C   1 
ATOM   1072 O  O   . LYS A 1 122 ? 9.627  -17.140 33.309 1.00 46.81  ? 123 LYS A O   1 
ATOM   1073 C  CB  . LYS A 1 122 ? 10.355 -16.821 30.118 1.00 45.88  ? 123 LYS A CB  1 
ATOM   1074 C  CG  . LYS A 1 122 ? 9.859  -16.031 28.912 1.00 63.47  ? 123 LYS A CG  1 
ATOM   1075 C  CD  . LYS A 1 122 ? 9.561  -16.932 27.716 1.00 74.13  ? 123 LYS A CD  1 
ATOM   1076 C  CE  . LYS A 1 122 ? 9.595  -16.206 26.388 1.00 83.64  ? 123 LYS A CE  1 
ATOM   1077 N  NZ  . LYS A 1 122 ? 8.559  -15.142 26.277 1.00 92.88  ? 123 LYS A NZ  1 
ATOM   1078 N  N   . PHE A 1 123 ? 11.849 -17.374 32.902 1.00 42.51  ? 124 PHE A N   1 
ATOM   1079 C  CA  . PHE A 1 123 ? 12.130 -18.228 34.061 1.00 42.95  ? 124 PHE A CA  1 
ATOM   1080 C  C   . PHE A 1 123 ? 11.934 -17.459 35.380 1.00 47.50  ? 124 PHE A C   1 
ATOM   1081 O  O   . PHE A 1 123 ? 11.386 -18.021 36.333 1.00 47.17  ? 124 PHE A O   1 
ATOM   1082 C  CB  . PHE A 1 123 ? 13.528 -18.847 33.957 1.00 43.48  ? 124 PHE A CB  1 
ATOM   1083 C  CG  . PHE A 1 123 ? 13.646 -20.148 33.181 1.00 45.58  ? 124 PHE A CG  1 
ATOM   1084 C  CD1 . PHE A 1 123 ? 13.096 -20.275 31.905 1.00 48.95  ? 124 PHE A CD1 1 
ATOM   1085 C  CD2 . PHE A 1 123 ? 14.366 -21.221 33.695 1.00 48.51  ? 124 PHE A CD2 1 
ATOM   1086 C  CE1 . PHE A 1 123 ? 13.221 -21.470 31.184 1.00 49.27  ? 124 PHE A CE1 1 
ATOM   1087 C  CE2 . PHE A 1 123 ? 14.499 -22.412 32.968 1.00 50.28  ? 124 PHE A CE2 1 
ATOM   1088 C  CZ  . PHE A 1 123 ? 13.923 -22.528 31.721 1.00 47.92  ? 124 PHE A CZ  1 
ATOM   1089 N  N   . ILE A 1 124 ? 12.323 -16.164 35.417 1.00 43.03  ? 125 ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 124 ? 12.114 -15.317 36.607 1.00 44.77  ? 125 ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 124 ? 10.613 -15.082 36.854 1.00 51.48  ? 125 ILE A C   1 
ATOM   1092 O  O   . ILE A 1 124 ? 10.155 -15.208 37.997 1.00 52.21  ? 125 ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 124 ? 12.950 -14.008 36.535 1.00 47.20  ? 125 ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 124 ? 14.446 -14.338 36.687 1.00 45.80  ? 125 ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 124 ? 12.514 -12.963 37.604 1.00 50.26  ? 125 ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 124 ? 15.381 -13.288 36.155 1.00 52.34  ? 125 ILE A CD1 1 
ATOM   1097 N  N   . LYS A 1 125 ? 9.850  -14.782 35.775 1.00 49.73  ? 126 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 125 ? 8.401  -14.529 35.828 1.00 52.51  ? 126 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 125 ? 7.625  -15.766 36.329 1.00 57.68  ? 126 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 125 ? 6.633  -15.616 37.042 1.00 58.16  ? 126 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 125 ? 7.885  -14.072 34.453 1.00 56.03  ? 126 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 125 ? 6.513  -13.404 34.487 1.00 74.54  ? 126 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 125 ? 5.904  -13.313 33.096 1.00 87.20  ? 126 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 125 ? 4.473  -12.833 33.131 1.00 101.98 ? 126 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 125 ? 3.834  -12.917 31.790 1.00 112.55 ? 126 LYS A NZ  1 
ATOM   1106 N  N   . ALA A 1 126 ? 8.098  -16.979 35.985 1.00 53.23  ? 127 ALA A N   1 
ATOM   1107 C  CA  . ALA A 1 126 ? 7.474  -18.230 36.428 1.00 54.84  ? 127 ALA A CA  1 
ATOM   1108 C  C   . ALA A 1 126 ? 7.630  -18.447 37.948 1.00 61.20  ? 127 ALA A C   1 
ATOM   1109 O  O   . ALA A 1 126 ? 6.756  -19.047 38.561 1.00 61.68  ? 127 ALA A O   1 
ATOM   1110 C  CB  . ALA A 1 126 ? 8.068  -19.406 35.661 1.00 53.90  ? 127 ALA A CB  1 
ATOM   1111 N  N   . SER A 1 127 ? 8.736  -17.964 38.546 1.00 59.70  ? 128 SER A N   1 
ATOM   1112 C  CA  . SER A 1 127 ? 9.016  -18.111 39.979 1.00 62.59  ? 128 SER A CA  1 
ATOM   1113 C  C   . SER A 1 127 ? 8.319  -17.068 40.883 1.00 70.89  ? 128 SER A C   1 
ATOM   1114 O  O   . SER A 1 127 ? 8.223  -17.297 42.092 1.00 73.19  ? 128 SER A O   1 
ATOM   1115 C  CB  . SER A 1 127 ? 10.521 -18.124 40.238 1.00 66.12  ? 128 SER A CB  1 
ATOM   1116 O  OG  . SER A 1 127 ? 11.069 -19.412 40.005 1.00 77.30  ? 128 SER A OG  1 
ATOM   1117 N  N   . GLU A 1 128 ? 7.818  -15.948 40.309 1.00 67.62  ? 129 GLU A N   1 
ATOM   1118 C  CA  . GLU A 1 128 ? 7.136  -14.895 41.073 1.00 93.27  ? 129 GLU A CA  1 
ATOM   1119 C  C   . GLU A 1 128 ? 5.682  -15.255 41.410 1.00 136.19 ? 129 GLU A C   1 
ATOM   1120 O  O   . GLU A 1 128 ? 5.416  -16.295 42.010 1.00 103.75 ? 129 GLU A O   1 
ATOM   1121 C  CB  . GLU A 1 128 ? 7.241  -13.524 40.371 1.00 93.82  ? 129 GLU A CB  1 
ATOM   1122 C  CG  . GLU A 1 128 ? 6.247  -13.294 39.238 1.00 104.23 ? 129 GLU A CG  1 
ATOM   1123 C  CD  . GLU A 1 128 ? 6.426  -12.047 38.389 1.00 124.81 ? 129 GLU A CD  1 
ATOM   1124 O  OE1 . GLU A 1 128 ? 7.514  -11.426 38.439 1.00 117.53 ? 129 GLU A OE1 1 
ATOM   1125 O  OE2 . GLU A 1 128 ? 5.472  -11.698 37.657 1.00 119.05 ? 129 GLU A OE2 1 
HETATM 1126 C  C   . ACE B 2 1   ? 21.244 -35.126 5.881  1.00 30.20  ? 0   ACE D C   1 
HETATM 1127 O  O   . ACE B 2 1   ? 21.308 -33.977 6.338  1.00 30.88  ? 0   ACE D O   1 
HETATM 1128 C  CH3 . ACE B 2 1   ? 21.437 -36.333 6.779  1.00 30.12  ? 0   ACE D CH3 1 
ATOM   1129 N  N   A TRP B 2 2   ? 20.987 -35.382 4.606  0.78 27.44  ? 1   TRP D N   1 
ATOM   1130 N  N   B TRP B 2 2   ? 21.024 -35.397 4.593  0.22 27.90  ? 1   TRP D N   1 
ATOM   1131 C  CA  A TRP B 2 2   ? 20.793 -34.328 3.619  0.78 26.53  ? 1   TRP D CA  1 
ATOM   1132 C  CA  B TRP B 2 2   ? 20.777 -34.354 3.595  0.22 27.36  ? 1   TRP D CA  1 
ATOM   1133 C  C   A TRP B 2 2   ? 19.298 -34.177 3.329  0.78 30.05  ? 1   TRP D C   1 
ATOM   1134 C  C   B TRP B 2 2   ? 19.279 -34.174 3.394  0.22 30.02  ? 1   TRP D C   1 
ATOM   1135 O  O   A TRP B 2 2   ? 18.563 -35.172 3.315  0.78 30.59  ? 1   TRP D O   1 
ATOM   1136 O  O   B TRP B 2 2   ? 18.529 -35.153 3.462  0.22 29.75  ? 1   TRP D O   1 
ATOM   1137 C  CB  A TRP B 2 2   ? 21.572 -34.666 2.336  0.78 24.99  ? 1   TRP D CB  1 
ATOM   1138 C  CB  B TRP B 2 2   ? 21.484 -34.644 2.246  0.22 26.19  ? 1   TRP D CB  1 
ATOM   1139 C  CG  A TRP B 2 2   ? 23.073 -34.621 2.518  0.78 25.13  ? 1   TRP D CG  1 
ATOM   1140 C  CG  B TRP B 2 2   ? 20.827 -35.682 1.379  0.22 27.22  ? 1   TRP D CG  1 
ATOM   1141 C  CD1 A TRP B 2 2   ? 23.878 -35.624 2.977  0.78 27.71  ? 1   TRP D CD1 1 
ATOM   1142 C  CD1 B TRP B 2 2   ? 21.132 -37.009 1.319  0.22 30.27  ? 1   TRP D CD1 1 
ATOM   1143 C  CD2 A TRP B 2 2   ? 23.926 -33.492 2.292  0.78 24.89  ? 1   TRP D CD2 1 
ATOM   1144 C  CD2 B TRP B 2 2   ? 19.775 -35.469 0.423  0.22 26.99  ? 1   TRP D CD2 1 
ATOM   1145 N  NE1 A TRP B 2 2   ? 25.186 -35.174 3.074  0.78 27.06  ? 1   TRP D NE1 1 
ATOM   1146 N  NE1 B TRP B 2 2   ? 20.307 -37.647 0.424  0.22 29.73  ? 1   TRP D NE1 1 
ATOM   1147 C  CE2 A TRP B 2 2   ? 25.254 -33.901 2.575  0.78 28.26  ? 1   TRP D CE2 1 
ATOM   1148 C  CE2 B TRP B 2 2   ? 19.472 -36.724 -0.151 0.22 30.95  ? 1   TRP D CE2 1 
ATOM   1149 C  CE3 A TRP B 2 2   ? 23.703 -32.171 1.865  0.78 25.42  ? 1   TRP D CE3 1 
ATOM   1150 C  CE3 B TRP B 2 2   ? 19.037 -34.344 0.015  0.22 28.07  ? 1   TRP D CE3 1 
ATOM   1151 C  CZ2 A TRP B 2 2   ? 26.350 -33.044 2.426  0.78 27.40  ? 1   TRP D CZ2 1 
ATOM   1152 C  CZ2 B TRP B 2 2   ? 18.475 -36.883 -1.123 0.22 30.20  ? 1   TRP D CZ2 1 
ATOM   1153 C  CZ3 A TRP B 2 2   ? 24.797 -31.342 1.665  0.78 26.31  ? 1   TRP D CZ3 1 
ATOM   1154 C  CZ3 B TRP B 2 2   ? 18.041 -34.505 -0.936 0.22 29.77  ? 1   TRP D CZ3 1 
ATOM   1155 C  CH2 A TRP B 2 2   ? 26.097 -31.771 1.968  0.78 27.41  ? 1   TRP D CH2 1 
ATOM   1156 C  CH2 B TRP B 2 2   ? 17.775 -35.759 -1.502 0.22 30.29  ? 1   TRP D CH2 1 
ATOM   1157 N  N   . VAL B 2 3   ? 18.844 -32.936 3.121  1.00 25.59  ? 2   VAL D N   1 
ATOM   1158 C  CA  . VAL B 2 3   ? 17.426 -32.613 2.879  1.00 25.47  ? 2   VAL D CA  1 
ATOM   1159 C  C   . VAL B 2 3   ? 17.286 -31.551 1.777  1.00 27.71  ? 2   VAL D C   1 
ATOM   1160 O  O   . VAL B 2 3   ? 18.257 -30.852 1.440  1.00 26.91  ? 2   VAL D O   1 
ATOM   1161 C  CB  . VAL B 2 3   ? 16.689 -32.124 4.184  1.00 28.55  ? 2   VAL D CB  1 
ATOM   1162 C  CG1 . VAL B 2 3   ? 16.726 -33.167 5.313  1.00 28.31  ? 2   VAL D CG1 1 
ATOM   1163 C  CG2 . VAL B 2 3   ? 17.227 -30.763 4.678  1.00 28.37  ? 2   VAL D CG2 1 
ATOM   1164 N  N   . ILE B 2 4   ? 16.049 -31.363 1.313  1.00 25.17  ? 3   ILE D N   1 
ATOM   1165 C  CA  . ILE B 2 4   ? 15.683 -30.276 0.413  1.00 26.21  ? 3   ILE D CA  1 
ATOM   1166 C  C   . ILE B 2 4   ? 15.307 -29.132 1.398  1.00 29.84  ? 3   ILE D C   1 
ATOM   1167 O  O   . ILE B 2 4   ? 14.301 -29.262 2.103  1.00 29.87  ? 3   ILE D O   1 
ATOM   1168 C  CB  . ILE B 2 4   ? 14.473 -30.633 -0.503 1.00 28.89  ? 3   ILE D CB  1 
ATOM   1169 C  CG1 . ILE B 2 4   ? 14.741 -31.897 -1.405 1.00 27.80  ? 3   ILE D CG1 1 
ATOM   1170 C  CG2 . ILE B 2 4   ? 14.060 -29.397 -1.343 1.00 30.95  ? 3   ILE D CG2 1 
ATOM   1171 C  CD1 . ILE B 2 4   ? 16.044 -31.802 -2.348 1.00 29.36  ? 3   ILE D CD1 1 
ATOM   1172 N  N   . PRO B 2 5   ? 16.096 -28.036 1.487  1.00 28.68  ? 4   PRO D N   1 
ATOM   1173 C  CA  . PRO B 2 5   ? 15.764 -26.961 2.445  1.00 29.13  ? 4   PRO D CA  1 
ATOM   1174 C  C   . PRO B 2 5   ? 14.499 -26.181 2.073  1.00 34.12  ? 4   PRO D C   1 
ATOM   1175 O  O   . PRO B 2 5   ? 14.195 -26.035 0.889  1.00 33.05  ? 4   PRO D O   1 
ATOM   1176 C  CB  . PRO B 2 5   ? 17.017 -26.065 2.416  1.00 30.96  ? 4   PRO D CB  1 
ATOM   1177 C  CG  . PRO B 2 5   ? 17.555 -26.249 1.012  1.00 34.72  ? 4   PRO D CG  1 
ATOM   1178 C  CD  . PRO B 2 5   ? 17.315 -27.710 0.707  1.00 30.10  ? 4   PRO D CD  1 
ATOM   1179 N  N   . ALA B 2 6   ? 13.851 -25.557 3.074  1.00 31.92  ? 5   ALA D N   1 
HETATM 1180 C  C4  . 7ZO C 3 .   ? 27.286 -10.314 11.833 1.00 28.17  ? 201 7ZO A C4  1 
HETATM 1181 C  C5  . 7ZO C 3 .   ? 25.271 -9.377  12.206 1.00 30.53  ? 201 7ZO A C5  1 
HETATM 1182 C  C6  . 7ZO C 3 .   ? 23.961 -10.716 18.109 1.00 30.03  ? 201 7ZO A C6  1 
HETATM 1183 C  C7  . 7ZO C 3 .   ? 23.476 -9.413  18.159 1.00 30.66  ? 201 7ZO A C7  1 
HETATM 1184 C  C8  . 7ZO C 3 .   ? 25.524 -10.049 16.396 1.00 27.34  ? 201 7ZO A C8  1 
HETATM 1185 C  C10 . 7ZO C 3 .   ? 26.363 -10.219 14.026 1.00 26.36  ? 201 7ZO A C10 1 
HETATM 1186 C  C1  . 7ZO C 3 .   ? 23.959 -8.429  17.302 1.00 29.00  ? 201 7ZO A C1  1 
HETATM 1187 C  C2  . 7ZO C 3 .   ? 24.974 -8.761  16.411 1.00 27.78  ? 201 7ZO A C2  1 
HETATM 1188 C  C3  . 7ZO C 3 .   ? 24.982 -11.041 17.220 1.00 28.05  ? 201 7ZO A C3  1 
HETATM 1189 C  C9  . 7ZO C 3 .   ? 27.405 -10.614 13.180 1.00 25.30  ? 201 7ZO A C9  1 
HETATM 1190 C  C11 . 7ZO C 3 .   ? 22.244 -10.533 19.725 1.00 34.91  ? 201 7ZO A C11 1 
HETATM 1191 C  C12 . 7ZO C 3 .   ? 23.203 -11.534 19.115 1.00 32.51  ? 201 7ZO A C12 1 
HETATM 1192 N  N13 . 7ZO C 3 .   ? 26.218 -9.691  11.325 1.00 32.44  ? 201 7ZO A N13 1 
HETATM 1193 N  N14 . 7ZO C 3 .   ? 25.270 -9.599  13.524 1.00 29.70  ? 201 7ZO A N14 1 
HETATM 1194 N  N15 . 7ZO C 3 .   ? 22.470 -9.331  19.132 1.00 30.81  ? 201 7ZO A N15 1 
HETATM 1195 N  N16 . 7ZO C 3 .   ? 26.372 -10.507 15.357 1.00 23.87  ? 201 7ZO A N16 1 
HETATM 1196 O  O17 . 7ZO C 3 .   ? 21.403 -10.754 20.594 1.00 34.47  ? 201 7ZO A O17 1 
HETATM 1197 CL CL1 . 7ZO C 3 .   ? 28.835 -11.384 13.760 0.99 26.64  ? 201 7ZO A CL1 1 
HETATM 1198 CL CL  . CL  D 4 .   ? 21.330 -15.200 22.574 1.00 35.12  ? 202 CL  A CL  1 
HETATM 1199 S  S   A DMS E 5 .   ? 17.575 -35.370 -1.228 0.78 49.34  ? 101 DMS D S   1 
HETATM 1200 O  O   A DMS E 5 .   ? 16.315 -35.122 -0.548 0.78 50.67  ? 101 DMS D O   1 
HETATM 1201 C  C1  A DMS E 5 .   ? 18.751 -34.513 -0.212 0.78 47.55  ? 101 DMS D C1  1 
HETATM 1202 C  C2  A DMS E 5 .   ? 17.972 -37.025 -0.781 0.78 48.97  ? 101 DMS D C2  1 
HETATM 1203 O  O   . HOH F 6 .   ? 35.628 -25.646 25.616 1.00 41.74  ? 301 HOH A O   1 
HETATM 1204 O  O   . HOH F 6 .   ? 25.871 -3.398  26.371 1.00 37.47  ? 302 HOH A O   1 
HETATM 1205 O  O   . HOH F 6 .   ? 41.322 -21.656 25.182 1.00 47.24  ? 303 HOH A O   1 
HETATM 1206 O  O   . HOH F 6 .   ? 38.412 -14.889 15.487 1.00 35.77  ? 304 HOH A O   1 
HETATM 1207 O  O   . HOH F 6 .   ? 37.632 -20.367 26.975 1.00 34.77  ? 305 HOH A O   1 
HETATM 1208 O  O   . HOH F 6 .   ? 37.929 2.480   19.639 1.00 43.53  ? 306 HOH A O   1 
HETATM 1209 O  O   . HOH F 6 .   ? 22.734 -5.345  19.850 1.00 59.65  ? 307 HOH A O   1 
HETATM 1210 O  O   . HOH F 6 .   ? 44.913 -11.161 18.655 1.00 57.53  ? 308 HOH A O   1 
HETATM 1211 O  O   . HOH F 6 .   ? 18.012 -29.361 7.656  1.00 34.56  ? 309 HOH A O   1 
HETATM 1212 O  O   . HOH F 6 .   ? 43.644 -6.563  31.967 1.00 48.17  ? 310 HOH A O   1 
HETATM 1213 O  O   . HOH F 6 .   ? 44.545 -0.883  17.943 1.00 57.80  ? 311 HOH A O   1 
HETATM 1214 O  O   . HOH F 6 .   ? 27.232 -35.320 11.823 1.00 59.58  ? 312 HOH A O   1 
HETATM 1215 O  O   . HOH F 6 .   ? 16.534 -27.596 -3.277 1.00 53.67  ? 313 HOH A O   1 
HETATM 1216 O  O   . HOH F 6 .   ? 33.338 -20.784 29.600 1.00 51.42  ? 314 HOH A O   1 
HETATM 1217 O  O   . HOH F 6 .   ? 20.810 -5.851  26.023 1.00 41.99  ? 315 HOH A O   1 
HETATM 1218 O  O   . HOH F 6 .   ? 29.942 -32.083 9.569  1.00 48.17  ? 316 HOH A O   1 
HETATM 1219 O  O   . HOH F 6 .   ? 19.813 -9.506  36.982 1.00 43.50  ? 317 HOH A O   1 
HETATM 1220 O  O   . HOH F 6 .   ? 30.306 1.508   33.956 1.00 62.24  ? 318 HOH A O   1 
HETATM 1221 O  O   . HOH F 6 .   ? 26.779 -31.945 16.116 1.00 46.80  ? 319 HOH A O   1 
HETATM 1222 O  O   . HOH F 6 .   ? 22.967 -28.249 12.643 1.00 26.50  ? 320 HOH A O   1 
HETATM 1223 O  O   . HOH F 6 .   ? 31.828 -0.814  15.856 1.00 41.06  ? 321 HOH A O   1 
HETATM 1224 O  O   . HOH F 6 .   ? 23.528 -5.696  32.948 1.00 39.48  ? 322 HOH A O   1 
HETATM 1225 O  O   . HOH F 6 .   ? 41.319 -16.889 15.211 1.00 37.29  ? 323 HOH A O   1 
HETATM 1226 O  O   . HOH F 6 .   ? 22.581 -27.592 17.724 1.00 54.49  ? 324 HOH A O   1 
HETATM 1227 O  O   . HOH F 6 .   ? 13.521 -14.323 21.752 1.00 66.90  ? 325 HOH A O   1 
HETATM 1228 O  O   . HOH F 6 .   ? 32.400 -24.762 32.265 1.00 63.93  ? 326 HOH A O   1 
HETATM 1229 O  O   . HOH F 6 .   ? 14.269 -16.767 23.439 1.00 44.50  ? 327 HOH A O   1 
HETATM 1230 O  O   . HOH F 6 .   ? 27.231 -10.119 35.853 1.00 41.03  ? 328 HOH A O   1 
HETATM 1231 O  O   . HOH F 6 .   ? 32.326 -8.894  39.674 1.00 57.21  ? 329 HOH A O   1 
HETATM 1232 O  O   . HOH F 6 .   ? 41.677 -12.838 14.201 1.00 93.27  ? 330 HOH A O   1 
HETATM 1233 O  O   . HOH F 6 .   ? 28.216 -23.693 31.679 1.00 42.11  ? 331 HOH A O   1 
HETATM 1234 O  O   . HOH F 6 .   ? 34.887 -18.875 13.861 0.50 30.26  ? 332 HOH A O   1 
HETATM 1235 O  O   . HOH F 6 .   ? 4.331  -20.123 37.934 1.00 63.04  ? 333 HOH A O   1 
HETATM 1236 O  O   . HOH F 6 .   ? 21.732 -29.649 -5.237 1.00 39.22  ? 334 HOH A O   1 
HETATM 1237 O  O   . HOH F 6 .   ? 7.077  -16.902 32.367 1.00 59.22  ? 335 HOH A O   1 
HETATM 1238 O  O   . HOH F 6 .   ? 29.592 -2.120  13.799 1.00 66.12  ? 336 HOH A O   1 
HETATM 1239 O  O   . HOH F 6 .   ? 28.256 -8.774  39.947 1.00 49.50  ? 337 HOH A O   1 
HETATM 1240 O  O   . HOH F 6 .   ? 30.270 -0.462  36.810 1.00 55.87  ? 338 HOH A O   1 
HETATM 1241 O  O   . HOH F 6 .   ? 27.340 -28.137 18.657 1.00 31.26  ? 339 HOH A O   1 
HETATM 1242 O  O   . HOH F 6 .   ? 12.630 -20.448 42.485 1.00 64.41  ? 340 HOH A O   1 
HETATM 1243 O  O   . HOH F 6 .   ? 26.801 -16.477 38.652 1.00 51.16  ? 341 HOH A O   1 
HETATM 1244 O  O   . HOH F 6 .   ? 26.436 -7.690  36.825 1.00 55.24  ? 342 HOH A O   1 
HETATM 1245 O  O   . HOH F 6 .   ? 26.037 -21.792 38.624 1.00 43.17  ? 343 HOH A O   1 
HETATM 1246 O  O   . HOH F 6 .   ? 25.704 -2.701  19.867 1.00 65.54  ? 344 HOH A O   1 
HETATM 1247 O  O   . HOH F 6 .   ? 43.918 -4.361  25.778 1.00 48.68  ? 345 HOH A O   1 
HETATM 1248 O  O   . HOH F 6 .   ? 27.173 -2.475  16.129 1.00 64.15  ? 346 HOH A O   1 
HETATM 1249 O  O   . HOH F 6 .   ? 41.302 -6.969  35.921 1.00 48.81  ? 347 HOH A O   1 
HETATM 1250 O  O   . HOH F 6 .   ? 21.490 -27.052 14.516 0.50 40.54  ? 348 HOH A O   1 
HETATM 1251 O  O   . HOH F 6 .   ? 15.388 -9.917  24.807 1.00 54.30  ? 349 HOH A O   1 
HETATM 1252 O  O   . HOH F 6 .   ? 20.542 -13.358 20.401 1.00 56.26  ? 350 HOH A O   1 
HETATM 1253 O  O   . HOH F 6 .   ? 21.930 -24.946 18.321 1.00 24.05  ? 351 HOH A O   1 
HETATM 1254 O  O   . HOH F 6 .   ? 24.840 -26.772 19.016 1.00 36.93  ? 352 HOH A O   1 
HETATM 1255 O  O   . HOH F 6 .   ? 24.043 -15.765 21.173 1.00 31.96  ? 353 HOH A O   1 
HETATM 1256 O  O   . HOH F 6 .   ? 44.415 -12.424 41.205 1.00 55.78  ? 354 HOH A O   1 
HETATM 1257 O  O   . HOH F 6 .   ? 20.810 -7.184  19.738 1.00 60.76  ? 355 HOH A O   1 
HETATM 1258 O  O   . HOH F 6 .   ? 36.869 -5.587  12.147 1.00 38.93  ? 356 HOH A O   1 
HETATM 1259 O  O   . HOH F 6 .   ? 21.433 -29.912 14.176 1.00 74.18  ? 357 HOH A O   1 
HETATM 1260 O  O   . HOH F 6 .   ? 45.982 -14.175 21.507 1.00 63.31  ? 358 HOH A O   1 
HETATM 1261 O  O   . HOH F 6 .   ? 29.081 -31.176 7.259  1.00 32.09  ? 359 HOH A O   1 
HETATM 1262 O  O   . HOH F 6 .   ? 29.390 -27.376 20.637 1.00 28.73  ? 360 HOH A O   1 
HETATM 1263 O  O   . HOH F 6 .   ? 26.065 -22.531 29.922 1.00 27.79  ? 361 HOH A O   1 
HETATM 1264 O  O   . HOH F 6 .   ? 28.504 -24.197 34.351 1.00 55.53  ? 362 HOH A O   1 
HETATM 1265 O  O   . HOH F 6 .   ? 37.505 3.427   15.660 1.00 44.26  ? 363 HOH A O   1 
HETATM 1266 O  O   . HOH F 6 .   ? 46.232 -15.871 27.638 1.00 63.77  ? 364 HOH A O   1 
HETATM 1267 O  O   A HOH F 6 .   ? 19.073 -22.958 4.248  0.60 39.12  ? 365 HOH A O   1 
HETATM 1268 O  O   . HOH F 6 .   ? 10.847 -11.321 34.425 1.00 55.33  ? 366 HOH A O   1 
HETATM 1269 O  O   . HOH F 6 .   ? 22.246 -34.074 26.322 1.00 76.98  ? 367 HOH A O   1 
HETATM 1270 O  O   . HOH F 6 .   ? 39.045 -18.928 33.357 1.00 53.26  ? 368 HOH A O   1 
HETATM 1271 O  O   . HOH F 6 .   ? 46.337 -29.800 21.258 1.00 70.73  ? 369 HOH A O   1 
HETATM 1272 O  O   . HOH F 6 .   ? 42.455 -10.461 15.453 1.00 50.57  ? 370 HOH A O   1 
HETATM 1273 O  O   . HOH F 6 .   ? 21.341 -31.286 29.940 1.00 66.29  ? 371 HOH A O   1 
HETATM 1274 O  O   . HOH F 6 .   ? 46.854 -21.862 17.783 1.00 43.00  ? 372 HOH A O   1 
HETATM 1275 O  O   . HOH F 6 .   ? 30.689 -28.811 22.671 1.00 40.28  ? 373 HOH A O   1 
HETATM 1276 O  O   . HOH F 6 .   ? 37.413 -6.442  34.265 1.00 42.19  ? 374 HOH A O   1 
HETATM 1277 O  O   . HOH F 6 .   ? 44.735 -8.566  17.884 1.00 63.89  ? 375 HOH A O   1 
HETATM 1278 O  O   . HOH F 6 .   ? 23.260 -17.123 44.353 1.00 64.19  ? 376 HOH A O   1 
HETATM 1279 O  O   . HOH F 6 .   ? 46.288 -18.918 19.680 1.00 52.07  ? 377 HOH A O   1 
HETATM 1280 O  O   . HOH F 6 .   ? 26.062 -19.157 41.754 1.00 74.12  ? 378 HOH A O   1 
HETATM 1281 O  O   . HOH F 6 .   ? 34.171 -7.843  35.616 1.00 35.69  ? 379 HOH A O   1 
HETATM 1282 O  O   . HOH F 6 .   ? 25.927 -4.517  17.875 1.00 49.93  ? 380 HOH A O   1 
HETATM 1283 O  O   . HOH F 6 .   ? 22.661 -34.012 8.856  1.00 34.36  ? 381 HOH A O   1 
HETATM 1284 O  O   . HOH F 6 .   ? 31.839 -31.832 14.627 1.00 45.38  ? 382 HOH A O   1 
HETATM 1285 O  O   . HOH F 6 .   ? 20.097 -15.715 40.823 1.00 36.62  ? 383 HOH A O   1 
HETATM 1286 O  O   . HOH F 6 .   ? 43.544 -10.655 35.326 1.00 66.36  ? 384 HOH A O   1 
HETATM 1287 O  O   . HOH F 6 .   ? 27.710 -23.019 13.861 0.50 28.87  ? 385 HOH A O   1 
HETATM 1288 O  O   . HOH F 6 .   ? 26.311 -7.874  9.074  1.00 47.34  ? 386 HOH A O   1 
HETATM 1289 O  O   . HOH F 6 .   ? 42.178 -6.153  11.972 1.00 66.64  ? 387 HOH A O   1 
HETATM 1290 O  O   . HOH F 6 .   ? 18.075 -34.606 8.314  1.00 35.00  ? 388 HOH A O   1 
HETATM 1291 O  O   . HOH F 6 .   ? 45.308 -12.673 23.655 1.00 48.03  ? 389 HOH A O   1 
HETATM 1292 O  O   . HOH F 6 .   ? 47.274 -25.203 21.571 1.00 56.78  ? 390 HOH A O   1 
HETATM 1293 O  O   . HOH F 6 .   ? 27.070 -1.668  21.964 1.00 57.38  ? 391 HOH A O   1 
HETATM 1294 O  O   . HOH F 6 .   ? 46.035 -8.844  44.107 1.00 53.98  ? 392 HOH A O   1 
HETATM 1295 O  O   . HOH F 6 .   ? 40.353 -19.606 29.006 1.00 37.10  ? 393 HOH A O   1 
HETATM 1296 O  O   . HOH F 6 .   ? 11.401 -14.875 40.654 1.00 91.02  ? 394 HOH A O   1 
HETATM 1297 O  O   . HOH F 6 .   ? 33.025 -29.644 21.573 1.00 45.10  ? 395 HOH A O   1 
HETATM 1298 O  O   . HOH F 6 .   ? 23.687 -15.693 17.821 1.00 43.78  ? 396 HOH A O   1 
HETATM 1299 O  O   . HOH F 6 .   ? 33.785 -33.045 12.308 1.00 45.66  ? 397 HOH A O   1 
HETATM 1300 O  O   . HOH F 6 .   ? 22.834 -14.772 40.348 1.00 36.09  ? 398 HOH A O   1 
HETATM 1301 O  O   . HOH F 6 .   ? 10.120 -11.706 39.901 1.00 67.04  ? 399 HOH A O   1 
HETATM 1302 O  O   . HOH F 6 .   ? 41.197 -17.098 35.192 1.00 45.39  ? 400 HOH A O   1 
HETATM 1303 O  O   . HOH F 6 .   ? 21.012 -23.090 42.068 1.00 50.29  ? 401 HOH A O   1 
HETATM 1304 O  O   . HOH F 6 .   ? 19.666 -27.411 10.114 1.00 56.72  ? 402 HOH A O   1 
HETATM 1305 O  O   . HOH F 6 .   ? 37.958 -16.297 12.731 1.00 54.36  ? 403 HOH A O   1 
HETATM 1306 O  O   . HOH F 6 .   ? 35.428 2.055   13.589 1.00 59.40  ? 404 HOH A O   1 
HETATM 1307 O  O   . HOH F 6 .   ? 45.491 -10.504 30.363 1.00 60.83  ? 405 HOH A O   1 
HETATM 1308 O  O   . HOH F 6 .   ? 22.422 -10.127 14.414 1.00 43.58  ? 406 HOH A O   1 
HETATM 1309 O  O   . HOH F 6 .   ? 46.984 -20.160 21.974 1.00 66.07  ? 407 HOH A O   1 
HETATM 1310 O  O   . HOH F 6 .   ? 34.777 -33.348 21.930 1.00 61.11  ? 408 HOH A O   1 
HETATM 1311 O  O   . HOH F 6 .   ? 32.121 -15.610 39.837 1.00 38.99  ? 409 HOH A O   1 
HETATM 1312 O  O   . HOH F 6 .   ? 41.981 -8.194  13.787 1.00 65.80  ? 410 HOH A O   1 
HETATM 1313 O  O   . HOH F 6 .   ? 44.576 -16.424 29.705 1.00 49.19  ? 411 HOH A O   1 
HETATM 1314 O  O   . HOH F 6 .   ? 35.202 -29.702 23.578 1.00 50.47  ? 412 HOH A O   1 
HETATM 1315 O  O   . HOH F 6 .   ? 30.336 -10.444 40.590 1.00 43.54  ? 413 HOH A O   1 
HETATM 1316 O  O   B HOH F 6 .   ? 37.259 -11.880 40.046 0.50 38.57  ? 414 HOH A O   1 
HETATM 1317 O  O   . HOH F 6 .   ? 29.551 -0.762  22.178 1.00 59.59  ? 415 HOH A O   1 
HETATM 1318 O  O   . HOH F 6 .   ? 45.924 -17.169 17.239 1.00 63.43  ? 416 HOH A O   1 
HETATM 1319 O  O   . HOH F 6 .   ? 39.947 -5.550  33.892 1.00 44.33  ? 417 HOH A O   1 
HETATM 1320 O  O   . HOH F 6 .   ? 37.217 -2.479  11.579 1.00 66.50  ? 418 HOH A O   1 
HETATM 1321 O  O   . HOH F 6 .   ? 33.926 -17.620 39.393 1.00 65.58  ? 419 HOH A O   1 
HETATM 1322 O  O   . HOH F 6 .   ? 27.492 -25.673 28.160 1.00 57.55  ? 420 HOH A O   1 
HETATM 1323 O  O   . HOH F 6 .   ? 44.794 -8.028  15.204 1.00 75.45  ? 421 HOH A O   1 
HETATM 1324 O  O   . HOH F 6 .   ? 44.362 -26.023 26.561 1.00 62.16  ? 422 HOH A O   1 
HETATM 1325 O  O   . HOH F 6 .   ? 33.530 -0.248  19.985 1.00 48.62  ? 423 HOH A O   1 
HETATM 1326 O  O   . HOH F 6 .   ? 23.488 -30.511 19.213 1.00 69.40  ? 424 HOH A O   1 
HETATM 1327 O  O   . HOH F 6 .   ? 26.171 -29.320 22.602 1.00 61.69  ? 425 HOH A O   1 
HETATM 1328 O  O   . HOH F 6 .   ? 28.256 -2.582  11.386 1.00 73.69  ? 426 HOH A O   1 
HETATM 1329 O  O   . HOH F 6 .   ? 28.710 -16.046 41.417 1.00 70.89  ? 427 HOH A O   1 
HETATM 1330 O  O   . HOH F 6 .   ? 29.926 -22.555 36.711 1.00 78.41  ? 428 HOH A O   1 
HETATM 1331 O  O   . HOH F 6 .   ? 42.849 -18.266 30.749 1.00 49.69  ? 429 HOH A O   1 
HETATM 1332 O  O   . HOH F 6 .   ? 45.851 -5.518  23.765 1.00 52.33  ? 430 HOH A O   1 
HETATM 1333 O  O   . HOH F 6 .   ? 31.860 -26.148 27.036 1.00 48.75  ? 431 HOH A O   1 
HETATM 1334 O  O   . HOH F 6 .   ? 25.771 -15.825 41.084 1.00 53.53  ? 432 HOH A O   1 
HETATM 1335 O  O   . HOH F 6 .   ? 32.463 -4.014  41.237 1.00 63.28  ? 433 HOH A O   1 
HETATM 1336 O  O   . HOH F 6 .   ? 37.738 -27.042 28.433 1.00 63.76  ? 434 HOH A O   1 
HETATM 1337 O  O   . HOH F 6 .   ? 47.970 -23.176 19.897 1.00 67.17  ? 435 HOH A O   1 
HETATM 1338 O  O   . HOH F 6 .   ? 31.938 0.178   13.319 1.00 63.14  ? 436 HOH A O   1 
HETATM 1339 O  O   . HOH F 6 .   ? 35.205 -4.082  10.659 1.00 48.98  ? 437 HOH A O   1 
HETATM 1340 O  O   . HOH F 6 .   ? 28.318 -29.200 26.856 1.00 84.28  ? 438 HOH A O   1 
HETATM 1341 O  O   . HOH F 6 .   ? 27.172 -34.658 17.924 1.00 79.30  ? 439 HOH A O   1 
HETATM 1342 O  O   . HOH F 6 .   ? 20.063 -35.313 10.157 1.00 42.04  ? 440 HOH A O   1 
HETATM 1343 O  O   . HOH F 6 .   ? 19.393 -31.693 13.955 1.00 74.61  ? 441 HOH A O   1 
HETATM 1344 O  O   . HOH F 6 .   ? 24.266 -21.484 41.064 1.00 60.83  ? 442 HOH A O   1 
HETATM 1345 O  O   . HOH F 6 .   ? 23.008 -2.799  26.204 1.00 61.91  ? 443 HOH A O   1 
HETATM 1346 O  O   . HOH F 6 .   ? 37.102 -24.398 27.532 1.00 58.11  ? 444 HOH A O   1 
HETATM 1347 O  O   . HOH F 6 .   ? 30.983 -34.417 14.798 1.00 65.97  ? 445 HOH A O   1 
HETATM 1348 O  O   . HOH F 6 .   ? 47.149 -12.992 28.568 1.00 64.67  ? 446 HOH A O   1 
HETATM 1349 O  O   . HOH F 6 .   ? 33.790 -10.908 41.582 0.50 56.98  ? 447 HOH A O   1 
HETATM 1350 O  O   . HOH F 6 .   ? 32.212 -1.024  22.228 1.00 61.03  ? 448 HOH A O   1 
HETATM 1351 O  O   . HOH F 6 .   ? 46.592 -14.632 17.983 1.00 68.59  ? 449 HOH A O   1 
HETATM 1352 O  O   . HOH F 6 .   ? 11.908 -18.611 22.543 1.00 62.88  ? 450 HOH A O   1 
HETATM 1353 O  O   . HOH F 6 .   ? 34.542 -18.744 36.209 1.00 66.36  ? 451 HOH A O   1 
HETATM 1354 O  O   . HOH F 6 .   ? 47.116 -11.870 25.521 1.00 71.34  ? 452 HOH A O   1 
HETATM 1355 O  O   . HOH F 6 .   ? 47.397 -28.585 17.800 1.00 66.84  ? 453 HOH A O   1 
HETATM 1356 O  O   . HOH F 6 .   ? 13.653 -16.203 39.763 1.00 76.45  ? 454 HOH A O   1 
HETATM 1357 O  O   A HOH F 6 .   ? 12.035 -20.674 27.881 0.78 52.84  ? 455 HOH A O   1 
HETATM 1358 O  O   . HOH F 6 .   ? 43.135 -3.080  33.795 1.00 62.79  ? 456 HOH A O   1 
HETATM 1359 O  O   . HOH F 6 .   ? 19.213 -7.496  35.272 1.00 61.45  ? 457 HOH A O   1 
HETATM 1360 O  O   . HOH F 6 .   ? 17.073 -28.044 9.804  1.00 56.63  ? 458 HOH A O   1 
HETATM 1361 O  O   . HOH F 6 .   ? 25.395 -5.689  35.239 1.00 59.78  ? 459 HOH A O   1 
HETATM 1362 O  O   . HOH F 6 .   ? 17.281 -8.041  24.780 1.00 59.33  ? 460 HOH A O   1 
HETATM 1363 O  O   . HOH F 6 .   ? 15.809 -15.473 41.235 1.00 65.78  ? 461 HOH A O   1 
HETATM 1364 O  O   . HOH F 6 .   ? 44.329 -13.424 13.861 0.50 74.38  ? 462 HOH A O   1 
HETATM 1365 O  O   . HOH F 6 .   ? 33.790 -14.023 41.583 0.50 44.92  ? 463 HOH A O   1 
HETATM 1366 O  O   . HOH F 6 .   ? 32.099 -23.812 34.854 1.00 72.08  ? 464 HOH A O   1 
HETATM 1367 O  O   . HOH F 6 .   ? 45.457 -12.806 16.275 1.00 73.87  ? 465 HOH A O   1 
HETATM 1368 O  O   . HOH F 6 .   ? 19.023 -28.035 13.861 0.50 72.60  ? 466 HOH A O   1 
HETATM 1369 O  O   . HOH F 6 .   ? 23.265 -4.572  17.282 1.00 73.11  ? 467 HOH A O   1 
HETATM 1370 O  O   . HOH F 6 .   ? 32.627 -20.512 37.045 1.00 79.42  ? 468 HOH A O   1 
HETATM 1371 O  O   . HOH F 6 .   ? 28.290 -29.879 24.220 1.00 69.52  ? 469 HOH A O   1 
HETATM 1372 O  O   . HOH F 6 .   ? 34.890 -23.676 32.642 1.00 64.51  ? 470 HOH A O   1 
HETATM 1373 O  O   . HOH F 6 .   ? 21.139 -5.610  34.797 1.00 62.67  ? 471 HOH A O   1 
HETATM 1374 O  O   . HOH F 6 .   ? 16.701 -6.619  34.613 1.00 83.63  ? 472 HOH A O   1 
HETATM 1375 O  O   . HOH F 6 .   ? 33.017 -0.640  42.929 1.00 60.41  ? 473 HOH A O   1 
HETATM 1376 O  O   . HOH G 6 .   ? 12.363 -24.236 -0.039 1.00 53.13  ? 201 HOH D O   1 
HETATM 1377 O  O   . HOH G 6 .   ? 15.016 -25.856 -1.833 1.00 47.16  ? 202 HOH D O   1 
HETATM 1378 O  O   . HOH G 6 .   ? 21.071 -38.265 4.035  1.00 49.68  ? 203 HOH D O   1 
HETATM 1379 O  O   . HOH G 6 .   ? 11.720 -23.537 2.967  1.00 55.55  ? 204 HOH D O   1 
HETATM 1380 O  O   . HOH G 6 .   ? 17.748 -36.410 6.091  1.00 44.25  ? 205 HOH D O   1 
HETATM 1381 O  O   . HOH G 6 .   ? 20.929 -39.530 -2.199 1.00 61.98  ? 206 HOH D O   1 
HETATM 1382 O  O   . HOH G 6 .   ? 18.679 -40.720 0.696  1.00 69.38  ? 207 HOH D O   1 
HETATM 1383 O  O   . HOH G 6 .   ? 10.634 -24.818 5.569  1.00 60.00  ? 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   ? 0.8174 1.0317 0.7637 0.0356  -0.1266 -0.0196 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8102 1.0186 0.7405 0.0187  -0.1175 -0.0228 6   ASP A CA  
3    C C   . ASP A 5   ? 0.7895 1.0283 0.7442 0.0061  -0.1130 -0.0401 6   ASP A C   
4    O O   . ASP A 5   ? 0.7810 1.0469 0.7631 0.0099  -0.1179 -0.0497 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8322 1.0090 0.7533 0.0101  -0.1005 -0.0156 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0253 1.1829 0.9140 0.0000  -0.0953 -0.0114 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0282 1.1991 0.9152 -0.0114 -0.0927 -0.0211 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1318 1.2604 0.9964 0.0025  -0.0926 0.0007  6   ASP A OD2 
9    N N   . SER A 6   ? 0.6849 0.9186 0.6292 -0.0094 -0.1032 -0.0451 7   SER A N   
10   C CA  . SER A 6   ? 0.6379 0.8928 0.6000 -0.0231 -0.0968 -0.0611 7   SER A CA  
11   C C   . SER A 6   ? 0.5828 0.8208 0.5560 -0.0342 -0.0784 -0.0636 7   SER A C   
12   O O   . SER A 6   ? 0.5697 0.8110 0.5455 -0.0473 -0.0700 -0.0737 7   SER A O   
13   C CB  . SER A 6   ? 0.7132 0.9760 0.6541 -0.0313 -0.1012 -0.0665 7   SER A CB  
14   O OG  . SER A 6   ? 0.8859 1.1213 0.7991 -0.0367 -0.0936 -0.0586 7   SER A OG  
15   N N   . CYS A 7   ? 0.4654 0.6853 0.4448 -0.0283 -0.0729 -0.0549 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4266 0.6298 0.4156 -0.0359 -0.0581 -0.0560 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4087 0.6259 0.4213 -0.0441 -0.0523 -0.0686 8   CYS A C   
18   O O   . CYS A 7   ? 0.3976 0.6379 0.4248 -0.0422 -0.0585 -0.0754 8   CYS A O   
19   C CB  . CYS A 7   ? 0.4429 0.6267 0.4329 -0.0271 -0.0558 -0.0444 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5265 0.6838 0.4863 -0.0227 -0.0560 -0.0303 8   CYS A SG  
21   N N   . ILE A 8   ? 0.2959 0.4981 0.3116 -0.0531 -0.0402 -0.0721 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2556 0.4597 0.2886 -0.0607 -0.0327 -0.0809 9   ILE A CA  
23   C C   . ILE A 8   ? 0.2824 0.4666 0.3202 -0.0553 -0.0276 -0.0722 9   ILE A C   
24   O O   . ILE A 8   ? 0.2783 0.4471 0.3060 -0.0493 -0.0276 -0.0623 9   ILE A O   
25   C CB  . ILE A 8   ? 0.2915 0.4911 0.3231 -0.0738 -0.0242 -0.0918 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3002 0.4765 0.3200 -0.0746 -0.0175 -0.0877 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3137 0.5372 0.3429 -0.0802 -0.0297 -0.1025 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3567 0.5243 0.3762 -0.0854 -0.0086 -0.0986 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2282 0.4114 0.2793 -0.0588 -0.0224 -0.0763 10  GLN A N   
30   N N   B GLN A 9   ? 0.2270 0.4123 0.2788 -0.0583 -0.0232 -0.0763 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2197 0.3847 0.2736 -0.0542 -0.0182 -0.0685 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2152 0.3833 0.2710 -0.0541 -0.0188 -0.0693 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2661 0.4147 0.3227 -0.0629 -0.0087 -0.0731 10  GLN A C   
34   C C   B GLN A 9   ? 0.2475 0.3979 0.3043 -0.0631 -0.0091 -0.0736 10  GLN A C   
35   O O   A GLN A 9   ? 0.2547 0.4108 0.3172 -0.0719 -0.0052 -0.0828 10  GLN A O   
36   O O   B GLN A 9   ? 0.2406 0.3967 0.3015 -0.0729 -0.0051 -0.0837 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2302 0.4084 0.2951 -0.0464 -0.0232 -0.0662 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2237 0.4069 0.2926 -0.0483 -0.0227 -0.0694 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2403 0.4018 0.3084 -0.0425 -0.0186 -0.0595 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.3029 0.4706 0.3771 -0.0476 -0.0162 -0.0656 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5606 0.7382 0.6430 -0.0376 -0.0212 -0.0619 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4528 0.6188 0.5289 -0.0356 -0.0206 -0.0567 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4326 0.6249 0.5273 -0.0447 -0.0179 -0.0722 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3280 0.5039 0.4019 -0.0262 -0.0293 -0.0527 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.5872 0.7622 0.6684 -0.0257 -0.0264 -0.0535 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.3291 0.4800 0.4072 -0.0356 -0.0147 -0.0534 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2516 0.3770 0.3026 -0.0602 -0.0049 -0.0665 11  PHE A N   
48   N N   B PHE A 10  ? 0.2115 0.3396 0.2638 -0.0596 -0.0056 -0.0663 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2501 0.3557 0.3002 -0.0661 0.0022  -0.0691 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2103 0.3174 0.2608 -0.0651 0.0015  -0.0683 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2655 0.3661 0.3202 -0.0648 0.0040  -0.0656 11  PHE A C   
52   C C   B PHE A 10  ? 0.2552 0.3579 0.3106 -0.0642 0.0035  -0.0653 11  PHE A C   
53   O O   A PHE A 10  ? 0.2438 0.3366 0.2975 -0.0572 0.0023  -0.0572 11  PHE A O   
54   O O   B PHE A 10  ? 0.2413 0.3387 0.2966 -0.0563 0.0014  -0.0571 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2712 0.3566 0.3141 -0.0633 0.0041  -0.0659 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2290 0.3175 0.2725 -0.0610 0.0026  -0.0636 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2937 0.3566 0.3328 -0.0680 0.0093  -0.0694 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.2515 0.3403 0.2905 -0.0652 0.0042  -0.0703 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3414 0.4013 0.3780 -0.0771 0.0135  -0.0787 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.2876 0.3941 0.3239 -0.0660 0.0007  -0.0726 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3179 0.3608 0.3540 -0.0631 0.0097  -0.0633 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.2900 0.3602 0.3264 -0.0680 0.0087  -0.0747 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3682 0.4018 0.3976 -0.0808 0.0182  -0.0810 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3041 0.4110 0.3355 -0.0710 0.0032  -0.0799 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3515 0.3703 0.3806 -0.0660 0.0129  -0.0655 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3324 0.4029 0.3660 -0.0717 0.0110  -0.0823 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3378 0.3502 0.3626 -0.0745 0.0172  -0.0738 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3027 0.3922 0.3340 -0.0739 0.0089  -0.0852 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2209 0.3271 0.2805 -0.0733 0.0083  -0.0731 12  THR A N   
70   C CA  . THR A 11  ? 0.2311 0.3356 0.2953 -0.0747 0.0118  -0.0725 12  THR A CA  
71   C C   . THR A 11  ? 0.2898 0.3672 0.3448 -0.0712 0.0141  -0.0639 12  THR A C   
72   O O   . THR A 11  ? 0.2692 0.3484 0.3278 -0.0657 0.0131  -0.0590 12  THR A O   
73   C CB  . THR A 11  ? 0.3359 0.4449 0.4028 -0.0885 0.0192  -0.0839 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3342 0.4733 0.4121 -0.0909 0.0156  -0.0928 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3880 0.4965 0.4593 -0.0924 0.0249  -0.0854 12  THR A CG2 
76   N N   A ARG A 12  ? 0.2660 0.3192 0.3096 -0.0736 0.0163  -0.0629 13  ARG A N   
77   N N   B ARG A 12  ? 0.2695 0.3226 0.3130 -0.0736 0.0163  -0.0629 13  ARG A N   
78   C CA  A ARG A 12  ? 0.2781 0.3058 0.3120 -0.0701 0.0168  -0.0558 13  ARG A CA  
79   C CA  B ARG A 12  ? 0.2828 0.3105 0.3167 -0.0701 0.0168  -0.0558 13  ARG A CA  
80   C C   A ARG A 12  ? 0.3011 0.3268 0.3358 -0.0590 0.0110  -0.0481 13  ARG A C   
81   C C   B ARG A 12  ? 0.3021 0.3280 0.3369 -0.0589 0.0110  -0.0481 13  ARG A C   
82   O O   A ARG A 12  ? 0.2906 0.2985 0.3188 -0.0555 0.0102  -0.0432 13  ARG A O   
83   O O   B ARG A 12  ? 0.2900 0.2984 0.3185 -0.0554 0.0102  -0.0431 13  ARG A O   
84   C CB  A ARG A 12  ? 0.3308 0.3312 0.3510 -0.0762 0.0204  -0.0584 13  ARG A CB  
85   C CB  B ARG A 12  ? 0.3446 0.3452 0.3650 -0.0758 0.0202  -0.0582 13  ARG A CB  
86   C CG  A ARG A 12  ? 0.4368 0.4308 0.4511 -0.0900 0.0286  -0.0655 13  ARG A CG  
87   C CG  B ARG A 12  ? 0.5022 0.4899 0.5136 -0.0879 0.0280  -0.0625 13  ARG A CG  
88   C CD  A ARG A 12  ? 0.5852 0.5718 0.5945 -0.0942 0.0330  -0.0633 13  ARG A CD  
89   C CD  B ARG A 12  ? 0.5961 0.5715 0.5994 -0.0981 0.0332  -0.0703 13  ARG A CD  
90   N NE  A ARG A 12  ? 0.6847 0.6398 0.6770 -0.0904 0.0314  -0.0554 13  ARG A NE  
91   N NE  B ARG A 12  ? 0.6555 0.6082 0.6495 -0.0922 0.0299  -0.0683 13  ARG A NE  
92   C CZ  A ARG A 12  ? 0.7808 0.7292 0.7681 -0.0894 0.0322  -0.0505 13  ARG A CZ  
93   C CZ  B ARG A 12  ? 0.7818 0.7382 0.7784 -0.0936 0.0301  -0.0746 13  ARG A CZ  
94   N NH1 A ARG A 12  ? 0.5023 0.4731 0.5020 -0.0914 0.0352  -0.0529 13  ARG A NH1 
95   N NH1 B ARG A 12  ? 0.7122 0.6480 0.7022 -0.0871 0.0273  -0.0737 13  ARG A NH1 
96   N NH2 A ARG A 12  ? 0.6660 0.5858 0.6361 -0.0858 0.0293  -0.0438 13  ARG A NH2 
97   N NH2 B ARG A 12  ? 0.4686 0.4502 0.4751 -0.1012 0.0327  -0.0828 13  ARG A NH2 
98   N N   . HIS A 13  ? 0.2371 0.2804 0.2781 -0.0543 0.0073  -0.0476 14  HIS A N   
99   C CA  . HIS A 13  ? 0.2215 0.2629 0.2622 -0.0463 0.0039  -0.0419 14  HIS A CA  
100  C C   . HIS A 13  ? 0.2633 0.2987 0.3040 -0.0413 0.0030  -0.0350 14  HIS A C   
101  O O   . HIS A 13  ? 0.2521 0.2753 0.2899 -0.0380 0.0020  -0.0323 14  HIS A O   
102  C CB  . HIS A 13  ? 0.2150 0.2736 0.2579 -0.0439 0.0011  -0.0419 14  HIS A CB  
103  C CG  . HIS A 13  ? 0.2372 0.2916 0.2778 -0.0387 0.0000  -0.0374 14  HIS A CG  
104  N ND1 . HIS A 13  ? 0.2477 0.2942 0.2876 -0.0388 0.0013  -0.0406 14  HIS A ND1 
105  C CD2 . HIS A 13  ? 0.2446 0.3016 0.2838 -0.0341 -0.0015 -0.0312 14  HIS A CD2 
106  C CE1 . HIS A 13  ? 0.2328 0.2801 0.2722 -0.0355 0.0012  -0.0373 14  HIS A CE1 
107  N NE2 . HIS A 13  ? 0.2356 0.2870 0.2729 -0.0332 -0.0001 -0.0310 14  HIS A NE2 
108  N N   . ALA A 14  ? 0.2218 0.2672 0.2669 -0.0403 0.0032  -0.0333 15  ALA A N   
109  C CA  . ALA A 14  ? 0.2287 0.2682 0.2737 -0.0359 0.0032  -0.0277 15  ALA A CA  
110  C C   . ALA A 14  ? 0.2633 0.2840 0.3016 -0.0388 0.0055  -0.0270 15  ALA A C   
111  O O   . ALA A 14  ? 0.2473 0.2587 0.2826 -0.0353 0.0042  -0.0229 15  ALA A O   
112  C CB  . ALA A 14  ? 0.2366 0.2900 0.2888 -0.0338 0.0033  -0.0279 15  ALA A CB  
113  N N   A SER A 15  ? 0.2482 0.2623 0.2822 -0.0460 0.0089  -0.0313 16  SER A N   
114  N N   B SER A 15  ? 0.2495 0.2635 0.2835 -0.0460 0.0089  -0.0313 16  SER A N   
115  N N   C SER A 15  ? 0.2445 0.2584 0.2785 -0.0460 0.0089  -0.0313 16  SER A N   
116  C CA  A SER A 15  ? 0.2638 0.2557 0.2858 -0.0496 0.0108  -0.0301 16  SER A CA  
117  C CA  B SER A 15  ? 0.2664 0.2582 0.2883 -0.0497 0.0108  -0.0301 16  SER A CA  
118  C CA  C SER A 15  ? 0.2588 0.2504 0.2807 -0.0495 0.0107  -0.0300 16  SER A CA  
119  C C   A SER A 15  ? 0.3204 0.2967 0.3357 -0.0451 0.0061  -0.0281 16  SER A C   
120  C C   B SER A 15  ? 0.3247 0.3006 0.3398 -0.0453 0.0062  -0.0281 16  SER A C   
121  C C   C SER A 15  ? 0.3225 0.2983 0.3375 -0.0453 0.0061  -0.0281 16  SER A C   
122  O O   A SER A 15  ? 0.3001 0.2626 0.3083 -0.0423 0.0036  -0.0244 16  SER A O   
123  O O   B SER A 15  ? 0.3104 0.2718 0.3178 -0.0427 0.0037  -0.0246 16  SER A O   
124  O O   C SER A 15  ? 0.3107 0.2717 0.3179 -0.0427 0.0037  -0.0246 16  SER A O   
125  C CB  A SER A 15  ? 0.3131 0.2990 0.3291 -0.0600 0.0166  -0.0357 16  SER A CB  
126  C CB  B SER A 15  ? 0.3195 0.3054 0.3355 -0.0601 0.0167  -0.0357 16  SER A CB  
127  C CB  C SER A 15  ? 0.3040 0.2896 0.3199 -0.0599 0.0168  -0.0354 16  SER A CB  
128  O OG  A SER A 15  ? 0.3797 0.3394 0.3788 -0.0640 0.0184  -0.0335 16  SER A OG  
129  O OG  B SER A 15  ? 0.3819 0.3865 0.4078 -0.0639 0.0210  -0.0398 16  SER A OG  
130  O OG  C SER A 15  ? 0.3498 0.3347 0.3647 -0.0635 0.0171  -0.0400 16  SER A OG  
131  N N   . ASP A 16  ? 0.2928 0.2731 0.3115 -0.0441 0.0046  -0.0314 17  ASP A N   
132  C CA  . ASP A 16  ? 0.2990 0.2681 0.3154 -0.0387 0.0002  -0.0319 17  ASP A CA  
133  C C   . ASP A 16  ? 0.2968 0.2736 0.3201 -0.0317 -0.0034 -0.0289 17  ASP A C   
134  O O   . ASP A 16  ? 0.2979 0.2642 0.3188 -0.0268 -0.0077 -0.0284 17  ASP A O   
135  C CB  . ASP A 16  ? 0.3190 0.2941 0.3395 -0.0398 0.0010  -0.0378 17  ASP A CB  
136  C CG  . ASP A 16  ? 0.4720 0.4341 0.4839 -0.0472 0.0047  -0.0422 17  ASP A CG  
137  O OD1 . ASP A 16  ? 0.4853 0.4308 0.4858 -0.0520 0.0070  -0.0404 17  ASP A OD1 
138  O OD2 . ASP A 16  ? 0.4850 0.4526 0.4999 -0.0496 0.0063  -0.0481 17  ASP A OD2 
139  N N   . VAL A 17  ? 0.2266 0.2210 0.2577 -0.0312 -0.0018 -0.0275 18  VAL A N   
140  C CA  . VAL A 17  ? 0.2158 0.2155 0.2514 -0.0270 -0.0033 -0.0250 18  VAL A CA  
141  C C   . VAL A 17  ? 0.2616 0.2506 0.2925 -0.0259 -0.0046 -0.0215 18  VAL A C   
142  O O   . VAL A 17  ? 0.2452 0.2308 0.2772 -0.0225 -0.0078 -0.0219 18  VAL A O   
143  C CB  . VAL A 17  ? 0.2425 0.2564 0.2816 -0.0271 -0.0011 -0.0227 18  VAL A CB  
144  C CG1 . VAL A 17  ? 0.2355 0.2494 0.2755 -0.0248 -0.0007 -0.0195 18  VAL A CG1 
145  C CG2 . VAL A 17  ? 0.2376 0.2616 0.2786 -0.0282 -0.0005 -0.0263 18  VAL A CG2 
146  N N   . LEU A 18  ? 0.2398 0.2255 0.2662 -0.0291 -0.0019 -0.0192 19  LEU A N   
147  C CA  . LEU A 18  ? 0.2529 0.2286 0.2732 -0.0294 -0.0020 -0.0165 19  LEU A CA  
148  C C   . LEU A 18  ? 0.2957 0.2532 0.3053 -0.0286 -0.0066 -0.0166 19  LEU A C   
149  O O   . LEU A 18  ? 0.2764 0.2288 0.2833 -0.0259 -0.0102 -0.0154 19  LEU A O   
150  C CB  . LEU A 18  ? 0.2681 0.2453 0.2867 -0.0338 0.0031  -0.0159 19  LEU A CB  
151  C CG  . LEU A 18  ? 0.3171 0.2869 0.3306 -0.0345 0.0046  -0.0138 19  LEU A CG  
152  C CD1 . LEU A 18  ? 0.3095 0.2871 0.3302 -0.0302 0.0044  -0.0118 19  LEU A CD1 
153  C CD2 . LEU A 18  ? 0.3698 0.3413 0.3824 -0.0398 0.0109  -0.0157 19  LEU A CD2 
154  N N   . LEU A 19  ? 0.2810 0.2281 0.2838 -0.0306 -0.0069 -0.0184 20  LEU A N   
155  C CA  . LEU A 19  ? 0.3112 0.2365 0.3008 -0.0282 -0.0125 -0.0180 20  LEU A CA  
156  C C   . LEU A 19  ? 0.3187 0.2491 0.3171 -0.0192 -0.0200 -0.0200 20  LEU A C   
157  O O   . LEU A 19  ? 0.3070 0.2272 0.2987 -0.0148 -0.0267 -0.0189 20  LEU A O   
158  C CB  . LEU A 19  ? 0.3417 0.2547 0.3236 -0.0317 -0.0105 -0.0203 20  LEU A CB  
159  C CG  . LEU A 19  ? 0.4771 0.3616 0.4413 -0.0286 -0.0164 -0.0192 20  LEU A CG  
160  C CD1 . LEU A 19  ? 0.5249 0.3877 0.4672 -0.0343 -0.0151 -0.0145 20  LEU A CD1 
161  C CD2 . LEU A 19  ? 0.5450 0.4182 0.5041 -0.0317 -0.0135 -0.0227 20  LEU A CD2 
162  N N   . ASN A 20  ? 0.2630 0.2108 0.2764 -0.0170 -0.0188 -0.0240 21  ASN A N   
163  C CA  . ASN A 20  ? 0.2486 0.2053 0.2735 -0.0100 -0.0241 -0.0284 21  ASN A CA  
164  C C   . ASN A 20  ? 0.2770 0.2433 0.3073 -0.0094 -0.0250 -0.0276 21  ASN A C   
165  O O   . ASN A 20  ? 0.2643 0.2326 0.2995 -0.0039 -0.0314 -0.0312 21  ASN A O   
166  C CB  . ASN A 20  ? 0.2608 0.2328 0.2982 -0.0100 -0.0206 -0.0338 21  ASN A CB  
167  C CG  . ASN A 20  ? 0.3960 0.3567 0.4298 -0.0081 -0.0220 -0.0374 21  ASN A CG  
168  O OD1 . ASN A 20  ? 0.3656 0.3061 0.3889 -0.0042 -0.0274 -0.0365 21  ASN A OD1 
169  N ND2 . ASN A 20  ? 0.3113 0.2822 0.3511 -0.0111 -0.0172 -0.0416 21  ASN A ND2 
170  N N   . LEU A 21  ? 0.2404 0.2132 0.2705 -0.0148 -0.0187 -0.0239 22  LEU A N   
171  C CA  . LEU A 21  ? 0.2358 0.2141 0.2689 -0.0155 -0.0183 -0.0233 22  LEU A CA  
172  C C   . LEU A 21  ? 0.2718 0.2361 0.2938 -0.0142 -0.0240 -0.0217 22  LEU A C   
173  O O   . LEU A 21  ? 0.2521 0.2206 0.2777 -0.0121 -0.0282 -0.0244 22  LEU A O   
174  C CB  . LEU A 21  ? 0.2274 0.2104 0.2600 -0.0201 -0.0108 -0.0193 22  LEU A CB  
175  C CG  . LEU A 21  ? 0.2535 0.2489 0.2933 -0.0212 -0.0063 -0.0200 22  LEU A CG  
176  C CD1 . LEU A 21  ? 0.2579 0.2544 0.2949 -0.0231 -0.0013 -0.0152 22  LEU A CD1 
177  C CD2 . LEU A 21  ? 0.3034 0.3085 0.3516 -0.0211 -0.0058 -0.0248 22  LEU A CD2 
178  N N   . ASN A 22  ? 0.2558 0.2037 0.2632 -0.0164 -0.0238 -0.0178 23  ASN A N   
179  C CA  . ASN A 22  ? 0.2786 0.2093 0.2700 -0.0161 -0.0293 -0.0156 23  ASN A CA  
180  C C   . ASN A 22  ? 0.3370 0.2611 0.3267 -0.0074 -0.0409 -0.0184 23  ASN A C   
181  O O   . ASN A 22  ? 0.3500 0.2693 0.3334 -0.0045 -0.0484 -0.0187 23  ASN A O   
182  C CB  . ASN A 22  ? 0.3118 0.2246 0.2855 -0.0223 -0.0248 -0.0117 23  ASN A CB  
183  C CG  . ASN A 22  ? 0.3985 0.2936 0.3526 -0.0247 -0.0278 -0.0090 23  ASN A CG  
184  O OD1 . ASN A 22  ? 0.3844 0.2855 0.3405 -0.0247 -0.0292 -0.0096 23  ASN A OD1 
185  N ND2 . ASN A 22  ? 0.4442 0.3161 0.3772 -0.0279 -0.0284 -0.0063 23  ASN A ND2 
186  N N   . ARG A 23  ? 0.3021 0.2264 0.2980 -0.0027 -0.0431 -0.0213 24  ARG A N   
187  C CA  . ARG A 23  ? 0.3079 0.2276 0.3058 0.0080  -0.0546 -0.0254 24  ARG A CA  
188  C C   . ARG A 23  ? 0.3465 0.2900 0.3645 0.0122  -0.0586 -0.0324 24  ARG A C   
189  O O   . ARG A 23  ? 0.3500 0.2918 0.3673 0.0198  -0.0696 -0.0352 24  ARG A O   
190  C CB  . ARG A 23  ? 0.3148 0.2321 0.3183 0.0117  -0.0541 -0.0287 24  ARG A CB  
191  C CG  . ARG A 23  ? 0.4047 0.2939 0.3860 0.0083  -0.0522 -0.0235 24  ARG A CG  
192  C CD  . ARG A 23  ? 0.4635 0.3544 0.4521 0.0081  -0.0476 -0.0276 24  ARG A CD  
193  N NE  . ARG A 23  ? 0.5671 0.4290 0.5339 0.0041  -0.0457 -0.0241 24  ARG A NE  
194  C CZ  . ARG A 23  ? 0.8066 0.6648 0.7745 0.0010  -0.0402 -0.0272 24  ARG A CZ  
195  N NH1 . ARG A 23  ? 0.5794 0.4617 0.5682 0.0014  -0.0363 -0.0335 24  ARG A NH1 
196  N NH2 . ARG A 23  ? 0.6864 0.5154 0.6324 -0.0039 -0.0378 -0.0246 24  ARG A NH2 
197  N N   . LEU A 24  ? 0.2917 0.2568 0.3260 0.0067  -0.0496 -0.0354 25  LEU A N   
198  C CA  . LEU A 24  ? 0.2685 0.2555 0.3203 0.0073  -0.0503 -0.0428 25  LEU A CA  
199  C C   . LEU A 24  ? 0.3389 0.3230 0.3828 0.0048  -0.0536 -0.0409 25  LEU A C   
200  O O   . LEU A 24  ? 0.3321 0.3265 0.3844 0.0092  -0.0616 -0.0477 25  LEU A O   
201  C CB  . LEU A 24  ? 0.2545 0.2578 0.3178 -0.0003 -0.0385 -0.0445 25  LEU A CB  
202  C CG  . LEU A 24  ? 0.3056 0.3162 0.3778 0.0005  -0.0343 -0.0483 25  LEU A CG  
203  C CD1 . LEU A 24  ? 0.2982 0.3222 0.3764 -0.0077 -0.0232 -0.0489 25  LEU A CD1 
204  C CD2 . LEU A 24  ? 0.3100 0.3307 0.3973 0.0090  -0.0414 -0.0587 25  LEU A CD2 
205  N N   . ARG A 25  ? 0.2994 0.2706 0.3279 -0.0022 -0.0476 -0.0332 26  ARG A N   
206  C CA  . ARG A 25  ? 0.3143 0.2806 0.3330 -0.0053 -0.0498 -0.0318 26  ARG A CA  
207  C C   . ARG A 25  ? 0.3822 0.3359 0.3882 0.0021  -0.0640 -0.0321 26  ARG A C   
208  O O   . ARG A 25  ? 0.3820 0.3439 0.3909 0.0035  -0.0708 -0.0369 26  ARG A O   
209  C CB  . ARG A 25  ? 0.3221 0.2756 0.3265 -0.0132 -0.0406 -0.0245 26  ARG A CB  
210  C CG  . ARG A 25  ? 0.3962 0.3443 0.3899 -0.0174 -0.0415 -0.0242 26  ARG A CG  
211  C CD  . ARG A 25  ? 0.4065 0.3455 0.3903 -0.0249 -0.0311 -0.0194 26  ARG A CD  
212  N NE  . ARG A 25  ? 0.4190 0.3402 0.3863 -0.0261 -0.0305 -0.0145 26  ARG A NE  
213  C CZ  . ARG A 25  ? 0.6068 0.5114 0.5540 -0.0311 -0.0295 -0.0119 26  ARG A CZ  
214  N NH1 . ARG A 25  ? 0.4871 0.3904 0.4278 -0.0341 -0.0307 -0.0137 26  ARG A NH1 
215  N NH2 . ARG A 25  ? 0.4723 0.3608 0.4046 -0.0344 -0.0267 -0.0085 26  ARG A NH2 
216  N N   A SER A 26  ? 0.3699 0.3026 0.3603 0.0063  -0.0686 -0.0272 27  SER A N   
217  N N   B SER A 26  ? 0.3652 0.2978 0.3556 0.0064  -0.0686 -0.0272 27  SER A N   
218  N N   C SER A 26  ? 0.3645 0.2971 0.3549 0.0064  -0.0686 -0.0272 27  SER A N   
219  C CA  A SER A 26  ? 0.4052 0.3188 0.3776 0.0144  -0.0828 -0.0256 27  SER A CA  
220  C CA  B SER A 26  ? 0.3981 0.3114 0.3701 0.0143  -0.0828 -0.0255 27  SER A CA  
221  C CA  C SER A 26  ? 0.3965 0.3095 0.3685 0.0144  -0.0828 -0.0254 27  SER A CA  
222  C C   A SER A 26  ? 0.4615 0.3923 0.4516 0.0260  -0.0960 -0.0346 27  SER A C   
223  C C   B SER A 26  ? 0.4618 0.3907 0.4508 0.0266  -0.0964 -0.0343 27  SER A C   
224  C C   C SER A 26  ? 0.4596 0.3881 0.4483 0.0266  -0.0965 -0.0342 27  SER A C   
225  O O   A SER A 26  ? 0.4824 0.4104 0.4644 0.0312  -0.1082 -0.0362 27  SER A O   
226  O O   B SER A 26  ? 0.4874 0.4100 0.4660 0.0330  -0.1098 -0.0351 27  SER A O   
227  O O   C SER A 26  ? 0.4829 0.4042 0.4607 0.0332  -0.1099 -0.0348 27  SER A O   
228  C CB  A SER A 26  ? 0.4746 0.3622 0.4296 0.0169  -0.0837 -0.0199 27  SER A CB  
229  C CB  B SER A 26  ? 0.4586 0.3436 0.4101 0.0153  -0.0828 -0.0188 27  SER A CB  
230  C CB  C SER A 26  ? 0.4573 0.3430 0.4100 0.0156  -0.0826 -0.0191 27  SER A CB  
231  O OG  A SER A 26  ? 0.6003 0.4728 0.5387 0.0056  -0.0721 -0.0133 27  SER A OG  
232  O OG  B SER A 26  ? 0.5362 0.4264 0.5020 0.0217  -0.0831 -0.0225 27  SER A OG  
233  O OG  C SER A 26  ? 0.5836 0.4446 0.5139 0.0239  -0.0966 -0.0161 27  SER A OG  
234  N N   . ARG A 27  ? 0.3975 0.3481 0.4125 0.0297  -0.0932 -0.0417 28  ARG A N   
235  C CA  . ARG A 27  ? 0.4052 0.3765 0.4425 0.0408  -0.1039 -0.0531 28  ARG A CA  
236  C C   . ARG A 27  ? 0.4188 0.4216 0.4786 0.0350  -0.0998 -0.0627 28  ARG A C   
237  O O   . ARG A 27  ? 0.4186 0.4447 0.5011 0.0420  -0.1068 -0.0747 28  ARG A O   
238  C CB  . ARG A 27  ? 0.4288 0.4034 0.4797 0.0471  -0.1022 -0.0573 28  ARG A CB  
239  C CG  . ARG A 27  ? 0.5669 0.5074 0.5939 0.0518  -0.1056 -0.0486 28  ARG A CG  
240  C CD  . ARG A 27  ? 0.6760 0.6190 0.7155 0.0555  -0.1011 -0.0529 28  ARG A CD  
241  N NE  . ARG A 27  ? 0.8879 0.8458 0.9486 0.0700  -0.1123 -0.0646 28  ARG A NE  
242  C CZ  . ARG A 27  ? 1.0899 1.0699 1.1761 0.0716  -0.1067 -0.0751 28  ARG A CZ  
243  N NH1 . ARG A 27  ? 0.9520 0.9470 1.0593 0.0855  -0.1169 -0.0874 28  ARG A NH1 
244  N NH2 . ARG A 27  ? 0.9211 0.9090 1.0119 0.0596  -0.0910 -0.0742 28  ARG A NH2 
245  N N   . ASP A 28  ? 0.3393 0.3422 0.3929 0.0221  -0.0883 -0.0583 29  ASP A N   
246  C CA  . ASP A 28  ? 0.3402 0.3665 0.4097 0.0136  -0.0817 -0.0660 29  ASP A CA  
247  C C   . ASP A 28  ? 0.3858 0.4365 0.4812 0.0111  -0.0729 -0.0755 29  ASP A C   
248  O O   . ASP A 28  ? 0.3955 0.4705 0.5102 0.0084  -0.0723 -0.0873 29  ASP A O   
249  C CB  . ASP A 28  ? 0.3786 0.4150 0.4503 0.0175  -0.0948 -0.0735 29  ASP A CB  
250  C CG  . ASP A 28  ? 0.4797 0.5315 0.5587 0.0053  -0.0863 -0.0791 29  ASP A CG  
251  O OD1 . ASP A 28  ? 0.4731 0.5146 0.5424 -0.0054 -0.0725 -0.0721 29  ASP A OD1 
252  O OD2 . ASP A 28  ? 0.5558 0.6300 0.6505 0.0066  -0.0934 -0.0913 29  ASP A OD2 
253  N N   . ILE A 29  ? 0.3067 0.3508 0.4013 0.0109  -0.0657 -0.0711 30  ILE A N   
254  C CA  . ILE A 29  ? 0.2785 0.3419 0.3928 0.0077  -0.0567 -0.0791 30  ILE A CA  
255  C C   . ILE A 29  ? 0.3144 0.3786 0.4252 -0.0055 -0.0411 -0.0751 30  ILE A C   
256  O O   . ILE A 29  ? 0.2813 0.3280 0.3759 -0.0088 -0.0357 -0.0640 30  ILE A O   
257  C CB  . ILE A 29  ? 0.3132 0.3706 0.4292 0.0153  -0.0584 -0.0786 30  ILE A CB  
258  C CG1 . ILE A 29  ? 0.3301 0.3862 0.4514 0.0305  -0.0747 -0.0843 30  ILE A CG1 
259  C CG2 . ILE A 29  ? 0.2864 0.3621 0.4189 0.0096  -0.0468 -0.0863 30  ILE A CG2 
260  C CD1 . ILE A 29  ? 0.3489 0.3874 0.4632 0.0382  -0.0770 -0.0807 30  ILE A CD1 
261  N N   A LEU A 30  ? 0.2771 0.3613 0.4028 -0.0132 -0.0338 -0.0850 31  LEU A N   
262  N N   B LEU A 30  ? 0.2779 0.3622 0.4038 -0.0131 -0.0340 -0.0851 31  LEU A N   
263  C CA  A LEU A 30  ? 0.2746 0.3576 0.3957 -0.0259 -0.0189 -0.0823 31  LEU A CA  
264  C CA  B LEU A 30  ? 0.2762 0.3600 0.3980 -0.0259 -0.0190 -0.0828 31  LEU A CA  
265  C C   A LEU A 30  ? 0.3097 0.3751 0.4130 -0.0312 -0.0154 -0.0723 31  LEU A C   
266  C C   B LEU A 30  ? 0.3119 0.3776 0.4154 -0.0312 -0.0154 -0.0725 31  LEU A C   
267  O O   A LEU A 30  ? 0.2921 0.3490 0.3866 -0.0387 -0.0045 -0.0666 31  LEU A O   
268  O O   B LEU A 30  ? 0.2965 0.3537 0.3913 -0.0386 -0.0045 -0.0667 31  LEU A O   
269  C CB  A LEU A 30  ? 0.2775 0.3564 0.3951 -0.0276 -0.0107 -0.0780 31  LEU A CB  
270  C CB  B LEU A 30  ? 0.2794 0.3605 0.3988 -0.0280 -0.0106 -0.0794 31  LEU A CB  
271  C CG  A LEU A 30  ? 0.3385 0.4365 0.4739 -0.0270 -0.0083 -0.0899 31  LEU A CG  
272  C CG  B LEU A 30  ? 0.3401 0.4416 0.4756 -0.0341 -0.0025 -0.0920 31  LEU A CG  
273  C CD1 A LEU A 30  ? 0.3265 0.4204 0.4539 -0.0346 0.0037  -0.0861 31  LEU A CD1 
274  C CD1 B LEU A 30  ? 0.3387 0.4502 0.4870 -0.0257 -0.0073 -0.0989 31  LEU A CD1 
275  C CD2 A LEU A 30  ? 0.3716 0.4938 0.5268 -0.0319 -0.0061 -0.1056 31  LEU A CD2 
276  C CD2 B LEU A 30  ? 0.3730 0.4668 0.4964 -0.0457 0.0118  -0.0868 31  LEU A CD2 
277  N N   . THR A 31  ? 0.2696 0.3293 0.3671 -0.0274 -0.0247 -0.0711 32  THR A N   
278  C CA  . THR A 31  ? 0.2712 0.3161 0.3534 -0.0330 -0.0209 -0.0642 32  THR A CA  
279  C C   . THR A 31  ? 0.3331 0.3891 0.4232 -0.0438 -0.0120 -0.0725 32  THR A C   
280  O O   . THR A 31  ? 0.3295 0.4064 0.4366 -0.0453 -0.0141 -0.0851 32  THR A O   
281  C CB  . THR A 31  ? 0.3467 0.3837 0.4193 -0.0277 -0.0327 -0.0626 32  THR A CB  
282  O OG1 . THR A 31  ? 0.3729 0.4282 0.4597 -0.0234 -0.0430 -0.0740 32  THR A OG1 
283  C CG2 . THR A 31  ? 0.3403 0.3598 0.3993 -0.0200 -0.0386 -0.0532 32  THR A CG2 
284  N N   . ASP A 32  ? 0.3061 0.3485 0.3849 -0.0516 -0.0010 -0.0666 33  ASP A N   
285  C CA  . ASP A 32  ? 0.3104 0.3576 0.3927 -0.0634 0.0099  -0.0736 33  ASP A CA  
286  C C   . ASP A 32  ? 0.3397 0.3734 0.4106 -0.0697 0.0142  -0.0716 33  ASP A C   
287  O O   . ASP A 32  ? 0.3398 0.3700 0.4086 -0.0804 0.0253  -0.0753 33  ASP A O   
288  C CB  . ASP A 32  ? 0.3358 0.3770 0.4141 -0.0683 0.0215  -0.0696 33  ASP A CB  
289  C CG  . ASP A 32  ? 0.4668 0.4876 0.5294 -0.0631 0.0233  -0.0553 33  ASP A CG  
290  O OD1 . ASP A 32  ? 0.4292 0.4391 0.4840 -0.0582 0.0187  -0.0489 33  ASP A OD1 
291  O OD2 . ASP A 32  ? 0.5960 0.6131 0.6545 -0.0643 0.0292  -0.0515 33  ASP A OD2 
292  N N   . VAL A 33  ? 0.2818 0.3059 0.3435 -0.0642 0.0067  -0.0663 34  VAL A N   
293  C CA  . VAL A 33  ? 0.2821 0.2936 0.3328 -0.0702 0.0110  -0.0657 34  VAL A CA  
294  C C   . VAL A 33  ? 0.3278 0.3372 0.3717 -0.0651 -0.0002 -0.0650 34  VAL A C   
295  O O   . VAL A 33  ? 0.3271 0.3345 0.3680 -0.0561 -0.0091 -0.0598 34  VAL A O   
296  C CB  . VAL A 33  ? 0.3254 0.3144 0.3628 -0.0714 0.0220  -0.0553 34  VAL A CB  
297  C CG1 . VAL A 33  ? 0.3128 0.2919 0.3426 -0.0621 0.0175  -0.0451 34  VAL A CG1 
298  C CG2 . VAL A 33  ? 0.3364 0.3123 0.3650 -0.0797 0.0302  -0.0577 34  VAL A CG2 
299  N N   A VAL A 34  ? 0.2972 0.3046 0.3359 -0.0719 0.0008  -0.0704 35  VAL A N   
300  N N   B VAL A 34  ? 0.3032 0.3108 0.3419 -0.0718 0.0006  -0.0704 35  VAL A N   
301  C CA  A VAL A 34  ? 0.3034 0.3047 0.3299 -0.0698 -0.0080 -0.0697 35  VAL A CA  
302  C CA  B VAL A 34  ? 0.3120 0.3132 0.3385 -0.0692 -0.0084 -0.0692 35  VAL A CA  
303  C C   A VAL A 34  ? 0.3499 0.3307 0.3620 -0.0752 0.0028  -0.0647 35  VAL A C   
304  C C   B VAL A 34  ? 0.3565 0.3378 0.3684 -0.0752 0.0020  -0.0651 35  VAL A C   
305  O O   A VAL A 34  ? 0.3530 0.3298 0.3662 -0.0836 0.0136  -0.0685 35  VAL A O   
306  O O   B VAL A 34  ? 0.3603 0.3387 0.3735 -0.0839 0.0123  -0.0697 35  VAL A O   
307  C CB  A VAL A 34  ? 0.3568 0.3755 0.3895 -0.0732 -0.0171 -0.0821 35  VAL A CB  
308  C CB  B VAL A 34  ? 0.3709 0.3896 0.4029 -0.0694 -0.0211 -0.0802 35  VAL A CB  
309  C CG1 A VAL A 34  ? 0.3669 0.3757 0.3815 -0.0722 -0.0259 -0.0807 35  VAL A CG1 
310  C CG1 B VAL A 34  ? 0.3752 0.4039 0.4140 -0.0816 -0.0142 -0.0920 35  VAL A CG1 
311  C CG2 A VAL A 34  ? 0.3507 0.3919 0.4009 -0.0659 -0.0284 -0.0887 35  VAL A CG2 
312  C CG2 B VAL A 34  ? 0.3844 0.3921 0.3980 -0.0648 -0.0323 -0.0762 35  VAL A CG2 
313  N N   . ILE A 35  ? 0.3089 0.2759 0.3075 -0.0707 0.0006  -0.0571 36  ILE A N   
314  C CA  . ILE A 35  ? 0.3096 0.2593 0.2960 -0.0749 0.0101  -0.0542 36  ILE A CA  
315  C C   . ILE A 35  ? 0.3826 0.3298 0.3557 -0.0790 0.0038  -0.0590 36  ILE A C   
316  O O   . ILE A 35  ? 0.3772 0.3238 0.3412 -0.0744 -0.0073 -0.0566 36  ILE A O   
317  C CB  . ILE A 35  ? 0.3336 0.2721 0.3151 -0.0689 0.0139  -0.0448 36  ILE A CB  
318  C CG1 . ILE A 35  ? 0.3253 0.2682 0.3187 -0.0637 0.0170  -0.0399 36  ILE A CG1 
319  C CG2 . ILE A 35  ? 0.3646 0.2884 0.3374 -0.0728 0.0244  -0.0445 36  ILE A CG2 
320  C CD1 . ILE A 35  ? 0.3499 0.2909 0.3495 -0.0678 0.0269  -0.0417 36  ILE A CD1 
321  N N   . VAL A 36  ? 0.3453 0.2890 0.3150 -0.0880 0.0109  -0.0657 37  VAL A N   
322  C CA  . VAL A 36  ? 0.3576 0.2992 0.3132 -0.0937 0.0058  -0.0717 37  VAL A CA  
323  C C   . VAL A 36  ? 0.4276 0.3498 0.3679 -0.0970 0.0156  -0.0687 37  VAL A C   
324  O O   . VAL A 36  ? 0.4084 0.3214 0.3522 -0.1001 0.0290  -0.0692 37  VAL A O   
325  C CB  . VAL A 36  ? 0.4101 0.3632 0.3728 -0.1032 0.0071  -0.0839 37  VAL A CB  
326  C CG1 . VAL A 36  ? 0.4270 0.3793 0.3740 -0.1095 0.0007  -0.0909 37  VAL A CG1 
327  C CG2 . VAL A 36  ? 0.4068 0.3829 0.3881 -0.1004 -0.0013 -0.0891 37  VAL A CG2 
328  N N   . VAL A 37  ? 0.4053 0.3201 0.3275 -0.0965 0.0089  -0.0662 38  VAL A N   
329  C CA  . VAL A 37  ? 0.4128 0.3110 0.3192 -0.1007 0.0181  -0.0649 38  VAL A CA  
330  C C   . VAL A 37  ? 0.4901 0.3842 0.3750 -0.1078 0.0110  -0.0703 38  VAL A C   
331  O O   . VAL A 37  ? 0.4718 0.3640 0.3422 -0.1047 -0.0017 -0.0667 38  VAL A O   
332  C CB  . VAL A 37  ? 0.4513 0.3427 0.3543 -0.0944 0.0187  -0.0559 38  VAL A CB  
333  C CG1 . VAL A 37  ? 0.4600 0.3382 0.3529 -0.0994 0.0315  -0.0569 38  VAL A CG1 
334  C CG2 . VAL A 37  ? 0.4250 0.3246 0.3490 -0.0861 0.0206  -0.0507 38  VAL A CG2 
335  N N   A SER A 38  ? 0.4897 0.3776 0.3673 -0.1175 0.0203  -0.0781 39  SER A N   
336  N N   B SER A 38  ? 0.4491 0.3457 0.3358 -0.1163 0.0166  -0.0797 39  SER A N   
337  C CA  A SER A 38  ? 0.5221 0.4051 0.3761 -0.1257 0.0144  -0.0839 39  SER A CA  
338  C CA  B SER A 38  ? 0.4634 0.3604 0.3345 -0.1253 0.0117  -0.0885 39  SER A CA  
339  C C   A SER A 38  ? 0.5788 0.4737 0.4274 -0.1217 -0.0064 -0.0845 39  SER A C   
340  C C   B SER A 38  ? 0.4968 0.4096 0.3680 -0.1210 -0.0081 -0.0903 39  SER A C   
341  O O   A SER A 38  ? 0.5935 0.4793 0.4178 -0.1212 -0.0169 -0.0812 39  SER A O   
342  O O   B SER A 38  ? 0.4660 0.3964 0.3584 -0.1191 -0.0112 -0.0948 39  SER A O   
343  C CB  A SER A 38  ? 0.5986 0.4634 0.4292 -0.1292 0.0201  -0.0803 39  SER A CB  
344  C CB  B SER A 38  ? 0.5318 0.4109 0.3771 -0.1316 0.0171  -0.0884 39  SER A CB  
345  O OG  A SER A 38  ? 0.7422 0.5986 0.5782 -0.1332 0.0387  -0.0833 39  SER A OG  
346  O OG  B SER A 38  ? 0.6215 0.4908 0.4726 -0.1357 0.0358  -0.0911 39  SER A OG  
347  N N   A ARG A 39  ? 0.5190 0.4336 0.3904 -0.1183 -0.0122 -0.0887 40  ARG A N   
348  N N   B ARG A 39  ? 0.4730 0.3793 0.3209 -0.1188 -0.0216 -0.0870 40  ARG A N   
349  C CA  A ARG A 39  ? 0.5199 0.4523 0.3956 -0.1125 -0.0317 -0.0918 40  ARG A CA  
350  C CA  B ARG A 39  ? 0.4811 0.4021 0.3298 -0.1118 -0.0426 -0.0889 40  ARG A CA  
351  C C   A ARG A 39  ? 0.5608 0.4891 0.4307 -0.0997 -0.0451 -0.0813 40  ARG A C   
352  C C   B ARG A 39  ? 0.5372 0.4652 0.4026 -0.0985 -0.0497 -0.0811 40  ARG A C   
353  O O   A ARG A 39  ? 0.5787 0.5125 0.4401 -0.0935 -0.0638 -0.0822 40  ARG A O   
354  O O   B ARG A 39  ? 0.5362 0.4859 0.4234 -0.0932 -0.0582 -0.0864 40  ARG A O   
355  C CB  A ARG A 39  ? 0.5463 0.4832 0.4055 -0.1196 -0.0419 -0.1013 40  ARG A CB  
356  C CB  B ARG A 39  ? 0.4951 0.4039 0.3095 -0.1134 -0.0564 -0.0882 40  ARG A CB  
357  C CG  A ARG A 39  ? 0.6816 0.6276 0.5507 -0.1322 -0.0313 -0.1144 40  ARG A CG  
358  C CG  B ARG A 39  ? 0.6033 0.5131 0.4050 -0.1266 -0.0532 -0.0994 40  ARG A CG  
359  C CD  A ARG A 39  ? 0.7757 0.7356 0.6353 -0.1370 -0.0464 -0.1255 40  ARG A CD  
360  C CD  B ARG A 39  ? 0.6105 0.5107 0.3771 -0.1277 -0.0699 -0.0995 40  ARG A CD  
361  N NE  A ARG A 39  ? 0.8627 0.8277 0.7263 -0.1518 -0.0350 -0.1391 40  ARG A NE  
362  N NE  B ARG A 39  ? 0.6143 0.5140 0.3667 -0.1418 -0.0650 -0.1105 40  ARG A NE  
363  C CZ  A ARG A 39  ? 1.0378 0.9864 0.8797 -0.1628 -0.0260 -0.1427 40  ARG A CZ  
364  C CZ  B ARG A 39  ? 0.7778 0.6987 0.5372 -0.1455 -0.0753 -0.1230 40  ARG A CZ  
365  N NH1 A ARG A 39  ? 0.8508 0.7775 0.6653 -0.1615 -0.0260 -0.1340 40  ARG A NH1 
366  N NH1 B ARG A 39  ? 0.5994 0.5458 0.3821 -0.1357 -0.0910 -0.1269 40  ARG A NH1 
367  N NH2 A ARG A 39  ? 0.8827 0.8358 0.7295 -0.1764 -0.0155 -0.1559 40  ARG A NH2 
368  N NH2 B ARG A 39  ? 0.6825 0.6008 0.4268 -0.1596 -0.0694 -0.1333 40  ARG A NH2 
369  N N   A GLU A 40  ? 0.4740 0.3923 0.3482 -0.0953 -0.0361 -0.0721 41  GLU A N   
370  N N   B GLU A 40  ? 0.4707 0.3820 0.3285 -0.0945 -0.0439 -0.0703 41  GLU A N   
371  C CA  A GLU A 40  ? 0.4629 0.3765 0.3349 -0.0844 -0.0452 -0.0627 41  GLU A CA  
372  C CA  B GLU A 40  ? 0.4471 0.3610 0.3162 -0.0829 -0.0497 -0.0627 41  GLU A CA  
373  C C   A GLU A 40  ? 0.4614 0.3898 0.3635 -0.0793 -0.0394 -0.0623 41  GLU A C   
374  C C   B GLU A 40  ? 0.4477 0.3791 0.3494 -0.0799 -0.0421 -0.0646 41  GLU A C   
375  O O   A GLU A 40  ? 0.4195 0.3474 0.3327 -0.0840 -0.0240 -0.0628 41  GLU A O   
376  O O   B GLU A 40  ? 0.4040 0.3375 0.3166 -0.0867 -0.0277 -0.0681 41  GLU A O   
377  C CB  A GLU A 40  ? 0.4942 0.3835 0.3434 -0.0863 -0.0383 -0.0538 41  GLU A CB  
378  C CB  B GLU A 40  ? 0.4743 0.3654 0.3250 -0.0821 -0.0440 -0.0522 41  GLU A CB  
379  C CG  A GLU A 40  ? 0.6889 0.5606 0.5033 -0.0926 -0.0439 -0.0540 41  GLU A CG  
380  C CG  B GLU A 40  ? 0.6925 0.5622 0.5077 -0.0896 -0.0449 -0.0509 41  GLU A CG  
381  C CD  A GLU A 40  ? 1.1429 0.9965 0.9312 -0.0866 -0.0573 -0.0455 41  GLU A CD  
382  C CD  B GLU A 40  ? 1.1747 1.0265 0.9611 -0.0842 -0.0604 -0.0438 41  GLU A CD  
383  O OE1 A GLU A 40  ? 1.1912 1.0222 0.9545 -0.0927 -0.0498 -0.0402 41  GLU A OE1 
384  O OE1 B GLU A 40  ? 1.1981 1.0583 0.9893 -0.0737 -0.0780 -0.0438 41  GLU A OE1 
385  O OE2 A GLU A 40  ? 1.1455 1.0065 0.9378 -0.0759 -0.0749 -0.0448 41  GLU A OE2 
386  O OE2 B GLU A 40  ? 1.2085 1.0365 0.9664 -0.0909 -0.0545 -0.0388 41  GLU A OE2 
387  N N   . GLN A 41  ? 0.4076 0.3489 0.3223 -0.0696 -0.0518 -0.0621 42  GLN A N   
388  C CA  . GLN A 41  ? 0.3898 0.3470 0.3321 -0.0662 -0.0465 -0.0636 42  GLN A CA  
389  C C   . GLN A 41  ? 0.4283 0.3790 0.3723 -0.0574 -0.0478 -0.0544 42  GLN A C   
390  O O   . GLN A 41  ? 0.4460 0.3880 0.3767 -0.0503 -0.0600 -0.0502 42  GLN A O   
391  C CB  . GLN A 41  ? 0.4122 0.3947 0.3730 -0.0636 -0.0576 -0.0743 42  GLN A CB  
392  C CG  . GLN A 41  ? 0.5965 0.5895 0.5605 -0.0745 -0.0538 -0.0857 42  GLN A CG  
393  C CD  . GLN A 41  ? 0.8366 0.8591 0.8237 -0.0740 -0.0620 -0.0988 42  GLN A CD  
394  O OE1 . GLN A 41  ? 0.7471 0.7845 0.7511 -0.0648 -0.0698 -0.1004 42  GLN A OE1 
395  N NE2 . GLN A 41  ? 0.8634 0.8961 0.8528 -0.0846 -0.0594 -0.1101 42  GLN A NE2 
396  N N   . PHE A 42  ? 0.3449 0.2978 0.3033 -0.0579 -0.0356 -0.0515 43  PHE A N   
397  C CA  . PHE A 42  ? 0.3425 0.2908 0.3037 -0.0508 -0.0354 -0.0439 43  PHE A CA  
398  C C   . PHE A 42  ? 0.3853 0.3503 0.3702 -0.0484 -0.0317 -0.0465 43  PHE A C   
399  O O   . PHE A 42  ? 0.3786 0.3465 0.3719 -0.0539 -0.0201 -0.0480 43  PHE A O   
400  C CB  . PHE A 42  ? 0.3700 0.3024 0.3212 -0.0545 -0.0233 -0.0370 43  PHE A CB  
401  C CG  . PHE A 42  ? 0.4115 0.3266 0.3381 -0.0594 -0.0234 -0.0354 43  PHE A CG  
402  C CD1 . PHE A 42  ? 0.4356 0.3472 0.3557 -0.0677 -0.0163 -0.0399 43  PHE A CD1 
403  C CD2 . PHE A 42  ? 0.4452 0.3451 0.3531 -0.0570 -0.0293 -0.0297 43  PHE A CD2 
404  C CE1 . PHE A 42  ? 0.4746 0.3701 0.3703 -0.0736 -0.0153 -0.0394 43  PHE A CE1 
405  C CE2 . PHE A 42  ? 0.5021 0.3839 0.3836 -0.0636 -0.0281 -0.0284 43  PHE A CE2 
406  C CZ  . PHE A 42  ? 0.4775 0.3582 0.3534 -0.0719 -0.0210 -0.0335 43  PHE A CZ  
407  N N   . ARG A 43  ? 0.3336 0.3075 0.3275 -0.0402 -0.0412 -0.0474 44  ARG A N   
408  C CA  . ARG A 43  ? 0.3069 0.2970 0.3222 -0.0384 -0.0374 -0.0507 44  ARG A CA  
409  C C   . ARG A 43  ? 0.3595 0.3406 0.3735 -0.0365 -0.0297 -0.0423 44  ARG A C   
410  O O   . ARG A 43  ? 0.3596 0.3272 0.3613 -0.0329 -0.0328 -0.0358 44  ARG A O   
411  C CB  . ARG A 43  ? 0.3180 0.3238 0.3458 -0.0300 -0.0508 -0.0576 44  ARG A CB  
412  C CG  . ARG A 43  ? 0.4258 0.4470 0.4595 -0.0314 -0.0597 -0.0685 44  ARG A CG  
413  C CD  . ARG A 43  ? 0.5563 0.6037 0.6147 -0.0258 -0.0669 -0.0800 44  ARG A CD  
414  N NE  . ARG A 43  ? 0.6738 0.7314 0.7485 -0.0309 -0.0535 -0.0823 44  ARG A NE  
415  C CZ  . ARG A 43  ? 0.8181 0.8901 0.9056 -0.0414 -0.0431 -0.0909 44  ARG A CZ  
416  N NH1 . ARG A 43  ? 0.7166 0.7990 0.8070 -0.0479 -0.0449 -0.1001 44  ARG A NH1 
417  N NH2 . ARG A 43  ? 0.6058 0.6816 0.7020 -0.0462 -0.0308 -0.0911 44  ARG A NH2 
418  N N   . ALA A 44  ? 0.3032 0.2910 0.3284 -0.0397 -0.0197 -0.0426 45  ALA A N   
419  C CA  . ALA A 44  ? 0.3010 0.2826 0.3253 -0.0376 -0.0136 -0.0353 45  ALA A CA  
420  C C   . ALA A 44  ? 0.3080 0.3004 0.3450 -0.0393 -0.0072 -0.0376 45  ALA A C   
421  O O   . ALA A 44  ? 0.2905 0.2944 0.3369 -0.0434 -0.0058 -0.0452 45  ALA A O   
422  C CB  . ALA A 44  ? 0.3157 0.2833 0.3292 -0.0411 -0.0053 -0.0296 45  ALA A CB  
423  N N   . HIS A 45  ? 0.2685 0.2573 0.3047 -0.0371 -0.0029 -0.0316 46  HIS A N   
424  C CA  . HIS A 45  ? 0.2527 0.2474 0.2951 -0.0393 0.0038  -0.0320 46  HIS A CA  
425  C C   . HIS A 45  ? 0.3029 0.2856 0.3371 -0.0424 0.0127  -0.0264 46  HIS A C   
426  O O   . HIS A 45  ? 0.2892 0.2632 0.3171 -0.0391 0.0133  -0.0204 46  HIS A O   
427  C CB  . HIS A 45  ? 0.2470 0.2450 0.2919 -0.0343 0.0016  -0.0292 46  HIS A CB  
428  C CG  . HIS A 45  ? 0.2885 0.2940 0.3402 -0.0293 -0.0074 -0.0341 46  HIS A CG  
429  N ND1 . HIS A 45  ? 0.3135 0.3101 0.3580 -0.0244 -0.0144 -0.0309 46  HIS A ND1 
430  C CD2 . HIS A 45  ? 0.2954 0.3153 0.3599 -0.0285 -0.0102 -0.0427 46  HIS A CD2 
431  C CE1 . HIS A 45  ? 0.2981 0.3011 0.3496 -0.0193 -0.0223 -0.0365 46  HIS A CE1 
432  N NE2 . HIS A 45  ? 0.2908 0.3100 0.3566 -0.0209 -0.0204 -0.0444 46  HIS A NE2 
433  N N   . LYS A 46  ? 0.2741 0.2556 0.3083 -0.0485 0.0199  -0.0290 47  LYS A N   
434  C CA  . LYS A 46  ? 0.2911 0.2573 0.3157 -0.0504 0.0282  -0.0236 47  LYS A CA  
435  C C   . LYS A 46  ? 0.3173 0.2787 0.3376 -0.0438 0.0281  -0.0154 47  LYS A C   
436  O O   . LYS A 46  ? 0.3017 0.2530 0.3168 -0.0400 0.0297  -0.0107 47  LYS A O   
437  C CB  . LYS A 46  ? 0.3307 0.2939 0.3530 -0.0588 0.0367  -0.0271 47  LYS A CB  
438  C CG  . LYS A 46  ? 0.3388 0.3051 0.3644 -0.0670 0.0390  -0.0359 47  LYS A CG  
439  C CD  . LYS A 46  ? 0.3429 0.3068 0.3663 -0.0778 0.0491  -0.0410 47  LYS A CD  
440  C CE  . LYS A 46  ? 0.3810 0.3544 0.4117 -0.0871 0.0507  -0.0527 47  LYS A CE  
441  N NZ  . LYS A 46  ? 0.4017 0.3728 0.4300 -0.1003 0.0626  -0.0594 47  LYS A NZ  
442  N N   . THR A 47  ? 0.2816 0.2518 0.3052 -0.0421 0.0260  -0.0150 48  THR A N   
443  C CA  . THR A 47  ? 0.2834 0.2510 0.3027 -0.0364 0.0251  -0.0082 48  THR A CA  
444  C C   . THR A 47  ? 0.2967 0.2658 0.3183 -0.0305 0.0205  -0.0059 48  THR A C   
445  O O   . THR A 47  ? 0.2785 0.2430 0.2971 -0.0259 0.0212  -0.0013 48  THR A O   
446  C CB  . THR A 47  ? 0.3360 0.3129 0.3570 -0.0371 0.0243  -0.0093 48  THR A CB  
447  O OG1 . THR A 47  ? 0.3418 0.3311 0.3731 -0.0366 0.0191  -0.0151 48  THR A OG1 
448  C CG2 . THR A 47  ? 0.3811 0.3535 0.3956 -0.0445 0.0317  -0.0110 48  THR A CG2 
449  N N   . VAL A 48  ? 0.2574 0.2318 0.2836 -0.0308 0.0159  -0.0094 49  VAL A N   
450  C CA  . VAL A 48  ? 0.2506 0.2241 0.2763 -0.0279 0.0133  -0.0080 49  VAL A CA  
451  C C   . VAL A 48  ? 0.2914 0.2558 0.3132 -0.0283 0.0174  -0.0071 49  VAL A C   
452  O O   . VAL A 48  ? 0.2778 0.2419 0.3003 -0.0252 0.0189  -0.0054 49  VAL A O   
453  C CB  . VAL A 48  ? 0.2779 0.2534 0.3040 -0.0286 0.0074  -0.0112 49  VAL A CB  
454  C CG1 . VAL A 48  ? 0.2718 0.2419 0.2929 -0.0285 0.0070  -0.0099 49  VAL A CG1 
455  C CG2 . VAL A 48  ? 0.2694 0.2533 0.3007 -0.0270 0.0039  -0.0130 49  VAL A CG2 
456  N N   . LEU A 49  ? 0.2576 0.2163 0.2767 -0.0324 0.0196  -0.0097 50  LEU A N   
457  C CA  . LEU A 49  ? 0.2687 0.2175 0.2836 -0.0334 0.0245  -0.0100 50  LEU A CA  
458  C C   . LEU A 49  ? 0.3023 0.2451 0.3170 -0.0285 0.0291  -0.0061 50  LEU A C   
459  O O   . LEU A 49  ? 0.2892 0.2298 0.3052 -0.0249 0.0312  -0.0059 50  LEU A O   
460  C CB  . LEU A 49  ? 0.2701 0.2144 0.2821 -0.0396 0.0266  -0.0144 50  LEU A CB  
461  C CG  . LEU A 49  ? 0.3035 0.2531 0.3147 -0.0430 0.0202  -0.0191 50  LEU A CG  
462  C CD1 . LEU A 49  ? 0.3095 0.2573 0.3193 -0.0495 0.0225  -0.0248 50  LEU A CD1 
463  C CD2 . LEU A 49  ? 0.3256 0.2708 0.3301 -0.0424 0.0178  -0.0184 50  LEU A CD2 
464  N N   . MET A 50  ? 0.2700 0.2106 0.2826 -0.0277 0.0302  -0.0032 51  MET A N   
465  C CA  . MET A 50  ? 0.2829 0.2143 0.2912 -0.0216 0.0326  0.0018  51  MET A CA  
466  C C   . MET A 50  ? 0.3028 0.2441 0.3170 -0.0137 0.0281  0.0041  51  MET A C   
467  O O   . MET A 50  ? 0.3025 0.2397 0.3179 -0.0066 0.0288  0.0055  51  MET A O   
468  C CB  . MET A 50  ? 0.3134 0.2382 0.3136 -0.0241 0.0346  0.0048  51  MET A CB  
469  C CG  . MET A 50  ? 0.3546 0.2700 0.3497 -0.0333 0.0408  0.0011  51  MET A CG  
470  S SD  . MET A 50  ? 0.4130 0.3261 0.3998 -0.0396 0.0441  0.0022  51  MET A SD  
471  C CE  . MET A 50  ? 0.3904 0.2772 0.3594 -0.0343 0.0481  0.0108  51  MET A CE  
472  N N   . ALA A 51  ? 0.2558 0.2107 0.2746 -0.0148 0.0234  0.0032  52  ALA A N   
473  C CA  . ALA A 51  ? 0.2575 0.2242 0.2824 -0.0092 0.0194  0.0038  52  ALA A CA  
474  C C   . ALA A 51  ? 0.3034 0.2748 0.3355 -0.0080 0.0208  -0.0001 52  ALA A C   
475  O O   . ALA A 51  ? 0.2943 0.2759 0.3336 -0.0028 0.0189  -0.0012 52  ALA A O   
476  C CB  . ALA A 51  ? 0.2548 0.2325 0.2819 -0.0127 0.0155  0.0023  52  ALA A CB  
477  N N   . CYS A 52  ? 0.2613 0.2266 0.2913 -0.0135 0.0242  -0.0033 53  CYS A N   
478  C CA  . CYS A 52  ? 0.2695 0.2372 0.3029 -0.0154 0.0274  -0.0080 53  CYS A CA  
479  C C   . CYS A 52  ? 0.3101 0.2696 0.3441 -0.0134 0.0331  -0.0103 53  CYS A C   
480  O O   . CYS A 52  ? 0.3061 0.2701 0.3449 -0.0143 0.0369  -0.0153 53  CYS A O   
481  C CB  . CYS A 52  ? 0.2805 0.2453 0.3073 -0.0235 0.0266  -0.0101 53  CYS A CB  
482  S SG  . CYS A 52  ? 0.3119 0.2844 0.3386 -0.0252 0.0206  -0.0092 53  CYS A SG  
483  N N   . SER A 53  ? 0.2862 0.2327 0.3142 -0.0129 0.0351  -0.0079 54  SER A N   
484  C CA  . SER A 53  ? 0.2804 0.2157 0.3068 -0.0127 0.0415  -0.0110 54  SER A CA  
485  C C   . SER A 53  ? 0.3503 0.2723 0.3737 -0.0058 0.0431  -0.0073 54  SER A C   
486  O O   . SER A 53  ? 0.3286 0.2425 0.3440 -0.0081 0.0421  -0.0031 54  SER A O   
487  C CB  . SER A 53  ? 0.3068 0.2349 0.3244 -0.0229 0.0435  -0.0137 54  SER A CB  
488  O OG  . SER A 53  ? 0.3548 0.2688 0.3673 -0.0249 0.0493  -0.0158 54  SER A OG  
489  N N   . GLY A 54  ? 0.3348 0.2531 0.3638 0.0023  0.0460  -0.0095 55  GLY A N   
490  C CA  . GLY A 54  ? 0.3420 0.2419 0.3654 0.0105  0.0475  -0.0057 55  GLY A CA  
491  C C   . GLY A 54  ? 0.3811 0.2607 0.3921 0.0021  0.0540  -0.0060 55  GLY A C   
492  O O   . GLY A 54  ? 0.3799 0.2413 0.3796 0.0035  0.0551  -0.0009 55  GLY A O   
493  N N   . LEU A 55  ? 0.3402 0.2220 0.3511 -0.0079 0.0585  -0.0124 56  LEU A N   
494  C CA  . LEU A 55  ? 0.3433 0.2092 0.3436 -0.0174 0.0643  -0.0148 56  LEU A CA  
495  C C   . LEU A 55  ? 0.3705 0.2375 0.3642 -0.0249 0.0615  -0.0114 56  LEU A C   
496  O O   . LEU A 55  ? 0.3685 0.2189 0.3526 -0.0283 0.0659  -0.0098 56  LEU A O   
497  C CB  . LEU A 55  ? 0.3331 0.2031 0.3334 -0.0264 0.0681  -0.0228 56  LEU A CB  
498  C CG  . LEU A 55  ? 0.4047 0.2597 0.3950 -0.0364 0.0744  -0.0271 56  LEU A CG  
499  C CD1 . LEU A 55  ? 0.4314 0.2638 0.4182 -0.0315 0.0827  -0.0285 56  LEU A CD1 
500  C CD2 . LEU A 55  ? 0.4354 0.2974 0.4228 -0.0463 0.0750  -0.0342 56  LEU A CD2 
501  N N   . PHE A 56  ? 0.3153 0.2006 0.3137 -0.0278 0.0551  -0.0111 57  PHE A N   
502  C CA  . PHE A 56  ? 0.3043 0.1942 0.2999 -0.0341 0.0525  -0.0099 57  PHE A CA  
503  C C   . PHE A 56  ? 0.3618 0.2451 0.3527 -0.0295 0.0521  -0.0034 57  PHE A C   
504  O O   . PHE A 56  ? 0.3499 0.2272 0.3342 -0.0363 0.0551  -0.0034 57  PHE A O   
505  C CB  . PHE A 56  ? 0.3045 0.2131 0.3060 -0.0367 0.0454  -0.0117 57  PHE A CB  
506  C CG  . PHE A 56  ? 0.3107 0.2218 0.3107 -0.0435 0.0449  -0.0178 57  PHE A CG  
507  C CD1 . PHE A 56  ? 0.3377 0.2440 0.3335 -0.0518 0.0479  -0.0230 57  PHE A CD1 
508  C CD2 . PHE A 56  ? 0.3269 0.2445 0.3277 -0.0426 0.0415  -0.0189 57  PHE A CD2 
509  C CE1 . PHE A 56  ? 0.3483 0.2568 0.3407 -0.0577 0.0461  -0.0288 57  PHE A CE1 
510  C CE2 . PHE A 56  ? 0.3596 0.2764 0.3541 -0.0490 0.0402  -0.0237 57  PHE A CE2 
511  C CZ  . PHE A 56  ? 0.3254 0.2381 0.3158 -0.0559 0.0419  -0.0285 57  PHE A CZ  
512  N N   . TYR A 57  ? 0.3270 0.2110 0.3203 -0.0185 0.0488  0.0015  58  TYR A N   
513  C CA  . TYR A 57  ? 0.3396 0.2143 0.3243 -0.0132 0.0474  0.0085  58  TYR A CA  
514  C C   . TYR A 57  ? 0.4155 0.2622 0.3852 -0.0155 0.0550  0.0106  58  TYR A C   
515  O O   . TYR A 57  ? 0.4148 0.2506 0.3720 -0.0210 0.0577  0.0137  58  TYR A O   
516  C CB  . TYR A 57  ? 0.3629 0.2442 0.3538 0.0003  0.0414  0.0119  58  TYR A CB  
517  C CG  . TYR A 57  ? 0.4231 0.2922 0.4018 0.0076  0.0382  0.0199  58  TYR A CG  
518  C CD1 . TYR A 57  ? 0.4428 0.3176 0.4152 0.0035  0.0353  0.0233  58  TYR A CD1 
519  C CD2 . TYR A 57  ? 0.4961 0.3458 0.4676 0.0188  0.0380  0.0239  58  TYR A CD2 
520  C CE1 . TYR A 57  ? 0.4765 0.3379 0.4334 0.0092  0.0323  0.0310  58  TYR A CE1 
521  C CE2 . TYR A 57  ? 0.5484 0.3834 0.5044 0.0263  0.0337  0.0323  58  TYR A CE2 
522  C CZ  . TYR A 57  ? 0.6324 0.4732 0.5800 0.0209  0.0309  0.0361  58  TYR A CZ  
523  O OH  . TYR A 57  ? 0.7198 0.5437 0.6480 0.0277  0.0266  0.0447  58  TYR A OH  
524  N N   A SER A 58  ? 0.3936 0.2273 0.3634 -0.0122 0.0594  0.0080  59  SER A N   
525  N N   B SER A 58  ? 0.3960 0.2298 0.3658 -0.0121 0.0594  0.0080  59  SER A N   
526  C CA  A SER A 58  ? 0.4219 0.2255 0.3768 -0.0144 0.0675  0.0090  59  SER A CA  
527  C CA  B SER A 58  ? 0.4259 0.2296 0.3808 -0.0143 0.0675  0.0090  59  SER A CA  
528  C C   A SER A 58  ? 0.4895 0.2887 0.4378 -0.0314 0.0749  0.0039  59  SER A C   
529  C C   B SER A 58  ? 0.4886 0.2883 0.4369 -0.0313 0.0747  0.0040  59  SER A C   
530  O O   A SER A 58  ? 0.5171 0.2945 0.4492 -0.0371 0.0810  0.0066  59  SER A O   
531  O O   B SER A 58  ? 0.5124 0.2914 0.4447 -0.0370 0.0804  0.0069  59  SER A O   
532  C CB  A SER A 58  ? 0.4587 0.2530 0.4184 -0.0075 0.0710  0.0049  59  SER A CB  
533  C CB  B SER A 58  ? 0.4709 0.2657 0.4309 -0.0080 0.0711  0.0046  59  SER A CB  
534  O OG  A SER A 58  ? 0.4808 0.2759 0.4459 0.0093  0.0649  0.0090  59  SER A OG  
535  O OG  B SER A 58  ? 0.5610 0.3239 0.5055 -0.0107 0.0797  0.0049  59  SER A OG  
536  N N   . ILE A 59  ? 0.4277 0.2476 0.3875 -0.0396 0.0740  -0.0039 60  ILE A N   
537  C CA  . ILE A 59  ? 0.4232 0.2463 0.3815 -0.0550 0.0789  -0.0112 60  ILE A CA  
538  C C   . ILE A 59  ? 0.4598 0.2887 0.4147 -0.0615 0.0788  -0.0097 60  ILE A C   
539  O O   . ILE A 59  ? 0.4764 0.2921 0.4213 -0.0726 0.0872  -0.0126 60  ILE A O   
540  C CB  . ILE A 59  ? 0.4353 0.2808 0.4059 -0.0597 0.0746  -0.0192 60  ILE A CB  
541  C CG1 . ILE A 59  ? 0.4360 0.2732 0.4065 -0.0579 0.0780  -0.0230 60  ILE A CG1 
542  C CG2 . ILE A 59  ? 0.4124 0.2687 0.3852 -0.0736 0.0760  -0.0275 60  ILE A CG2 
543  C CD1 . ILE A 59  ? 0.4717 0.3286 0.4500 -0.0603 0.0722  -0.0285 60  ILE A CD1 
544  N N   . PHE A 60  ? 0.3970 0.2457 0.3602 -0.0561 0.0705  -0.0067 61  PHE A N   
545  C CA  . PHE A 60  ? 0.3922 0.2500 0.3546 -0.0630 0.0709  -0.0076 61  PHE A CA  
546  C C   . PHE A 60  ? 0.4521 0.2902 0.3972 -0.0610 0.0743  0.0008  61  PHE A C   
547  O O   . PHE A 60  ? 0.4599 0.3021 0.4010 -0.0692 0.0774  -0.0009 61  PHE A O   
548  C CB  . PHE A 60  ? 0.3769 0.2634 0.3550 -0.0599 0.0614  -0.0100 61  PHE A CB  
549  C CG  . PHE A 60  ? 0.3700 0.2716 0.3598 -0.0632 0.0578  -0.0180 61  PHE A CG  
550  C CD1 . PHE A 60  ? 0.4057 0.3106 0.3975 -0.0745 0.0621  -0.0271 61  PHE A CD1 
551  C CD2 . PHE A 60  ? 0.3823 0.2936 0.3790 -0.0556 0.0503  -0.0168 61  PHE A CD2 
552  C CE1 . PHE A 60  ? 0.4071 0.3253 0.4072 -0.0766 0.0569  -0.0343 61  PHE A CE1 
553  C CE2 . PHE A 60  ? 0.4114 0.3325 0.4136 -0.0587 0.0464  -0.0231 61  PHE A CE2 
554  C CZ  . PHE A 60  ? 0.3868 0.3111 0.3902 -0.0683 0.0488  -0.0314 61  PHE A CZ  
555  N N   . THR A 61  ? 0.4311 0.2459 0.3641 -0.0511 0.0745  0.0087  62  THR A N   
556  C CA  . THR A 61  ? 0.4569 0.2465 0.3676 -0.0493 0.0773  0.0175  62  THR A CA  
557  C C   . THR A 61  ? 0.5639 0.3206 0.4557 -0.0585 0.0893  0.0168  62  THR A C   
558  O O   . THR A 61  ? 0.5873 0.3160 0.4549 -0.0603 0.0940  0.0236  62  THR A O   
559  C CB  . THR A 61  ? 0.5458 0.3296 0.4528 -0.0314 0.0683  0.0270  62  THR A CB  
560  O OG1 . THR A 61  ? 0.5176 0.2956 0.4320 -0.0218 0.0671  0.0261  62  THR A OG1 
561  C CG2 . THR A 61  ? 0.4749 0.2882 0.3955 -0.0256 0.0582  0.0278  62  THR A CG2 
562  N N   . ASP A 62  ? 0.5109 0.2696 0.4114 -0.0657 0.0945  0.0081  63  ASP A N   
563  C CA  . ASP A 62  ? 0.5424 0.2711 0.4260 -0.0771 0.1072  0.0052  63  ASP A CA  
564  C C   . ASP A 62  ? 0.6281 0.3629 0.5076 -0.0961 0.1156  -0.0016 63  ASP A C   
565  O O   . ASP A 62  ? 0.5910 0.3591 0.4906 -0.1025 0.1126  -0.0107 63  ASP A O   
566  C CB  . ASP A 62  ? 0.5456 0.2772 0.4404 -0.0796 0.1100  -0.0035 63  ASP A CB  
567  C CG  . ASP A 62  ? 0.7324 0.4354 0.6108 -0.0943 0.1240  -0.0086 63  ASP A CG  
568  O OD1 . ASP A 62  ? 0.8114 0.4778 0.6711 -0.0887 0.1290  -0.0025 63  ASP A OD1 
569  O OD2 . ASP A 62  ? 0.7444 0.4613 0.6283 -0.1114 0.1301  -0.0192 63  ASP A OD2 
570  N N   . GLN A 63  ? 0.6613 0.3627 0.5141 -0.1054 0.1265  0.0019  64  GLN A N   
571  C CA  . GLN A 63  ? 0.6836 0.3875 0.5294 -0.1254 0.1372  -0.0051 64  GLN A CA  
572  C C   . GLN A 63  ? 0.7262 0.4546 0.5915 -0.1418 0.1434  -0.0220 64  GLN A C   
573  O O   . GLN A 63  ? 0.7386 0.4899 0.6130 -0.1543 0.1469  -0.0310 64  GLN A O   
574  C CB  . GLN A 63  ? 0.7611 0.4174 0.5696 -0.1336 0.1495  0.0020  64  GLN A CB  
575  C CG  . GLN A 63  ? 1.0428 0.6805 0.8298 -0.1208 0.1427  0.0173  64  GLN A CG  
576  N N   . LEU A 64  ? 0.6383 0.3638 0.5107 -0.1420 0.1444  -0.0275 65  LEU A N   
577  C CA  . LEU A 64  ? 0.6099 0.3611 0.5011 -0.1565 0.1480  -0.0440 65  LEU A CA  
578  C C   . LEU A 64  ? 0.6231 0.4153 0.5428 -0.1469 0.1333  -0.0486 65  LEU A C   
579  O O   . LEU A 64  ? 0.6307 0.4545 0.5687 -0.1556 0.1315  -0.0607 65  LEU A O   
580  C CB  . LEU A 64  ? 0.6345 0.3613 0.5165 -0.1640 0.1573  -0.0493 65  LEU A CB  
581  C CG  . LEU A 64  ? 0.7460 0.4371 0.6032 -0.1824 0.1753  -0.0526 65  LEU A CG  
582  C CD1 . LEU A 64  ? 0.7648 0.4314 0.6143 -0.1864 0.1827  -0.0570 65  LEU A CD1 
583  C CD2 . LEU A 64  ? 0.7942 0.5094 0.6606 -0.2046 0.1841  -0.0678 65  LEU A CD2 
584  N N   . LYS A 65  ? 0.5253 0.3163 0.4485 -0.1294 0.1232  -0.0400 66  LYS A N   
585  C CA  . LYS A 65  ? 0.4924 0.3157 0.4373 -0.1214 0.1105  -0.0436 66  LYS A CA  
586  C C   . LYS A 65  ? 0.5435 0.3937 0.5013 -0.1152 0.1008  -0.0416 66  LYS A C   
587  O O   . LYS A 65  ? 0.5072 0.3853 0.4824 -0.1133 0.0918  -0.0477 66  LYS A O   
588  C CB  . LYS A 65  ? 0.5079 0.3210 0.4519 -0.1075 0.1053  -0.0371 66  LYS A CB  
589  C CG  . LYS A 65  ? 0.5105 0.2995 0.4446 -0.1131 0.1146  -0.0413 66  LYS A CG  
590  C CD  . LYS A 65  ? 0.4857 0.2717 0.4232 -0.0996 0.1092  -0.0375 66  LYS A CD  
591  C CE  . LYS A 65  ? 0.5794 0.3373 0.5059 -0.1027 0.1192  -0.0408 66  LYS A CE  
592  N NZ  . LYS A 65  ? 0.5984 0.3202 0.5073 -0.0960 0.1256  -0.0318 66  LYS A NZ  
593  N N   . CYS A 66  ? 0.5503 0.3906 0.4977 -0.1122 0.1024  -0.0332 67  CYS A N   
594  C CA  . CYS A 66  ? 0.5414 0.4049 0.4992 -0.1070 0.0945  -0.0316 67  CYS A CA  
595  C C   . CYS A 66  ? 0.5852 0.4787 0.5608 -0.1176 0.0945  -0.0454 67  CYS A C   
596  O O   . CYS A 66  ? 0.5755 0.4931 0.5656 -0.1115 0.0855  -0.0470 67  CYS A O   
597  C CB  . CYS A 66  ? 0.5771 0.4220 0.5166 -0.1052 0.0983  -0.0219 67  CYS A CB  
598  S SG  . CYS A 66  ? 0.6700 0.4958 0.5905 -0.1257 0.1153  -0.0270 67  CYS A SG  
599  N N   . ASN A 67  ? 0.5383 0.4298 0.5130 -0.1333 0.1046  -0.0563 68  ASN A N   
600  C CA  . ASN A 67  ? 0.5365 0.4575 0.5295 -0.1450 0.1061  -0.0723 68  ASN A CA  
601  C C   . ASN A 67  ? 0.5577 0.5012 0.5687 -0.1445 0.0977  -0.0826 68  ASN A C   
602  O O   . ASN A 67  ? 0.5337 0.5054 0.5629 -0.1520 0.0963  -0.0971 68  ASN A O   
603  C CB  . ASN A 67  ? 0.5641 0.4717 0.5455 -0.1647 0.1233  -0.0798 68  ASN A CB  
604  C CG  . ASN A 67  ? 0.7808 0.6720 0.7448 -0.1670 0.1306  -0.0719 68  ASN A CG  
605  O OD1 . ASN A 67  ? 0.8183 0.6779 0.7578 -0.1775 0.1439  -0.0683 68  ASN A OD1 
606  N ND2 . ASN A 67  ? 0.6305 0.5401 0.6040 -0.1572 0.1220  -0.0686 68  ASN A ND2 
607  N N   . LEU A 68  ? 0.5096 0.4421 0.5157 -0.1355 0.0916  -0.0761 69  LEU A N   
608  C CA  . LEU A 68  ? 0.4880 0.4383 0.5059 -0.1353 0.0833  -0.0849 69  LEU A CA  
609  C C   . LEU A 68  ? 0.4829 0.4582 0.5158 -0.1227 0.0672  -0.0843 69  LEU A C   
610  O O   . LEU A 68  ? 0.4546 0.4245 0.4842 -0.1110 0.0623  -0.0731 69  LEU A O   
611  C CB  . LEU A 68  ? 0.5007 0.4279 0.5054 -0.1321 0.0846  -0.0791 69  LEU A CB  
612  C CG  . LEU A 68  ? 0.5779 0.4770 0.5669 -0.1440 0.0999  -0.0810 69  LEU A CG  
613  C CD1 . LEU A 68  ? 0.5846 0.4629 0.5631 -0.1380 0.1002  -0.0756 69  LEU A CD1 
614  C CD2 . LEU A 68  ? 0.5871 0.5002 0.5835 -0.1621 0.1065  -0.0981 69  LEU A CD2 
615  N N   . SER A 69  ? 0.4196 0.4211 0.4680 -0.1249 0.0589  -0.0968 70  SER A N   
616  C CA  A SER A 69  ? 0.4020 0.4247 0.4628 -0.1127 0.0425  -0.0974 70  SER A CA  
617  C CA  B SER A 69  ? 0.4066 0.4284 0.4669 -0.1124 0.0426  -0.0968 70  SER A CA  
618  C C   . SER A 69  ? 0.4237 0.4390 0.4758 -0.1061 0.0331  -0.0931 70  SER A C   
619  O O   . SER A 69  ? 0.3779 0.4007 0.4324 -0.0951 0.0199  -0.0899 70  SER A O   
620  C CB  A SER A 69  ? 0.4439 0.4991 0.5262 -0.1172 0.0373  -0.1141 70  SER A CB  
621  C CB  B SER A 69  ? 0.4542 0.5089 0.5364 -0.1160 0.0372  -0.1127 70  SER A CB  
622  O OG  A SER A 69  ? 0.5251 0.5892 0.6161 -0.1236 0.0465  -0.1191 70  SER A OG  
623  O OG  B SER A 69  ? 0.5425 0.6076 0.6294 -0.1264 0.0380  -0.1258 70  SER A OG  
624  N N   . VAL A 70  ? 0.3898 0.3891 0.4303 -0.1137 0.0406  -0.0939 71  VAL A N   
625  C CA  . VAL A 70  ? 0.3843 0.3751 0.4142 -0.1104 0.0344  -0.0914 71  VAL A CA  
626  C C   . VAL A 70  ? 0.4197 0.3815 0.4338 -0.1117 0.0460  -0.0831 71  VAL A C   
627  O O   . VAL A 70  ? 0.4171 0.3661 0.4269 -0.1211 0.0588  -0.0859 71  VAL A O   
628  C CB  . VAL A 70  ? 0.4532 0.4594 0.4872 -0.1189 0.0296  -0.1056 71  VAL A CB  
629  C CG1 . VAL A 70  ? 0.4622 0.4578 0.4814 -0.1168 0.0239  -0.1031 71  VAL A CG1 
630  C CG2 . VAL A 70  ? 0.4465 0.4843 0.4993 -0.1157 0.0167  -0.1155 71  VAL A CG2 
631  N N   . ILE A 71  ? 0.3488 0.2998 0.3541 -0.1026 0.0419  -0.0740 72  ILE A N   
632  C CA  . ILE A 71  ? 0.3508 0.2778 0.3442 -0.1015 0.0511  -0.0677 72  ILE A CA  
633  C C   . ILE A 71  ? 0.3991 0.3229 0.3834 -0.1022 0.0472  -0.0702 72  ILE A C   
634  O O   . ILE A 71  ? 0.3859 0.3170 0.3683 -0.0962 0.0367  -0.0674 72  ILE A O   
635  C CB  . ILE A 71  ? 0.3741 0.2918 0.3666 -0.0907 0.0525  -0.0557 72  ILE A CB  
636  C CG1 . ILE A 71  ? 0.3874 0.3058 0.3847 -0.0909 0.0567  -0.0529 72  ILE A CG1 
637  C CG2 . ILE A 71  ? 0.4031 0.2995 0.3865 -0.0875 0.0604  -0.0511 72  ILE A CG2 
638  C CD1 . ILE A 71  ? 0.4468 0.3478 0.4372 -0.1006 0.0701  -0.0557 72  ILE A CD1 
639  N N   . ASN A 72  ? 0.3764 0.2865 0.3527 -0.1100 0.0564  -0.0753 73  ASN A N   
640  C CA  . ASN A 72  ? 0.3788 0.2842 0.3442 -0.1125 0.0547  -0.0786 73  ASN A CA  
641  C C   . ASN A 72  ? 0.4247 0.3115 0.3836 -0.1069 0.0628  -0.0723 73  ASN A C   
642  O O   . ASN A 72  ? 0.4148 0.2853 0.3730 -0.1075 0.0742  -0.0719 73  ASN A O   
643  C CB  . ASN A 72  ? 0.4286 0.3326 0.3897 -0.1258 0.0600  -0.0909 73  ASN A CB  
644  C CG  . ASN A 72  ? 0.6574 0.5838 0.6282 -0.1323 0.0525  -0.1001 73  ASN A CG  
645  O OD1 . ASN A 72  ? 0.5311 0.4754 0.5047 -0.1283 0.0383  -0.1015 73  ASN A OD1 
646  N ND2 . ASN A 72  ? 0.6119 0.5372 0.5877 -0.1425 0.0621  -0.1076 73  ASN A ND2 
647  N N   . LEU A 73  ? 0.3652 0.2533 0.3185 -0.1017 0.0574  -0.0684 74  LEU A N   
648  C CA  . LEU A 73  ? 0.3657 0.2406 0.3155 -0.0972 0.0654  -0.0652 74  LEU A CA  
649  C C   . LEU A 73  ? 0.4236 0.2870 0.3627 -0.1054 0.0737  -0.0735 74  LEU A C   
650  O O   . LEU A 73  ? 0.4307 0.2977 0.3619 -0.1147 0.0705  -0.0808 74  LEU A O   
651  C CB  . LEU A 73  ? 0.3597 0.2405 0.3079 -0.0906 0.0588  -0.0590 74  LEU A CB  
652  C CG  . LEU A 73  ? 0.3902 0.2817 0.3483 -0.0824 0.0511  -0.0512 74  LEU A CG  
653  C CD1 . LEU A 73  ? 0.3800 0.2724 0.3356 -0.0772 0.0489  -0.0462 74  LEU A CD1 
654  C CD2 . LEU A 73  ? 0.3885 0.2771 0.3575 -0.0775 0.0565  -0.0475 74  LEU A CD2 
655  N N   . ASP A 74  ? 0.3838 0.2345 0.3235 -0.1016 0.0840  -0.0733 75  ASP A N   
656  C CA  . ASP A 74  ? 0.4175 0.2559 0.3484 -0.1083 0.0940  -0.0819 75  ASP A CA  
657  C C   . ASP A 74  ? 0.4830 0.3273 0.3988 -0.1164 0.0884  -0.0862 75  ASP A C   
658  O O   . ASP A 74  ? 0.4549 0.3066 0.3677 -0.1129 0.0809  -0.0808 75  ASP A O   
659  C CB  . ASP A 74  ? 0.4414 0.2709 0.3791 -0.0994 0.1034  -0.0808 75  ASP A CB  
660  C CG  . ASP A 74  ? 0.5982 0.4138 0.5300 -0.1047 0.1159  -0.0908 75  ASP A CG  
661  O OD1 . ASP A 74  ? 0.6181 0.4360 0.5385 -0.1127 0.1170  -0.0967 75  ASP A OD1 
662  O OD2 . ASP A 74  ? 0.6368 0.4375 0.5738 -0.1005 0.1248  -0.0927 75  ASP A OD2 
663  N N   . PRO A 75  ? 0.4954 0.3349 0.3995 -0.1278 0.0914  -0.0958 76  PRO A N   
664  C CA  . PRO A 75  ? 0.5077 0.3507 0.3929 -0.1355 0.0845  -0.0992 76  PRO A CA  
665  C C   . PRO A 75  ? 0.5533 0.3908 0.4285 -0.1350 0.0890  -0.0980 76  PRO A C   
666  O O   . PRO A 75  ? 0.5748 0.4133 0.4318 -0.1397 0.0813  -0.0972 76  PRO A O   
667  C CB  . PRO A 75  ? 0.5515 0.3890 0.4270 -0.1480 0.0896  -0.1110 76  PRO A CB  
668  C CG  . PRO A 75  ? 0.6071 0.4325 0.4948 -0.1468 0.1036  -0.1143 76  PRO A CG  
669  C CD  . PRO A 75  ? 0.5215 0.3505 0.4264 -0.1349 0.1010  -0.1041 76  PRO A CD  
670  N N   . GLU A 76  ? 0.5041 0.3357 0.3904 -0.1293 0.1010  -0.0982 77  GLU A N   
671  C CA  . GLU A 76  ? 0.5278 0.3574 0.4083 -0.1298 0.1073  -0.0992 77  GLU A CA  
672  C C   . GLU A 76  ? 0.5308 0.3692 0.4130 -0.1235 0.0980  -0.0893 77  GLU A C   
673  O O   . GLU A 76  ? 0.5295 0.3666 0.4025 -0.1268 0.1015  -0.0899 77  GLU A O   
674  C CB  . GLU A 76  ? 0.5607 0.3851 0.4570 -0.1240 0.1222  -0.1045 77  GLU A CB  
675  C CG  . GLU A 76  ? 0.8219 0.6340 0.7119 -0.1320 0.1345  -0.1165 77  GLU A CG  
676  C CD  . GLU A 76  ? 1.2538 1.0623 1.1244 -0.1440 0.1416  -0.1252 77  GLU A CD  
677  O OE1 . GLU A 76  ? 1.2685 1.0790 1.1450 -0.1420 0.1510  -0.1290 77  GLU A OE1 
678  O OE2 . GLU A 76  ? 1.2503 1.0548 1.0994 -0.1560 0.1377  -0.1290 77  GLU A OE2 
679  N N   . ILE A 77  ? 0.4517 0.2984 0.3456 -0.1155 0.0877  -0.0812 78  ILE A N   
680  C CA  . ILE A 77  ? 0.4323 0.2864 0.3284 -0.1095 0.0792  -0.0724 78  ILE A CA  
681  C C   . ILE A 77  ? 0.4988 0.3504 0.3719 -0.1156 0.0684  -0.0701 78  ILE A C   
682  O O   . ILE A 77  ? 0.4809 0.3337 0.3458 -0.1185 0.0588  -0.0709 78  ILE A O   
683  C CB  . ILE A 77  ? 0.4486 0.3118 0.3642 -0.0990 0.0729  -0.0652 78  ILE A CB  
684  C CG1 . ILE A 77  ? 0.4581 0.3193 0.3920 -0.0917 0.0830  -0.0663 78  ILE A CG1 
685  C CG2 . ILE A 77  ? 0.4050 0.2755 0.3221 -0.0935 0.0642  -0.0572 78  ILE A CG2 
686  C CD1 . ILE A 77  ? 0.5382 0.4004 0.4802 -0.0873 0.0926  -0.0687 78  ILE A CD1 
687  N N   . ASN A 78  ? 0.4949 0.3430 0.3582 -0.1170 0.0695  -0.0672 79  ASN A N   
688  C CA  . ASN A 78  ? 0.5120 0.3516 0.3490 -0.1221 0.0601  -0.0633 79  ASN A CA  
689  C C   . ASN A 78  ? 0.4980 0.3435 0.3404 -0.1131 0.0452  -0.0544 79  ASN A C   
690  O O   . ASN A 78  ? 0.4474 0.3003 0.3074 -0.1059 0.0467  -0.0501 79  ASN A O   
691  C CB  . ASN A 78  ? 0.5750 0.4060 0.3994 -0.1290 0.0708  -0.0649 79  ASN A CB  
692  C CG  . ASN A 78  ? 0.8008 0.6170 0.5936 -0.1349 0.0627  -0.0596 79  ASN A CG  
693  O OD1 . ASN A 78  ? 0.6477 0.4621 0.4397 -0.1318 0.0597  -0.0534 79  ASN A OD1 
694  N ND2 . ASN A 78  ? 0.7270 0.5304 0.4910 -0.1434 0.0586  -0.0620 79  ASN A ND2 
695  N N   . PRO A 79  ? 0.4858 0.3294 0.3142 -0.1126 0.0302  -0.0523 80  PRO A N   
696  C CA  . PRO A 79  ? 0.4715 0.3212 0.3067 -0.1030 0.0162  -0.0452 80  PRO A CA  
697  C C   . PRO A 79  ? 0.5189 0.3596 0.3457 -0.1010 0.0159  -0.0383 80  PRO A C   
698  O O   . PRO A 79  ? 0.4925 0.3417 0.3362 -0.0926 0.0120  -0.0338 80  PRO A O   
699  C CB  . PRO A 79  ? 0.5177 0.3650 0.3351 -0.1035 0.0005  -0.0463 80  PRO A CB  
700  C CG  . PRO A 79  ? 0.5827 0.4300 0.3946 -0.1127 0.0069  -0.0551 80  PRO A CG  
701  C CD  . PRO A 79  ? 0.5323 0.3696 0.3391 -0.1201 0.0246  -0.0573 80  PRO A CD  
702  N N   . GLU A 80  ? 0.5017 0.3246 0.3016 -0.1099 0.0210  -0.0380 81  GLU A N   
703  C CA  . GLU A 80  ? 0.5027 0.3149 0.2926 -0.1104 0.0224  -0.0324 81  GLU A CA  
704  C C   . GLU A 80  ? 0.5048 0.3311 0.3229 -0.1078 0.0347  -0.0338 81  GLU A C   
705  O O   . GLU A 80  ? 0.4785 0.3080 0.3054 -0.1020 0.0310  -0.0290 81  GLU A O   
706  C CB  . GLU A 80  ? 0.5603 0.3484 0.3126 -0.1231 0.0276  -0.0327 81  GLU A CB  
707  C CG  . GLU A 80  ? 0.7150 0.4880 0.4526 -0.1249 0.0280  -0.0266 81  GLU A CG  
708  C CD  . GLU A 80  ? 1.0909 0.8388 0.7918 -0.1401 0.0379  -0.0275 81  GLU A CD  
709  O OE1 . GLU A 80  ? 1.0749 0.8004 0.7498 -0.1420 0.0326  -0.0206 81  GLU A OE1 
710  O OE2 . GLU A 80  ? 1.0329 0.7821 0.7303 -0.1507 0.0519  -0.0354 81  GLU A OE2 
711  N N   . GLY A 81  ? 0.4694 0.3043 0.3016 -0.1112 0.0482  -0.0409 82  GLY A N   
712  C CA  . GLY A 81  ? 0.4433 0.2933 0.3034 -0.1066 0.0581  -0.0432 82  GLY A CA  
713  C C   . GLY A 81  ? 0.4507 0.3147 0.3346 -0.0944 0.0495  -0.0383 82  GLY A C   
714  O O   . GLY A 81  ? 0.4217 0.2941 0.3197 -0.0894 0.0500  -0.0357 82  GLY A O   
715  N N   . PHE A 82  ? 0.3852 0.2523 0.2728 -0.0907 0.0418  -0.0379 83  PHE A N   
716  C CA  . PHE A 82  ? 0.3539 0.2335 0.2618 -0.0810 0.0349  -0.0342 83  PHE A CA  
717  C C   . PHE A 82  ? 0.4009 0.2796 0.3045 -0.0767 0.0244  -0.0281 83  PHE A C   
718  O O   . PHE A 82  ? 0.3692 0.2575 0.2891 -0.0704 0.0237  -0.0253 83  PHE A O   
719  C CB  . PHE A 82  ? 0.3705 0.2541 0.2823 -0.0802 0.0297  -0.0367 83  PHE A CB  
720  C CG  . PHE A 82  ? 0.3644 0.2606 0.2967 -0.0723 0.0258  -0.0340 83  PHE A CG  
721  C CD1 . PHE A 82  ? 0.3868 0.2880 0.3359 -0.0685 0.0341  -0.0339 83  PHE A CD1 
722  C CD2 . PHE A 82  ? 0.3682 0.2703 0.3020 -0.0682 0.0138  -0.0319 83  PHE A CD2 
723  C CE1 . PHE A 82  ? 0.3810 0.2912 0.3447 -0.0625 0.0311  -0.0310 83  PHE A CE1 
724  C CE2 . PHE A 82  ? 0.3788 0.2927 0.3307 -0.0624 0.0119  -0.0305 83  PHE A CE2 
725  C CZ  . PHE A 82  ? 0.3667 0.2838 0.3318 -0.0605 0.0209  -0.0297 83  PHE A CZ  
726  N N   . CYS A 83  ? 0.4155 0.2817 0.2965 -0.0795 0.0155  -0.0263 84  CYS A N   
727  C CA  . CYS A 83  ? 0.4384 0.2990 0.3122 -0.0745 0.0046  -0.0207 84  CYS A CA  
728  C C   . CYS A 83  ? 0.4498 0.3080 0.3258 -0.0757 0.0118  -0.0183 84  CYS A C   
729  O O   . CYS A 83  ? 0.4135 0.2782 0.3014 -0.0692 0.0073  -0.0154 84  CYS A O   
730  C CB  . CYS A 83  ? 0.5018 0.3437 0.3451 -0.0774 -0.0055 -0.0189 84  CYS A CB  
731  S SG  . CYS A 83  ? 0.5849 0.4155 0.4174 -0.0688 -0.0208 -0.0122 84  CYS A SG  
732  N N   . ILE A 84  ? 0.4097 0.2609 0.2761 -0.0849 0.0237  -0.0212 85  ILE A N   
733  C CA  . ILE A 84  ? 0.3927 0.2443 0.2622 -0.0885 0.0324  -0.0216 85  ILE A CA  
734  C C   . ILE A 84  ? 0.3818 0.2561 0.2836 -0.0806 0.0353  -0.0227 85  ILE A C   
735  O O   . ILE A 84  ? 0.3726 0.2515 0.2816 -0.0784 0.0345  -0.0209 85  ILE A O   
736  C CB  . ILE A 84  ? 0.4450 0.2883 0.3005 -0.1011 0.0462  -0.0273 85  ILE A CB  
737  C CG1 . ILE A 84  ? 0.4881 0.3031 0.3040 -0.1104 0.0430  -0.0244 85  ILE A CG1 
738  C CG2 . ILE A 84  ? 0.4281 0.2828 0.2988 -0.1047 0.0581  -0.0320 85  ILE A CG2 
739  C CD1 . ILE A 84  ? 0.6012 0.4076 0.4002 -0.1233 0.0555  -0.0310 85  ILE A CD1 
740  N N   . LEU A 85  ? 0.3417 0.2280 0.2602 -0.0768 0.0386  -0.0256 86  LEU A N   
741  C CA  . LEU A 85  ? 0.3203 0.2245 0.2650 -0.0687 0.0403  -0.0257 86  LEU A CA  
742  C C   . LEU A 85  ? 0.3577 0.2675 0.3104 -0.0609 0.0301  -0.0208 86  LEU A C   
743  O O   . LEU A 85  ? 0.3265 0.2472 0.2933 -0.0560 0.0299  -0.0194 86  LEU A O   
744  C CB  . LEU A 85  ? 0.3278 0.2373 0.2839 -0.0667 0.0472  -0.0298 86  LEU A CB  
745  C CG  . LEU A 85  ? 0.4005 0.3103 0.3568 -0.0726 0.0594  -0.0370 86  LEU A CG  
746  C CD1 . LEU A 85  ? 0.4136 0.3253 0.3797 -0.0694 0.0652  -0.0412 86  LEU A CD1 
747  C CD2 . LEU A 85  ? 0.4052 0.3287 0.3764 -0.0707 0.0638  -0.0395 86  LEU A CD2 
748  N N   . LEU A 86  ? 0.3286 0.2328 0.2731 -0.0599 0.0215  -0.0191 87  LEU A N   
749  C CA  . LEU A 86  ? 0.3181 0.2294 0.2715 -0.0531 0.0124  -0.0164 87  LEU A CA  
750  C C   . LEU A 86  ? 0.3534 0.2609 0.3021 -0.0518 0.0082  -0.0136 87  LEU A C   
751  O O   . LEU A 86  ? 0.3232 0.2405 0.2850 -0.0468 0.0062  -0.0124 87  LEU A O   
752  C CB  . LEU A 86  ? 0.3187 0.2275 0.2656 -0.0527 0.0039  -0.0177 87  LEU A CB  
753  C CG  . LEU A 86  ? 0.3700 0.2898 0.3296 -0.0462 -0.0044 -0.0178 87  LEU A CG  
754  C CD1 . LEU A 86  ? 0.3418 0.2746 0.3203 -0.0441 0.0018  -0.0184 87  LEU A CD1 
755  C CD2 . LEU A 86  ? 0.4042 0.3245 0.3587 -0.0459 -0.0138 -0.0213 87  LEU A CD2 
756  N N   . ASP A 87  ? 0.3564 0.2472 0.2841 -0.0571 0.0075  -0.0126 88  ASP A N   
757  C CA  . ASP A 87  ? 0.3553 0.2371 0.2746 -0.0577 0.0053  -0.0102 88  ASP A CA  
758  C C   . ASP A 87  ? 0.3784 0.2726 0.3128 -0.0591 0.0140  -0.0121 88  ASP A C   
759  O O   . ASP A 87  ? 0.3756 0.2741 0.3170 -0.0557 0.0111  -0.0110 88  ASP A O   
760  C CB  . ASP A 87  ? 0.4140 0.2713 0.3035 -0.0656 0.0058  -0.0089 88  ASP A CB  
761  C CG  . ASP A 87  ? 0.5970 0.4393 0.4678 -0.0619 -0.0071 -0.0060 88  ASP A CG  
762  O OD1 . ASP A 87  ? 0.6032 0.4562 0.4874 -0.0525 -0.0170 -0.0060 88  ASP A OD1 
763  O OD2 . ASP A 87  ? 0.6306 0.4508 0.4729 -0.0684 -0.0076 -0.0044 88  ASP A OD2 
764  N N   . PHE A 88  ? 0.3310 0.2322 0.2714 -0.0637 0.0242  -0.0158 89  PHE A N   
765  C CA  . PHE A 88  ? 0.3039 0.2212 0.2618 -0.0637 0.0312  -0.0191 89  PHE A CA  
766  C C   . PHE A 88  ? 0.3003 0.2343 0.2784 -0.0540 0.0264  -0.0172 89  PHE A C   
767  O O   . PHE A 88  ? 0.2796 0.2231 0.2667 -0.0525 0.0262  -0.0178 89  PHE A O   
768  C CB  . PHE A 88  ? 0.3145 0.2386 0.2785 -0.0677 0.0417  -0.0249 89  PHE A CB  
769  C CG  . PHE A 88  ? 0.3050 0.2501 0.2915 -0.0641 0.0463  -0.0291 89  PHE A CG  
770  C CD1 . PHE A 88  ? 0.3168 0.2679 0.3056 -0.0698 0.0506  -0.0332 89  PHE A CD1 
771  C CD2 . PHE A 88  ? 0.3097 0.2679 0.3140 -0.0545 0.0451  -0.0288 89  PHE A CD2 
772  C CE1 . PHE A 88  ? 0.3043 0.2782 0.3153 -0.0655 0.0527  -0.0380 89  PHE A CE1 
773  C CE2 . PHE A 88  ? 0.3331 0.3105 0.3568 -0.0490 0.0464  -0.0320 89  PHE A CE2 
774  C CZ  . PHE A 88  ? 0.3066 0.2938 0.3349 -0.0542 0.0497  -0.0371 89  PHE A CZ  
775  N N   . MET A 89  ? 0.2549 0.1919 0.2388 -0.0487 0.0234  -0.0156 90  MET A N   
776  C CA  . MET A 89  ? 0.2366 0.1858 0.2350 -0.0413 0.0200  -0.0136 90  MET A CA  
777  C C   . MET A 89  ? 0.2979 0.2485 0.2966 -0.0393 0.0137  -0.0119 90  MET A C   
778  O O   . MET A 89  ? 0.2788 0.2408 0.2880 -0.0359 0.0134  -0.0116 90  MET A O   
779  C CB  . MET A 89  ? 0.2517 0.1990 0.2510 -0.0389 0.0182  -0.0127 90  MET A CB  
780  C CG  . MET A 89  ? 0.2854 0.2310 0.2865 -0.0397 0.0251  -0.0147 90  MET A CG  
781  S SD  . MET A 89  ? 0.3352 0.2778 0.3371 -0.0386 0.0237  -0.0143 90  MET A SD  
782  C CE  . MET A 89  ? 0.3390 0.2730 0.3370 -0.0418 0.0325  -0.0181 90  MET A CE  
783  N N   . TYR A 90  ? 0.2762 0.2149 0.2628 -0.0406 0.0081  -0.0111 91  TYR A N   
784  C CA  . TYR A 90  ? 0.2707 0.2086 0.2576 -0.0373 0.0016  -0.0104 91  TYR A CA  
785  C C   . TYR A 90  ? 0.3221 0.2520 0.3010 -0.0411 0.0028  -0.0107 91  TYR A C   
786  O O   . TYR A 90  ? 0.3157 0.2436 0.2951 -0.0382 -0.0018 -0.0108 91  TYR A O   
787  C CB  . TYR A 90  ? 0.2915 0.2212 0.2712 -0.0344 -0.0068 -0.0102 91  TYR A CB  
788  C CG  . TYR A 90  ? 0.2955 0.2378 0.2879 -0.0307 -0.0089 -0.0119 91  TYR A CG  
789  C CD1 . TYR A 90  ? 0.3138 0.2574 0.3065 -0.0331 -0.0057 -0.0127 91  TYR A CD1 
790  C CD2 . TYR A 90  ? 0.2947 0.2474 0.2986 -0.0262 -0.0125 -0.0139 91  TYR A CD2 
791  C CE1 . TYR A 90  ? 0.3135 0.2667 0.3161 -0.0318 -0.0062 -0.0152 91  TYR A CE1 
792  C CE2 . TYR A 90  ? 0.2867 0.2505 0.3011 -0.0251 -0.0130 -0.0169 91  TYR A CE2 
793  C CZ  . TYR A 90  ? 0.3313 0.2950 0.3447 -0.0284 -0.0094 -0.0173 91  TYR A CZ  
794  O OH  . TYR A 90  ? 0.3032 0.2765 0.3256 -0.0293 -0.0086 -0.0213 91  TYR A OH  
795  N N   . THR A 91  ? 0.2805 0.2050 0.2519 -0.0483 0.0100  -0.0121 92  THR A N   
796  C CA  . THR A 91  ? 0.2958 0.2096 0.2566 -0.0545 0.0126  -0.0133 92  THR A CA  
797  C C   . THR A 91  ? 0.3272 0.2529 0.2961 -0.0613 0.0222  -0.0182 92  THR A C   
798  O O   . THR A 91  ? 0.3394 0.2594 0.3023 -0.0674 0.0253  -0.0206 92  THR A O   
799  C CB  . THR A 91  ? 0.3978 0.2841 0.3316 -0.0602 0.0116  -0.0112 92  THR A CB  
800  O OG1 . THR A 91  ? 0.3880 0.2726 0.3157 -0.0669 0.0189  -0.0129 92  THR A OG1 
801  C CG2 . THR A 91  ? 0.4033 0.2770 0.3275 -0.0526 -0.0002 -0.0074 92  THR A CG2 
802  N N   . SER A 92  ? 0.2752 0.2154 0.2560 -0.0607 0.0272  -0.0206 93  SER A N   
803  C CA  . SER A 92  ? 0.2635 0.2184 0.2549 -0.0661 0.0362  -0.0273 93  SER A CA  
804  C C   . SER A 92  ? 0.3230 0.2630 0.2974 -0.0786 0.0451  -0.0311 93  SER A C   
805  O O   . SER A 92  ? 0.3207 0.2734 0.3040 -0.0847 0.0540  -0.0388 93  SER A O   
806  C CB  . SER A 92  ? 0.2872 0.2559 0.2892 -0.0672 0.0364  -0.0310 93  SER A CB  
807  O OG  . SER A 92  ? 0.3436 0.3225 0.3561 -0.0578 0.0287  -0.0275 93  SER A OG  
808  N N   A ARG A 93  ? 0.3162 0.2303 0.2661 -0.0820 0.0424  -0.0265 94  ARG A N   
809  N N   B ARG A 93  ? 0.3085 0.2221 0.2579 -0.0823 0.0425  -0.0266 94  ARG A N   
810  C CA  A ARG A 93  ? 0.3436 0.2372 0.2698 -0.0948 0.0503  -0.0286 94  ARG A CA  
811  C CA  B ARG A 93  ? 0.3312 0.2259 0.2582 -0.0954 0.0511  -0.0292 94  ARG A CA  
812  C C   A ARG A 93  ? 0.4007 0.2900 0.3205 -0.0955 0.0525  -0.0286 94  ARG A C   
813  C C   B ARG A 93  ? 0.3956 0.2841 0.3145 -0.0959 0.0526  -0.0286 94  ARG A C   
814  O O   A ARG A 93  ? 0.3790 0.2629 0.2952 -0.0878 0.0437  -0.0233 94  ARG A O   
815  O O   B ARG A 93  ? 0.3799 0.2616 0.2939 -0.0884 0.0435  -0.0230 94  ARG A O   
816  C CB  A ARG A 93  ? 0.4021 0.2647 0.2997 -0.0979 0.0447  -0.0228 94  ARG A CB  
817  C CB  B ARG A 93  ? 0.3687 0.2330 0.2672 -0.1010 0.0480  -0.0248 94  ARG A CB  
818  C CG  A ARG A 93  ? 0.4719 0.3347 0.3734 -0.0980 0.0433  -0.0234 94  ARG A CG  
819  C CG  B ARG A 93  ? 0.3776 0.2453 0.2807 -0.1063 0.0519  -0.0286 94  ARG A CG  
820  C CD  A ARG A 93  ? 0.6037 0.4341 0.4785 -0.0966 0.0352  -0.0169 94  ARG A CD  
821  C CD  B ARG A 93  ? 0.5343 0.3733 0.4150 -0.1057 0.0451  -0.0228 94  ARG A CD  
822  N NE  A ARG A 93  ? 0.7006 0.4989 0.5410 -0.1084 0.0405  -0.0154 94  ARG A NE  
823  N NE  B ARG A 93  ? 0.6111 0.4554 0.4991 -0.1100 0.0487  -0.0273 94  ARG A NE  
824  C CZ  A ARG A 93  ? 0.8526 0.6339 0.6756 -0.1226 0.0507  -0.0187 94  ARG A CZ  
825  C CZ  B ARG A 93  ? 0.7852 0.6017 0.6497 -0.1188 0.0518  -0.0270 94  ARG A CZ  
826  N NH1 A ARG A 93  ? 0.7077 0.4566 0.4953 -0.1341 0.0558  -0.0167 94  ARG A NH1 
827  N NH1 B ARG A 93  ? 0.6487 0.4725 0.5222 -0.1232 0.0556  -0.0323 94  ARG A NH1 
828  N NH2 A ARG A 93  ? 0.6525 0.4482 0.4917 -0.1264 0.0562  -0.0246 94  ARG A NH2 
829  N NH2 B ARG A 93  ? 0.6397 0.4189 0.4694 -0.1237 0.0510  -0.0215 94  ARG A NH2 
830  N N   . LEU A 94  ? 0.3663 0.2594 0.2854 -0.1054 0.0648  -0.0361 95  LEU A N   
831  C CA  . LEU A 94  ? 0.3719 0.2611 0.2847 -0.1077 0.0691  -0.0380 95  LEU A CA  
832  C C   . LEU A 94  ? 0.4586 0.3213 0.3381 -0.1229 0.0765  -0.0392 95  LEU A C   
833  O O   . LEU A 94  ? 0.4575 0.3196 0.3325 -0.1355 0.0884  -0.0462 95  LEU A O   
834  C CB  . LEU A 94  ? 0.3552 0.2720 0.2970 -0.1049 0.0774  -0.0469 95  LEU A CB  
835  C CG  . LEU A 94  ? 0.4072 0.3227 0.3476 -0.1058 0.0829  -0.0505 95  LEU A CG  
836  C CD1 . LEU A 94  ? 0.3840 0.2967 0.3268 -0.0942 0.0722  -0.0433 95  LEU A CD1 
837  C CD2 . LEU A 94  ? 0.4123 0.3527 0.3795 -0.1046 0.0931  -0.0616 95  LEU A CD2 
838  N N   . ASN A 95  ? 0.4529 0.2936 0.3077 -0.1225 0.0696  -0.0330 96  ASN A N   
839  C CA  . ASN A 95  ? 0.4997 0.3104 0.3161 -0.1363 0.0747  -0.0325 96  ASN A CA  
840  C C   . ASN A 95  ? 0.5504 0.3676 0.3674 -0.1451 0.0878  -0.0412 96  ASN A C   
841  O O   . ASN A 95  ? 0.5516 0.3609 0.3569 -0.1440 0.0843  -0.0397 96  ASN A O   
842  C CB  . ASN A 95  ? 0.5528 0.3376 0.3415 -0.1304 0.0591  -0.0223 96  ASN A CB  
843  C CG  . ASN A 95  ? 0.8119 0.5607 0.5547 -0.1437 0.0619  -0.0198 96  ASN A CG  
844  O OD1 . ASN A 95  ? 0.7346 0.4708 0.4608 -0.1588 0.0753  -0.0239 96  ASN A OD1 
845  N ND2 . ASN A 95  ? 0.7482 0.4792 0.4681 -0.1391 0.0495  -0.0135 96  ASN A ND2 
846  N N   . LEU A 96  ? 0.4963 0.3311 0.3304 -0.1531 0.1026  -0.0519 97  LEU A N   
847  C CA  . LEU A 96  ? 0.5079 0.3538 0.3493 -0.1604 0.1166  -0.0629 97  LEU A CA  
848  C C   . LEU A 96  ? 0.5874 0.4084 0.3926 -0.1810 0.1294  -0.0671 97  LEU A C   
849  O O   . LEU A 96  ? 0.5855 0.3985 0.3799 -0.1926 0.1369  -0.0696 97  LEU A O   
850  C CB  . LEU A 96  ? 0.4945 0.3763 0.3774 -0.1561 0.1245  -0.0737 97  LEU A CB  
851  C CG  . LEU A 96  ? 0.5614 0.4641 0.4672 -0.1545 0.1347  -0.0852 97  LEU A CG  
852  C CD1 . LEU A 96  ? 0.5534 0.4533 0.4623 -0.1419 0.1255  -0.0794 97  LEU A CD1 
853  C CD2 . LEU A 96  ? 0.5413 0.4793 0.4879 -0.1472 0.1386  -0.0948 97  LEU A CD2 
854  N N   . ARG A 97  ? 0.5613 0.3674 0.3443 -0.1867 0.1320  -0.0678 98  ARG A N   
855  C CA  . ARG A 97  ? 0.6096 0.3878 0.3515 -0.2074 0.1442  -0.0712 98  ARG A CA  
856  C C   . ARG A 97  ? 0.6375 0.4251 0.3834 -0.2148 0.1577  -0.0829 98  ARG A C   
857  O O   . ARG A 97  ? 0.5890 0.3939 0.3586 -0.2022 0.1528  -0.0843 98  ARG A O   
858  C CB  . ARG A 97  ? 0.6672 0.4058 0.3625 -0.2080 0.1301  -0.0571 98  ARG A CB  
859  C CG  . ARG A 97  ? 0.7786 0.5032 0.4666 -0.2001 0.1163  -0.0457 98  ARG A CG  
860  C CD  . ARG A 97  ? 1.0127 0.7018 0.6602 -0.1956 0.0990  -0.0323 98  ARG A CD  
861  N NE  . ARG A 97  ? 1.2935 0.9447 0.8888 -0.2137 0.1063  -0.0313 98  ARG A NE  
862  C CZ  . ARG A 97  ? 1.5559 1.1753 1.1166 -0.2272 0.1127  -0.0284 98  ARG A CZ  
863  N NH1 . ARG A 97  ? 1.4398 1.0224 0.9495 -0.2444 0.1198  -0.0272 98  ARG A NH1 
864  N NH2 . ARG A 97  ? 1.4029 1.0250 0.9772 -0.2247 0.1128  -0.0271 98  ARG A NH2 
865  N N   . GLU A 98  ? 0.6371 0.4111 0.3578 -0.2361 0.1757  -0.0920 99  GLU A N   
866  C CA  . GLU A 98  ? 0.6445 0.4257 0.3660 -0.2454 0.1908  -0.1051 99  GLU A CA  
867  C C   . GLU A 98  ? 0.6977 0.4679 0.4059 -0.2371 0.1790  -0.0985 99  GLU A C   
868  O O   . GLU A 98  ? 0.6847 0.4743 0.4171 -0.2320 0.1843  -0.1074 99  GLU A O   
869  C CB  . GLU A 98  ? 0.7128 0.4705 0.3951 -0.2723 0.2102  -0.1130 99  GLU A CB  
870  C CG  . GLU A 98  ? 0.8745 0.6415 0.5589 -0.2839 0.2286  -0.1291 99  GLU A CG  
871  C CD  . GLU A 98  ? 1.3239 1.0667 0.9666 -0.3126 0.2493  -0.1377 99  GLU A CD  
872  O OE1 . GLU A 98  ? 1.3256 1.0260 0.9140 -0.3233 0.2441  -0.1256 99  GLU A OE1 
873  O OE2 . GLU A 98  ? 1.3546 1.1204 1.0184 -0.3243 0.2710  -0.1572 99  GLU A OE2 
874  N N   . GLY A 99  ? 0.6840 0.4241 0.3556 -0.2350 0.1628  -0.0837 100 GLY A N   
875  C CA  . GLY A 99  ? 0.7006 0.4301 0.3566 -0.2284 0.1499  -0.0778 100 GLY A CA  
876  C C   . GLY A 99  ? 0.6973 0.4504 0.3909 -0.2070 0.1356  -0.0739 100 GLY A C   
877  O O   . GLY A 99  ? 0.6982 0.4493 0.3867 -0.2029 0.1285  -0.0731 100 GLY A O   
878  N N   . ASN A 100 ? 0.6135 0.3889 0.3440 -0.1942 0.1316  -0.0722 101 ASN A N   
879  C CA  . ASN A 100 ? 0.5748 0.3697 0.3373 -0.1752 0.1189  -0.0681 101 ASN A CA  
880  C C   . ASN A 100 ? 0.5813 0.4080 0.3903 -0.1662 0.1270  -0.0766 101 ASN A C   
881  O O   . ASN A 100 ? 0.5362 0.3761 0.3690 -0.1519 0.1187  -0.0739 101 ASN A O   
882  C CB  . ASN A 100 ? 0.5733 0.3615 0.3325 -0.1641 0.1002  -0.0548 101 ASN A CB  
883  C CG  . ASN A 100 ? 0.6422 0.4380 0.4157 -0.1625 0.1021  -0.0534 101 ASN A CG  
884  O OD1 . ASN A 100 ? 0.5148 0.3328 0.3168 -0.1627 0.1134  -0.0619 101 ASN A OD1 
885  N ND2 . ASN A 100 ? 0.5577 0.3366 0.3133 -0.1598 0.0902  -0.0433 101 ASN A ND2 
886  N N   . ILE A 101 ? 0.5414 0.3803 0.3630 -0.1741 0.1427  -0.0871 102 ILE A N   
887  C CA  . ILE A 101 ? 0.5111 0.3814 0.3772 -0.1638 0.1483  -0.0953 102 ILE A CA  
888  C C   . ILE A 101 ? 0.5302 0.4120 0.4181 -0.1536 0.1497  -0.1005 102 ILE A C   
889  O O   . ILE A 101 ? 0.4812 0.3805 0.3998 -0.1376 0.1434  -0.0987 102 ILE A O   
890  C CB  . ILE A 101 ? 0.5602 0.4446 0.4371 -0.1752 0.1654  -0.1086 102 ILE A CB  
891  C CG1 . ILE A 101 ? 0.5428 0.4624 0.4680 -0.1609 0.1668  -0.1163 102 ILE A CG1 
892  C CG2 . ILE A 101 ? 0.5653 0.4404 0.4224 -0.1934 0.1833  -0.1210 102 ILE A CG2 
893  C CD1 . ILE A 101 ? 0.5438 0.4818 0.4841 -0.1679 0.1754  -0.1252 102 ILE A CD1 
894  N N   . MET A 102 ? 0.5186 0.3886 0.3888 -0.1628 0.1579  -0.1069 103 MET A N   
895  C CA  . MET A 102 ? 0.5168 0.3940 0.4055 -0.1541 0.1602  -0.1125 103 MET A CA  
896  C C   . MET A 102 ? 0.5335 0.4062 0.4250 -0.1410 0.1438  -0.1008 103 MET A C   
897  O O   . MET A 102 ? 0.4959 0.3807 0.4149 -0.1275 0.1422  -0.1018 103 MET A O   
898  C CB  . MET A 102 ? 0.5837 0.4487 0.4514 -0.1684 0.1735  -0.1231 103 MET A CB  
899  C CG  . MET A 102 ? 0.6685 0.5413 0.5379 -0.1821 0.1931  -0.1381 103 MET A CG  
900  S SD  . MET A 102 ? 0.7161 0.6256 0.6385 -0.1698 0.2017  -0.1506 103 MET A SD  
901  C CE  . MET A 102 ? 0.6730 0.5889 0.6205 -0.1558 0.2050  -0.1589 103 MET A CE  
902  N N   . ALA A 103 ? 0.5035 0.3586 0.3666 -0.1448 0.1315  -0.0902 104 ALA A N   
903  C CA  . ALA A 103 ? 0.4981 0.3511 0.3639 -0.1342 0.1161  -0.0808 104 ALA A CA  
904  C C   . ALA A 103 ? 0.4916 0.3595 0.3835 -0.1203 0.1079  -0.0739 104 ALA A C   
905  O O   . ALA A 103 ? 0.4595 0.3344 0.3698 -0.1093 0.1029  -0.0713 104 ALA A O   
906  C CB  . ALA A 103 ? 0.5345 0.3688 0.3663 -0.1405 0.1042  -0.0728 104 ALA A CB  
907  N N   . VAL A 104 ? 0.4170 0.2884 0.3086 -0.1222 0.1077  -0.0714 105 VAL A N   
908  C CA  . VAL A 104 ? 0.3868 0.2728 0.3015 -0.1103 0.1003  -0.0657 105 VAL A CA  
909  C C   . VAL A 104 ? 0.4158 0.3211 0.3634 -0.0997 0.1061  -0.0717 105 VAL A C   
910  O O   . VAL A 104 ? 0.3921 0.3041 0.3555 -0.0874 0.0979  -0.0659 105 VAL A O   
911  C CB  . VAL A 104 ? 0.4356 0.3201 0.3419 -0.1160 0.0997  -0.0631 105 VAL A CB  
912  C CG1 . VAL A 104 ? 0.3970 0.2997 0.3294 -0.1046 0.0942  -0.0598 105 VAL A CG1 
913  C CG2 . VAL A 104 ? 0.4519 0.3139 0.3258 -0.1213 0.0896  -0.0543 105 VAL A CG2 
914  N N   A MET A 105 ? 0.3927 0.3063 0.3500 -0.1040 0.1198  -0.0835 106 MET A N   
915  N N   B MET A 105 ? 0.3949 0.3087 0.3524 -0.1040 0.1198  -0.0835 106 MET A N   
916  C CA  A MET A 105 ? 0.3906 0.3222 0.3797 -0.0917 0.1240  -0.0900 106 MET A CA  
917  C CA  B MET A 105 ? 0.3912 0.3230 0.3805 -0.0916 0.1240  -0.0900 106 MET A CA  
918  C C   A MET A 105 ? 0.4305 0.3542 0.4239 -0.0827 0.1212  -0.0880 106 MET A C   
919  C C   B MET A 105 ? 0.4381 0.3619 0.4316 -0.0827 0.1213  -0.0880 106 MET A C   
920  O O   A MET A 105 ? 0.3939 0.3247 0.4064 -0.0685 0.1158  -0.0845 106 MET A O   
921  O O   B MET A 105 ? 0.4110 0.3419 0.4235 -0.0685 0.1158  -0.0844 106 MET A O   
922  C CB  A MET A 105 ? 0.4347 0.3782 0.4350 -0.0979 0.1396  -0.1054 106 MET A CB  
923  C CB  B MET A 105 ? 0.4348 0.3786 0.4354 -0.0979 0.1397  -0.1054 106 MET A CB  
924  C CG  A MET A 105 ? 0.4718 0.4363 0.5076 -0.0823 0.1416  -0.1126 106 MET A CG  
925  C CG  B MET A 105 ? 0.4722 0.4375 0.5083 -0.0824 0.1414  -0.1126 106 MET A CG  
926  S SD  A MET A 105 ? 0.5383 0.5246 0.5937 -0.0890 0.1594  -0.1333 106 MET A SD  
927  S SD  B MET A 105 ? 0.5418 0.5262 0.5962 -0.0890 0.1601  -0.1337 106 MET A SD  
928  C CE  A MET A 105 ? 0.5238 0.4926 0.5647 -0.0974 0.1726  -0.1428 106 MET A CE  
929  C CE  B MET A 105 ? 0.4986 0.4933 0.5853 -0.0666 0.1587  -0.1392 106 MET A CE  
930  N N   . ALA A 106 ? 0.4228 0.3306 0.3965 -0.0916 0.1252  -0.0904 107 ALA A N   
931  C CA  . ALA A 106 ? 0.4192 0.3170 0.3941 -0.0861 0.1241  -0.0898 107 ALA A CA  
932  C C   . ALA A 106 ? 0.4219 0.3166 0.3968 -0.0783 0.1104  -0.0776 107 ALA A C   
933  O O   . ALA A 106 ? 0.3959 0.2894 0.3838 -0.0679 0.1089  -0.0756 107 ALA A O   
934  C CB  . ALA A 106 ? 0.4503 0.3328 0.4011 -0.0996 0.1298  -0.0950 107 ALA A CB  
935  N N   . THR A 107 ? 0.3677 0.2604 0.3281 -0.0831 0.1008  -0.0698 108 THR A N   
936  C CA  . THR A 107 ? 0.3609 0.2535 0.3226 -0.0768 0.0885  -0.0600 108 THR A CA  
937  C C   . THR A 107 ? 0.3900 0.2952 0.3735 -0.0643 0.0853  -0.0558 108 THR A C   
938  O O   . THR A 107 ? 0.3593 0.2629 0.3497 -0.0568 0.0810  -0.0512 108 THR A O   
939  C CB  . THR A 107 ? 0.4534 0.3407 0.3952 -0.0835 0.0788  -0.0542 108 THR A CB  
940  O OG1 . THR A 107 ? 0.4475 0.3228 0.3667 -0.0948 0.0817  -0.0586 108 THR A OG1 
941  C CG2 . THR A 107 ? 0.4267 0.3151 0.3708 -0.0781 0.0673  -0.0473 108 THR A CG2 
942  N N   . ALA A 108 ? 0.3445 0.2617 0.3373 -0.0631 0.0878  -0.0580 109 ALA A N   
943  C CA  . ALA A 108 ? 0.3190 0.2503 0.3317 -0.0516 0.0837  -0.0550 109 ALA A CA  
944  C C   . ALA A 108 ? 0.3487 0.2812 0.3778 -0.0400 0.0873  -0.0581 109 ALA A C   
945  O O   . ALA A 108 ? 0.3311 0.2658 0.3690 -0.0292 0.0810  -0.0521 109 ALA A O   
946  C CB  . ALA A 108 ? 0.3183 0.2638 0.3377 -0.0549 0.0868  -0.0595 109 ALA A CB  
947  N N   . MET A 109 ? 0.3360 0.2643 0.3667 -0.0422 0.0974  -0.0673 110 MET A N   
948  C CA  . MET A 109 ? 0.3394 0.2646 0.3841 -0.0299 0.1008  -0.0706 110 MET A CA  
949  C C   . MET A 109 ? 0.3772 0.2838 0.4122 -0.0270 0.0965  -0.0628 110 MET A C   
950  O O   . MET A 109 ? 0.3803 0.2830 0.4225 -0.0148 0.0924  -0.0578 110 MET A O   
951  C CB  . MET A 109 ? 0.3864 0.3102 0.4347 -0.0338 0.1136  -0.0836 110 MET A CB  
952  C CG  . MET A 109 ? 0.4479 0.3934 0.5134 -0.0334 0.1195  -0.0938 110 MET A CG  
953  S SD  . MET A 109 ? 0.5459 0.4906 0.6119 -0.0430 0.1368  -0.1110 110 MET A SD  
954  C CE  . MET A 109 ? 0.5190 0.4548 0.6015 -0.0251 0.1389  -0.1150 110 MET A CE  
955  N N   . TYR A 110 ? 0.3694 0.2648 0.3865 -0.0388 0.0969  -0.0618 111 TYR A N   
956  C CA  . TYR A 110 ? 0.3743 0.2545 0.3818 -0.0399 0.0942  -0.0568 111 TYR A CA  
957  C C   . TYR A 110 ? 0.3845 0.2688 0.3937 -0.0345 0.0840  -0.0464 111 TYR A C   
958  O O   . TYR A 110 ? 0.3757 0.2494 0.3848 -0.0288 0.0831  -0.0420 111 TYR A O   
959  C CB  . TYR A 110 ? 0.3893 0.2632 0.3791 -0.0543 0.0951  -0.0598 111 TYR A CB  
960  C CG  . TYR A 110 ? 0.3899 0.2543 0.3710 -0.0584 0.0912  -0.0563 111 TYR A CG  
961  C CD1 . TYR A 110 ? 0.4321 0.2808 0.4112 -0.0587 0.0979  -0.0596 111 TYR A CD1 
962  C CD2 . TYR A 110 ? 0.3830 0.2541 0.3578 -0.0629 0.0816  -0.0513 111 TYR A CD2 
963  C CE1 . TYR A 110 ? 0.4046 0.2460 0.3762 -0.0648 0.0958  -0.0583 111 TYR A CE1 
964  C CE2 . TYR A 110 ? 0.3835 0.2500 0.3531 -0.0678 0.0787  -0.0508 111 TYR A CE2 
965  C CZ  . TYR A 110 ? 0.4143 0.2667 0.3822 -0.0698 0.0864  -0.0547 111 TYR A CZ  
966  O OH  . TYR A 110 ? 0.4080 0.2575 0.3713 -0.0769 0.0849  -0.0560 111 TYR A OH  
967  N N   . LEU A 111 ? 0.3295 0.2270 0.3385 -0.0370 0.0773  -0.0429 112 LEU A N   
968  C CA  . LEU A 111 ? 0.3140 0.2169 0.3245 -0.0331 0.0684  -0.0346 112 LEU A CA  
969  C C   . LEU A 111 ? 0.3540 0.2639 0.3775 -0.0205 0.0660  -0.0312 112 LEU A C   
970  O O   . LEU A 111 ? 0.3372 0.2494 0.3610 -0.0167 0.0596  -0.0245 112 LEU A O   
971  C CB  . LEU A 111 ? 0.2952 0.2075 0.3001 -0.0397 0.0623  -0.0329 112 LEU A CB  
972  C CG  . LEU A 111 ? 0.3417 0.2474 0.3317 -0.0501 0.0602  -0.0344 112 LEU A CG  
973  C CD1 . LEU A 111 ? 0.3432 0.2549 0.3268 -0.0534 0.0525  -0.0316 112 LEU A CD1 
974  C CD2 . LEU A 111 ? 0.3584 0.2579 0.3460 -0.0513 0.0581  -0.0329 112 LEU A CD2 
975  N N   . GLN A 112 ? 0.3287 0.2439 0.3636 -0.0141 0.0707  -0.0369 113 GLN A N   
976  C CA  . GLN A 112 ? 0.3358 0.2608 0.3849 -0.0005 0.0669  -0.0355 113 GLN A CA  
977  C C   . GLN A 112 ? 0.3469 0.2903 0.4009 -0.0012 0.0599  -0.0326 113 GLN A C   
978  O O   . GLN A 112 ? 0.3258 0.2709 0.3790 0.0040  0.0526  -0.0254 113 GLN A O   
979  C CB  . GLN A 112 ? 0.3644 0.2731 0.4093 0.0094  0.0639  -0.0285 113 GLN A CB  
980  C CG  . GLN A 112 ? 0.3999 0.2870 0.4393 0.0103  0.0718  -0.0319 113 GLN A CG  
981  C CD  . GLN A 112 ? 0.5365 0.4016 0.5639 0.0148  0.0699  -0.0236 113 GLN A CD  
982  O OE1 . GLN A 112 ? 0.4670 0.3326 0.4936 0.0232  0.0628  -0.0162 113 GLN A OE1 
983  N NE2 . GLN A 112 ? 0.5079 0.3522 0.5236 0.0079  0.0768  -0.0251 113 GLN A NE2 
984  N N   . MET A 113 ? 0.3033 0.2582 0.3595 -0.0096 0.0631  -0.0386 114 MET A N   
985  C CA  . MET A 113 ? 0.2911 0.2615 0.3505 -0.0129 0.0588  -0.0380 114 MET A CA  
986  C C   . MET A 113 ? 0.3541 0.3426 0.4304 -0.0108 0.0639  -0.0481 114 MET A C   
987  O O   . MET A 113 ? 0.3281 0.3192 0.4023 -0.0210 0.0718  -0.0557 114 MET A O   
988  C CB  . MET A 113 ? 0.3116 0.2746 0.3548 -0.0262 0.0592  -0.0368 114 MET A CB  
989  C CG  . MET A 113 ? 0.3374 0.2880 0.3686 -0.0273 0.0533  -0.0290 114 MET A CG  
990  S SD  . MET A 113 ? 0.3782 0.3195 0.3907 -0.0397 0.0513  -0.0284 114 MET A SD  
991  C CE  . MET A 113 ? 0.3340 0.2859 0.3482 -0.0409 0.0461  -0.0263 114 MET A CE  
992  N N   . GLU A 114 ? 0.3487 0.3486 0.4413 0.0030  0.0599  -0.0490 115 GLU A N   
993  C CA  . GLU A 114 ? 0.3694 0.3899 0.4835 0.0086  0.0638  -0.0605 115 GLU A CA  
994  C C   . GLU A 114 ? 0.3737 0.4143 0.4949 -0.0022 0.0678  -0.0689 115 GLU A C   
995  O O   . GLU A 114 ? 0.3609 0.4132 0.4937 -0.0061 0.0771  -0.0812 115 GLU A O   
996  C CB  . GLU A 114 ? 0.4045 0.4343 0.5334 0.0273  0.0549  -0.0587 115 GLU A CB  
997  C CG  . GLU A 114 ? 0.6038 0.6100 0.7246 0.0382  0.0529  -0.0520 115 GLU A CG  
998  N N   . HIS A 115 ? 0.3157 0.3595 0.4297 -0.0080 0.0624  -0.0634 116 HIS A N   
999  C CA  . HIS A 115 ? 0.3323 0.3917 0.4507 -0.0196 0.0673  -0.0716 116 HIS A CA  
1000 C C   . HIS A 115 ? 0.3627 0.4081 0.4642 -0.0364 0.0781  -0.0753 116 HIS A C   
1001 O O   . HIS A 115 ? 0.3585 0.4159 0.4664 -0.0459 0.0877  -0.0867 116 HIS A O   
1002 C CB  . HIS A 115 ? 0.3524 0.4172 0.4673 -0.0211 0.0591  -0.0656 116 HIS A CB  
1003 C CG  . HIS A 115 ? 0.4028 0.4859 0.5344 -0.0067 0.0494  -0.0649 116 HIS A CG  
1004 N ND1 . HIS A 115 ? 0.4334 0.5438 0.5895 -0.0004 0.0501  -0.0765 116 HIS A ND1 
1005 C CD2 . HIS A 115 ? 0.4248 0.5032 0.5508 0.0018  0.0388  -0.0545 116 HIS A CD2 
1006 C CE1 . HIS A 115 ? 0.4275 0.5474 0.5907 0.0130  0.0383  -0.0719 116 HIS A CE1 
1007 N NE2 . HIS A 115 ? 0.4271 0.5272 0.5711 0.0139  0.0320  -0.0585 116 HIS A NE2 
1008 N N   . VAL A 116 ? 0.2985 0.3190 0.3780 -0.0403 0.0768  -0.0665 117 VAL A N   
1009 C CA  . VAL A 116 ? 0.3123 0.3163 0.3716 -0.0550 0.0852  -0.0690 117 VAL A CA  
1010 C C   . VAL A 116 ? 0.3804 0.3883 0.4478 -0.0566 0.0966  -0.0803 117 VAL A C   
1011 O O   . VAL A 116 ? 0.3567 0.3653 0.4181 -0.0699 0.1075  -0.0893 117 VAL A O   
1012 C CB  . VAL A 116 ? 0.3544 0.3344 0.3902 -0.0574 0.0791  -0.0582 117 VAL A CB  
1013 C CG1 . VAL A 116 ? 0.3688 0.3315 0.3819 -0.0713 0.0864  -0.0610 117 VAL A CG1 
1014 C CG2 . VAL A 116 ? 0.3469 0.3246 0.3761 -0.0568 0.0693  -0.0495 117 VAL A CG2 
1015 N N   . VAL A 117 ? 0.3350 0.3435 0.4147 -0.0435 0.0951  -0.0805 118 VAL A N   
1016 C CA  . VAL A 117 ? 0.3387 0.3510 0.4290 -0.0426 0.1058  -0.0922 118 VAL A CA  
1017 C C   . VAL A 117 ? 0.3991 0.4385 0.5116 -0.0450 0.1137  -0.1069 118 VAL A C   
1018 O O   . VAL A 117 ? 0.3974 0.4385 0.5081 -0.0565 0.1269  -0.1185 118 VAL A O   
1019 C CB  . VAL A 117 ? 0.3790 0.3858 0.4797 -0.0260 0.1018  -0.0897 118 VAL A CB  
1020 C CG1 . VAL A 117 ? 0.3815 0.3924 0.4954 -0.0237 0.1133  -0.1034 118 VAL A CG1 
1021 C CG2 . VAL A 117 ? 0.3772 0.3584 0.4559 -0.0274 0.0966  -0.0778 118 VAL A CG2 
1022 N N   A ASP A 118 ? 0.3650 0.4266 0.4990 -0.0341 0.1062  -0.1078 119 ASP A N   
1023 N N   B ASP A 118 ? 0.3536 0.4143 0.4849 -0.0362 0.1061  -0.1070 119 ASP A N   
1024 C CA  A ASP A 118 ? 0.3703 0.4635 0.5304 -0.0347 0.1119  -0.1233 119 ASP A CA  
1025 C CA  B ASP A 118 ? 0.3520 0.4436 0.5078 -0.0380 0.1118  -0.1219 119 ASP A CA  
1026 C C   A ASP A 118 ? 0.4320 0.5283 0.5818 -0.0570 0.1242  -0.1318 119 ASP A C   
1027 C C   B ASP A 118 ? 0.3918 0.4829 0.5339 -0.0608 0.1238  -0.1291 119 ASP A C   
1028 O O   A ASP A 118 ? 0.4408 0.5553 0.6061 -0.0635 0.1366  -0.1485 119 ASP A O   
1029 O O   B ASP A 118 ? 0.3875 0.4925 0.5409 -0.0689 0.1372  -0.1450 119 ASP A O   
1030 C CB  A ASP A 118 ? 0.3851 0.4996 0.5642 -0.0210 0.0989  -0.1205 119 ASP A CB  
1031 C CB  B ASP A 118 ? 0.3682 0.4801 0.5413 -0.0254 0.0989  -0.1186 119 ASP A CB  
1032 C CG  A ASP A 118 ? 0.5455 0.6653 0.7424 0.0024  0.0893  -0.1186 119 ASP A CG  
1033 C CG  B ASP A 118 ? 0.5410 0.6900 0.7443 -0.0249 0.1027  -0.1356 119 ASP A CG  
1034 O OD1 A ASP A 118 ? 0.5855 0.7092 0.7965 0.0095  0.0954  -0.1283 119 ASP A OD1 
1035 O OD1 B ASP A 118 ? 0.5668 0.7323 0.7928 -0.0177 0.1086  -0.1490 119 ASP A OD1 
1036 O OD2 A ASP A 118 ? 0.6177 0.7362 0.8130 0.0136  0.0758  -0.1076 119 ASP A OD2 
1037 O OD2 B ASP A 118 ? 0.5980 0.7605 0.8035 -0.0315 0.0999  -0.1365 119 ASP A OD2 
1038 N N   A THR A 119 ? 0.3872 0.4641 0.5100 -0.0686 0.1212  -0.1210 120 THR A N   
1039 N N   B THR A 119 ? 0.3428 0.4161 0.4596 -0.0713 0.1199  -0.1182 120 THR A N   
1040 C CA  A THR A 119 ? 0.3955 0.4667 0.5007 -0.0901 0.1318  -0.1261 120 THR A CA  
1041 C CA  B THR A 119 ? 0.3537 0.4203 0.4524 -0.0930 0.1312  -0.1239 120 THR A CA  
1042 C C   A THR A 119 ? 0.4389 0.4896 0.5218 -0.1040 0.1442  -0.1299 120 THR A C   
1043 C C   B THR A 119 ? 0.4120 0.4576 0.4882 -0.1063 0.1434  -0.1274 120 THR A C   
1044 O O   A THR A 119 ? 0.4440 0.5005 0.5249 -0.1199 0.1589  -0.1428 120 THR A O   
1045 O O   B THR A 119 ? 0.4062 0.4517 0.4735 -0.1242 0.1571  -0.1376 120 THR A O   
1046 C CB  A THR A 119 ? 0.5045 0.5604 0.5894 -0.0942 0.1226  -0.1130 120 THR A CB  
1047 C CB  B THR A 119 ? 0.3808 0.4316 0.4579 -0.0995 0.1236  -0.1120 120 THR A CB  
1048 O OG1 A THR A 119 ? 0.4940 0.5729 0.6025 -0.0816 0.1127  -0.1125 120 THR A OG1 
1049 O OG1 B THR A 119 ? 0.3940 0.4428 0.4591 -0.1195 0.1356  -0.1204 120 THR A OG1 
1050 C CG2 A THR A 119 ? 0.5146 0.5606 0.5790 -0.1156 0.1327  -0.1173 120 THR A CG2 
1051 C CG2 B THR A 119 ? 0.3114 0.3294 0.3584 -0.0992 0.1160  -0.0966 120 THR A CG2 
1052 N N   . CYS A 120 ? 0.3866 0.4134 0.4516 -0.0992 0.1390  -0.1194 121 CYS A N   
1053 C CA  . CYS A 120 ? 0.4085 0.4153 0.4509 -0.1113 0.1493  -0.1228 121 CYS A CA  
1054 C C   . CYS A 120 ? 0.4747 0.5014 0.5394 -0.1130 0.1641  -0.1413 121 CYS A C   
1055 O O   . CYS A 120 ? 0.4742 0.4960 0.5250 -0.1309 0.1789  -0.1514 121 CYS A O   
1056 C CB  . CYS A 120 ? 0.4045 0.3908 0.4338 -0.1026 0.1403  -0.1113 121 CYS A CB  
1057 S SG  . CYS A 120 ? 0.4559 0.4162 0.4535 -0.1053 0.1260  -0.0929 121 CYS A SG  
1058 N N   . ARG A 121 ? 0.4377 0.4869 0.5368 -0.0942 0.1599  -0.1464 122 ARG A N   
1059 C CA  . ARG A 121 ? 0.4455 0.5185 0.5735 -0.0907 0.1717  -0.1654 122 ARG A CA  
1060 C C   . ARG A 121 ? 0.4923 0.5890 0.6315 -0.1061 0.1847  -0.1817 122 ARG A C   
1061 O O   . ARG A 121 ? 0.4881 0.5910 0.6300 -0.1184 0.2017  -0.1979 122 ARG A O   
1062 C CB  . ARG A 121 ? 0.4503 0.5425 0.6119 -0.0651 0.1606  -0.1655 122 ARG A CB  
1063 C CG  . ARG A 121 ? 0.6647 0.7354 0.8202 -0.0518 0.1549  -0.1570 122 ARG A CG  
1064 C CD  . ARG A 121 ? 0.8493 0.9375 1.0380 -0.0317 0.1547  -0.1675 122 ARG A CD  
1065 N NE  . ARG A 121 ? 0.9632 1.0476 1.1591 -0.0103 0.1377  -0.1545 122 ARG A NE  
1066 C CZ  . ARG A 121 ? 1.0995 1.1574 1.2822 -0.0011 0.1320  -0.1433 122 ARG A CZ  
1067 N NH1 . ARG A 121 ? 0.8754 0.9104 1.0390 -0.0108 0.1410  -0.1439 122 ARG A NH1 
1068 N NH2 . ARG A 121 ? 0.9418 0.9954 1.1286 0.0167  0.1177  -0.1319 122 ARG A NH2 
1069 N N   . LYS A 122 ? 0.4517 0.5609 0.5965 -0.1071 0.1779  -0.1784 123 LYS A N   
1070 C CA  . LYS A 122 ? 0.4600 0.5919 0.6154 -0.1228 0.1897  -0.1937 123 LYS A CA  
1071 C C   . LYS A 122 ? 0.5205 0.6269 0.6381 -0.1504 0.2047  -0.1951 123 LYS A C   
1072 O O   . LYS A 122 ? 0.5113 0.6320 0.6354 -0.1665 0.2226  -0.2134 123 LYS A O   
1073 C CB  . LYS A 122 ? 0.4762 0.6238 0.6431 -0.1174 0.1776  -0.1883 123 LYS A CB  
1074 C CG  . LYS A 122 ? 0.6753 0.8544 0.8817 -0.0923 0.1646  -0.1914 123 LYS A CG  
1075 C CD  . LYS A 122 ? 0.7997 0.9987 1.0182 -0.0901 0.1549  -0.1901 123 LYS A CD  
1076 C CE  . LYS A 122 ? 0.9070 1.1221 1.1487 -0.0636 0.1361  -0.1835 123 LYS A CE  
1077 N NZ  . LYS A 122 ? 1.0010 1.2474 1.2807 -0.0472 0.1364  -0.1992 123 LYS A NZ  
1078 N N   . PHE A 123 ? 0.4898 0.5582 0.5672 -0.1557 0.1973  -0.1763 124 PHE A N   
1079 C CA  . PHE A 123 ? 0.5201 0.5573 0.5547 -0.1798 0.2083  -0.1745 124 PHE A CA  
1080 C C   . PHE A 123 ? 0.5842 0.6128 0.6080 -0.1894 0.2232  -0.1846 124 PHE A C   
1081 O O   . PHE A 123 ? 0.5892 0.6098 0.5934 -0.2121 0.2406  -0.1950 124 PHE A O   
1082 C CB  . PHE A 123 ? 0.5508 0.5521 0.5490 -0.1785 0.1936  -0.1523 124 PHE A CB  
1083 C CG  . PHE A 123 ? 0.5816 0.5785 0.5719 -0.1822 0.1868  -0.1449 124 PHE A CG  
1084 C CD1 . PHE A 123 ? 0.6023 0.6304 0.6273 -0.1713 0.1806  -0.1486 124 PHE A CD1 
1085 C CD2 . PHE A 123 ? 0.6454 0.6053 0.5924 -0.1953 0.1853  -0.1336 124 PHE A CD2 
1086 C CE1 . PHE A 123 ? 0.6105 0.6339 0.6277 -0.1754 0.1750  -0.1427 124 PHE A CE1 
1087 C CE2 . PHE A 123 ? 0.6725 0.6259 0.6120 -0.1979 0.1793  -0.1271 124 PHE A CE2 
1088 C CZ  . PHE A 123 ? 0.6201 0.6057 0.5951 -0.1888 0.1749  -0.1321 124 PHE A CZ  
1089 N N   . ILE A 124 ? 0.5227 0.5529 0.5594 -0.1732 0.2178  -0.1830 125 ILE A N   
1090 C CA  . ILE A 124 ? 0.5490 0.5732 0.5790 -0.1808 0.2320  -0.1943 125 ILE A CA  
1091 C C   . ILE A 124 ? 0.6116 0.6699 0.6744 -0.1871 0.2507  -0.2197 125 ILE A C   
1092 O O   . ILE A 124 ? 0.6287 0.6804 0.6746 -0.2076 0.2696  -0.2323 125 ILE A O   
1093 C CB  . ILE A 124 ? 0.5813 0.5963 0.6159 -0.1624 0.2216  -0.1863 125 ILE A CB  
1094 C CG1 . ILE A 124 ? 0.5882 0.5680 0.5840 -0.1635 0.2078  -0.1653 125 ILE A CG1 
1095 C CG2 . ILE A 124 ? 0.6184 0.6344 0.6567 -0.1672 0.2374  -0.2020 125 ILE A CG2 
1096 C CD1 . ILE A 124 ? 0.6702 0.6443 0.6743 -0.1438 0.1936  -0.1546 125 ILE A CD1 
1097 N N   . LYS A 125 ? 0.5618 0.6572 0.6705 -0.1699 0.2453  -0.2277 126 LYS A N   
1098 C CA  . LYS A 125 ? 0.5703 0.7059 0.7188 -0.1716 0.2600  -0.2534 126 LYS A CA  
1099 C C   . LYS A 125 ? 0.6375 0.7794 0.7747 -0.1997 0.2777  -0.2663 126 LYS A C   
1100 O O   . LYS A 125 ? 0.6324 0.7939 0.7837 -0.2129 0.2979  -0.2890 126 LYS A O   
1101 C CB  . LYS A 125 ? 0.5871 0.7586 0.7830 -0.1454 0.2456  -0.2562 126 LYS A CB  
1102 C CG  . LYS A 125 ? 0.7913 1.0059 1.0349 -0.1385 0.2566  -0.2829 126 LYS A CG  
1103 C CD  . LYS A 125 ? 0.9250 1.1769 1.2112 -0.1161 0.2414  -0.2860 126 LYS A CD  
1104 C CE  . LYS A 125 ? 1.0798 1.3793 1.4156 -0.1101 0.2516  -0.3148 126 LYS A CE  
1105 N NZ  . LYS A 125 ? 1.1880 1.5256 1.5628 -0.0904 0.2358  -0.3187 126 LYS A NZ  
1106 N N   . ALA A 126 ? 0.5964 0.7197 0.7064 -0.2099 0.2713  -0.2523 127 ALA A N   
1107 C CA  . ALA A 126 ? 0.6235 0.7446 0.7156 -0.2380 0.2878  -0.2619 127 ALA A CA  
1108 C C   . ALA A 126 ? 0.7305 0.8176 0.7771 -0.2641 0.3063  -0.2648 127 ALA A C   
1109 O O   . ALA A 126 ? 0.7364 0.8299 0.7772 -0.2885 0.3275  -0.2819 127 ALA A O   
1110 C CB  . ALA A 126 ? 0.6243 0.7278 0.6957 -0.2398 0.2746  -0.2444 127 ALA A CB  
1111 N N   . SER A 127 ? 0.7345 0.7860 0.7480 -0.2598 0.2986  -0.2488 128 SER A N   
1112 C CA  . SER A 127 ? 0.7988 0.8148 0.7644 -0.2826 0.3129  -0.2492 128 SER A CA  
1113 C C   . SER A 127 ? 0.8933 0.9255 0.8747 -0.2879 0.3316  -0.2705 128 SER A C   
1114 O O   . SER A 127 ? 0.9424 0.9516 0.8868 -0.3119 0.3489  -0.2767 128 SER A O   
1115 C CB  . SER A 127 ? 0.8724 0.8449 0.7950 -0.2765 0.2954  -0.2239 128 SER A CB  
1116 O OG  . SER A 127 ? 1.0347 0.9794 0.9231 -0.2846 0.2870  -0.2080 128 SER A OG  
1117 N N   . GLU A 128 ? 0.8218 0.8916 0.8558 -0.2657 0.3286  -0.2822 129 GLU A N   
1118 C CA  . GLU A 128 ? 1.1340 1.2212 1.1885 -0.2672 0.3457  -0.3038 129 GLU A CA  
1119 C C   . GLU A 128 ? 1.6581 1.7794 1.7371 -0.2862 0.3705  -0.3329 129 GLU A C   
1120 O O   . GLU A 128 ? 1.2630 1.3694 1.3097 -0.3146 0.3855  -0.3367 129 GLU A O   
1121 C CB  . GLU A 128 ? 1.1198 1.2278 1.2171 -0.2348 0.3320  -0.3040 129 GLU A CB  
1122 C CG  . GLU A 128 ? 1.2157 1.3723 1.3723 -0.2156 0.3273  -0.3173 129 GLU A CG  
1123 C CD  . GLU A 128 ? 1.4597 1.6300 1.6524 -0.1817 0.3101  -0.3131 129 GLU A CD  
1124 O OE1 . GLU A 128 ? 1.3848 1.5246 1.5560 -0.1711 0.2983  -0.2953 129 GLU A OE1 
1125 O OE2 . GLU A 128 ? 1.3568 1.5680 1.5988 -0.1656 0.3082  -0.3280 129 GLU A OE2 
1129 N N   A TRP B 2   ? 0.2239 0.4700 0.3486 -0.0551 -0.0134 -0.0817 1   TRP D N   
1130 N N   B TRP B 2   ? 0.2298 0.4759 0.3545 -0.0551 -0.0135 -0.0817 1   TRP D N   
1131 C CA  A TRP B 2   ? 0.2124 0.4582 0.3373 -0.0553 -0.0123 -0.0824 1   TRP D CA  
1132 C CA  B TRP B 2   ? 0.2229 0.4688 0.3480 -0.0553 -0.0124 -0.0824 1   TRP D CA  
1133 C C   A TRP B 2   ? 0.2564 0.5016 0.3839 -0.0553 -0.0123 -0.0807 1   TRP D C   
1134 C C   B TRP B 2   ? 0.2560 0.5012 0.3836 -0.0554 -0.0122 -0.0806 1   TRP D C   
1135 O O   A TRP B 2   ? 0.2627 0.5075 0.3920 -0.0552 -0.0133 -0.0799 1   TRP D O   
1136 O O   B TRP B 2   ? 0.2521 0.4969 0.3813 -0.0553 -0.0131 -0.0798 1   TRP D O   
1137 C CB  A TRP B 2   ? 0.1933 0.4388 0.3176 -0.0555 -0.0140 -0.0844 1   TRP D CB  
1138 C CB  B TRP B 2   ? 0.2085 0.4539 0.3329 -0.0556 -0.0140 -0.0842 1   TRP D CB  
1139 C CG  A TRP B 2   ? 0.1956 0.4416 0.3176 -0.0557 -0.0139 -0.0882 1   TRP D CG  
1140 C CG  B TRP B 2   ? 0.2200 0.4664 0.3478 -0.0556 -0.0161 -0.0833 1   TRP D CG  
1141 C CD1 A TRP B 2   ? 0.2279 0.4744 0.3505 -0.0553 -0.0161 -0.0900 1   TRP D CD1 
1142 C CD1 B TRP B 2   ? 0.2572 0.5050 0.3881 -0.0557 -0.0180 -0.0840 1   TRP D CD1 
1143 C CD2 A TRP B 2   ? 0.1938 0.4393 0.3127 -0.0563 -0.0114 -0.0915 1   TRP D CD2 
1144 C CD2 B TRP B 2   ? 0.2164 0.4632 0.3457 -0.0554 -0.0162 -0.0822 1   TRP D CD2 
1145 N NE1 A TRP B 2   ? 0.2203 0.4672 0.3405 -0.0553 -0.0153 -0.0949 1   TRP D NE1 
1146 N NE1 B TRP B 2   ? 0.2481 0.4982 0.3833 -0.0557 -0.0186 -0.0835 1   TRP D NE1 
1147 C CE2 A TRP B 2   ? 0.2365 0.4828 0.3543 -0.0562 -0.0121 -0.0963 1   TRP D CE2 
1148 C CE2 B TRP B 2   ? 0.2642 0.5139 0.3980 -0.0554 -0.0176 -0.0826 1   TRP D CE2 
1149 C CE3 A TRP B 2   ? 0.2015 0.4456 0.3187 -0.0568 -0.0085 -0.0912 1   TRP D CE3 
1150 C CE3 B TRP B 2   ? 0.2311 0.4764 0.3591 -0.0549 -0.0155 -0.0810 1   TRP D CE3 
1151 C CZ2 A TRP B 2   ? 0.2268 0.4729 0.3415 -0.0567 -0.0093 -0.1017 1   TRP D CZ2 
1152 C CZ2 B TRP B 2   ? 0.2528 0.5050 0.3896 -0.0548 -0.0178 -0.0823 1   TRP D CZ2 
1153 C CZ3 A TRP B 2   ? 0.2141 0.4573 0.3281 -0.0575 -0.0057 -0.0956 1   TRP D CZ3 
1154 C CZ3 B TRP B 2   ? 0.2516 0.4980 0.3816 -0.0541 -0.0166 -0.0804 1   TRP D CZ3 
1155 C CH2 A TRP B 2   ? 0.2281 0.4726 0.3408 -0.0575 -0.0058 -0.1012 1   TRP D CH2 
1156 C CH2 B TRP B 2   ? 0.2554 0.5058 0.3896 -0.0540 -0.0175 -0.0813 1   TRP D CH2 
1157 N N   . VAL B 3   ? 0.1997 0.4446 0.3280 -0.0554 -0.0109 -0.0806 2   VAL D N   
1158 C CA  . VAL B 3   ? 0.1973 0.4415 0.3288 -0.0552 -0.0114 -0.0801 2   VAL D CA  
1159 C C   . VAL B 3   ? 0.2266 0.4688 0.3576 -0.0545 -0.0119 -0.0796 2   VAL D C   
1160 O O   . VAL B 3   ? 0.2177 0.4589 0.3458 -0.0547 -0.0108 -0.0797 2   VAL D O   
1161 C CB  . VAL B 3   ? 0.2347 0.4805 0.3697 -0.0569 -0.0097 -0.0810 2   VAL D CB  
1162 C CG1 . VAL B 3   ? 0.2316 0.4785 0.3655 -0.0582 -0.0093 -0.0809 2   VAL D CG1 
1163 C CG2 . VAL B 3   ? 0.2310 0.4790 0.3678 -0.0577 -0.0073 -0.0818 2   VAL D CG2 
1164 N N   . ILE B 4   ? 0.1939 0.4351 0.3275 -0.0535 -0.0134 -0.0795 3   ILE D N   
1165 C CA  . ILE B 4   ? 0.2078 0.4466 0.3413 -0.0525 -0.0146 -0.0785 3   ILE D CA  
1166 C C   . ILE B 4   ? 0.2521 0.4912 0.3905 -0.0534 -0.0131 -0.0795 3   ILE D C   
1167 O O   . ILE B 4   ? 0.2502 0.4909 0.3937 -0.0541 -0.0134 -0.0817 3   ILE D O   
1168 C CB  . ILE B 4   ? 0.2415 0.4798 0.3763 -0.0505 -0.0174 -0.0788 3   ILE D CB  
1169 C CG1 . ILE B 4   ? 0.2275 0.4684 0.3603 -0.0500 -0.0182 -0.0787 3   ILE D CG1 
1170 C CG2 . ILE B 4   ? 0.2689 0.5037 0.4032 -0.0491 -0.0194 -0.0773 3   ILE D CG2 
1171 C CD1 . ILE B 4   ? 0.2491 0.4897 0.3766 -0.0513 -0.0184 -0.0772 3   ILE D CD1 
1172 N N   . PRO B 5   ? 0.2377 0.4761 0.3758 -0.0540 -0.0110 -0.0789 4   PRO D N   
1173 C CA  . PRO B 5   ? 0.2401 0.4810 0.3856 -0.0553 -0.0090 -0.0805 4   PRO D CA  
1174 C C   . PRO B 5   ? 0.3021 0.5408 0.4534 -0.0544 -0.0117 -0.0808 4   PRO D C   
1175 O O   . PRO B 5   ? 0.2914 0.5253 0.4390 -0.0522 -0.0147 -0.0787 4   PRO D O   
1176 C CB  . PRO B 5   ? 0.2640 0.5047 0.4076 -0.0556 -0.0054 -0.0801 4   PRO D CB  
1177 C CG  . PRO B 5   ? 0.3163 0.5514 0.4513 -0.0544 -0.0070 -0.0779 4   PRO D CG  
1178 C CD  . PRO B 5   ? 0.2587 0.4946 0.3905 -0.0540 -0.0098 -0.0777 4   PRO D CD  
1179 N N   . ALA B 6   ? 0.2698 0.5125 0.4306 -0.0564 -0.0108 -0.0838 5   ALA D N   
# 
