data_7GUI
# 
_entry.id   7GUI 
# 
_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   7GUI         pdb_00007gui 10.2210/pdb7gui/pdb 
WWPDB D_1001406653 ?            ?                   
# 
_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                        7GUI 
_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 84  HOH HOH A . 
F 6 HOH 3   303 81  HOH HOH A . 
F 6 HOH 4   304 159 HOH HOH A . 
F 6 HOH 5   305 88  HOH HOH A . 
F 6 HOH 6   306 15  HOH HOH A . 
F 6 HOH 7   307 189 HOH HOH A . 
F 6 HOH 8   308 166 HOH HOH A . 
F 6 HOH 9   309 23  HOH HOH A . 
F 6 HOH 10  310 92  HOH HOH A . 
F 6 HOH 11  311 230 HOH HOH A . 
F 6 HOH 12  312 130 HOH HOH A . 
F 6 HOH 13  313 114 HOH HOH A . 
F 6 HOH 14  314 149 HOH HOH A . 
F 6 HOH 15  315 32  HOH HOH A . 
F 6 HOH 16  316 87  HOH HOH A . 
F 6 HOH 17  317 24  HOH HOH A . 
F 6 HOH 18  318 14  HOH HOH A . 
F 6 HOH 19  319 5   HOH HOH A . 
F 6 HOH 20  320 187 HOH HOH A . 
F 6 HOH 21  321 83  HOH HOH A . 
F 6 HOH 22  322 85  HOH HOH A . 
F 6 HOH 23  323 143 HOH HOH A . 
F 6 HOH 24  324 44  HOH HOH A . 
F 6 HOH 25  325 109 HOH HOH A . 
F 6 HOH 26  326 196 HOH HOH A . 
F 6 HOH 27  327 63  HOH HOH A . 
F 6 HOH 28  328 33  HOH HOH A . 
F 6 HOH 29  329 103 HOH HOH A . 
F 6 HOH 30  330 113 HOH HOH A . 
F 6 HOH 31  331 94  HOH HOH A . 
F 6 HOH 32  332 135 HOH HOH A . 
F 6 HOH 33  333 90  HOH HOH A . 
F 6 HOH 34  334 134 HOH HOH A . 
F 6 HOH 35  335 3   HOH HOH A . 
F 6 HOH 36  336 165 HOH HOH A . 
F 6 HOH 37  337 97  HOH HOH A . 
F 6 HOH 38  338 13  HOH HOH A . 
F 6 HOH 39  339 49  HOH HOH A . 
F 6 HOH 40  340 105 HOH HOH A . 
F 6 HOH 41  341 213 HOH HOH A . 
F 6 HOH 42  342 112 HOH HOH A . 
F 6 HOH 43  343 141 HOH HOH A . 
F 6 HOH 44  344 136 HOH HOH A . 
F 6 HOH 45  345 100 HOH HOH A . 
F 6 HOH 46  346 11  HOH HOH A . 
F 6 HOH 47  347 50  HOH HOH A . 
F 6 HOH 48  348 180 HOH HOH A . 
F 6 HOH 49  349 51  HOH HOH A . 
F 6 HOH 50  350 123 HOH HOH A . 
F 6 HOH 51  351 117 HOH HOH A . 
F 6 HOH 52  352 35  HOH HOH A . 
F 6 HOH 53  353 110 HOH HOH A . 
F 6 HOH 54  354 6   HOH HOH A . 
F 6 HOH 55  355 18  HOH HOH A . 
F 6 HOH 56  356 184 HOH HOH A . 
F 6 HOH 57  357 116 HOH HOH A . 
F 6 HOH 58  358 74  HOH HOH A . 
F 6 HOH 59  359 115 HOH HOH A . 
F 6 HOH 60  360 102 HOH HOH A . 
F 6 HOH 61  361 151 HOH HOH A . 
F 6 HOH 62  362 121 HOH HOH A . 
F 6 HOH 63  363 150 HOH HOH A . 
F 6 HOH 64  364 86  HOH HOH A . 
F 6 HOH 65  365 95  HOH HOH A . 
F 6 HOH 66  366 89  HOH HOH A . 
F 6 HOH 67  367 107 HOH HOH A . 
F 6 HOH 68  368 231 HOH HOH A . 
F 6 HOH 69  369 26  HOH HOH A . 
F 6 HOH 70  370 25  HOH HOH A . 
F 6 HOH 71  371 192 HOH HOH A . 
F 6 HOH 72  372 62  HOH HOH A . 
F 6 HOH 73  373 101 HOH HOH A . 
F 6 HOH 74  374 147 HOH HOH A . 
F 6 HOH 75  375 28  HOH HOH A . 
F 6 HOH 76  376 20  HOH HOH A . 
F 6 HOH 77  377 66  HOH HOH A . 
F 6 HOH 78  378 22  HOH HOH A . 
F 6 HOH 79  379 178 HOH HOH A . 
F 6 HOH 80  380 164 HOH HOH A . 
F 6 HOH 81  381 57  HOH HOH A . 
F 6 HOH 82  382 168 HOH HOH A . 
F 6 HOH 83  383 39  HOH HOH A . 
F 6 HOH 84  384 104 HOH HOH A . 
F 6 HOH 85  385 119 HOH HOH A . 
F 6 HOH 86  386 246 HOH HOH A . 
F 6 HOH 87  387 10  HOH HOH A . 
F 6 HOH 88  388 29  HOH HOH A . 
F 6 HOH 89  389 99  HOH HOH A . 
F 6 HOH 90  390 21  HOH HOH A . 
F 6 HOH 91  391 60  HOH HOH A . 
F 6 HOH 92  392 244 HOH HOH A . 
F 6 HOH 93  393 40  HOH HOH A . 
F 6 HOH 94  394 238 HOH HOH A . 
F 6 HOH 95  395 82  HOH HOH A . 
F 6 HOH 96  396 56  HOH HOH A . 
F 6 HOH 97  397 27  HOH HOH A . 
F 6 HOH 98  398 93  HOH HOH A . 
F 6 HOH 99  399 30  HOH HOH A . 
F 6 HOH 100 400 242 HOH HOH A . 
F 6 HOH 101 401 239 HOH HOH A . 
F 6 HOH 102 402 96  HOH HOH A . 
F 6 HOH 103 403 53  HOH HOH A . 
F 6 HOH 104 404 36  HOH HOH A . 
F 6 HOH 105 405 75  HOH HOH A . 
F 6 HOH 106 406 52  HOH HOH A . 
F 6 HOH 107 407 37  HOH HOH A . 
F 6 HOH 108 408 17  HOH HOH A . 
F 6 HOH 109 409 38  HOH HOH A . 
F 6 HOH 110 410 193 HOH HOH A . 
F 6 HOH 111 411 171 HOH HOH A . 
F 6 HOH 112 412 167 HOH HOH A . 
F 6 HOH 113 413 45  HOH HOH A . 
F 6 HOH 114 414 209 HOH HOH A . 
F 6 HOH 115 415 176 HOH HOH A . 
F 6 HOH 116 416 237 HOH HOH A . 
F 6 HOH 117 417 69  HOH HOH A . 
F 6 HOH 118 418 54  HOH HOH A . 
F 6 HOH 119 419 148 HOH HOH A . 
F 6 HOH 120 420 200 HOH HOH A . 
F 6 HOH 121 421 241 HOH HOH A . 
F 6 HOH 122 422 203 HOH HOH A . 
F 6 HOH 123 423 186 HOH HOH A . 
F 6 HOH 124 424 146 HOH HOH A . 
F 6 HOH 125 425 55  HOH HOH A . 
F 6 HOH 126 426 43  HOH HOH A . 
F 6 HOH 127 427 79  HOH HOH A . 
F 6 HOH 128 428 98  HOH HOH A . 
F 6 HOH 129 429 145 HOH HOH A . 
F 6 HOH 130 430 31  HOH HOH A . 
F 6 HOH 131 431 153 HOH HOH A . 
F 6 HOH 132 432 139 HOH HOH A . 
F 6 HOH 133 433 185 HOH HOH A . 
F 6 HOH 134 434 106 HOH HOH A . 
F 6 HOH 135 435 158 HOH HOH A . 
F 6 HOH 136 436 191 HOH HOH A . 
F 6 HOH 137 437 188 HOH HOH A . 
F 6 HOH 138 438 232 HOH HOH A . 
F 6 HOH 139 439 80  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 143 443 137 HOH HOH A . 
F 6 HOH 144 444 221 HOH HOH A . 
F 6 HOH 145 445 169 HOH HOH A . 
F 6 HOH 146 446 140 HOH HOH A . 
F 6 HOH 147 447 108 HOH HOH A . 
F 6 HOH 148 448 247 HOH HOH A . 
F 6 HOH 149 449 206 HOH HOH A . 
F 6 HOH 150 450 70  HOH HOH A . 
F 6 HOH 151 451 228 HOH HOH A . 
F 6 HOH 152 452 131 HOH HOH A . 
F 6 HOH 153 453 161 HOH HOH A . 
F 6 HOH 154 454 243 HOH HOH A . 
F 6 HOH 155 455 215 HOH HOH A . 
F 6 HOH 156 456 212 HOH HOH A . 
F 6 HOH 157 457 183 HOH HOH A . 
F 6 HOH 158 458 59  HOH HOH A . 
F 6 HOH 159 459 142 HOH HOH A . 
F 6 HOH 160 460 73  HOH HOH A . 
F 6 HOH 161 461 245 HOH HOH A . 
F 6 HOH 162 462 170 HOH HOH A . 
F 6 HOH 163 463 175 HOH HOH A . 
F 6 HOH 164 464 179 HOH HOH A . 
F 6 HOH 165 465 65  HOH HOH A . 
F 6 HOH 166 466 181 HOH HOH A . 
F 6 HOH 167 467 195 HOH HOH A . 
F 6 HOH 168 468 152 HOH HOH A . 
F 6 HOH 169 469 208 HOH HOH A . 
F 6 HOH 170 470 61  HOH HOH A . 
F 6 HOH 171 471 233 HOH HOH A . 
F 6 HOH 172 472 144 HOH HOH A . 
F 6 HOH 173 473 225 HOH HOH A . 
G 6 HOH 1   201 77  HOH HOH D . 
G 6 HOH 2   202 71  HOH HOH D . 
G 6 HOH 3   203 68  HOH HOH D . 
G 6 HOH 4   204 47  HOH HOH D . 
G 6 HOH 5   205 58  HOH HOH D . 
G 6 HOH 6   206 240 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           7GUI 
_cell.length_a           67.580 
_cell.length_b           67.580 
_cell.length_c           166.210 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        120.000 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7GUI 
_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          7GUI 
_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   65.99 
_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                     7GUI 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.880 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   21726 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.116 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        9.600 
_reflns.B_iso_Wilson_estimate        29.920 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.123 
_reflns.pdbx_Rpim_I_all              0.041 
_reflns.pdbx_CC_half                 0.992 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     197520 
_reflns.pdbx_scaling_rejects         119 
_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  ? 11602 1245 ? 1.043 ? ? ? 9.300 ? 2.100  ? ? ? ? ? ? 100.000 1.104 0.357 0.821 ? 
1 2 9.000 33.880 ? 1645  240  ? 0.112 ? ? ? 6.900 ? 16.600 ? ? ? ? ? ? 98.800  0.120 0.043 0.977 ? 
# 
_refine.entry_id                                 7GUI 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.8000 
_refine.ls_d_res_low                             33.8800 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    100.0000 
_refine.ls_number_reflns_obs                     21657 
_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                          0.1840 
_refine.ls_R_factor_R_work                       0.1820 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2090 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.2000 
_refine.ls_number_reflns_R_free                  1126 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               35.1300 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.4422 
_refine.aniso_B[2][2]                            -0.4422 
_refine.aniso_B[3][3]                            0.8845 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9580 
_refine.correlation_coeff_Fo_to_Fc_free          0.9490 
_refine.overall_SU_R_Cruickshank_DPI             0.0950 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0950 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1090 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.1040 
_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                                128.160 
_refine.B_iso_min                                17.130 
_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                        7GUI 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.200 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.8000 
_refine_hist.d_res_low                        33.8800 
_refine_hist.pdbx_number_atoms_ligand         23 
_refine_hist.number_atoms_solvent             181 
_refine_hist.number_atoms_total               1230 
_refine_hist.pdbx_number_residues_total       130 
_refine_hist.pdbx_B_iso_mean_ligand           29.78 
_refine_hist.pdbx_B_iso_mean_solvent          52.49 
_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      1645 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1236 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1693 0.920  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.450  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    16.210 ? ?      ?            
# 
_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               99.8200 
_refine_ls_shell.number_reflns_R_work             2680 
_refine_ls_shell.R_factor_all                     0.2597 
_refine_ls_shell.R_factor_R_work                  0.2593 
_refine_ls_shell.R_factor_R_free                  0.2682 
_refine_ls_shell.percent_reflns_R_free            4.6300 
_refine_ls_shell.number_reflns_R_free             130 
_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                  7GUI 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 1 at 9.06 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUI 
_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 7GUI       7GUI   ? 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 7GUI A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUI D 1 ? 6   ? 7GUI   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 7GUI GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUI PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUI GLY A 3 ? UNP P41182 ? ? 'expression tag' 4 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6380  ? 
1 MORE         -68   ? 
1 'SSA (A^2)'  13270 ? 
# 
_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 27.7016666667 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ARG A 12  ? ARG A 27  ? ARG A 13  ARG A 28  1 ? 16 
HELX_P HELX_P2 AA2 HIS A 45  ? SER A 53  ? HIS A 46  SER A 54  1 ? 9  
HELX_P HELX_P3 AA3 SER A 53  ? THR A 61  ? SER A 54  THR A 62  1 ? 9  
HELX_P HELX_P4 AA4 LEU A 64  ? LEU A 68  ? LEU A 65  LEU A 69  5 ? 5  
HELX_P HELX_P5 AA5 ASN A 78  ? SER A 92  ? ASN A 79  SER A 93  1 ? 15 
HELX_P HELX_P6 AA6 ASN A 100 ? GLN A 112 ? ASN A 101 GLN A 113 1 ? 13 
HELX_P HELX_P7 AA7 MET A 113 ? GLU A 128 ? MET A 114 GLU A 129 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N A ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 ACE B 1 ? TRP B 2 A ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
2 ACE B 1 ? TRP B 2 B ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 40 ? ALA A 44 ? GLU A 41 ALA A 45 
AA1 2 VAL A 33 ? VAL A 37 ? VAL A 34 VAL A 38 
AA1 3 VAL A 70 ? ASN A 72 ? VAL A 71 ASN A 73 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 40 ? O GLU A 41 N VAL A 37 ? N VAL A 38 
AA1 2 3 N VAL A 36 ? N VAL A 37 O ILE A 71 ? O ILE A 72 
# 
_pdbx_entry_details.entry_id                   7GUI 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 39  ? A 38.06   48.50   
2 1 SER A 39  ? B 62.17   -109.58 
3 1 SER A 93  ? ? 77.15   -1.09   
4 1 SER A 93  ? ? 77.15   -3.12   
5 1 GLN A 113 ? ? 62.32   63.78   
6 1 MET A 114 ? ? -119.63 79.69   
# 
_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   10.71 
# 
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 336 ? F HOH . 
2 1 A HOH 380 ? F HOH . 
3 1 A HOH 445 ? F HOH . 
4 1 A HOH 463 ? F HOH . 
5 1 A HOH 464 ? F HOH . 
6 1 A HOH 467 ? F HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 29.2805 -16.6200 24.3685 0.0011  -0.0582 -0.0571 -0.0393 0.0261  -0.0180 1.0030 1.8488 2.1698 
0.4171 -0.3186 1.1861 0.1411 -0.0925 -0.0485 -0.0573 0.0930 0.0746 0.2615 0.0192 -0.0560 
'X-RAY DIFFRACTION' 2 ? refined 18.9623 -32.3913 1.8231  -0.1040 0.1122  -0.0360 -0.0474 -0.0151 -0.0821 0.6140 0.0877 0.0000 
0.2532 -0.2155 0.2219 0.0141 0.0016  -0.0157 -0.0047 0.0204 0.0305 0.0003 0.0153 0.0056  
# 
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                    7GUI 
_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]   0.006016 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASP A 1 5   ? 17.549 -21.152 -4.876 1.00 65.86  ? 6   ASP A N   1 
ATOM   2    C  CA  . ASP A 1 5   ? 18.403 -22.061 -5.646 1.00 64.86  ? 6   ASP A CA  1 
ATOM   3    C  C   . ASP A 1 5   ? 17.901 -23.523 -5.562 1.00 64.89  ? 6   ASP A C   1 
ATOM   4    O  O   . ASP A 1 5   ? 16.819 -23.779 -5.023 1.00 65.61  ? 6   ASP A O   1 
ATOM   5    C  CB  . ASP A 1 5   ? 19.870 -21.950 -5.161 1.00 65.56  ? 6   ASP A CB  1 
ATOM   6    C  CG  . ASP A 1 5   ? 20.905 -22.023 -6.275 1.00 79.08  ? 6   ASP A CG  1 
ATOM   7    O  OD1 . ASP A 1 5   ? 20.980 -23.077 -6.955 1.00 79.58  ? 6   ASP A OD1 1 
ATOM   8    O  OD2 . ASP A 1 5   ? 21.651 -21.034 -6.457 1.00 85.98  ? 6   ASP A OD2 1 
ATOM   9    N  N   . SER A 1 6   ? 18.684 -24.469 -6.113 1.00 56.36  ? 7   SER A N   1 
ATOM   10   C  CA  . SER A 1 6   ? 18.394 -25.901 -6.090 1.00 53.94  ? 7   SER A CA  1 
ATOM   11   C  C   . SER A 1 6   ? 19.390 -26.647 -5.145 1.00 49.89  ? 7   SER A C   1 
ATOM   12   O  O   . SER A 1 6   ? 19.704 -27.819 -5.367 1.00 49.35  ? 7   SER A O   1 
ATOM   13   C  CB  . SER A 1 6   ? 18.440 -26.466 -7.506 1.00 59.73  ? 7   SER A CB  1 
ATOM   14   O  OG  . SER A 1 6   ? 19.710 -26.269 -8.108 1.00 72.26  ? 7   SER A OG  1 
ATOM   15   N  N   . CYS A 1 7   ? 19.862 -25.966 -4.081 1.00 40.44  ? 8   CYS A N   1 
ATOM   16   C  CA  . CYS A 1 7   ? 20.808 -26.551 -3.119 1.00 36.81  ? 8   CYS A CA  1 
ATOM   17   C  C   . CYS A 1 7   ? 20.188 -27.713 -2.317 1.00 36.52  ? 8   CYS A C   1 
ATOM   18   O  O   . CYS A 1 7   ? 18.973 -27.761 -2.134 1.00 36.47  ? 8   CYS A O   1 
ATOM   19   C  CB  . CYS A 1 7   ? 21.318 -25.470 -2.164 1.00 37.41  ? 8   CYS A CB  1 
ATOM   20   S  SG  . CYS A 1 7   ? 22.432 -24.245 -2.914 1.00 42.26  ? 8   CYS A SG  1 
ATOM   21   N  N   . ILE A 1 8   ? 21.027 -28.619 -1.813 1.00 27.59  ? 9   ILE A N   1 
ATOM   22   C  CA  . ILE A 1 8   ? 20.661 -29.617 -0.807 1.00 24.84  ? 9   ILE A CA  1 
ATOM   23   C  C   . ILE A 1 8   ? 21.259 -29.077 0.490  1.00 26.96  ? 9   ILE A C   1 
ATOM   24   O  O   . ILE A 1 8   ? 22.199 -28.279 0.439  1.00 25.32  ? 9   ILE A O   1 
ATOM   25   C  CB  . ILE A 1 8   ? 21.037 -31.094 -1.114 1.00 27.83  ? 9   ILE A CB  1 
ATOM   26   C  CG1 . ILE A 1 8   ? 22.561 -31.266 -1.399 1.00 27.76  ? 9   ILE A CG1 1 
ATOM   27   C  CG2 . ILE A 1 8   ? 20.167 -31.632 -2.262 1.00 29.45  ? 9   ILE A CG2 1 
ATOM   28   C  CD1 . ILE A 1 8   ? 23.064 -32.722 -1.551 1.00 31.73  ? 9   ILE A CD1 1 
ATOM   29   N  N   A GLN A 1 9   ? 20.771 -29.520 1.649  0.57 22.05  ? 10  GLN A N   1 
ATOM   30   N  N   B GLN A 1 9   ? 20.670 -29.440 1.630  0.43 22.34  ? 10  GLN A N   1 
ATOM   31   C  CA  A GLN A 1 9   ? 21.305 -29.010 2.913  0.57 20.99  ? 10  GLN A CA  1 
ATOM   32   C  CA  B GLN A 1 9   ? 21.097 -28.960 2.940  0.43 21.29  ? 10  GLN A CA  1 
ATOM   33   C  C   A GLN A 1 9   ? 21.643 -30.134 3.891  0.57 24.25  ? 10  GLN A C   1 
ATOM   34   C  C   B GLN A 1 9   ? 21.569 -30.111 3.818  0.43 23.72  ? 10  GLN A C   1 
ATOM   35   O  O   A GLN A 1 9   ? 20.843 -31.051 4.063  0.57 23.90  ? 10  GLN A O   1 
ATOM   36   O  O   B GLN A 1 9   ? 20.954 -31.175 3.818  0.43 23.28  ? 10  GLN A O   1 
ATOM   37   C  CB  A GLN A 1 9   ? 20.291 -28.019 3.533  0.57 22.24  ? 10  GLN A CB  1 
ATOM   38   C  CB  B GLN A 1 9   ? 19.931 -28.196 3.615  0.43 22.61  ? 10  GLN A CB  1 
ATOM   39   C  CG  A GLN A 1 9   ? 20.737 -27.386 4.853  0.57 20.85  ? 10  GLN A CG  1 
ATOM   40   C  CG  B GLN A 1 9   ? 20.101 -27.935 5.129  0.43 32.20  ? 10  GLN A CG  1 
ATOM   41   C  CD  A GLN A 1 9   ? 19.592 -26.678 5.534  0.57 48.92  ? 10  GLN A CD  1 
ATOM   42   C  CD  B GLN A 1 9   ? 20.092 -26.481 5.530  0.43 39.69  ? 10  GLN A CD  1 
ATOM   43   O  OE1 A GLN A 1 9   ? 18.624 -27.292 5.998  0.57 40.44  ? 10  GLN A OE1 1 
ATOM   44   O  OE1 B GLN A 1 9   ? 19.788 -25.578 4.736  0.43 28.46  ? 10  GLN A OE1 1 
ATOM   45   N  NE2 A GLN A 1 9   ? 19.678 -25.362 5.612  0.57 52.63  ? 10  GLN A NE2 1 
ATOM   46   N  NE2 B GLN A 1 9   ? 20.421 -26.224 6.794  0.43 27.89  ? 10  GLN A NE2 1 
ATOM   47   N  N   A PHE A 1 10  ? 22.810 -30.053 4.548  0.78 21.95  ? 11  PHE A N   1 
ATOM   48   N  N   B PHE A 1 10  ? 22.637 -29.881 4.586  0.22 20.41  ? 11  PHE A N   1 
ATOM   49   C  CA  A PHE A 1 10  ? 23.185 -31.061 5.542  0.78 21.60  ? 11  PHE A CA  1 
ATOM   50   C  CA  B PHE A 1 10  ? 23.153 -30.854 5.539  0.22 20.14  ? 11  PHE A CA  1 
ATOM   51   C  C   A PHE A 1 10  ? 22.712 -30.557 6.906  0.78 23.61  ? 11  PHE A C   1 
ATOM   52   C  C   B PHE A 1 10  ? 22.628 -30.415 6.890  0.22 23.35  ? 11  PHE A C   1 
ATOM   53   O  O   A PHE A 1 10  ? 23.284 -29.599 7.454  0.78 22.29  ? 11  PHE A O   1 
ATOM   54   O  O   B PHE A 1 10  ? 23.055 -29.373 7.407  0.22 22.18  ? 11  PHE A O   1 
ATOM   55   C  CB  A PHE A 1 10  ? 24.709 -31.368 5.504  0.78 22.86  ? 11  PHE A CB  1 
ATOM   56   C  CB  B PHE A 1 10  ? 24.689 -30.911 5.474  0.22 21.40  ? 11  PHE A CB  1 
ATOM   57   C  CG  A PHE A 1 10  ? 25.080 -32.567 6.350  0.78 23.80  ? 11  PHE A CG  1 
ATOM   58   C  CG  B PHE A 1 10  ? 25.167 -31.838 4.383  0.22 23.55  ? 11  PHE A CG  1 
ATOM   59   C  CD1 A PHE A 1 10  ? 24.692 -33.852 5.977  0.78 27.28  ? 11  PHE A CD1 1 
ATOM   60   C  CD1 B PHE A 1 10  ? 25.050 -31.483 3.042  0.22 27.26  ? 11  PHE A CD1 1 
ATOM   61   C  CD2 A PHE A 1 10  ? 25.849 -32.417 7.497  0.78 25.65  ? 11  PHE A CD2 1 
ATOM   62   C  CD2 B PHE A 1 10  ? 25.688 -33.086 4.690  0.22 26.66  ? 11  PHE A CD2 1 
ATOM   63   C  CE1 A PHE A 1 10  ? 25.018 -34.961 6.777  0.78 28.47  ? 11  PHE A CE1 1 
ATOM   64   C  CE1 B PHE A 1 10  ? 25.481 -32.345 2.034  0.22 28.67  ? 11  PHE A CE1 1 
ATOM   65   C  CE2 A PHE A 1 10  ? 26.170 -33.518 8.296  0.78 27.84  ? 11  PHE A CE2 1 
ATOM   66   C  CE2 B PHE A 1 10  ? 26.104 -33.954 3.678  0.22 30.16  ? 11  PHE A CE2 1 
ATOM   67   C  CZ  A PHE A 1 10  ? 25.765 -34.782 7.925  0.78 26.00  ? 11  PHE A CZ  1 
ATOM   68   C  CZ  B PHE A 1 10  ? 26.011 -33.571 2.361  0.22 28.29  ? 11  PHE A CZ  1 
ATOM   69   N  N   . THR A 1 11  ? 21.620 -31.147 7.410  1.00 20.45  ? 12  THR A N   1 
ATOM   70   C  CA  . THR A 1 11  ? 20.943 -30.768 8.673  1.00 21.05  ? 12  THR A CA  1 
ATOM   71   C  C   . THR A 1 11  ? 21.899 -30.521 9.877  1.00 24.25  ? 12  THR A C   1 
ATOM   72   O  O   . THR A 1 11  ? 21.763 -29.500 10.563 1.00 23.52  ? 12  THR A O   1 
ATOM   73   C  CB  . THR A 1 11  ? 19.872 -31.815 9.022  1.00 28.76  ? 12  THR A CB  1 
ATOM   74   O  OG1 . THR A 1 11  ? 18.933 -31.898 7.930  1.00 28.42  ? 12  THR A OG1 1 
ATOM   75   C  CG2 . THR A 1 11  ? 19.107 -31.470 10.313 1.00 33.07  ? 12  THR A CG2 1 
ATOM   76   N  N   A ARG A 1 12  ? 22.843 -31.447 10.108 0.50 21.69  ? 13  ARG A N   1 
ATOM   77   N  N   B ARG A 1 12  ? 22.837 -31.448 10.120 0.50 21.80  ? 13  ARG A N   1 
ATOM   78   C  CA  A ARG A 1 12  ? 23.766 -31.383 11.253 0.50 21.86  ? 13  ARG A CA  1 
ATOM   79   C  CA  B ARG A 1 12  ? 23.758 -31.370 11.265 0.50 21.99  ? 13  ARG A CA  1 
ATOM   80   C  C   A ARG A 1 12  ? 25.019 -30.509 11.052 0.50 23.68  ? 13  ARG A C   1 
ATOM   81   C  C   B ARG A 1 12  ? 24.997 -30.474 11.070 0.50 23.61  ? 13  ARG A C   1 
ATOM   82   O  O   A ARG A 1 12  ? 25.845 -30.428 11.972 0.50 22.00  ? 13  ARG A O   1 
ATOM   83   O  O   B ARG A 1 12  ? 25.795 -30.351 12.011 0.50 21.79  ? 13  ARG A O   1 
ATOM   84   C  CB  A ARG A 1 12  ? 24.185 -32.809 11.677 0.50 25.52  ? 13  ARG A CB  1 
ATOM   85   C  CB  B ARG A 1 12  ? 24.204 -32.785 11.666 0.50 26.03  ? 13  ARG A CB  1 
ATOM   86   C  CG  A ARG A 1 12  ? 23.052 -33.690 12.231 0.50 34.49  ? 13  ARG A CG  1 
ATOM   87   C  CG  B ARG A 1 12  ? 23.241 -33.497 12.618 0.50 37.17  ? 13  ARG A CG  1 
ATOM   88   C  CD  A ARG A 1 12  ? 22.512 -33.212 13.572 0.50 45.99  ? 13  ARG A CD  1 
ATOM   89   C  CD  B ARG A 1 12  ? 22.970 -34.943 12.239 0.50 45.01  ? 13  ARG A CD  1 
ATOM   90   N  NE  A ARG A 1 12  ? 23.477 -33.369 14.663 0.50 51.43  ? 13  ARG A NE  1 
ATOM   91   N  NE  B ARG A 1 12  ? 24.185 -35.718 11.966 0.50 48.09  ? 13  ARG A NE  1 
ATOM   92   C  CZ  A ARG A 1 12  ? 23.417 -32.715 15.819 0.50 58.60  ? 13  ARG A CZ  1 
ATOM   93   C  CZ  B ARG A 1 12  ? 24.369 -36.457 10.874 0.50 57.79  ? 13  ARG A CZ  1 
ATOM   94   N  NH1 A ARG A 1 12  ? 22.453 -31.830 16.042 0.50 39.72  ? 13  ARG A NH1 1 
ATOM   95   N  NH1 B ARG A 1 12  ? 25.497 -37.136 10.708 0.50 49.25  ? 13  ARG A NH1 1 
ATOM   96   N  NH2 A ARG A 1 12  ? 24.328 -32.931 16.757 0.50 47.75  ? 13  ARG A NH2 1 
ATOM   97   N  NH2 B ARG A 1 12  ? 23.423 -36.532 9.946  0.50 35.00  ? 13  ARG A NH2 1 
ATOM   98   N  N   . HIS A 1 13  ? 25.167 -29.865 9.878  1.00 20.03  ? 14  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 13  ? 26.375 -29.062 9.567  1.00 19.56  ? 14  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 13  ? 26.658 -27.960 10.573 1.00 21.36  ? 14  HIS A C   1 
ATOM   101  O  O   . HIS A 1 13  ? 27.796 -27.870 11.051 1.00 20.61  ? 14  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 13  ? 26.354 -28.490 8.140  1.00 19.70  ? 14  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 13  ? 27.631 -27.754 7.813  1.00 21.08  ? 14  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 13  ? 28.812 -28.434 7.608  1.00 21.66  ? 14  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 13  ? 27.865 -26.426 7.690  1.00 22.07  ? 14  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 13  ? 29.730 -27.514 7.357  1.00 21.15  ? 14  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 13  ? 29.202 -26.288 7.381  1.00 21.30  ? 14  HIS A NE2 1 
ATOM   108  N  N   . ALA A 1 14  ? 25.667 -27.087 10.846 1.00 18.79  ? 15  ALA A N   1 
ATOM   109  C  CA  . ALA A 1 14  ? 25.886 -25.958 11.782 1.00 18.53  ? 15  ALA A CA  1 
ATOM   110  C  C   . ALA A 1 14  ? 26.303 -26.446 13.182 1.00 21.26  ? 15  ALA A C   1 
ATOM   111  O  O   . ALA A 1 14  ? 27.216 -25.869 13.782 1.00 18.99  ? 15  ALA A O   1 
ATOM   112  C  CB  . ALA A 1 14  ? 24.642 -25.069 11.852 1.00 19.97  ? 15  ALA A CB  1 
ATOM   113  N  N   A SER A 1 15  ? 25.636 -27.490 13.689 0.38 19.08  ? 16  SER A N   1 
ATOM   114  N  N   B SER A 1 15  ? 25.640 -27.501 13.690 0.33 19.43  ? 16  SER A N   1 
ATOM   115  N  N   C SER A 1 15  ? 25.636 -27.498 13.699 0.29 18.81  ? 16  SER A N   1 
ATOM   116  C  CA  A SER A 1 15  ? 25.932 -28.071 14.994 0.38 19.32  ? 16  SER A CA  1 
ATOM   117  C  CA  B SER A 1 15  ? 25.930 -28.097 14.996 0.33 19.85  ? 16  SER A CA  1 
ATOM   118  C  CA  C SER A 1 15  ? 25.939 -28.073 15.011 0.29 18.91  ? 16  SER A CA  1 
ATOM   119  C  C   A SER A 1 15  ? 27.345 -28.671 15.024 0.38 23.20  ? 16  SER A C   1 
ATOM   120  C  C   B SER A 1 15  ? 27.341 -28.684 15.029 0.33 23.63  ? 16  SER A C   1 
ATOM   121  C  C   C SER A 1 15  ? 27.339 -28.700 15.042 0.29 23.35  ? 16  SER A C   1 
ATOM   122  O  O   A SER A 1 15  ? 28.067 -28.457 16.000 0.38 20.66  ? 16  SER A O   1 
ATOM   123  O  O   B SER A 1 15  ? 28.056 -28.484 16.013 0.33 21.50  ? 16  SER A O   1 
ATOM   124  O  O   C SER A 1 15  ? 28.047 -28.537 16.037 0.29 21.51  ? 16  SER A O   1 
ATOM   125  C  CB  A SER A 1 15  ? 24.881 -29.117 15.361 0.38 22.77  ? 16  SER A CB  1 
ATOM   126  C  CB  B SER A 1 15  ? 24.900 -29.172 15.338 0.33 23.95  ? 16  SER A CB  1 
ATOM   127  C  CB  C SER A 1 15  ? 24.868 -29.080 15.430 0.29 21.88  ? 16  SER A CB  1 
ATOM   128  O  OG  A SER A 1 15  ? 25.158 -29.671 16.635 0.38 25.36  ? 16  SER A OG  1 
ATOM   129  O  OG  B SER A 1 15  ? 23.593 -28.628 15.388 0.33 29.53  ? 16  SER A OG  1 
ATOM   130  O  OG  C SER A 1 15  ? 24.835 -30.205 14.568 0.29 23.63  ? 16  SER A OG  1 
ATOM   131  N  N   . ASP A 1 16  ? 27.748 -29.380 13.947 1.00 21.35  ? 17  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 16  ? 29.091 -29.991 13.830 1.00 22.35  ? 17  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 16  ? 30.153 -28.882 13.781 1.00 22.15  ? 17  ASP A C   1 
ATOM   134  O  O   . ASP A 1 16  ? 31.213 -29.027 14.387 1.00 21.77  ? 17  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 16  ? 29.186 -30.875 12.576 1.00 24.06  ? 17  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 16  ? 28.415 -32.191 12.647 1.00 34.63  ? 17  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 16  ? 27.859 -32.506 13.729 1.00 34.34  ? 17  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 16  ? 28.357 -32.900 11.617 1.00 35.36  ? 17  ASP A OD2 1 
ATOM   139  N  N   . VAL A 1 17  ? 29.867 -27.772 13.057 1.00 17.70  ? 18  VAL A N   1 
ATOM   140  C  CA  . VAL A 1 17  ? 30.808 -26.638 13.020 1.00 17.36  ? 18  VAL A CA  1 
ATOM   141  C  C   . VAL A 1 17  ? 31.001 -26.075 14.443 1.00 20.44  ? 18  VAL A C   1 
ATOM   142  O  O   . VAL A 1 17  ? 32.130 -25.875 14.889 1.00 19.37  ? 18  VAL A O   1 
ATOM   143  C  CB  . VAL A 1 17  ? 30.330 -25.527 12.041 1.00 19.17  ? 18  VAL A CB  1 
ATOM   144  C  CG1 . VAL A 1 17  ? 31.105 -24.221 12.263 1.00 19.36  ? 18  VAL A CG1 1 
ATOM   145  C  CG2 . VAL A 1 17  ? 30.429 -25.999 10.587 1.00 18.59  ? 18  VAL A CG2 1 
ATOM   146  N  N   . LEU A 1 18  ? 29.899 -25.854 15.166 1.00 18.44  ? 19  LEU A N   1 
ATOM   147  C  CA  . LEU A 1 18  ? 30.001 -25.266 16.499 1.00 18.92  ? 19  LEU A CA  1 
ATOM   148  C  C   . LEU A 1 18  ? 30.749 -26.201 17.463 1.00 21.58  ? 19  LEU A C   1 
ATOM   149  O  O   . LEU A 1 18  ? 31.592 -25.729 18.244 1.00 19.66  ? 19  LEU A O   1 
ATOM   150  C  CB  . LEU A 1 18  ? 28.610 -24.904 17.038 1.00 19.84  ? 19  LEU A CB  1 
ATOM   151  C  CG  . LEU A 1 18  ? 28.634 -23.974 18.281 1.00 22.85  ? 19  LEU A CG  1 
ATOM   152  C  CD1 . LEU A 1 18  ? 29.174 -22.572 17.934 1.00 23.08  ? 19  LEU A CD1 1 
ATOM   153  C  CD2 . LEU A 1 18  ? 27.239 -23.865 18.875 1.00 27.01  ? 19  LEU A CD2 1 
ATOM   154  N  N   . LEU A 1 19  ? 30.474 -27.515 17.359 1.00 19.98  ? 20  LEU A N   1 
ATOM   155  C  CA  . LEU A 1 19  ? 31.144 -28.550 18.162 1.00 21.27  ? 20  LEU A CA  1 
ATOM   156  C  C   . LEU A 1 19  ? 32.658 -28.486 17.925 1.00 22.16  ? 20  LEU A C   1 
ATOM   157  O  O   . LEU A 1 19  ? 33.440 -28.476 18.893 1.00 21.25  ? 20  LEU A O   1 
ATOM   158  C  CB  . LEU A 1 19  ? 30.595 -29.941 17.799 1.00 23.36  ? 20  LEU A CB  1 
ATOM   159  C  CG  . LEU A 1 19  ? 31.167 -31.097 18.593 1.00 31.82  ? 20  LEU A CG  1 
ATOM   160  C  CD1 . LEU A 1 19  ? 30.690 -31.035 20.056 1.00 34.24  ? 20  LEU A CD1 1 
ATOM   161  C  CD2 . LEU A 1 19  ? 30.726 -32.421 17.981 1.00 36.50  ? 20  LEU A CD2 1 
ATOM   162  N  N   . ASN A 1 20  ? 33.072 -28.369 16.648 1.00 18.66  ? 21  ASN A N   1 
ATOM   163  C  CA  . ASN A 1 20  ? 34.493 -28.256 16.303 1.00 19.10  ? 21  ASN A CA  1 
ATOM   164  C  C   . ASN A 1 20  ? 35.125 -26.948 16.791 1.00 20.99  ? 21  ASN A C   1 
ATOM   165  O  O   . ASN A 1 20  ? 36.280 -26.954 17.220 1.00 20.06  ? 21  ASN A O   1 
ATOM   166  C  CB  . ASN A 1 20  ? 34.694 -28.478 14.818 1.00 20.70  ? 21  ASN A CB  1 
ATOM   167  C  CG  . ASN A 1 20  ? 34.630 -29.950 14.472 1.00 30.59  ? 21  ASN A CG  1 
ATOM   168  O  OD1 . ASN A 1 20  ? 34.786 -30.819 15.338 1.00 27.58  ? 21  ASN A OD1 1 
ATOM   169  N  ND2 . ASN A 1 20  ? 34.378 -30.271 13.210 1.00 23.01  ? 21  ASN A ND2 1 
ATOM   170  N  N   . LEU A 1 21  ? 34.378 -25.830 16.721 1.00 18.48  ? 22  LEU A N   1 
ATOM   171  C  CA  . LEU A 1 21  ? 34.862 -24.543 17.249 1.00 18.39  ? 22  LEU A CA  1 
ATOM   172  C  C   . LEU A 1 21  ? 35.067 -24.684 18.757 1.00 20.59  ? 22  LEU A C   1 
ATOM   173  O  O   . LEU A 1 21  ? 36.052 -24.170 19.301 1.00 18.76  ? 22  LEU A O   1 
ATOM   174  C  CB  . LEU A 1 21  ? 33.864 -23.400 16.936 1.00 17.91  ? 22  LEU A CB  1 
ATOM   175  C  CG  . LEU A 1 21  ? 33.778 -23.032 15.434 1.00 20.71  ? 22  LEU A CG  1 
ATOM   176  C  CD1 . LEU A 1 21  ? 32.687 -21.968 15.198 1.00 20.57  ? 22  LEU A CD1 1 
ATOM   177  C  CD2 . LEU A 1 21  ? 35.139 -22.555 14.878 1.00 23.77  ? 22  LEU A CD2 1 
ATOM   178  N  N   . ASN A 1 22  ? 34.130 -25.374 19.452 1.00 17.94  ? 23  ASN A N   1 
ATOM   179  C  CA  . ASN A 1 22  ? 34.318 -25.575 20.896 1.00 19.32  ? 23  ASN A CA  1 
ATOM   180  C  C   . ASN A 1 22  ? 35.553 -26.473 21.199 1.00 23.39  ? 23  ASN A C   1 
ATOM   181  O  O   . ASN A 1 22  ? 36.264 -26.228 22.176 1.00 23.29  ? 23  ASN A O   1 
ATOM   182  C  CB  . ASN A 1 22  ? 33.059 -26.125 21.546 1.00 21.07  ? 23  ASN A CB  1 
ATOM   183  C  CG  . ASN A 1 22  ? 33.092 -25.995 23.054 1.00 27.88  ? 23  ASN A CG  1 
ATOM   184  O  OD1 . ASN A 1 22  ? 33.597 -25.016 23.611 1.00 24.95  ? 23  ASN A OD1 1 
ATOM   185  N  ND2 . ASN A 1 22  ? 32.564 -26.984 23.723 1.00 28.40  ? 23  ASN A ND2 1 
ATOM   186  N  N   . ARG A 1 23  ? 35.828 -27.491 20.347 1.00 20.84  ? 24  ARG A N   1 
ATOM   187  C  CA  . ARG A 1 23  ? 37.020 -28.347 20.520 1.00 22.26  ? 24  ARG A CA  1 
ATOM   188  C  C   . ARG A 1 23  ? 38.294 -27.508 20.357 1.00 26.07  ? 24  ARG A C   1 
ATOM   189  O  O   . ARG A 1 23  ? 39.237 -27.679 21.121 1.00 25.95  ? 24  ARG A O   1 
ATOM   190  C  CB  . ARG A 1 23  ? 37.025 -29.486 19.494 1.00 20.83  ? 24  ARG A CB  1 
ATOM   191  C  CG  . ARG A 1 23  ? 36.036 -30.589 19.832 1.00 27.84  ? 24  ARG A CG  1 
ATOM   192  C  CD  . ARG A 1 23  ? 35.749 -31.450 18.611 1.00 30.92  ? 24  ARG A CD  1 
ATOM   193  N  NE  . ARG A 1 23  ? 34.910 -32.590 18.962 1.00 38.09  ? 24  ARG A NE  1 
ATOM   194  C  CZ  . ARG A 1 23  ? 34.406 -33.458 18.092 1.00 57.39  ? 24  ARG A CZ  1 
ATOM   195  N  NH1 . ARG A 1 23  ? 34.607 -33.297 16.786 1.00 43.38  ? 24  ARG A NH1 1 
ATOM   196  N  NH2 . ARG A 1 23  ? 33.686 -34.488 18.516 1.00 44.41  ? 24  ARG A NH2 1 
ATOM   197  N  N   . LEU A 1 24  ? 38.301 -26.563 19.397 1.00 22.47  ? 25  LEU A N   1 
ATOM   198  C  CA  . LEU A 1 24  ? 39.441 -25.661 19.227 1.00 21.34  ? 25  LEU A CA  1 
ATOM   199  C  C   . LEU A 1 24  ? 39.608 -24.784 20.473 1.00 24.86  ? 25  LEU A C   1 
ATOM   200  O  O   . LEU A 1 24  ? 40.738 -24.620 20.967 1.00 25.13  ? 25  LEU A O   1 
ATOM   201  C  CB  . LEU A 1 24  ? 39.257 -24.771 18.004 1.00 20.34  ? 25  LEU A CB  1 
ATOM   202  C  CG  . LEU A 1 24  ? 39.230 -25.472 16.622 1.00 24.08  ? 25  LEU A CG  1 
ATOM   203  C  CD1 . LEU A 1 24  ? 39.051 -24.427 15.510 1.00 24.07  ? 25  LEU A CD1 1 
ATOM   204  C  CD2 . LEU A 1 24  ? 40.512 -26.317 16.392 1.00 26.40  ? 25  LEU A CD2 1 
ATOM   205  N  N   . ARG A 1 25  ? 38.491 -24.250 21.004 1.00 21.28  ? 26  ARG A N   1 
ATOM   206  C  CA  . ARG A 1 25  ? 38.555 -23.448 22.238 1.00 22.00  ? 26  ARG A CA  1 
ATOM   207  C  C   . ARG A 1 25  ? 39.175 -24.273 23.411 1.00 26.72  ? 26  ARG A C   1 
ATOM   208  O  O   . ARG A 1 25  ? 40.065 -23.759 24.120 1.00 26.76  ? 26  ARG A O   1 
ATOM   209  C  CB  . ARG A 1 25  ? 37.153 -22.955 22.646 1.00 22.21  ? 26  ARG A CB  1 
ATOM   210  C  CG  . ARG A 1 25  ? 37.249 -22.052 23.889 1.00 26.10  ? 26  ARG A CG  1 
ATOM   211  C  CD  . ARG A 1 25  ? 35.928 -21.439 24.252 1.00 27.38  ? 26  ARG A CD  1 
ATOM   212  N  NE  . ARG A 1 25  ? 34.928 -22.436 24.633 1.00 27.93  ? 26  ARG A NE  1 
ATOM   213  C  CZ  . ARG A 1 25  ? 34.316 -22.475 25.812 1.00 39.89  ? 26  ARG A CZ  1 
ATOM   214  N  NH1 . ARG A 1 25  ? 34.668 -21.635 26.782 1.00 34.89  ? 26  ARG A NH1 1 
ATOM   215  N  NH2 . ARG A 1 25  ? 33.375 -23.378 26.045 1.00 29.59  ? 26  ARG A NH2 1 
ATOM   216  N  N   A SER A 1 26  ? 38.686 -25.505 23.613 0.40 25.12  ? 27  SER A N   1 
ATOM   217  N  N   B SER A 1 26  ? 38.691 -25.513 23.620 0.35 24.99  ? 27  SER A N   1 
ATOM   218  N  N   C SER A 1 26  ? 38.693 -25.518 23.612 0.25 24.56  ? 27  SER A N   1 
ATOM   219  C  CA  A SER A 1 26  ? 39.158 -26.422 24.658 0.40 26.78  ? 27  SER A CA  1 
ATOM   220  C  CA  B SER A 1 26  ? 39.160 -26.405 24.693 0.35 26.58  ? 27  SER A CA  1 
ATOM   221  C  CA  C SER A 1 26  ? 39.143 -26.444 24.665 0.25 25.95  ? 27  SER A CA  1 
ATOM   222  C  C   A SER A 1 26  ? 40.672 -26.596 24.591 0.40 31.74  ? 27  SER A C   1 
ATOM   223  C  C   B SER A 1 26  ? 40.657 -26.726 24.600 0.35 31.96  ? 27  SER A C   1 
ATOM   224  C  C   C SER A 1 26  ? 40.644 -26.747 24.591 0.25 31.59  ? 27  SER A C   1 
ATOM   225  O  O   A SER A 1 26  ? 41.351 -26.518 25.620 0.40 32.34  ? 27  SER A O   1 
ATOM   226  O  O   B SER A 1 26  ? 41.308 -26.903 25.633 0.35 32.83  ? 27  SER A O   1 
ATOM   227  O  O   C SER A 1 26  ? 41.279 -26.950 25.629 0.25 32.41  ? 27  SER A O   1 
ATOM   228  C  CB  A SER A 1 26  ? 38.503 -27.791 24.497 0.40 31.22  ? 27  SER A CB  1 
ATOM   229  C  CB  B SER A 1 26  ? 38.331 -27.686 24.742 0.35 30.60  ? 27  SER A CB  1 
ATOM   230  C  CB  C SER A 1 26  ? 38.343 -27.743 24.609 0.25 29.42  ? 27  SER A CB  1 
ATOM   231  O  OG  A SER A 1 26  ? 37.163 -27.811 24.954 0.40 39.14  ? 27  SER A OG  1 
ATOM   232  O  OG  B SER A 1 26  ? 38.586 -28.549 23.646 0.35 37.01  ? 27  SER A OG  1 
ATOM   233  O  OG  C SER A 1 26  ? 38.790 -28.688 25.569 0.25 36.18  ? 27  SER A OG  1 
ATOM   234  N  N   . ARG A 1 27  ? 41.198 -26.797 23.369 1.00 28.14  ? 28  ARG A N   1 
ATOM   235  C  CA  . ARG A 1 27  ? 42.625 -27.066 23.127 1.00 29.88  ? 28  ARG A CA  1 
ATOM   236  C  C   . ARG A 1 27  ? 43.447 -25.786 22.936 1.00 32.28  ? 28  ARG A C   1 
ATOM   237  O  O   . ARG A 1 27  ? 44.661 -25.852 22.700 1.00 33.06  ? 28  ARG A O   1 
ATOM   238  C  CB  . ARG A 1 27  ? 42.768 -28.040 21.958 1.00 32.78  ? 28  ARG A CB  1 
ATOM   239  C  CG  . ARG A 1 27  ? 41.993 -29.338 22.191 1.00 41.87  ? 28  ARG A CG  1 
ATOM   240  C  CD  . ARG A 1 27  ? 41.983 -30.215 20.968 1.00 49.15  ? 28  ARG A CD  1 
ATOM   241  N  NE  . ARG A 1 27  ? 43.317 -30.754 20.706 1.00 66.09  ? 28  ARG A NE  1 
ATOM   242  C  CZ  . ARG A 1 27  ? 43.833 -30.897 19.494 1.00 83.27  ? 28  ARG A CZ  1 
ATOM   243  N  NH1 . ARG A 1 27  ? 45.055 -31.387 19.340 1.00 73.59  ? 28  ARG A NH1 1 
ATOM   244  N  NH2 . ARG A 1 27  ? 43.136 -30.546 18.426 1.00 69.89  ? 28  ARG A NH2 1 
ATOM   245  N  N   . ASP A 1 28  ? 42.788 -24.627 23.085 1.00 26.30  ? 29  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 28  ? 43.366 -23.284 22.950 1.00 27.37  ? 29  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 28  ? 43.977 -23.061 21.542 1.00 31.60  ? 29  ASP A C   1 
ATOM   248  O  O   . ASP A 1 28  ? 45.024 -22.422 21.393 1.00 32.51  ? 29  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 28  ? 44.391 -23.002 24.084 1.00 30.58  ? 29  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 28  ? 44.703 -21.537 24.263 1.00 38.42  ? 29  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 28  ? 43.785 -20.706 24.065 1.00 37.45  ? 29  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 28  ? 45.863 -21.215 24.597 1.00 43.34  ? 29  ASP A OD2 1 
ATOM   253  N  N   . ILE A 1 29  ? 43.318 -23.599 20.518 1.00 25.82  ? 30  ILE A N   1 
ATOM   254  C  CA  . ILE A 1 29  ? 43.805 -23.499 19.139 1.00 24.96  ? 30  ILE A CA  1 
ATOM   255  C  C   . ILE A 1 29  ? 43.203 -22.311 18.429 1.00 28.00  ? 30  ILE A C   1 
ATOM   256  O  O   . ILE A 1 29  ? 41.967 -22.192 18.340 1.00 25.04  ? 30  ILE A O   1 
ATOM   257  C  CB  . ILE A 1 29  ? 43.586 -24.821 18.351 1.00 27.78  ? 30  ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 29  ? 44.383 -25.990 18.996 1.00 29.53  ? 30  ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 29  ? 43.959 -24.650 16.857 1.00 26.97  ? 30  ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 29  ? 43.912 -27.380 18.484 1.00 32.22  ? 30  ILE A CD1 1 
ATOM   261  N  N   A LEU A 1 30  ? 44.081 -21.421 17.918 0.54 25.71  ? 31  LEU A N   1 
ATOM   262  N  N   B LEU A 1 30  ? 44.085 -21.423 17.920 0.46 26.46  ? 31  LEU A N   1 
ATOM   263  C  CA  A LEU A 1 30  ? 43.726 -20.216 17.160 0.54 25.02  ? 31  LEU A CA  1 
ATOM   264  C  CA  B LEU A 1 30  ? 43.755 -20.210 17.167 0.46 26.22  ? 31  LEU A CA  1 
ATOM   265  C  C   A LEU A 1 30  ? 42.835 -19.222 17.919 0.54 27.33  ? 31  LEU A C   1 
ATOM   266  C  C   B LEU A 1 30  ? 42.847 -19.221 17.917 0.46 28.05  ? 31  LEU A C   1 
ATOM   267  O  O   A LEU A 1 30  ? 42.213 -18.362 17.290 0.54 25.28  ? 31  LEU A O   1 
ATOM   268  O  O   B LEU A 1 30  ? 42.226 -18.364 17.283 0.46 26.19  ? 31  LEU A O   1 
ATOM   269  C  CB  A LEU A 1 30  ? 43.118 -20.556 15.790 0.54 24.81  ? 31  LEU A CB  1 
ATOM   270  C  CB  B LEU A 1 30  ? 43.194 -20.531 15.782 0.46 26.40  ? 31  LEU A CB  1 
ATOM   271  C  CG  A LEU A 1 30  ? 44.074 -21.171 14.733 0.54 30.21  ? 31  LEU A CG  1 
ATOM   272  C  CG  B LEU A 1 30  ? 44.247 -20.457 14.677 0.46 32.58  ? 31  LEU A CG  1 
ATOM   273  C  CD1 A LEU A 1 30  ? 43.527 -20.956 13.370 0.54 28.31  ? 31  LEU A CD1 1 
ATOM   274  C  CD1 B LEU A 1 30  ? 44.561 -21.830 14.117 0.46 33.32  ? 31  LEU A CD1 1 
ATOM   275  C  CD2 A LEU A 1 30  ? 45.467 -20.553 14.778 0.54 34.31  ? 31  LEU A CD2 1 
ATOM   276  C  CD2 B LEU A 1 30  ? 43.819 -19.507 13.594 0.46 34.33  ? 31  LEU A CD2 1 
ATOM   277  N  N   . THR A 1 31  ? 42.840 -19.282 19.263 1.00 24.97  ? 32  THR A N   1 
ATOM   278  C  CA  . THR A 1 31  ? 42.127 -18.298 20.101 1.00 24.30  ? 32  THR A CA  1 
ATOM   279  C  C   . THR A 1 31  ? 42.945 -17.013 19.907 1.00 29.82  ? 32  THR A C   1 
ATOM   280  O  O   . THR A 1 31  ? 44.179 -17.071 19.772 1.00 29.87  ? 32  THR A O   1 
ATOM   281  C  CB  . THR A 1 31  ? 42.058 -18.717 21.573 1.00 30.21  ? 32  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 31  ? 43.358 -19.095 21.987 1.00 31.76  ? 32  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 31  ? 41.061 -19.863 21.815 1.00 26.84  ? 32  THR A CG2 1 
ATOM   284  N  N   . ASP A 1 32  ? 42.265 -15.885 19.745 1.00 26.33  ? 33  ASP A N   1 
ATOM   285  C  CA  . ASP A 1 32  ? 42.934 -14.638 19.387 1.00 26.53  ? 33  ASP A CA  1 
ATOM   286  C  C   . ASP A 1 32  ? 42.599 -13.481 20.297 1.00 28.24  ? 33  ASP A C   1 
ATOM   287  O  O   . ASP A 1 32  ? 42.950 -12.333 20.004 1.00 28.50  ? 33  ASP A O   1 
ATOM   288  C  CB  . ASP A 1 32  ? 42.612 -14.299 17.920 1.00 27.52  ? 33  ASP A CB  1 
ATOM   289  C  CG  . ASP A 1 32  ? 41.122 -14.281 17.591 1.00 34.76  ? 33  ASP A CG  1 
ATOM   290  O  OD1 . ASP A 1 32  ? 40.295 -14.350 18.537 1.00 30.22  ? 33  ASP A OD1 1 
ATOM   291  O  OD2 . ASP A 1 32  ? 40.785 -14.218 16.399 1.00 42.86  ? 33  ASP A OD2 1 
ATOM   292  N  N   . VAL A 1 33  ? 41.936 -13.771 21.417 1.00 22.87  ? 34  VAL A N   1 
ATOM   293  C  CA  . VAL A 1 33  ? 41.623 -12.722 22.400 1.00 22.98  ? 34  VAL A CA  1 
ATOM   294  C  C   . VAL A 1 33  ? 41.453 -13.320 23.790 1.00 26.43  ? 34  VAL A C   1 
ATOM   295  O  O   . VAL A 1 33  ? 41.062 -14.490 23.929 1.00 25.52  ? 34  VAL A O   1 
ATOM   296  C  CB  . VAL A 1 33  ? 40.353 -11.882 21.971 1.00 25.71  ? 34  VAL A CB  1 
ATOM   297  C  CG1 . VAL A 1 33  ? 39.043 -12.666 22.133 1.00 23.78  ? 34  VAL A CG1 1 
ATOM   298  C  CG2 . VAL A 1 33  ? 40.270 -10.536 22.722 1.00 25.61  ? 34  VAL A CG2 1 
ATOM   299  N  N   A VAL A 1 34  ? 41.742 -12.505 24.816 0.53 23.52  ? 35  VAL A N   1 
ATOM   300  N  N   B VAL A 1 34  ? 41.746 -12.516 24.817 0.47 23.86  ? 35  VAL A N   1 
ATOM   301  C  CA  A VAL A 1 34  ? 41.512 -12.827 26.219 0.53 23.02  ? 35  VAL A CA  1 
ATOM   302  C  CA  B VAL A 1 34  ? 41.478 -12.881 26.197 0.47 23.57  ? 35  VAL A CA  1 
ATOM   303  C  C   A VAL A 1 34  ? 40.451 -11.836 26.702 0.53 26.25  ? 35  VAL A C   1 
ATOM   304  C  C   B VAL A 1 34  ? 40.492 -11.854 26.770 0.47 26.66  ? 35  VAL A C   1 
ATOM   305  O  O   A VAL A 1 34  ? 40.606 -10.628 26.505 0.53 26.34  ? 35  VAL A O   1 
ATOM   306  O  O   B VAL A 1 34  ? 40.709 -10.647 26.650 0.47 26.83  ? 35  VAL A O   1 
ATOM   307  C  CB  A VAL A 1 34  ? 42.804 -12.734 27.082 0.53 27.32  ? 35  VAL A CB  1 
ATOM   308  C  CB  B VAL A 1 34  ? 42.730 -13.157 27.077 0.47 28.24  ? 35  VAL A CB  1 
ATOM   309  C  CG1 A VAL A 1 34  ? 42.513 -12.988 28.565 0.53 27.51  ? 35  VAL A CG1 1 
ATOM   310  C  CG1 B VAL A 1 34  ? 43.581 -11.912 27.288 0.47 28.97  ? 35  VAL A CG1 1 
ATOM   311  C  CG2 A VAL A 1 34  ? 43.872 -13.689 26.583 0.53 27.66  ? 35  VAL A CG2 1 
ATOM   312  C  CG2 B VAL A 1 34  ? 42.335 -13.777 28.414 0.47 28.41  ? 35  VAL A CG2 1 
ATOM   313  N  N   . ILE A 1 35  ? 39.379 -12.344 27.316 1.00 22.34  ? 36  ILE A N   1 
ATOM   314  C  CA  . ILE A 1 35  ? 38.333 -11.518 27.922 1.00 22.32  ? 36  ILE A CA  1 
ATOM   315  C  C   . ILE A 1 35  ? 38.623 -11.553 29.427 1.00 26.94  ? 36  ILE A C   1 
ATOM   316  O  O   . ILE A 1 35  ? 38.646 -12.635 30.034 1.00 26.02  ? 36  ILE A O   1 
ATOM   317  C  CB  . ILE A 1 35  ? 36.894 -12.000 27.595 1.00 23.83  ? 36  ILE A CB  1 
ATOM   318  C  CG1 . ILE A 1 35  ? 36.648 -12.168 26.068 1.00 23.13  ? 36  ILE A CG1 1 
ATOM   319  C  CG2 . ILE A 1 35  ? 35.855 -11.092 28.231 1.00 25.16  ? 36  ILE A CG2 1 
ATOM   320  C  CD1 . ILE A 1 35  ? 36.972 -10.896 25.163 1.00 22.09  ? 36  ILE A CD1 1 
ATOM   321  N  N   . VAL A 1 36  ? 38.859 -10.372 30.013 1.00 24.40  ? 37  VAL A N   1 
ATOM   322  C  CA  . VAL A 1 36  ? 39.179 -10.227 31.437 1.00 25.13  ? 37  VAL A CA  1 
ATOM   323  C  C   . VAL A 1 36  ? 37.915 -9.789  32.172 1.00 29.29  ? 37  VAL A C   1 
ATOM   324  O  O   . VAL A 1 36  ? 37.315 -8.760  31.828 1.00 27.85  ? 37  VAL A O   1 
ATOM   325  C  CB  . VAL A 1 36  ? 40.368 -9.246  31.665 1.00 29.48  ? 37  VAL A CB  1 
ATOM   326  C  CG1 . VAL A 1 36  ? 40.675 -9.066  33.153 1.00 30.50  ? 37  VAL A CG1 1 
ATOM   327  C  CG2 . VAL A 1 36  ? 41.617 -9.716  30.928 1.00 30.35  ? 37  VAL A CG2 1 
ATOM   328  N  N   . VAL A 1 37  ? 37.517 -10.575 33.194 1.00 26.12  ? 38  VAL A N   1 
ATOM   329  C  CA  . VAL A 1 37  ? 36.316 -10.342 33.997 1.00 26.84  ? 38  VAL A CA  1 
ATOM   330  C  C   . VAL A 1 37  ? 36.781 -10.403 35.443 1.00 32.08  ? 38  VAL A C   1 
ATOM   331  O  O   . VAL A 1 37  ? 37.019 -11.493 35.964 1.00 29.93  ? 38  VAL A O   1 
ATOM   332  C  CB  . VAL A 1 37  ? 35.188 -11.356 33.664 1.00 30.52  ? 38  VAL A CB  1 
ATOM   333  C  CG1 . VAL A 1 37  ? 33.872 -10.937 34.313 1.00 30.38  ? 38  VAL A CG1 1 
ATOM   334  C  CG2 . VAL A 1 37  ? 35.015 -11.517 32.151 1.00 29.52  ? 38  VAL A CG2 1 
ATOM   335  N  N   A SER A 1 38  ? 36.680 -9.289  36.202 0.50 31.11  ? 39  SER A N   1 
ATOM   336  N  N   B SER A 1 38  ? 37.297 -9.210  35.838 0.50 29.11  ? 39  SER A N   1 
ATOM   337  C  CA  A SER A 1 38  ? 37.048 -9.277  37.636 0.50 32.77  ? 39  SER A CA  1 
ATOM   338  C  CA  B SER A 1 38  ? 37.967 -8.841  37.073 0.50 29.61  ? 39  SER A CA  1 
ATOM   339  C  C   A SER A 1 38  ? 38.311 -10.152 37.936 0.50 37.20  ? 39  SER A C   1 
ATOM   340  C  C   B SER A 1 38  ? 39.257 -9.656  37.223 0.50 32.48  ? 39  SER A C   1 
ATOM   341  O  O   A SER A 1 38  ? 38.274 -11.008 38.824 0.50 36.67  ? 39  SER A O   1 
ATOM   342  O  O   B SER A 1 38  ? 40.170 -9.438  36.424 0.50 31.08  ? 39  SER A O   1 
ATOM   343  C  CB  A SER A 1 38  ? 35.865 -9.708  38.511 0.50 38.35  ? 39  SER A CB  1 
ATOM   344  C  CB  B SER A 1 38  ? 37.018 -8.897  38.264 0.50 33.84  ? 39  SER A CB  1 
ATOM   345  O  OG  A SER A 1 38  ? 34.809 -8.758  38.535 0.50 49.60  ? 39  SER A OG  1 
ATOM   346  O  OG  B SER A 1 38  ? 36.063 -7.858  38.112 0.50 39.20  ? 39  SER A OG  1 
ATOM   347  N  N   A ARG A 1 39  ? 39.395 -9.969  37.133 0.50 33.92  ? 40  ARG A N   1 
ATOM   348  N  N   B ARG A 1 39  ? 39.340 -10.616 38.164 0.50 29.58  ? 40  ARG A N   1 
ATOM   349  C  CA  A ARG A 1 39  ? 40.677 -10.701 37.210 0.50 34.72  ? 40  ARG A CA  1 
ATOM   350  C  CA  B ARG A 1 39  ? 40.572 -11.400 38.273 0.50 30.49  ? 40  ARG A CA  1 
ATOM   351  C  C   A ARG A 1 39  ? 40.542 -12.239 36.970 0.50 37.32  ? 40  ARG A C   1 
ATOM   352  C  C   B ARG A 1 39  ? 40.691 -12.417 37.098 0.50 34.89  ? 40  ARG A C   1 
ATOM   353  O  O   A ARG A 1 39  ? 41.308 -13.052 37.526 0.50 38.04  ? 40  ARG A O   1 
ATOM   354  O  O   B ARG A 1 39  ? 41.704 -12.425 36.382 0.50 34.97  ? 40  ARG A O   1 
ATOM   355  C  CB  A ARG A 1 39  ? 41.451 -10.404 38.510 0.50 37.09  ? 40  ARG A CB  1 
ATOM   356  C  CB  B ARG A 1 39  ? 40.724 -12.040 39.675 0.50 31.60  ? 40  ARG A CB  1 
ATOM   357  C  CG  A ARG A 1 39  ? 41.959 -8.973  38.651 0.50 48.15  ? 40  ARG A CG  1 
ATOM   358  C  CG  B ARG A 1 39  ? 41.004 -11.000 40.775 0.50 39.45  ? 40  ARG A CG  1 
ATOM   359  C  CD  A ARG A 1 39  ? 43.053 -8.913  39.700 0.50 54.57  ? 40  ARG A CD  1 
ATOM   360  C  CD  B ARG A 1 39  ? 41.381 -11.606 42.121 0.50 39.14  ? 40  ARG A CD  1 
ATOM   361  N  NE  A ARG A 1 39  ? 43.412 -7.542  40.068 0.50 61.63  ? 40  ARG A NE  1 
ATOM   362  N  NE  B ARG A 1 39  ? 41.531 -10.589 43.165 0.50 39.78  ? 40  ARG A NE  1 
ATOM   363  C  CZ  A ARG A 1 39  ? 42.852 -6.858  41.061 0.50 74.56  ? 40  ARG A CZ  1 
ATOM   364  C  CZ  B ARG A 1 39  ? 42.685 -10.031 43.528 0.50 53.71  ? 40  ARG A CZ  1 
ATOM   365  N  NH1 A ARG A 1 39  ? 41.878 -7.399  41.785 0.50 60.03  ? 40  ARG A NH1 1 
ATOM   366  N  NH1 B ARG A 1 39  ? 43.815 -10.369 42.921 0.50 40.97  ? 40  ARG A NH1 1 
ATOM   367  N  NH2 A ARG A 1 39  ? 43.251 -5.622  41.330 0.50 61.73  ? 40  ARG A NH2 1 
ATOM   368  N  NH2 B ARG A 1 39  ? 42.715 -9.126  44.494 0.50 45.54  ? 40  ARG A NH2 1 
ATOM   369  N  N   A GLU A 1 40  ? 39.564 -12.622 36.144 0.50 30.72  ? 41  GLU A N   1 
ATOM   370  N  N   B GLU A 1 40  ? 39.607 -13.161 36.832 0.50 29.31  ? 41  GLU A N   1 
ATOM   371  C  CA  A GLU A 1 40  ? 39.348 -13.992 35.678 0.50 29.79  ? 41  GLU A CA  1 
ATOM   372  C  CA  B GLU A 1 40  ? 39.544 -14.226 35.823 0.50 28.04  ? 41  GLU A CA  1 
ATOM   373  C  C   A GLU A 1 40  ? 39.480 -13.872 34.166 0.50 31.09  ? 41  GLU A C   1 
ATOM   374  C  C   B GLU A 1 40  ? 39.787 -13.780 34.368 0.50 29.69  ? 41  GLU A C   1 
ATOM   375  O  O   A GLU A 1 40  ? 38.883 -12.972 33.567 0.50 28.26  ? 41  GLU A O   1 
ATOM   376  O  O   B GLU A 1 40  ? 39.484 -12.652 33.987 0.50 26.37  ? 41  GLU A O   1 
ATOM   377  C  CB  A GLU A 1 40  ? 37.984 -14.557 36.112 0.50 31.12  ? 41  GLU A CB  1 
ATOM   378  C  CB  B GLU A 1 40  ? 38.215 -15.004 35.924 0.50 29.16  ? 41  GLU A CB  1 
ATOM   379  C  CG  A GLU A 1 40  ? 37.891 -14.786 37.614 0.50 45.43  ? 41  GLU A CG  1 
ATOM   380  C  CG  B GLU A 1 40  ? 37.724 -15.182 37.356 0.50 44.48  ? 41  GLU A CG  1 
ATOM   381  C  CD  A GLU A 1 40  ? 37.833 -16.234 38.061 0.50 78.94  ? 41  GLU A CD  1 
ATOM   382  C  CD  B GLU A 1 40  ? 37.893 -16.535 38.019 0.50 79.97  ? 41  GLU A CD  1 
ATOM   383  O  OE1 A GLU A 1 40  ? 36.804 -16.625 38.659 0.50 80.66  ? 41  GLU A OE1 1 
ATOM   384  O  OE1 B GLU A 1 40  ? 38.931 -17.199 37.793 0.50 81.33  ? 41  GLU A OE1 1 
ATOM   385  O  OE2 A GLU A 1 40  ? 38.815 -16.975 37.825 0.50 78.67  ? 41  GLU A OE2 1 
ATOM   386  O  OE2 B GLU A 1 40  ? 36.986 -16.919 38.793 0.50 80.83  ? 41  GLU A OE2 1 
ATOM   387  N  N   . GLN A 1 41  ? 40.323 -14.715 33.559 1.00 27.30  ? 42  GLN A N   1 
ATOM   388  C  CA  . GLN A 1 41  ? 40.650 -14.576 32.149 1.00 26.37  ? 42  GLN A CA  1 
ATOM   389  C  C   . GLN A 1 41  ? 40.028 -15.688 31.342 1.00 29.53  ? 42  GLN A C   1 
ATOM   390  O  O   . GLN A 1 41  ? 40.104 -16.844 31.751 1.00 30.15  ? 42  GLN A O   1 
ATOM   391  C  CB  . GLN A 1 41  ? 42.182 -14.603 31.987 1.00 29.09  ? 42  GLN A CB  1 
ATOM   392  C  CG  . GLN A 1 41  ? 42.858 -13.356 32.551 1.00 42.99  ? 42  GLN A CG  1 
ATOM   393  C  CD  . GLN A 1 41  ? 44.327 -13.237 32.222 1.00 62.78  ? 42  GLN A CD  1 
ATOM   394  O  OE1 . GLN A 1 41  ? 44.908 -14.015 31.451 1.00 55.53  ? 42  GLN A OE1 1 
ATOM   395  N  NE2 . GLN A 1 41  ? 44.959 -12.235 32.808 1.00 66.78  ? 42  GLN A NE2 1 
ATOM   396  N  N   . PHE A 1 42  ? 39.423 -15.342 30.193 1.00 22.98  ? 43  PHE A N   1 
ATOM   397  C  CA  . PHE A 1 42  ? 38.789 -16.338 29.313 1.00 23.34  ? 43  PHE A CA  1 
ATOM   398  C  C   . PHE A 1 42  ? 39.316 -16.181 27.909 1.00 27.70  ? 43  PHE A C   1 
ATOM   399  O  O   . PHE A 1 42  ? 39.149 -15.114 27.318 1.00 27.74  ? 43  PHE A O   1 
ATOM   400  C  CB  . PHE A 1 42  ? 37.258 -16.162 29.316 1.00 24.56  ? 43  PHE A CB  1 
ATOM   401  C  CG  . PHE A 1 42  ? 36.638 -16.256 30.690 1.00 26.39  ? 43  PHE A CG  1 
ATOM   402  C  CD1 . PHE A 1 42  ? 36.523 -15.127 31.502 1.00 28.50  ? 43  PHE A CD1 1 
ATOM   403  C  CD2 . PHE A 1 42  ? 36.152 -17.470 31.169 1.00 28.82  ? 43  PHE A CD2 1 
ATOM   404  C  CE1 . PHE A 1 42  ? 35.959 -15.217 32.777 1.00 30.69  ? 43  PHE A CE1 1 
ATOM   405  C  CE2 . PHE A 1 42  ? 35.577 -17.557 32.439 1.00 31.89  ? 43  PHE A CE2 1 
ATOM   406  C  CZ  . PHE A 1 42  ? 35.485 -16.432 33.238 1.00 29.98  ? 43  PHE A CZ  1 
ATOM   407  N  N   . ARG A 1 43  ? 39.918 -17.244 27.350 1.00 24.31  ? 44  ARG A N   1 
ATOM   408  C  CA  . ARG A 1 43  ? 40.433 -17.201 25.978 1.00 22.77  ? 44  ARG A CA  1 
ATOM   409  C  C   . ARG A 1 43  ? 39.300 -17.592 25.019 1.00 25.98  ? 44  ARG A C   1 
ATOM   410  O  O   . ARG A 1 43  ? 38.495 -18.488 25.321 1.00 24.37  ? 44  ARG A O   1 
ATOM   411  C  CB  . ARG A 1 43  ? 41.656 -18.129 25.803 1.00 24.84  ? 44  ARG A CB  1 
ATOM   412  C  CG  . ARG A 1 43  ? 42.899 -17.698 26.628 1.00 33.07  ? 44  ARG A CG  1 
ATOM   413  C  CD  . ARG A 1 43  ? 44.223 -18.089 25.961 1.00 43.34  ? 44  ARG A CD  1 
ATOM   414  N  NE  . ARG A 1 43  ? 44.243 -17.654 24.556 1.00 53.49  ? 44  ARG A NE  1 
ATOM   415  C  CZ  . ARG A 1 43  ? 44.851 -16.566 24.093 1.00 65.42  ? 44  ARG A CZ  1 
ATOM   416  N  NH1 . ARG A 1 43  ? 45.590 -15.817 24.898 1.00 56.94  ? 44  ARG A NH1 1 
ATOM   417  N  NH2 . ARG A 1 43  ? 44.767 -16.248 22.809 1.00 48.09  ? 44  ARG A NH2 1 
ATOM   418  N  N   . ALA A 1 44  ? 39.218 -16.921 23.871 1.00 22.32  ? 45  ALA A N   1 
ATOM   419  C  CA  . ALA A 1 44  ? 38.142 -17.229 22.909 1.00 22.61  ? 45  ALA A CA  1 
ATOM   420  C  C   . ALA A 1 44  ? 38.542 -16.824 21.497 1.00 23.69  ? 45  ALA A C   1 
ATOM   421  O  O   . ALA A 1 44  ? 39.638 -16.292 21.276 1.00 22.68  ? 45  ALA A O   1 
ATOM   422  C  CB  . ALA A 1 44  ? 36.857 -16.494 23.312 1.00 23.82  ? 45  ALA A CB  1 
ATOM   423  N  N   . HIS A 1 45  ? 37.633 -17.063 20.541 1.00 20.07  ? 46  HIS A N   1 
ATOM   424  C  CA  . HIS A 1 45  ? 37.812 -16.642 19.159 1.00 19.28  ? 46  HIS A CA  1 
ATOM   425  C  C   . HIS A 1 45  ? 36.916 -15.404 18.966 1.00 22.70  ? 46  HIS A C   1 
ATOM   426  O  O   . HIS A 1 45  ? 35.701 -15.462 19.229 1.00 21.59  ? 46  HIS A O   1 
ATOM   427  C  CB  . HIS A 1 45  ? 37.374 -17.763 18.193 1.00 18.49  ? 46  HIS A CB  1 
ATOM   428  C  CG  . HIS A 1 45  ? 38.112 -19.060 18.403 1.00 21.90  ? 46  HIS A CG  1 
ATOM   429  N  ND1 . HIS A 1 45  ? 37.573 -20.081 19.170 1.00 23.99  ? 46  HIS A ND1 1 
ATOM   430  C  CD2 . HIS A 1 45  ? 39.348 -19.435 17.986 1.00 22.75  ? 46  HIS A CD2 1 
ATOM   431  C  CE1 . HIS A 1 45  ? 38.486 -21.047 19.190 1.00 23.07  ? 46  HIS A CE1 1 
ATOM   432  N  NE2 . HIS A 1 45  ? 39.568 -20.710 18.477 1.00 22.98  ? 46  HIS A NE2 1 
ATOM   433  N  N   . LYS A 1 46  ? 37.511 -14.303 18.516 1.00 21.04  ? 47  LYS A N   1 
ATOM   434  C  CA  . LYS A 1 46  ? 36.767 -13.061 18.243 1.00 20.68  ? 47  LYS A CA  1 
ATOM   435  C  C   . LYS A 1 46  ? 35.538 -13.309 17.372 1.00 22.65  ? 47  LYS A C   1 
ATOM   436  O  O   . LYS A 1 46  ? 34.474 -12.787 17.693 1.00 21.01  ? 47  LYS A O   1 
ATOM   437  C  CB  . LYS A 1 46  ? 37.662 -12.044 17.528 1.00 22.85  ? 47  LYS A CB  1 
ATOM   438  C  CG  . LYS A 1 46  ? 38.710 -11.449 18.451 1.00 22.83  ? 47  LYS A CG  1 
ATOM   439  C  CD  . LYS A 1 46  ? 39.607 -10.477 17.676 1.00 22.69  ? 47  LYS A CD  1 
ATOM   440  C  CE  . LYS A 1 46  ? 40.776 -10.098 18.542 1.00 27.89  ? 47  LYS A CE  1 
ATOM   441  N  NZ  . LYS A 1 46  ? 41.673 -9.156  17.825 1.00 29.78  ? 47  LYS A NZ  1 
ATOM   442  N  N   . THR A 1 47  ? 35.670 -14.121 16.302 1.00 19.64  ? 48  THR A N   1 
ATOM   443  C  CA  . THR A 1 47  ? 34.520 -14.333 15.400 1.00 19.51  ? 48  THR A CA  1 
ATOM   444  C  C   . THR A 1 47  ? 33.344 -15.004 16.068 1.00 20.70  ? 48  THR A C   1 
ATOM   445  O  O   . THR A 1 47  ? 32.202 -14.632 15.781 1.00 19.32  ? 48  THR A O   1 
ATOM   446  C  CB  . THR A 1 47  ? 34.920 -15.053 14.122 1.00 26.58  ? 48  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 47  ? 35.530 -16.273 14.486 1.00 26.38  ? 48  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 47  ? 35.819 -14.191 13.230 1.00 29.21  ? 48  THR A CG2 1 
ATOM   449  N  N   . VAL A 1 48  ? 33.602 -15.967 16.953 1.00 17.60  ? 49  VAL A N   1 
ATOM   450  C  CA  . VAL A 1 48  ? 32.506 -16.660 17.655 1.00 18.12  ? 49  VAL A CA  1 
ATOM   451  C  C   . VAL A 1 48  ? 31.840 -15.661 18.617 1.00 20.13  ? 49  VAL A C   1 
ATOM   452  O  O   . VAL A 1 48  ? 30.606 -15.615 18.719 1.00 18.09  ? 49  VAL A O   1 
ATOM   453  C  CB  . VAL A 1 48  ? 33.004 -17.930 18.409 1.00 20.72  ? 49  VAL A CB  1 
ATOM   454  C  CG1 . VAL A 1 48  ? 31.882 -18.537 19.268 1.00 21.16  ? 49  VAL A CG1 1 
ATOM   455  C  CG2 . VAL A 1 48  ? 33.518 -18.983 17.411 1.00 20.15  ? 49  VAL A CG2 1 
ATOM   456  N  N   . LEU A 1 49  ? 32.660 -14.885 19.353 1.00 17.50  ? 50  LEU A N   1 
ATOM   457  C  CA  . LEU A 1 49  ? 32.098 -13.872 20.275 1.00 17.93  ? 50  LEU A CA  1 
ATOM   458  C  C   . LEU A 1 49  ? 31.196 -12.882 19.507 1.00 20.53  ? 50  LEU A C   1 
ATOM   459  O  O   . LEU A 1 49  ? 30.090 -12.574 19.953 1.00 19.14  ? 50  LEU A O   1 
ATOM   460  C  CB  . LEU A 1 49  ? 33.244 -13.084 20.963 1.00 17.96  ? 50  LEU A CB  1 
ATOM   461  C  CG  . LEU A 1 49  ? 34.192 -13.874 21.904 1.00 20.54  ? 50  LEU A CG  1 
ATOM   462  C  CD1 . LEU A 1 49  ? 35.229 -12.914 22.534 1.00 21.44  ? 50  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A 1 49  ? 33.401 -14.604 23.004 1.00 23.23  ? 50  LEU A CD2 1 
ATOM   464  N  N   . MET A 1 50  ? 31.654 -12.415 18.344 1.00 17.73  ? 51  MET A N   1 
ATOM   465  C  CA  . MET A 1 50  ? 30.880 -11.489 17.510 1.00 18.68  ? 51  MET A CA  1 
ATOM   466  C  C   . MET A 1 50  ? 29.587 -12.128 17.019 1.00 21.67  ? 51  MET A C   1 
ATOM   467  O  O   . MET A 1 50  ? 28.549 -11.469 17.031 1.00 22.03  ? 51  MET A O   1 
ATOM   468  C  CB  . MET A 1 50  ? 31.691 -11.009 16.302 1.00 20.30  ? 51  MET A CB  1 
ATOM   469  C  CG  . MET A 1 50  ? 32.914 -10.200 16.678 1.00 23.00  ? 51  MET A CG  1 
ATOM   470  S  SD  . MET A 1 50  ? 33.937 -10.093 15.207 1.00 26.97  ? 51  MET A SD  1 
ATOM   471  C  CE  . MET A 1 50  ? 33.159 -8.742  14.412 1.00 23.91  ? 51  MET A CE  1 
ATOM   472  N  N   . ALA A 1 51  ? 29.643 -13.414 16.628 1.00 19.21  ? 52  ALA A N   1 
ATOM   473  C  CA  . ALA A 1 51  ? 28.479 -14.145 16.105 1.00 19.53  ? 52  ALA A CA  1 
ATOM   474  C  C   . ALA A 1 51  ? 27.373 -14.318 17.173 1.00 22.13  ? 52  ALA A C   1 
ATOM   475  O  O   . ALA A 1 51  ? 26.211 -14.512 16.824 1.00 23.30  ? 52  ALA A O   1 
ATOM   476  C  CB  . ALA A 1 51  ? 28.915 -15.519 15.573 1.00 19.64  ? 52  ALA A CB  1 
ATOM   477  N  N   . CYS A 1 52  ? 27.753 -14.262 18.464 1.00 19.11  ? 53  CYS A N   1 
ATOM   478  C  CA  . CYS A 1 52  ? 26.852 -14.498 19.591 1.00 19.38  ? 53  CYS A CA  1 
ATOM   479  C  C   . CYS A 1 52  ? 26.400 -13.273 20.366 1.00 22.60  ? 53  CYS A C   1 
ATOM   480  O  O   . CYS A 1 52  ? 25.432 -13.385 21.131 1.00 22.65  ? 53  CYS A O   1 
ATOM   481  C  CB  . CYS A 1 52  ? 27.515 -15.487 20.544 1.00 19.38  ? 53  CYS A CB  1 
ATOM   482  S  SG  . CYS A 1 52  ? 27.809 -17.115 19.822 1.00 22.76  ? 53  CYS A SG  1 
ATOM   483  N  N   . SER A 1 53  ? 27.149 -12.173 20.284 1.00 19.66  ? 54  SER A N   1 
ATOM   484  C  CA  . SER A 1 53  ? 26.941 -11.024 21.161 1.00 18.21  ? 54  SER A CA  1 
ATOM   485  C  C   . SER A 1 53  ? 26.985 -9.702  20.419 1.00 23.63  ? 54  SER A C   1 
ATOM   486  O  O   . SER A 1 53  ? 27.958 -9.426  19.711 1.00 21.65  ? 54  SER A O   1 
ATOM   487  C  CB  . SER A 1 53  ? 28.034 -11.082 22.231 1.00 19.79  ? 54  SER A CB  1 
ATOM   488  O  OG  . SER A 1 53  ? 28.441 -9.834  22.778 1.00 24.09  ? 54  SER A OG  1 
ATOM   489  N  N   . GLY A 1 54  ? 25.955 -8.879  20.618 1.00 22.27  ? 55  GLY A N   1 
ATOM   490  C  CA  . GLY A 1 54  ? 25.901 -7.542  20.029 1.00 22.60  ? 55  GLY A CA  1 
ATOM   491  C  C   . GLY A 1 54  ? 27.023 -6.662  20.541 1.00 25.75  ? 55  GLY A C   1 
ATOM   492  O  O   . GLY A 1 54  ? 27.559 -5.836  19.788 1.00 25.75  ? 55  GLY A O   1 
ATOM   493  N  N   . LEU A 1 55  ? 27.428 -6.864  21.822 1.00 23.14  ? 56  LEU A N   1 
ATOM   494  C  CA  . LEU A 1 55  ? 28.531 -6.088  22.403 1.00 23.12  ? 56  LEU A CA  1 
ATOM   495  C  C   . LEU A 1 55  ? 29.851 -6.433  21.699 1.00 24.29  ? 56  LEU A C   1 
ATOM   496  O  O   . LEU A 1 55  ? 30.543 -5.513  21.246 1.00 24.00  ? 56  LEU A O   1 
ATOM   497  C  CB  . LEU A 1 55  ? 28.659 -6.294  23.928 1.00 23.11  ? 56  LEU A CB  1 
ATOM   498  C  CG  . LEU A 1 55  ? 29.693 -5.377  24.618 1.00 27.78  ? 56  LEU A CG  1 
ATOM   499  C  CD1 . LEU A 1 55  ? 29.237 -3.896  24.614 1.00 28.55  ? 56  LEU A CD1 1 
ATOM   500  C  CD2 . LEU A 1 55  ? 29.981 -5.846  26.030 1.00 27.41  ? 56  LEU A CD2 1 
ATOM   501  N  N   . PHE A 1 56  ? 30.179 -7.742  21.585 1.00 20.61  ? 57  PHE A N   1 
ATOM   502  C  CA  . PHE A 1 56  ? 31.434 -8.142  20.915 1.00 20.05  ? 57  PHE A CA  1 
ATOM   503  C  C   . PHE A 1 56  ? 31.422 -7.801  19.442 1.00 23.93  ? 57  PHE A C   1 
ATOM   504  O  O   . PHE A 1 56  ? 32.465 -7.429  18.907 1.00 22.45  ? 57  PHE A O   1 
ATOM   505  C  CB  . PHE A 1 56  ? 31.794 -9.597  21.175 1.00 20.98  ? 57  PHE A CB  1 
ATOM   506  C  CG  . PHE A 1 56  ? 32.211 -9.828  22.613 1.00 21.51  ? 57  PHE A CG  1 
ATOM   507  C  CD1 . PHE A 1 56  ? 33.291 -9.135  23.165 1.00 23.15  ? 57  PHE A CD1 1 
ATOM   508  C  CD2 . PHE A 1 56  ? 31.554 -10.773 23.403 1.00 22.08  ? 57  PHE A CD2 1 
ATOM   509  C  CE1 . PHE A 1 56  ? 33.674 -9.345  24.503 1.00 24.20  ? 57  PHE A CE1 1 
ATOM   510  C  CE2 . PHE A 1 56  ? 31.968 -11.015 24.724 1.00 24.98  ? 57  PHE A CE2 1 
ATOM   511  C  CZ  . PHE A 1 56  ? 33.008 -10.280 25.272 1.00 23.43  ? 57  PHE A CZ  1 
ATOM   512  N  N   . TYR A 1 57  ? 30.243 -7.877  18.795 1.00 22.03  ? 58  TYR A N   1 
ATOM   513  C  CA  . TYR A 1 57  ? 30.129 -7.468  17.391 1.00 23.36  ? 58  TYR A CA  1 
ATOM   514  C  C   . TYR A 1 57  ? 30.564 -5.994  17.236 1.00 27.51  ? 58  TYR A C   1 
ATOM   515  O  O   . TYR A 1 57  ? 31.366 -5.684  16.349 1.00 25.69  ? 58  TYR A O   1 
ATOM   516  C  CB  . TYR A 1 57  ? 28.691 -7.682  16.898 1.00 25.45  ? 58  TYR A CB  1 
ATOM   517  C  CG  . TYR A 1 57  ? 28.471 -7.166  15.497 1.00 28.67  ? 58  TYR A CG  1 
ATOM   518  C  CD1 . TYR A 1 57  ? 29.021 -7.820  14.397 1.00 29.74  ? 58  TYR A CD1 1 
ATOM   519  C  CD2 . TYR A 1 57  ? 27.716 -6.021  15.270 1.00 33.47  ? 58  TYR A CD2 1 
ATOM   520  C  CE1 . TYR A 1 57  ? 28.821 -7.342  13.100 1.00 32.00  ? 58  TYR A CE1 1 
ATOM   521  C  CE2 . TYR A 1 57  ? 27.512 -5.536  13.984 1.00 36.72  ? 58  TYR A CE2 1 
ATOM   522  C  CZ  . TYR A 1 57  ? 28.058 -6.204  12.905 1.00 43.75  ? 58  TYR A CZ  1 
ATOM   523  O  OH  . TYR A 1 57  ? 27.825 -5.709  11.656 1.00 50.83  ? 58  TYR A OH  1 
ATOM   524  N  N   A SER A 1 58  ? 30.031 -5.098  18.091 0.52 24.96  ? 59  SER A N   1 
ATOM   525  N  N   B SER A 1 58  ? 30.029 -5.105  18.095 0.48 25.19  ? 59  SER A N   1 
ATOM   526  C  CA  A SER A 1 58  ? 30.355 -3.669  18.089 0.52 25.98  ? 59  SER A CA  1 
ATOM   527  C  CA  B SER A 1 58  ? 30.346 -3.679  18.113 0.48 26.30  ? 59  SER A CA  1 
ATOM   528  C  C   A SER A 1 58  ? 31.839 -3.424  18.405 0.52 30.35  ? 59  SER A C   1 
ATOM   529  C  C   B SER A 1 58  ? 31.841 -3.457  18.381 0.48 30.33  ? 59  SER A C   1 
ATOM   530  O  O   A SER A 1 58  ? 32.473 -2.613  17.735 0.52 31.58  ? 59  SER A O   1 
ATOM   531  O  O   B SER A 1 58  ? 32.479 -2.695  17.658 0.48 31.31  ? 59  SER A O   1 
ATOM   532  C  CB  A SER A 1 58  ? 29.452 -2.924  19.068 0.52 28.75  ? 59  SER A CB  1 
ATOM   533  C  CB  B SER A 1 58  ? 29.506 -2.970  19.173 0.48 29.59  ? 59  SER A CB  1 
ATOM   534  O  OG  A SER A 1 58  ? 28.107 -2.954  18.615 0.52 30.53  ? 59  SER A OG  1 
ATOM   535  O  OG  B SER A 1 58  ? 29.787 -1.581  19.185 0.48 35.48  ? 59  SER A OG  1 
ATOM   536  N  N   . ILE A 1 59  ? 32.397 -4.154  19.394 1.00 26.34  ? 60  ILE A N   1 
ATOM   537  C  CA  . ILE A 1 59  ? 33.807 -4.039  19.803 1.00 25.36  ? 60  ILE A CA  1 
ATOM   538  C  C   . ILE A 1 59  ? 34.750 -4.420  18.675 1.00 28.07  ? 60  ILE A C   1 
ATOM   539  O  O   . ILE A 1 59  ? 35.644 -3.631  18.334 1.00 28.63  ? 60  ILE A O   1 
ATOM   540  C  CB  . ILE A 1 59  ? 34.128 -4.876  21.109 1.00 26.72  ? 60  ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 59  ? 33.415 -4.300  22.356 1.00 27.16  ? 60  ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 59  ? 35.664 -4.978  21.363 1.00 24.93  ? 60  ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 59  ? 33.418 -5.282  23.589 1.00 29.52  ? 60  ILE A CD1 1 
ATOM   544  N  N   . PHE A 1 60  ? 34.559 -5.613  18.087 1.00 23.04  ? 61  PHE A N   1 
ATOM   545  C  CA  . PHE A 1 60  ? 35.533 -6.072  17.106 1.00 24.05  ? 61  PHE A CA  1 
ATOM   546  C  C   . PHE A 1 60  ? 35.307 -5.531  15.689 1.00 28.23  ? 61  PHE A C   1 
ATOM   547  O  O   . PHE A 1 60  ? 36.157 -5.773  14.833 1.00 28.83  ? 61  PHE A O   1 
ATOM   548  C  CB  . PHE A 1 60  ? 35.682 -7.602  17.146 1.00 24.50  ? 61  PHE A CB  1 
ATOM   549  C  CG  . PHE A 1 60  ? 36.114 -8.102  18.516 1.00 24.61  ? 61  PHE A CG  1 
ATOM   550  C  CD1 . PHE A 1 60  ? 37.315 -7.676  19.088 1.00 27.79  ? 61  PHE A CD1 1 
ATOM   551  C  CD2 . PHE A 1 60  ? 35.308 -8.972  19.239 1.00 25.47  ? 61  PHE A CD2 1 
ATOM   552  C  CE1 . PHE A 1 60  ? 37.705 -8.129  20.356 1.00 28.55  ? 61  PHE A CE1 1 
ATOM   553  C  CE2 . PHE A 1 60  ? 35.711 -9.450  20.495 1.00 28.06  ? 61  PHE A CE2 1 
ATOM   554  C  CZ  . PHE A 1 60  ? 36.892 -9.009  21.057 1.00 26.28  ? 61  PHE A CZ  1 
ATOM   555  N  N   . THR A 1 61  ? 34.245 -4.740  15.454 1.00 25.59  ? 62  THR A N   1 
ATOM   556  C  CA  . THR A 1 61  ? 34.082 -4.044  14.164 1.00 26.69  ? 62  THR A CA  1 
ATOM   557  C  C   . THR A 1 61  ? 34.628 -2.616  14.300 1.00 33.61  ? 62  THR A C   1 
ATOM   558  O  O   . THR A 1 61  ? 34.687 -1.865  13.315 1.00 33.37  ? 62  THR A O   1 
ATOM   559  C  CB  . THR A 1 61  ? 32.657 -4.076  13.612 1.00 33.50  ? 62  THR A CB  1 
ATOM   560  O  OG1 . THR A 1 61  ? 31.763 -3.568  14.593 1.00 30.05  ? 62  THR A OG1 1 
ATOM   561  C  CG2 . THR A 1 61  ? 32.232 -5.467  13.117 1.00 29.13  ? 62  THR A CG2 1 
ATOM   562  N  N   . ASP A 1 62  ? 35.075 -2.250  15.512 1.00 30.28  ? 63  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 62  ? 35.674 -0.936  15.718 1.00 31.56  ? 63  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 62  ? 37.098 -0.996  15.175 1.00 37.02  ? 63  ASP A C   1 
ATOM   565  O  O   . ASP A 1 62  ? 37.848 -1.892  15.553 1.00 34.89  ? 63  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 62  ? 35.662 -0.542  17.199 1.00 32.72  ? 63  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 62  ? 36.410 0.751   17.415 1.00 44.39  ? 63  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 62  ? 35.801 1.820   17.228 1.00 49.27  ? 63  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 62  ? 37.629 0.691   17.694 1.00 44.29  ? 63  ASP A OD2 1 
ATOM   570  N  N   . GLN A 1 63  ? 37.483 -0.019  14.323 1.00 38.09  ? 64  GLN A N   1 
ATOM   571  C  CA  . GLN A 1 63  ? 38.791 0.010   13.672 1.00 39.58  ? 64  GLN A CA  1 
ATOM   572  C  C   . GLN A 1 63  ? 39.983 -0.051  14.634 1.00 44.26  ? 64  GLN A C   1 
ATOM   573  O  O   . GLN A 1 63  ? 41.022 -0.567  14.229 1.00 46.55  ? 64  GLN A O   1 
ATOM   574  C  CB  . GLN A 1 63  ? 38.919 1.204   12.712 1.00 43.24  ? 64  GLN A CB  1 
ATOM   575  C  CG  . GLN A 1 63  ? 38.066 1.066   11.453 1.00 62.92  ? 64  GLN A CG  1 
ATOM   576  N  N   . LEU A 1 64  ? 39.861 0.477   15.881 1.00 37.76  ? 65  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 64  ? 40.964 0.402   16.848 1.00 36.48  ? 65  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 64  ? 40.875 -0.840  17.711 1.00 39.49  ? 65  LEU A C   1 
ATOM   579  O  O   . LEU A 1 64  ? 41.898 -1.434  18.033 1.00 41.55  ? 65  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 64  ? 40.981 1.616   17.795 1.00 37.23  ? 65  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 64  ? 41.618 2.886   17.277 1.00 44.10  ? 65  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 64  ? 41.493 3.979   18.303 1.00 44.93  ? 65  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 64  ? 43.092 2.687   16.927 1.00 48.53  ? 65  LEU A CD2 1 
ATOM   584  N  N   . LYS A 1 65  ? 39.672 -1.175  18.184 1.00 32.45  ? 66  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 65  ? 39.513 -2.295  19.110 1.00 30.50  ? 66  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 65  ? 39.644 -3.652  18.448 1.00 35.33  ? 66  LYS A C   1 
ATOM   587  O  O   . LYS A 1 65  ? 40.010 -4.602  19.132 1.00 34.02  ? 66  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 65  ? 38.191 -2.210  19.891 1.00 31.26  ? 66  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 65  ? 38.075 -0.980  20.779 1.00 31.54  ? 66  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 65  ? 36.792 -1.065  21.599 1.00 29.63  ? 66  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 65  ? 36.497 0.251   22.293 1.00 33.96  ? 66  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 65  ? 35.916 1.260   21.376 1.00 35.43  ? 66  LYS A NZ  1 
ATOM   593  N  N   . CYS A 1 66  ? 39.368 -3.742  17.127 1.00 35.12  ? 67  CYS A N   1 
ATOM   594  C  CA  . CYS A 1 66  ? 39.470 -5.000  16.363 1.00 35.11  ? 67  CYS A CA  1 
ATOM   595  C  C   . CYS A 1 66  ? 40.866 -5.633  16.499 1.00 40.16  ? 67  CYS A C   1 
ATOM   596  O  O   . CYS A 1 66  ? 41.002 -6.848  16.332 1.00 40.35  ? 67  CYS A O   1 
ATOM   597  C  CB  . CYS A 1 66  ? 39.101 -4.780  14.897 1.00 36.54  ? 67  CYS A CB  1 
ATOM   598  S  SG  . CYS A 1 66  ? 40.276 -3.751  13.968 1.00 42.64  ? 67  CYS A SG  1 
ATOM   599  N  N   . ASN A 1 67  ? 41.891 -4.795  16.792 1.00 36.19  ? 68  ASN A N   1 
ATOM   600  C  CA  . ASN A 1 67  ? 43.291 -5.200  16.908 1.00 37.14  ? 68  ASN A CA  1 
ATOM   601  C  C   . ASN A 1 67  ? 43.776 -5.491  18.334 1.00 40.22  ? 68  ASN A C   1 
ATOM   602  O  O   . ASN A 1 67  ? 44.942 -5.855  18.526 1.00 40.20  ? 68  ASN A O   1 
ATOM   603  C  CB  . ASN A 1 67  ? 44.198 -4.173  16.221 1.00 39.74  ? 68  ASN A CB  1 
ATOM   604  C  CG  . ASN A 1 67  ? 43.980 -4.141  14.721 1.00 54.15  ? 68  ASN A CG  1 
ATOM   605  O  OD1 . ASN A 1 67  ? 43.936 -3.075  14.107 1.00 55.36  ? 68  ASN A OD1 1 
ATOM   606  N  ND2 . ASN A 1 67  ? 43.794 -5.306  14.095 1.00 44.22  ? 68  ASN A ND2 1 
ATOM   607  N  N   . LEU A 1 68  ? 42.890 -5.374  19.322 1.00 36.57  ? 69  LEU A N   1 
ATOM   608  C  CA  . LEU A 1 68  ? 43.267 -5.644  20.704 1.00 35.65  ? 69  LEU A CA  1 
ATOM   609  C  C   . LEU A 1 68  ? 43.239 -7.146  20.975 1.00 36.62  ? 69  LEU A C   1 
ATOM   610  O  O   . LEU A 1 68  ? 42.337 -7.827  20.478 1.00 34.44  ? 69  LEU A O   1 
ATOM   611  C  CB  . LEU A 1 68  ? 42.284 -4.938  21.658 1.00 35.89  ? 69  LEU A CB  1 
ATOM   612  C  CG  . LEU A 1 68  ? 42.302 -3.402  21.635 1.00 40.71  ? 69  LEU A CG  1 
ATOM   613  C  CD1 . LEU A 1 68  ? 41.227 -2.848  22.540 1.00 40.58  ? 69  LEU A CD1 1 
ATOM   614  C  CD2 . LEU A 1 68  ? 43.685 -2.838  22.039 1.00 42.42  ? 69  LEU A CD2 1 
ATOM   615  N  N   . SER A 1 69  ? 44.212 -7.631  21.780 1.00 32.82  ? 70  SER A N   1 
ATOM   616  C  CA  A SER A 1 69  ? 44.346 -9.033  22.190 0.42 31.93  ? 70  SER A CA  1 
ATOM   617  C  CA  B SER A 1 69  ? 44.295 -9.043  22.163 0.58 32.26  ? 70  SER A CA  1 
ATOM   618  C  C   . SER A 1 69  ? 43.702 -9.241  23.567 1.00 32.89  ? 70  SER A C   1 
ATOM   619  O  O   . SER A 1 69  ? 43.512 -10.373 24.003 1.00 28.87  ? 70  SER A O   1 
ATOM   620  C  CB  A SER A 1 69  ? 45.821 -9.428  22.247 0.42 36.45  ? 70  SER A CB  1 
ATOM   621  C  CB  B SER A 1 69  ? 45.738 -9.539  22.104 0.58 37.36  ? 70  SER A CB  1 
ATOM   622  O  OG  A SER A 1 69  ? 46.422 -9.349  20.966 0.42 41.72  ? 70  SER A OG  1 
ATOM   623  O  OG  B SER A 1 69  ? 46.559 -8.824  23.010 0.58 43.99  ? 70  SER A OG  1 
ATOM   624  N  N   . VAL A 1 70  ? 43.413 -8.134  24.277 1.00 29.75  ? 71  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 70  ? 42.806 -8.163  25.613 1.00 28.80  ? 71  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 70  ? 41.632 -7.186  25.646 1.00 30.43  ? 71  VAL A C   1 
ATOM   627  O  O   . VAL A 1 70  ? 41.787 -6.010  25.266 1.00 30.18  ? 71  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 70  ? 43.845 -7.814  26.735 1.00 34.11  ? 71  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 70  ? 43.201 -7.820  28.127 1.00 34.09  ? 71  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 70  ? 45.054 -8.750  26.699 1.00 35.07  ? 71  VAL A CG2 1 
ATOM   631  N  N   . ILE A 1 71  ? 40.482 -7.658  26.154 1.00 24.71  ? 72  ILE A N   1 
ATOM   632  C  CA  . ILE A 1 71  ? 39.276 -6.853  26.371 1.00 23.88  ? 72  ILE A CA  1 
ATOM   633  C  C   . ILE A 1 71  ? 38.883 -6.967  27.844 1.00 28.07  ? 72  ILE A C   1 
ATOM   634  O  O   . ILE A 1 71  ? 38.683 -8.074  28.347 1.00 27.59  ? 72  ILE A O   1 
ATOM   635  C  CB  . ILE A 1 71  ? 38.102 -7.219  25.401 1.00 25.22  ? 72  ILE A CB  1 
ATOM   636  C  CG1 . ILE A 1 71  ? 38.503 -7.079  23.898 1.00 26.14  ? 72  ILE A CG1 1 
ATOM   637  C  CG2 . ILE A 1 71  ? 36.819 -6.425  25.727 1.00 26.21  ? 72  ILE A CG2 1 
ATOM   638  C  CD1 . ILE A 1 71  ? 38.883 -5.644  23.400 1.00 30.82  ? 72  ILE A CD1 1 
ATOM   639  N  N   . ASN A 1 72  ? 38.755 -5.821  28.530 1.00 25.33  ? 73  ASN A N   1 
ATOM   640  C  CA  . ASN A 1 72  ? 38.360 -5.801  29.930 1.00 26.10  ? 73  ASN A CA  1 
ATOM   641  C  C   . ASN A 1 72  ? 36.885 -5.471  30.043 1.00 28.11  ? 73  ASN A C   1 
ATOM   642  O  O   . ASN A 1 72  ? 36.456 -4.393  29.612 1.00 26.08  ? 73  ASN A O   1 
ATOM   643  C  CB  . ASN A 1 72  ? 39.181 -4.758  30.720 1.00 28.32  ? 73  ASN A CB  1 
ATOM   644  C  CG  . ASN A 1 72  ? 40.661 -4.959  30.652 1.00 46.69  ? 73  ASN A CG  1 
ATOM   645  O  OD1 . ASN A 1 72  ? 41.184 -5.983  31.062 1.00 35.77  ? 73  ASN A OD1 1 
ATOM   646  N  ND2 . ASN A 1 72  ? 41.377 -3.974  30.152 1.00 43.18  ? 73  ASN A ND2 1 
ATOM   647  N  N   . LEU A 1 73  ? 36.114 -6.359  30.668 1.00 23.12  ? 74  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 73  ? 34.694 -6.103  30.857 1.00 22.57  ? 74  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 73  ? 34.460 -5.201  32.064 1.00 26.18  ? 74  LEU A C   1 
ATOM   650  O  O   . LEU A 1 73  ? 35.344 -5.041  32.917 1.00 27.15  ? 74  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 73  ? 33.873 -7.400  30.993 1.00 22.56  ? 74  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 73  ? 33.944 -8.413  29.815 1.00 25.65  ? 74  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 73  ? 32.820 -9.472  29.947 1.00 25.27  ? 74  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 73  ? 33.931 -7.714  28.434 1.00 27.07  ? 74  LEU A CD2 1 
ATOM   655  N  N   . ASP A 1 74  ? 33.262 -4.631  32.130 1.00 22.81  ? 75  ASP A N   1 
ATOM   656  C  CA  . ASP A 1 74  ? 32.839 -3.726  33.208 1.00 24.83  ? 75  ASP A CA  1 
ATOM   657  C  C   . ASP A 1 74  ? 33.000 -4.476  34.551 1.00 30.42  ? 75  ASP A C   1 
ATOM   658  O  O   . ASP A 1 74  ? 32.637 -5.651  34.627 1.00 28.93  ? 75  ASP A O   1 
ATOM   659  C  CB  . ASP A 1 74  ? 31.374 -3.317  32.982 1.00 26.91  ? 75  ASP A CB  1 
ATOM   660  C  CG  . ASP A 1 74  ? 30.840 -2.289  33.969 1.00 36.09  ? 75  ASP A CG  1 
ATOM   661  O  OD1 . ASP A 1 74  ? 30.715 -2.621  35.167 1.00 37.54  ? 75  ASP A OD1 1 
ATOM   662  O  OD2 . ASP A 1 74  ? 30.508 -1.174  33.537 1.00 39.33  ? 75  ASP A OD2 1 
ATOM   663  N  N   . PRO A 1 75  ? 33.583 -3.835  35.589 1.00 31.99  ? 76  PRO A N   1 
ATOM   664  C  CA  . PRO A 1 75  ? 33.797 -4.549  36.868 1.00 32.24  ? 76  PRO A CA  1 
ATOM   665  C  C   . PRO A 1 75  ? 32.557 -5.109  37.538 1.00 34.83  ? 76  PRO A C   1 
ATOM   666  O  O   . PRO A 1 75  ? 32.701 -5.955  38.414 1.00 35.84  ? 76  PRO A O   1 
ATOM   667  C  CB  . PRO A 1 75  ? 34.487 -3.512  37.759 1.00 34.83  ? 76  PRO A CB  1 
ATOM   668  C  CG  . PRO A 1 75  ? 34.187 -2.180  37.125 1.00 40.44  ? 76  PRO A CG  1 
ATOM   669  C  CD  . PRO A 1 75  ? 34.100 -2.451  35.651 1.00 34.48  ? 76  PRO A CD  1 
ATOM   670  N  N   . GLU A 1 76  ? 31.352 -4.672  37.139 1.00 31.32  ? 77  GLU A N   1 
ATOM   671  C  CA  . GLU A 1 76  ? 30.117 -5.196  37.728 1.00 32.58  ? 77  GLU A CA  1 
ATOM   672  C  C   . GLU A 1 76  ? 29.799 -6.599  37.179 1.00 32.65  ? 77  GLU A C   1 
ATOM   673  O  O   . GLU A 1 76  ? 28.955 -7.297  37.746 1.00 32.07  ? 77  GLU A O   1 
ATOM   674  C  CB  . GLU A 1 76  ? 28.934 -4.240  37.471 1.00 35.40  ? 77  GLU A CB  1 
ATOM   675  C  CG  . GLU A 1 76  ? 28.886 -3.047  38.414 1.00 55.26  ? 77  GLU A CG  1 
ATOM   676  C  CD  . GLU A 1 76  ? 28.362 -3.364  39.802 1.00 88.50  ? 77  GLU A CD  1 
ATOM   677  O  OE1 . GLU A 1 76  ? 27.136 -3.577  39.941 1.00 89.92  ? 77  GLU A OE1 1 
ATOM   678  O  OE2 . GLU A 1 76  ? 29.181 -3.409  40.749 1.00 88.14  ? 77  GLU A OE2 1 
ATOM   679  N  N   . ILE A 1 77  ? 30.476 -7.008  36.088 1.00 27.22  ? 78  ILE A N   1 
ATOM   680  C  CA  . ILE A 1 77  ? 30.229 -8.320  35.481 1.00 26.34  ? 78  ILE A CA  1 
ATOM   681  C  C   . ILE A 1 77  ? 30.824 -9.432  36.322 1.00 30.66  ? 78  ILE A C   1 
ATOM   682  O  O   . ILE A 1 77  ? 31.995 -9.390  36.690 1.00 29.54  ? 78  ILE A O   1 
ATOM   683  C  CB  . ILE A 1 77  ? 30.670 -8.379  33.996 1.00 28.12  ? 78  ILE A CB  1 
ATOM   684  C  CG1 . ILE A 1 77  ? 29.934 -7.297  33.145 1.00 29.38  ? 78  ILE A CG1 1 
ATOM   685  C  CG2 . ILE A 1 77  ? 30.481 -9.805  33.419 1.00 23.47  ? 78  ILE A CG2 1 
ATOM   686  C  CD1 . ILE A 1 77  ? 28.318 -7.308  33.213 1.00 34.78  ? 78  ILE A CD1 1 
ATOM   687  N  N   . ASN A 1 78  ? 30.002 -10.426 36.600 1.00 29.88  ? 79  ASN A N   1 
ATOM   688  C  CA  . ASN A 1 78  ? 30.340 -11.597 37.383 1.00 30.73  ? 79  ASN A CA  1 
ATOM   689  C  C   . ASN A 1 78  ? 31.067 -12.640 36.511 1.00 30.62  ? 79  ASN A C   1 
ATOM   690  O  O   . ASN A 1 78  ? 30.532 -13.035 35.478 1.00 28.56  ? 79  ASN A O   1 
ATOM   691  C  CB  . ASN A 1 78  ? 29.039 -12.165 37.987 1.00 33.92  ? 79  ASN A CB  1 
ATOM   692  C  CG  . ASN A 1 78  ? 29.213 -13.466 38.720 1.00 49.69  ? 79  ASN A CG  1 
ATOM   693  O  OD1 . ASN A 1 78  ? 28.840 -14.525 38.216 1.00 36.61  ? 79  ASN A OD1 1 
ATOM   694  N  ND2 . ASN A 1 78  ? 29.780 -13.411 39.921 1.00 44.01  ? 79  ASN A ND2 1 
ATOM   695  N  N   . PRO A 1 79  ? 32.263 -13.135 36.924 1.00 27.96  ? 80  PRO A N   1 
ATOM   696  C  CA  . PRO A 1 79  ? 32.972 -14.139 36.101 1.00 27.65  ? 80  PRO A CA  1 
ATOM   697  C  C   . PRO A 1 79  ? 32.191 -15.434 35.857 1.00 30.44  ? 80  PRO A C   1 
ATOM   698  O  O   . PRO A 1 79  ? 32.271 -15.986 34.757 1.00 29.76  ? 80  PRO A O   1 
ATOM   699  C  CB  . PRO A 1 79  ? 34.247 -14.408 36.904 1.00 30.84  ? 80  PRO A CB  1 
ATOM   700  C  CG  . PRO A 1 79  ? 34.434 -13.177 37.741 1.00 35.57  ? 80  PRO A CG  1 
ATOM   701  C  CD  . PRO A 1 79  ? 33.058 -12.764 38.114 1.00 31.37  ? 80  PRO A CD  1 
ATOM   702  N  N   . GLU A 1 80  ? 31.430 -15.918 36.861 1.00 27.63  ? 81  GLU A N   1 
ATOM   703  C  CA  . GLU A 1 80  ? 30.662 -17.156 36.654 1.00 27.54  ? 81  GLU A CA  1 
ATOM   704  C  C   . GLU A 1 80  ? 29.579 -16.941 35.584 1.00 28.72  ? 81  GLU A C   1 
ATOM   705  O  O   . GLU A 1 80  ? 29.435 -17.786 34.708 1.00 26.49  ? 81  GLU A O   1 
ATOM   706  C  CB  . GLU A 1 80  ? 30.054 -17.672 37.965 1.00 30.16  ? 81  GLU A CB  1 
ATOM   707  C  CG  . GLU A 1 80  ? 29.402 -19.038 37.773 1.00 40.44  ? 81  GLU A CG  1 
ATOM   708  C  CD  . GLU A 1 80  ? 28.573 -19.583 38.922 1.00 66.67  ? 81  GLU A CD  1 
ATOM   709  O  OE1 . GLU A 1 80  ? 28.546 -20.823 39.086 1.00 64.41  ? 81  GLU A OE1 1 
ATOM   710  O  OE2 . GLU A 1 80  ? 27.938 -18.782 39.648 1.00 63.36  ? 81  GLU A OE2 1 
ATOM   711  N  N   . GLY A 1 81  ? 28.869 -15.803 35.651 1.00 27.31  ? 82  GLY A N   1 
ATOM   712  C  CA  . GLY A 1 81  ? 27.857 -15.434 34.664 1.00 26.74  ? 82  GLY A CA  1 
ATOM   713  C  C   . GLY A 1 81  ? 28.466 -15.399 33.271 1.00 27.51  ? 82  GLY A C   1 
ATOM   714  O  O   . GLY A 1 81  ? 27.899 -15.942 32.308 1.00 25.07  ? 82  GLY A O   1 
ATOM   715  N  N   . PHE A 1 82  ? 29.663 -14.800 33.162 1.00 23.61  ? 83  PHE A N   1 
ATOM   716  C  CA  . PHE A 1 82  ? 30.347 -14.752 31.873 1.00 22.13  ? 83  PHE A CA  1 
ATOM   717  C  C   . PHE A 1 82  ? 30.709 -16.148 31.398 1.00 23.92  ? 83  PHE A C   1 
ATOM   718  O  O   . PHE A 1 82  ? 30.510 -16.452 30.233 1.00 22.78  ? 83  PHE A O   1 
ATOM   719  C  CB  . PHE A 1 82  ? 31.618 -13.886 31.916 1.00 23.15  ? 83  PHE A CB  1 
ATOM   720  C  CG  . PHE A 1 82  ? 32.212 -13.762 30.529 1.00 23.26  ? 83  PHE A CG  1 
ATOM   721  C  CD1 . PHE A 1 82  ? 31.655 -12.894 29.590 1.00 25.71  ? 83  PHE A CD1 1 
ATOM   722  C  CD2 . PHE A 1 82  ? 33.285 -14.555 30.140 1.00 23.54  ? 83  PHE A CD2 1 
ATOM   723  C  CE1 . PHE A 1 82  ? 32.151 -12.833 28.285 1.00 25.85  ? 83  PHE A CE1 1 
ATOM   724  C  CE2 . PHE A 1 82  ? 33.793 -14.481 28.837 1.00 25.11  ? 83  PHE A CE2 1 
ATOM   725  C  CZ  . PHE A 1 82  ? 33.207 -13.640 27.915 1.00 23.86  ? 83  PHE A CZ  1 
ATOM   726  N  N   . CYS A 1 83  ? 31.294 -16.970 32.279 1.00 23.94  ? 84  CYS A N   1 
ATOM   727  C  CA  . CYS A 1 83  ? 31.710 -18.340 31.945 1.00 25.75  ? 84  CYS A CA  1 
ATOM   728  C  C   . CYS A 1 83  ? 30.514 -19.152 31.378 1.00 27.00  ? 84  CYS A C   1 
ATOM   729  O  O   . CYS A 1 83  ? 30.650 -19.843 30.356 1.00 25.42  ? 84  CYS A O   1 
ATOM   730  C  CB  . CYS A 1 83  ? 32.310 -19.016 33.175 1.00 29.80  ? 84  CYS A CB  1 
ATOM   731  S  SG  . CYS A 1 83  ? 32.955 -20.679 32.846 1.00 35.77  ? 84  CYS A SG  1 
ATOM   732  N  N   . ILE A 1 84  ? 29.344 -19.053 32.048 1.00 23.64  ? 85  ILE A N   1 
ATOM   733  C  CA  . ILE A 1 84  ? 28.115 -19.757 31.632 1.00 22.48  ? 85  ILE A CA  1 
ATOM   734  C  C   . ILE A 1 84  ? 27.702 -19.307 30.218 1.00 23.54  ? 85  ILE A C   1 
ATOM   735  O  O   . ILE A 1 84  ? 27.338 -20.144 29.359 1.00 21.32  ? 85  ILE A O   1 
ATOM   736  C  CB  . ILE A 1 84  ? 26.993 -19.531 32.692 1.00 25.59  ? 85  ILE A CB  1 
ATOM   737  C  CG1 . ILE A 1 84  ? 27.271 -20.371 33.979 1.00 26.46  ? 85  ILE A CG1 1 
ATOM   738  C  CG2 . ILE A 1 84  ? 25.575 -19.822 32.115 1.00 25.10  ? 85  ILE A CG2 1 
ATOM   739  C  CD1 . ILE A 1 84  ? 26.554 -19.804 35.203 1.00 33.06  ? 85  ILE A CD1 1 
ATOM   740  N  N   . LEU A 1 85  ? 27.783 -18.008 29.971 1.00 21.51  ? 86  LEU A N   1 
ATOM   741  C  CA  . LEU A 1 85  ? 27.430 -17.453 28.660 1.00 21.46  ? 86  LEU A CA  1 
ATOM   742  C  C   . LEU A 1 85  ? 28.434 -17.808 27.588 1.00 23.54  ? 86  LEU A C   1 
ATOM   743  O  O   . LEU A 1 85  ? 28.026 -18.077 26.459 1.00 21.48  ? 86  LEU A O   1 
ATOM   744  C  CB  . LEU A 1 85  ? 27.176 -15.960 28.729 1.00 22.23  ? 86  LEU A CB  1 
ATOM   745  C  CG  . LEU A 1 85  ? 25.880 -15.580 29.487 1.00 27.99  ? 86  LEU A CG  1 
ATOM   746  C  CD1 . LEU A 1 85  ? 25.811 -14.112 29.674 1.00 29.52  ? 86  LEU A CD1 1 
ATOM   747  C  CD2 . LEU A 1 85  ? 24.625 -16.053 28.736 1.00 29.20  ? 86  LEU A CD2 1 
ATOM   748  N  N   . LEU A 1 86  ? 29.742 -17.822 27.933 1.00 21.05  ? 87  LEU A N   1 
ATOM   749  C  CA  . LEU A 1 86  ? 30.775 -18.238 26.975 1.00 20.38  ? 87  LEU A CA  1 
ATOM   750  C  C   . LEU A 1 86  ? 30.542 -19.711 26.579 1.00 23.33  ? 87  LEU A C   1 
ATOM   751  O  O   . LEU A 1 86  ? 30.620 -20.060 25.400 1.00 22.26  ? 87  LEU A O   1 
ATOM   752  C  CB  . LEU A 1 86  ? 32.177 -18.023 27.569 1.00 20.32  ? 87  LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 86  ? 33.337 -18.333 26.610 1.00 24.72  ? 87  LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 86  ? 33.306 -17.412 25.364 1.00 23.83  ? 87  LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 86  ? 34.705 -18.237 27.354 1.00 28.84  ? 87  LEU A CD2 1 
ATOM   756  N  N   . ASP A 1 87  ? 30.233 -20.575 27.563 1.00 21.52  ? 88  ASP A N   1 
ATOM   757  C  CA  . ASP A 1 87  ? 29.902 -21.971 27.287 1.00 21.12  ? 88  ASP A CA  1 
ATOM   758  C  C   . ASP A 1 87  ? 28.703 -22.071 26.354 1.00 23.57  ? 88  ASP A C   1 
ATOM   759  O  O   . ASP A 1 87  ? 28.747 -22.843 25.402 1.00 23.39  ? 88  ASP A O   1 
ATOM   760  C  CB  . ASP A 1 87  ? 29.612 -22.703 28.599 1.00 24.22  ? 88  ASP A CB  1 
ATOM   761  C  CG  . ASP A 1 87  ? 30.864 -23.042 29.383 1.00 38.02  ? 88  ASP A CG  1 
ATOM   762  O  OD1 . ASP A 1 87  ? 31.975 -22.969 28.795 1.00 36.49  ? 88  ASP A OD1 1 
ATOM   763  O  OD2 . ASP A 1 87  ? 30.737 -23.388 30.585 1.00 38.60  ? 88  ASP A OD2 1 
ATOM   764  N  N   . PHE A 1 88  ? 27.648 -21.288 26.612 1.00 21.05  ? 89  PHE A N   1 
ATOM   765  C  CA  . PHE A 1 88  ? 26.458 -21.227 25.742 1.00 20.08  ? 89  PHE A CA  1 
ATOM   766  C  C   . PHE A 1 88  ? 26.830 -20.835 24.302 1.00 20.96  ? 89  PHE A C   1 
ATOM   767  O  O   . PHE A 1 88  ? 26.347 -21.438 23.329 1.00 18.88  ? 89  PHE A O   1 
ATOM   768  C  CB  . PHE A 1 88  ? 25.405 -20.258 26.332 1.00 20.61  ? 89  PHE A CB  1 
ATOM   769  C  CG  . PHE A 1 88  ? 24.290 -19.982 25.353 1.00 20.99  ? 89  PHE A CG  1 
ATOM   770  C  CD1 . PHE A 1 88  ? 23.324 -20.947 25.085 1.00 22.94  ? 89  PHE A CD1 1 
ATOM   771  C  CD2 . PHE A 1 88  ? 24.276 -18.804 24.601 1.00 22.52  ? 89  PHE A CD2 1 
ATOM   772  C  CE1 . PHE A 1 88  ? 22.328 -20.719 24.137 1.00 22.98  ? 89  PHE A CE1 1 
ATOM   773  C  CE2 . PHE A 1 88  ? 23.283 -18.581 23.637 1.00 25.42  ? 89  PHE A CE2 1 
ATOM   774  C  CZ  . PHE A 1 88  ? 22.314 -19.536 23.414 1.00 24.09  ? 89  PHE A CZ  1 
ATOM   775  N  N   . MET A 1 89  ? 27.658 -19.803 24.159 1.00 17.81  ? 90  MET A N   1 
ATOM   776  C  CA  . MET A 1 89  ? 28.088 -19.364 22.819 1.00 17.13  ? 90  MET A CA  1 
ATOM   777  C  C   . MET A 1 89  ? 28.648 -20.514 22.006 1.00 21.29  ? 90  MET A C   1 
ATOM   778  O  O   . MET A 1 89  ? 28.284 -20.663 20.843 1.00 21.19  ? 90  MET A O   1 
ATOM   779  C  CB  . MET A 1 89  ? 29.165 -18.265 22.921 1.00 17.87  ? 90  MET A CB  1 
ATOM   780  C  CG  . MET A 1 89  ? 28.633 -16.978 23.496 1.00 20.06  ? 90  MET A CG  1 
ATOM   781  S  SD  . MET A 1 89  ? 29.993 -15.765 23.385 1.00 22.92  ? 90  MET A SD  1 
ATOM   782  C  CE  . MET A 1 89  ? 29.379 -14.525 24.555 1.00 22.95  ? 90  MET A CE  1 
ATOM   783  N  N   . TYR A 1 90  ? 29.501 -21.347 22.637 1.00 18.16  ? 91  TYR A N   1 
ATOM   784  C  CA  . TYR A 1 90  ? 30.175 -22.441 21.948 1.00 18.05  ? 91  TYR A CA  1 
ATOM   785  C  C   . TYR A 1 90  ? 29.422 -23.767 21.928 1.00 21.61  ? 91  TYR A C   1 
ATOM   786  O  O   . TYR A 1 90  ? 29.914 -24.722 21.310 1.00 20.64  ? 91  TYR A O   1 
ATOM   787  C  CB  . TYR A 1 90  ? 31.552 -22.654 22.583 1.00 19.10  ? 91  TYR A CB  1 
ATOM   788  C  CG  . TYR A 1 90  ? 32.609 -21.687 22.084 1.00 19.90  ? 91  TYR A CG  1 
ATOM   789  C  CD1 . TYR A 1 90  ? 32.780 -20.439 22.682 1.00 21.38  ? 91  TYR A CD1 1 
ATOM   790  C  CD2 . TYR A 1 90  ? 33.444 -22.027 21.019 1.00 20.91  ? 91  TYR A CD2 1 
ATOM   791  C  CE1 . TYR A 1 90  ? 33.772 -19.560 22.243 1.00 20.89  ? 91  TYR A CE1 1 
ATOM   792  C  CE2 . TYR A 1 90  ? 34.469 -21.178 20.604 1.00 21.07  ? 91  TYR A CE2 1 
ATOM   793  C  CZ  . TYR A 1 90  ? 34.608 -19.936 21.200 1.00 22.68  ? 91  TYR A CZ  1 
ATOM   794  O  OH  . TYR A 1 90  ? 35.634 -19.128 20.793 1.00 21.79  ? 91  TYR A OH  1 
ATOM   795  N  N   . THR A 1 91  ? 28.263 -23.864 22.620 1.00 18.94  ? 92  THR A N   1 
ATOM   796  C  CA  . THR A 1 91  ? 27.576 -25.164 22.681 1.00 20.22  ? 92  THR A CA  1 
ATOM   797  C  C   . THR A 1 91  ? 26.066 -25.135 22.417 1.00 22.30  ? 92  THR A C   1 
ATOM   798  O  O   . THR A 1 91  ? 25.488 -26.217 22.246 1.00 21.77  ? 92  THR A O   1 
ATOM   799  C  CB  . THR A 1 91  ? 27.773 -25.847 24.074 1.00 25.19  ? 92  THR A CB  1 
ATOM   800  O  OG1 . THR A 1 91  ? 27.109 -25.078 25.083 1.00 24.55  ? 92  THR A OG1 1 
ATOM   801  C  CG2 . THR A 1 91  ? 29.249 -26.062 24.457 1.00 25.02  ? 92  THR A CG2 1 
ATOM   802  N  N   . SER A 1 92  ? 25.417 -23.956 22.526 1.00 18.58  ? 93  SER A N   1 
ATOM   803  C  CA  . SER A 1 92  ? 23.938 -23.759 22.481 1.00 18.38  ? 93  SER A CA  1 
ATOM   804  C  C   . SER A 1 92  ? 23.280 -24.167 23.824 1.00 22.64  ? 93  SER A C   1 
ATOM   805  O  O   . SER A 1 92  ? 22.068 -24.029 23.958 1.00 23.08  ? 93  SER A O   1 
ATOM   806  C  CB  . SER A 1 92  ? 23.280 -24.578 21.355 1.00 20.74  ? 93  SER A CB  1 
ATOM   807  O  OG  . SER A 1 92  ? 23.920 -24.394 20.102 1.00 25.84  ? 93  SER A OG  1 
ATOM   808  N  N   A ARG A 1 93  ? 24.081 -24.644 24.800 0.60 20.84  ? 94  ARG A N   1 
ATOM   809  N  N   B ARG A 1 93  ? 24.061 -24.685 24.796 0.40 19.74  ? 94  ARG A N   1 
ATOM   810  C  CA  A ARG A 1 93  ? 23.590 -25.111 26.100 0.60 22.02  ? 94  ARG A CA  1 
ATOM   811  C  CA  B ARG A 1 93  ? 23.507 -25.117 26.084 0.40 20.40  ? 94  ARG A CA  1 
ATOM   812  C  C   A ARG A 1 93  ? 23.798 -24.049 27.167 0.60 25.17  ? 94  ARG A C   1 
ATOM   813  C  C   B ARG A 1 93  ? 23.785 -24.106 27.178 0.40 24.50  ? 94  ARG A C   1 
ATOM   814  O  O   A ARG A 1 93  ? 24.922 -23.562 27.356 0.60 23.63  ? 94  ARG A O   1 
ATOM   815  O  O   B ARG A 1 93  ? 24.931 -23.683 27.372 0.40 23.14  ? 94  ARG A O   1 
ATOM   816  C  CB  A ARG A 1 93  ? 24.302 -26.409 26.513 0.60 25.23  ? 94  ARG A CB  1 
ATOM   817  C  CB  B ARG A 1 93  ? 23.970 -26.529 26.468 0.40 21.32  ? 94  ARG A CB  1 
ATOM   818  C  CG  A ARG A 1 93  ? 24.166 -27.546 25.490 0.60 31.99  ? 94  ARG A CG  1 
ATOM   819  C  CG  B ARG A 1 93  ? 23.329 -27.595 25.588 0.40 19.52  ? 94  ARG A CG  1 
ATOM   820  C  CD  A ARG A 1 93  ? 25.123 -28.691 25.792 0.60 38.00  ? 94  ARG A CD  1 
ATOM   821  C  CD  B ARG A 1 93  ? 24.079 -28.905 25.605 0.40 32.09  ? 94  ARG A CD  1 
ATOM   822  N  NE  A ARG A 1 93  ? 24.880 -29.263 27.118 0.60 42.52  ? 94  ARG A NE  1 
ATOM   823  N  NE  B ARG A 1 93  ? 23.478 -29.874 24.685 0.40 40.09  ? 94  ARG A NE  1 
ATOM   824  C  CZ  A ARG A 1 93  ? 24.003 -30.230 27.367 0.60 54.68  ? 94  ARG A CZ  1 
ATOM   825  C  CZ  B ARG A 1 93  ? 23.351 -31.173 24.938 0.40 52.75  ? 94  ARG A CZ  1 
ATOM   826  N  NH1 A ARG A 1 93  ? 23.838 -30.681 28.602 0.60 40.00  ? 94  ARG A NH1 1 
ATOM   827  N  NH1 B ARG A 1 93  ? 22.801 -31.979 24.039 0.40 39.47  ? 94  ARG A NH1 1 
ATOM   828  N  NH2 A ARG A 1 93  ? 23.286 -30.757 26.381 0.60 42.50  ? 94  ARG A NH2 1 
ATOM   829  N  NH2 B ARG A 1 93  ? 23.773 -31.677 26.090 0.40 42.03  ? 94  ARG A NH2 1 
ATOM   830  N  N   . LEU A 1 94  ? 22.714 -23.709 27.874 1.00 22.09  ? 95  LEU A N   1 
ATOM   831  C  CA  . LEU A 1 94  ? 22.744 -22.706 28.923 1.00 22.14  ? 95  LEU A CA  1 
ATOM   832  C  C   . LEU A 1 94  ? 22.499 -23.340 30.287 1.00 27.76  ? 95  LEU A C   1 
ATOM   833  O  O   . LEU A 1 94  ? 21.417 -23.883 30.544 1.00 27.35  ? 95  LEU A O   1 
ATOM   834  C  CB  . LEU A 1 94  ? 21.717 -21.613 28.603 1.00 22.00  ? 95  LEU A CB  1 
ATOM   835  C  CG  . LEU A 1 94  ? 21.740 -20.397 29.545 1.00 26.30  ? 95  LEU A CG  1 
ATOM   836  C  CD1 . LEU A 1 94  ? 23.026 -19.576 29.333 1.00 25.07  ? 95  LEU A CD1 1 
ATOM   837  C  CD2 . LEU A 1 94  ? 20.494 -19.554 29.367 1.00 27.47  ? 95  LEU A CD2 1 
ATOM   838  N  N   . ASN A 1 95  ? 23.508 -23.253 31.173 1.00 27.15  ? 96  ASN A N   1 
ATOM   839  C  CA  . ASN A 1 95  ? 23.428 -23.815 32.530 1.00 28.40  ? 96  ASN A CA  1 
ATOM   840  C  C   . ASN A 1 95  ? 22.715 -22.805 33.451 1.00 32.52  ? 96  ASN A C   1 
ATOM   841  O  O   . ASN A 1 95  ? 23.354 -22.110 34.240 1.00 32.18  ? 96  ASN A O   1 
ATOM   842  C  CB  . ASN A 1 95  ? 24.842 -24.182 33.058 1.00 31.65  ? 96  ASN A CB  1 
ATOM   843  C  CG  . ASN A 1 95  ? 24.826 -24.804 34.456 1.00 49.42  ? 96  ASN A CG  1 
ATOM   844  O  OD1 . ASN A 1 95  ? 23.836 -25.385 34.897 1.00 41.38  ? 96  ASN A OD1 1 
ATOM   845  N  ND2 . ASN A 1 95  ? 25.914 -24.675 35.195 1.00 42.73  ? 96  ASN A ND2 1 
ATOM   846  N  N   . LEU A 1 96  ? 21.402 -22.689 33.293 1.00 29.55  ? 97  LEU A N   1 
ATOM   847  C  CA  . LEU A 1 96  ? 20.594 -21.727 34.040 1.00 30.69  ? 97  LEU A CA  1 
ATOM   848  C  C   . LEU A 1 96  ? 20.046 -22.368 35.302 1.00 34.68  ? 97  LEU A C   1 
ATOM   849  O  O   . LEU A 1 96  ? 19.386 -23.414 35.234 1.00 33.54  ? 97  LEU A O   1 
ATOM   850  C  CB  . LEU A 1 96  ? 19.480 -21.227 33.108 1.00 31.44  ? 97  LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 96  ? 18.739 -19.957 33.463 1.00 37.71  ? 97  LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 96  ? 19.715 -18.742 33.578 1.00 37.57  ? 97  LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 96  ? 17.646 -19.697 32.430 1.00 38.12  ? 97  LEU A CD2 1 
ATOM   854  N  N   . ARG A 1 97  ? 20.380 -21.774 36.474 1.00 31.97  ? 98  ARG A N   1 
ATOM   855  C  CA  . ARG A 1 97  ? 19.982 -22.291 37.793 1.00 34.19  ? 98  ARG A CA  1 
ATOM   856  C  C   . ARG A 1 97  ? 19.451 -21.168 38.679 1.00 36.09  ? 98  ARG A C   1 
ATOM   857  O  O   . ARG A 1 97  ? 19.786 -19.998 38.454 1.00 33.74  ? 98  ARG A O   1 
ATOM   858  C  CB  . ARG A 1 97  ? 21.182 -22.972 38.491 1.00 35.79  ? 98  ARG A CB  1 
ATOM   859  C  CG  . ARG A 1 97  ? 21.821 -24.118 37.684 1.00 42.41  ? 98  ARG A CG  1 
ATOM   860  C  CD  . ARG A 1 97  ? 23.088 -24.681 38.320 1.00 58.25  ? 98  ARG A CD  1 
ATOM   861  N  NE  . ARG A 1 97  ? 22.857 -25.191 39.678 1.00 77.15  ? 98  ARG A NE  1 
ATOM   862  C  CZ  . ARG A 1 97  ? 22.394 -26.406 39.967 1.00 97.39  ? 98  ARG A CZ  1 
ATOM   863  N  NH1 . ARG A 1 97  ? 22.207 -26.768 41.230 1.00 86.07  ? 98  ARG A NH1 1 
ATOM   864  N  NH2 . ARG A 1 97  ? 22.112 -27.267 38.995 1.00 86.75  ? 98  ARG A NH2 1 
ATOM   865  N  N   . GLU A 1 98  ? 18.635 -21.505 39.703 1.00 34.41  ? 99  GLU A N   1 
ATOM   866  C  CA  . GLU A 1 98  ? 18.115 -20.481 40.624 1.00 35.11  ? 99  GLU A CA  1 
ATOM   867  C  C   . GLU A 1 98  ? 19.250 -19.601 41.188 1.00 40.10  ? 99  GLU A C   1 
ATOM   868  O  O   . GLU A 1 98  ? 19.085 -18.387 41.294 1.00 40.15  ? 99  GLU A O   1 
ATOM   869  C  CB  . GLU A 1 98  ? 17.333 -21.143 41.785 1.00 38.60  ? 99  GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 98  ? 16.638 -20.154 42.704 1.00 49.61  ? 99  GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 98  ? 15.914 -20.779 43.881 1.00 83.60  ? 99  GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 98  ? 16.479 -21.692 44.528 1.00 81.04  ? 99  GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 98  ? 14.775 -20.343 44.164 1.00 87.70  ? 99  GLU A OE2 1 
ATOM   874  N  N   . GLY A 1 99  ? 20.385 -20.225 41.507 1.00 38.12  ? 100 GLY A N   1 
ATOM   875  C  CA  . GLY A 1 99  ? 21.549 -19.555 42.083 1.00 38.26  ? 100 GLY A CA  1 
ATOM   876  C  C   . GLY A 1 99  ? 22.356 -18.667 41.153 1.00 38.98  ? 100 GLY A C   1 
ATOM   877  O  O   . GLY A 1 99  ? 23.167 -17.862 41.620 1.00 38.51  ? 100 GLY A O   1 
ATOM   878  N  N   . ASN A 1 100 ? 22.145 -18.777 39.835 1.00 33.69  ? 101 ASN A N   1 
ATOM   879  C  CA  . ASN A 1 100 ? 22.929 -17.961 38.903 1.00 31.23  ? 101 ASN A CA  1 
ATOM   880  C  C   . ASN A 1 100 ? 22.097 -17.094 37.953 1.00 34.90  ? 101 ASN A C   1 
ATOM   881  O  O   . ASN A 1 100 ? 22.678 -16.292 37.213 1.00 32.78  ? 101 ASN A O   1 
ATOM   882  C  CB  . ASN A 1 100 ? 23.900 -18.865 38.103 1.00 30.13  ? 101 ASN A CB  1 
ATOM   883  C  CG  . ASN A 1 100 ? 23.236 -19.811 37.114 1.00 36.76  ? 101 ASN A CG  1 
ATOM   884  O  OD1 . ASN A 1 100 ? 22.194 -19.502 36.531 1.00 29.06  ? 101 ASN A OD1 1 
ATOM   885  N  ND2 . ASN A 1 100 ? 23.853 -20.964 36.851 1.00 31.15  ? 101 ASN A ND2 1 
ATOM   886  N  N   . ILE A 1 101 ? 20.757 -17.282 37.928 1.00 32.61  ? 102 ILE A N   1 
ATOM   887  C  CA  . ILE A 1 101 ? 19.884 -16.626 36.939 1.00 32.11  ? 102 ILE A CA  1 
ATOM   888  C  C   . ILE A 1 101 ? 20.016 -15.094 36.915 1.00 34.02  ? 102 ILE A C   1 
ATOM   889  O  O   . ILE A 1 101 ? 20.049 -14.516 35.820 1.00 31.36  ? 102 ILE A O   1 
ATOM   890  C  CB  . ILE A 1 101 ? 18.406 -17.076 37.025 1.00 36.37  ? 102 ILE A CB  1 
ATOM   891  C  CG1 . ILE A 1 101 ? 17.579 -16.483 35.847 1.00 36.79  ? 102 ILE A CG1 1 
ATOM   892  C  CG2 . ILE A 1 101 ? 17.768 -16.823 38.400 1.00 35.74  ? 102 ILE A CG2 1 
ATOM   893  C  CD1 . ILE A 1 101 ? 16.393 -17.314 35.417 1.00 38.49  ? 102 ILE A CD1 1 
ATOM   894  N  N   . MET A 1 102 ? 20.105 -14.442 38.085 1.00 32.11  ? 103 MET A N   1 
ATOM   895  C  CA  . MET A 1 102 ? 20.258 -12.988 38.112 1.00 32.86  ? 103 MET A CA  1 
ATOM   896  C  C   . MET A 1 102 ? 21.568 -12.534 37.475 1.00 34.09  ? 103 MET A C   1 
ATOM   897  O  O   . MET A 1 102 ? 21.539 -11.607 36.672 1.00 31.57  ? 103 MET A O   1 
ATOM   898  C  CB  . MET A 1 102 ? 20.083 -12.415 39.533 1.00 37.21  ? 103 MET A CB  1 
ATOM   899  C  CG  . MET A 1 102 ? 18.708 -12.704 40.144 1.00 43.93  ? 103 MET A CG  1 
ATOM   900  S  SD  . MET A 1 102 ? 17.278 -12.311 39.087 1.00 50.18  ? 103 MET A SD  1 
ATOM   901  C  CE  . MET A 1 102 ? 17.318 -10.499 39.139 1.00 47.76  ? 103 MET A CE  1 
ATOM   902  N  N   . ALA A 1 103 ? 22.705 -13.205 37.793 1.00 31.77  ? 104 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 103 ? 24.025 -12.870 37.215 1.00 31.15  ? 104 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 103 ? 24.030 -13.167 35.714 1.00 31.82  ? 104 ALA A C   1 
ATOM   905  O  O   . ALA A 1 103 ? 24.523 -12.354 34.922 1.00 29.12  ? 104 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 103 ? 25.127 -13.673 37.897 1.00 32.64  ? 104 ALA A CB  1 
ATOM   907  N  N   . VAL A 1 104 ? 23.449 -14.316 35.320 1.00 27.20  ? 105 VAL A N   1 
ATOM   908  C  CA  . VAL A 1 104 ? 23.379 -14.687 33.897 1.00 25.08  ? 105 VAL A CA  1 
ATOM   909  C  C   . VAL A 1 104 ? 22.579 -13.654 33.099 1.00 27.36  ? 105 VAL A C   1 
ATOM   910  O  O   . VAL A 1 104 ? 23.077 -13.199 32.062 1.00 26.04  ? 105 VAL A O   1 
ATOM   911  C  CB  . VAL A 1 104 ? 22.891 -16.141 33.674 1.00 28.11  ? 105 VAL A CB  1 
ATOM   912  C  CG1 . VAL A 1 104 ? 22.641 -16.431 32.189 1.00 26.42  ? 105 VAL A CG1 1 
ATOM   913  C  CG2 . VAL A 1 104 ? 23.898 -17.132 34.245 1.00 27.90  ? 105 VAL A CG2 1 
ATOM   914  N  N   A MET A 1 105 ? 21.373 -13.274 33.569 0.65 25.74  ? 106 MET A N   1 
ATOM   915  N  N   B MET A 1 105 ? 21.373 -13.273 33.569 0.35 26.15  ? 106 MET A N   1 
ATOM   916  C  CA  A MET A 1 105 ? 20.555 -12.281 32.857 0.65 27.01  ? 106 MET A CA  1 
ATOM   917  C  CA  B MET A 1 105 ? 20.548 -12.281 32.868 0.35 27.25  ? 106 MET A CA  1 
ATOM   918  C  C   A MET A 1 105 ? 21.266 -10.923 32.751 0.65 30.65  ? 106 MET A C   1 
ATOM   919  C  C   B MET A 1 105 ? 21.257 -10.927 32.754 0.35 31.03  ? 106 MET A C   1 
ATOM   920  O  O   A MET A 1 105 ? 21.240 -10.302 31.682 0.65 29.57  ? 106 MET A O   1 
ATOM   921  O  O   B MET A 1 105 ? 21.236 -10.322 31.678 0.35 30.13  ? 106 MET A O   1 
ATOM   922  C  CB  A MET A 1 105 ? 19.189 -12.099 33.528 0.65 30.71  ? 106 MET A CB  1 
ATOM   923  C  CB  B MET A 1 105 ? 19.181 -12.107 33.538 0.35 31.12  ? 106 MET A CB  1 
ATOM   924  C  CG  A MET A 1 105 ? 18.263 -11.192 32.731 0.65 34.61  ? 106 MET A CG  1 
ATOM   925  C  CG  B MET A 1 105 ? 18.236 -11.255 32.717 0.35 35.40  ? 106 MET A CG  1 
ATOM   926  S  SD  A MET A 1 105 ? 16.580 -11.227 33.359 0.65 40.28  ? 106 MET A SD  1 
ATOM   927  S  SD  B MET A 1 105 ? 16.654 -11.010 33.528 0.35 41.61  ? 106 MET A SD  1 
ATOM   928  C  CE  A MET A 1 105 ? 16.719 -10.094 34.792 0.65 38.10  ? 106 MET A CE  1 
ATOM   929  C  CE  B MET A 1 105 ? 16.183 -9.469  32.804 0.35 39.11  ? 106 MET A CE  1 
ATOM   930  N  N   . ALA A 1 106 ? 21.881 -10.458 33.853 1.00 28.54  ? 107 ALA A N   1 
ATOM   931  C  CA  . ALA A 1 106 ? 22.620 -9.169  33.870 1.00 28.36  ? 107 ALA A CA  1 
ATOM   932  C  C   . ALA A 1 106 ? 23.777 -9.206  32.866 1.00 28.53  ? 107 ALA A C   1 
ATOM   933  O  O   . ALA A 1 106 ? 23.945 -8.251  32.091 1.00 26.51  ? 107 ALA A O   1 
ATOM   934  C  CB  . ALA A 1 106 ? 23.135 -8.861  35.271 1.00 29.87  ? 107 ALA A CB  1 
ATOM   935  N  N   . THR A 1 107 ? 24.515 -10.332 32.819 1.00 24.88  ? 108 THR A N   1 
ATOM   936  C  CA  . THR A 1 107 ? 25.621 -10.509 31.878 1.00 24.05  ? 108 THR A CA  1 
ATOM   937  C  C   . THR A 1 107 ? 25.102 -10.564 30.425 1.00 26.97  ? 108 THR A C   1 
ATOM   938  O  O   . THR A 1 107 ? 25.689 -9.901  29.562 1.00 24.56  ? 108 THR A O   1 
ATOM   939  C  CB  . THR A 1 107 ? 26.538 -11.687 32.260 1.00 29.78  ? 108 THR A CB  1 
ATOM   940  O  OG1 . THR A 1 107 ? 26.821 -11.644 33.663 1.00 28.94  ? 108 THR A OG1 1 
ATOM   941  C  CG2 . THR A 1 107 ? 27.859 -11.683 31.464 1.00 28.71  ? 108 THR A CG2 1 
ATOM   942  N  N   . ALA A 1 108 ? 23.986 -11.296 30.170 1.00 24.18  ? 109 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 108 ? 23.396 -11.389 28.826 1.00 23.00  ? 109 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 108 ? 22.883 -10.019 28.360 1.00 25.39  ? 109 ALA A C   1 
ATOM   945  O  O   . ALA A 1 108 ? 23.031 -9.682  27.185 1.00 23.61  ? 109 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 108 ? 22.287 -12.442 28.792 1.00 23.77  ? 109 ALA A CB  1 
ATOM   947  N  N   . MET A 1 109 ? 22.340 -9.189  29.281 1.00 23.61  ? 110 MET A N   1 
ATOM   948  C  CA  . MET A 1 109 ? 21.896 -7.846  28.888 1.00 23.82  ? 110 MET A CA  1 
ATOM   949  C  C   . MET A 1 109 ? 23.093 -6.978  28.445 1.00 26.83  ? 110 MET A C   1 
ATOM   950  O  O   . MET A 1 109 ? 23.040 -6.327  27.401 1.00 26.95  ? 110 MET A O   1 
ATOM   951  C  CB  . MET A 1 109 ? 21.142 -7.184  30.045 1.00 27.25  ? 110 MET A CB  1 
ATOM   952  C  CG  . MET A 1 109 ? 19.746 -7.744  30.203 1.00 32.74  ? 110 MET A CG  1 
ATOM   953  S  SD  . MET A 1 109 ? 18.994 -7.185  31.745 1.00 40.73  ? 110 MET A SD  1 
ATOM   954  C  CE  . MET A 1 109 ? 18.723 -5.458  31.353 1.00 38.99  ? 110 MET A CE  1 
ATOM   955  N  N   . TYR A 1 110 ? 24.178 -7.026  29.216 1.00 24.98  ? 111 TYR A N   1 
ATOM   956  C  CA  . TYR A 1 110 ? 25.420 -6.296  28.934 1.00 25.17  ? 111 TYR A CA  1 
ATOM   957  C  C   . TYR A 1 110 ? 26.048 -6.787  27.604 1.00 26.93  ? 111 TYR A C   1 
ATOM   958  O  O   . TYR A 1 110 ? 26.451 -5.965  26.771 1.00 25.17  ? 111 TYR A O   1 
ATOM   959  C  CB  . TYR A 1 110 ? 26.387 -6.517  30.105 1.00 25.83  ? 111 TYR A CB  1 
ATOM   960  C  CG  . TYR A 1 110 ? 27.807 -6.040  29.873 1.00 25.94  ? 111 TYR A CG  1 
ATOM   961  C  CD1 . TYR A 1 110 ? 28.128 -4.686  29.932 1.00 28.60  ? 111 TYR A CD1 1 
ATOM   962  C  CD2 . TYR A 1 110 ? 28.842 -6.951  29.665 1.00 25.63  ? 111 TYR A CD2 1 
ATOM   963  C  CE1 . TYR A 1 110 ? 29.440 -4.245  29.734 1.00 25.81  ? 111 TYR A CE1 1 
ATOM   964  C  CE2 . TYR A 1 110 ? 30.160 -6.527  29.505 1.00 25.79  ? 111 TYR A CE2 1 
ATOM   965  C  CZ  . TYR A 1 110 ? 30.453 -5.172  29.551 1.00 26.58  ? 111 TYR A CZ  1 
ATOM   966  O  OH  . TYR A 1 110 ? 31.753 -4.764  29.426 1.00 25.56  ? 111 TYR A OH  1 
ATOM   967  N  N   . LEU A 1 111 ? 26.081 -8.114  27.389 1.00 23.08  ? 112 LEU A N   1 
ATOM   968  C  CA  . LEU A 1 111 ? 26.674 -8.702  26.182 1.00 21.32  ? 112 LEU A CA  1 
ATOM   969  C  C   . LEU A 1 111 ? 25.756 -8.570  24.963 1.00 24.95  ? 112 LEU A C   1 
ATOM   970  O  O   . LEU A 1 111 ? 26.196 -8.823  23.843 1.00 23.97  ? 112 LEU A O   1 
ATOM   971  C  CB  . LEU A 1 111 ? 27.035 -10.179 26.420 1.00 19.96  ? 112 LEU A CB  1 
ATOM   972  C  CG  . LEU A 1 111 ? 28.151 -10.451 27.458 1.00 22.98  ? 112 LEU A CG  1 
ATOM   973  C  CD1 . LEU A 1 111 ? 28.427 -11.977 27.551 1.00 22.30  ? 112 LEU A CD1 1 
ATOM   974  C  CD2 . LEU A 1 111 ? 29.464 -9.664  27.109 1.00 24.50  ? 112 LEU A CD2 1 
ATOM   975  N  N   . GLN A 1 112 ? 24.479 -8.210  25.192 1.00 23.35  ? 113 GLN A N   1 
ATOM   976  C  CA  . GLN A 1 112 ? 23.461 -8.067  24.140 1.00 23.76  ? 113 GLN A CA  1 
ATOM   977  C  C   . GLN A 1 112 ? 23.241 -9.425  23.454 1.00 25.76  ? 113 GLN A C   1 
ATOM   978  O  O   . GLN A 1 112 ? 23.551 -9.615  22.274 1.00 24.29  ? 113 GLN A O   1 
ATOM   979  C  CB  . GLN A 1 112 ? 23.831 -6.955  23.136 1.00 25.15  ? 113 GLN A CB  1 
ATOM   980  C  CG  . GLN A 1 112 ? 24.030 -5.575  23.789 1.00 28.35  ? 113 GLN A CG  1 
ATOM   981  C  CD  . GLN A 1 112 ? 24.741 -4.641  22.837 1.00 40.74  ? 113 GLN A CD  1 
ATOM   982  O  OE1 . GLN A 1 112 ? 24.590 -4.730  21.627 1.00 30.64  ? 113 GLN A OE1 1 
ATOM   983  N  NE2 . GLN A 1 112 ? 25.549 -3.742  23.356 1.00 34.83  ? 113 GLN A NE2 1 
ATOM   984  N  N   . MET A 1 113 ? 22.747 -10.384 24.247 1.00 22.81  ? 114 MET A N   1 
ATOM   985  C  CA  . MET A 1 113 ? 22.440 -11.760 23.813 1.00 22.08  ? 114 MET A CA  1 
ATOM   986  C  C   . MET A 1 113 ? 20.935 -11.908 24.077 1.00 28.28  ? 114 MET A C   1 
ATOM   987  O  O   . MET A 1 113 ? 20.511 -12.386 25.137 1.00 27.05  ? 114 MET A O   1 
ATOM   988  C  CB  . MET A 1 113 ? 23.293 -12.736 24.633 1.00 22.97  ? 114 MET A CB  1 
ATOM   989  C  CG  . MET A 1 113 ? 24.789 -12.600 24.322 1.00 24.45  ? 114 MET A CG  1 
ATOM   990  S  SD  . MET A 1 113 ? 25.797 -13.646 25.369 1.00 27.08  ? 114 MET A SD  1 
ATOM   991  C  CE  . MET A 1 113 ? 25.425 -15.312 24.615 1.00 24.27  ? 114 MET A CE  1 
ATOM   992  N  N   . GLU A 1 114 ? 20.134 -11.360 23.149 1.00 28.39  ? 115 GLU A N   1 
ATOM   993  C  CA  . GLU A 1 114 ? 18.677 -11.213 23.288 1.00 30.82  ? 115 GLU A CA  1 
ATOM   994  C  C   . GLU A 1 114 ? 17.917 -12.497 23.597 1.00 31.96  ? 115 GLU A C   1 
ATOM   995  O  O   . GLU A 1 114 ? 16.988 -12.445 24.399 1.00 32.65  ? 115 GLU A O   1 
ATOM   996  C  CB  . GLU A 1 114 ? 18.064 -10.523 22.061 1.00 34.21  ? 115 GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 114 ? 18.632 -9.132  21.818 1.00 47.32  ? 115 GLU A CG  1 
ATOM   998  N  N   . HIS A 1 115 ? 18.285 -13.636 22.980 1.00 27.35  ? 116 HIS A N   1 
ATOM   999  C  CA  . HIS A 1 115 ? 17.554 -14.877 23.262 1.00 29.11  ? 116 HIS A CA  1 
ATOM   1000 C  C   . HIS A 1 115 ? 17.768 -15.356 24.697 1.00 30.83  ? 116 HIS A C   1 
ATOM   1001 O  O   . HIS A 1 115 ? 16.810 -15.805 25.331 1.00 31.50  ? 116 HIS A O   1 
ATOM   1002 C  CB  . HIS A 1 115 ? 17.860 -15.971 22.240 1.00 30.80  ? 116 HIS A CB  1 
ATOM   1003 C  CG  . HIS A 1 115 ? 17.398 -15.633 20.860 1.00 35.74  ? 116 HIS A CG  1 
ATOM   1004 N  ND1 . HIS A 1 115 ? 16.060 -15.430 20.580 1.00 39.44  ? 116 HIS A ND1 1 
ATOM   1005 C  CD2 . HIS A 1 115 ? 18.109 -15.511 19.716 1.00 37.28  ? 116 HIS A CD2 1 
ATOM   1006 C  CE1 . HIS A 1 115 ? 16.003 -15.156 19.286 1.00 39.15  ? 116 HIS A CE1 1 
ATOM   1007 N  NE2 . HIS A 1 115 ? 17.209 -15.205 18.726 1.00 38.35  ? 116 HIS A NE2 1 
ATOM   1008 N  N   . VAL A 1 116 ? 18.997 -15.191 25.229 1.00 24.69  ? 117 VAL A N   1 
ATOM   1009 C  CA  . VAL A 1 116 ? 19.300 -15.538 26.624 1.00 24.69  ? 117 VAL A CA  1 
ATOM   1010 C  C   . VAL A 1 116 ? 18.512 -14.631 27.577 1.00 29.57  ? 117 VAL A C   1 
ATOM   1011 O  O   . VAL A 1 116 ? 17.902 -15.119 28.537 1.00 27.35  ? 117 VAL A O   1 
ATOM   1012 C  CB  . VAL A 1 116 ? 20.814 -15.549 26.941 1.00 27.14  ? 117 VAL A CB  1 
ATOM   1013 C  CG1 . VAL A 1 116 ? 21.052 -15.819 28.429 1.00 27.41  ? 117 VAL A CG1 1 
ATOM   1014 C  CG2 . VAL A 1 116 ? 21.537 -16.591 26.082 1.00 26.02  ? 117 VAL A CG2 1 
ATOM   1015 N  N   . VAL A 1 117 ? 18.511 -13.307 27.304 1.00 26.47  ? 118 VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 117 ? 17.761 -12.343 28.125 1.00 27.55  ? 118 VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 117 ? 16.269 -12.757 28.186 1.00 34.18  ? 118 VAL A C   1 
ATOM   1018 O  O   . VAL A 1 117 ? 15.697 -12.801 29.281 1.00 33.93  ? 118 VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 117 ? 17.948 -10.876 27.638 1.00 30.45  ? 118 VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 117 ? 17.104 -9.896  28.475 1.00 31.24  ? 118 VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 117 ? 19.421 -10.466 27.679 1.00 29.32  ? 118 VAL A CG2 1 
ATOM   1022 N  N   A ASP A 1 118 ? 15.636 -12.971 27.015 0.41 32.63  ? 119 ASP A N   1 
ATOM   1023 N  N   B ASP A 1 118 ? 15.709 -13.175 27.033 0.59 31.55  ? 119 ASP A N   1 
ATOM   1024 C  CA  A ASP A 1 118 ? 14.211 -13.318 26.888 0.41 34.46  ? 119 ASP A CA  1 
ATOM   1025 C  CA  B ASP A 1 118 ? 14.326 -13.646 26.893 0.59 32.80  ? 119 ASP A CA  1 
ATOM   1026 C  C   A ASP A 1 118 ? 13.778 -14.525 27.722 0.41 38.69  ? 119 ASP A C   1 
ATOM   1027 C  C   B ASP A 1 118 ? 14.014 -14.854 27.789 0.59 34.94  ? 119 ASP A C   1 
ATOM   1028 O  O   A ASP A 1 118 ? 12.690 -14.505 28.291 0.41 40.00  ? 119 ASP A O   1 
ATOM   1029 O  O   B ASP A 1 118 ? 13.056 -14.779 28.555 0.59 35.13  ? 119 ASP A O   1 
ATOM   1030 C  CB  A ASP A 1 118 ? 13.825 -13.515 25.411 0.41 36.70  ? 119 ASP A CB  1 
ATOM   1031 C  CB  B ASP A 1 118 ? 14.002 -13.952 25.417 0.59 34.99  ? 119 ASP A CB  1 
ATOM   1032 C  CG  A ASP A 1 118 ? 13.615 -12.233 24.627 0.41 49.99  ? 119 ASP A CG  1 
ATOM   1033 C  CG  B ASP A 1 118 ? 12.546 -14.299 25.151 0.59 49.72  ? 119 ASP A CG  1 
ATOM   1034 O  OD1 A ASP A 1 118 ? 13.076 -11.262 25.203 0.41 53.86  ? 119 ASP A OD1 1 
ATOM   1035 O  OD1 B ASP A 1 118 ? 11.667 -13.476 25.491 0.59 52.59  ? 119 ASP A OD1 1 
ATOM   1036 O  OD2 A ASP A 1 118 ? 13.980 -12.201 23.435 0.41 55.44  ? 119 ASP A OD2 1 
ATOM   1037 O  OD2 B ASP A 1 118 ? 12.289 -15.383 24.588 0.59 55.18  ? 119 ASP A OD2 1 
ATOM   1038 N  N   A THR A 1 119 ? 14.627 -15.560 27.803 0.41 34.05  ? 120 THR A N   1 
ATOM   1039 N  N   B THR A 1 119 ? 14.819 -15.947 27.726 0.59 30.04  ? 120 THR A N   1 
ATOM   1040 C  CA  A THR A 1 119 ? 14.352 -16.786 28.556 0.41 34.34  ? 120 THR A CA  1 
ATOM   1041 C  CA  B THR A 1 119 ? 14.539 -17.126 28.566 0.59 30.57  ? 120 THR A CA  1 
ATOM   1042 C  C   A THR A 1 119 ? 14.540 -16.575 30.037 0.41 36.82  ? 120 THR A C   1 
ATOM   1043 C  C   B THR A 1 119 ? 14.732 -16.837 30.069 0.59 34.70  ? 120 THR A C   1 
ATOM   1044 O  O   A THR A 1 119 ? 13.702 -17.034 30.817 0.41 37.00  ? 120 THR A O   1 
ATOM   1045 O  O   B THR A 1 119 ? 14.062 -17.475 30.882 0.59 34.19  ? 120 THR A O   1 
ATOM   1046 C  CB  A THR A 1 119 ? 15.163 -17.924 27.983 0.41 42.34  ? 120 THR A CB  1 
ATOM   1047 C  CB  B THR A 1 119 ? 15.293 -18.390 28.109 0.59 31.16  ? 120 THR A CB  1 
ATOM   1048 O  OG1 A THR A 1 119 ? 14.723 -18.030 26.648 0.41 43.19  ? 120 THR A OG1 1 
ATOM   1049 O  OG1 B THR A 1 119 ? 14.663 -19.515 28.728 0.59 32.85  ? 120 THR A OG1 1 
ATOM   1050 C  CG2 A THR A 1 119 ? 14.915 -19.244 28.692 0.41 42.06  ? 120 THR A CG2 1 
ATOM   1051 C  CG2 B THR A 1 119 ? 16.773 -18.381 28.480 0.59 24.34  ? 120 THR A CG2 1 
ATOM   1052 N  N   . CYS A 1 120 ? 15.635 -15.886 30.429 1.00 32.00  ? 121 CYS A N   1 
ATOM   1053 C  CA  . CYS A 1 120 ? 15.887 -15.528 31.837 1.00 32.51  ? 121 CYS A CA  1 
ATOM   1054 C  C   . CYS A 1 120 ? 14.675 -14.791 32.366 1.00 37.95  ? 121 CYS A C   1 
ATOM   1055 O  O   . CYS A 1 120 ? 14.176 -15.139 33.443 1.00 37.79  ? 121 CYS A O   1 
ATOM   1056 C  CB  . CYS A 1 120 ? 17.143 -14.676 31.958 1.00 31.40  ? 121 CYS A CB  1 
ATOM   1057 S  SG  . CYS A 1 120 ? 18.678 -15.604 31.767 1.00 33.79  ? 121 CYS A SG  1 
ATOM   1058 N  N   . ARG A 1 121 ? 14.156 -13.811 31.572 1.00 35.61  ? 122 ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 121 ? 12.950 -13.047 31.924 1.00 37.84  ? 122 ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 121 ? 11.760 -13.994 32.185 1.00 42.69  ? 122 ARG A C   1 
ATOM   1061 O  O   . ARG A 1 121 ? 11.022 -13.807 33.160 1.00 43.11  ? 122 ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 121 ? 12.581 -12.070 30.800 1.00 40.25  ? 122 ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 121 ? 13.437 -10.820 30.765 1.00 55.56  ? 122 ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 121 ? 12.617 -9.592  30.417 1.00 70.88  ? 122 ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 121 ? 13.015 -9.020  29.129 1.00 80.84  ? 122 ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 121 ? 13.943 -8.078  28.975 1.00 91.43  ? 122 ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 121 ? 14.589 -7.592  30.029 1.00 73.11  ? 122 ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 121 ? 14.235 -7.618  27.766 1.00 79.51  ? 122 ARG A NH2 1 
ATOM   1069 N  N   . LYS A 1 122 ? 11.591 -15.010 31.318 1.00 40.30  ? 123 LYS A N   1 
ATOM   1070 C  CA  . LYS A 1 122 ? 10.500 -15.991 31.415 1.00 41.46  ? 123 LYS A CA  1 
ATOM   1071 C  C   . LYS A 1 122 ? 10.645 -16.901 32.632 1.00 44.96  ? 123 LYS A C   1 
ATOM   1072 O  O   . LYS A 1 122 ? 9.655  -17.145 33.317 1.00 44.79  ? 123 LYS A O   1 
ATOM   1073 C  CB  . LYS A 1 122 ? 10.392 -16.828 30.121 1.00 43.35  ? 123 LYS A CB  1 
ATOM   1074 C  CG  . LYS A 1 122 ? 9.849  -16.046 28.931 1.00 61.79  ? 123 LYS A CG  1 
ATOM   1075 C  CD  . LYS A 1 122 ? 9.558  -16.951 27.735 1.00 73.36  ? 123 LYS A CD  1 
ATOM   1076 C  CE  . LYS A 1 122 ? 9.603  -16.225 26.408 1.00 84.27  ? 123 LYS A CE  1 
ATOM   1077 N  NZ  . LYS A 1 122 ? 8.550  -15.182 26.280 1.00 93.50  ? 123 LYS A NZ  1 
ATOM   1078 N  N   . PHE A 1 123 ? 11.872 -17.415 32.898 1.00 40.23  ? 124 PHE A N   1 
ATOM   1079 C  CA  . PHE A 1 123 ? 12.146 -18.283 34.052 1.00 40.66  ? 124 PHE A CA  1 
ATOM   1080 C  C   . PHE A 1 123 ? 11.938 -17.522 35.370 1.00 46.27  ? 124 PHE A C   1 
ATOM   1081 O  O   . PHE A 1 123 ? 11.376 -18.085 36.315 1.00 46.72  ? 124 PHE A O   1 
ATOM   1082 C  CB  . PHE A 1 123 ? 13.552 -18.892 33.961 1.00 40.96  ? 124 PHE A CB  1 
ATOM   1083 C  CG  . PHE A 1 123 ? 13.679 -20.187 33.175 1.00 42.48  ? 124 PHE A CG  1 
ATOM   1084 C  CD1 . PHE A 1 123 ? 13.124 -20.311 31.902 1.00 45.63  ? 124 PHE A CD1 1 
ATOM   1085 C  CD2 . PHE A 1 123 ? 14.416 -21.255 33.678 1.00 45.03  ? 124 PHE A CD2 1 
ATOM   1086 C  CE1 . PHE A 1 123 ? 13.250 -21.505 31.176 1.00 45.75  ? 124 PHE A CE1 1 
ATOM   1087 C  CE2 . PHE A 1 123 ? 14.546 -22.446 32.946 1.00 46.55  ? 124 PHE A CE2 1 
ATOM   1088 C  CZ  . PHE A 1 123 ? 13.966 -22.559 31.703 1.00 43.83  ? 124 PHE A CZ  1 
ATOM   1089 N  N   . ILE A 1 124 ? 12.325 -16.228 35.407 1.00 41.74  ? 125 ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 124 ? 12.119 -15.368 36.586 1.00 43.04  ? 125 ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 124 ? 10.620 -15.123 36.826 1.00 49.79  ? 125 ILE A C   1 
ATOM   1092 O  O   . ILE A 1 124 ? 10.163 -15.235 37.968 1.00 50.58  ? 125 ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 124 ? 12.961 -14.061 36.507 1.00 44.81  ? 125 ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 124 ? 14.452 -14.385 36.697 1.00 43.26  ? 125 ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 124 ? 12.509 -13.008 37.562 1.00 47.25  ? 125 ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 124 ? 15.403 -13.364 36.105 1.00 49.73  ? 125 ILE A CD1 1 
ATOM   1097 N  N   . LYS A 1 125 ? 9.856  -14.839 35.744 1.00 48.24  ? 126 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 125 ? 8.406  -14.586 35.802 1.00 50.85  ? 126 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 125 ? 7.629  -15.816 36.315 1.00 56.25  ? 126 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 125 ? 6.637  -15.660 37.027 1.00 56.85  ? 126 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 125 ? 7.881  -14.144 34.427 1.00 54.10  ? 126 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 125 ? 6.542  -13.413 34.477 1.00 72.38  ? 126 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 125 ? 5.908  -13.323 33.097 1.00 85.07  ? 126 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 125 ? 4.482  -12.833 33.153 1.00 99.79  ? 126 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 125 ? 3.811  -12.943 31.830 1.00 110.39 ? 126 LYS A NZ  1 
ATOM   1106 N  N   . ALA A 1 126 ? 8.103  -17.030 35.978 1.00 51.81  ? 127 ALA A N   1 
ATOM   1107 C  CA  . ALA A 1 126 ? 7.486  -18.282 36.425 1.00 53.44  ? 127 ALA A CA  1 
ATOM   1108 C  C   . ALA A 1 126 ? 7.628  -18.491 37.945 1.00 59.30  ? 127 ALA A C   1 
ATOM   1109 O  O   . ALA A 1 126 ? 6.759  -19.106 38.548 1.00 59.89  ? 127 ALA A O   1 
ATOM   1110 C  CB  . ALA A 1 126 ? 8.093  -19.459 35.671 1.00 52.50  ? 127 ALA A CB  1 
ATOM   1111 N  N   . SER A 1 127 ? 8.719  -17.987 38.554 1.00 57.26  ? 128 SER A N   1 
ATOM   1112 C  CA  . SER A 1 127 ? 8.987  -18.133 39.991 1.00 60.06  ? 128 SER A CA  1 
ATOM   1113 C  C   . SER A 1 127 ? 8.308  -17.073 40.887 1.00 68.16  ? 128 SER A C   1 
ATOM   1114 O  O   . SER A 1 127 ? 8.242  -17.275 42.103 1.00 70.43  ? 128 SER A O   1 
ATOM   1115 C  CB  . SER A 1 127 ? 10.490 -18.176 40.256 1.00 63.79  ? 128 SER A CB  1 
ATOM   1116 O  OG  . SER A 1 127 ? 11.009 -19.480 40.045 1.00 74.76  ? 128 SER A OG  1 
ATOM   1117 N  N   . GLU A 1 128 ? 7.786  -15.969 40.301 1.00 64.73  ? 129 GLU A N   1 
ATOM   1118 C  CA  . GLU A 1 128 ? 7.119  -14.907 41.064 1.00 85.71  ? 129 GLU A CA  1 
ATOM   1119 C  C   . GLU A 1 128 ? 5.669  -15.258 41.416 1.00 128.16 ? 129 GLU A C   1 
ATOM   1120 O  O   . GLU A 1 128 ? 5.411  -16.282 42.046 1.00 95.90  ? 129 GLU A O   1 
ATOM   1121 C  CB  . GLU A 1 128 ? 7.229  -13.539 40.358 1.00 86.16  ? 129 GLU A CB  1 
ATOM   1122 C  CG  . GLU A 1 128 ? 6.252  -13.311 39.212 1.00 96.53  ? 129 GLU A CG  1 
ATOM   1123 C  CD  . GLU A 1 128 ? 6.442  -12.058 38.375 1.00 118.14 ? 129 GLU A CD  1 
ATOM   1124 O  OE1 . GLU A 1 128 ? 7.544  -11.462 38.412 1.00 111.76 ? 129 GLU A OE1 1 
ATOM   1125 O  OE2 . GLU A 1 128 ? 5.483  -11.680 37.664 1.00 112.65 ? 129 GLU A OE2 1 
HETATM 1126 C  C   . ACE B 2 1   ? 21.259 -35.117 5.873  1.00 27.96  ? 0   ACE D C   1 
HETATM 1127 O  O   . ACE B 2 1   ? 21.323 -33.962 6.328  1.00 28.54  ? 0   ACE D O   1 
HETATM 1128 C  CH3 . ACE B 2 1   ? 21.455 -36.318 6.774  1.00 27.84  ? 0   ACE D CH3 1 
ATOM   1129 N  N   A TRP B 2 2   ? 20.987 -35.382 4.599  0.78 26.48  ? 1   TRP D N   1 
ATOM   1130 N  N   B TRP B 2 2   ? 21.021 -35.395 4.589  0.22 26.93  ? 1   TRP D N   1 
ATOM   1131 C  CA  A TRP B 2 2   ? 20.785 -34.337 3.607  0.78 25.42  ? 1   TRP D CA  1 
ATOM   1132 C  CA  B TRP B 2 2   ? 20.764 -34.360 3.588  0.22 26.29  ? 1   TRP D CA  1 
ATOM   1133 C  C   A TRP B 2 2   ? 19.287 -34.186 3.316  0.78 29.39  ? 1   TRP D C   1 
ATOM   1134 C  C   B TRP B 2 2   ? 19.265 -34.179 3.394  0.22 29.30  ? 1   TRP D C   1 
ATOM   1135 O  O   A TRP B 2 2   ? 18.553 -35.185 3.288  0.78 29.08  ? 1   TRP D O   1 
ATOM   1136 O  O   B TRP B 2 2   ? 18.511 -35.155 3.467  0.22 28.82  ? 1   TRP D O   1 
ATOM   1137 C  CB  A TRP B 2 2   ? 21.576 -34.671 2.325  0.78 24.27  ? 1   TRP D CB  1 
ATOM   1138 C  CB  B TRP B 2 2   ? 21.467 -34.649 2.237  0.22 25.12  ? 1   TRP D CB  1 
ATOM   1139 C  CG  A TRP B 2 2   ? 23.074 -34.635 2.516  0.78 24.61  ? 1   TRP D CG  1 
ATOM   1140 C  CG  B TRP B 2 2   ? 20.817 -35.694 1.373  0.22 26.08  ? 1   TRP D CG  1 
ATOM   1141 C  CD1 A TRP B 2 2   ? 23.869 -35.642 2.982  0.78 27.42  ? 1   TRP D CD1 1 
ATOM   1142 C  CD1 B TRP B 2 2   ? 21.140 -37.016 1.309  0.22 29.12  ? 1   TRP D CD1 1 
ATOM   1143 C  CD2 A TRP B 2 2   ? 23.941 -33.517 2.278  0.78 24.00  ? 1   TRP D CD2 1 
ATOM   1144 C  CD2 B TRP B 2 2   ? 19.761 -35.493 0.418  0.22 25.87  ? 1   TRP D CD2 1 
ATOM   1145 N  NE1 A TRP B 2 2   ? 25.180 -35.212 3.065  0.78 26.68  ? 1   TRP D NE1 1 
ATOM   1146 N  NE1 B TRP B 2 2   ? 20.323 -37.662 0.413  0.22 28.66  ? 1   TRP D NE1 1 
ATOM   1147 C  CE2 A TRP B 2 2   ? 25.262 -33.938 2.570  0.78 27.62  ? 1   TRP D CE2 1 
ATOM   1148 C  CE2 B TRP B 2 2   ? 19.474 -36.750 -0.159 0.22 29.89  ? 1   TRP D CE2 1 
ATOM   1149 C  CE3 A TRP B 2 2   ? 23.734 -32.194 1.844  0.78 24.41  ? 1   TRP D CE3 1 
ATOM   1150 C  CE3 B TRP B 2 2   ? 19.007 -34.376 0.014  0.22 26.90  ? 1   TRP D CE3 1 
ATOM   1151 C  CZ2 A TRP B 2 2   ? 26.369 -33.088 2.431  0.78 26.24  ? 1   TRP D CZ2 1 
ATOM   1152 C  CZ2 B TRP B 2 2   ? 18.478 -36.920 -1.128 0.22 29.05  ? 1   TRP D CZ2 1 
ATOM   1153 C  CZ3 A TRP B 2 2   ? 24.838 -31.373 1.661  0.78 25.00  ? 1   TRP D CZ3 1 
ATOM   1154 C  CZ3 B TRP B 2 2   ? 18.012 -34.548 -0.936 0.22 28.50  ? 1   TRP D CZ3 1 
ATOM   1155 C  CH2 A TRP B 2 2   ? 26.132 -31.815 1.969  0.78 25.92  ? 1   TRP D CH2 1 
ATOM   1156 C  CH2 B TRP B 2 2   ? 17.761 -35.805 -1.503 0.22 29.03  ? 1   TRP D CH2 1 
ATOM   1157 N  N   . VAL B 2 3   ? 18.839 -32.939 3.122  1.00 25.04  ? 2   VAL D N   1 
ATOM   1158 C  CA  . VAL B 2 3   ? 17.428 -32.594 2.883  1.00 24.35  ? 2   VAL D CA  1 
ATOM   1159 C  C   . VAL B 2 3   ? 17.287 -31.546 1.779  1.00 26.13  ? 2   VAL D C   1 
ATOM   1160 O  O   . VAL B 2 3   ? 18.250 -30.846 1.440  1.00 24.68  ? 2   VAL D O   1 
ATOM   1161 C  CB  . VAL B 2 3   ? 16.714 -32.075 4.187  1.00 27.22  ? 2   VAL D CB  1 
ATOM   1162 C  CG1 . VAL B 2 3   ? 16.705 -33.123 5.303  1.00 27.19  ? 2   VAL D CG1 1 
ATOM   1163 C  CG2 . VAL B 2 3   ? 17.311 -30.741 4.685  1.00 26.79  ? 2   VAL D CG2 1 
ATOM   1164 N  N   . ILE B 2 4   ? 16.046 -31.371 1.309  1.00 23.56  ? 3   ILE D N   1 
ATOM   1165 C  CA  . ILE B 2 4   ? 15.684 -30.279 0.416  1.00 24.11  ? 3   ILE D CA  1 
ATOM   1166 C  C   . ILE B 2 4   ? 15.300 -29.142 1.397  1.00 27.37  ? 3   ILE D C   1 
ATOM   1167 O  O   . ILE B 2 4   ? 14.289 -29.282 2.105  1.00 26.29  ? 3   ILE D O   1 
ATOM   1168 C  CB  . ILE B 2 4   ? 14.480 -30.647 -0.491 1.00 26.06  ? 3   ILE D CB  1 
ATOM   1169 C  CG1 . ILE B 2 4   ? 14.749 -31.934 -1.349 1.00 24.93  ? 3   ILE D CG1 1 
ATOM   1170 C  CG2 . ILE B 2 4   ? 14.058 -29.425 -1.355 1.00 27.31  ? 3   ILE D CG2 1 
ATOM   1171 C  CD1 . ILE B 2 4   ? 16.039 -31.875 -2.325 1.00 28.44  ? 3   ILE D CD1 1 
ATOM   1172 N  N   . PRO B 2 5   ? 16.092 -28.054 1.497  1.00 26.77  ? 4   PRO D N   1 
ATOM   1173 C  CA  . PRO B 2 5   ? 15.753 -26.986 2.456  1.00 27.38  ? 4   PRO D CA  1 
ATOM   1174 C  C   . PRO B 2 5   ? 14.491 -26.207 2.081  1.00 31.47  ? 4   PRO D C   1 
ATOM   1175 O  O   . PRO B 2 5   ? 14.220 -26.016 0.897  1.00 30.90  ? 4   PRO D O   1 
ATOM   1176 C  CB  . PRO B 2 5   ? 17.000 -26.088 2.456  1.00 29.20  ? 4   PRO D CB  1 
ATOM   1177 C  CG  . PRO B 2 5   ? 17.583 -26.271 1.065  1.00 32.49  ? 4   PRO D CG  1 
ATOM   1178 C  CD  . PRO B 2 5   ? 17.312 -27.723 0.719  1.00 27.95  ? 4   PRO D CD  1 
ATOM   1179 N  N   . ALA B 2 6   ? 13.856 -25.578 3.084  1.00 29.32  ? 5   ALA D N   1 
HETATM 1180 C  C4  . 7ZO C 3 .   ? 27.300 -10.317 11.834 1.00 27.80  ? 201 7ZO A C4  1 
HETATM 1181 C  C5  . 7ZO C 3 .   ? 25.274 -9.396  12.199 1.00 29.67  ? 201 7ZO A C5  1 
HETATM 1182 C  C6  . 7ZO C 3 .   ? 23.973 -10.754 18.091 1.00 26.46  ? 201 7ZO A C6  1 
HETATM 1183 C  C7  . 7ZO C 3 .   ? 23.477 -9.456  18.147 1.00 27.59  ? 201 7ZO A C7  1 
HETATM 1184 C  C8  . 7ZO C 3 .   ? 25.533 -10.065 16.385 1.00 24.84  ? 201 7ZO A C8  1 
HETATM 1185 C  C10 . 7ZO C 3 .   ? 26.359 -10.243 14.018 1.00 25.35  ? 201 7ZO A C10 1 
HETATM 1186 C  C1  . 7ZO C 3 .   ? 23.953 -8.463  17.295 1.00 26.41  ? 201 7ZO A C1  1 
HETATM 1187 C  C2  . 7ZO C 3 .   ? 24.974 -8.783  16.405 1.00 25.30  ? 201 7ZO A C2  1 
HETATM 1188 C  C3  . 7ZO C 3 .   ? 24.998 -11.066 17.203 1.00 24.64  ? 201 7ZO A C3  1 
HETATM 1189 C  C9  . 7ZO C 3 .   ? 27.411 -10.626 13.179 1.00 25.79  ? 201 7ZO A C9  1 
HETATM 1190 C  C11 . 7ZO C 3 .   ? 22.258 -10.592 19.710 1.00 31.82  ? 201 7ZO A C11 1 
HETATM 1191 C  C12 . 7ZO C 3 .   ? 23.229 -11.581 19.100 1.00 28.98  ? 201 7ZO A C12 1 
HETATM 1192 N  N13 . 7ZO C 3 .   ? 26.234 -9.693  11.325 1.00 29.74  ? 201 7ZO A N13 1 
HETATM 1193 N  N14 . 7ZO C 3 .   ? 25.262 -9.632  13.516 1.00 28.17  ? 201 7ZO A N14 1 
HETATM 1194 N  N15 . 7ZO C 3 .   ? 22.472 -9.386  19.120 1.00 28.50  ? 201 7ZO A N15 1 
HETATM 1195 N  N16 . 7ZO C 3 .   ? 26.374 -10.533 15.349 1.00 23.67  ? 201 7ZO A N16 1 
HETATM 1196 O  O17 . 7ZO C 3 .   ? 21.416 -10.825 20.578 1.00 31.32  ? 201 7ZO A O17 1 
HETATM 1197 CL CL1 . 7ZO C 3 .   ? 28.835 -11.401 13.768 0.99 24.91  ? 201 7ZO A CL1 1 
HETATM 1198 CL CL  . CL  D 4 .   ? 21.317 -15.226 22.550 1.00 33.34  ? 202 CL  A CL  1 
HETATM 1199 S  S   A DMS E 5 .   ? 17.582 -35.385 -1.238 0.78 44.64  ? 101 DMS D S   1 
HETATM 1200 O  O   A DMS E 5 .   ? 16.306 -35.144 -0.576 0.78 46.30  ? 101 DMS D O   1 
HETATM 1201 C  C1  A DMS E 5 .   ? 18.730 -34.498 -0.214 0.78 42.64  ? 101 DMS D C1  1 
HETATM 1202 C  C2  A DMS E 5 .   ? 17.999 -37.029 -0.773 0.78 44.31  ? 101 DMS D C2  1 
HETATM 1203 O  O   . HOH F 6 .   ? 35.683 -25.713 25.562 1.00 38.64  ? 301 HOH A O   1 
HETATM 1204 O  O   . HOH F 6 .   ? 37.958 2.438   19.645 1.00 41.26  ? 302 HOH A O   1 
HETATM 1205 O  O   . HOH F 6 .   ? 25.875 -3.418  26.385 1.00 32.41  ? 303 HOH A O   1 
HETATM 1206 O  O   . HOH F 6 .   ? 44.486 -0.868  17.864 1.00 50.44  ? 304 HOH A O   1 
HETATM 1207 O  O   . HOH F 6 .   ? 41.319 -21.696 25.225 1.00 41.35  ? 305 HOH A O   1 
HETATM 1208 O  O   . HOH F 6 .   ? 38.406 -14.915 15.431 1.00 31.74  ? 306 HOH A O   1 
HETATM 1209 O  O   . HOH F 6 .   ? 33.322 -20.806 29.595 1.00 47.41  ? 307 HOH A O   1 
HETATM 1210 O  O   . HOH F 6 .   ? 22.759 -5.323  19.773 1.00 55.83  ? 308 HOH A O   1 
HETATM 1211 O  O   . HOH F 6 .   ? 19.910 -9.502  36.981 1.00 39.43  ? 309 HOH A O   1 
HETATM 1212 O  O   . HOH F 6 .   ? 45.018 -11.266 18.674 1.00 55.66  ? 310 HOH A O   1 
HETATM 1213 O  O   . HOH F 6 .   ? 27.252 -35.333 11.829 1.00 58.75  ? 311 HOH A O   1 
HETATM 1214 O  O   . HOH F 6 .   ? 43.643 -6.639  31.908 1.00 47.31  ? 312 HOH A O   1 
HETATM 1215 O  O   . HOH F 6 .   ? 16.563 -27.501 -3.285 1.00 53.95  ? 313 HOH A O   1 
HETATM 1216 O  O   . HOH F 6 .   ? 20.804 -5.875  25.977 1.00 40.74  ? 314 HOH A O   1 
HETATM 1217 O  O   . HOH F 6 .   ? 37.568 -20.382 26.994 1.00 32.77  ? 315 HOH A O   1 
HETATM 1218 O  O   . HOH F 6 .   ? 26.860 -31.941 16.167 1.00 46.65  ? 316 HOH A O   1 
HETATM 1219 O  O   . HOH F 6 .   ? 27.272 -10.125 35.849 1.00 39.40  ? 317 HOH A O   1 
HETATM 1220 O  O   . HOH F 6 .   ? 41.331 -16.970 15.151 1.00 35.07  ? 318 HOH A O   1 
HETATM 1221 O  O   . HOH F 6 .   ? 22.962 -28.258 12.639 1.00 24.43  ? 319 HOH A O   1 
HETATM 1222 O  O   . HOH F 6 .   ? 32.475 -24.714 32.177 1.00 59.11  ? 320 HOH A O   1 
HETATM 1223 O  O   . HOH F 6 .   ? 23.418 -5.717  32.885 1.00 38.41  ? 321 HOH A O   1 
HETATM 1224 O  O   . HOH F 6 .   ? 31.773 -0.802  15.847 1.00 38.07  ? 322 HOH A O   1 
HETATM 1225 O  O   . HOH F 6 .   ? 30.304 1.501   33.912 1.00 61.75  ? 323 HOH A O   1 
HETATM 1226 O  O   . HOH F 6 .   ? 43.606 -10.795 35.348 1.00 58.87  ? 324 HOH A O   1 
HETATM 1227 O  O   . HOH F 6 .   ? 20.459 -13.357 20.415 1.00 46.98  ? 325 HOH A O   1 
HETATM 1228 O  O   . HOH F 6 .   ? 13.510 -14.331 21.821 1.00 65.82  ? 326 HOH A O   1 
HETATM 1229 O  O   . HOH F 6 .   ? 29.909 -32.068 9.551  1.00 43.62  ? 327 HOH A O   1 
HETATM 1230 O  O   . HOH F 6 .   ? 17.996 -29.362 7.670  1.00 32.72  ? 328 HOH A O   1 
HETATM 1231 O  O   . HOH F 6 .   ? 22.583 -27.622 17.700 1.00 52.77  ? 329 HOH A O   1 
HETATM 1232 O  O   . HOH F 6 .   ? 41.641 -12.772 14.261 1.00 85.21  ? 330 HOH A O   1 
HETATM 1233 O  O   . HOH F 6 .   ? 30.297 -0.496  36.816 1.00 49.09  ? 331 HOH A O   1 
HETATM 1234 O  O   . HOH F 6 .   ? 32.327 -8.951  39.637 1.00 53.94  ? 332 HOH A O   1 
HETATM 1235 O  O   . HOH F 6 .   ? 26.822 -16.491 38.683 1.00 48.00  ? 333 HOH A O   1 
HETATM 1236 O  O   . HOH F 6 .   ? 19.057 -24.869 32.951 1.00 37.79  ? 334 HOH A O   1 
HETATM 1237 O  O   . HOH F 6 .   ? 21.927 -24.942 18.321 1.00 23.16  ? 335 HOH A O   1 
HETATM 1238 O  O   . HOH F 6 .   ? 34.920 -18.856 13.851 0.50 25.76  ? 336 HOH A O   1 
HETATM 1239 O  O   . HOH F 6 .   ? 14.266 -16.834 23.388 1.00 41.94  ? 337 HOH A O   1 
HETATM 1240 O  O   . HOH F 6 .   ? 27.328 -28.149 18.643 1.00 31.10  ? 338 HOH A O   1 
HETATM 1241 O  O   . HOH F 6 .   ? 26.038 -21.797 38.612 1.00 37.53  ? 339 HOH A O   1 
HETATM 1242 O  O   . HOH F 6 .   ? 4.361  -20.216 37.851 1.00 61.18  ? 340 HOH A O   1 
HETATM 1243 O  O   . HOH F 6 .   ? 7.081  -16.962 32.416 1.00 55.13  ? 341 HOH A O   1 
HETATM 1244 O  O   . HOH F 6 .   ? 12.595 -20.405 42.515 1.00 59.47  ? 342 HOH A O   1 
HETATM 1245 O  O   . HOH F 6 .   ? 29.556 -2.174  13.777 1.00 64.26  ? 343 HOH A O   1 
HETATM 1246 O  O   . HOH F 6 .   ? 25.756 -2.804  20.009 1.00 59.80  ? 344 HOH A O   1 
HETATM 1247 O  O   . HOH F 6 .   ? 15.439 -9.923  24.824 1.00 51.71  ? 345 HOH A O   1 
HETATM 1248 O  O   . HOH F 6 .   ? 26.129 -22.551 29.912 1.00 26.54  ? 346 HOH A O   1 
HETATM 1249 O  O   . HOH F 6 .   ? 28.260 -8.844  39.912 1.00 47.73  ? 347 HOH A O   1 
HETATM 1250 O  O   . HOH F 6 .   ? 29.011 -31.166 7.233  1.00 30.01  ? 348 HOH A O   1 
HETATM 1251 O  O   . HOH F 6 .   ? 41.327 -6.986  35.883 1.00 44.66  ? 349 HOH A O   1 
HETATM 1252 O  O   . HOH F 6 .   ? 23.180 -17.041 44.260 1.00 61.74  ? 350 HOH A O   1 
HETATM 1253 O  O   . HOH F 6 .   ? 27.236 -2.447  16.040 1.00 63.29  ? 351 HOH A O   1 
HETATM 1254 O  O   . HOH F 6 .   ? 28.193 -23.726 31.633 1.00 40.94  ? 352 HOH A O   1 
HETATM 1255 O  O   . HOH F 6 .   ? 43.960 -4.347  25.719 1.00 44.33  ? 353 HOH A O   1 
HETATM 1256 O  O   . HOH F 6 .   ? 29.385 -27.359 20.628 1.00 25.61  ? 354 HOH A O   1 
HETATM 1257 O  O   . HOH F 6 .   ? 36.845 -5.569  12.150 1.00 36.58  ? 355 HOH A O   1 
HETATM 1258 O  O   . HOH F 6 .   ? 41.195 -7.709  46.340 1.00 53.04  ? 356 HOH A O   1 
HETATM 1259 O  O   . HOH F 6 .   ? 44.493 -12.467 41.223 1.00 53.20  ? 357 HOH A O   1 
HETATM 1260 O  O   . HOH F 6 .   ? 46.052 -14.163 21.486 1.00 59.64  ? 358 HOH A O   1 
HETATM 1261 O  O   . HOH F 6 .   ? 21.467 -30.004 14.179 1.00 70.92  ? 359 HOH A O   1 
HETATM 1262 O  O   . HOH F 6 .   ? 20.847 -7.183  19.653 1.00 56.17  ? 360 HOH A O   1 
HETATM 1263 O  O   . HOH F 6 .   ? 21.460 -27.058 14.514 0.50 41.97  ? 361 HOH A O   1 
HETATM 1264 O  O   . HOH F 6 .   ? 28.519 -24.228 34.295 1.00 55.76  ? 362 HOH A O   1 
HETATM 1265 O  O   . HOH F 6 .   ? 46.233 -15.849 27.624 1.00 63.20  ? 363 HOH A O   1 
HETATM 1266 O  O   . HOH F 6 .   ? 24.865 -26.789 18.998 1.00 32.94  ? 364 HOH A O   1 
HETATM 1267 O  O   . HOH F 6 .   ? 42.451 -10.331 15.401 1.00 46.43  ? 365 HOH A O   1 
HETATM 1268 O  O   . HOH F 6 .   ? 30.732 -28.812 22.644 1.00 40.17  ? 366 HOH A O   1 
HETATM 1269 O  O   . HOH F 6 .   ? 25.875 -4.490  17.886 1.00 49.04  ? 367 HOH A O   1 
HETATM 1270 O  O   A HOH F 6 .   ? 19.073 -22.971 4.272  0.60 37.30  ? 368 HOH A O   1 
HETATM 1271 O  O   . HOH F 6 .   ? 24.046 -15.826 21.169 1.00 29.18  ? 369 HOH A O   1 
HETATM 1272 O  O   . HOH F 6 .   ? 39.074 -18.930 33.325 1.00 49.92  ? 370 HOH A O   1 
HETATM 1273 O  O   . HOH F 6 .   ? 47.220 -25.296 21.675 1.00 52.98  ? 371 HOH A O   1 
HETATM 1274 O  O   . HOH F 6 .   ? 22.255 -34.044 26.158 1.00 74.96  ? 372 HOH A O   1 
HETATM 1275 O  O   . HOH F 6 .   ? 10.819 -11.311 34.445 1.00 50.27  ? 373 HOH A O   1 
HETATM 1276 O  O   . HOH F 6 .   ? 46.276 -29.731 21.272 1.00 72.17  ? 374 HOH A O   1 
HETATM 1277 O  O   . HOH F 6 .   ? 37.390 -6.456  34.252 1.00 38.79  ? 375 HOH A O   1 
HETATM 1278 O  O   . HOH F 6 .   ? 22.686 -34.030 8.858  1.00 32.32  ? 376 HOH A O   1 
HETATM 1279 O  O   . HOH F 6 .   ? 46.877 -21.869 17.888 1.00 42.64  ? 377 HOH A O   1 
HETATM 1280 O  O   . HOH F 6 .   ? 34.143 -7.840  35.603 1.00 33.26  ? 378 HOH A O   1 
HETATM 1281 O  O   . HOH F 6 .   ? 46.251 -19.018 19.738 1.00 50.59  ? 379 HOH A O   1 
HETATM 1282 O  O   . HOH F 6 .   ? 27.642 -23.058 13.851 0.50 25.39  ? 380 HOH A O   1 
HETATM 1283 O  O   . HOH F 6 .   ? 26.376 -7.942  9.088  1.00 46.80  ? 381 HOH A O   1 
HETATM 1284 O  O   . HOH F 6 .   ? 18.052 -24.311 39.794 1.00 42.74  ? 382 HOH A O   1 
HETATM 1285 O  O   . HOH F 6 .   ? 45.246 -12.627 23.587 1.00 48.11  ? 383 HOH A O   1 
HETATM 1286 O  O   . HOH F 6 .   ? 44.760 -8.664  17.924 1.00 62.38  ? 384 HOH A O   1 
HETATM 1287 O  O   . HOH F 6 .   ? 26.026 -19.175 41.778 1.00 74.79  ? 385 HOH A O   1 
HETATM 1288 O  O   . HOH F 6 .   ? 11.361 -14.931 40.580 1.00 84.19  ? 386 HOH A O   1 
HETATM 1289 O  O   . HOH F 6 .   ? 20.120 -15.731 40.799 1.00 34.11  ? 387 HOH A O   1 
HETATM 1290 O  O   . HOH F 6 .   ? 18.048 -34.624 8.341  1.00 32.01  ? 388 HOH A O   1 
HETATM 1291 O  O   . HOH F 6 .   ? 33.056 -29.661 21.507 1.00 42.59  ? 389 HOH A O   1 
HETATM 1292 O  O   . HOH F 6 .   ? 40.352 -19.595 28.991 1.00 34.92  ? 390 HOH A O   1 
HETATM 1293 O  O   . HOH F 6 .   ? 46.049 -8.860  43.994 1.00 48.77  ? 391 HOH A O   1 
HETATM 1294 O  O   . HOH F 6 .   ? 17.468 -24.535 -2.287 1.00 62.43  ? 392 HOH A O   1 
HETATM 1295 O  O   . HOH F 6 .   ? 31.876 -31.859 14.574 1.00 43.15  ? 393 HOH A O   1 
HETATM 1296 O  O   . HOH F 6 .   ? 42.123 -6.130  11.812 1.00 64.78  ? 394 HOH A O   1 
HETATM 1297 O  O   . HOH F 6 .   ? 37.927 -16.263 12.765 1.00 47.20  ? 395 HOH A O   1 
HETATM 1298 O  O   . HOH F 6 .   ? 21.051 -23.067 42.060 1.00 47.85  ? 396 HOH A O   1 
HETATM 1299 O  O   . HOH F 6 .   ? 22.829 -14.770 40.320 1.00 33.39  ? 397 HOH A O   1 
HETATM 1300 O  O   . HOH F 6 .   ? 22.447 -10.042 14.400 1.00 40.31  ? 398 HOH A O   1 
HETATM 1301 O  O   . HOH F 6 .   ? 23.664 -15.703 17.813 1.00 42.22  ? 399 HOH A O   1 
HETATM 1302 O  O   . HOH F 6 .   ? 19.688 -27.428 10.028 1.00 59.57  ? 400 HOH A O   1 
HETATM 1303 O  O   . HOH F 6 .   ? 45.477 -10.546 30.382 1.00 58.33  ? 401 HOH A O   1 
HETATM 1304 O  O   . HOH F 6 .   ? 47.053 -20.173 22.030 1.00 64.12  ? 402 HOH A O   1 
HETATM 1305 O  O   . HOH F 6 .   ? 44.585 -16.445 29.693 1.00 49.58  ? 403 HOH A O   1 
HETATM 1306 O  O   . HOH F 6 .   ? 41.183 -17.094 35.203 1.00 43.39  ? 404 HOH A O   1 
HETATM 1307 O  O   . HOH F 6 .   ? 34.825 -33.335 21.888 1.00 59.27  ? 405 HOH A O   1 
HETATM 1308 O  O   . HOH F 6 .   ? 33.698 -33.068 12.284 1.00 42.01  ? 406 HOH A O   1 
HETATM 1309 O  O   . HOH F 6 .   ? 32.098 -15.597 39.799 1.00 34.88  ? 407 HOH A O   1 
HETATM 1310 O  O   . HOH F 6 .   ? 30.339 -10.494 40.563 1.00 41.34  ? 408 HOH A O   1 
HETATM 1311 O  O   . HOH F 6 .   ? 27.176 -1.580  21.968 1.00 50.39  ? 409 HOH A O   1 
HETATM 1312 O  O   . HOH F 6 .   ? 35.465 2.157   13.633 1.00 57.99  ? 410 HOH A O   1 
HETATM 1313 O  O   . HOH F 6 .   ? 25.940 -29.221 22.512 1.00 58.43  ? 411 HOH A O   1 
HETATM 1314 O  O   . HOH F 6 .   ? 37.139 -2.416  11.539 1.00 60.66  ? 412 HOH A O   1 
HETATM 1315 O  O   . HOH F 6 .   ? 35.227 -29.782 23.561 1.00 48.60  ? 413 HOH A O   1 
HETATM 1316 O  O   . HOH F 6 .   ? 29.690 -0.825  22.192 1.00 57.84  ? 414 HOH A O   1 
HETATM 1317 O  O   B HOH F 6 .   ? 37.264 -11.923 40.076 0.50 36.49  ? 415 HOH A O   1 
HETATM 1318 O  O   . HOH F 6 .   ? 41.997 -8.133  13.667 1.00 60.45  ? 416 HOH A O   1 
HETATM 1319 O  O   . HOH F 6 .   ? 39.918 -5.541  33.904 1.00 44.95  ? 417 HOH A O   1 
HETATM 1320 O  O   . HOH F 6 .   ? 33.518 -0.267  19.998 1.00 46.65  ? 418 HOH A O   1 
HETATM 1321 O  O   . HOH F 6 .   ? 28.353 -2.603  11.356 1.00 71.55  ? 419 HOH A O   1 
HETATM 1322 O  O   . HOH F 6 .   ? 44.270 -25.928 26.691 1.00 60.08  ? 420 HOH A O   1 
HETATM 1323 O  O   . HOH F 6 .   ? 28.731 -16.038 41.353 1.00 70.27  ? 421 HOH A O   1 
HETATM 1324 O  O   . HOH F 6 .   ? 10.296 -11.729 39.964 1.00 63.45  ? 422 HOH A O   1 
HETATM 1325 O  O   . HOH F 6 .   ? 33.888 -17.615 39.429 1.00 62.62  ? 423 HOH A O   1 
HETATM 1326 O  O   . HOH F 6 .   ? 23.432 -30.352 19.215 1.00 64.60  ? 424 HOH A O   1 
HETATM 1327 O  O   . HOH F 6 .   ? 27.445 -25.620 28.203 1.00 54.36  ? 425 HOH A O   1 
HETATM 1328 O  O   . HOH F 6 .   ? 25.600 -15.848 41.042 1.00 51.74  ? 426 HOH A O   1 
HETATM 1329 O  O   . HOH F 6 .   ? 45.833 -17.071 16.991 1.00 67.72  ? 427 HOH A O   1 
HETATM 1330 O  O   . HOH F 6 .   ? 42.835 -18.256 30.731 1.00 48.82  ? 428 HOH A O   1 
HETATM 1331 O  O   . HOH F 6 .   ? 29.814 -22.641 36.695 1.00 74.97  ? 429 HOH A O   1 
HETATM 1332 O  O   . HOH F 6 .   ? 45.747 -5.508  23.726 1.00 46.81  ? 430 HOH A O   1 
HETATM 1333 O  O   . HOH F 6 .   ? 44.867 -8.209  15.232 1.00 72.46  ? 431 HOH A O   1 
HETATM 1334 O  O   . HOH F 6 .   ? 32.008 0.163   13.311 1.00 57.77  ? 432 HOH A O   1 
HETATM 1335 O  O   . HOH F 6 .   ? 32.461 -4.089  41.210 1.00 63.53  ? 433 HOH A O   1 
HETATM 1336 O  O   . HOH F 6 .   ? 31.936 -26.273 27.048 1.00 46.23  ? 434 HOH A O   1 
HETATM 1337 O  O   . HOH F 6 .   ? 27.072 -34.521 17.959 1.00 73.12  ? 435 HOH A O   1 
HETATM 1338 O  O   . HOH F 6 .   ? 47.954 -23.402 19.865 1.00 66.64  ? 436 HOH A O   1 
HETATM 1339 O  O   . HOH F 6 .   ? 37.656 -27.114 28.471 1.00 61.86  ? 437 HOH A O   1 
HETATM 1340 O  O   . HOH F 6 .   ? 28.366 -29.216 26.765 1.00 81.42  ? 438 HOH A O   1 
HETATM 1341 O  O   . HOH F 6 .   ? 35.206 -4.099  10.607 1.00 46.40  ? 439 HOH A O   1 
HETATM 1342 O  O   . HOH F 6 .   ? 20.055 -35.270 10.149 1.00 41.60  ? 440 HOH A O   1 
HETATM 1343 O  O   . HOH F 6 .   ? 19.443 -31.815 13.985 1.00 71.34  ? 441 HOH A O   1 
HETATM 1344 O  O   . HOH F 6 .   ? 24.291 -21.502 41.029 1.00 53.84  ? 442 HOH A O   1 
HETATM 1345 O  O   . HOH F 6 .   ? 37.015 -24.449 27.553 1.00 57.00  ? 443 HOH A O   1 
HETATM 1346 O  O   . HOH F 6 .   ? 47.115 -12.998 28.504 1.00 60.90  ? 444 HOH A O   1 
HETATM 1347 O  O   . HOH F 6 .   ? 33.790 -10.875 41.552 0.50 54.64  ? 445 HOH A O   1 
HETATM 1348 O  O   . HOH F 6 .   ? 22.991 -2.707  26.163 1.00 63.97  ? 446 HOH A O   1 
HETATM 1349 O  O   . HOH F 6 .   ? 31.010 -34.428 14.787 1.00 62.32  ? 447 HOH A O   1 
HETATM 1350 O  O   . HOH F 6 .   ? 12.035 -18.528 22.358 1.00 59.71  ? 448 HOH A O   1 
HETATM 1351 O  O   . HOH F 6 .   ? 46.618 -14.653 17.964 1.00 69.86  ? 449 HOH A O   1 
HETATM 1352 O  O   . HOH F 6 .   ? 34.540 -18.844 36.118 1.00 63.12  ? 450 HOH A O   1 
HETATM 1353 O  O   A HOH F 6 .   ? 12.041 -20.627 27.874 0.78 47.61  ? 451 HOH A O   1 
HETATM 1354 O  O   . HOH F 6 .   ? 47.317 -28.604 17.685 1.00 61.00  ? 452 HOH A O   1 
HETATM 1355 O  O   . HOH F 6 .   ? 47.050 -11.883 25.486 1.00 65.90  ? 453 HOH A O   1 
HETATM 1356 O  O   . HOH F 6 .   ? 32.346 -1.069  22.302 1.00 62.11  ? 454 HOH A O   1 
HETATM 1357 O  O   . HOH F 6 .   ? 43.106 -3.034  33.735 1.00 59.16  ? 455 HOH A O   1 
HETATM 1358 O  O   . HOH F 6 .   ? 13.694 -16.166 39.847 1.00 74.57  ? 456 HOH A O   1 
HETATM 1359 O  O   . HOH F 6 .   ? 19.259 -7.538  35.248 1.00 58.90  ? 457 HOH A O   1 
HETATM 1360 O  O   . HOH F 6 .   ? 15.959 -15.525 41.205 1.00 59.96  ? 458 HOH A O   1 
HETATM 1361 O  O   . HOH F 6 .   ? 17.096 -28.132 9.886  1.00 53.29  ? 459 HOH A O   1 
HETATM 1362 O  O   . HOH F 6 .   ? 25.378 -5.698  35.209 1.00 56.27  ? 460 HOH A O   1 
HETATM 1363 O  O   . HOH F 6 .   ? 17.337 -8.047  24.762 1.00 57.29  ? 461 HOH A O   1 
HETATM 1364 O  O   . HOH F 6 .   ? 28.013 -29.855 24.146 1.00 66.94  ? 462 HOH A O   1 
HETATM 1365 O  O   . HOH F 6 .   ? 33.790 -13.923 41.553 0.50 41.07  ? 463 HOH A O   1 
HETATM 1366 O  O   . HOH F 6 .   ? 44.255 -13.467 13.851 0.50 67.18  ? 464 HOH A O   1 
HETATM 1367 O  O   . HOH F 6 .   ? 32.115 -23.864 34.756 1.00 65.46  ? 465 HOH A O   1 
HETATM 1368 O  O   . HOH F 6 .   ? 32.532 -20.487 36.975 1.00 70.53  ? 466 HOH A O   1 
HETATM 1369 O  O   . HOH F 6 .   ? 18.998 -28.049 13.851 0.50 68.81  ? 467 HOH A O   1 
HETATM 1370 O  O   . HOH F 6 .   ? 45.440 -12.780 16.220 1.00 71.79  ? 468 HOH A O   1 
HETATM 1371 O  O   . HOH F 6 .   ? 23.235 -4.540  17.192 1.00 72.40  ? 469 HOH A O   1 
HETATM 1372 O  O   . HOH F 6 .   ? 21.150 -5.637  34.727 1.00 59.30  ? 470 HOH A O   1 
HETATM 1373 O  O   . HOH F 6 .   ? 34.955 -23.688 32.785 1.00 63.83  ? 471 HOH A O   1 
HETATM 1374 O  O   . HOH F 6 .   ? 16.713 -6.657  34.617 1.00 77.09  ? 472 HOH A O   1 
HETATM 1375 O  O   . HOH F 6 .   ? 33.094 -0.575  42.949 1.00 60.46  ? 473 HOH A O   1 
HETATM 1376 O  O   . HOH G 6 .   ? 12.311 -24.285 0.021  1.00 48.76  ? 201 HOH D O   1 
HETATM 1377 O  O   . HOH G 6 .   ? 15.017 -25.798 -1.815 1.00 42.79  ? 202 HOH D O   1 
HETATM 1378 O  O   . HOH G 6 .   ? 11.698 -23.559 3.075  1.00 53.39  ? 203 HOH D O   1 
HETATM 1379 O  O   . HOH G 6 .   ? 20.995 -38.331 4.052  1.00 45.94  ? 204 HOH D O   1 
HETATM 1380 O  O   . HOH G 6 .   ? 17.768 -36.377 6.120  1.00 40.52  ? 205 HOH D O   1 
HETATM 1381 O  O   . HOH G 6 .   ? 20.904 -39.545 -2.223 1.00 62.12  ? 206 HOH D O   1 
HETATM 1382 O  O   . HOH G 6 .   ? 18.656 -40.727 0.675  1.00 69.77  ? 207 HOH D O   1 
HETATM 1383 O  O   . HOH G 6 .   ? 10.678 -24.830 5.527  1.00 56.48  ? 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   ? 0.8072 0.9957 0.6995 0.0388  -0.1286 -0.0268 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8033 0.9835 0.6778 0.0226  -0.1202 -0.0291 6   ASP A CA  
3    C C   . ASP A 5   ? 0.7856 0.9960 0.6839 0.0094  -0.1163 -0.0455 6   ASP A C   
4    O O   . ASP A 5   ? 0.7757 1.0149 0.7023 0.0125  -0.1213 -0.0552 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8258 0.9746 0.6905 0.0139  -0.1026 -0.0216 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0159 1.1424 0.8464 0.0050  -0.0977 -0.0170 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0193 1.1570 0.8473 -0.0065 -0.0955 -0.0259 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1211 1.2183 0.9273 0.0082  -0.0949 -0.0054 6   ASP A OD2 
9    N N   . SER A 6   ? 0.6839 0.8871 0.5706 -0.0058 -0.1067 -0.0495 7   SER A N   
10   C CA  . SER A 6   ? 0.6405 0.8644 0.5445 -0.0201 -0.1005 -0.0645 7   SER A CA  
11   C C   . SER A 6   ? 0.5908 0.7988 0.5059 -0.0316 -0.0816 -0.0660 7   SER A C   
12   O O   . SER A 6   ? 0.5829 0.7926 0.4997 -0.0449 -0.0731 -0.0750 7   SER A O   
13   C CB  . SER A 6   ? 0.7199 0.9482 0.6015 -0.0279 -0.1053 -0.0696 7   SER A CB  
14   O OG  . SER A 6   ? 0.8981 1.0966 0.7509 -0.0327 -0.0973 -0.0613 7   SER A OG  
15   N N   . CYS A 7   ? 0.4740 0.6662 0.3963 -0.0256 -0.0757 -0.0575 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4301 0.6067 0.3617 -0.0338 -0.0604 -0.0579 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4133 0.6054 0.3689 -0.0426 -0.0545 -0.0699 8   CYS A C   
18   O O   . CYS A 7   ? 0.3995 0.6155 0.3707 -0.0407 -0.0610 -0.0768 8   CYS A O   
19   C CB  . CYS A 7   ? 0.4431 0.6021 0.3763 -0.0249 -0.0575 -0.0469 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5242 0.6551 0.4266 -0.0196 -0.0577 -0.0332 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3041 0.4818 0.2624 -0.0520 -0.0420 -0.0726 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2623 0.4433 0.2382 -0.0602 -0.0341 -0.0809 9   ILE A CA  
23   C C   . ILE A 8   ? 0.2932 0.4566 0.2745 -0.0550 -0.0285 -0.0724 9   ILE A C   
24   O O   . ILE A 8   ? 0.2811 0.4287 0.2522 -0.0487 -0.0283 -0.0628 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3029 0.4782 0.2764 -0.0736 -0.0253 -0.0906 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3145 0.4656 0.2746 -0.0743 -0.0184 -0.0859 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3167 0.5143 0.2879 -0.0801 -0.0312 -0.1014 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3686 0.5094 0.3275 -0.0853 -0.0089 -0.0953 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2258 0.3906 0.2214 -0.0589 -0.0231 -0.0766 10  GLN A N   
30   N N   B GLN A 9   ? 0.2285 0.3954 0.2248 -0.0582 -0.0240 -0.0766 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2168 0.3650 0.2156 -0.0544 -0.0184 -0.0690 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2189 0.3705 0.2196 -0.0541 -0.0192 -0.0697 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2625 0.3952 0.2637 -0.0634 -0.0083 -0.0729 10  GLN A C   
34   C C   B GLN A 9   ? 0.2551 0.3897 0.2566 -0.0634 -0.0089 -0.0732 10  GLN A C   
35   O O   A GLN A 9   ? 0.2534 0.3939 0.2606 -0.0729 -0.0046 -0.0824 10  GLN A O   
36   O O   B GLN A 9   ? 0.2463 0.3864 0.2516 -0.0735 -0.0048 -0.0829 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2237 0.3866 0.2349 -0.0468 -0.0234 -0.0676 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2250 0.3937 0.2404 -0.0486 -0.0232 -0.0708 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2104 0.3575 0.2243 -0.0425 -0.0187 -0.0604 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.3489 0.5044 0.3703 -0.0480 -0.0163 -0.0671 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5556 0.7189 0.5844 -0.0375 -0.0211 -0.0629 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4435 0.5978 0.4668 -0.0357 -0.0208 -0.0587 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4390 0.6169 0.4806 -0.0448 -0.0177 -0.0728 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.2988 0.4625 0.3200 -0.0261 -0.0299 -0.0553 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.6038 0.7644 0.6314 -0.0256 -0.0263 -0.0549 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.2980 0.4384 0.3234 -0.0356 -0.0147 -0.0551 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2429 0.3530 0.2383 -0.0607 -0.0041 -0.0660 11  PHE A N   
48   N N   B PHE A 10  ? 0.2219 0.3349 0.2187 -0.0598 -0.0050 -0.0657 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2451 0.3364 0.2393 -0.0669 0.0036  -0.0681 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2258 0.3189 0.2207 -0.0655 0.0027  -0.0672 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2696 0.3580 0.2694 -0.0654 0.0055  -0.0650 11  PHE A C   
52   C C   B PHE A 10  ? 0.2653 0.3560 0.2661 -0.0646 0.0048  -0.0647 11  PHE A C   
53   O O   A PHE A 10  ? 0.2555 0.3369 0.2545 -0.0575 0.0037  -0.0569 11  PHE A O   
54   O O   B PHE A 10  ? 0.2518 0.3379 0.2528 -0.0566 0.0027  -0.0569 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2707 0.3411 0.2568 -0.0640 0.0059  -0.0643 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2509 0.3246 0.2378 -0.0614 0.0042  -0.0620 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2911 0.3401 0.2732 -0.0689 0.0118  -0.0671 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.2805 0.3525 0.2619 -0.0660 0.0059  -0.0682 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3375 0.3826 0.3163 -0.0782 0.0162  -0.0758 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3239 0.4102 0.3017 -0.0658 0.0021  -0.0697 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3216 0.3521 0.3009 -0.0641 0.0126  -0.0610 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3268 0.3813 0.3050 -0.0706 0.0114  -0.0728 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3635 0.3834 0.3348 -0.0821 0.0216  -0.0776 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3442 0.4289 0.3161 -0.0712 0.0048  -0.0765 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3597 0.3668 0.3314 -0.0672 0.0165  -0.0626 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3732 0.4257 0.3472 -0.0748 0.0139  -0.0798 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3403 0.3405 0.3072 -0.0758 0.0211  -0.0704 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3450 0.4136 0.3164 -0.0756 0.0111  -0.0819 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2254 0.3207 0.2308 -0.0740 0.0098  -0.0726 12  THR A N   
70   C CA  . THR A 11  ? 0.2311 0.3266 0.2422 -0.0755 0.0135  -0.0726 12  THR A CA  
71   C C   . THR A 11  ? 0.2832 0.3529 0.2853 -0.0717 0.0161  -0.0639 12  THR A C   
72   O O   . THR A 11  ? 0.2716 0.3440 0.2779 -0.0661 0.0150  -0.0594 12  THR A O   
73   C CB  . THR A 11  ? 0.3261 0.4262 0.3403 -0.0896 0.0212  -0.0839 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3084 0.4376 0.3338 -0.0924 0.0173  -0.0931 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3786 0.4798 0.3980 -0.0935 0.0271  -0.0858 12  THR A CG2 
76   N N   A ARG A 12  ? 0.2630 0.3084 0.2528 -0.0741 0.0188  -0.0621 13  ARG A N   
77   N N   B ARG A 12  ? 0.2643 0.3096 0.2542 -0.0741 0.0189  -0.0622 13  ARG A N   
78   C CA  A ARG A 12  ? 0.2766 0.2974 0.2566 -0.0704 0.0198  -0.0550 13  ARG A CA  
79   C CA  B ARG A 12  ? 0.2781 0.2990 0.2582 -0.0704 0.0198  -0.0550 13  ARG A CA  
80   C C   A ARG A 12  ? 0.3004 0.3186 0.2808 -0.0591 0.0139  -0.0474 13  ARG A C   
81   C C   B ARG A 12  ? 0.2993 0.3178 0.2799 -0.0591 0.0139  -0.0473 13  ARG A C   
82   O O   A ARG A 12  ? 0.2871 0.2879 0.2609 -0.0555 0.0134  -0.0425 13  ARG A O   
83   O O   B ARG A 12  ? 0.2841 0.2856 0.2583 -0.0555 0.0134  -0.0423 13  ARG A O   
84   C CB  A ARG A 12  ? 0.3368 0.3305 0.3025 -0.0767 0.0242  -0.0571 13  ARG A CB  
85   C CB  B ARG A 12  ? 0.3430 0.3370 0.3089 -0.0764 0.0240  -0.0569 13  ARG A CB  
86   C CG  A ARG A 12  ? 0.4544 0.4419 0.4143 -0.0904 0.0327  -0.0641 13  ARG A CG  
87   C CG  B ARG A 12  ? 0.4907 0.4731 0.4483 -0.0884 0.0322  -0.0613 13  ARG A CG  
88   C CD  A ARG A 12  ? 0.6031 0.5849 0.5593 -0.0938 0.0369  -0.0620 13  ARG A CD  
89   C CD  B ARG A 12  ? 0.5974 0.5667 0.5460 -0.0989 0.0380  -0.0686 13  ARG A CD  
90   N NE  A ARG A 12  ? 0.6881 0.6391 0.6270 -0.0897 0.0358  -0.0541 13  ARG A NE  
91   N NE  B ARG A 12  ? 0.6476 0.5938 0.5858 -0.0931 0.0351  -0.0659 13  ARG A NE  
92   C CZ  A ARG A 12  ? 0.7829 0.7271 0.7165 -0.0891 0.0370  -0.0498 13  ARG A CZ  
93   C CZ  B ARG A 12  ? 0.7691 0.7176 0.7090 -0.0949 0.0354  -0.0716 13  ARG A CZ  
94   N NH1 A ARG A 12  ? 0.5324 0.4982 0.4785 -0.0917 0.0401  -0.0529 13  ARG A NH1 
95   N NH1 B ARG A 12  ? 0.6706 0.5981 0.6027 -0.0885 0.0331  -0.0700 13  ARG A NH1 
96   N NH2 A ARG A 12  ? 0.6607 0.5769 0.5768 -0.0851 0.0344  -0.0430 13  ARG A NH2 
97   N NH2 B ARG A 12  ? 0.4691 0.4417 0.4189 -0.1028 0.0377  -0.0799 13  ARG A NH2 
98   N N   . HIS A 13  ? 0.2466 0.2812 0.2332 -0.0543 0.0097  -0.0469 14  HIS A N   
99   C CA  . HIS A 13  ? 0.2418 0.2737 0.2278 -0.0462 0.0062  -0.0411 14  HIS A CA  
100  C C   . HIS A 13  ? 0.2659 0.2931 0.2525 -0.0410 0.0053  -0.0349 14  HIS A C   
101  O O   . HIS A 13  ? 0.2615 0.2768 0.2450 -0.0375 0.0045  -0.0320 14  HIS A O   
102  C CB  . HIS A 13  ? 0.2378 0.2851 0.2256 -0.0437 0.0030  -0.0413 14  HIS A CB  
103  C CG  . HIS A 13  ? 0.2579 0.3001 0.2431 -0.0382 0.0019  -0.0369 14  HIS A CG  
104  N ND1 . HIS A 13  ? 0.2686 0.3020 0.2523 -0.0384 0.0036  -0.0395 14  HIS A ND1 
105  C CD2 . HIS A 13  ? 0.2698 0.3145 0.2541 -0.0332 0.0002  -0.0313 14  HIS A CD2 
106  C CE1 . HIS A 13  ? 0.2623 0.2957 0.2456 -0.0347 0.0035  -0.0363 14  HIS A CE1 
107  N NE2 . HIS A 13  ? 0.2631 0.3014 0.2450 -0.0322 0.0018  -0.0309 14  HIS A NE2 
108  N N   . ALA A 14  ? 0.2281 0.2661 0.2198 -0.0399 0.0051  -0.0338 15  ALA A N   
109  C CA  . ALA A 14  ? 0.2263 0.2595 0.2184 -0.0353 0.0051  -0.0286 15  ALA A CA  
110  C C   . ALA A 14  ? 0.2690 0.2844 0.2543 -0.0382 0.0078  -0.0277 15  ALA A C   
111  O O   . ALA A 14  ? 0.2442 0.2507 0.2266 -0.0344 0.0065  -0.0237 15  ALA A O   
112  C CB  . ALA A 14  ? 0.2371 0.2848 0.2370 -0.0332 0.0049  -0.0293 15  ALA A CB  
113  N N   A SER A 15  ? 0.2448 0.2542 0.2260 -0.0455 0.0115  -0.0318 16  SER A N   
114  N N   B SER A 15  ? 0.2493 0.2586 0.2304 -0.0455 0.0115  -0.0318 16  SER A N   
115  N N   C SER A 15  ? 0.2414 0.2507 0.2226 -0.0455 0.0115  -0.0318 16  SER A N   
116  C CA  A SER A 15  ? 0.2588 0.2470 0.2281 -0.0490 0.0138  -0.0305 16  SER A CA  
117  C CA  B SER A 15  ? 0.2657 0.2536 0.2347 -0.0491 0.0139  -0.0306 16  SER A CA  
118  C CA  C SER A 15  ? 0.2538 0.2417 0.2229 -0.0490 0.0138  -0.0305 16  SER A CA  
119  C C   A SER A 15  ? 0.3160 0.2879 0.2777 -0.0445 0.0095  -0.0280 16  SER A C   
120  C C   B SER A 15  ? 0.3214 0.2932 0.2830 -0.0446 0.0096  -0.0280 16  SER A C   
121  C C   C SER A 15  ? 0.3181 0.2896 0.2795 -0.0447 0.0096  -0.0280 16  SER A C   
122  O O   A SER A 15  ? 0.2906 0.2493 0.2451 -0.0415 0.0072  -0.0244 16  SER A O   
123  O O   B SER A 15  ? 0.3015 0.2598 0.2557 -0.0416 0.0073  -0.0245 16  SER A O   
124  O O   C SER A 15  ? 0.3020 0.2595 0.2556 -0.0419 0.0074  -0.0245 16  SER A O   
125  C CB  A SER A 15  ? 0.3062 0.2891 0.2698 -0.0595 0.0201  -0.0360 16  SER A CB  
126  C CB  B SER A 15  ? 0.3214 0.3038 0.2847 -0.0596 0.0201  -0.0360 16  SER A CB  
127  C CB  C SER A 15  ? 0.2952 0.2777 0.2585 -0.0596 0.0202  -0.0358 16  SER A CB  
128  O OG  A SER A 15  ? 0.3531 0.3107 0.2997 -0.0633 0.0225  -0.0337 16  SER A OG  
129  O OG  B SER A 15  ? 0.3824 0.3834 0.3561 -0.0637 0.0242  -0.0406 16  SER A OG  
130  O OG  C SER A 15  ? 0.3182 0.2994 0.2801 -0.0634 0.0208  -0.0401 16  SER A OG  
131  N N   . ASP A 16  ? 0.2907 0.2654 0.2551 -0.0437 0.0081  -0.0309 17  ASP A N   
132  C CA  . ASP A 16  ? 0.3084 0.2712 0.2696 -0.0382 0.0040  -0.0307 17  ASP A CA  
133  C C   . ASP A 16  ? 0.3009 0.2714 0.2694 -0.0309 0.0002  -0.0280 17  ASP A C   
134  O O   . ASP A 16  ? 0.3001 0.2607 0.2662 -0.0259 -0.0039 -0.0272 17  ASP A O   
135  C CB  . ASP A 16  ? 0.3276 0.2946 0.2920 -0.0397 0.0049  -0.0360 17  ASP A CB  
136  C CG  . ASP A 16  ? 0.4687 0.4230 0.4241 -0.0474 0.0091  -0.0401 17  ASP A CG  
137  O OD1 . ASP A 16  ? 0.4737 0.4129 0.4182 -0.0522 0.0118  -0.0386 17  ASP A OD1 
138  O OD2 . ASP A 16  ? 0.4759 0.4341 0.4335 -0.0500 0.0107  -0.0454 17  ASP A OD2 
139  N N   . VAL A 17  ? 0.2360 0.2237 0.2126 -0.0305 0.0013  -0.0269 18  VAL A N   
140  C CA  . VAL A 17  ? 0.2285 0.2212 0.2098 -0.0259 -0.0004 -0.0247 18  VAL A CA  
141  C C   . VAL A 17  ? 0.2719 0.2557 0.2491 -0.0246 -0.0016 -0.0215 18  VAL A C   
142  O O   . VAL A 17  ? 0.2592 0.2395 0.2374 -0.0210 -0.0047 -0.0218 18  VAL A O   
143  C CB  . VAL A 17  ? 0.2455 0.2521 0.2307 -0.0259 0.0013  -0.0230 18  VAL A CB  
144  C CG1 . VAL A 17  ? 0.2474 0.2542 0.2340 -0.0231 0.0016  -0.0201 18  VAL A CG1 
145  C CG2 . VAL A 17  ? 0.2351 0.2497 0.2216 -0.0272 0.0019  -0.0263 18  VAL A CG2 
146  N N   . LEU A 18  ? 0.2487 0.2300 0.2218 -0.0279 0.0010  -0.0196 19  LEU A N   
147  C CA  . LEU A 18  ? 0.2596 0.2322 0.2270 -0.0278 0.0008  -0.0171 19  LEU A CA  
148  C C   . LEU A 18  ? 0.3028 0.2578 0.2594 -0.0269 -0.0034 -0.0170 19  LEU A C   
149  O O   . LEU A 18  ? 0.2809 0.2313 0.2349 -0.0238 -0.0071 -0.0159 19  LEU A O   
150  C CB  . LEU A 18  ? 0.2710 0.2457 0.2370 -0.0324 0.0058  -0.0170 19  LEU A CB  
151  C CG  . LEU A 18  ? 0.3128 0.2813 0.2742 -0.0327 0.0072  -0.0151 19  LEU A CG  
152  C CD1 . LEU A 18  ? 0.3104 0.2870 0.2795 -0.0281 0.0067  -0.0134 19  LEU A CD1 
153  C CD2 . LEU A 18  ? 0.3652 0.3355 0.3258 -0.0381 0.0135  -0.0171 19  LEU A CD2 
154  N N   . LEU A 19  ? 0.2885 0.2329 0.2379 -0.0291 -0.0033 -0.0185 20  LEU A N   
155  C CA  . LEU A 19  ? 0.3165 0.2394 0.2522 -0.0266 -0.0083 -0.0178 20  LEU A CA  
156  C C   . LEU A 19  ? 0.3238 0.2507 0.2675 -0.0176 -0.0158 -0.0194 20  LEU A C   
157  O O   . LEU A 19  ? 0.3178 0.2348 0.2546 -0.0129 -0.0223 -0.0183 20  LEU A O   
158  C CB  . LEU A 19  ? 0.3499 0.2602 0.2773 -0.0306 -0.0057 -0.0198 20  LEU A CB  
159  C CG  . LEU A 19  ? 0.4727 0.3547 0.3816 -0.0275 -0.0107 -0.0183 20  LEU A CG  
160  C CD1 . LEU A 19  ? 0.5170 0.3790 0.4049 -0.0325 -0.0095 -0.0140 20  LEU A CD1 
161  C CD2 . LEU A 19  ? 0.5382 0.4080 0.4408 -0.0314 -0.0071 -0.0213 20  LEU A CD2 
162  N N   . ASN A 20  ? 0.2690 0.2123 0.2277 -0.0156 -0.0148 -0.0231 21  ASN A N   
163  C CA  . ASN A 20  ? 0.2681 0.2197 0.2381 -0.0085 -0.0199 -0.0272 21  ASN A CA  
164  C C   . ASN A 20  ? 0.2866 0.2482 0.2627 -0.0076 -0.0212 -0.0269 21  ASN A C   
165  O O   . ASN A 20  ? 0.2726 0.2360 0.2535 -0.0019 -0.0275 -0.0303 21  ASN A O   
166  C CB  . ASN A 20  ? 0.2799 0.2450 0.2616 -0.0090 -0.0163 -0.0320 21  ASN A CB  
167  C CG  . ASN A 20  ? 0.4106 0.3638 0.3878 -0.0074 -0.0173 -0.0350 21  ASN A CG  
168  O OD1 . ASN A 20  ? 0.3827 0.3163 0.3490 -0.0036 -0.0222 -0.0338 21  ASN A OD1 
169  N ND2 . ASN A 20  ? 0.3097 0.2718 0.2926 -0.0106 -0.0125 -0.0387 21  ASN A ND2 
170  N N   . LEU A 21  ? 0.2524 0.2208 0.2289 -0.0127 -0.0154 -0.0238 22  LEU A N   
171  C CA  . LEU A 21  ? 0.2482 0.2226 0.2281 -0.0132 -0.0152 -0.0235 22  LEU A CA  
172  C C   . LEU A 21  ? 0.2840 0.2454 0.2529 -0.0117 -0.0208 -0.0219 22  LEU A C   
173  O O   . LEU A 21  ? 0.2582 0.2237 0.2307 -0.0093 -0.0252 -0.0247 22  LEU A O   
174  C CB  . LEU A 21  ? 0.2405 0.2197 0.2203 -0.0178 -0.0081 -0.0199 22  LEU A CB  
175  C CG  . LEU A 21  ? 0.2697 0.2603 0.2567 -0.0188 -0.0038 -0.0208 22  LEU A CG  
176  C CD1 . LEU A 21  ? 0.2681 0.2604 0.2528 -0.0207 0.0009  -0.0165 22  LEU A CD1 
177  C CD2 . LEU A 21  ? 0.3028 0.3019 0.2983 -0.0185 -0.0033 -0.0255 22  LEU A CD2 
178  N N   . ASN A 22  ? 0.2606 0.2062 0.2146 -0.0140 -0.0204 -0.0181 23  ASN A N   
179  C CA  . ASN A 22  ? 0.2889 0.2183 0.2271 -0.0133 -0.0258 -0.0161 23  ASN A CA  
180  C C   . ASN A 22  ? 0.3434 0.2658 0.2794 -0.0046 -0.0370 -0.0185 23  ASN A C   
181  O O   . ASN A 22  ? 0.3454 0.2640 0.2756 -0.0013 -0.0444 -0.0190 23  ASN A O   
182  C CB  . ASN A 22  ? 0.3227 0.2347 0.2431 -0.0196 -0.0211 -0.0122 23  ASN A CB  
183  C CG  . ASN A 22  ? 0.4209 0.3163 0.3220 -0.0214 -0.0240 -0.0098 23  ASN A CG  
184  O OD1 . ASN A 22  ? 0.3810 0.2826 0.2845 -0.0209 -0.0260 -0.0106 23  ASN A OD1 
185  N ND2 . ASN A 22  ? 0.4424 0.3148 0.3220 -0.0247 -0.0238 -0.0070 23  ASN A ND2 
186  N N   . ARG A 23  ? 0.3095 0.2313 0.2510 -0.0001 -0.0389 -0.0209 24  ARG A N   
187  C CA  . ARG A 23  ? 0.3286 0.2455 0.2716 0.0105  -0.0500 -0.0245 24  ARG A CA  
188  C C   . ARG A 23  ? 0.3623 0.3025 0.3256 0.0149  -0.0543 -0.0314 24  ARG A C   
189  O O   . ARG A 23  ? 0.3616 0.3003 0.3241 0.0227  -0.0653 -0.0342 24  ARG A O   
190  C CB  . ARG A 23  ? 0.3100 0.2238 0.2578 0.0137  -0.0489 -0.0272 24  ARG A CB  
191  C CG  . ARG A 23  ? 0.4154 0.3016 0.3408 0.0103  -0.0467 -0.0221 24  ARG A CG  
192  C CD  . ARG A 23  ? 0.4517 0.3391 0.3839 0.0093  -0.0415 -0.0255 24  ARG A CD  
193  N NE  . ARG A 23  ? 0.5595 0.4184 0.4694 0.0053  -0.0391 -0.0219 24  ARG A NE  
194  C CZ  . ARG A 23  ? 0.8056 0.6597 0.7155 0.0017  -0.0333 -0.0245 24  ARG A CZ  
195  N NH1 . ARG A 23  ? 0.6136 0.4905 0.5441 0.0016  -0.0296 -0.0303 24  ARG A NH1 
196  N NH2 . ARG A 23  ? 0.6581 0.4836 0.5456 -0.0032 -0.0304 -0.0219 24  ARG A NH2 
197  N N   . LEU A 24  ? 0.3043 0.2652 0.2842 0.0094  -0.0457 -0.0346 25  LEU A N   
198  C CA  . LEU A 24  ? 0.2768 0.2591 0.2747 0.0102  -0.0468 -0.0420 25  LEU A CA  
199  C C   . LEU A 24  ? 0.3245 0.3051 0.3152 0.0082  -0.0504 -0.0408 25  LEU A C   
200  O O   . LEU A 24  ? 0.3215 0.3123 0.3208 0.0130  -0.0586 -0.0475 25  LEU A O   
201  C CB  . LEU A 24  ? 0.2552 0.2529 0.2649 0.0026  -0.0353 -0.0438 25  LEU A CB  
202  C CG  . LEU A 24  ? 0.2978 0.3012 0.3158 0.0030  -0.0308 -0.0469 25  LEU A CG  
203  C CD1 . LEU A 24  ? 0.2918 0.3071 0.3157 -0.0051 -0.0200 -0.0475 25  LEU A CD1 
204  C CD2 . LEU A 24  ? 0.3192 0.3317 0.3519 0.0115  -0.0376 -0.0568 25  LEU A CD2 
205  N N   . ARG A 25  ? 0.2880 0.2569 0.2637 0.0013  -0.0446 -0.0334 26  ARG A N   
206  C CA  . ARG A 25  ? 0.3017 0.2664 0.2679 -0.0015 -0.0470 -0.0325 26  ARG A CA  
207  C C   . ARG A 25  ? 0.3700 0.3223 0.3231 0.0062  -0.0611 -0.0327 26  ARG A C   
208  O O   . ARG A 25  ? 0.3667 0.3273 0.3229 0.0081  -0.0682 -0.0376 26  ARG A O   
209  C CB  . ARG A 25  ? 0.3134 0.2657 0.2650 -0.0092 -0.0381 -0.0254 26  ARG A CB  
210  C CG  . ARG A 25  ? 0.3670 0.3154 0.3091 -0.0131 -0.0392 -0.0257 26  ARG A CG  
211  C CD  . ARG A 25  ? 0.3897 0.3291 0.3215 -0.0205 -0.0292 -0.0210 26  ARG A CD  
212  N NE  . ARG A 25  ? 0.4082 0.3299 0.3231 -0.0218 -0.0282 -0.0160 26  ARG A NE  
213  C CZ  . ARG A 25  ? 0.5718 0.4773 0.4666 -0.0266 -0.0269 -0.0134 26  ARG A CZ  
214  N NH1 . ARG A 25  ? 0.5110 0.4154 0.3993 -0.0293 -0.0281 -0.0153 26  ARG A NH1 
215  N NH2 . ARG A 25  ? 0.4516 0.3412 0.3314 -0.0299 -0.0236 -0.0099 26  ARG A NH2 
216  N N   A SER A 26  ? 0.3621 0.2935 0.2990 0.0102  -0.0649 -0.0275 27  SER A N   
217  N N   B SER A 26  ? 0.3606 0.2918 0.2973 0.0103  -0.0650 -0.0275 27  SER A N   
218  N N   C SER A 26  ? 0.3550 0.2863 0.2919 0.0103  -0.0650 -0.0275 27  SER A N   
219  C CA  A SER A 26  ? 0.3956 0.3079 0.3139 0.0185  -0.0787 -0.0257 27  SER A CA  
220  C CA  B SER A 26  ? 0.3933 0.3053 0.3112 0.0185  -0.0788 -0.0257 27  SER A CA  
221  C CA  C SER A 26  ? 0.3855 0.2972 0.3033 0.0185  -0.0787 -0.0256 27  SER A CA  
222  C C   A SER A 26  ? 0.4470 0.3760 0.3829 0.0301  -0.0917 -0.0345 27  SER A C   
223  C C   B SER A 26  ? 0.4509 0.3779 0.3855 0.0308  -0.0924 -0.0341 27  SER A C   
224  C C   C SER A 26  ? 0.4465 0.3731 0.3808 0.0309  -0.0923 -0.0340 27  SER A C   
225  O O   A SER A 26  ? 0.4581 0.3848 0.3860 0.0354  -0.1039 -0.0362 27  SER A O   
226  O O   B SER A 26  ? 0.4679 0.3881 0.3915 0.0378  -0.1058 -0.0349 27  SER A O   
227  O O   C SER A 26  ? 0.4631 0.3822 0.3860 0.0379  -0.1058 -0.0346 27  SER A O   
228  C CB  A SER A 26  ? 0.4659 0.3531 0.3674 0.0210  -0.0787 -0.0201 27  SER A CB  
229  C CB  B SER A 26  ? 0.4608 0.3446 0.3573 0.0192  -0.0781 -0.0188 27  SER A CB  
230  C CB  C SER A 26  ? 0.4449 0.3297 0.3432 0.0195  -0.0777 -0.0191 27  SER A CB  
231  O OG  A SER A 26  ? 0.5798 0.4478 0.4598 0.0106  -0.0693 -0.0130 27  SER A OG  
232  O OG  B SER A 26  ? 0.5363 0.4240 0.4460 0.0251  -0.0782 -0.0218 27  SER A OG  
233  O OG  C SER A 26  ? 0.5462 0.4066 0.4220 0.0284  -0.0913 -0.0162 27  SER A OG  
234  N N   . ARG A 27  ? 0.3868 0.3348 0.3476 0.0336  -0.0890 -0.0412 28  ARG A N   
235  C CA  . ARG A 27  ? 0.3949 0.3627 0.3777 0.0447  -0.0998 -0.0522 28  ARG A CA  
236  C C   . ARG A 27  ? 0.4069 0.4061 0.4134 0.0393  -0.0964 -0.0621 28  ARG A C   
237  O O   . ARG A 27  ? 0.4016 0.4234 0.4309 0.0463  -0.1034 -0.0739 28  ARG A O   
238  C CB  . ARG A 27  ? 0.4266 0.3966 0.4224 0.0505  -0.0976 -0.0556 28  ARG A CB  
239  C CG  . ARG A 27  ? 0.5613 0.4976 0.5320 0.0550  -0.1005 -0.0467 28  ARG A CG  
240  C CD  . ARG A 27  ? 0.6492 0.5868 0.6316 0.0581  -0.0955 -0.0503 28  ARG A CD  
241  N NE  . ARG A 27  ? 0.8519 0.8040 0.8554 0.0723  -0.1063 -0.0614 28  ARG A NE  
242  C CZ  . ARG A 27  ? 1.0540 1.0271 1.0829 0.0734  -0.1004 -0.0713 28  ARG A CZ  
243  N NH1 . ARG A 27  ? 0.9193 0.9073 0.9693 0.0869  -0.1102 -0.0830 28  ARG A NH1 
244  N NH2 . ARG A 27  ? 0.8806 0.8607 0.9141 0.0612  -0.0850 -0.0702 28  ARG A NH2 
245  N N   . ASP A 28  ? 0.3328 0.3327 0.3337 0.0266  -0.0855 -0.0583 29  ASP A N   
246  C CA  . ASP A 28  ? 0.3331 0.3562 0.3505 0.0183  -0.0792 -0.0662 29  ASP A CA  
247  C C   . ASP A 28  ? 0.3702 0.4164 0.4139 0.0156  -0.0704 -0.0754 29  ASP A C   
248  O O   . ASP A 28  ? 0.3673 0.4372 0.4308 0.0130  -0.0700 -0.0872 29  ASP A O   
249  C CB  . ASP A 28  ? 0.3695 0.4029 0.3894 0.0226  -0.0926 -0.0738 29  ASP A CB  
250  C CG  . ASP A 28  ? 0.4607 0.5101 0.4890 0.0110  -0.0848 -0.0800 29  ASP A CG  
251  O OD1 . ASP A 28  ? 0.4547 0.4945 0.4738 0.0002  -0.0712 -0.0735 29  ASP A OD1 
252  O OD2 . ASP A 28  ? 0.5104 0.5817 0.5547 0.0126  -0.0923 -0.0922 29  ASP A OD2 
253  N N   . ILE A 29  ? 0.2998 0.3390 0.3424 0.0150  -0.0629 -0.0708 30  ILE A N   
254  C CA  . ILE A 29  ? 0.2761 0.3335 0.3388 0.0118  -0.0539 -0.0787 30  ILE A CA  
255  C C   . ILE A 29  ? 0.3153 0.3734 0.3751 -0.0013 -0.0386 -0.0752 30  ILE A C   
256  O O   . ILE A 29  ? 0.2890 0.3301 0.3323 -0.0047 -0.0333 -0.0642 30  ILE A O   
257  C CB  . ILE A 29  ? 0.3138 0.3644 0.3775 0.0190  -0.0553 -0.0776 30  ILE A CB  
258  C CG1 . ILE A 29  ? 0.3349 0.3841 0.4030 0.0342  -0.0713 -0.0827 30  ILE A CG1 
259  C CG2 . ILE A 29  ? 0.2921 0.3597 0.3729 0.0134  -0.0438 -0.0853 30  ILE A CG2 
260  C CD1 . ILE A 29  ? 0.3771 0.4090 0.4379 0.0415  -0.0731 -0.0788 30  ILE A CD1 
261  N N   A LEU A 30  ? 0.2748 0.3520 0.3502 -0.0086 -0.0315 -0.0852 31  LEU A N   
262  N N   B LEU A 30  ? 0.2841 0.3614 0.3596 -0.0085 -0.0315 -0.0852 31  LEU A N   
263  C CA  A LEU A 30  ? 0.2677 0.3437 0.3392 -0.0210 -0.0167 -0.0831 31  LEU A CA  
264  C CA  B LEU A 30  ? 0.2827 0.3591 0.3545 -0.0210 -0.0168 -0.0834 31  LEU A CA  
265  C C   A LEU A 30  ? 0.3082 0.3681 0.3620 -0.0262 -0.0135 -0.0737 31  LEU A C   
266  C C   B LEU A 30  ? 0.3172 0.3772 0.3712 -0.0262 -0.0135 -0.0738 31  LEU A C   
267  O O   A LEU A 30  ? 0.2878 0.3393 0.3332 -0.0336 -0.0026 -0.0685 31  LEU A O   
268  O O   B LEU A 30  ? 0.2992 0.3510 0.3448 -0.0336 -0.0026 -0.0686 31  LEU A O   
269  C CB  A LEU A 30  ? 0.2680 0.3389 0.3357 -0.0231 -0.0083 -0.0788 31  LEU A CB  
270  C CB  B LEU A 30  ? 0.2874 0.3594 0.3561 -0.0233 -0.0082 -0.0796 31  LEU A CB  
271  C CG  A LEU A 30  ? 0.3245 0.4130 0.4102 -0.0226 -0.0055 -0.0905 31  LEU A CG  
272  C CG  B LEU A 30  ? 0.3537 0.4446 0.4394 -0.0285 -0.0004 -0.0921 31  LEU A CG  
273  C CD1 A LEU A 30  ? 0.3050 0.3880 0.3827 -0.0297 0.0062  -0.0867 31  LEU A CD1 
274  C CD1 B LEU A 30  ? 0.3571 0.4551 0.4538 -0.0200 -0.0054 -0.0973 31  LEU A CD1 
275  C CD2 A LEU A 30  ? 0.3623 0.4736 0.4678 -0.0280 -0.0026 -0.1058 31  LEU A CD2 
276  C CD2 B LEU A 30  ? 0.3820 0.4655 0.4568 -0.0400 0.0140  -0.0882 31  LEU A CD2 
277  N N   . THR A 31  ? 0.2819 0.3372 0.3298 -0.0223 -0.0229 -0.0725 32  THR A N   
278  C CA  . THR A 31  ? 0.2828 0.3247 0.3158 -0.0278 -0.0194 -0.0662 32  THR A CA  
279  C C   . THR A 31  ? 0.3460 0.3992 0.3879 -0.0381 -0.0108 -0.0751 32  THR A C   
280  O O   . THR A 31  ? 0.3340 0.4075 0.3934 -0.0392 -0.0130 -0.0875 32  THR A O   
281  C CB  . THR A 31  ? 0.3635 0.3981 0.3863 -0.0225 -0.0312 -0.0643 32  THR A CB  
282  O OG1 . THR A 31  ? 0.3729 0.4246 0.4094 -0.0177 -0.0418 -0.0751 32  THR A OG1 
283  C CG2 . THR A 31  ? 0.3316 0.3486 0.3397 -0.0154 -0.0365 -0.0544 32  THR A CG2 
284  N N   . ASP A 32  ? 0.3098 0.3501 0.3407 -0.0458 0.0001  -0.0697 33  ASP A N   
285  C CA  . ASP A 32  ? 0.3094 0.3542 0.3444 -0.0572 0.0111  -0.0770 33  ASP A CA  
286  C C   . ASP A 32  ? 0.3390 0.3715 0.3627 -0.0633 0.0154  -0.0754 33  ASP A C   
287  O O   . ASP A 32  ? 0.3438 0.3731 0.3661 -0.0737 0.0264  -0.0798 33  ASP A O   
288  C CB  . ASP A 32  ? 0.3255 0.3634 0.3566 -0.0616 0.0228  -0.0732 33  ASP A CB  
289  C CG  . ASP A 32  ? 0.4295 0.4472 0.4441 -0.0570 0.0247  -0.0590 33  ASP A CG  
290  O OD1 . ASP A 32  ? 0.3778 0.3860 0.3844 -0.0524 0.0198  -0.0527 33  ASP A OD1 
291  O OD2 . ASP A 32  ? 0.5354 0.5478 0.5452 -0.0582 0.0309  -0.0549 33  ASP A OD2 
292  N N   . VAL A 33  ? 0.2770 0.3009 0.2911 -0.0579 0.0077  -0.0699 34  VAL A N   
293  C CA  . VAL A 33  ? 0.2858 0.2984 0.2890 -0.0637 0.0117  -0.0697 34  VAL A CA  
294  C C   . VAL A 33  ? 0.3323 0.3435 0.3283 -0.0586 0.0000  -0.0688 34  VAL A C   
295  O O   . VAL A 33  ? 0.3225 0.3318 0.3153 -0.0499 -0.0089 -0.0633 34  VAL A O   
296  C CB  . VAL A 33  ? 0.3321 0.3228 0.3218 -0.0651 0.0228  -0.0596 34  VAL A CB  
297  C CG1 . VAL A 33  ? 0.3137 0.2947 0.2950 -0.0562 0.0183  -0.0491 34  VAL A CG1 
298  C CG2 . VAL A 33  ? 0.3377 0.3167 0.3188 -0.0731 0.0306  -0.0623 34  VAL A CG2 
299  N N   A VAL A 34  ? 0.2976 0.3074 0.2886 -0.0650 0.0007  -0.0742 35  VAL A N   
300  N N   B VAL A 34  ? 0.3020 0.3118 0.2929 -0.0650 0.0006  -0.0742 35  VAL A N   
301  C CA  A VAL A 34  ? 0.2974 0.3015 0.2758 -0.0627 -0.0085 -0.0732 35  VAL A CA  
302  C CA  B VAL A 34  ? 0.3045 0.3083 0.2827 -0.0622 -0.0087 -0.0728 35  VAL A CA  
303  C C   A VAL A 34  ? 0.3498 0.3343 0.3134 -0.0681 0.0022  -0.0684 35  VAL A C   
304  C C   B VAL A 34  ? 0.3549 0.3398 0.3183 -0.0681 0.0016  -0.0687 35  VAL A C   
305  O O   A VAL A 34  ? 0.3515 0.3327 0.3166 -0.0763 0.0130  -0.0725 35  VAL A O   
306  O O   B VAL A 34  ? 0.3573 0.3397 0.3223 -0.0766 0.0118  -0.0736 35  VAL A O   
307  C CB  A VAL A 34  ? 0.3440 0.3653 0.3287 -0.0655 -0.0181 -0.0857 35  VAL A CB  
308  C CB  B VAL A 34  ? 0.3560 0.3770 0.3399 -0.0619 -0.0216 -0.0836 35  VAL A CB  
309  C CG1 A VAL A 34  ? 0.3559 0.3676 0.3219 -0.0639 -0.0275 -0.0838 35  VAL A CG1 
310  C CG1 B VAL A 34  ? 0.3593 0.3907 0.3509 -0.0737 -0.0151 -0.0958 35  VAL A CG1 
311  C CG2 A VAL A 34  ? 0.3349 0.3781 0.3378 -0.0584 -0.0290 -0.0923 35  VAL A CG2 
312  C CG2 B VAL A 34  ? 0.3683 0.3782 0.3330 -0.0573 -0.0329 -0.0794 35  VAL A CG2 
313  N N   . ILE A 35  ? 0.3095 0.2803 0.2589 -0.0639 0.0002  -0.0604 36  ILE A N   
314  C CA  . ILE A 35  ? 0.3190 0.2732 0.2559 -0.0681 0.0097  -0.0575 36  ILE A CA  
315  C C   . ILE A 35  ? 0.3829 0.3345 0.3061 -0.0718 0.0031  -0.0620 36  ILE A C   
316  O O   . ILE A 35  ? 0.3748 0.3253 0.2886 -0.0672 -0.0081 -0.0594 36  ILE A O   
317  C CB  . ILE A 35  ? 0.3436 0.2866 0.2752 -0.0625 0.0137  -0.0478 36  ILE A CB  
318  C CG1 . ILE A 35  ? 0.3294 0.2765 0.2728 -0.0577 0.0171  -0.0431 36  ILE A CG1 
319  C CG2 . ILE A 35  ? 0.3683 0.2972 0.2906 -0.0663 0.0239  -0.0472 36  ILE A CG2 
320  C CD1 . ILE A 35  ? 0.3145 0.2601 0.2648 -0.0618 0.0272  -0.0454 36  ILE A CD1 
321  N N   . VAL A 36  ? 0.3529 0.3015 0.2728 -0.0805 0.0099  -0.0689 37  VAL A N   
322  C CA  . VAL A 36  ? 0.3676 0.3139 0.2731 -0.0858 0.0045  -0.0747 37  VAL A CA  
323  C C   . VAL A 36  ? 0.4321 0.3592 0.3215 -0.0891 0.0141  -0.0713 37  VAL A C   
324  O O   . VAL A 36  ? 0.4156 0.3342 0.3084 -0.0922 0.0277  -0.0715 37  VAL A O   
325  C CB  . VAL A 36  ? 0.4162 0.3744 0.3294 -0.0949 0.0055  -0.0872 37  VAL A CB  
326  C CG1 . VAL A 36  ? 0.4351 0.3916 0.3320 -0.1009 -0.0008 -0.0939 37  VAL A CG1 
327  C CG2 . VAL A 36  ? 0.4132 0.3942 0.3456 -0.0921 -0.0032 -0.0929 37  VAL A CG2 
328  N N   . VAL A 37  ? 0.4009 0.3199 0.2716 -0.0884 0.0074  -0.0684 38  VAL A N   
329  C CA  . VAL A 37  ? 0.4212 0.3233 0.2754 -0.0925 0.0166  -0.0665 38  VAL A CA  
330  C C   . VAL A 37  ? 0.4965 0.3936 0.3287 -0.0990 0.0094  -0.0718 38  VAL A C   
331  O O   . VAL A 37  ? 0.4752 0.3695 0.2926 -0.0957 -0.0032 -0.0682 38  VAL A O   
332  C CB  . VAL A 37  ? 0.4713 0.3663 0.3220 -0.0865 0.0179  -0.0574 38  VAL A CB  
333  C CG1 . VAL A 37  ? 0.4776 0.3591 0.3178 -0.0916 0.0309  -0.0579 38  VAL A CG1 
334  C CG2 . VAL A 37  ? 0.4485 0.3523 0.3207 -0.0789 0.0199  -0.0525 38  VAL A CG2 
335  N N   A SER A 38  ? 0.4887 0.3797 0.3136 -0.1084 0.0185  -0.0793 39  SER A N   
336  N N   B SER A 38  ? 0.4574 0.3571 0.2914 -0.1072 0.0148  -0.0811 39  SER A N   
337  C CA  A SER A 38  ? 0.5198 0.4049 0.3205 -0.1159 0.0124  -0.0849 39  SER A CA  
338  C CA  B SER A 38  ? 0.4691 0.3687 0.2871 -0.1155 0.0094  -0.0897 39  SER A CA  
339  C C   A SER A 38  ? 0.5737 0.4704 0.3694 -0.1115 -0.0087 -0.0859 39  SER A C   
340  C C   B SER A 38  ? 0.5002 0.4152 0.3187 -0.1109 -0.0107 -0.0919 39  SER A C   
341  O O   A SER A 38  ? 0.5787 0.4652 0.3495 -0.1106 -0.0192 -0.0825 39  SER A O   
342  O O   B SER A 38  ? 0.4690 0.4023 0.3098 -0.1090 -0.0138 -0.0966 39  SER A O   
343  C CB  A SER A 38  ? 0.6049 0.4708 0.3813 -0.1194 0.0184  -0.0809 39  SER A CB  
344  C CB  B SER A 38  ? 0.5381 0.4186 0.3292 -0.1214 0.0149  -0.0889 39  SER A CB  
345  O OG  A SER A 38  ? 0.7489 0.6064 0.5293 -0.1243 0.0371  -0.0839 39  SER A OG  
346  O OG  B SER A 38  ? 0.6070 0.4785 0.4041 -0.1258 0.0338  -0.0912 39  SER A OG  
347  N N   A ARG A 39  ? 0.5174 0.4346 0.3367 -0.1082 -0.0147 -0.0906 40  ARG A N   
348  N N   B ARG A 39  ? 0.4739 0.3814 0.2685 -0.1083 -0.0243 -0.0888 40  ARG A N   
349  C CA  A ARG A 39  ? 0.5204 0.4548 0.3440 -0.1021 -0.0346 -0.0941 40  ARG A CA  
350  C CA  B ARG A 39  ? 0.4798 0.4022 0.2763 -0.1010 -0.0453 -0.0911 40  ARG A CA  
351  C C   A ARG A 39  ? 0.5571 0.4866 0.3742 -0.0895 -0.0476 -0.0836 40  ARG A C   
352  C C   B ARG A 39  ? 0.5271 0.4570 0.3416 -0.0883 -0.0515 -0.0837 40  ARG A C   
353  O O   A ARG A 39  ? 0.5685 0.5016 0.3753 -0.0832 -0.0663 -0.0844 40  ARG A O   
354  O O   B ARG A 39  ? 0.5127 0.4648 0.3514 -0.0838 -0.0582 -0.0894 40  ARG A O   
355  C CB  A ARG A 39  ? 0.5548 0.4929 0.3615 -0.1086 -0.0451 -0.1037 40  ARG A CB  
356  C CB  B ARG A 39  ? 0.5099 0.4191 0.2716 -0.1014 -0.0598 -0.0902 40  ARG A CB  
357  C CG  A ARG A 39  ? 0.6880 0.6363 0.5054 -0.1210 -0.0352 -0.1169 40  ARG A CG  
358  C CG  B ARG A 39  ? 0.6139 0.5231 0.3618 -0.1140 -0.0572 -0.1010 40  ARG A CG  
359  C CD  A ARG A 39  ? 0.7680 0.7295 0.5758 -0.1249 -0.0511 -0.1281 40  ARG A CD  
360  C CD  B ARG A 39  ? 0.6252 0.5240 0.3379 -0.1139 -0.0747 -0.1012 40  ARG A CD  
361  N NE  A ARG A 39  ? 0.8542 0.8215 0.6661 -0.1395 -0.0404 -0.1417 40  ARG A NE  
362  N NE  B ARG A 39  ? 0.6388 0.5363 0.3363 -0.1275 -0.0704 -0.1119 40  ARG A NE  
363  C CZ  A ARG A 39  ? 1.0311 0.9814 0.8203 -0.1503 -0.0316 -0.1448 40  ARG A CZ  
364  C CZ  B ARG A 39  ? 0.8055 0.7244 0.5110 -0.1310 -0.0808 -0.1248 40  ARG A CZ  
365  N NH1 A ARG A 39  ? 0.8642 0.7915 0.6251 -0.1488 -0.0311 -0.1356 40  ARG A NH1 
366  N NH1 B ARG A 39  ? 0.6267 0.5722 0.3576 -0.1216 -0.0959 -0.1295 40  ARG A NH1 
367  N NH2 A ARG A 39  ? 0.8652 0.8208 0.6594 -0.1637 -0.0217 -0.1581 40  ARG A NH2 
368  N NH2 B ARG A 39  ? 0.7086 0.6239 0.3979 -0.1445 -0.0755 -0.1346 40  ARG A NH2 
369  N N   A GLU A 40  ? 0.4748 0.3952 0.2972 -0.0856 -0.0381 -0.0744 41  GLU A N   
370  N N   B GLU A 40  ? 0.4654 0.3780 0.2703 -0.0843 -0.0463 -0.0726 41  GLU A N   
371  C CA  A GLU A 40  ? 0.4656 0.3808 0.2855 -0.0750 -0.0466 -0.0651 41  GLU A CA  
372  C CA  B GLU A 40  ? 0.4444 0.3597 0.2612 -0.0733 -0.0512 -0.0650 41  GLU A CA  
373  C C   A GLU A 40  ? 0.4666 0.3973 0.3173 -0.0704 -0.0406 -0.0646 41  GLU A C   
374  C C   B GLU A 40  ? 0.4482 0.3818 0.2983 -0.0710 -0.0434 -0.0671 41  GLU A C   
375  O O   A GLU A 40  ? 0.4272 0.3577 0.2891 -0.0753 -0.0252 -0.0649 41  GLU A O   
376  O O   B GLU A 40  ? 0.4016 0.3377 0.2627 -0.0780 -0.0291 -0.0705 41  GLU A O   
377  C CB  A GLU A 40  ? 0.4986 0.3890 0.2949 -0.0771 -0.0391 -0.0560 41  GLU A CB  
378  C CB  B GLU A 40  ? 0.4726 0.3648 0.2706 -0.0729 -0.0447 -0.0543 41  GLU A CB  
379  C CG  A GLU A 40  ? 0.6977 0.5697 0.4586 -0.0825 -0.0450 -0.0560 41  GLU A CG  
380  C CG  B GLU A 40  ? 0.6863 0.5560 0.4480 -0.0797 -0.0456 -0.0528 41  GLU A CG  
381  C CD  A GLU A 40  ? 1.1373 0.9904 0.8718 -0.0761 -0.0579 -0.0475 41  GLU A CD  
382  C CD  B GLU A 40  ? 1.1516 1.0028 0.8841 -0.0738 -0.0609 -0.0459 41  GLU A CD  
383  O OE1 A GLU A 40  ? 1.1756 1.0053 0.8840 -0.0821 -0.0502 -0.0422 41  GLU A OE1 
384  O OE1 B GLU A 40  ? 1.1639 1.0240 0.9022 -0.0631 -0.0783 -0.0461 41  GLU A OE1 
385  O OE2 A GLU A 40  ? 1.1297 0.9904 0.8690 -0.0653 -0.0751 -0.0469 41  GLU A OE2 
386  O OE2 B GLU A 40  ? 1.1806 1.0073 0.8832 -0.0802 -0.0552 -0.0410 41  GLU A OE2 
387  N N   . GLN A 41  ? 0.4099 0.3536 0.2736 -0.0609 -0.0530 -0.0649 42  GLN A N   
388  C CA  . GLN A 41  ? 0.3833 0.3434 0.2751 -0.0579 -0.0479 -0.0665 42  GLN A CA  
389  C C   . GLN A 41  ? 0.4253 0.3784 0.3185 -0.0496 -0.0485 -0.0572 42  GLN A C   
390  O O   . GLN A 41  ? 0.4403 0.3848 0.3203 -0.0423 -0.0605 -0.0529 42  GLN A O   
391  C CB  . GLN A 41  ? 0.4032 0.3883 0.3138 -0.0546 -0.0598 -0.0773 42  GLN A CB  
392  C CG  . GLN A 41  ? 0.5741 0.5705 0.4889 -0.0652 -0.0565 -0.0891 42  GLN A CG  
393  C CD  . GLN A 41  ? 0.8069 0.8327 0.7459 -0.0644 -0.0648 -0.1024 42  GLN A CD  
394  O OE1 . GLN A 41  ? 0.7044 0.7446 0.6608 -0.0555 -0.0720 -0.1039 42  GLN A OE1 
395  N NE2 . GLN A 41  ? 0.8529 0.8896 0.7947 -0.0745 -0.0631 -0.1140 42  GLN A NE2 
396  N N   . PHE A 42  ? 0.3368 0.2921 0.2443 -0.0507 -0.0359 -0.0541 43  PHE A N   
397  C CA  . PHE A 42  ? 0.3419 0.2925 0.2523 -0.0440 -0.0353 -0.0464 43  PHE A CA  
398  C C   . PHE A 42  ? 0.3836 0.3509 0.3182 -0.0418 -0.0318 -0.0493 43  PHE A C   
399  O O   . PHE A 42  ? 0.3799 0.3508 0.3235 -0.0474 -0.0204 -0.0510 43  PHE A O   
400  C CB  . PHE A 42  ? 0.3660 0.3010 0.2662 -0.0479 -0.0229 -0.0394 43  PHE A CB  
401  C CG  . PHE A 42  ? 0.4033 0.3209 0.2785 -0.0525 -0.0230 -0.0376 43  PHE A CG  
402  C CD1 . PHE A 42  ? 0.4333 0.3478 0.3019 -0.0605 -0.0163 -0.0422 43  PHE A CD1 
403  C CD2 . PHE A 42  ? 0.4457 0.3476 0.3017 -0.0501 -0.0283 -0.0317 43  PHE A CD2 
404  C CE1 . PHE A 42  ? 0.4747 0.3728 0.3185 -0.0660 -0.0153 -0.0414 43  PHE A CE1 
405  C CE2 . PHE A 42  ? 0.4996 0.3830 0.3289 -0.0563 -0.0269 -0.0303 43  PHE A CE2 
406  C CZ  . PHE A 42  ? 0.4777 0.3602 0.3013 -0.0643 -0.0204 -0.0354 43  PHE A CZ  
407  N N   . ARG A 43  ? 0.3350 0.3103 0.2783 -0.0336 -0.0411 -0.0497 44  ARG A N   
408  C CA  . ARG A 43  ? 0.3030 0.2942 0.2681 -0.0322 -0.0372 -0.0532 44  ARG A CA  
409  C C   . ARG A 43  ? 0.3470 0.3293 0.3109 -0.0308 -0.0292 -0.0447 44  ARG A C   
410  O O   . ARG A 43  ? 0.3355 0.3041 0.2863 -0.0273 -0.0319 -0.0379 44  ARG A O   
411  C CB  . ARG A 43  ? 0.3198 0.3262 0.2978 -0.0238 -0.0503 -0.0599 44  ARG A CB  
412  C CG  . ARG A 43  ? 0.4166 0.4386 0.4012 -0.0246 -0.0595 -0.0711 44  ARG A CG  
413  C CD  . ARG A 43  ? 0.5297 0.5773 0.5397 -0.0192 -0.0663 -0.0825 44  ARG A CD  
414  N NE  . ARG A 43  ? 0.6496 0.7068 0.6761 -0.0248 -0.0525 -0.0847 44  ARG A NE  
415  C CZ  . ARG A 43  ? 0.7912 0.8629 0.8314 -0.0350 -0.0424 -0.0939 44  ARG A CZ  
416  N NH1 . ARG A 43  ? 0.6788 0.7618 0.7228 -0.0408 -0.0450 -0.1035 44  ARG A NH1 
417  N NH2 . ARG A 43  ? 0.5679 0.6424 0.6167 -0.0402 -0.0298 -0.0940 44  ARG A NH2 
418  N N   . ALA A 44  ? 0.2946 0.2835 0.2701 -0.0341 -0.0192 -0.0453 45  ALA A N   
419  C CA  . ALA A 44  ? 0.3007 0.2833 0.2752 -0.0325 -0.0128 -0.0380 45  ALA A CA  
420  C C   . ALA A 44  ? 0.3066 0.2993 0.2942 -0.0342 -0.0062 -0.0404 45  ALA A C   
421  O O   . ALA A 44  ? 0.2866 0.2907 0.2842 -0.0379 -0.0050 -0.0482 45  ALA A O   
422  C CB  . ALA A 44  ? 0.3240 0.2935 0.2875 -0.0360 -0.0046 -0.0324 45  ALA A CB  
423  N N   . HIS A 45  ? 0.2626 0.2512 0.2489 -0.0325 -0.0016 -0.0344 46  HIS A N   
424  C CA  . HIS A 45  ? 0.2487 0.2425 0.2415 -0.0346 0.0053  -0.0349 46  HIS A CA  
425  C C   . HIS A 45  ? 0.2984 0.2809 0.2831 -0.0376 0.0141  -0.0298 46  HIS A C   
426  O O   . HIS A 45  ? 0.2893 0.2637 0.2674 -0.0347 0.0146  -0.0239 46  HIS A O   
427  C CB  . HIS A 45  ? 0.2372 0.2333 0.2321 -0.0300 0.0032  -0.0319 46  HIS A CB  
428  C CG  . HIS A 45  ? 0.2759 0.2790 0.2773 -0.0251 -0.0057 -0.0363 46  HIS A CG  
429  N ND1 . HIS A 45  ? 0.3078 0.3022 0.3014 -0.0205 -0.0126 -0.0328 46  HIS A ND1 
430  C CD2 . HIS A 45  ? 0.2779 0.2944 0.2922 -0.0241 -0.0085 -0.0446 46  HIS A CD2 
431  C CE1 . HIS A 45  ? 0.2920 0.2922 0.2923 -0.0154 -0.0204 -0.0378 46  HIS A CE1 
432  N NE2 . HIS A 45  ? 0.2809 0.2964 0.2958 -0.0167 -0.0184 -0.0457 46  HIS A NE2 
433  N N   . LYS A 46  ? 0.2777 0.2588 0.2628 -0.0435 0.0214  -0.0328 47  LYS A N   
434  C CA  . LYS A 46  ? 0.2813 0.2478 0.2568 -0.0452 0.0296  -0.0279 47  LYS A CA  
435  C C   . LYS A 46  ? 0.3095 0.2709 0.2804 -0.0390 0.0297  -0.0198 47  LYS A C   
436  O O   . LYS A 46  ? 0.2936 0.2458 0.2591 -0.0355 0.0313  -0.0153 47  LYS A O   
437  C CB  . LYS A 46  ? 0.3105 0.2735 0.2842 -0.0531 0.0383  -0.0318 47  LYS A CB  
438  C CG  . LYS A 46  ? 0.3075 0.2747 0.2854 -0.0608 0.0402  -0.0409 47  LYS A CG  
439  C CD  . LYS A 46  ? 0.3078 0.2710 0.2834 -0.0712 0.0508  -0.0462 47  LYS A CD  
440  C CE  . LYS A 46  ? 0.3670 0.3413 0.3513 -0.0797 0.0517  -0.0582 47  LYS A CE  
441  N NZ  . LYS A 46  ? 0.3928 0.3636 0.3750 -0.0923 0.0640  -0.0652 47  LYS A NZ  
442  N N   . THR A 47  ? 0.2677 0.2367 0.2417 -0.0373 0.0275  -0.0192 48  THR A N   
443  C CA  . THR A 47  ? 0.2687 0.2347 0.2381 -0.0319 0.0268  -0.0125 48  THR A CA  
444  C C   . THR A 47  ? 0.2822 0.2505 0.2537 -0.0265 0.0220  -0.0098 48  THR A C   
445  O O   . THR A 47  ? 0.2671 0.2315 0.2355 -0.0220 0.0226  -0.0054 48  THR A O   
446  C CB  . THR A 47  ? 0.3553 0.3286 0.3260 -0.0326 0.0261  -0.0134 48  THR A CB  
447  O OG1 . THR A 47  ? 0.3454 0.3307 0.3264 -0.0324 0.0210  -0.0186 48  THR A OG1 
448  C CG2 . THR A 47  ? 0.3926 0.3603 0.3570 -0.0393 0.0337  -0.0153 48  THR A CG2 
449  N N   . VAL A 48  ? 0.2397 0.2135 0.2157 -0.0270 0.0174  -0.0129 49  VAL A N   
450  C CA  . VAL A 48  ? 0.2467 0.2202 0.2218 -0.0244 0.0147  -0.0112 49  VAL A CA  
451  C C   . VAL A 48  ? 0.2758 0.2416 0.2473 -0.0247 0.0187  -0.0104 49  VAL A C   
452  O O   . VAL A 48  ? 0.2499 0.2157 0.2219 -0.0219 0.0201  -0.0088 49  VAL A O   
453  C CB  . VAL A 48  ? 0.2789 0.2541 0.2543 -0.0251 0.0089  -0.0139 49  VAL A CB  
454  C CG1 . VAL A 48  ? 0.2877 0.2583 0.2579 -0.0253 0.0085  -0.0124 49  VAL A CG1 
455  C CG2 . VAL A 48  ? 0.2677 0.2500 0.2480 -0.0236 0.0055  -0.0154 49  VAL A CG2 
456  N N   . LEU A 49  ? 0.2451 0.2057 0.2141 -0.0284 0.0207  -0.0132 50  LEU A N   
457  C CA  . LEU A 49  ? 0.2549 0.2068 0.2197 -0.0293 0.0256  -0.0136 50  LEU A CA  
458  C C   . LEU A 49  ? 0.2897 0.2360 0.2543 -0.0245 0.0303  -0.0100 50  LEU A C   
459  O O   . LEU A 49  ? 0.2725 0.2168 0.2381 -0.0213 0.0326  -0.0098 50  LEU A O   
460  C CB  . LEU A 49  ? 0.2576 0.2051 0.2196 -0.0351 0.0276  -0.0180 50  LEU A CB  
461  C CG  . LEU A 49  ? 0.2887 0.2414 0.2501 -0.0383 0.0211  -0.0225 50  LEU A CG  
462  C CD1 . LEU A 49  ? 0.3011 0.2522 0.2613 -0.0445 0.0234  -0.0284 50  LEU A CD1 
463  C CD2 . LEU A 49  ? 0.3265 0.2752 0.2808 -0.0379 0.0184  -0.0214 50  LEU A CD2 
464  N N   . MET A 50  ? 0.2559 0.1993 0.2185 -0.0238 0.0315  -0.0077 51  MET A N   
465  C CA  . MET A 50  ? 0.2723 0.2068 0.2306 -0.0178 0.0341  -0.0031 51  MET A CA  
466  C C   . MET A 50  ? 0.3051 0.2492 0.2690 -0.0102 0.0295  -0.0007 51  MET A C   
467  O O   . MET A 50  ? 0.3105 0.2511 0.2755 -0.0034 0.0303  0.0006  51  MET A O   
468  C CB  . MET A 50  ? 0.2980 0.2250 0.2483 -0.0200 0.0363  -0.0007 51  MET A CB  
469  C CG  . MET A 50  ? 0.3368 0.2547 0.2823 -0.0287 0.0427  -0.0046 51  MET A CG  
470  S SD  . MET A 50  ? 0.3909 0.3053 0.3286 -0.0344 0.0461  -0.0040 51  MET A SD  
471  C CE  . MET A 50  ? 0.3668 0.2554 0.2863 -0.0289 0.0504  0.0039  51  MET A CE  
472  N N   . ALA A 51  ? 0.2682 0.2249 0.2366 -0.0115 0.0248  -0.0013 52  ALA A N   
473  C CA  . ALA A 51  ? 0.2665 0.2347 0.2409 -0.0065 0.0207  -0.0006 52  ALA A CA  
474  C C   . ALA A 51  ? 0.2953 0.2688 0.2769 -0.0055 0.0222  -0.0042 52  ALA A C   
475  O O   . ALA A 51  ? 0.3043 0.2879 0.2930 -0.0006 0.0203  -0.0052 52  ALA A O   
476  C CB  . ALA A 51  ? 0.2640 0.2419 0.2405 -0.0100 0.0169  -0.0017 52  ALA A CB  
477  N N   . CYS A 52  ? 0.2596 0.2275 0.2390 -0.0109 0.0256  -0.0070 53  CYS A N   
478  C CA  . CYS A 52  ? 0.2609 0.2318 0.2437 -0.0129 0.0288  -0.0113 53  CYS A CA  
479  C C   . CYS A 52  ? 0.3039 0.2675 0.2872 -0.0109 0.0345  -0.0136 53  CYS A C   
480  O O   . CYS A 52  ? 0.3013 0.2698 0.2895 -0.0118 0.0383  -0.0183 53  CYS A O   
481  C CB  . CYS A 52  ? 0.2642 0.2320 0.2403 -0.0209 0.0280  -0.0130 53  CYS A CB  
482  S SG  . CYS A 52  ? 0.3047 0.2793 0.2808 -0.0227 0.0221  -0.0119 53  CYS A SG  
483  N N   . SER A 53  ? 0.2729 0.2240 0.2503 -0.0100 0.0365  -0.0115 54  SER A N   
484  C CA  . SER A 53  ? 0.2586 0.1993 0.2341 -0.0098 0.0429  -0.0145 54  SER A CA  
485  C C   . SER A 53  ? 0.3325 0.2604 0.3049 -0.0028 0.0447  -0.0111 54  SER A C   
486  O O   . SER A 53  ? 0.3128 0.2325 0.2773 -0.0047 0.0437  -0.0073 54  SER A O   
487  C CB  . SER A 53  ? 0.2838 0.2175 0.2506 -0.0195 0.0448  -0.0170 54  SER A CB  
488  O OG  . SER A 53  ? 0.3446 0.2647 0.3059 -0.0215 0.0506  -0.0191 54  SER A OG  
489  N N   . GLY A 54  ? 0.3147 0.2393 0.2922 0.0050  0.0478  -0.0132 55  GLY A N   
490  C CA  . GLY A 54  ? 0.3268 0.2337 0.2983 0.0131  0.0496  -0.0099 55  GLY A CA  
491  C C   . GLY A 54  ? 0.3774 0.2647 0.3365 0.0051  0.0562  -0.0104 55  GLY A C   
492  O O   . GLY A 54  ? 0.3870 0.2565 0.3348 0.0066  0.0575  -0.0058 55  GLY A O   
493  N N   . LEU A 55  ? 0.3435 0.2332 0.3026 -0.0048 0.0604  -0.0163 56  LEU A N   
494  C CA  . LEU A 55  ? 0.3517 0.2264 0.3004 -0.0140 0.0663  -0.0188 56  LEU A CA  
495  C C   . LEU A 55  ? 0.3684 0.2437 0.3110 -0.0210 0.0633  -0.0160 56  LEU A C   
496  O O   . LEU A 55  ? 0.3731 0.2322 0.3065 -0.0239 0.0679  -0.0149 56  LEU A O   
497  C CB  . LEU A 55  ? 0.3504 0.2289 0.2988 -0.0229 0.0698  -0.0262 56  LEU A CB  
498  C CG  . LEU A 55  ? 0.4176 0.2818 0.3560 -0.0325 0.0760  -0.0307 56  LEU A CG  
499  C CD1 . LEU A 55  ? 0.4359 0.2787 0.3701 -0.0278 0.0846  -0.0320 56  LEU A CD1 
500  C CD2 . LEU A 55  ? 0.4118 0.2826 0.3472 -0.0420 0.0763  -0.0372 56  LEU A CD2 
501  N N   . PHE A 56  ? 0.3141 0.2069 0.2619 -0.0238 0.0566  -0.0155 57  PHE A N   
502  C CA  . PHE A 56  ? 0.3066 0.2033 0.2520 -0.0297 0.0539  -0.0147 57  PHE A CA  
503  C C   . PHE A 56  ? 0.3597 0.2492 0.3004 -0.0251 0.0539  -0.0087 57  PHE A C   
504  O O   . PHE A 56  ? 0.3452 0.2283 0.2796 -0.0316 0.0571  -0.0093 57  PHE A O   
505  C CB  . PHE A 56  ? 0.3104 0.2249 0.2618 -0.0323 0.0466  -0.0161 57  PHE A CB  
506  C CG  . PHE A 56  ? 0.3169 0.2337 0.2667 -0.0388 0.0460  -0.0217 57  PHE A CG  
507  C CD1 . PHE A 56  ? 0.3405 0.2528 0.2863 -0.0467 0.0488  -0.0270 57  PHE A CD1 
508  C CD2 . PHE A 56  ? 0.3218 0.2449 0.2721 -0.0381 0.0425  -0.0222 57  PHE A CD2 
509  C CE1 . PHE A 56  ? 0.3543 0.2689 0.2965 -0.0523 0.0468  -0.0324 57  PHE A CE1 
510  C CE2 . PHE A 56  ? 0.3610 0.2833 0.3049 -0.0442 0.0411  -0.0267 57  PHE A CE2 
511  C CZ  . PHE A 56  ? 0.3440 0.2625 0.2839 -0.0506 0.0425  -0.0316 57  PHE A CZ  
512  N N   . TYR A 57  ? 0.3347 0.2249 0.2775 -0.0145 0.0507  -0.0039 58  TYR A N   
513  C CA  . TYR A 57  ? 0.3578 0.2380 0.2919 -0.0089 0.0496  0.0026  58  TYR A CA  
514  C C   . TYR A 57  ? 0.4244 0.2773 0.3434 -0.0109 0.0575  0.0040  58  TYR A C   
515  O O   . TYR A 57  ? 0.4091 0.2509 0.3160 -0.0160 0.0605  0.0066  58  TYR A O   
516  C CB  . TYR A 57  ? 0.3801 0.2669 0.3200 0.0041  0.0435  0.0061  58  TYR A CB  
517  C CG  . TYR A 57  ? 0.4293 0.3031 0.3568 0.0116  0.0407  0.0134  58  TYR A CG  
518  C CD1 . TYR A 57  ? 0.4433 0.3218 0.3649 0.0082  0.0375  0.0165  58  TYR A CD1 
519  C CD2 . TYR A 57  ? 0.4990 0.3539 0.4188 0.0225  0.0411  0.0170  58  TYR A CD2 
520  C CE1 . TYR A 57  ? 0.4820 0.3462 0.3877 0.0142  0.0348  0.0236  58  TYR A CE1 
521  C CE2 . TYR A 57  ? 0.5507 0.3899 0.4545 0.0303  0.0372  0.0247  58  TYR A CE2 
522  C CZ  . TYR A 57  ? 0.6410 0.4847 0.5366 0.0256  0.0341  0.0282  58  TYR A CZ  
523  O OH  . TYR A 57  ? 0.7431 0.5690 0.6191 0.0328  0.0301  0.0361  58  TYR A OH  
524  N N   A SER A 58  ? 0.3962 0.2373 0.3149 -0.0076 0.0621  0.0017  59  SER A N   
525  N N   B SER A 58  ? 0.3990 0.2402 0.3178 -0.0076 0.0621  0.0017  59  SER A N   
526  C CA  A SER A 58  ? 0.4239 0.2357 0.3274 -0.0095 0.0707  0.0023  59  SER A CA  
527  C CA  B SER A 58  ? 0.4278 0.2399 0.3317 -0.0094 0.0706  0.0022  59  SER A CA  
528  C C   A SER A 58  ? 0.4827 0.2901 0.3802 -0.0260 0.0780  -0.0031 59  SER A C   
529  C C   B SER A 58  ? 0.4823 0.2902 0.3800 -0.0259 0.0778  -0.0030 59  SER A C   
530  O O   A SER A 58  ? 0.5109 0.2965 0.3925 -0.0313 0.0846  -0.0011 59  SER A O   
531  O O   B SER A 58  ? 0.5070 0.2939 0.3888 -0.0311 0.0840  -0.0008 59  SER A O   
532  C CB  A SER A 58  ? 0.4604 0.2639 0.3681 -0.0027 0.0741  -0.0011 59  SER A CB  
533  C CB  B SER A 58  ? 0.4702 0.2751 0.3788 -0.0037 0.0743  -0.0018 59  SER A CB  
534  O OG  A SER A 58  ? 0.4798 0.2864 0.3936 0.0136  0.0677  0.0027  59  SER A OG  
535  O OG  B SER A 58  ? 0.5605 0.3342 0.4535 -0.0052 0.0831  -0.0016 59  SER A OG  
536  N N   . ILE A 59  ? 0.4211 0.2491 0.3306 -0.0342 0.0766  -0.0103 60  ILE A N   
537  C CA  . ILE A 59  ? 0.4081 0.2390 0.3166 -0.0491 0.0814  -0.0177 60  ILE A CA  
538  C C   . ILE A 59  ? 0.4417 0.2773 0.3475 -0.0551 0.0814  -0.0168 60  ILE A C   
539  O O   . ILE A 59  ? 0.4567 0.2785 0.3525 -0.0654 0.0901  -0.0199 60  ILE A O   
540  C CB  . ILE A 59  ? 0.4137 0.2669 0.3346 -0.0539 0.0766  -0.0250 60  ILE A CB  
541  C CG1 . ILE A 59  ? 0.4221 0.2677 0.3422 -0.0525 0.0801  -0.0285 60  ILE A CG1 
542  C CG2 . ILE A 59  ? 0.3867 0.2502 0.3103 -0.0674 0.0779  -0.0335 60  ILE A CG2 
543  C CD1 . ILE A 59  ? 0.4429 0.3079 0.3707 -0.0551 0.0738  -0.0333 60  ILE A CD1 
544  N N   . PHE A 60  ? 0.3689 0.2233 0.2830 -0.0499 0.0729  -0.0135 61  PHE A N   
545  C CA  . PHE A 60  ? 0.3794 0.2413 0.2931 -0.0566 0.0735  -0.0148 61  PHE A CA  
546  C C   . PHE A 60  ? 0.4448 0.2867 0.3413 -0.0544 0.0773  -0.0072 61  PHE A C   
547  O O   . PHE A 60  ? 0.4523 0.2974 0.3456 -0.0621 0.0804  -0.0091 61  PHE A O   
548  C CB  . PHE A 60  ? 0.3706 0.2602 0.3000 -0.0541 0.0638  -0.0168 61  PHE A CB  
549  C CG  . PHE A 60  ? 0.3629 0.2680 0.3041 -0.0573 0.0597  -0.0241 61  PHE A CG  
550  C CD1 . PHE A 60  ? 0.4010 0.3099 0.3449 -0.0682 0.0638  -0.0335 61  PHE A CD1 
551  C CD2 . PHE A 60  ? 0.3685 0.2833 0.3161 -0.0501 0.0520  -0.0222 61  PHE A CD2 
552  C CE1 . PHE A 60  ? 0.4034 0.3259 0.3555 -0.0701 0.0581  -0.0400 61  PHE A CE1 
553  C CE2 . PHE A 60  ? 0.3960 0.3211 0.3492 -0.0530 0.0476  -0.0280 61  PHE A CE2 
554  C CZ  . PHE A 60  ? 0.3717 0.3004 0.3266 -0.0622 0.0498  -0.0364 61  PHE A CZ  
555  N N   . THR A 61  ? 0.4227 0.2427 0.3069 -0.0445 0.0776  0.0005  62  THR A N   
556  C CA  . THR A 61  ? 0.4528 0.2469 0.3144 -0.0422 0.0810  0.0085  62  THR A CA  
557  C C   . THR A 61  ? 0.5573 0.3195 0.4002 -0.0510 0.0934  0.0071  62  THR A C   
558  O O   . THR A 61  ? 0.5720 0.3053 0.3905 -0.0521 0.0988  0.0133  62  THR A O   
559  C CB  . THR A 61  ? 0.5424 0.3308 0.3997 -0.0248 0.0721  0.0179  62  THR A CB  
560  O OG1 . THR A 61  ? 0.4977 0.2820 0.3620 -0.0158 0.0709  0.0172  62  THR A OG1 
561  C CG2 . THR A 61  ? 0.4732 0.2896 0.3440 -0.0192 0.0616  0.0192  62  THR A CG2 
562  N N   . ASP A 62  ? 0.5110 0.2767 0.3629 -0.0584 0.0985  -0.0014 63  ASP A N   
563  C CA  . ASP A 62  ? 0.5423 0.2791 0.3777 -0.0692 0.1116  -0.0048 63  ASP A CA  
564  C C   . ASP A 62  ? 0.6113 0.3523 0.4430 -0.0875 0.1202  -0.0119 63  ASP A C   
565  O O   . ASP A 62  ? 0.5667 0.3401 0.4189 -0.0941 0.1170  -0.0205 63  ASP A O   
566  C CB  . ASP A 62  ? 0.5521 0.2929 0.3984 -0.0720 0.1141  -0.0128 63  ASP A CB  
567  C CG  . ASP A 62  ? 0.7146 0.4274 0.5446 -0.0858 0.1286  -0.0184 63  ASP A CG  
568  O OD1 . ASP A 62  ? 0.7947 0.4720 0.6055 -0.0800 0.1340  -0.0125 63  ASP A OD1 
569  O OD2 . ASP A 62  ? 0.7070 0.4328 0.5431 -0.1025 0.1346  -0.0291 63  ASP A OD2 
570  N N   . GLN A 63  ? 0.6449 0.3522 0.4500 -0.0958 0.1317  -0.0090 64  GLN A N   
571  C CA  . GLN A 63  ? 0.6652 0.3741 0.4645 -0.1148 0.1425  -0.0166 64  GLN A CA  
572  C C   . GLN A 63  ? 0.7095 0.4429 0.5291 -0.1311 0.1483  -0.0331 64  GLN A C   
573  O O   . GLN A 63  ? 0.7284 0.4828 0.5576 -0.1432 0.1519  -0.0421 64  GLN A O   
574  C CB  . GLN A 63  ? 0.7398 0.4013 0.5018 -0.1224 0.1557  -0.0105 64  GLN A CB  
575  C CG  . GLN A 63  ? 1.0030 0.6447 0.7428 -0.1092 0.1491  0.0044  64  GLN A CG  
576  N N   . LEU A 64  ? 0.6254 0.3574 0.4518 -0.1316 0.1492  -0.0383 65  LEU A N   
577  C CA  . LEU A 64  ? 0.5943 0.3518 0.4399 -0.1461 0.1525  -0.0545 65  LEU A CA  
578  C C   . LEU A 64  ? 0.6095 0.4076 0.4835 -0.1371 0.1371  -0.0581 65  LEU A C   
579  O O   . LEU A 64  ? 0.6189 0.4478 0.5120 -0.1457 0.1349  -0.0701 65  LEU A O   
580  C CB  . LEU A 64  ? 0.6144 0.3494 0.4508 -0.1535 0.1619  -0.0599 65  LEU A CB  
581  C CG  . LEU A 64  ? 0.7215 0.4209 0.5332 -0.1709 0.1807  -0.0637 65  LEU A CG  
582  C CD1 . LEU A 64  ? 0.7417 0.4196 0.5459 -0.1760 0.1886  -0.0689 65  LEU A CD1 
583  C CD2 . LEU A 64  ? 0.7670 0.4884 0.5885 -0.1920 0.1894  -0.0786 65  LEU A CD2 
584  N N   . LYS A 65  ? 0.5198 0.3170 0.3961 -0.1204 0.1269  -0.0490 66  LYS A N   
585  C CA  . LYS A 65  ? 0.4772 0.3066 0.3751 -0.1130 0.1136  -0.0518 66  LYS A CA  
586  C C   . LYS A 65  ? 0.5256 0.3804 0.4365 -0.1070 0.1037  -0.0496 66  LYS A C   
587  O O   . LYS A 65  ? 0.4940 0.3762 0.4224 -0.1055 0.0943  -0.0553 66  LYS A O   
588  C CB  . LYS A 65  ? 0.4903 0.3109 0.3865 -0.0996 0.1081  -0.0448 66  LYS A CB  
589  C CG  . LYS A 65  ? 0.5043 0.3033 0.3909 -0.1050 0.1171  -0.0492 66  LYS A CG  
590  C CD  . LYS A 65  ? 0.4802 0.2766 0.3692 -0.0919 0.1116  -0.0445 66  LYS A CD  
591  C CE  . LYS A 65  ? 0.5477 0.3174 0.4251 -0.0950 0.1219  -0.0478 66  LYS A CE  
592  N NZ  . LYS A 65  ? 0.5843 0.3184 0.4434 -0.0890 0.1294  -0.0395 66  LYS A NZ  
593  N N   . CYS A 66  ? 0.5300 0.3738 0.4304 -0.1037 0.1056  -0.0415 67  CYS A N   
594  C CA  . CYS A 66  ? 0.5193 0.3847 0.4301 -0.0988 0.0976  -0.0397 67  CYS A CA  
595  C C   . CYS A 66  ? 0.5674 0.4617 0.4967 -0.1092 0.0974  -0.0533 67  CYS A C   
596  O O   . CYS A 66  ? 0.5571 0.4747 0.5011 -0.1034 0.0882  -0.0544 67  CYS A O   
597  C CB  . CYS A 66  ? 0.5500 0.3959 0.4424 -0.0968 0.1019  -0.0306 67  CYS A CB  
598  S SG  . CYS A 66  ? 0.6401 0.4658 0.5142 -0.1163 0.1196  -0.0366 67  CYS A SG  
599  N N   . ASN A 67  ? 0.5177 0.4103 0.4470 -0.1243 0.1077  -0.0645 68  ASN A N   
600  C CA  . ASN A 67  ? 0.5136 0.4351 0.4623 -0.1354 0.1087  -0.0802 68  ASN A CA  
601  C C   . ASN A 67  ? 0.5388 0.4838 0.5057 -0.1353 0.1000  -0.0904 68  ASN A C   
602  O O   . ASN A 67  ? 0.5231 0.4956 0.5089 -0.1425 0.0983  -0.1046 68  ASN A O   
603  C CB  . ASN A 67  ? 0.5543 0.4630 0.4927 -0.1542 0.1263  -0.0886 68  ASN A CB  
604  C CG  . ASN A 67  ? 0.7487 0.6393 0.6694 -0.1555 0.1337  -0.0806 68  ASN A CG  
605  O OD1 . ASN A 67  ? 0.7831 0.6414 0.6790 -0.1648 0.1472  -0.0772 68  ASN A OD1 
606  N ND2 . ASN A 67  ? 0.6141 0.5218 0.5441 -0.1460 0.1249  -0.0770 68  ASN A ND2 
607  N N   . LEU A 68  ? 0.4974 0.4330 0.4589 -0.1269 0.0937  -0.0838 69  LEU A N   
608  C CA  . LEU A 68  ? 0.4757 0.4298 0.4492 -0.1268 0.0847  -0.0921 69  LEU A CA  
609  C C   . LEU A 68  ? 0.4752 0.4532 0.4631 -0.1144 0.0684  -0.0907 69  LEU A C   
610  O O   . LEU A 68  ? 0.4510 0.4229 0.4348 -0.1033 0.0638  -0.0792 69  LEU A O   
611  C CB  . LEU A 68  ? 0.4906 0.4230 0.4500 -0.1235 0.0858  -0.0859 69  LEU A CB  
612  C CG  . LEU A 68  ? 0.5658 0.4711 0.5097 -0.1350 0.1014  -0.0882 69  LEU A CG  
613  C CD1 . LEU A 68  ? 0.5747 0.4600 0.5070 -0.1290 0.1017  -0.0822 69  LEU A CD1 
614  C CD2 . LEU A 68  ? 0.5802 0.4992 0.5324 -0.1524 0.1079  -0.1056 69  LEU A CD2 
615  N N   . SER A 69  ? 0.4130 0.4170 0.4169 -0.1163 0.0595  -0.1027 70  SER A N   
616  C CA  A SER A 69  ? 0.3910 0.4154 0.4068 -0.1044 0.0429  -0.1027 70  SER A CA  
617  C CA  B SER A 69  ? 0.3957 0.4192 0.4109 -0.1041 0.0430  -0.1021 70  SER A CA  
618  C C   . SER A 69  ? 0.4084 0.4264 0.4149 -0.0980 0.0331  -0.0981 70  SER A C   
619  O O   . SER A 69  ? 0.3545 0.3795 0.3628 -0.0874 0.0199  -0.0945 70  SER A O   
620  C CB  A SER A 69  ? 0.4302 0.4862 0.4683 -0.1085 0.0375  -0.1192 70  SER A CB  
621  C CB  B SER A 69  ? 0.4421 0.4973 0.4800 -0.1072 0.0374  -0.1178 70  SER A CB  
622  O OG  A SER A 69  ? 0.4915 0.5550 0.5388 -0.1151 0.0473  -0.1247 70  SER A OG  
623  O OG  B SER A 69  ? 0.5206 0.5870 0.5639 -0.1171 0.0377  -0.1310 70  SER A OG  
624  N N   . VAL A 70  ? 0.3774 0.3805 0.3723 -0.1056 0.0405  -0.0992 71  VAL A N   
625  C CA  . VAL A 70  ? 0.3718 0.3670 0.3553 -0.1023 0.0341  -0.0964 71  VAL A CA  
626  C C   . VAL A 70  ? 0.4073 0.3744 0.3746 -0.1039 0.0460  -0.0881 71  VAL A C   
627  O O   . VAL A 70  ? 0.4095 0.3643 0.3728 -0.1131 0.0591  -0.0913 71  VAL A O   
628  C CB  . VAL A 70  ? 0.4326 0.4431 0.4205 -0.1106 0.0290  -0.1105 71  VAL A CB  
629  C CG1 . VAL A 70  ? 0.4412 0.4411 0.4132 -0.1085 0.0231  -0.1076 71  VAL A CG1 
630  C CG2 . VAL A 70  ? 0.4282 0.4692 0.4351 -0.1071 0.0157  -0.1204 71  VAL A CG2 
631  N N   . ILE A 71  ? 0.3416 0.2982 0.2993 -0.0952 0.0418  -0.0787 72  ILE A N   
632  C CA  . ILE A 71  ? 0.3429 0.2763 0.2880 -0.0943 0.0511  -0.0723 72  ILE A CA  
633  C C   . ILE A 71  ? 0.4002 0.3308 0.3357 -0.0948 0.0467  -0.0742 72  ILE A C   
634  O O   . ILE A 71  ? 0.3924 0.3300 0.3258 -0.0889 0.0360  -0.0711 72  ILE A O   
635  C CB  . ILE A 71  ? 0.3635 0.2874 0.3074 -0.0840 0.0529  -0.0603 72  ILE A CB  
636  C CG1 . ILE A 71  ? 0.3733 0.2976 0.3225 -0.0843 0.0575  -0.0581 72  ILE A CG1 
637  C CG2 . ILE A 71  ? 0.3860 0.2895 0.3201 -0.0810 0.0610  -0.0555 72  ILE A CG2 
638  C CD1 . ILE A 71  ? 0.4402 0.3480 0.3829 -0.0935 0.0710  -0.0615 72  ILE A CD1 
639  N N   . ASN A 72  ? 0.3725 0.2901 0.2997 -0.1025 0.0558  -0.0793 73  ASN A N   
640  C CA  . ASN A 72  ? 0.3877 0.3007 0.3033 -0.1048 0.0538  -0.0821 73  ASN A CA  
641  C C   . ASN A 72  ? 0.4217 0.3164 0.3299 -0.0997 0.0621  -0.0755 73  ASN A C   
642  O O   . ASN A 72  ? 0.4013 0.2806 0.3088 -0.1005 0.0738  -0.0752 73  ASN A O   
643  C CB  . ASN A 72  ? 0.4175 0.3296 0.3290 -0.1176 0.0587  -0.0944 73  ASN A CB  
644  C CG  . ASN A 72  ? 0.6394 0.5733 0.5614 -0.1237 0.0511  -0.1041 73  ASN A CG  
645  O OD1 . ASN A 72  ? 0.4944 0.4455 0.4193 -0.1197 0.0366  -0.1054 73  ASN A OD1 
646  N ND2 . ASN A 72  ? 0.5933 0.5265 0.5210 -0.1337 0.0610  -0.1119 73  ASN A ND2 
647  N N   . LEU A 73  ? 0.3604 0.2558 0.2624 -0.0948 0.0566  -0.0712 74  LEU A N   
648  C CA  . LEU A 73  ? 0.3590 0.2415 0.2569 -0.0906 0.0649  -0.0674 74  LEU A CA  
649  C C   . LEU A 73  ? 0.4124 0.2833 0.2990 -0.0985 0.0730  -0.0751 74  LEU A C   
650  O O   . LEU A 73  ? 0.4262 0.3003 0.3050 -0.1074 0.0696  -0.0825 74  LEU A O   
651  C CB  . LEU A 73  ? 0.3581 0.2452 0.2538 -0.0843 0.0585  -0.0610 74  LEU A CB  
652  C CG  . LEU A 73  ? 0.3902 0.2879 0.2963 -0.0762 0.0508  -0.0535 74  LEU A CG  
653  C CD1 . LEU A 73  ? 0.3863 0.2842 0.2896 -0.0713 0.0489  -0.0481 74  LEU A CD1 
654  C CD2 . LEU A 73  ? 0.4050 0.3010 0.3227 -0.0718 0.0563  -0.0504 74  LEU A CD2 
655  N N   . ASP A 74  ? 0.3738 0.2327 0.2603 -0.0950 0.0833  -0.0744 75  ASP A N   
656  C CA  . ASP A 74  ? 0.4067 0.2529 0.2837 -0.1015 0.0935  -0.0824 75  ASP A CA  
657  C C   . ASP A 74  ? 0.4812 0.3318 0.3427 -0.1091 0.0876  -0.0862 75  ASP A C   
658  O O   . ASP A 74  ? 0.4612 0.3184 0.3198 -0.1055 0.0803  -0.0807 75  ASP A O   
659  C CB  . ASP A 74  ? 0.4340 0.2712 0.3172 -0.0932 0.1034  -0.0807 75  ASP A CB  
660  C CG  . ASP A 74  ? 0.5572 0.3805 0.4336 -0.0984 0.1160  -0.0899 75  ASP A CG  
661  O OD1 . ASP A 74  ? 0.5793 0.4037 0.4435 -0.1064 0.1167  -0.0953 75  ASP A OD1 
662  O OD2 . ASP A 74  ? 0.6011 0.4105 0.4826 -0.0941 0.1252  -0.0916 75  ASP A OD2 
663  N N   . PRO A 75  ? 0.5069 0.3525 0.3561 -0.1200 0.0902  -0.0954 76  PRO A N   
664  C CA  . PRO A 75  ? 0.5158 0.3635 0.3458 -0.1271 0.0829  -0.0985 76  PRO A CA  
665  C C   . PRO A 75  ? 0.5544 0.3953 0.3737 -0.1268 0.0878  -0.0967 76  PRO A C   
666  O O   . PRO A 75  ? 0.5737 0.4140 0.3741 -0.1314 0.0803  -0.0963 76  PRO A O   
667  C CB  . PRO A 75  ? 0.5536 0.3960 0.3736 -0.1391 0.0875  -0.1100 76  PRO A CB  
668  C CG  . PRO A 75  ? 0.6244 0.4557 0.4564 -0.1383 0.1021  -0.1133 76  PRO A CG  
669  C CD  . PRO A 75  ? 0.5414 0.3776 0.3912 -0.1270 0.0995  -0.1037 76  PRO A CD  
670  N N   . GLU A 76  ? 0.5081 0.3436 0.3384 -0.1214 0.1001  -0.0963 77  GLU A N   
671  C CA  . GLU A 76  ? 0.5274 0.3595 0.3511 -0.1221 0.1067  -0.0968 77  GLU A CA  
672  C C   . GLU A 76  ? 0.5246 0.3652 0.3507 -0.1159 0.0978  -0.0874 77  GLU A C   
673  O O   . GLU A 76  ? 0.5214 0.3594 0.3377 -0.1193 0.1015  -0.0877 77  GLU A O   
674  C CB  . GLU A 76  ? 0.5598 0.3869 0.3984 -0.1171 0.1222  -0.1017 77  GLU A CB  
675  C CG  . GLU A 76  ? 0.8182 0.6328 0.6485 -0.1255 0.1344  -0.1131 77  GLU A CG  
676  C CD  . GLU A 76  ? 1.2478 1.0572 1.0577 -0.1368 0.1409  -0.1204 77  GLU A CD  
677  O OE1 . GLU A 76  ? 1.2633 1.0743 1.0790 -0.1349 0.1504  -0.1232 77  GLU A OE1 
678  O OE2 . GLU A 76  ? 1.2523 1.0568 1.0400 -0.1480 0.1365  -0.1241 77  GLU A OE2 
679  N N   . ILE A 77  ? 0.4487 0.2985 0.2870 -0.1082 0.0873  -0.0800 78  ILE A N   
680  C CA  . ILE A 77  ? 0.4340 0.2912 0.2755 -0.1022 0.0790  -0.0715 78  ILE A CA  
681  C C   . ILE A 77  ? 0.4976 0.3512 0.3161 -0.1077 0.0679  -0.0692 78  ILE A C   
682  O O   . ILE A 77  ? 0.4860 0.3404 0.2959 -0.1104 0.0583  -0.0707 78  ILE A O   
683  C CB  . ILE A 77  ? 0.4464 0.3137 0.3081 -0.0923 0.0728  -0.0651 78  ILE A CB  
684  C CG1 . ILE A 77  ? 0.4567 0.3230 0.3367 -0.0855 0.0832  -0.0661 78  ILE A CG1 
685  C CG2 . ILE A 77  ? 0.3847 0.2589 0.2480 -0.0870 0.0641  -0.0574 78  ILE A CG2 
686  C CD1 . ILE A 77  ? 0.5224 0.3892 0.4098 -0.0817 0.0933  -0.0681 78  ILE A CD1 
687  N N   . ASN A 78  ? 0.4925 0.3417 0.3010 -0.1090 0.0692  -0.0661 79  ASN A N   
688  C CA  . ASN A 78  ? 0.5153 0.3548 0.2973 -0.1135 0.0597  -0.0625 79  ASN A CA  
689  C C   . ASN A 78  ? 0.5098 0.3559 0.2979 -0.1046 0.0450  -0.0542 79  ASN A C   
690  O O   . ASN A 78  ? 0.4753 0.3290 0.2809 -0.0982 0.0468  -0.0501 79  ASN A O   
691  C CB  . ASN A 78  ? 0.5638 0.3932 0.3319 -0.1205 0.0708  -0.0636 79  ASN A CB  
692  C CG  . ASN A 78  ? 0.7793 0.5928 0.5158 -0.1255 0.0627  -0.0584 79  ASN A CG  
693  O OD1 . ASN A 78  ? 0.6143 0.4261 0.3507 -0.1227 0.0603  -0.0525 79  ASN A OD1 
694  N ND2 . ASN A 78  ? 0.7219 0.5215 0.4288 -0.1333 0.0582  -0.0606 79  ASN A ND2 
695  N N   . PRO A 79  ? 0.4816 0.3254 0.2554 -0.1037 0.0298  -0.0524 80  PRO A N   
696  C CA  . PRO A 79  ? 0.4729 0.3233 0.2543 -0.0942 0.0159  -0.0459 80  PRO A CA  
697  C C   . PRO A 79  ? 0.5143 0.3552 0.2871 -0.0923 0.0160  -0.0389 80  PRO A C   
698  O O   . PRO A 79  ? 0.4970 0.3468 0.2869 -0.0844 0.0121  -0.0347 80  PRO A O   
699  C CB  . PRO A 79  ? 0.5200 0.3678 0.2839 -0.0940 0.0000  -0.0473 80  PRO A CB  
700  C CG  . PRO A 79  ? 0.5817 0.4296 0.3402 -0.1028 0.0060  -0.0558 80  PRO A CG  
701  C CD  . PRO A 79  ? 0.5341 0.3714 0.2866 -0.1103 0.0237  -0.0574 80  PRO A CD  
702  N N   . GLU A 80  ? 0.4942 0.3161 0.2395 -0.1008 0.0215  -0.0384 81  GLU A N   
703  C CA  . GLU A 80  ? 0.5002 0.3109 0.2354 -0.1014 0.0234  -0.0328 81  GLU A CA  
704  C C   . GLU A 80  ? 0.5006 0.3261 0.2645 -0.0996 0.0359  -0.0341 81  GLU A C   
705  O O   . GLU A 80  ? 0.4681 0.2972 0.2411 -0.0943 0.0326  -0.0296 81  GLU A O   
706  C CB  . GLU A 80  ? 0.5545 0.3398 0.2516 -0.1133 0.0289  -0.0328 81  GLU A CB  
707  C CG  . GLU A 80  ? 0.6945 0.4645 0.3775 -0.1152 0.0304  -0.0271 81  GLU A CG  
708  C CD  . GLU A 80  ? 1.0482 0.7914 0.6936 -0.1296 0.0404  -0.0277 81  GLU A CD  
709  O OE1 . GLU A 80  ? 1.0358 0.7563 0.6552 -0.1311 0.0358  -0.0212 81  GLU A OE1 
710  O OE2 . GLU A 80  ? 1.0080 0.7510 0.6485 -0.1400 0.0538  -0.0351 81  GLU A OE2 
711  N N   . GLY A 81  ? 0.4751 0.3094 0.2530 -0.1032 0.0491  -0.0409 82  GLY A N   
712  C CA  . GLY A 81  ? 0.4533 0.3032 0.2595 -0.0995 0.0593  -0.0431 82  GLY A CA  
713  C C   . GLY A 81  ? 0.4499 0.3150 0.2805 -0.0878 0.0507  -0.0387 82  GLY A C   
714  O O   . GLY A 81  ? 0.4112 0.2849 0.2562 -0.0834 0.0516  -0.0363 82  GLY A O   
715  N N   . PHE A 82  ? 0.3980 0.2667 0.2323 -0.0839 0.0426  -0.0384 83  PHE A N   
716  C CA  . PHE A 82  ? 0.3679 0.2499 0.2229 -0.0747 0.0355  -0.0351 83  PHE A CA  
717  C C   . PHE A 82  ? 0.3922 0.2732 0.2434 -0.0705 0.0253  -0.0293 83  PHE A C   
718  O O   . PHE A 82  ? 0.3689 0.2598 0.2367 -0.0646 0.0248  -0.0267 83  PHE A O   
719  C CB  . PHE A 82  ? 0.3780 0.2644 0.2370 -0.0737 0.0300  -0.0378 83  PHE A CB  
720  C CG  . PHE A 82  ? 0.3679 0.2676 0.2481 -0.0662 0.0261  -0.0356 83  PHE A CG  
721  C CD1 . PHE A 82  ? 0.3914 0.2967 0.2886 -0.0629 0.0344  -0.0356 83  PHE A CD1 
722  C CD2 . PHE A 82  ? 0.3690 0.2744 0.2509 -0.0620 0.0141  -0.0337 83  PHE A CD2 
723  C CE1 . PHE A 82  ? 0.3851 0.2998 0.2973 -0.0571 0.0315  -0.0331 83  PHE A CE1 
724  C CE2 . PHE A 82  ? 0.3786 0.2962 0.2792 -0.0565 0.0122  -0.0326 83  PHE A CE2 
725  C CZ  . PHE A 82  ? 0.3571 0.2783 0.2711 -0.0549 0.0213  -0.0319 83  PHE A CZ  
726  N N   . CYS A 83  ? 0.4046 0.2723 0.2327 -0.0727 0.0165  -0.0275 84  CYS A N   
727  C CA  . CYS A 83  ? 0.4317 0.2938 0.2528 -0.0677 0.0059  -0.0221 84  CYS A CA  
728  C C   . CYS A 83  ? 0.4476 0.3072 0.2711 -0.0693 0.0136  -0.0196 84  CYS A C   
729  O O   . CYS A 83  ? 0.4215 0.2875 0.2567 -0.0632 0.0093  -0.0168 84  CYS A O   
730  C CB  . CYS A 83  ? 0.4999 0.3425 0.2900 -0.0699 -0.0040 -0.0203 84  CYS A CB  
731  S SG  . CYS A 83  ? 0.5830 0.4141 0.3621 -0.0613 -0.0188 -0.0138 84  CYS A SG  
732  N N   . ILE A 84  ? 0.4111 0.2628 0.2243 -0.0784 0.0256  -0.0222 85  ILE A N   
733  C CA  . ILE A 84  ? 0.3954 0.2472 0.2117 -0.0824 0.0347  -0.0225 85  ILE A CA  
734  C C   . ILE A 84  ? 0.3901 0.2653 0.2392 -0.0753 0.0375  -0.0237 85  ILE A C   
735  O O   . ILE A 84  ? 0.3578 0.2377 0.2145 -0.0733 0.0367  -0.0220 85  ILE A O   
736  C CB  . ILE A 84  ? 0.4425 0.2852 0.2446 -0.0946 0.0486  -0.0279 85  ILE A CB  
737  C CG1 . ILE A 84  ? 0.4767 0.2901 0.2385 -0.1030 0.0458  -0.0250 85  ILE A CG1 
738  C CG2 . ILE A 84  ? 0.4275 0.2814 0.2450 -0.0987 0.0608  -0.0324 85  ILE A CG2 
739  C CD1 . ILE A 84  ? 0.5691 0.3731 0.3139 -0.1155 0.0585  -0.0312 85  ILE A CD1 
740  N N   . LEU A 85  ? 0.3547 0.2423 0.2205 -0.0716 0.0403  -0.0265 86  LEU A N   
741  C CA  . LEU A 85  ? 0.3389 0.2450 0.2314 -0.0641 0.0420  -0.0268 86  LEU A CA  
742  C C   . LEU A 85  ? 0.3605 0.2726 0.2614 -0.0565 0.0318  -0.0222 86  LEU A C   
743  O O   . LEU A 85  ? 0.3260 0.2490 0.2412 -0.0521 0.0317  -0.0210 86  LEU A O   
744  C CB  . LEU A 85  ? 0.3427 0.2550 0.2468 -0.0622 0.0486  -0.0309 86  LEU A CB  
745  C CG  . LEU A 85  ? 0.4157 0.3279 0.3198 -0.0681 0.0610  -0.0376 86  LEU A CG  
746  C CD1 . LEU A 85  ? 0.4316 0.3455 0.3443 -0.0654 0.0667  -0.0417 86  LEU A CD1 
747  C CD2 . LEU A 85  ? 0.4212 0.3473 0.3412 -0.0664 0.0658  -0.0401 86  LEU A CD2 
748  N N   . LEU A 86  ? 0.3334 0.2402 0.2262 -0.0551 0.0231  -0.0207 87  LEU A N   
749  C CA  . LEU A 86  ? 0.3195 0.2334 0.2213 -0.0485 0.0140  -0.0183 87  LEU A CA  
750  C C   . LEU A 86  ? 0.3600 0.2695 0.2569 -0.0473 0.0101  -0.0153 87  LEU A C   
751  O O   . LEU A 86  ? 0.3387 0.2580 0.2489 -0.0427 0.0082  -0.0141 87  LEU A O   
752  C CB  . LEU A 86  ? 0.3217 0.2331 0.2172 -0.0476 0.0053  -0.0197 87  LEU A CB  
753  C CG  . LEU A 86  ? 0.3695 0.2918 0.2779 -0.0412 -0.0030 -0.0198 87  LEU A CG  
754  C CD1 . LEU A 86  ? 0.3474 0.2829 0.2750 -0.0393 0.0030  -0.0205 87  LEU A CD1 
755  C CD2 . LEU A 86  ? 0.4231 0.3460 0.3265 -0.0403 -0.0128 -0.0233 87  LEU A CD2 
756  N N   . ASP A 87  ? 0.3498 0.2423 0.2254 -0.0524 0.0097  -0.0142 88  ASP A N   
757  C CA  . ASP A 87  ? 0.3506 0.2339 0.2179 -0.0530 0.0079  -0.0117 88  ASP A CA  
758  C C   . ASP A 87  ? 0.3725 0.2681 0.2551 -0.0549 0.0166  -0.0135 88  ASP A C   
759  O O   . ASP A 87  ? 0.3665 0.2663 0.2561 -0.0517 0.0137  -0.0124 88  ASP A O   
760  C CB  . ASP A 87  ? 0.4081 0.2666 0.2453 -0.0603 0.0088  -0.0103 88  ASP A CB  
761  C CG  . ASP A 87  ? 0.5941 0.4378 0.4127 -0.0560 -0.0041 -0.0076 88  ASP A CG  
762  O OD1 . ASP A 87  ? 0.5665 0.4212 0.3987 -0.0468 -0.0140 -0.0076 88  ASP A OD1 
763  O OD2 . ASP A 87  ? 0.6184 0.4399 0.4083 -0.0618 -0.0044 -0.0060 88  ASP A OD2 
764  N N   . PHE A 88  ? 0.3362 0.2388 0.2249 -0.0596 0.0266  -0.0172 89  PHE A N   
765  C CA  . PHE A 88  ? 0.3125 0.2313 0.2191 -0.0600 0.0337  -0.0205 89  PHE A CA  
766  C C   . PHE A 88  ? 0.3113 0.2469 0.2382 -0.0508 0.0287  -0.0188 89  PHE A C   
767  O O   . PHE A 88  ? 0.2788 0.2237 0.2148 -0.0496 0.0285  -0.0194 89  PHE A O   
768  C CB  . PHE A 88  ? 0.3150 0.2404 0.2275 -0.0640 0.0441  -0.0261 89  PHE A CB  
769  C CG  . PHE A 88  ? 0.3052 0.2518 0.2406 -0.0610 0.0485  -0.0303 89  PHE A CG  
770  C CD1 . PHE A 88  ? 0.3272 0.2794 0.2652 -0.0668 0.0531  -0.0343 89  PHE A CD1 
771  C CD2 . PHE A 88  ? 0.3140 0.2742 0.2673 -0.0517 0.0470  -0.0301 89  PHE A CD2 
772  C CE1 . PHE A 88  ? 0.3125 0.2875 0.2731 -0.0631 0.0551  -0.0392 89  PHE A CE1 
773  C CE2 . PHE A 88  ? 0.3379 0.3172 0.3109 -0.0467 0.0484  -0.0335 89  PHE A CE2 
774  C CZ  . PHE A 88  ? 0.3163 0.3049 0.2941 -0.0520 0.0518  -0.0384 89  PHE A CZ  
775  N N   . MET A 89  ? 0.2686 0.2074 0.2010 -0.0455 0.0254  -0.0173 90  MET A N   
776  C CA  . MET A 89  ? 0.2509 0.2019 0.1981 -0.0383 0.0219  -0.0156 90  MET A CA  
777  C C   . MET A 89  ? 0.3032 0.2552 0.2507 -0.0364 0.0157  -0.0138 90  MET A C   
778  O O   . MET A 89  ? 0.2949 0.2576 0.2526 -0.0336 0.0156  -0.0137 90  MET A O   
779  C CB  . MET A 89  ? 0.2604 0.2100 0.2088 -0.0356 0.0199  -0.0148 90  MET A CB  
780  C CG  . MET A 89  ? 0.2880 0.2363 0.2379 -0.0364 0.0266  -0.0169 90  MET A CG  
781  S SD  . MET A 89  ? 0.3247 0.2705 0.2756 -0.0349 0.0250  -0.0168 90  MET A SD  
782  C CE  . MET A 89  ? 0.3291 0.2671 0.2758 -0.0382 0.0334  -0.0205 90  MET A CE  
783  N N   . TYR A 90  ? 0.2717 0.2115 0.2067 -0.0374 0.0102  -0.0128 91  TYR A N   
784  C CA  . TYR A 90  ? 0.2706 0.2093 0.2059 -0.0343 0.0040  -0.0119 91  TYR A CA  
785  C C   . TYR A 90  ? 0.3213 0.2516 0.2483 -0.0382 0.0056  -0.0121 91  TYR A C   
786  O O   . TYR A 90  ? 0.3098 0.2376 0.2369 -0.0354 0.0012  -0.0119 91  TYR A O   
787  C CB  . TYR A 90  ? 0.2891 0.2196 0.2170 -0.0310 -0.0043 -0.0117 91  TYR A CB  
788  C CG  . TYR A 90  ? 0.2907 0.2337 0.2316 -0.0272 -0.0067 -0.0135 91  TYR A CG  
789  C CD1 . TYR A 90  ? 0.3089 0.2534 0.2501 -0.0293 -0.0040 -0.0146 91  TYR A CD1 
790  C CD2 . TYR A 90  ? 0.2966 0.2490 0.2487 -0.0229 -0.0103 -0.0153 91  TYR A CD2 
791  C CE1 . TYR A 90  ? 0.2959 0.2502 0.2475 -0.0279 -0.0047 -0.0173 91  TYR A CE1 
792  C CE2 . TYR A 90  ? 0.2914 0.2548 0.2544 -0.0216 -0.0109 -0.0185 91  TYR A CE2 
793  C CZ  . TYR A 90  ? 0.3118 0.2757 0.2741 -0.0246 -0.0078 -0.0193 91  TYR A CZ  
794  O OH  . TYR A 90  ? 0.2942 0.2676 0.2661 -0.0252 -0.0071 -0.0235 91  TYR A OH  
795  N N   . THR A 91  ? 0.2917 0.2167 0.2112 -0.0455 0.0129  -0.0134 92  THR A N   
796  C CA  . THR A 91  ? 0.3150 0.2293 0.2239 -0.0517 0.0160  -0.0145 92  THR A CA  
797  C C   . THR A 91  ? 0.3344 0.2608 0.2519 -0.0587 0.0256  -0.0195 92  THR A C   
798  O O   . THR A 91  ? 0.3316 0.2522 0.2433 -0.0650 0.0290  -0.0218 92  THR A O   
799  C CB  . THR A 91  ? 0.3962 0.2831 0.2779 -0.0569 0.0154  -0.0124 92  THR A CB  
800  O OG1 . THR A 91  ? 0.3906 0.2759 0.2663 -0.0634 0.0227  -0.0142 92  THR A OG1 
801  C CG2 . THR A 91  ? 0.4016 0.2759 0.2733 -0.0490 0.0038  -0.0085 92  THR A CG2 
802  N N   . SER A 92  ? 0.2784 0.2194 0.2082 -0.0582 0.0302  -0.0220 93  SER A N   
803  C CA  . SER A 92  ? 0.2672 0.2230 0.2082 -0.0637 0.0392  -0.0288 93  SER A CA  
804  C C   . SER A 92  ? 0.3317 0.2726 0.2558 -0.0757 0.0484  -0.0324 93  SER A C   
805  O O   . SER A 92  ? 0.3299 0.2835 0.2635 -0.0819 0.0573  -0.0400 93  SER A O   
806  C CB  . SER A 92  ? 0.2891 0.2581 0.2407 -0.0653 0.0395  -0.0324 93  SER A CB  
807  O OG  . SER A 92  ? 0.3468 0.3260 0.3089 -0.0561 0.0316  -0.0291 93  SER A OG  
808  N N   A ARG A 93  ? 0.3260 0.2408 0.2251 -0.0787 0.0460  -0.0277 94  ARG A N   
809  N N   B ARG A 93  ? 0.3122 0.2267 0.2110 -0.0790 0.0461  -0.0278 94  ARG A N   
810  C CA  A ARG A 93  ? 0.3556 0.2499 0.2312 -0.0910 0.0544  -0.0298 94  ARG A CA  
811  C CA  B ARG A 93  ? 0.3345 0.2297 0.2108 -0.0915 0.0550  -0.0303 94  ARG A CA  
812  C C   A ARG A 93  ? 0.3992 0.2890 0.2681 -0.0913 0.0563  -0.0297 94  ARG A C   
813  C C   B ARG A 93  ? 0.3912 0.2803 0.2593 -0.0917 0.0564  -0.0297 94  ARG A C   
814  O O   A ARG A 93  ? 0.3831 0.2672 0.2475 -0.0836 0.0472  -0.0244 94  ARG A O   
815  O O   B ARG A 93  ? 0.3781 0.2605 0.2408 -0.0840 0.0471  -0.0241 94  ARG A O   
816  C CB  A ARG A 93  ? 0.4163 0.2795 0.2628 -0.0939 0.0495  -0.0242 94  ARG A CB  
817  C CB  B ARG A 93  ? 0.3659 0.2308 0.2136 -0.0967 0.0525  -0.0259 94  ARG A CB  
818  C CG  A ARG A 93  ? 0.5005 0.3640 0.3511 -0.0942 0.0482  -0.0247 94  ARG A CG  
819  C CG  B ARG A 93  ? 0.3399 0.2086 0.1931 -0.1016 0.0562  -0.0295 94  ARG A CG  
820  C CD  A ARG A 93  ? 0.5961 0.4278 0.4201 -0.0922 0.0404  -0.0181 94  ARG A CD  
821  C CD  B ARG A 93  ? 0.5169 0.3562 0.3463 -0.1013 0.0502  -0.0239 94  ARG A CD  
822  N NE  A ARG A 93  ? 0.6758 0.4747 0.4649 -0.1031 0.0460  -0.0165 94  ARG A NE  
823  N NE  B ARG A 93  ? 0.6145 0.4582 0.4505 -0.1066 0.0545  -0.0283 94  ARG A NE  
824  C CZ  A ARG A 93  ? 0.8414 0.6230 0.6133 -0.1170 0.0567  -0.0199 94  ARG A CZ  
825  C CZ  B ARG A 93  ? 0.7926 0.6076 0.6040 -0.1153 0.0583  -0.0279 94  ARG A CZ  
826  N NH1 A ARG A 93  ? 0.6784 0.4269 0.4145 -0.1275 0.0622  -0.0179 94  ARG A NH1 
827  N NH1 B ARG A 93  ? 0.6196 0.4408 0.4391 -0.1207 0.0627  -0.0332 94  ARG A NH1 
828  N NH2 A ARG A 93  ? 0.6767 0.4730 0.4651 -0.1215 0.0625  -0.0258 94  ARG A NH2 
829  N NH2 B ARG A 93  ? 0.6809 0.4589 0.4573 -0.1190 0.0577  -0.0223 94  ARG A NH2 
830  N N   . LEU A 94  ? 0.3591 0.2525 0.2278 -0.1010 0.0687  -0.0371 95  LEU A N   
831  C CA  . LEU A 94  ? 0.3631 0.2526 0.2255 -0.1030 0.0729  -0.0389 95  LEU A CA  
832  C C   . LEU A 94  ? 0.4545 0.3168 0.2834 -0.1175 0.0809  -0.0401 95  LEU A C   
833  O O   . LEU A 94  ? 0.4509 0.3124 0.2759 -0.1300 0.0934  -0.0471 95  LEU A O   
834  C CB  . LEU A 94  ? 0.3423 0.2595 0.2339 -0.1008 0.0810  -0.0476 95  LEU A CB  
835  C CG  . LEU A 94  ? 0.3980 0.3135 0.2878 -0.1011 0.0859  -0.0507 95  LEU A CG  
836  C CD1 . LEU A 94  ? 0.3831 0.2957 0.2739 -0.0897 0.0745  -0.0433 95  LEU A CD1 
837  C CD2 . LEU A 94  ? 0.3957 0.3357 0.3124 -0.1002 0.0960  -0.0614 95  LEU A CD2 
838  N N   . ASN A 95  ? 0.4629 0.3026 0.2662 -0.1165 0.0739  -0.0338 96  ASN A N   
839  C CA  . ASN A 95  ? 0.5020 0.3107 0.2665 -0.1294 0.0793  -0.0331 96  ASN A CA  
840  C C   . ASN A 95  ? 0.5521 0.3665 0.3171 -0.1380 0.0923  -0.0415 96  ASN A C   
841  O O   . ASN A 95  ? 0.5549 0.3607 0.3072 -0.1367 0.0886  -0.0398 96  ASN A O   
842  C CB  . ASN A 95  ? 0.5609 0.3441 0.2975 -0.1230 0.0637  -0.0232 96  ASN A CB  
843  C CG  . ASN A 95  ? 0.8137 0.5600 0.5041 -0.1352 0.0670  -0.0208 96  ASN A CG  
844  O OD1 . ASN A 95  ? 0.7220 0.4548 0.3956 -0.1500 0.0809  -0.0249 96  ASN A OD1 
845  N ND2 . ASN A 95  ? 0.7424 0.4714 0.4099 -0.1300 0.0545  -0.0148 96  ASN A ND2 
846  N N   . LEU A 96  ? 0.5028 0.3345 0.2855 -0.1462 0.1072  -0.0519 97  LEU A N   
847  C CA  . LEU A 96  ? 0.5115 0.3533 0.3012 -0.1534 0.1210  -0.0624 97  LEU A CA  
848  C C   . LEU A 96  ? 0.5829 0.3985 0.3364 -0.1733 0.1347  -0.0667 97  LEU A C   
849  O O   . LEU A 96  ? 0.5744 0.3820 0.3179 -0.1847 0.1429  -0.0694 97  LEU A O   
850  C CB  . LEU A 96  ? 0.4946 0.3731 0.3270 -0.1493 0.1285  -0.0728 97  LEU A CB  
851  C CG  . LEU A 96  ? 0.5601 0.4585 0.4143 -0.1486 0.1390  -0.0840 97  LEU A CG  
852  C CD1 . LEU A 96  ? 0.5579 0.4546 0.4150 -0.1363 0.1296  -0.0784 97  LEU A CD1 
853  C CD2 . LEU A 96  ? 0.5395 0.4738 0.4352 -0.1425 0.1431  -0.0937 97  LEU A CD2 
854  N N   . ARG A 97  ? 0.5618 0.3611 0.2919 -0.1785 0.1373  -0.0670 98  ARG A N   
855  C CA  . ARG A 97  ? 0.6136 0.3832 0.3021 -0.1982 0.1501  -0.0702 98  ARG A CA  
856  C C   . ARG A 97  ? 0.6337 0.4117 0.3260 -0.2055 0.1637  -0.0815 98  ARG A C   
857  O O   . ARG A 97  ? 0.5892 0.3863 0.3063 -0.1934 0.1586  -0.0829 98  ARG A O   
858  C CB  . ARG A 97  ? 0.6629 0.3928 0.3043 -0.1978 0.1360  -0.0566 98  ARG A CB  
859  C CG  . ARG A 97  ? 0.7527 0.4706 0.3881 -0.1891 0.1216  -0.0455 98  ARG A CG  
860  C CD  . ARG A 97  ? 0.9791 0.6612 0.5729 -0.1842 0.1046  -0.0327 98  ARG A CD  
861  N NE  . ARG A 97  ? 1.2490 0.8918 0.7905 -0.2012 0.1127  -0.0319 98  ARG A NE  
862  C CZ  . ARG A 97  ? 1.5275 1.1381 1.0346 -0.2142 0.1202  -0.0295 98  ARG A CZ  
863  N NH1 . ARG A 97  ? 1.4139 0.9864 0.8700 -0.2304 0.1282  -0.0286 98  ARG A NH1 
864  N NH2 . ARG A 97  ? 1.3867 1.0011 0.9082 -0.2122 0.1205  -0.0283 98  ARG A NH2 
865  N N   . GLU A 98  ? 0.6266 0.3883 0.2925 -0.2262 0.1820  -0.0900 99  GLU A N   
866  C CA  . GLU A 98  ? 0.6330 0.4009 0.3001 -0.2346 0.1967  -0.1022 99  GLU A CA  
867  C C   . GLU A 98  ? 0.7046 0.4617 0.3575 -0.2260 0.1842  -0.0954 99  GLU A C   
868  O O   . GLU A 98  ? 0.6908 0.4673 0.3675 -0.2212 0.1891  -0.1036 99  GLU A O   
869  C CB  . GLU A 98  ? 0.6989 0.4411 0.3267 -0.2605 0.2170  -0.1101 99  GLU A CB  
870  C CG  . GLU A 98  ? 0.8340 0.5853 0.4655 -0.2715 0.2356  -0.1257 99  GLU A CG  
871  C CD  . GLU A 98  ? 1.2875 1.0118 0.8770 -0.2989 0.2571  -0.1341 99  GLU A CD  
872  O OE1 . GLU A 98  ? 1.2877 0.9689 0.8227 -0.3086 0.2523  -0.1225 99  GLU A OE1 
873  O OE2 . GLU A 98  ? 1.3256 1.0710 0.9357 -0.3106 0.2789  -0.1528 99  GLU A OE2 
874  N N   . GLY A 99  ? 0.7017 0.4289 0.3177 -0.2233 0.1680  -0.0812 100 GLY A N   
875  C CA  . GLY A 99  ? 0.7128 0.4291 0.3120 -0.2163 0.1543  -0.0751 100 GLY A CA  
876  C C   . GLY A 99  ? 0.7006 0.4428 0.3376 -0.1959 0.1394  -0.0715 100 GLY A C   
877  O O   . GLY A 99  ? 0.6975 0.4373 0.3283 -0.1918 0.1319  -0.0705 100 GLY A O   
878  N N   . ASN A 100 ? 0.6130 0.3793 0.2879 -0.1841 0.1356  -0.0701 101 ASN A N   
879  C CA  . ASN A 100 ? 0.5639 0.3515 0.2711 -0.1659 0.1223  -0.0663 101 ASN A CA  
880  C C   . ASN A 100 ? 0.5838 0.4042 0.3379 -0.1579 0.1304  -0.0745 101 ASN A C   
881  O O   . ASN A 100 ? 0.5441 0.3791 0.3222 -0.1442 0.1216  -0.0718 101 ASN A O   
882  C CB  . ASN A 100 ? 0.5526 0.3350 0.2571 -0.1550 0.1037  -0.0538 101 ASN A CB  
883  C CG  . ASN A 100 ? 0.6288 0.4195 0.3485 -0.1537 0.1059  -0.0526 101 ASN A CG  
884  O OD1 . ASN A 100 ? 0.5138 0.3272 0.2632 -0.1541 0.1170  -0.0607 101 ASN A OD1 
885  N ND2 . ASN A 100 ? 0.5693 0.3432 0.2711 -0.1509 0.0944  -0.0431 101 ASN A ND2 
886  N N   . ILE A 101 ? 0.5469 0.3785 0.3137 -0.1661 0.1465  -0.0846 102 ILE A N   
887  C CA  . ILE A 101 ? 0.5146 0.3786 0.3266 -0.1565 0.1519  -0.0925 102 ILE A CA  
888  C C   . ILE A 101 ? 0.5276 0.4039 0.3612 -0.1466 0.1528  -0.0972 102 ILE A C   
889  O O   . ILE A 101 ? 0.4773 0.3724 0.3417 -0.1314 0.1461  -0.0955 102 ILE A O   
890  C CB  . ILE A 101 ? 0.5603 0.4376 0.3839 -0.1678 0.1693  -0.1054 102 ILE A CB  
891  C CG1 . ILE A 101 ? 0.5374 0.4508 0.4098 -0.1543 0.1702  -0.1126 102 ILE A CG1 
892  C CG2 . ILE A 101 ? 0.5626 0.4290 0.3665 -0.1852 0.1877  -0.1172 102 ILE A CG2 
893  C CD1 . ILE A 101 ? 0.5475 0.4789 0.4359 -0.1615 0.1795  -0.1218 102 ILE A CD1 
894  N N   . MET A 102 ? 0.5137 0.3772 0.3291 -0.1553 0.1610  -0.1031 103 MET A N   
895  C CA  . MET A 102 ? 0.5148 0.3859 0.3479 -0.1468 0.1628  -0.1081 103 MET A CA  
896  C C   . MET A 102 ? 0.5304 0.3986 0.3661 -0.1341 0.1459  -0.0969 103 MET A C   
897  O O   . MET A 102 ? 0.4849 0.3665 0.3481 -0.1212 0.1439  -0.0977 103 MET A O   
898  C CB  . MET A 102 ? 0.5817 0.4390 0.3931 -0.1604 0.1762  -0.1179 103 MET A CB  
899  C CG  . MET A 102 ? 0.6642 0.5276 0.4773 -0.1739 0.1962  -0.1321 103 MET A CG  
900  S SD  . MET A 102 ? 0.7129 0.6137 0.5799 -0.1625 0.2050  -0.1443 103 MET A SD  
901  C CE  . MET A 102 ? 0.6723 0.5798 0.5626 -0.1495 0.2084  -0.1519 103 MET A CE  
902  N N   . ALA A 103 ? 0.5164 0.3670 0.3237 -0.1373 0.1335  -0.0869 104 ALA A N   
903  C CA  . ALA A 103 ? 0.5077 0.3578 0.3180 -0.1268 0.1176  -0.0780 104 ALA A CA  
904  C C   . ALA A 103 ? 0.5019 0.3682 0.3390 -0.1137 0.1094  -0.0716 104 ALA A C   
905  O O   . ALA A 103 ? 0.4586 0.3333 0.3144 -0.1030 0.1041  -0.0694 104 ALA A O   
906  C CB  . ALA A 103 ? 0.5445 0.3752 0.3205 -0.1323 0.1056  -0.0705 104 ALA A CB  
907  N N   . VAL A 104 ? 0.4423 0.3117 0.2796 -0.1156 0.1095  -0.0694 105 VAL A N   
908  C CA  . VAL A 104 ? 0.4022 0.2873 0.2633 -0.1044 0.1021  -0.0642 105 VAL A CA  
909  C C   . VAL A 104 ? 0.4135 0.3186 0.3076 -0.0945 0.1078  -0.0699 105 VAL A C   
910  O O   . VAL A 104 ? 0.3890 0.3015 0.2987 -0.0827 0.0994  -0.0646 105 VAL A O   
911  C CB  . VAL A 104 ? 0.4438 0.3272 0.2972 -0.1098 0.1020  -0.0619 105 VAL A CB  
912  C CG1 . VAL A 104 ? 0.4071 0.3095 0.2872 -0.0991 0.0962  -0.0588 105 VAL A CG1 
913  C CG2 . VAL A 104 ? 0.4598 0.3201 0.2803 -0.1148 0.0922  -0.0536 105 VAL A CG2 
914  N N   A MET A 105 ? 0.3871 0.3001 0.2910 -0.0988 0.1217  -0.0810 106 MET A N   
915  N N   B MET A 105 ? 0.3922 0.3053 0.2962 -0.0988 0.1217  -0.0810 106 MET A N   
916  C CA  A MET A 105 ? 0.3863 0.3180 0.3221 -0.0871 0.1259  -0.0873 106 MET A CA  
917  C CA  B MET A 105 ? 0.3894 0.3210 0.3251 -0.0872 0.1260  -0.0874 106 MET A CA  
918  C C   A MET A 105 ? 0.4334 0.3582 0.3730 -0.0783 0.1230  -0.0854 106 MET A C   
919  C C   B MET A 105 ? 0.4382 0.3631 0.3778 -0.0783 0.1231  -0.0854 106 MET A C   
920  O O   A MET A 105 ? 0.4105 0.3436 0.3696 -0.0646 0.1177  -0.0824 106 MET A O   
921  O O   B MET A 105 ? 0.4176 0.3507 0.3766 -0.0647 0.1177  -0.0823 106 MET A O   
922  C CB  A MET A 105 ? 0.4261 0.3684 0.3725 -0.0935 0.1419  -0.1019 106 MET A CB  
923  C CB  B MET A 105 ? 0.4313 0.3736 0.3776 -0.0937 0.1420  -0.1020 106 MET A CB  
924  C CG  A MET A 105 ? 0.4564 0.4203 0.4383 -0.0788 0.1441  -0.1091 106 MET A CG  
925  C CG  B MET A 105 ? 0.4661 0.4306 0.4481 -0.0792 0.1441  -0.1091 106 MET A CG  
926  S SD  A MET A 105 ? 0.5149 0.4994 0.5162 -0.0859 0.1622  -0.1287 106 MET A SD  
927  S SD  B MET A 105 ? 0.5334 0.5148 0.5328 -0.0860 0.1633  -0.1293 106 MET A SD  
928  C CE  A MET A 105 ? 0.4977 0.4649 0.4850 -0.0932 0.1755  -0.1376 106 MET A CE  
929  C CE  B MET A 105 ? 0.4863 0.4806 0.5189 -0.0640 0.1616  -0.1343 106 MET A CE  
930  N N   . ALA A 106 ? 0.4191 0.3272 0.3381 -0.0868 0.1268  -0.0874 107 ALA A N   
931  C CA  . ALA A 106 ? 0.4196 0.3188 0.3393 -0.0814 0.1256  -0.0868 107 ALA A CA  
932  C C   . ALA A 106 ? 0.4222 0.3196 0.3424 -0.0738 0.1118  -0.0756 107 ALA A C   
933  O O   . ALA A 106 ? 0.3920 0.2896 0.3255 -0.0637 0.1103  -0.0739 107 ALA A O   
934  C CB  . ALA A 106 ? 0.4524 0.3353 0.3472 -0.0942 0.1311  -0.0915 107 ALA A CB  
935  N N   . THR A 107 ? 0.3813 0.2764 0.2875 -0.0782 0.1021  -0.0683 108 THR A N   
936  C CA  . THR A 107 ? 0.3700 0.2659 0.2780 -0.0720 0.0897  -0.0593 108 THR A CA  
937  C C   . THR A 107 ? 0.3951 0.3043 0.3253 -0.0601 0.0864  -0.0554 108 THR A C   
938  O O   . THR A 107 ? 0.3624 0.2710 0.2998 -0.0527 0.0821  -0.0512 108 THR A O   
939  C CB  . THR A 107 ? 0.4511 0.3410 0.3393 -0.0782 0.0798  -0.0539 108 THR A CB  
940  O OG1 . THR A 107 ? 0.4525 0.3295 0.3178 -0.0888 0.0826  -0.0580 108 THR A OG1 
941  C CG2 . THR A 107 ? 0.4359 0.3277 0.3271 -0.0727 0.0681  -0.0476 108 THR A CG2 
942  N N   . ALA A 108 ? 0.3528 0.2735 0.2924 -0.0593 0.0892  -0.0575 109 ALA A N   
943  C CA  . ALA A 108 ? 0.3261 0.2615 0.2862 -0.0483 0.0853  -0.0550 109 ALA A CA  
944  C C   . ALA A 108 ? 0.3504 0.2878 0.3266 -0.0372 0.0890  -0.0580 109 ALA A C   
945  O O   . ALA A 108 ? 0.3240 0.2642 0.3090 -0.0267 0.0827  -0.0524 109 ALA A O   
946  C CB  . ALA A 108 ? 0.3291 0.2779 0.2962 -0.0518 0.0885  -0.0591 109 ALA A CB  
947  N N   . MET A 109 ? 0.3288 0.2619 0.3063 -0.0393 0.0993  -0.0666 110 MET A N   
948  C CA  . MET A 109 ? 0.3277 0.2586 0.3187 -0.0273 0.1026  -0.0695 110 MET A CA  
949  C C   . MET A 109 ? 0.3751 0.2883 0.3562 -0.0242 0.0982  -0.0623 110 MET A C   
950  O O   . MET A 109 ? 0.3750 0.2854 0.3636 -0.0123 0.0943  -0.0578 110 MET A O   
951  C CB  . MET A 109 ? 0.3709 0.2997 0.3647 -0.0312 0.1156  -0.0816 110 MET A CB  
952  C CG  . MET A 109 ? 0.4278 0.3774 0.4388 -0.0311 0.1216  -0.0912 110 MET A CG  
953  S SD  . MET A 109 ? 0.5300 0.4772 0.5404 -0.0406 0.1390  -0.1070 110 MET A SD  
954  C CE  . MET A 109 ? 0.5051 0.4449 0.5316 -0.0230 0.1413  -0.1106 110 MET A CE  
955  N N   . TYR A 110 ? 0.3614 0.2631 0.3245 -0.0355 0.0986  -0.0614 111 TYR A N   
956  C CA  . TYR A 110 ? 0.3719 0.2592 0.3254 -0.0364 0.0957  -0.0568 111 TYR A CA  
957  C C   . TYR A 110 ? 0.3919 0.2837 0.3477 -0.0312 0.0855  -0.0473 111 TYR A C   
958  O O   . TYR A 110 ? 0.3728 0.2550 0.3287 -0.0254 0.0846  -0.0434 111 TYR A O   
959  C CB  . TYR A 110 ? 0.3884 0.2689 0.3241 -0.0503 0.0963  -0.0596 111 TYR A CB  
960  C CG  . TYR A 110 ? 0.3956 0.2672 0.3228 -0.0541 0.0922  -0.0567 111 TYR A CG  
961  C CD1 . TYR A 110 ? 0.4350 0.2918 0.3598 -0.0543 0.0990  -0.0601 111 TYR A CD1 
962  C CD2 . TYR A 110 ? 0.3915 0.2694 0.3130 -0.0582 0.0824  -0.0522 111 TYR A CD2 
963  C CE1 . TYR A 110 ? 0.4044 0.2543 0.3220 -0.0601 0.0969  -0.0593 111 TYR A CE1 
964  C CE2 . TYR A 110 ? 0.3964 0.2703 0.3131 -0.0627 0.0793  -0.0522 111 TYR A CE2 
965  C CZ  . TYR A 110 ? 0.4116 0.2721 0.3263 -0.0647 0.0871  -0.0561 111 TYR A CZ  
966  O OH  . TYR A 110 ? 0.4009 0.2589 0.3114 -0.0714 0.0855  -0.0579 111 TYR A OH  
967  N N   . LEU A 111 ? 0.3387 0.2431 0.2949 -0.0335 0.0787  -0.0440 112 LEU A N   
968  C CA  . LEU A 111 ? 0.3139 0.2238 0.2722 -0.0297 0.0697  -0.0363 112 LEU A CA  
969  C C   . LEU A 111 ? 0.3531 0.2702 0.3246 -0.0176 0.0674  -0.0332 112 LEU A C   
970  O O   . LEU A 111 ? 0.3399 0.2590 0.3118 -0.0137 0.0611  -0.0270 112 LEU A O   
971  C CB  . LEU A 111 ? 0.2957 0.2140 0.2488 -0.0361 0.0634  -0.0345 112 LEU A CB  
972  C CG  . LEU A 111 ? 0.3413 0.2526 0.2793 -0.0460 0.0613  -0.0361 112 LEU A CG  
973  C CD1 . LEU A 111 ? 0.3330 0.2496 0.2648 -0.0491 0.0536  -0.0332 112 LEU A CD1 
974  C CD2 . LEU A 111 ? 0.3633 0.2687 0.2988 -0.0471 0.0591  -0.0352 112 LEU A CD2 
975  N N   . GLN A 112 ? 0.3274 0.2498 0.3098 -0.0116 0.0723  -0.0385 113 GLN A N   
976  C CA  . GLN A 112 ? 0.3245 0.2568 0.3212 0.0016  0.0688  -0.0373 113 GLN A CA  
977  C C   . GLN A 112 ? 0.3423 0.2922 0.3443 0.0007  0.0617  -0.0346 113 GLN A C   
978  O O   . GLN A 112 ? 0.3234 0.2748 0.3247 0.0059  0.0544  -0.0280 113 GLN A O   
979  C CB  . GLN A 112 ? 0.3488 0.2656 0.3412 0.0115  0.0661  -0.0310 113 GLN A CB  
980  C CG  . GLN A 112 ? 0.3984 0.2944 0.3844 0.0121  0.0742  -0.0341 113 GLN A CG  
981  C CD  . GLN A 112 ? 0.5663 0.4411 0.5406 0.0170  0.0725  -0.0267 113 GLN A CD  
982  O OE1 . GLN A 112 ? 0.4382 0.3137 0.4123 0.0256  0.0655  -0.0200 113 GLN A OE1 
983  N NE2 . GLN A 112 ? 0.5023 0.3568 0.4645 0.0104  0.0794  -0.0280 113 GLN A NE2 
984  N N   . MET A 113 ? 0.3006 0.2612 0.3049 -0.0076 0.0649  -0.0402 114 MET A N   
985  C CA  . MET A 113 ? 0.2852 0.2606 0.2932 -0.0110 0.0605  -0.0396 114 MET A CA  
986  C C   . MET A 113 ? 0.3521 0.3452 0.3770 -0.0093 0.0658  -0.0493 114 MET A C   
987  O O   . MET A 113 ? 0.3367 0.3318 0.3593 -0.0195 0.0737  -0.0562 114 MET A O   
988  C CB  . MET A 113 ? 0.3046 0.2719 0.2962 -0.0239 0.0607  -0.0381 114 MET A CB  
989  C CG  . MET A 113 ? 0.3314 0.2865 0.3111 -0.0247 0.0547  -0.0308 114 MET A CG  
990  S SD  . MET A 113 ? 0.3740 0.3198 0.3352 -0.0365 0.0526  -0.0300 114 MET A SD  
991  C CE  . MET A 113 ? 0.3341 0.2902 0.2980 -0.0374 0.0473  -0.0278 114 MET A CE  
992  N N   . GLU A 114 ? 0.3442 0.3492 0.3855 0.0040  0.0619  -0.0505 115 GLU A N   
993  C CA  . GLU A 114 ? 0.3609 0.3863 0.4239 0.0093  0.0659  -0.0616 115 GLU A CA  
994  C C   . GLU A 114 ? 0.3665 0.4110 0.4369 -0.0016 0.0700  -0.0696 115 GLU A C   
995  O O   . GLU A 114 ? 0.3676 0.4233 0.4495 -0.0057 0.0795  -0.0814 115 GLU A O   
996  C CB  . GLU A 114 ? 0.3956 0.4308 0.4733 0.0275  0.0570  -0.0602 115 GLU A CB  
997  C CG  . GLU A 114 ? 0.5723 0.5847 0.6411 0.0384  0.0551  -0.0534 115 GLU A CG  
998  N N   . HIS A 115 ? 0.3093 0.3569 0.3732 -0.0071 0.0643  -0.0645 116 HIS A N   
999  C CA  . HIS A 115 ? 0.3250 0.3874 0.3937 -0.0188 0.0693  -0.0724 116 HIS A CA  
1000 C C   . HIS A 115 ? 0.3573 0.4051 0.4090 -0.0351 0.0803  -0.0757 116 HIS A C   
1001 O O   . HIS A 115 ? 0.3598 0.4189 0.4184 -0.0444 0.0902  -0.0869 116 HIS A O   
1002 C CB  . HIS A 115 ? 0.3460 0.4131 0.4110 -0.0206 0.0611  -0.0668 116 HIS A CB  
1003 C CG  . HIS A 115 ? 0.3973 0.4820 0.4786 -0.0064 0.0510  -0.0659 116 HIS A CG  
1004 N ND1 . HIS A 115 ? 0.4269 0.5386 0.5329 0.0000  0.0511  -0.0771 116 HIS A ND1 
1005 C CD2 . HIS A 115 ? 0.4209 0.4998 0.4956 0.0017  0.0404  -0.0558 116 HIS A CD2 
1006 C CE1 . HIS A 115 ? 0.4185 0.5386 0.5305 0.0131  0.0392  -0.0724 116 HIS A CE1 
1007 N NE2 . HIS A 115 ? 0.4218 0.5215 0.5140 0.0137  0.0332  -0.0594 116 HIS A NE2 
1008 N N   . VAL A 116 ? 0.2952 0.3184 0.3245 -0.0386 0.0789  -0.0670 117 VAL A N   
1009 C CA  . VAL A 116 ? 0.3078 0.3138 0.3165 -0.0527 0.0874  -0.0690 117 VAL A CA  
1010 C C   . VAL A 116 ? 0.3659 0.3754 0.3823 -0.0543 0.0989  -0.0796 117 VAL A C   
1011 O O   . VAL A 116 ? 0.3399 0.3491 0.3503 -0.0673 0.1100  -0.0881 117 VAL A O   
1012 C CB  . VAL A 116 ? 0.3547 0.3370 0.3397 -0.0546 0.0811  -0.0584 117 VAL A CB  
1013 C CG1 . VAL A 116 ? 0.3717 0.3360 0.3336 -0.0680 0.0885  -0.0608 117 VAL A CG1 
1014 C CG2 . VAL A 116 ? 0.3434 0.3234 0.3220 -0.0539 0.0712  -0.0501 117 VAL A CG2 
1015 N N   . VAL A 117 ? 0.3219 0.3331 0.3506 -0.0415 0.0973  -0.0798 118 VAL A N   
1016 C CA  . VAL A 117 ? 0.3312 0.3457 0.3698 -0.0407 0.1081  -0.0908 118 VAL A CA  
1017 C C   . VAL A 117 ? 0.3989 0.4397 0.4601 -0.0435 0.1164  -0.1052 118 VAL A C   
1018 O O   . VAL A 117 ? 0.3962 0.4377 0.4553 -0.0549 0.1298  -0.1161 118 VAL A O   
1019 C CB  . VAL A 117 ? 0.3661 0.3762 0.4147 -0.0244 0.1040  -0.0883 118 VAL A CB  
1020 C CG1 . VAL A 117 ? 0.3708 0.3845 0.4318 -0.0223 0.1158  -0.1011 118 VAL A CG1 
1021 C CG2 . VAL A 117 ? 0.3674 0.3527 0.3939 -0.0252 0.0985  -0.0767 118 VAL A CG2 
1022 N N   A ASP A 118 ? 0.3645 0.4278 0.4476 -0.0331 0.1088  -0.1064 119 ASP A N   
1023 N N   B ASP A 118 ? 0.3521 0.4143 0.4323 -0.0353 0.1087  -0.1056 119 ASP A N   
1024 C CA  A ASP A 118 ? 0.3683 0.4626 0.4783 -0.0339 0.1146  -0.1215 119 ASP A CA  
1025 C CA  B ASP A 118 ? 0.3496 0.4420 0.4548 -0.0375 0.1145  -0.1201 119 ASP A CA  
1026 C C   A ASP A 118 ? 0.4243 0.5208 0.5248 -0.0556 0.1270  -0.1299 119 ASP A C   
1027 C C   B ASP A 118 ? 0.3818 0.4723 0.4737 -0.0598 0.1268  -0.1271 119 ASP A C   
1028 O O   A ASP A 118 ? 0.4292 0.5442 0.5463 -0.0619 0.1394  -0.1461 119 ASP A O   
1029 O O   B ASP A 118 ? 0.3760 0.4794 0.4793 -0.0678 0.1405  -0.1423 119 ASP A O   
1030 C CB  A ASP A 118 ? 0.3829 0.4989 0.5126 -0.0203 0.1014  -0.1193 119 ASP A CB  
1031 C CB  B ASP A 118 ? 0.3644 0.4775 0.4875 -0.0254 0.1014  -0.1174 119 ASP A CB  
1032 C CG  A ASP A 118 ? 0.5435 0.6654 0.6905 0.0025  0.0919  -0.1177 119 ASP A CG  
1033 C CG  B ASP A 118 ? 0.5286 0.6781 0.6825 -0.0251 0.1053  -0.1341 119 ASP A CG  
1034 O OD1 A ASP A 118 ? 0.5872 0.7121 0.7470 0.0091  0.0985  -0.1267 119 ASP A OD1 
1035 O OD1 B ASP A 118 ? 0.5517 0.7178 0.7285 -0.0178 0.1109  -0.1468 119 ASP A OD1 
1036 O OD2 A ASP A 118 ? 0.6129 0.7345 0.7589 0.0138  0.0782  -0.1076 119 ASP A OD2 
1037 O OD2 B ASP A 118 ? 0.5926 0.7550 0.7490 -0.0322 0.1027  -0.1355 119 ASP A OD2 
1038 N N   A THR A 119 ? 0.3813 0.4578 0.4544 -0.0670 0.1243  -0.1195 120 THR A N   
1039 N N   B THR A 119 ? 0.3340 0.4067 0.4007 -0.0699 0.1229  -0.1167 120 THR A N   
1040 C CA  A THR A 119 ? 0.3928 0.4629 0.4491 -0.0879 0.1352  -0.1246 120 THR A CA  
1041 C CA  B THR A 119 ? 0.3494 0.4140 0.3982 -0.0912 0.1345  -0.1221 120 THR A CA  
1042 C C   A THR A 119 ? 0.4391 0.4875 0.4723 -0.1012 0.1478  -0.1277 120 THR A C   
1043 C C   B THR A 119 ? 0.4166 0.4594 0.4425 -0.1037 0.1469  -0.1251 120 THR A C   
1044 O O   A THR A 119 ? 0.4404 0.4935 0.4719 -0.1168 0.1628  -0.1403 120 THR A O   
1045 O O   B THR A 119 ? 0.4132 0.4550 0.4307 -0.1211 0.1611  -0.1352 120 THR A O   
1046 C CB  A THR A 119 ? 0.5055 0.5611 0.5421 -0.0919 0.1259  -0.1122 120 THR A CB  
1047 C CB  B THR A 119 ? 0.3693 0.4182 0.3965 -0.0974 0.1268  -0.1108 120 THR A CB  
1048 O OG1 A THR A 119 ? 0.4996 0.5802 0.5611 -0.0807 0.1167  -0.1132 120 THR A OG1 
1049 O OG1 B THR A 119 ? 0.3957 0.4413 0.4112 -0.1170 0.1393  -0.1190 120 THR A OG1 
1050 C CG2 A THR A 119 ? 0.5134 0.5564 0.5283 -0.1129 0.1364  -0.1161 120 THR A CG2 
1051 C CG2 B THR A 119 ? 0.3040 0.3204 0.3005 -0.0966 0.1190  -0.0955 120 THR A CG2 
1052 N N   . CYS A 120 ? 0.3921 0.4171 0.4066 -0.0962 0.1423  -0.1172 121 CYS A N   
1053 C CA  . CYS A 120 ? 0.4131 0.4174 0.4046 -0.1075 0.1528  -0.1201 121 CYS A CA  
1054 C C   . CYS A 120 ? 0.4681 0.4917 0.4823 -0.1091 0.1676  -0.1378 121 CYS A C   
1055 O O   . CYS A 120 ? 0.4725 0.4902 0.4732 -0.1264 0.1828  -0.1476 121 CYS A O   
1056 C CB  . CYS A 120 ? 0.4104 0.3948 0.3879 -0.0989 0.1434  -0.1087 121 CYS A CB  
1057 S SG  . CYS A 120 ? 0.4596 0.4187 0.4056 -0.1009 0.1288  -0.0910 121 CYS A SG  
1058 N N   . ARG A 121 ? 0.4192 0.4661 0.4678 -0.0908 0.1632  -0.1426 122 ARG A N   
1059 C CA  . ARG A 121 ? 0.4303 0.5001 0.5074 -0.0880 0.1754  -0.1610 122 ARG A CA  
1060 C C   . ARG A 121 ? 0.4804 0.5722 0.5693 -0.1033 0.1887  -0.1769 122 ARG A C   
1061 O O   . ARG A 121 ? 0.4827 0.5802 0.5751 -0.1148 0.2060  -0.1925 122 ARG A O   
1062 C CB  . ARG A 121 ? 0.4424 0.5332 0.5536 -0.0634 0.1645  -0.1618 122 ARG A CB  
1063 C CG  . ARG A 121 ? 0.6456 0.7158 0.7495 -0.0497 0.1578  -0.1523 122 ARG A CG  
1064 C CD  . ARG A 121 ? 0.8232 0.9107 0.9593 -0.0305 0.1579  -0.1624 122 ARG A CD  
1065 N NE  . ARG A 121 ? 0.9474 1.0330 1.0911 -0.0094 0.1409  -0.1503 122 ARG A NE  
1066 C CZ  . ARG A 121 ? 1.0948 1.1549 1.2242 -0.0004 0.1349  -0.1391 122 ARG A CZ  
1067 N NH1 . ARG A 121 ? 0.8776 0.9140 0.9864 -0.0099 0.1437  -0.1388 122 ARG A NH1 
1068 N NH2 . ARG A 121 ? 0.9434 1.0005 1.0772 0.0172  0.1206  -0.1285 122 ARG A NH2 
1069 N N   . LYS A 122 ? 0.4444 0.5481 0.5385 -0.1048 0.1819  -0.1738 123 LYS A N   
1070 C CA  . LYS A 122 ? 0.4482 0.5733 0.5537 -0.1205 0.1940  -0.1890 123 LYS A CA  
1071 C C   . LYS A 122 ? 0.5141 0.6124 0.5819 -0.1471 0.2093  -0.1903 123 LYS A C   
1072 O O   . LYS A 122 ? 0.5053 0.6165 0.5801 -0.1629 0.2277  -0.2081 123 LYS A O   
1073 C CB  . LYS A 122 ? 0.4624 0.6042 0.5804 -0.1152 0.1816  -0.1844 123 LYS A CB  
1074 C CG  . LYS A 122 ? 0.6713 0.8466 0.8299 -0.0914 0.1689  -0.1883 123 LYS A CG  
1075 C CD  . LYS A 122 ? 0.8069 1.0023 0.9781 -0.0896 0.1591  -0.1876 123 LYS A CD  
1076 C CE  . LYS A 122 ? 0.9318 1.1442 1.1259 -0.0638 0.1398  -0.1813 123 LYS A CE  
1077 N NZ  . LYS A 122 ? 1.0251 1.2697 1.2578 -0.0480 0.1401  -0.1967 123 LYS A NZ  
1078 N N   . PHE A 123 ? 0.4802 0.5410 0.5073 -0.1521 0.2019  -0.1720 124 PHE A N   
1079 C CA  . PHE A 123 ? 0.5108 0.5391 0.4949 -0.1753 0.2134  -0.1702 124 PHE A CA  
1080 C C   . PHE A 123 ? 0.5890 0.6074 0.5617 -0.1846 0.2285  -0.1797 124 PHE A C   
1081 O O   . PHE A 123 ? 0.6041 0.6131 0.5577 -0.2065 0.2465  -0.1899 124 PHE A O   
1082 C CB  . PHE A 123 ? 0.5387 0.5316 0.4858 -0.1736 0.1985  -0.1487 124 PHE A CB  
1083 C CG  . PHE A 123 ? 0.5616 0.5508 0.5017 -0.1772 0.1917  -0.1419 124 PHE A CG  
1084 C CD1 . PHE A 123 ? 0.5790 0.6003 0.5545 -0.1670 0.1853  -0.1460 124 PHE A CD1 
1085 C CD2 . PHE A 123 ? 0.6208 0.5726 0.5175 -0.1891 0.1902  -0.1308 124 PHE A CD2 
1086 C CE1 . PHE A 123 ? 0.5842 0.6014 0.5526 -0.1711 0.1798  -0.1406 124 PHE A CE1 
1087 C CE2 . PHE A 123 ? 0.6443 0.5902 0.5341 -0.1918 0.1844  -0.1250 124 PHE A CE2 
1088 C CZ  . PHE A 123 ? 0.5868 0.5657 0.5129 -0.1835 0.1799  -0.1303 124 PHE A CZ  
1089 N N   . ILE A 124 ? 0.5268 0.5475 0.5115 -0.1688 0.2227  -0.1776 125 ILE A N   
1090 C CA  . ILE A 124 ? 0.5480 0.5615 0.5256 -0.1757 0.2369  -0.1879 125 ILE A CA  
1091 C C   . ILE A 124 ? 0.6115 0.6579 0.6225 -0.1820 0.2559  -0.2124 125 ILE A C   
1092 O O   . ILE A 124 ? 0.6300 0.6678 0.6241 -0.2016 0.2751  -0.2244 125 ILE A O   
1093 C CB  . ILE A 124 ? 0.5720 0.5774 0.5531 -0.1575 0.2259  -0.1796 125 ILE A CB  
1094 C CG1 . ILE A 124 ? 0.5773 0.5478 0.5186 -0.1585 0.2122  -0.1595 125 ILE A CG1 
1095 C CG2 . ILE A 124 ? 0.6016 0.6073 0.5862 -0.1619 0.2418  -0.1943 125 ILE A CG2 
1096 C CD1 . ILE A 124 ? 0.6576 0.6247 0.6073 -0.1388 0.1968  -0.1485 125 ILE A CD1 
1097 N N   . LYS A 125 ? 0.5638 0.6482 0.6211 -0.1659 0.2503  -0.2204 126 LYS A N   
1098 C CA  . LYS A 125 ? 0.5704 0.6938 0.6680 -0.1680 0.2655  -0.2454 126 LYS A CA  
1099 C C   . LYS A 125 ? 0.6408 0.7686 0.7278 -0.1955 0.2838  -0.2583 126 LYS A C   
1100 O O   . LYS A 125 ? 0.6377 0.7832 0.7391 -0.2083 0.3043  -0.2802 126 LYS A O   
1101 C CB  . LYS A 125 ? 0.5830 0.7442 0.7285 -0.1431 0.2509  -0.2485 126 LYS A CB  
1102 C CG  . LYS A 125 ? 0.7848 0.9873 0.9779 -0.1360 0.2619  -0.2739 126 LYS A CG  
1103 C CD  . LYS A 125 ? 0.9178 1.1596 1.1549 -0.1148 0.2468  -0.2780 126 LYS A CD  
1104 C CE  . LYS A 125 ? 1.0723 1.3602 1.3589 -0.1094 0.2577  -0.3060 126 LYS A CE  
1105 N NZ  . LYS A 125 ? 1.1797 1.5079 1.5069 -0.0912 0.2422  -0.3111 126 LYS A NZ  
1106 N N   . ALA A 126 ? 0.5996 0.7091 0.6599 -0.2054 0.2775  -0.2454 127 ALA A N   
1107 C CA  . ALA A 126 ? 0.6274 0.7328 0.6703 -0.2328 0.2946  -0.2550 127 ALA A CA  
1108 C C   . ALA A 126 ? 0.7288 0.7984 0.7259 -0.2577 0.3137  -0.2577 127 ALA A C   
1109 O O   . ALA A 126 ? 0.7366 0.8105 0.7283 -0.2816 0.3353  -0.2743 127 ALA A O   
1110 C CB  . ALA A 126 ? 0.6281 0.7165 0.6503 -0.2346 0.2814  -0.2384 127 ALA A CB  
1111 N N   . SER A 127 ? 0.7259 0.7604 0.6892 -0.2530 0.3060  -0.2421 128 SER A N   
1112 C CA  . SER A 127 ? 0.7900 0.7871 0.7048 -0.2748 0.3209  -0.2423 128 SER A CA  
1113 C C   . SER A 127 ? 0.8828 0.8941 0.8128 -0.2795 0.3394  -0.2620 128 SER A C   
1114 O O   . SER A 127 ? 0.9329 0.9182 0.8250 -0.3021 0.3567  -0.2674 128 SER A O   
1115 C CB  . SER A 127 ? 0.8666 0.8206 0.7366 -0.2688 0.3032  -0.2174 128 SER A CB  
1116 O OG  . SER A 127 ? 1.0260 0.9527 0.8620 -0.2771 0.2958  -0.2030 128 SER A OG  
1117 N N   . GLU A 128 ? 0.8088 0.8590 0.7918 -0.2586 0.3363  -0.2733 129 GLU A N   
1118 C CA  . GLU A 128 ? 1.0627 1.1285 1.0653 -0.2599 0.3532  -0.2933 129 GLU A CA  
1119 C C   . GLU A 128 ? 1.5815 1.6788 1.6091 -0.2788 0.3788  -0.3217 129 GLU A C   
1120 O O   . GLU A 128 ? 1.1896 1.2696 1.1847 -0.3064 0.3946  -0.3258 129 GLU A O   
1121 C CB  . GLU A 128 ? 1.0469 1.1351 1.0915 -0.2286 0.3390  -0.2929 129 GLU A CB  
1122 C CG  . GLU A 128 ? 1.1417 1.2795 1.2464 -0.2102 0.3338  -0.3057 129 GLU A CG  
1123 C CD  . GLU A 128 ? 1.3987 1.5518 1.5385 -0.1775 0.3163  -0.3013 129 GLU A CD  
1124 O OE1 . GLU A 128 ? 1.3354 1.4589 1.4522 -0.1671 0.3039  -0.2834 129 GLU A OE1 
1125 O OE2 . GLU A 128 ? 1.2986 1.4931 1.4884 -0.1621 0.3148  -0.3162 129 GLU A OE2 
1129 N N   A TRP B 2   ? 0.2421 0.4584 0.3056 -0.0469 -0.0158 -0.0813 1   TRP D N   
1130 N N   B TRP B 2   ? 0.2478 0.4641 0.3113 -0.0469 -0.0158 -0.0813 1   TRP D N   
1131 C CA  A TRP B 2   ? 0.2284 0.4447 0.2928 -0.0470 -0.0155 -0.0822 1   TRP D CA  
1132 C CA  B TRP B 2   ? 0.2394 0.4557 0.3039 -0.0470 -0.0155 -0.0822 1   TRP D CA  
1133 C C   A TRP B 2   ? 0.2785 0.4941 0.3442 -0.0475 -0.0153 -0.0820 1   TRP D C   
1134 C C   B TRP B 2   ? 0.2773 0.4930 0.3431 -0.0475 -0.0152 -0.0820 1   TRP D C   
1135 O O   A TRP B 2   ? 0.2749 0.4894 0.3405 -0.0475 -0.0155 -0.0816 1   TRP D O   
1136 O O   B TRP B 2   ? 0.2715 0.4862 0.3372 -0.0476 -0.0154 -0.0816 1   TRP D O   
1137 C CB  A TRP B 2   ? 0.2141 0.4297 0.2784 -0.0465 -0.0162 -0.0826 1   TRP D CB  
1138 C CB  B TRP B 2   ? 0.2248 0.4404 0.2892 -0.0465 -0.0162 -0.0826 1   TRP D CB  
1139 C CG  A TRP B 2   ? 0.2185 0.4347 0.2820 -0.0460 -0.0164 -0.0834 1   TRP D CG  
1140 C CG  B TRP B 2   ? 0.2369 0.4517 0.3021 -0.0467 -0.0166 -0.0824 1   TRP D CG  
1141 C CD1 A TRP B 2   ? 0.2542 0.4703 0.3175 -0.0455 -0.0170 -0.0831 1   TRP D CD1 
1142 C CD1 B TRP B 2   ? 0.2754 0.4897 0.3414 -0.0465 -0.0168 -0.0824 1   TRP D CD1 
1143 C CD2 A TRP B 2   ? 0.2107 0.4276 0.2737 -0.0459 -0.0159 -0.0847 1   TRP D CD2 
1144 C CD2 B TRP B 2   ? 0.2339 0.4492 0.3000 -0.0471 -0.0166 -0.0823 1   TRP D CD2 
1145 N NE1 A TRP B 2   ? 0.2447 0.4616 0.3073 -0.0451 -0.0171 -0.0844 1   TRP D NE1 
1146 N NE1 B TRP B 2   ? 0.2691 0.4836 0.3364 -0.0470 -0.0166 -0.0827 1   TRP D NE1 
1147 C CE2 A TRP B 2   ? 0.2566 0.4739 0.3189 -0.0454 -0.0162 -0.0856 1   TRP D CE2 
1148 C CE2 B TRP B 2   ? 0.2844 0.4997 0.3514 -0.0474 -0.0166 -0.0827 1   TRP D CE2 
1149 C CE3 A TRP B 2   ? 0.2155 0.4328 0.2792 -0.0462 -0.0149 -0.0851 1   TRP D CE3 
1150 C CE3 B TRP B 2   ? 0.2464 0.4623 0.3131 -0.0473 -0.0166 -0.0819 1   TRP D CE3 
1151 C CZ2 A TRP B 2   ? 0.2392 0.4572 0.3008 -0.0452 -0.0156 -0.0874 1   TRP D CZ2 
1152 C CZ2 B TRP B 2   ? 0.2730 0.4897 0.3410 -0.0479 -0.0165 -0.0830 1   TRP D CZ2 
1153 C CZ3 A TRP B 2   ? 0.2230 0.4407 0.2862 -0.0460 -0.0142 -0.0866 1   TRP D CZ3 
1154 C CZ3 B TRP B 2   ? 0.2662 0.4830 0.3337 -0.0477 -0.0168 -0.0817 1   TRP D CZ3 
1155 C CH2 A TRP B 2   ? 0.2349 0.4530 0.2969 -0.0456 -0.0145 -0.0880 1   TRP D CH2 
1156 C CH2 B TRP B 2   ? 0.2726 0.4901 0.3405 -0.0480 -0.0168 -0.0824 1   TRP D CH2 
1157 N N   . VAL B 3   ? 0.2226 0.4388 0.2899 -0.0478 -0.0147 -0.0823 2   VAL D N   
1158 C CA  . VAL B 3   ? 0.2133 0.4292 0.2827 -0.0482 -0.0146 -0.0822 2   VAL D CA  
1159 C C   . VAL B 3   ? 0.2351 0.4514 0.3064 -0.0480 -0.0147 -0.0817 2   VAL D C   
1160 O O   . VAL B 3   ? 0.2166 0.4334 0.2879 -0.0477 -0.0145 -0.0817 2   VAL D O   
1161 C CB  . VAL B 3   ? 0.2489 0.4655 0.3199 -0.0494 -0.0135 -0.0831 2   VAL D CB  
1162 C CG1 . VAL B 3   ? 0.2493 0.4658 0.3181 -0.0500 -0.0135 -0.0831 2   VAL D CG1 
1163 C CG2 . VAL B 3   ? 0.2420 0.4605 0.3152 -0.0499 -0.0122 -0.0840 2   VAL D CG2 
1164 N N   . ILE B 4   ? 0.2019 0.4182 0.2752 -0.0481 -0.0150 -0.0813 3   ILE D N   
1165 C CA  . ILE B 4   ? 0.2077 0.4247 0.2836 -0.0479 -0.0153 -0.0801 3   ILE D CA  
1166 C C   . ILE B 4   ? 0.2476 0.4648 0.3276 -0.0485 -0.0139 -0.0808 3   ILE D C   
1167 O O   . ILE B 4   ? 0.2335 0.4504 0.3151 -0.0492 -0.0135 -0.0818 3   ILE D O   
1168 C CB  . ILE B 4   ? 0.2320 0.4496 0.3087 -0.0478 -0.0163 -0.0793 3   ILE D CB  
1169 C CG1 . ILE B 4   ? 0.2184 0.4368 0.2919 -0.0477 -0.0171 -0.0795 3   ILE D CG1 
1170 C CG2 . ILE B 4   ? 0.2464 0.4651 0.3263 -0.0475 -0.0168 -0.0774 3   ILE D CG2 
1171 C CD1 . ILE B 4   ? 0.2632 0.4825 0.3348 -0.0477 -0.0176 -0.0789 3   ILE D CD1 
1172 N N   . PRO B 5   ? 0.2391 0.4569 0.3210 -0.0484 -0.0127 -0.0808 4   PRO D N   
1173 C CA  . PRO B 5   ? 0.2448 0.4636 0.3319 -0.0494 -0.0109 -0.0821 4   PRO D CA  
1174 C C   . PRO B 5   ? 0.2948 0.5135 0.3875 -0.0495 -0.0109 -0.0812 4   PRO D C   
1175 O O   . PRO B 5   ? 0.2874 0.5059 0.3805 -0.0485 -0.0122 -0.0789 4   PRO D O   
1176 C CB  . PRO B 5   ? 0.2673 0.4870 0.3553 -0.0491 -0.0094 -0.0825 4   PRO D CB  
1177 C CG  . PRO B 5   ? 0.3102 0.5289 0.3951 -0.0479 -0.0108 -0.0805 4   PRO D CG  
1178 C CD  . PRO B 5   ? 0.2546 0.4726 0.3349 -0.0477 -0.0128 -0.0801 4   PRO D CD  
1179 N N   . ALA B 6   ? 0.2656 0.4852 0.3634 -0.0509 -0.0093 -0.0831 5   ALA D N   
# 
