data_9F71
# 
_entry.id   9F71 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9F71         pdb_00009f71 10.2210/pdb9f71/pdb 
WWPDB D_1292138347 ?            ?                   
# 
_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       2025-05-14 
_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             ? 
# 
_database_PDB_caveat.id     1 
_database_PDB_caveat.text   'A1IAB A 1901 HAS WRONG CHIRALITY AT ATOM C15' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9F71 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB '9F6W contains the same protein complexed with a similar ligand' 9F6W unspecified 
PDB '9F70 contains the same protein complexed with a similar ligand' 9F70 unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              graziano.lolli@unitn.it 
_pdbx_contact_author.name_first         Graziano 
_pdbx_contact_author.name_last          Lolli 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8536-5599 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dalle Vedove, A.' 1 ? 
'Cazzanelli, G.'   2 ? 
'Caflisch, A.'     3 ? 
'Lolli, G.'        4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Unusual backfolded binding poses of BAZ2A bromodomain binders' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dalle Vedove, A.' 1 ? 
primary 'Cazzanelli, G.'   2 ? 
primary 
;D'Agostino, V.G.
;
3 ? 
primary 'Caflisch, A.'     4 ? 
primary 'Lolli, G.'        5 ? 
# 
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 'Bromodomain adjacent to zinc finger domain protein 2A' 12363.872 1  ? E1845H/L1848S 
'Bromodomain (residues 1796-1899)' 
'Bromodomain (residues 1796-1899).First two residues SM derive from the expression tag. E1845H/L1848S' 
2 non-polymer syn 
'1-[2,4-dimethyl-5-[(3~{R})-3-[4-(pyrrolidin-1-ylmethyl)-1~{H}-pyrazol-3-yl]piperidin-1-yl]carbonyl-1~{H}-pyrrol-3-yl]ethanone' 
397.514   1  ? ?             ?                                  ? 
3 non-polymer syn 1,2-ETHANEDIOL 62.068    1  ? ?             ?                                  ? 
4 non-polymer syn 'MAGNESIUM ION' 24.305    1  ? ?             ?                                  ? 
5 water       nat water 18.015    42 ? ?             ?                                  ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Transcription termination factor I-interacting protein 5,Tip5,hWALp3' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMHSDLTFCEIILMEMESHDAAWPFLEPVNPRLVSGYRRIIKNPMDFSTMRHRLSRGGYTSSEEFAADALLVFDNCQTFN
EDDSEVGKAGHIMRRFFESRWEEFY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMHSDLTFCEIILMEMESHDAAWPFLEPVNPRLVSGYRRIIKNPMDFSTMRHRLSRGGYTSSEEFAADALLVFDNCQTFN
EDDSEVGKAGHIMRRFFESRWEEFY
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '1-[2,4-dimethyl-5-[(3~{R})-3-[4-(pyrrolidin-1-ylmethyl)-1~{H}-pyrazol-3-yl]piperidin-1-yl]carbonyl-1~{H}-pyrrol-3-yl]ethanone' 
A1IAB 
3 1,2-ETHANEDIOL                                                                                                                  
EDO   
4 'MAGNESIUM ION'                                                                                                                 
MG    
5 water                                                                                                                           
HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   HIS n 
1 4   SER n 
1 5   ASP n 
1 6   LEU n 
1 7   THR n 
1 8   PHE n 
1 9   CYS n 
1 10  GLU n 
1 11  ILE n 
1 12  ILE n 
1 13  LEU n 
1 14  MET n 
1 15  GLU n 
1 16  MET n 
1 17  GLU n 
1 18  SER n 
1 19  HIS n 
1 20  ASP n 
1 21  ALA n 
1 22  ALA n 
1 23  TRP n 
1 24  PRO n 
1 25  PHE n 
1 26  LEU n 
1 27  GLU n 
1 28  PRO n 
1 29  VAL n 
1 30  ASN n 
1 31  PRO n 
1 32  ARG n 
1 33  LEU n 
1 34  VAL n 
1 35  SER n 
1 36  GLY n 
1 37  TYR n 
1 38  ARG n 
1 39  ARG n 
1 40  ILE n 
1 41  ILE n 
1 42  LYS n 
1 43  ASN n 
1 44  PRO n 
1 45  MET n 
1 46  ASP n 
1 47  PHE n 
1 48  SER n 
1 49  THR n 
1 50  MET n 
1 51  ARG n 
1 52  HIS n 
1 53  ARG n 
1 54  LEU n 
1 55  SER n 
1 56  ARG n 
1 57  GLY n 
1 58  GLY n 
1 59  TYR n 
1 60  THR n 
1 61  SER n 
1 62  SER n 
1 63  GLU n 
1 64  GLU n 
1 65  PHE n 
1 66  ALA n 
1 67  ALA n 
1 68  ASP n 
1 69  ALA n 
1 70  LEU n 
1 71  LEU n 
1 72  VAL n 
1 73  PHE n 
1 74  ASP n 
1 75  ASN n 
1 76  CYS n 
1 77  GLN n 
1 78  THR n 
1 79  PHE n 
1 80  ASN n 
1 81  GLU n 
1 82  ASP n 
1 83  ASP n 
1 84  SER n 
1 85  GLU n 
1 86  VAL n 
1 87  GLY n 
1 88  LYS n 
1 89  ALA n 
1 90  GLY n 
1 91  HIS n 
1 92  ILE n 
1 93  MET n 
1 94  ARG n 
1 95  ARG n 
1 96  PHE n 
1 97  PHE n 
1 98  GLU n 
1 99  SER n 
1 100 ARG n 
1 101 TRP n 
1 102 GLU n 
1 103 GLU n 
1 104 PHE n 
1 105 TYR 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                   105 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'BAZ2A, KIAA0314, TIP5' 
_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 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_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               ? 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_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_
_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 
A1IAB non-polymer         . 
'1-[2,4-dimethyl-5-[(3~{R})-3-[4-(pyrrolidin-1-ylmethyl)-1~{H}-pyrazol-3-yl]piperidin-1-yl]carbonyl-1~{H}-pyrrol-3-yl]ethanone' ? 
'C22 H31 N5 O2'  397.514 
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 
CYS   'L-peptide linking' y CYSTEINE ?                 'C3 H7 N O2 S'   121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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 
MG    non-polymer         . 'MAGNESIUM ION' ?                 'Mg 2'           24.305  
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   SER 1   1794 ?    ?   ?   A . n 
A 1 2   MET 2   1795 ?    ?   ?   A . n 
A 1 3   HIS 3   1796 1796 HIS HIS A . n 
A 1 4   SER 4   1797 1797 SER SER A . n 
A 1 5   ASP 5   1798 1798 ASP ASP A . n 
A 1 6   LEU 6   1799 1799 LEU LEU A . n 
A 1 7   THR 7   1800 1800 THR THR A . n 
A 1 8   PHE 8   1801 1801 PHE PHE A . n 
A 1 9   CYS 9   1802 1802 CYS CYS A . n 
A 1 10  GLU 10  1803 1803 GLU GLU A . n 
A 1 11  ILE 11  1804 1804 ILE ILE A . n 
A 1 12  ILE 12  1805 1805 ILE ILE A . n 
A 1 13  LEU 13  1806 1806 LEU LEU A . n 
A 1 14  MET 14  1807 1807 MET MET A . n 
A 1 15  GLU 15  1808 1808 GLU GLU A . n 
A 1 16  MET 16  1809 1809 MET MET A . n 
A 1 17  GLU 17  1810 1810 GLU GLU A . n 
A 1 18  SER 18  1811 1811 SER SER A . n 
A 1 19  HIS 19  1812 1812 HIS HIS A . n 
A 1 20  ASP 20  1813 1813 ASP ASP A . n 
A 1 21  ALA 21  1814 1814 ALA ALA A . n 
A 1 22  ALA 22  1815 1815 ALA ALA A . n 
A 1 23  TRP 23  1816 1816 TRP TRP A . n 
A 1 24  PRO 24  1817 1817 PRO PRO A . n 
A 1 25  PHE 25  1818 1818 PHE PHE A . n 
A 1 26  LEU 26  1819 1819 LEU LEU A . n 
A 1 27  GLU 27  1820 1820 GLU GLU A . n 
A 1 28  PRO 28  1821 1821 PRO PRO A . n 
A 1 29  VAL 29  1822 1822 VAL VAL A . n 
A 1 30  ASN 30  1823 1823 ASN ASN A . n 
A 1 31  PRO 31  1824 1824 PRO PRO A . n 
A 1 32  ARG 32  1825 1825 ARG ARG A . n 
A 1 33  LEU 33  1826 1826 LEU LEU A . n 
A 1 34  VAL 34  1827 1827 VAL VAL A . n 
A 1 35  SER 35  1828 1828 SER SER A . n 
A 1 36  GLY 36  1829 1829 GLY GLY A . n 
A 1 37  TYR 37  1830 1830 TYR TYR A . n 
A 1 38  ARG 38  1831 1831 ARG ARG A . n 
A 1 39  ARG 39  1832 1832 ARG ARG A . n 
A 1 40  ILE 40  1833 1833 ILE ILE A . n 
A 1 41  ILE 41  1834 1834 ILE ILE A . n 
A 1 42  LYS 42  1835 1835 LYS LYS A . n 
A 1 43  ASN 43  1836 1836 ASN ASN A . n 
A 1 44  PRO 44  1837 1837 PRO PRO A . n 
A 1 45  MET 45  1838 1838 MET MET A . n 
A 1 46  ASP 46  1839 1839 ASP ASP A . n 
A 1 47  PHE 47  1840 1840 PHE PHE A . n 
A 1 48  SER 48  1841 1841 SER SER A . n 
A 1 49  THR 49  1842 1842 THR THR A . n 
A 1 50  MET 50  1843 1843 MET MET A . n 
A 1 51  ARG 51  1844 1844 ARG ARG A . n 
A 1 52  HIS 52  1845 1845 HIS HIS A . n 
A 1 53  ARG 53  1846 1846 ARG ARG A . n 
A 1 54  LEU 54  1847 1847 LEU LEU A . n 
A 1 55  SER 55  1848 1848 SER SER A . n 
A 1 56  ARG 56  1849 1849 ARG ARG A . n 
A 1 57  GLY 57  1850 1850 GLY GLY A . n 
A 1 58  GLY 58  1851 1851 GLY GLY A . n 
A 1 59  TYR 59  1852 1852 TYR TYR A . n 
A 1 60  THR 60  1853 1853 THR THR A . n 
A 1 61  SER 61  1854 1854 SER SER A . n 
A 1 62  SER 62  1855 1855 SER SER A . n 
A 1 63  GLU 63  1856 1856 GLU GLU A . n 
A 1 64  GLU 64  1857 1857 GLU GLU A . n 
A 1 65  PHE 65  1858 1858 PHE PHE A . n 
A 1 66  ALA 66  1859 1859 ALA ALA A . n 
A 1 67  ALA 67  1860 1860 ALA ALA A . n 
A 1 68  ASP 68  1861 1861 ASP ASP A . n 
A 1 69  ALA 69  1862 1862 ALA ALA A . n 
A 1 70  LEU 70  1863 1863 LEU LEU A . n 
A 1 71  LEU 71  1864 1864 LEU LEU A . n 
A 1 72  VAL 72  1865 1865 VAL VAL A . n 
A 1 73  PHE 73  1866 1866 PHE PHE A . n 
A 1 74  ASP 74  1867 1867 ASP ASP A . n 
A 1 75  ASN 75  1868 1868 ASN ASN A . n 
A 1 76  CYS 76  1869 1869 CYS CYS A . n 
A 1 77  GLN 77  1870 1870 GLN GLN A . n 
A 1 78  THR 78  1871 1871 THR THR A . n 
A 1 79  PHE 79  1872 1872 PHE PHE A . n 
A 1 80  ASN 80  1873 1873 ASN ASN A . n 
A 1 81  GLU 81  1874 1874 GLU GLU A . n 
A 1 82  ASP 82  1875 1875 ASP ASP A . n 
A 1 83  ASP 83  1876 1876 ASP ASP A . n 
A 1 84  SER 84  1877 1877 SER SER A . n 
A 1 85  GLU 85  1878 1878 GLU GLU A . n 
A 1 86  VAL 86  1879 1879 VAL VAL A . n 
A 1 87  GLY 87  1880 1880 GLY GLY A . n 
A 1 88  LYS 88  1881 1881 LYS LYS A . n 
A 1 89  ALA 89  1882 1882 ALA ALA A . n 
A 1 90  GLY 90  1883 1883 GLY GLY A . n 
A 1 91  HIS 91  1884 1884 HIS HIS A . n 
A 1 92  ILE 92  1885 1885 ILE ILE A . n 
A 1 93  MET 93  1886 1886 MET MET A . n 
A 1 94  ARG 94  1887 1887 ARG ARG A . n 
A 1 95  ARG 95  1888 1888 ARG ARG A . n 
A 1 96  PHE 96  1889 1889 PHE PHE A . n 
A 1 97  PHE 97  1890 1890 PHE PHE A . n 
A 1 98  GLU 98  1891 1891 GLU GLU A . n 
A 1 99  SER 99  1892 1892 SER SER A . n 
A 1 100 ARG 100 1893 1893 ARG ARG A . n 
A 1 101 TRP 101 1894 1894 TRP TRP A . n 
A 1 102 GLU 102 1895 1895 GLU GLU A . n 
A 1 103 GLU 103 1896 1896 GLU GLU A . n 
A 1 104 PHE 104 1897 1897 PHE PHE A . n 
A 1 105 TYR 105 1898 1898 TYR TYR A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IAB 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IAB 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
B 2 A1IAB 1  1901 1901 A1IAB D18 A . 
C 3 EDO   1  1902 2001 EDO   EDO A . 
D 4 MG    1  1903 1    MG    MG  A . 
E 5 HOH   1  2001 2    HOH   HOH A . 
E 5 HOH   2  2002 22   HOH   HOH A . 
E 5 HOH   3  2003 33   HOH   HOH A . 
E 5 HOH   4  2004 10   HOH   HOH A . 
E 5 HOH   5  2005 9    HOH   HOH A . 
E 5 HOH   6  2006 11   HOH   HOH A . 
E 5 HOH   7  2007 24   HOH   HOH A . 
E 5 HOH   8  2008 17   HOH   HOH A . 
E 5 HOH   9  2009 13   HOH   HOH A . 
E 5 HOH   10 2010 39   HOH   HOH A . 
E 5 HOH   11 2011 28   HOH   HOH A . 
E 5 HOH   12 2012 1    HOH   HOH A . 
E 5 HOH   13 2013 23   HOH   HOH A . 
E 5 HOH   14 2014 14   HOH   HOH A . 
E 5 HOH   15 2015 12   HOH   HOH A . 
E 5 HOH   16 2016 34   HOH   HOH A . 
E 5 HOH   17 2017 21   HOH   HOH A . 
E 5 HOH   18 2018 5    HOH   HOH A . 
E 5 HOH   19 2019 7    HOH   HOH A . 
E 5 HOH   20 2020 8    HOH   HOH A . 
E 5 HOH   21 2021 19   HOH   HOH A . 
E 5 HOH   22 2022 20   HOH   HOH A . 
E 5 HOH   23 2023 27   HOH   HOH A . 
E 5 HOH   24 2024 38   HOH   HOH A . 
E 5 HOH   25 2025 3    HOH   HOH A . 
E 5 HOH   26 2026 4    HOH   HOH A . 
E 5 HOH   27 2027 15   HOH   HOH A . 
E 5 HOH   28 2028 25   HOH   HOH A . 
E 5 HOH   29 2029 31   HOH   HOH A . 
E 5 HOH   30 2030 36   HOH   HOH A . 
E 5 HOH   31 2031 6    HOH   HOH A . 
E 5 HOH   32 2032 40   HOH   HOH A . 
E 5 HOH   33 2033 16   HOH   HOH A . 
E 5 HOH   34 2034 37   HOH   HOH A . 
E 5 HOH   35 2035 26   HOH   HOH A . 
E 5 HOH   36 2036 29   HOH   HOH A . 
E 5 HOH   37 2037 35   HOH   HOH A . 
E 5 HOH   38 2038 43   HOH   HOH A . 
E 5 HOH   39 2039 41   HOH   HOH A . 
E 5 HOH   40 2040 44   HOH   HOH A . 
E 5 HOH   41 2041 32   HOH   HOH A . 
E 5 HOH   42 2042 18   HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.11.1_2575: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F71 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     93.465 
_cell.length_a_esd                 ? 
_cell.length_b                     93.465 
_cell.length_b_esd                 ? 
_cell.length_c                     33.190 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9F71 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 31 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9F71 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.38 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          63.66 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20% PEG3350, 0.2 M MgCl2' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-05-25 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9997 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ELETTRA BEAMLINE 11.2C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9997 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   11.2C 
_diffrn_source.pdbx_synchrotron_site       ELETTRA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F71 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.35 
_reflns.d_resolution_low                               80.94 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     7143 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                17.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.02 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.107 
_reflns.pdbx_Rpim_I_all                                0.025 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       126823 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.104 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.35 
_reflns_shell.d_res_low                                     2.43 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           7930 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             681 
_reflns_shell.percent_possible_obs                          100.0 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               11.6 
_reflns_shell.pdbx_chi_squared                              1.00 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.5 
_reflns_shell.pdbx_Rrim_I_all                               1.031 
_reflns_shell.pdbx_Rpim_I_all                               0.298 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.813 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.985 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9F71 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.350 
_refine.ls_d_res_low                             40.472 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     7128 
_refine.ls_number_reflns_R_free                  331 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 4.64 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1846 
_refine.ls_R_factor_R_free                       0.2292 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1825 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.68 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.28 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.350 
_refine_hist.d_res_low                        40.472 
_refine_hist.number_atoms_solvent             42 
_refine_hist.number_atoms_total               928 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        852 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  ? 951  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.719  ? 1287 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 21.520 ? 359  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.045  ? 121  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 166  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.3503 2.9609 . . 157 3341 100.00 . . . . 0.2290 . . . . . . . . . . . 0.2813 
'X-RAY DIFFRACTION' 2.9609 40.472 . . 174 3456 100.00 . . . . 0.1689 . . . . . . . . . . . 0.2137 
# 
_struct.entry_id                     9F71 
_struct.title                        'BAZ2A bromodomain in complex with acetylpyrrole derivative compound 26-TND18' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9F71 
_struct_keywords.text            'Four helical bundle, 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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BAZ2A_HUMAN 
_struct_ref.pdbx_db_accession          Q9UIF9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;HSDLTFCEIILMEMESHDAAWPFLEPVNPRLVSGYRRIIKNPMDFSTMRERLLRGGYTSSEEFAADALLVFDNCQTFNED
DSEVGKAGHIMRRFFESRWEEFY
;
_struct_ref.pdbx_align_begin           1796 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9F71 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 105 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9UIF9 
_struct_ref_seq.db_align_beg                  1796 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1898 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1796 
_struct_ref_seq.pdbx_auth_seq_align_end       1898 
# 
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 9F71 SER A 1  ? UNP Q9UIF9 ?   ?    'expression tag'      1794 1 
1 9F71 MET A 2  ? UNP Q9UIF9 ?   ?    'expression tag'      1795 2 
1 9F71 HIS A 52 ? UNP Q9UIF9 GLU 1845 'engineered mutation' 1845 3 
1 9F71 SER A 55 ? UNP Q9UIF9 LEU 1848 'engineered mutation' 1848 4 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 900  ? 
1 MORE         -2   ? 
1 'SSA (A^2)'  6270 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
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 HIS A 3  ? HIS A 19  ? HIS A 1796 HIS A 1812 1 ? 17 
HELX_P HELX_P2 AA2 ASP A 20 ? TRP A 23  ? ASP A 1813 TRP A 1816 5 ? 4  
HELX_P HELX_P3 AA3 ASN A 30 ? VAL A 34  ? ASN A 1823 VAL A 1827 5 ? 5  
HELX_P HELX_P4 AA4 GLY A 36 ? ILE A 41  ? GLY A 1829 ILE A 1834 1 ? 6  
HELX_P HELX_P5 AA5 ASP A 46 ? ARG A 56  ? ASP A 1839 ARG A 1849 1 ? 11 
HELX_P HELX_P6 AA6 SER A 61 ? ASN A 80  ? SER A 1854 ASN A 1873 1 ? 20 
HELX_P HELX_P7 AA7 SER A 84 ? GLU A 103 ? SER A 1877 GLU A 1896 1 ? 20 
# 
_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 
metalc1 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 1903 A HOH 2010 1_555 ? ? ? ? ? ? ? 2.348 ? ? 
metalc2 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 1903 A HOH 2032 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc3 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 1903 A HOH 2038 6_554 ? ? ? ? ? ? ? 2.305 ? ? 
metalc4 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 1903 A HOH 2039 6_554 ? ? ? ? ? ? ? 2.474 ? ? 
metalc5 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 1903 A HOH 2040 6_554 ? ? ? ? ? ? ? 2.707 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O ? E HOH . ? A HOH 2010 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2032 ? 1_555 98.1  ? 
2  O ? E HOH . ? A HOH 2010 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2038 ? 6_554 93.2  ? 
3  O ? E HOH . ? A HOH 2032 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2038 ? 6_554 162.3 ? 
4  O ? E HOH . ? A HOH 2010 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2039 ? 6_554 83.2  ? 
5  O ? E HOH . ? A HOH 2032 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2039 ? 6_554 61.5  ? 
6  O ? E HOH . ? A HOH 2038 ? 6_554 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2039 ? 6_554 106.7 ? 
7  O ? E HOH . ? A HOH 2010 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2040 ? 6_554 96.6  ? 
8  O ? E HOH . ? A HOH 2032 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2040 ? 6_554 79.7  ? 
9  O ? E HOH . ? A HOH 2038 ? 6_554 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2040 ? 6_554 112.6 ? 
10 O ? E HOH . ? A HOH 2039 ? 6_554 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2040 ? 6_554 140.6 ? 
# 
_pdbx_entry_details.entry_id                   9F71 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C15 
_pdbx_validate_chiral.label_alt_id    B 
_pdbx_validate_chiral.auth_asym_id    A 
_pdbx_validate_chiral.auth_comp_id    A1IAB 
_pdbx_validate_chiral.auth_seq_id     1901 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         'WRONG HAND' 
_pdbx_validate_chiral.omega           . 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     2029 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_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[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -34.5808 25.6996 -12.2256 0.3508 ? -0.0963 ? 0.0434 ? 0.5562 ? 0.0963  ? 0.4898 ? 1.5366 ? 0.6529 
? 0.3822  ? 2.8035 ? 0.1826 ? 3.2429 ? 0.1563  ? -0.4348 ? -0.3899 ? 0.3597  ? -0.3624 ? 0.1823  ? 0.5861 ? -0.4649 ? 0.1977 ? 
2 'X-RAY DIFFRACTION' ? refined -32.6993 27.8355 -24.4327 0.3730 ? -0.0478 ? 0.0050 ? 0.5058 ? -0.0443 ? 0.4204 ? 1.8708 ? 1.1576 
? -0.2147 ? 1.1478 ? 0.3801 ? 2.3567 ? -0.1223 ? 0.1011  ? -0.3344 ? -0.2902 ? 0.0411  ? -0.0880 ? 0.1447 ? -0.5115 ? 0.0858 ? 
3 'X-RAY DIFFRACTION' ? refined -26.4913 31.8090 -12.9006 0.2670 ? -0.0312 ? 0.0107 ? 0.4062 ? 0.0096  ? 0.3457 ? 2.6128 ? 0.9483 
? 0.5634  ? 3.5504 ? 0.7184 ? 3.9272 ? 0.0582  ? -0.1870 ? -0.2826 ? 0.0621  ? -0.2143 ? -0.2159 ? 0.0867 ? -0.1514 ? 0.1980 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1796 through 1823 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1824 through 1854 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1855 through 1898 )
;
# 
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 SER 1794 ? A SER 1 
2 1 Y 1 A MET 1795 ? A MET 2 
# 
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 
A1IAB C01  C  N N 1   
A1IAB C02  C  N N 2   
A1IAB C04  C  Y N 3   
A1IAB C05  C  Y N 4   
A1IAB C06  C  N N 5   
A1IAB C08  C  Y N 6   
A1IAB C09  C  N N 7   
A1IAB C12  C  N N 8   
A1IAB C13  C  N N 9   
A1IAB C14  C  N N 10  
A1IAB C15  C  N R 11  
A1IAB C16  C  N N 12  
A1IAB C17  C  Y N 13  
A1IAB C18  C  Y N 14  
A1IAB C19  C  N N 15  
A1IAB C21  C  N N 16  
A1IAB C22  C  N N 17  
A1IAB C23  C  N N 18  
A1IAB C24  C  N N 19  
A1IAB C25  C  Y N 20  
A1IAB C28  C  Y N 21  
A1IAB C29  C  N N 22  
A1IAB N07  N  Y N 23  
A1IAB N11  N  N N 24  
A1IAB N20  N  N N 25  
A1IAB N26  N  Y N 26  
A1IAB N27  N  Y N 27  
A1IAB O03  O  N N 28  
A1IAB O10  O  N N 29  
A1IAB H1   H  N N 30  
A1IAB H2   H  N N 31  
A1IAB H3   H  N N 32  
A1IAB H4   H  N N 33  
A1IAB H5   H  N N 34  
A1IAB H6   H  N N 35  
A1IAB H7   H  N N 36  
A1IAB H8   H  N N 37  
A1IAB H9   H  N N 38  
A1IAB H10  H  N N 39  
A1IAB H11  H  N N 40  
A1IAB H12  H  N N 41  
A1IAB H13  H  N N 42  
A1IAB H14  H  N N 43  
A1IAB H15  H  N N 44  
A1IAB H16  H  N N 45  
A1IAB H17  H  N N 46  
A1IAB H18  H  N N 47  
A1IAB H19  H  N N 48  
A1IAB H20  H  N N 49  
A1IAB H21  H  N N 50  
A1IAB H22  H  N N 51  
A1IAB H23  H  N N 52  
A1IAB H24  H  N N 53  
A1IAB H25  H  N N 54  
A1IAB H26  H  N N 55  
A1IAB H27  H  N N 56  
A1IAB H28  H  N N 57  
A1IAB H29  H  N N 58  
A1IAB H30  H  N N 59  
A1IAB H32  H  N N 60  
ALA   N    N  N N 61  
ALA   CA   C  N S 62  
ALA   C    C  N N 63  
ALA   O    O  N N 64  
ALA   CB   C  N N 65  
ALA   OXT  O  N N 66  
ALA   H    H  N N 67  
ALA   H2   H  N N 68  
ALA   HA   H  N N 69  
ALA   HB1  H  N N 70  
ALA   HB2  H  N N 71  
ALA   HB3  H  N N 72  
ALA   HXT  H  N N 73  
ARG   N    N  N N 74  
ARG   CA   C  N S 75  
ARG   C    C  N N 76  
ARG   O    O  N N 77  
ARG   CB   C  N N 78  
ARG   CG   C  N N 79  
ARG   CD   C  N N 80  
ARG   NE   N  N N 81  
ARG   CZ   C  N N 82  
ARG   NH1  N  N N 83  
ARG   NH2  N  N N 84  
ARG   OXT  O  N N 85  
ARG   H    H  N N 86  
ARG   H2   H  N N 87  
ARG   HA   H  N N 88  
ARG   HB2  H  N N 89  
ARG   HB3  H  N N 90  
ARG   HG2  H  N N 91  
ARG   HG3  H  N N 92  
ARG   HD2  H  N N 93  
ARG   HD3  H  N N 94  
ARG   HE   H  N N 95  
ARG   HH11 H  N N 96  
ARG   HH12 H  N N 97  
ARG   HH21 H  N N 98  
ARG   HH22 H  N N 99  
ARG   HXT  H  N N 100 
ASN   N    N  N N 101 
ASN   CA   C  N S 102 
ASN   C    C  N N 103 
ASN   O    O  N N 104 
ASN   CB   C  N N 105 
ASN   CG   C  N N 106 
ASN   OD1  O  N N 107 
ASN   ND2  N  N N 108 
ASN   OXT  O  N N 109 
ASN   H    H  N N 110 
ASN   H2   H  N N 111 
ASN   HA   H  N N 112 
ASN   HB2  H  N N 113 
ASN   HB3  H  N N 114 
ASN   HD21 H  N N 115 
ASN   HD22 H  N N 116 
ASN   HXT  H  N N 117 
ASP   N    N  N N 118 
ASP   CA   C  N S 119 
ASP   C    C  N N 120 
ASP   O    O  N N 121 
ASP   CB   C  N N 122 
ASP   CG   C  N N 123 
ASP   OD1  O  N N 124 
ASP   OD2  O  N N 125 
ASP   OXT  O  N N 126 
ASP   H    H  N N 127 
ASP   H2   H  N N 128 
ASP   HA   H  N N 129 
ASP   HB2  H  N N 130 
ASP   HB3  H  N N 131 
ASP   HD2  H  N N 132 
ASP   HXT  H  N N 133 
CYS   N    N  N N 134 
CYS   CA   C  N R 135 
CYS   C    C  N N 136 
CYS   O    O  N N 137 
CYS   CB   C  N N 138 
CYS   SG   S  N N 139 
CYS   OXT  O  N N 140 
CYS   H    H  N N 141 
CYS   H2   H  N N 142 
CYS   HA   H  N N 143 
CYS   HB2  H  N N 144 
CYS   HB3  H  N N 145 
CYS   HG   H  N N 146 
CYS   HXT  H  N N 147 
EDO   C1   C  N N 148 
EDO   O1   O  N N 149 
EDO   C2   C  N N 150 
EDO   O2   O  N N 151 
EDO   H11  H  N N 152 
EDO   H12  H  N N 153 
EDO   HO1  H  N N 154 
EDO   H21  H  N N 155 
EDO   H22  H  N N 156 
EDO   HO2  H  N N 157 
GLN   N    N  N N 158 
GLN   CA   C  N S 159 
GLN   C    C  N N 160 
GLN   O    O  N N 161 
GLN   CB   C  N N 162 
GLN   CG   C  N N 163 
GLN   CD   C  N N 164 
GLN   OE1  O  N N 165 
GLN   NE2  N  N N 166 
GLN   OXT  O  N N 167 
GLN   H    H  N N 168 
GLN   H2   H  N N 169 
GLN   HA   H  N N 170 
GLN   HB2  H  N N 171 
GLN   HB3  H  N N 172 
GLN   HG2  H  N N 173 
GLN   HG3  H  N N 174 
GLN   HE21 H  N N 175 
GLN   HE22 H  N N 176 
GLN   HXT  H  N N 177 
GLU   N    N  N N 178 
GLU   CA   C  N S 179 
GLU   C    C  N N 180 
GLU   O    O  N N 181 
GLU   CB   C  N N 182 
GLU   CG   C  N N 183 
GLU   CD   C  N N 184 
GLU   OE1  O  N N 185 
GLU   OE2  O  N N 186 
GLU   OXT  O  N N 187 
GLU   H    H  N N 188 
GLU   H2   H  N N 189 
GLU   HA   H  N N 190 
GLU   HB2  H  N N 191 
GLU   HB3  H  N N 192 
GLU   HG2  H  N N 193 
GLU   HG3  H  N N 194 
GLU   HE2  H  N N 195 
GLU   HXT  H  N N 196 
GLY   N    N  N N 197 
GLY   CA   C  N N 198 
GLY   C    C  N N 199 
GLY   O    O  N N 200 
GLY   OXT  O  N N 201 
GLY   H    H  N N 202 
GLY   H2   H  N N 203 
GLY   HA2  H  N N 204 
GLY   HA3  H  N N 205 
GLY   HXT  H  N N 206 
HIS   N    N  N N 207 
HIS   CA   C  N S 208 
HIS   C    C  N N 209 
HIS   O    O  N N 210 
HIS   CB   C  N N 211 
HIS   CG   C  Y N 212 
HIS   ND1  N  Y N 213 
HIS   CD2  C  Y N 214 
HIS   CE1  C  Y N 215 
HIS   NE2  N  Y N 216 
HIS   OXT  O  N N 217 
HIS   H    H  N N 218 
HIS   H2   H  N N 219 
HIS   HA   H  N N 220 
HIS   HB2  H  N N 221 
HIS   HB3  H  N N 222 
HIS   HD1  H  N N 223 
HIS   HD2  H  N N 224 
HIS   HE1  H  N N 225 
HIS   HE2  H  N N 226 
HIS   HXT  H  N N 227 
HOH   O    O  N N 228 
HOH   H1   H  N N 229 
HOH   H2   H  N N 230 
ILE   N    N  N N 231 
ILE   CA   C  N S 232 
ILE   C    C  N N 233 
ILE   O    O  N N 234 
ILE   CB   C  N S 235 
ILE   CG1  C  N N 236 
ILE   CG2  C  N N 237 
ILE   CD1  C  N N 238 
ILE   OXT  O  N N 239 
ILE   H    H  N N 240 
ILE   H2   H  N N 241 
ILE   HA   H  N N 242 
ILE   HB   H  N N 243 
ILE   HG12 H  N N 244 
ILE   HG13 H  N N 245 
ILE   HG21 H  N N 246 
ILE   HG22 H  N N 247 
ILE   HG23 H  N N 248 
ILE   HD11 H  N N 249 
ILE   HD12 H  N N 250 
ILE   HD13 H  N N 251 
ILE   HXT  H  N N 252 
LEU   N    N  N N 253 
LEU   CA   C  N S 254 
LEU   C    C  N N 255 
LEU   O    O  N N 256 
LEU   CB   C  N N 257 
LEU   CG   C  N N 258 
LEU   CD1  C  N N 259 
LEU   CD2  C  N N 260 
LEU   OXT  O  N N 261 
LEU   H    H  N N 262 
LEU   H2   H  N N 263 
LEU   HA   H  N N 264 
LEU   HB2  H  N N 265 
LEU   HB3  H  N N 266 
LEU   HG   H  N N 267 
LEU   HD11 H  N N 268 
LEU   HD12 H  N N 269 
LEU   HD13 H  N N 270 
LEU   HD21 H  N N 271 
LEU   HD22 H  N N 272 
LEU   HD23 H  N N 273 
LEU   HXT  H  N N 274 
LYS   N    N  N N 275 
LYS   CA   C  N S 276 
LYS   C    C  N N 277 
LYS   O    O  N N 278 
LYS   CB   C  N N 279 
LYS   CG   C  N N 280 
LYS   CD   C  N N 281 
LYS   CE   C  N N 282 
LYS   NZ   N  N N 283 
LYS   OXT  O  N N 284 
LYS   H    H  N N 285 
LYS   H2   H  N N 286 
LYS   HA   H  N N 287 
LYS   HB2  H  N N 288 
LYS   HB3  H  N N 289 
LYS   HG2  H  N N 290 
LYS   HG3  H  N N 291 
LYS   HD2  H  N N 292 
LYS   HD3  H  N N 293 
LYS   HE2  H  N N 294 
LYS   HE3  H  N N 295 
LYS   HZ1  H  N N 296 
LYS   HZ2  H  N N 297 
LYS   HZ3  H  N N 298 
LYS   HXT  H  N N 299 
MET   N    N  N N 300 
MET   CA   C  N S 301 
MET   C    C  N N 302 
MET   O    O  N N 303 
MET   CB   C  N N 304 
MET   CG   C  N N 305 
MET   SD   S  N N 306 
MET   CE   C  N N 307 
MET   OXT  O  N N 308 
MET   H    H  N N 309 
MET   H2   H  N N 310 
MET   HA   H  N N 311 
MET   HB2  H  N N 312 
MET   HB3  H  N N 313 
MET   HG2  H  N N 314 
MET   HG3  H  N N 315 
MET   HE1  H  N N 316 
MET   HE2  H  N N 317 
MET   HE3  H  N N 318 
MET   HXT  H  N N 319 
MG    MG   MG N N 320 
PHE   N    N  N N 321 
PHE   CA   C  N S 322 
PHE   C    C  N N 323 
PHE   O    O  N N 324 
PHE   CB   C  N N 325 
PHE   CG   C  Y N 326 
PHE   CD1  C  Y N 327 
PHE   CD2  C  Y N 328 
PHE   CE1  C  Y N 329 
PHE   CE2  C  Y N 330 
PHE   CZ   C  Y N 331 
PHE   OXT  O  N N 332 
PHE   H    H  N N 333 
PHE   H2   H  N N 334 
PHE   HA   H  N N 335 
PHE   HB2  H  N N 336 
PHE   HB3  H  N N 337 
PHE   HD1  H  N N 338 
PHE   HD2  H  N N 339 
PHE   HE1  H  N N 340 
PHE   HE2  H  N N 341 
PHE   HZ   H  N N 342 
PHE   HXT  H  N N 343 
PRO   N    N  N N 344 
PRO   CA   C  N S 345 
PRO   C    C  N N 346 
PRO   O    O  N N 347 
PRO   CB   C  N N 348 
PRO   CG   C  N N 349 
PRO   CD   C  N N 350 
PRO   OXT  O  N N 351 
PRO   H    H  N N 352 
PRO   HA   H  N N 353 
PRO   HB2  H  N N 354 
PRO   HB3  H  N N 355 
PRO   HG2  H  N N 356 
PRO   HG3  H  N N 357 
PRO   HD2  H  N N 358 
PRO   HD3  H  N N 359 
PRO   HXT  H  N N 360 
SER   N    N  N N 361 
SER   CA   C  N S 362 
SER   C    C  N N 363 
SER   O    O  N N 364 
SER   CB   C  N N 365 
SER   OG   O  N N 366 
SER   OXT  O  N N 367 
SER   H    H  N N 368 
SER   H2   H  N N 369 
SER   HA   H  N N 370 
SER   HB2  H  N N 371 
SER   HB3  H  N N 372 
SER   HG   H  N N 373 
SER   HXT  H  N N 374 
THR   N    N  N N 375 
THR   CA   C  N S 376 
THR   C    C  N N 377 
THR   O    O  N N 378 
THR   CB   C  N R 379 
THR   OG1  O  N N 380 
THR   CG2  C  N N 381 
THR   OXT  O  N N 382 
THR   H    H  N N 383 
THR   H2   H  N N 384 
THR   HA   H  N N 385 
THR   HB   H  N N 386 
THR   HG1  H  N N 387 
THR   HG21 H  N N 388 
THR   HG22 H  N N 389 
THR   HG23 H  N N 390 
THR   HXT  H  N N 391 
TRP   N    N  N N 392 
TRP   CA   C  N S 393 
TRP   C    C  N N 394 
TRP   O    O  N N 395 
TRP   CB   C  N N 396 
TRP   CG   C  Y N 397 
TRP   CD1  C  Y N 398 
TRP   CD2  C  Y N 399 
TRP   NE1  N  Y N 400 
TRP   CE2  C  Y N 401 
TRP   CE3  C  Y N 402 
TRP   CZ2  C  Y N 403 
TRP   CZ3  C  Y N 404 
TRP   CH2  C  Y N 405 
TRP   OXT  O  N N 406 
TRP   H    H  N N 407 
TRP   H2   H  N N 408 
TRP   HA   H  N N 409 
TRP   HB2  H  N N 410 
TRP   HB3  H  N N 411 
TRP   HD1  H  N N 412 
TRP   HE1  H  N N 413 
TRP   HE3  H  N N 414 
TRP   HZ2  H  N N 415 
TRP   HZ3  H  N N 416 
TRP   HH2  H  N N 417 
TRP   HXT  H  N N 418 
TYR   N    N  N N 419 
TYR   CA   C  N S 420 
TYR   C    C  N N 421 
TYR   O    O  N N 422 
TYR   CB   C  N N 423 
TYR   CG   C  Y N 424 
TYR   CD1  C  Y N 425 
TYR   CD2  C  Y N 426 
TYR   CE1  C  Y N 427 
TYR   CE2  C  Y N 428 
TYR   CZ   C  Y N 429 
TYR   OH   O  N N 430 
TYR   OXT  O  N N 431 
TYR   H    H  N N 432 
TYR   H2   H  N N 433 
TYR   HA   H  N N 434 
TYR   HB2  H  N N 435 
TYR   HB3  H  N N 436 
TYR   HD1  H  N N 437 
TYR   HD2  H  N N 438 
TYR   HE1  H  N N 439 
TYR   HE2  H  N N 440 
TYR   HH   H  N N 441 
TYR   HXT  H  N N 442 
VAL   N    N  N N 443 
VAL   CA   C  N S 444 
VAL   C    C  N N 445 
VAL   O    O  N N 446 
VAL   CB   C  N N 447 
VAL   CG1  C  N N 448 
VAL   CG2  C  N N 449 
VAL   OXT  O  N N 450 
VAL   H    H  N N 451 
VAL   H2   H  N N 452 
VAL   HA   H  N N 453 
VAL   HB   H  N N 454 
VAL   HG11 H  N N 455 
VAL   HG12 H  N N 456 
VAL   HG13 H  N N 457 
VAL   HG21 H  N N 458 
VAL   HG22 H  N N 459 
VAL   HG23 H  N N 460 
VAL   HXT  H  N N 461 
# 
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 
A1IAB C01 C02  sing N N 1   
A1IAB C02 O03  doub N N 2   
A1IAB C02 C04  sing N N 3   
A1IAB C29 C28  sing N N 4   
A1IAB C13 C14  sing N N 5   
A1IAB C13 C12  sing N N 6   
A1IAB C04 C28  sing Y N 7   
A1IAB C04 C05  doub Y N 8   
A1IAB C28 C08  doub Y N 9   
A1IAB C14 C15  sing N N 10  
A1IAB C05 C06  sing N N 11  
A1IAB C05 N07  sing Y N 12  
A1IAB C15 C17  sing N N 13  
A1IAB C15 C16  sing N N 14  
A1IAB C08 N07  sing Y N 15  
A1IAB C08 C09  sing N N 16  
A1IAB C12 N11  sing N N 17  
A1IAB C21 N20  sing N N 18  
A1IAB C21 C22  sing N N 19  
A1IAB C19 N20  sing N N 20  
A1IAB C19 C18  sing N N 21  
A1IAB C09 N11  sing N N 22  
A1IAB C09 O10  doub N N 23  
A1IAB N11 C16  sing N N 24  
A1IAB C17 C18  sing Y N 25  
A1IAB C17 N27  doub Y N 26  
A1IAB N20 C24  sing N N 27  
A1IAB C18 C25  doub Y N 28  
A1IAB N27 N26  sing Y N 29  
A1IAB C22 C23  sing N N 30  
A1IAB C25 N26  sing Y N 31  
A1IAB C24 C23  sing N N 32  
A1IAB C01 H1   sing N N 33  
A1IAB C01 H2   sing N N 34  
A1IAB C01 H3   sing N N 35  
A1IAB C06 H4   sing N N 36  
A1IAB C06 H5   sing N N 37  
A1IAB C06 H6   sing N N 38  
A1IAB C12 H7   sing N N 39  
A1IAB C12 H8   sing N N 40  
A1IAB C13 H9   sing N N 41  
A1IAB C13 H10  sing N N 42  
A1IAB C14 H11  sing N N 43  
A1IAB C14 H12  sing N N 44  
A1IAB C15 H13  sing N N 45  
A1IAB C16 H14  sing N N 46  
A1IAB C16 H15  sing N N 47  
A1IAB C19 H16  sing N N 48  
A1IAB C19 H17  sing N N 49  
A1IAB C21 H18  sing N N 50  
A1IAB C21 H19  sing N N 51  
A1IAB C22 H20  sing N N 52  
A1IAB C22 H21  sing N N 53  
A1IAB C23 H22  sing N N 54  
A1IAB C23 H23  sing N N 55  
A1IAB C24 H24  sing N N 56  
A1IAB C24 H25  sing N N 57  
A1IAB C25 H26  sing N N 58  
A1IAB C29 H27  sing N N 59  
A1IAB C29 H28  sing N N 60  
A1IAB C29 H29  sing N N 61  
A1IAB N07 H30  sing N N 62  
A1IAB N26 H32  sing N N 63  
ALA   N   CA   sing N N 64  
ALA   N   H    sing N N 65  
ALA   N   H2   sing N N 66  
ALA   CA  C    sing N N 67  
ALA   CA  CB   sing N N 68  
ALA   CA  HA   sing N N 69  
ALA   C   O    doub N N 70  
ALA   C   OXT  sing N N 71  
ALA   CB  HB1  sing N N 72  
ALA   CB  HB2  sing N N 73  
ALA   CB  HB3  sing N N 74  
ALA   OXT HXT  sing N N 75  
ARG   N   CA   sing N N 76  
ARG   N   H    sing N N 77  
ARG   N   H2   sing N N 78  
ARG   CA  C    sing N N 79  
ARG   CA  CB   sing N N 80  
ARG   CA  HA   sing N N 81  
ARG   C   O    doub N N 82  
ARG   C   OXT  sing N N 83  
ARG   CB  CG   sing N N 84  
ARG   CB  HB2  sing N N 85  
ARG   CB  HB3  sing N N 86  
ARG   CG  CD   sing N N 87  
ARG   CG  HG2  sing N N 88  
ARG   CG  HG3  sing N N 89  
ARG   CD  NE   sing N N 90  
ARG   CD  HD2  sing N N 91  
ARG   CD  HD3  sing N N 92  
ARG   NE  CZ   sing N N 93  
ARG   NE  HE   sing N N 94  
ARG   CZ  NH1  sing N N 95  
ARG   CZ  NH2  doub N N 96  
ARG   NH1 HH11 sing N N 97  
ARG   NH1 HH12 sing N N 98  
ARG   NH2 HH21 sing N N 99  
ARG   NH2 HH22 sing N N 100 
ARG   OXT HXT  sing N N 101 
ASN   N   CA   sing N N 102 
ASN   N   H    sing N N 103 
ASN   N   H2   sing N N 104 
ASN   CA  C    sing N N 105 
ASN   CA  CB   sing N N 106 
ASN   CA  HA   sing N N 107 
ASN   C   O    doub N N 108 
ASN   C   OXT  sing N N 109 
ASN   CB  CG   sing N N 110 
ASN   CB  HB2  sing N N 111 
ASN   CB  HB3  sing N N 112 
ASN   CG  OD1  doub N N 113 
ASN   CG  ND2  sing N N 114 
ASN   ND2 HD21 sing N N 115 
ASN   ND2 HD22 sing N N 116 
ASN   OXT HXT  sing N N 117 
ASP   N   CA   sing N N 118 
ASP   N   H    sing N N 119 
ASP   N   H2   sing N N 120 
ASP   CA  C    sing N N 121 
ASP   CA  CB   sing N N 122 
ASP   CA  HA   sing N N 123 
ASP   C   O    doub N N 124 
ASP   C   OXT  sing N N 125 
ASP   CB  CG   sing N N 126 
ASP   CB  HB2  sing N N 127 
ASP   CB  HB3  sing N N 128 
ASP   CG  OD1  doub N N 129 
ASP   CG  OD2  sing N N 130 
ASP   OD2 HD2  sing N N 131 
ASP   OXT HXT  sing N N 132 
CYS   N   CA   sing N N 133 
CYS   N   H    sing N N 134 
CYS   N   H2   sing N N 135 
CYS   CA  C    sing N N 136 
CYS   CA  CB   sing N N 137 
CYS   CA  HA   sing N N 138 
CYS   C   O    doub N N 139 
CYS   C   OXT  sing N N 140 
CYS   CB  SG   sing N N 141 
CYS   CB  HB2  sing N N 142 
CYS   CB  HB3  sing N N 143 
CYS   SG  HG   sing N N 144 
CYS   OXT HXT  sing N N 145 
EDO   C1  O1   sing N N 146 
EDO   C1  C2   sing N N 147 
EDO   C1  H11  sing N N 148 
EDO   C1  H12  sing N N 149 
EDO   O1  HO1  sing N N 150 
EDO   C2  O2   sing N N 151 
EDO   C2  H21  sing N N 152 
EDO   C2  H22  sing N N 153 
EDO   O2  HO2  sing N N 154 
GLN   N   CA   sing N N 155 
GLN   N   H    sing N N 156 
GLN   N   H2   sing N N 157 
GLN   CA  C    sing N N 158 
GLN   CA  CB   sing N N 159 
GLN   CA  HA   sing N N 160 
GLN   C   O    doub N N 161 
GLN   C   OXT  sing N N 162 
GLN   CB  CG   sing N N 163 
GLN   CB  HB2  sing N N 164 
GLN   CB  HB3  sing N N 165 
GLN   CG  CD   sing N N 166 
GLN   CG  HG2  sing N N 167 
GLN   CG  HG3  sing N N 168 
GLN   CD  OE1  doub N N 169 
GLN   CD  NE2  sing N N 170 
GLN   NE2 HE21 sing N N 171 
GLN   NE2 HE22 sing N N 172 
GLN   OXT HXT  sing N N 173 
GLU   N   CA   sing N N 174 
GLU   N   H    sing N N 175 
GLU   N   H2   sing N N 176 
GLU   CA  C    sing N N 177 
GLU   CA  CB   sing N N 178 
GLU   CA  HA   sing N N 179 
GLU   C   O    doub N N 180 
GLU   C   OXT  sing N N 181 
GLU   CB  CG   sing N N 182 
GLU   CB  HB2  sing N N 183 
GLU   CB  HB3  sing N N 184 
GLU   CG  CD   sing N N 185 
GLU   CG  HG2  sing N N 186 
GLU   CG  HG3  sing N N 187 
GLU   CD  OE1  doub N N 188 
GLU   CD  OE2  sing N N 189 
GLU   OE2 HE2  sing N N 190 
GLU   OXT HXT  sing N N 191 
GLY   N   CA   sing N N 192 
GLY   N   H    sing N N 193 
GLY   N   H2   sing N N 194 
GLY   CA  C    sing N N 195 
GLY   CA  HA2  sing N N 196 
GLY   CA  HA3  sing N N 197 
GLY   C   O    doub N N 198 
GLY   C   OXT  sing N N 199 
GLY   OXT HXT  sing N N 200 
HIS   N   CA   sing N N 201 
HIS   N   H    sing N N 202 
HIS   N   H2   sing N N 203 
HIS   CA  C    sing N N 204 
HIS   CA  CB   sing N N 205 
HIS   CA  HA   sing N N 206 
HIS   C   O    doub N N 207 
HIS   C   OXT  sing N N 208 
HIS   CB  CG   sing N N 209 
HIS   CB  HB2  sing N N 210 
HIS   CB  HB3  sing N N 211 
HIS   CG  ND1  sing Y N 212 
HIS   CG  CD2  doub Y N 213 
HIS   ND1 CE1  doub Y N 214 
HIS   ND1 HD1  sing N N 215 
HIS   CD2 NE2  sing Y N 216 
HIS   CD2 HD2  sing N N 217 
HIS   CE1 NE2  sing Y N 218 
HIS   CE1 HE1  sing N N 219 
HIS   NE2 HE2  sing N N 220 
HIS   OXT HXT  sing N N 221 
HOH   O   H1   sing N N 222 
HOH   O   H2   sing N N 223 
ILE   N   CA   sing N N 224 
ILE   N   H    sing N N 225 
ILE   N   H2   sing N N 226 
ILE   CA  C    sing N N 227 
ILE   CA  CB   sing N N 228 
ILE   CA  HA   sing N N 229 
ILE   C   O    doub N N 230 
ILE   C   OXT  sing N N 231 
ILE   CB  CG1  sing N N 232 
ILE   CB  CG2  sing N N 233 
ILE   CB  HB   sing N N 234 
ILE   CG1 CD1  sing N N 235 
ILE   CG1 HG12 sing N N 236 
ILE   CG1 HG13 sing N N 237 
ILE   CG2 HG21 sing N N 238 
ILE   CG2 HG22 sing N N 239 
ILE   CG2 HG23 sing N N 240 
ILE   CD1 HD11 sing N N 241 
ILE   CD1 HD12 sing N N 242 
ILE   CD1 HD13 sing N N 243 
ILE   OXT HXT  sing N N 244 
LEU   N   CA   sing N N 245 
LEU   N   H    sing N N 246 
LEU   N   H2   sing N N 247 
LEU   CA  C    sing N N 248 
LEU   CA  CB   sing N N 249 
LEU   CA  HA   sing N N 250 
LEU   C   O    doub N N 251 
LEU   C   OXT  sing N N 252 
LEU   CB  CG   sing N N 253 
LEU   CB  HB2  sing N N 254 
LEU   CB  HB3  sing N N 255 
LEU   CG  CD1  sing N N 256 
LEU   CG  CD2  sing N N 257 
LEU   CG  HG   sing N N 258 
LEU   CD1 HD11 sing N N 259 
LEU   CD1 HD12 sing N N 260 
LEU   CD1 HD13 sing N N 261 
LEU   CD2 HD21 sing N N 262 
LEU   CD2 HD22 sing N N 263 
LEU   CD2 HD23 sing N N 264 
LEU   OXT HXT  sing N N 265 
LYS   N   CA   sing N N 266 
LYS   N   H    sing N N 267 
LYS   N   H2   sing N N 268 
LYS   CA  C    sing N N 269 
LYS   CA  CB   sing N N 270 
LYS   CA  HA   sing N N 271 
LYS   C   O    doub N N 272 
LYS   C   OXT  sing N N 273 
LYS   CB  CG   sing N N 274 
LYS   CB  HB2  sing N N 275 
LYS   CB  HB3  sing N N 276 
LYS   CG  CD   sing N N 277 
LYS   CG  HG2  sing N N 278 
LYS   CG  HG3  sing N N 279 
LYS   CD  CE   sing N N 280 
LYS   CD  HD2  sing N N 281 
LYS   CD  HD3  sing N N 282 
LYS   CE  NZ   sing N N 283 
LYS   CE  HE2  sing N N 284 
LYS   CE  HE3  sing N N 285 
LYS   NZ  HZ1  sing N N 286 
LYS   NZ  HZ2  sing N N 287 
LYS   NZ  HZ3  sing N N 288 
LYS   OXT HXT  sing N N 289 
MET   N   CA   sing N N 290 
MET   N   H    sing N N 291 
MET   N   H2   sing N N 292 
MET   CA  C    sing N N 293 
MET   CA  CB   sing N N 294 
MET   CA  HA   sing N N 295 
MET   C   O    doub N N 296 
MET   C   OXT  sing N N 297 
MET   CB  CG   sing N N 298 
MET   CB  HB2  sing N N 299 
MET   CB  HB3  sing N N 300 
MET   CG  SD   sing N N 301 
MET   CG  HG2  sing N N 302 
MET   CG  HG3  sing N N 303 
MET   SD  CE   sing N N 304 
MET   CE  HE1  sing N N 305 
MET   CE  HE2  sing N N 306 
MET   CE  HE3  sing N N 307 
MET   OXT HXT  sing N N 308 
PHE   N   CA   sing N N 309 
PHE   N   H    sing N N 310 
PHE   N   H2   sing N N 311 
PHE   CA  C    sing N N 312 
PHE   CA  CB   sing N N 313 
PHE   CA  HA   sing N N 314 
PHE   C   O    doub N N 315 
PHE   C   OXT  sing N N 316 
PHE   CB  CG   sing N N 317 
PHE   CB  HB2  sing N N 318 
PHE   CB  HB3  sing N N 319 
PHE   CG  CD1  doub Y N 320 
PHE   CG  CD2  sing Y N 321 
PHE   CD1 CE1  sing Y N 322 
PHE   CD1 HD1  sing N N 323 
PHE   CD2 CE2  doub Y N 324 
PHE   CD2 HD2  sing N N 325 
PHE   CE1 CZ   doub Y N 326 
PHE   CE1 HE1  sing N N 327 
PHE   CE2 CZ   sing Y N 328 
PHE   CE2 HE2  sing N N 329 
PHE   CZ  HZ   sing N N 330 
PHE   OXT HXT  sing N N 331 
PRO   N   CA   sing N N 332 
PRO   N   CD   sing N N 333 
PRO   N   H    sing N N 334 
PRO   CA  C    sing N N 335 
PRO   CA  CB   sing N N 336 
PRO   CA  HA   sing N N 337 
PRO   C   O    doub N N 338 
PRO   C   OXT  sing N N 339 
PRO   CB  CG   sing N N 340 
PRO   CB  HB2  sing N N 341 
PRO   CB  HB3  sing N N 342 
PRO   CG  CD   sing N N 343 
PRO   CG  HG2  sing N N 344 
PRO   CG  HG3  sing N N 345 
PRO   CD  HD2  sing N N 346 
PRO   CD  HD3  sing N N 347 
PRO   OXT HXT  sing N N 348 
SER   N   CA   sing N N 349 
SER   N   H    sing N N 350 
SER   N   H2   sing N N 351 
SER   CA  C    sing N N 352 
SER   CA  CB   sing N N 353 
SER   CA  HA   sing N N 354 
SER   C   O    doub N N 355 
SER   C   OXT  sing N N 356 
SER   CB  OG   sing N N 357 
SER   CB  HB2  sing N N 358 
SER   CB  HB3  sing N N 359 
SER   OG  HG   sing N N 360 
SER   OXT HXT  sing N N 361 
THR   N   CA   sing N N 362 
THR   N   H    sing N N 363 
THR   N   H2   sing N N 364 
THR   CA  C    sing N N 365 
THR   CA  CB   sing N N 366 
THR   CA  HA   sing N N 367 
THR   C   O    doub N N 368 
THR   C   OXT  sing N N 369 
THR   CB  OG1  sing N N 370 
THR   CB  CG2  sing N N 371 
THR   CB  HB   sing N N 372 
THR   OG1 HG1  sing N N 373 
THR   CG2 HG21 sing N N 374 
THR   CG2 HG22 sing N N 375 
THR   CG2 HG23 sing N N 376 
THR   OXT HXT  sing N N 377 
TRP   N   CA   sing N N 378 
TRP   N   H    sing N N 379 
TRP   N   H2   sing N N 380 
TRP   CA  C    sing N N 381 
TRP   CA  CB   sing N N 382 
TRP   CA  HA   sing N N 383 
TRP   C   O    doub N N 384 
TRP   C   OXT  sing N N 385 
TRP   CB  CG   sing N N 386 
TRP   CB  HB2  sing N N 387 
TRP   CB  HB3  sing N N 388 
TRP   CG  CD1  doub Y N 389 
TRP   CG  CD2  sing Y N 390 
TRP   CD1 NE1  sing Y N 391 
TRP   CD1 HD1  sing N N 392 
TRP   CD2 CE2  doub Y N 393 
TRP   CD2 CE3  sing Y N 394 
TRP   NE1 CE2  sing Y N 395 
TRP   NE1 HE1  sing N N 396 
TRP   CE2 CZ2  sing Y N 397 
TRP   CE3 CZ3  doub Y N 398 
TRP   CE3 HE3  sing N N 399 
TRP   CZ2 CH2  doub Y N 400 
TRP   CZ2 HZ2  sing N N 401 
TRP   CZ3 CH2  sing Y N 402 
TRP   CZ3 HZ3  sing N N 403 
TRP   CH2 HH2  sing N N 404 
TRP   OXT HXT  sing N N 405 
TYR   N   CA   sing N N 406 
TYR   N   H    sing N N 407 
TYR   N   H2   sing N N 408 
TYR   CA  C    sing N N 409 
TYR   CA  CB   sing N N 410 
TYR   CA  HA   sing N N 411 
TYR   C   O    doub N N 412 
TYR   C   OXT  sing N N 413 
TYR   CB  CG   sing N N 414 
TYR   CB  HB2  sing N N 415 
TYR   CB  HB3  sing N N 416 
TYR   CG  CD1  doub Y N 417 
TYR   CG  CD2  sing Y N 418 
TYR   CD1 CE1  sing Y N 419 
TYR   CD1 HD1  sing N N 420 
TYR   CD2 CE2  doub Y N 421 
TYR   CD2 HD2  sing N N 422 
TYR   CE1 CZ   doub Y N 423 
TYR   CE1 HE1  sing N N 424 
TYR   CE2 CZ   sing Y N 425 
TYR   CE2 HE2  sing N N 426 
TYR   CZ  OH   sing N N 427 
TYR   OH  HH   sing N N 428 
TYR   OXT HXT  sing N N 429 
VAL   N   CA   sing N N 430 
VAL   N   H    sing N N 431 
VAL   N   H2   sing N N 432 
VAL   CA  C    sing N N 433 
VAL   CA  CB   sing N N 434 
VAL   CA  HA   sing N N 435 
VAL   C   O    doub N N 436 
VAL   C   OXT  sing N N 437 
VAL   CB  CG1  sing N N 438 
VAL   CB  CG2  sing N N 439 
VAL   CB  HB   sing N N 440 
VAL   CG1 HG11 sing N N 441 
VAL   CG1 HG12 sing N N 442 
VAL   CG1 HG13 sing N N 443 
VAL   CG2 HG21 sing N N 444 
VAL   CG2 HG22 sing N N 445 
VAL   CG2 HG23 sing N N 446 
VAL   OXT HXT  sing N N 447 
# 
_pdbx_audit_support.funding_organization   'Italian Association for Cancer Research' 
_pdbx_audit_support.country                Italy 
_pdbx_audit_support.grant_number           'MFAG 2017 - ID. 19882' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5MGJ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9F71 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.010699 
_atom_sites.fract_transf_matrix[1][2]   0.006177 
_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]   0.012354 
_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]   0.030130 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
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   . HIS   A 1 3   ? -29.463 7.593  -11.084 1.00 123.91 ? 1796 HIS   A N   1 
ATOM   2   C  CA  . HIS   A 1 3   ? -28.339 8.526  -11.047 1.00 122.53 ? 1796 HIS   A CA  1 
ATOM   3   C  C   . HIS   A 1 3   ? -28.460 9.483  -9.859  1.00 119.80 ? 1796 HIS   A C   1 
ATOM   4   O  O   . HIS   A 1 3   ? -29.503 10.106 -9.651  1.00 117.31 ? 1796 HIS   A O   1 
ATOM   5   C  CB  . HIS   A 1 3   ? -28.261 9.312  -12.357 1.00 122.02 ? 1796 HIS   A CB  1 
ATOM   6   C  CG  . HIS   A 1 3   ? -26.878 9.415  -12.924 1.00 122.93 ? 1796 HIS   A CG  1 
ATOM   7   N  ND1 . HIS   A 1 3   ? -25.743 9.275  -12.152 1.00 124.44 ? 1796 HIS   A ND1 1 
ATOM   8   C  CD2 . HIS   A 1 3   ? -26.447 9.638  -14.189 1.00 121.58 ? 1796 HIS   A CD2 1 
ATOM   9   C  CE1 . HIS   A 1 3   ? -24.674 9.411  -12.917 1.00 123.97 ? 1796 HIS   A CE1 1 
ATOM   10  N  NE2 . HIS   A 1 3   ? -25.074 9.632  -14.157 1.00 122.62 ? 1796 HIS   A NE2 1 
ATOM   11  N  N   . SER   A 1 4   ? -27.389 9.587  -9.072  1.00 120.82 ? 1797 SER   A N   1 
ATOM   12  C  CA  . SER   A 1 4   ? -27.370 10.550 -7.978  1.00 120.10 ? 1797 SER   A CA  1 
ATOM   13  C  C   . SER   A 1 4   ? -27.068 11.958 -8.478  1.00 118.23 ? 1797 SER   A C   1 
ATOM   14  O  O   . SER   A 1 4   ? -27.459 12.940 -7.834  1.00 117.55 ? 1797 SER   A O   1 
ATOM   15  C  CB  . SER   A 1 4   ? -26.349 10.123 -6.921  1.00 120.96 ? 1797 SER   A CB  1 
ATOM   16  O  OG  . SER   A 1 4   ? -25.138 9.687  -7.521  1.00 120.81 ? 1797 SER   A OG  1 
ATOM   17  N  N   . ASP   A 1 5   ? -26.384 12.069 -9.621  1.00 116.78 ? 1798 ASP   A N   1 
ATOM   18  C  CA  . ASP   A 1 5   ? -26.125 13.374 -10.222 1.00 112.47 ? 1798 ASP   A CA  1 
ATOM   19  C  C   . ASP   A 1 5   ? -27.404 13.969 -10.802 1.00 105.45 ? 1798 ASP   A C   1 
ATOM   20  O  O   . ASP   A 1 5   ? -27.740 15.130 -10.534 1.00 103.65 ? 1798 ASP   A O   1 
ATOM   21  C  CB  . ASP   A 1 5   ? -25.042 13.245 -11.298 1.00 114.90 ? 1798 ASP   A CB  1 
ATOM   22  C  CG  . ASP   A 1 5   ? -23.661 12.984 -10.710 1.00 119.18 ? 1798 ASP   A CG  1 
ATOM   23  O  OD1 . ASP   A 1 5   ? -22.720 13.746 -11.021 1.00 117.94 ? 1798 ASP   A OD1 1 
ATOM   24  O  OD2 . ASP   A 1 5   ? -23.521 12.027 -9.920  1.00 123.47 ? 1798 ASP   A OD2 1 
ATOM   25  N  N   . LEU   A 1 6   ? -28.135 13.181 -11.598 1.00 97.46  ? 1799 LEU   A N   1 
ATOM   26  C  CA  . LEU   A 1 6   ? -29.414 13.644 -12.127 1.00 84.85  ? 1799 LEU   A CA  1 
ATOM   27  C  C   . LEU   A 1 6   ? -30.410 13.929 -11.012 1.00 77.83  ? 1799 LEU   A C   1 
ATOM   28  O  O   . LEU   A 1 6   ? -31.282 14.792 -11.164 1.00 75.07  ? 1799 LEU   A O   1 
ATOM   29  C  CB  . LEU   A 1 6   ? -29.979 12.608 -13.098 1.00 83.53  ? 1799 LEU   A CB  1 
ATOM   30  C  CG  . LEU   A 1 6   ? -29.222 12.480 -14.423 1.00 80.58  ? 1799 LEU   A CG  1 
ATOM   31  C  CD1 . LEU   A 1 6   ? -29.553 11.170 -15.129 1.00 83.80  ? 1799 LEU   A CD1 1 
ATOM   32  C  CD2 . LEU   A 1 6   ? -29.543 13.666 -15.317 1.00 71.81  ? 1799 LEU   A CD2 1 
ATOM   33  N  N   . THR   A 1 7   ? -30.287 13.223 -9.884  1.00 73.46  ? 1800 THR   A N   1 
ATOM   34  C  CA  . THR   A 1 7   ? -31.180 13.443 -8.751  1.00 70.94  ? 1800 THR   A CA  1 
ATOM   35  C  C   . THR   A 1 7   ? -31.071 14.870 -8.228  1.00 69.52  ? 1800 THR   A C   1 
ATOM   36  O  O   . THR   A 1 7   ? -32.084 15.556 -8.032  1.00 64.84  ? 1800 THR   A O   1 
ATOM   37  C  CB  . THR   A 1 7   ? -30.861 12.438 -7.640  1.00 73.08  ? 1800 THR   A CB  1 
ATOM   38  O  OG1 . THR   A 1 7   ? -31.244 11.120 -8.055  1.00 76.09  ? 1800 THR   A OG1 1 
ATOM   39  C  CG2 . THR   A 1 7   ? -31.592 12.804 -6.351  1.00 67.92  ? 1800 THR   A CG2 1 
ATOM   40  N  N   . PHE   A 1 8   ? -29.843 15.338 -7.989  1.00 67.17  ? 1801 PHE   A N   1 
ATOM   41  C  CA  . PHE   A 1 8   ? -29.683 16.685 -7.457  1.00 65.19  ? 1801 PHE   A CA  1 
ATOM   42  C  C   . PHE   A 1 8   ? -30.004 17.748 -8.498  1.00 65.90  ? 1801 PHE   A C   1 
ATOM   43  O  O   . PHE   A 1 8   ? -30.441 18.846 -8.138  1.00 65.36  ? 1801 PHE   A O   1 
ATOM   44  C  CB  . PHE   A 1 8   ? -28.269 16.892 -6.923  1.00 74.04  ? 1801 PHE   A CB  1 
ATOM   45  C  CG  . PHE   A 1 8   ? -28.110 18.172 -6.154  1.00 82.13  ? 1801 PHE   A CG  1 
ATOM   46  C  CD1 . PHE   A 1 8   ? -28.644 18.297 -4.878  1.00 83.31  ? 1801 PHE   A CD1 1 
ATOM   47  C  CD2 . PHE   A 1 8   ? -27.452 19.259 -6.709  1.00 83.82  ? 1801 PHE   A CD2 1 
ATOM   48  C  CE1 . PHE   A 1 8   ? -28.511 19.476 -4.158  1.00 81.70  ? 1801 PHE   A CE1 1 
ATOM   49  C  CE2 . PHE   A 1 8   ? -27.318 20.443 -5.997  1.00 84.61  ? 1801 PHE   A CE2 1 
ATOM   50  C  CZ  . PHE   A 1 8   ? -27.850 20.550 -4.717  1.00 82.46  ? 1801 PHE   A CZ  1 
ATOM   51  N  N   . CYS   A 1 9   ? -29.791 17.452 -9.783  1.00 66.31  ? 1802 CYS   A N   1 
ATOM   52  C  CA  . CYS   A 1 9   ? -30.166 18.402 -10.826 1.00 63.24  ? 1802 CYS   A CA  1 
ATOM   53  C  C   . CYS   A 1 9   ? -31.660 18.698 -10.774 1.00 58.20  ? 1802 CYS   A C   1 
ATOM   54  O  O   . CYS   A 1 9   ? -32.081 19.860 -10.841 1.00 49.25  ? 1802 CYS   A O   1 
ATOM   55  C  CB  . CYS   A 1 9   ? -29.767 17.862 -12.201 1.00 63.13  ? 1802 CYS   A CB  1 
ATOM   56  S  SG  . CYS   A 1 9   ? -27.985 17.687 -12.427 1.00 70.11  ? 1802 CYS   A SG  1 
ATOM   57  N  N   . GLU   A 1 10  ? -32.475 17.651 -10.634 1.00 57.61  ? 1803 GLU   A N   1 
ATOM   58  C  CA  . GLU   A 1 10  ? -33.915 17.833 -10.490 1.00 59.35  ? 1803 GLU   A CA  1 
ATOM   59  C  C   . GLU   A 1 10  ? -34.244 18.651 -9.242  1.00 56.82  ? 1803 GLU   A C   1 
ATOM   60  O  O   . GLU   A 1 10  ? -35.172 19.470 -9.250  1.00 55.61  ? 1803 GLU   A O   1 
ATOM   61  C  CB  . GLU   A 1 10  ? -34.594 16.460 -10.466 1.00 63.88  ? 1803 GLU   A CB  1 
ATOM   62  C  CG  . GLU   A 1 10  ? -36.090 16.473 -10.255 1.00 75.68  ? 1803 GLU   A CG  1 
ATOM   63  C  CD  . GLU   A 1 10  ? -36.813 17.440 -11.171 1.00 80.47  ? 1803 GLU   A CD  1 
ATOM   64  O  OE1 . GLU   A 1 10  ? -37.295 18.485 -10.664 1.00 83.31  ? 1803 GLU   A OE1 1 
ATOM   65  O  OE2 . GLU   A 1 10  ? -36.897 17.150 -12.389 1.00 76.41  ? 1803 GLU   A OE2 1 
ATOM   66  N  N   . ILE   A 1 11  ? -33.472 18.470 -8.169  1.00 56.58  ? 1804 ILE   A N   1 
ATOM   67  C  CA  . ILE   A 1 11  ? -33.703 19.247 -6.949  1.00 55.90  ? 1804 ILE   A CA  1 
ATOM   68  C  C   . ILE   A 1 11  ? -33.391 20.718 -7.188  1.00 53.14  ? 1804 ILE   A C   1 
ATOM   69  O  O   . ILE   A 1 11  ? -34.184 21.608 -6.853  1.00 51.50  ? 1804 ILE   A O   1 
ATOM   70  C  CB  . ILE   A 1 11  ? -32.867 18.687 -5.783  1.00 59.46  ? 1804 ILE   A CB  1 
ATOM   71  C  CG1 . ILE   A 1 11  ? -33.315 17.266 -5.441  1.00 59.00  ? 1804 ILE   A CG1 1 
ATOM   72  C  CG2 . ILE   A 1 11  ? -32.948 19.616 -4.567  1.00 54.61  ? 1804 ILE   A CG2 1 
ATOM   73  C  CD1 . ILE   A 1 11  ? -32.490 16.617 -4.367  1.00 56.98  ? 1804 ILE   A CD1 1 
ATOM   74  N  N   . ILE   A 1 12  ? -32.225 20.997 -7.773  1.00 51.99  ? 1805 ILE   A N   1 
ATOM   75  C  CA  . ILE   A 1 12  ? -31.800 22.381 -7.931  1.00 54.02  ? 1805 ILE   A CA  1 
ATOM   76  C  C   . ILE   A 1 12  ? -32.599 23.079 -9.028  1.00 54.55  ? 1805 ILE   A C   1 
ATOM   77  O  O   . ILE   A 1 12  ? -32.865 24.283 -8.935  1.00 57.72  ? 1805 ILE   A O   1 
ATOM   78  C  CB  . ILE   A 1 12  ? -30.280 22.441 -8.184  1.00 58.18  ? 1805 ILE   A CB  1 
ATOM   79  C  CG1 . ILE   A 1 12  ? -29.772 23.873 -8.047  1.00 61.95  ? 1805 ILE   A CG1 1 
ATOM   80  C  CG2 . ILE   A 1 12  ? -29.914 21.873 -9.552  1.00 56.47  ? 1805 ILE   A CG2 1 
ATOM   81  C  CD1 . ILE   A 1 12  ? -28.269 23.953 -8.025  1.00 67.13  ? 1805 ILE   A CD1 1 
ATOM   82  N  N   . LEU   A 1 13  ? -33.011 22.352 -10.070 1.00 51.94  ? 1806 LEU   A N   1 
ATOM   83  C  CA  . LEU   A 1 13  ? -33.882 22.962 -11.070 1.00 53.09  ? 1806 LEU   A CA  1 
ATOM   84  C  C   . LEU   A 1 13  ? -35.231 23.323 -10.463 1.00 55.51  ? 1806 LEU   A C   1 
ATOM   85  O  O   . LEU   A 1 13  ? -35.803 24.371 -10.785 1.00 52.52  ? 1806 LEU   A O   1 
ATOM   86  C  CB  . LEU   A 1 13  ? -34.068 22.030 -12.269 1.00 55.66  ? 1806 LEU   A CB  1 
ATOM   87  C  CG  . LEU   A 1 13  ? -34.972 22.573 -13.385 1.00 58.33  ? 1806 LEU   A CG  1 
ATOM   88  C  CD1 . LEU   A 1 13  ? -34.497 23.939 -13.851 1.00 52.98  ? 1806 LEU   A CD1 1 
ATOM   89  C  CD2 . LEU   A 1 13  ? -35.042 21.613 -14.566 1.00 56.51  ? 1806 LEU   A CD2 1 
ATOM   90  N  N   . MET   A 1 14  ? -35.750 22.467 -9.580  1.00 53.79  ? 1807 MET   A N   1 
ATOM   91  C  CA  . MET   A 1 14  ? -37.016 22.760 -8.921  1.00 55.55  ? 1807 MET   A CA  1 
ATOM   92  C  C   . MET   A 1 14  ? -36.928 24.053 -8.121  1.00 56.73  ? 1807 MET   A C   1 
ATOM   93  O  O   . MET   A 1 14  ? -37.840 24.889 -8.169  1.00 57.17  ? 1807 MET   A O   1 
ATOM   94  C  CB  . MET   A 1 14  ? -37.407 21.588 -8.020  1.00 62.24  ? 1807 MET   A CB  1 
ATOM   95  C  CG  . MET   A 1 14  ? -38.768 21.718 -7.360  1.00 69.29  ? 1807 MET   A CG  1 
ATOM   96  S  SD  . MET   A 1 14  ? -38.712 21.304 -5.608  1.00 83.18  ? 1807 MET   A SD  1 
ATOM   97  C  CE  . MET   A 1 14  ? -38.050 22.820 -4.909  1.00 75.74  ? 1807 MET   A CE  1 
ATOM   98  N  N   . GLU   A 1 15  ? -35.827 24.239 -7.389  1.00 55.43  ? 1808 GLU   A N   1 
ATOM   99  C  CA  . GLU   A 1 15  ? -35.673 25.425 -6.557  1.00 54.89  ? 1808 GLU   A CA  1 
ATOM   100 C  C   . GLU   A 1 15  ? -35.476 26.682 -7.392  1.00 49.35  ? 1808 GLU   A C   1 
ATOM   101 O  O   . GLU   A 1 15  ? -35.928 27.761 -6.996  1.00 51.09  ? 1808 GLU   A O   1 
ATOM   102 C  CB  . GLU   A 1 15  ? -34.503 25.229 -5.594  1.00 57.83  ? 1808 GLU   A CB  1 
ATOM   103 C  CG  . GLU   A 1 15  ? -34.759 24.163 -4.538  1.00 65.74  ? 1808 GLU   A CG  1 
ATOM   104 C  CD  . GLU   A 1 15  ? -33.501 23.753 -3.801  1.00 74.13  ? 1808 GLU   A CD  1 
ATOM   105 O  OE1 . GLU   A 1 15  ? -32.403 23.940 -4.359  1.00 78.26  ? 1808 GLU   A OE1 1 
ATOM   106 O  OE2 . GLU   A 1 15  ? -33.608 23.248 -2.663  1.00 78.41  ? 1808 GLU   A OE2 1 
ATOM   107 N  N   . MET   A 1 16  ? -34.812 26.570 -8.542  1.00 48.73  ? 1809 MET   A N   1 
ATOM   108 C  CA  . MET   A 1 16  ? -34.637 27.742 -9.391  1.00 49.14  ? 1809 MET   A CA  1 
ATOM   109 C  C   . MET   A 1 16  ? -35.948 28.140 -10.054 1.00 48.02  ? 1809 MET   A C   1 
ATOM   110 O  O   . MET   A 1 16  ? -36.267 29.329 -10.129 1.00 47.85  ? 1809 MET   A O   1 
ATOM   111 C  CB  . MET   A 1 16  ? -33.551 27.482 -10.437 1.00 49.70  ? 1809 MET   A CB  1 
ATOM   112 C  CG  . MET   A 1 16  ? -32.137 27.468 -9.869  1.00 56.50  ? 1809 MET   A CG  1 
ATOM   113 S  SD  . MET   A 1 16  ? -30.860 27.416 -11.140 1.00 61.23  ? 1809 MET   A SD  1 
ATOM   114 C  CE  . MET   A 1 16  ? -31.085 25.762 -11.795 1.00 62.27  ? 1809 MET   A CE  1 
ATOM   115 N  N   . GLU   A 1 17  ? -36.728 27.159 -10.524 1.00 48.33  ? 1810 GLU   A N   1 
ATOM   116 C  CA  . GLU   A 1 17  ? -38.014 27.457 -11.152 1.00 53.16  ? 1810 GLU   A CA  1 
ATOM   117 C  C   . GLU   A 1 17  ? -38.959 28.184 -10.202 1.00 52.71  ? 1810 GLU   A C   1 
ATOM   118 O  O   . GLU   A 1 17  ? -39.765 29.011 -10.644 1.00 53.36  ? 1810 GLU   A O   1 
ATOM   119 C  CB  . GLU   A 1 17  ? -38.669 26.168 -11.651 1.00 56.19  ? 1810 GLU   A CB  1 
ATOM   120 C  CG  . GLU   A 1 17  ? -38.043 25.584 -12.913 1.00 62.89  ? 1810 GLU   A CG  1 
ATOM   121 C  CD  . GLU   A 1 17  ? -38.625 24.227 -13.275 1.00 67.13  ? 1810 GLU   A CD  1 
ATOM   122 O  OE1 . GLU   A 1 17  ? -39.020 23.488 -12.351 1.00 67.98  ? 1810 GLU   A OE1 1 
ATOM   123 O  OE2 . GLU   A 1 17  ? -38.698 23.903 -14.481 1.00 67.21  ? 1810 GLU   A OE2 1 
ATOM   124 N  N   . SER   A 1 18  ? -38.867 27.903 -8.902  1.00 49.29  ? 1811 SER   A N   1 
ATOM   125 C  CA  . SER   A 1 18  ? -39.755 28.481 -7.904  1.00 59.84  ? 1811 SER   A CA  1 
ATOM   126 C  C   . SER   A 1 18  ? -39.194 29.736 -7.251  1.00 60.32  ? 1811 SER   A C   1 
ATOM   127 O  O   . SER   A 1 18  ? -39.902 30.373 -6.463  1.00 61.58  ? 1811 SER   A O   1 
ATOM   128 C  CB  . SER   A 1 18  ? -40.059 27.439 -6.824  1.00 69.45  ? 1811 SER   A CB  1 
ATOM   129 O  OG  . SER   A 1 18  ? -38.873 26.774 -6.419  1.00 76.08  ? 1811 SER   A OG  1 
ATOM   130 N  N   . HIS   A 1 19  ? -37.953 30.102 -7.556  1.00 52.51  ? 1812 HIS   A N   1 
ATOM   131 C  CA  . HIS   A 1 19  ? -37.325 31.258 -6.935  1.00 54.73  ? 1812 HIS   A CA  1 
ATOM   132 C  C   . HIS   A 1 19  ? -38.067 32.540 -7.312  1.00 55.94  ? 1812 HIS   A C   1 
ATOM   133 O  O   . HIS   A 1 19  ? -38.625 32.660 -8.406  1.00 58.97  ? 1812 HIS   A O   1 
ATOM   134 C  CB  . HIS   A 1 19  ? -35.858 31.337 -7.370  1.00 49.29  ? 1812 HIS   A CB  1 
ATOM   135 C  CG  . HIS   A 1 19  ? -34.991 32.151 -6.465  1.00 44.63  ? 1812 HIS   A CG  1 
ATOM   136 N  ND1 . HIS   A 1 19  ? -35.030 33.529 -6.437  1.00 46.43  ? 1812 HIS   A ND1 1 
ATOM   137 C  CD2 . HIS   A 1 19  ? -34.047 31.781 -5.567  1.00 46.19  ? 1812 HIS   A CD2 1 
ATOM   138 C  CE1 . HIS   A 1 19  ? -34.154 33.973 -5.552  1.00 45.77  ? 1812 HIS   A CE1 1 
ATOM   139 N  NE2 . HIS   A 1 19  ? -33.545 32.932 -5.009  1.00 44.29  ? 1812 HIS   A NE2 1 
ATOM   140 N  N   . ASP   A 1 20  ? -38.068 33.506 -6.389  1.00 51.12  ? 1813 ASP   A N   1 
ATOM   141 C  CA  . ASP   A 1 20  ? -38.676 34.809 -6.663  1.00 53.39  ? 1813 ASP   A CA  1 
ATOM   142 C  C   . ASP   A 1 20  ? -38.064 35.463 -7.898  1.00 54.93  ? 1813 ASP   A C   1 
ATOM   143 O  O   . ASP   A 1 20  ? -38.780 35.972 -8.768  1.00 55.77  ? 1813 ASP   A O   1 
ATOM   144 C  CB  . ASP   A 1 20  ? -38.516 35.732 -5.453  1.00 62.72  ? 1813 ASP   A CB  1 
ATOM   145 C  CG  . ASP   A 1 20  ? -39.663 35.618 -4.471  1.00 71.45  ? 1813 ASP   A CG  1 
ATOM   146 O  OD1 . ASP   A 1 20  ? -40.799 35.336 -4.909  1.00 75.92  ? 1813 ASP   A OD1 1 
ATOM   147 O  OD2 . ASP   A 1 20  ? -39.428 35.820 -3.261  1.00 75.53  ? 1813 ASP   A OD2 1 
ATOM   148 N  N   . ALA   A 1 21  ? -36.734 35.468 -7.986  1.00 46.82  ? 1814 ALA   A N   1 
ATOM   149 C  CA  . ALA   A 1 21  ? -36.020 36.160 -9.051  1.00 44.65  ? 1814 ALA   A CA  1 
ATOM   150 C  C   . ALA   A 1 21  ? -35.885 35.331 -10.328 1.00 40.82  ? 1814 ALA   A C   1 
ATOM   151 O  O   . ALA   A 1 21  ? -35.072 35.679 -11.186 1.00 35.38  ? 1814 ALA   A O   1 
ATOM   152 C  CB  . ALA   A 1 21  ? -34.634 36.584 -8.560  1.00 37.28  ? 1814 ALA   A CB  1 
ATOM   153 N  N   . ALA   A 1 22  ? -36.652 34.257 -10.485 1.00 46.87  ? 1815 ALA   A N   1 
ATOM   154 C  CA  . ALA   A 1 22  ? -36.568 33.426 -11.678 1.00 45.28  ? 1815 ALA   A CA  1 
ATOM   155 C  C   . ALA   A 1 22  ? -37.454 33.912 -12.814 1.00 47.35  ? 1815 ALA   A C   1 
ATOM   156 O  O   . ALA   A 1 22  ? -37.446 33.302 -13.890 1.00 49.01  ? 1815 ALA   A O   1 
ATOM   157 C  CB  . ALA   A 1 22  ? -36.937 31.986 -11.339 1.00 43.48  ? 1815 ALA   A CB  1 
ATOM   158 N  N   . TRP   A 1 23  ? -38.195 35.000 -12.614 1.00 44.63  ? 1816 TRP   A N   1 
ATOM   159 C  CA  . TRP   A 1 23  ? -39.167 35.421 -13.617 1.00 47.35  ? 1816 TRP   A CA  1 
ATOM   160 C  C   . TRP   A 1 23  ? -38.595 35.704 -15.010 1.00 49.22  ? 1816 TRP   A C   1 
ATOM   161 O  O   . TRP   A 1 23  ? -39.345 35.512 -15.983 1.00 53.54  ? 1816 TRP   A O   1 
ATOM   162 C  CB  . TRP   A 1 23  ? -39.937 36.643 -13.095 1.00 43.83  ? 1816 TRP   A CB  1 
ATOM   163 C  CG  . TRP   A 1 23  ? -39.079 37.823 -12.776 1.00 48.24  ? 1816 TRP   A CG  1 
ATOM   164 C  CD1 . TRP   A 1 23  ? -38.475 38.100 -11.587 1.00 51.53  ? 1816 TRP   A CD1 1 
ATOM   165 C  CD2 . TRP   A 1 23  ? -38.736 38.895 -13.660 1.00 50.45  ? 1816 TRP   A CD2 1 
ATOM   166 N  NE1 . TRP   A 1 23  ? -37.773 39.281 -11.674 1.00 50.54  ? 1816 TRP   A NE1 1 
ATOM   167 C  CE2 . TRP   A 1 23  ? -37.916 39.786 -12.939 1.00 50.01  ? 1816 TRP   A CE2 1 
ATOM   168 C  CE3 . TRP   A 1 23  ? -39.038 39.184 -14.993 1.00 52.35  ? 1816 TRP   A CE3 1 
ATOM   169 C  CZ2 . TRP   A 1 23  ? -37.396 40.947 -13.505 1.00 51.45  ? 1816 TRP   A CZ2 1 
ATOM   170 C  CZ3 . TRP   A 1 23  ? -38.521 40.339 -15.555 1.00 52.99  ? 1816 TRP   A CZ3 1 
ATOM   171 C  CH2 . TRP   A 1 23  ? -37.710 41.206 -14.811 1.00 53.40  ? 1816 TRP   A CH2 1 
ATOM   172 N  N   . PRO   A 1 24  ? -37.345 36.149 -15.203 1.00 45.41  ? 1817 PRO   A N   1 
ATOM   173 C  CA  . PRO   A 1 24  ? -36.866 36.348 -16.581 1.00 43.99  ? 1817 PRO   A CA  1 
ATOM   174 C  C   . PRO   A 1 24  ? -36.439 35.077 -17.298 1.00 41.72  ? 1817 PRO   A C   1 
ATOM   175 O  O   . PRO   A 1 24  ? -36.158 35.130 -18.504 1.00 45.84  ? 1817 PRO   A O   1 
ATOM   176 C  CB  . PRO   A 1 24  ? -35.633 37.256 -16.403 1.00 42.82  ? 1817 PRO   A CB  1 
ATOM   177 C  CG  . PRO   A 1 24  ? -35.717 37.778 -15.002 1.00 40.02  ? 1817 PRO   A CG  1 
ATOM   178 C  CD  . PRO   A 1 24  ? -36.364 36.673 -14.236 1.00 39.55  ? 1817 PRO   A CD  1 
ATOM   179 N  N   . PHE   A 1 25  ? -36.392 33.942 -16.608 1.00 40.54  ? 1818 PHE   A N   1 
ATOM   180 C  CA  . PHE   A 1 25  ? -35.716 32.758 -17.123 1.00 41.83  ? 1818 PHE   A CA  1 
ATOM   181 C  C   . PHE   A 1 25  ? -36.650 31.562 -17.232 1.00 44.91  ? 1818 PHE   A C   1 
ATOM   182 O  O   . PHE   A 1 25  ? -36.188 30.457 -17.544 1.00 50.61  ? 1818 PHE   A O   1 
ATOM   183 C  CB  . PHE   A 1 25  ? -34.496 32.413 -16.261 1.00 38.34  ? 1818 PHE   A CB  1 
ATOM   184 C  CG  . PHE   A 1 25  ? -33.634 33.603 -15.956 1.00 37.80  ? 1818 PHE   A CG  1 
ATOM   185 C  CD1 . PHE   A 1 25  ? -32.956 34.257 -16.972 1.00 36.75  ? 1818 PHE   A CD1 1 
ATOM   186 C  CD2 . PHE   A 1 25  ? -33.527 34.088 -14.660 1.00 41.11  ? 1818 PHE   A CD2 1 
ATOM   187 C  CE1 . PHE   A 1 25  ? -32.169 35.361 -16.703 1.00 39.42  ? 1818 PHE   A CE1 1 
ATOM   188 C  CE2 . PHE   A 1 25  ? -32.742 35.195 -14.379 1.00 39.70  ? 1818 PHE   A CE2 1 
ATOM   189 C  CZ  . PHE   A 1 25  ? -32.061 35.832 -15.404 1.00 42.11  ? 1818 PHE   A CZ  1 
ATOM   190 N  N   . LEU   A 1 26  ? -37.952 31.753 -17.004 1.00 45.91  ? 1819 LEU   A N   1 
ATOM   191 C  CA  . LEU   A 1 26  ? -38.889 30.638 -17.016 1.00 50.73  ? 1819 LEU   A CA  1 
ATOM   192 C  C   . LEU   A 1 26  ? -39.272 30.193 -18.421 1.00 56.17  ? 1819 LEU   A C   1 
ATOM   193 O  O   . LEU   A 1 26  ? -39.722 29.055 -18.593 1.00 63.25  ? 1819 LEU   A O   1 
ATOM   194 C  CB  . LEU   A 1 26  ? -40.144 31.009 -16.226 1.00 52.34  ? 1819 LEU   A CB  1 
ATOM   195 C  CG  . LEU   A 1 26  ? -39.862 31.185 -14.733 1.00 52.77  ? 1819 LEU   A CG  1 
ATOM   196 C  CD1 . LEU   A 1 26  ? -41.089 31.666 -13.970 1.00 46.72  ? 1819 LEU   A CD1 1 
ATOM   197 C  CD2 . LEU   A 1 26  ? -39.341 29.879 -14.156 1.00 49.09  ? 1819 LEU   A CD2 1 
ATOM   198 N  N   . GLU   A 1 27  ? -39.106 31.045 -19.422 1.00 54.08  ? 1820 GLU   A N   1 
ATOM   199 C  CA  . GLU   A 1 27  ? -39.415 30.701 -20.800 1.00 55.69  ? 1820 GLU   A CA  1 
ATOM   200 C  C   . GLU   A 1 27  ? -38.387 31.365 -21.702 1.00 51.59  ? 1820 GLU   A C   1 
ATOM   201 O  O   . GLU   A 1 27  ? -37.723 32.323 -21.292 1.00 49.78  ? 1820 GLU   A O   1 
ATOM   202 C  CB  . GLU   A 1 27  ? -40.842 31.129 -21.177 1.00 59.12  ? 1820 GLU   A CB  1 
ATOM   203 C  CG  . GLU   A 1 27  ? -41.079 32.626 -21.238 1.00 66.45  ? 1820 GLU   A CG  1 
ATOM   204 C  CD  . GLU   A 1 27  ? -42.561 32.984 -21.210 1.00 79.70  ? 1820 GLU   A CD  1 
ATOM   205 O  OE1 . GLU   A 1 27  ? -43.088 33.258 -20.109 1.00 83.89  ? 1820 GLU   A OE1 1 
ATOM   206 O  OE2 . GLU   A 1 27  ? -43.199 32.980 -22.286 1.00 83.32  ? 1820 GLU   A OE2 1 
ATOM   207 N  N   . PRO   A 1 28  ? -38.206 30.854 -22.922 1.00 44.45  ? 1821 PRO   A N   1 
ATOM   208 C  CA  . PRO   A 1 28  ? -37.210 31.444 -23.830 1.00 42.69  ? 1821 PRO   A CA  1 
ATOM   209 C  C   . PRO   A 1 28  ? -37.534 32.887 -24.187 1.00 45.58  ? 1821 PRO   A C   1 
ATOM   210 O  O   . PRO   A 1 28  ? -38.697 33.270 -24.320 1.00 50.47  ? 1821 PRO   A O   1 
ATOM   211 C  CB  . PRO   A 1 28  ? -37.279 30.539 -25.067 1.00 45.91  ? 1821 PRO   A CB  1 
ATOM   212 C  CG  . PRO   A 1 28  ? -37.814 29.230 -24.555 1.00 48.93  ? 1821 PRO   A CG  1 
ATOM   213 C  CD  . PRO   A 1 28  ? -38.783 29.609 -23.467 1.00 47.86  ? 1821 PRO   A CD  1 
ATOM   214 N  N   . VAL   A 1 29  ? -36.480 33.689 -24.345 1.00 45.71  ? 1822 VAL   A N   1 
ATOM   215 C  CA  . VAL   A 1 29  ? -36.640 35.039 -24.869 1.00 49.68  ? 1822 VAL   A CA  1 
ATOM   216 C  C   . VAL   A 1 29  ? -37.209 34.975 -26.277 1.00 52.55  ? 1822 VAL   A C   1 
ATOM   217 O  O   . VAL   A 1 29  ? -36.778 34.165 -27.107 1.00 49.89  ? 1822 VAL   A O   1 
ATOM   218 C  CB  . VAL   A 1 29  ? -35.293 35.778 -24.859 1.00 52.88  ? 1822 VAL   A CB  1 
ATOM   219 C  CG1 . VAL   A 1 29  ? -35.402 37.110 -25.604 1.00 46.60  ? 1822 VAL   A CG1 1 
ATOM   220 C  CG2 . VAL   A 1 29  ? -34.827 35.986 -23.435 1.00 56.62  ? 1822 VAL   A CG2 1 
ATOM   221 N  N   . ASN   A 1 30  ? -38.192 35.831 -26.554 1.00 54.03  ? 1823 ASN   A N   1 
ATOM   222 C  CA  . ASN   A 1 30  ? -38.741 35.949 -27.897 1.00 52.74  ? 1823 ASN   A CA  1 
ATOM   223 C  C   . ASN   A 1 30  ? -37.922 36.988 -28.652 1.00 47.11  ? 1823 ASN   A C   1 
ATOM   224 O  O   . ASN   A 1 30  ? -38.064 38.188 -28.373 1.00 47.14  ? 1823 ASN   A O   1 
ATOM   225 C  CB  . ASN   A 1 30  ? -40.206 36.354 -27.849 1.00 55.68  ? 1823 ASN   A CB  1 
ATOM   226 C  CG  . ASN   A 1 30  ? -40.875 36.324 -29.216 1.00 61.28  ? 1823 ASN   A CG  1 
ATOM   227 O  OD1 . ASN   A 1 30  ? -40.215 36.371 -30.254 1.00 59.64  ? 1823 ASN   A OD1 1 
ATOM   228 N  ND2 . ASN   A 1 30  ? -42.201 36.257 -29.218 1.00 66.82  ? 1823 ASN   A ND2 1 
ATOM   229 N  N   . PRO   A 1 31  ? -37.073 36.588 -29.603 1.00 48.84  ? 1824 PRO   A N   1 
ATOM   230 C  CA  . PRO   A 1 31  ? -36.239 37.586 -30.298 1.00 52.01  ? 1824 PRO   A CA  1 
ATOM   231 C  C   . PRO   A 1 31  ? -37.044 38.602 -31.092 1.00 54.48  ? 1824 PRO   A C   1 
ATOM   232 O  O   . PRO   A 1 31  ? -36.580 39.734 -31.280 1.00 57.34  ? 1824 PRO   A O   1 
ATOM   233 C  CB  . PRO   A 1 31  ? -35.346 36.727 -31.204 1.00 53.02  ? 1824 PRO   A CB  1 
ATOM   234 C  CG  . PRO   A 1 31  ? -36.106 35.447 -31.395 1.00 48.75  ? 1824 PRO   A CG  1 
ATOM   235 C  CD  . PRO   A 1 31  ? -36.871 35.223 -30.120 1.00 45.46  ? 1824 PRO   A CD  1 
ATOM   236 N  N   . ARG   A 1 32  ? -38.243 38.238 -31.558 1.00 51.99  ? 1825 ARG   A N   1 
ATOM   237 C  CA  . ARG   A 1 32  ? -39.104 39.214 -32.221 1.00 58.11  ? 1825 ARG   A CA  1 
ATOM   238 C  C   . ARG   A 1 32  ? -39.423 40.394 -31.311 1.00 59.36  ? 1825 ARG   A C   1 
ATOM   239 O  O   . ARG   A 1 32  ? -39.660 41.506 -31.798 1.00 59.47  ? 1825 ARG   A O   1 
ATOM   240 C  CB  . ARG   A 1 32  ? -40.407 38.554 -32.678 1.00 55.89  ? 1825 ARG   A CB  1 
ATOM   241 C  CG  . ARG   A 1 32  ? -40.280 37.547 -33.816 1.00 57.66  ? 1825 ARG   A CG  1 
ATOM   242 C  CD  . ARG   A 1 32  ? -41.594 36.790 -33.958 1.00 58.37  ? 1825 ARG   A CD  1 
ATOM   243 N  NE  . ARG   A 1 32  ? -41.635 35.860 -35.083 1.00 60.38  ? 1825 ARG   A NE  1 
ATOM   244 C  CZ  . ARG   A 1 32  ? -42.659 35.045 -35.328 1.00 64.70  ? 1825 ARG   A CZ  1 
ATOM   245 N  NH1 . ARG   A 1 32  ? -43.716 35.047 -34.522 1.00 60.95  ? 1825 ARG   A NH1 1 
ATOM   246 N  NH2 . ARG   A 1 32  ? -42.634 34.229 -36.374 1.00 64.91  ? 1825 ARG   A NH2 1 
ATOM   247 N  N   . LEU   A 1 33  ? -39.431 40.177 -29.994 1.00 57.76  ? 1826 LEU   A N   1 
ATOM   248 C  CA  . LEU   A 1 33  ? -39.832 41.196 -29.033 1.00 58.12  ? 1826 LEU   A CA  1 
ATOM   249 C  C   . LEU   A 1 33  ? -38.660 41.939 -28.401 1.00 58.27  ? 1826 LEU   A C   1 
ATOM   250 O  O   . LEU   A 1 33  ? -38.890 42.912 -27.675 1.00 54.91  ? 1826 LEU   A O   1 
ATOM   251 C  CB  . LEU   A 1 33  ? -40.688 40.558 -27.925 1.00 61.56  ? 1826 LEU   A CB  1 
ATOM   252 C  CG  . LEU   A 1 33  ? -41.958 39.845 -28.406 1.00 64.62  ? 1826 LEU   A CG  1 
ATOM   253 C  CD1 . LEU   A 1 33  ? -42.590 39.015 -27.297 1.00 61.19  ? 1826 LEU   A CD1 1 
ATOM   254 C  CD2 . LEU   A 1 33  ? -42.950 40.863 -28.930 1.00 67.83  ? 1826 LEU   A CD2 1 
ATOM   255 N  N   . VAL   A 1 34  ? -37.420 41.521 -28.662 1.00 60.14  ? 1827 VAL   A N   1 
ATOM   256 C  CA  . VAL   A 1 34  ? -36.232 42.100 -28.034 1.00 56.71  ? 1827 VAL   A CA  1 
ATOM   257 C  C   . VAL   A 1 34  ? -35.237 42.454 -29.129 1.00 53.03  ? 1827 VAL   A C   1 
ATOM   258 O  O   . VAL   A 1 34  ? -34.648 41.561 -29.751 1.00 52.76  ? 1827 VAL   A O   1 
ATOM   259 C  CB  . VAL   A 1 34  ? -35.588 41.148 -27.015 1.00 51.38  ? 1827 VAL   A CB  1 
ATOM   260 C  CG1 . VAL   A 1 34  ? -34.440 41.845 -26.307 1.00 46.25  ? 1827 VAL   A CG1 1 
ATOM   261 C  CG2 . VAL   A 1 34  ? -36.621 40.637 -26.016 1.00 51.80  ? 1827 VAL   A CG2 1 
ATOM   262 N  N   . SER   A 1 35  ? -35.023 43.749 -29.344 1.00 53.70  ? 1828 SER   A N   1 
ATOM   263 C  CA  . SER   A 1 35  ? -34.149 44.186 -30.424 1.00 60.34  ? 1828 SER   A CA  1 
ATOM   264 C  C   . SER   A 1 35  ? -32.702 43.791 -30.147 1.00 57.12  ? 1828 SER   A C   1 
ATOM   265 O  O   . SER   A 1 35  ? -32.152 44.101 -29.084 1.00 56.75  ? 1828 SER   A O   1 
ATOM   266 C  CB  . SER   A 1 35  ? -34.257 45.699 -30.611 1.00 68.05  ? 1828 SER   A CB  1 
ATOM   267 O  OG  . SER   A 1 35  ? -33.485 46.124 -31.721 1.00 72.86  ? 1828 SER   A OG  1 
ATOM   268 N  N   . GLY   A 1 36  ? -32.083 43.111 -31.114 1.00 54.51  ? 1829 GLY   A N   1 
ATOM   269 C  CA  . GLY   A 1 36  ? -30.682 42.761 -31.038 1.00 49.87  ? 1829 GLY   A CA  1 
ATOM   270 C  C   . GLY   A 1 36  ? -30.379 41.450 -30.344 1.00 50.66  ? 1829 GLY   A C   1 
ATOM   271 O  O   . GLY   A 1 36  ? -29.217 41.014 -30.359 1.00 47.13  ? 1829 GLY   A O   1 
ATOM   272 N  N   . TYR   A 1 37  ? -31.379 40.801 -29.744 1.00 51.86  ? 1830 TYR   A N   1 
ATOM   273 C  CA  . TYR   A 1 37  ? -31.111 39.591 -28.973 1.00 50.05  ? 1830 TYR   A CA  1 
ATOM   274 C  C   . TYR   A 1 37  ? -30.573 38.476 -29.860 1.00 47.02  ? 1830 TYR   A C   1 
ATOM   275 O  O   . TYR   A 1 37  ? -29.595 37.803 -29.510 1.00 46.80  ? 1830 TYR   A O   1 
ATOM   276 C  CB  . TYR   A 1 37  ? -32.374 39.128 -28.252 1.00 45.03  ? 1830 TYR   A CB  1 
ATOM   277 C  CG  . TYR   A 1 37  ? -32.065 38.113 -27.178 1.00 46.45  ? 1830 TYR   A CG  1 
ATOM   278 C  CD1 . TYR   A 1 37  ? -31.629 38.518 -25.920 1.00 49.60  ? 1830 TYR   A CD1 1 
ATOM   279 C  CD2 . TYR   A 1 37  ? -32.185 36.753 -27.424 1.00 46.00  ? 1830 TYR   A CD2 1 
ATOM   280 C  CE1 . TYR   A 1 37  ? -31.327 37.593 -24.926 1.00 50.72  ? 1830 TYR   A CE1 1 
ATOM   281 C  CE2 . TYR   A 1 37  ? -31.888 35.815 -26.441 1.00 48.74  ? 1830 TYR   A CE2 1 
ATOM   282 C  CZ  . TYR   A 1 37  ? -31.459 36.241 -25.192 1.00 55.38  ? 1830 TYR   A CZ  1 
ATOM   283 O  OH  . TYR   A 1 37  ? -31.167 35.309 -24.215 1.00 57.62  ? 1830 TYR   A OH  1 
ATOM   284 N  N   . ARG   A 1 38  ? -31.229 38.252 -31.003 1.00 44.45  ? 1831 ARG   A N   1 
ATOM   285 C  CA  . ARG   A 1 38  ? -30.785 37.240 -31.956 1.00 47.59  ? 1831 ARG   A CA  1 
ATOM   286 C  C   . ARG   A 1 38  ? -29.330 37.462 -32.356 1.00 47.90  ? 1831 ARG   A C   1 
ATOM   287 O  O   . ARG   A 1 38  ? -28.532 36.519 -32.396 1.00 45.92  ? 1831 ARG   A O   1 
ATOM   288 C  CB  . ARG   A 1 38  ? -31.699 37.279 -33.184 1.00 57.70  ? 1831 ARG   A CB  1 
ATOM   289 C  CG  . ARG   A 1 38  ? -31.517 36.138 -34.169 1.00 66.21  ? 1831 ARG   A CG  1 
ATOM   290 C  CD  . ARG   A 1 38  ? -32.146 36.456 -35.534 1.00 71.58  ? 1831 ARG   A CD  1 
ATOM   291 N  NE  . ARG   A 1 38  ? -33.562 36.830 -35.466 1.00 74.84  ? 1831 ARG   A NE  1 
ATOM   292 C  CZ  . ARG   A 1 38  ? -34.565 35.968 -35.299 1.00 70.48  ? 1831 ARG   A CZ  1 
ATOM   293 N  NH1 . ARG   A 1 38  ? -34.316 34.672 -35.159 1.00 64.37  ? 1831 ARG   A NH1 1 
ATOM   294 N  NH2 . ARG   A 1 38  ? -35.820 36.403 -35.262 1.00 69.05  ? 1831 ARG   A NH2 1 
ATOM   295 N  N   . ARG   A 1 39  ? -28.964 38.715 -32.621 1.00 48.38  ? 1832 ARG   A N   1 
ATOM   296 C  CA  . ARG   A 1 39  ? -27.625 39.038 -33.095 1.00 47.30  ? 1832 ARG   A CA  1 
ATOM   297 C  C   . ARG   A 1 39  ? -26.563 38.850 -32.011 1.00 47.19  ? 1832 ARG   A C   1 
ATOM   298 O  O   . ARG   A 1 39  ? -25.417 38.509 -32.327 1.00 44.26  ? 1832 ARG   A O   1 
ATOM   299 C  CB  . ARG   A 1 39  ? -27.637 40.475 -33.628 1.00 46.25  ? 1832 ARG   A CB  1 
ATOM   300 C  CG  . ARG   A 1 39  ? -26.292 41.094 -33.933 1.00 49.05  ? 1832 ARG   A CG  1 
ATOM   301 C  CD  . ARG   A 1 39  ? -26.456 42.531 -34.441 1.00 49.36  ? 1832 ARG   A CD  1 
ATOM   302 N  NE  . ARG   A 1 39  ? -27.300 43.347 -33.565 1.00 63.16  ? 1832 ARG   A NE  1 
ATOM   303 C  CZ  . ARG   A 1 39  ? -26.857 44.073 -32.538 1.00 62.46  ? 1832 ARG   A CZ  1 
ATOM   304 N  NH1 . ARG   A 1 39  ? -25.567 44.097 -32.233 1.00 64.21  ? 1832 ARG   A NH1 1 
ATOM   305 N  NH2 . ARG   A 1 39  ? -27.709 44.779 -31.811 1.00 60.90  ? 1832 ARG   A NH2 1 
ATOM   306 N  N   . ILE   A 1 40  ? -26.918 39.039 -30.736 1.00 40.70  ? 1833 ILE   A N   1 
ATOM   307 C  CA  . ILE   A 1 40  ? -25.937 39.110 -29.651 1.00 43.13  ? 1833 ILE   A CA  1 
ATOM   308 C  C   . ILE   A 1 40  ? -25.778 37.779 -28.914 1.00 46.50  ? 1833 ILE   A C   1 
ATOM   309 O  O   . ILE   A 1 40  ? -24.676 37.434 -28.471 1.00 47.91  ? 1833 ILE   A O   1 
ATOM   310 C  CB  . ILE   A 1 40  ? -26.314 40.243 -28.675 1.00 39.61  ? 1833 ILE   A CB  1 
ATOM   311 C  CG1 . ILE   A 1 40  ? -25.900 41.592 -29.256 1.00 37.98  ? 1833 ILE   A CG1 1 
ATOM   312 C  CG2 . ILE   A 1 40  ? -25.684 40.037 -27.305 1.00 38.43  ? 1833 ILE   A CG2 1 
ATOM   313 C  CD1 . ILE   A 1 40  ? -26.566 42.771 -28.594 1.00 34.36  ? 1833 ILE   A CD1 1 
ATOM   314 N  N   . ILE   A 1 41  ? -26.860 37.017 -28.777 1.00 39.87  ? 1834 ILE   A N   1 
ATOM   315 C  CA  . ILE   A 1 41  ? -26.862 35.793 -27.978 1.00 38.83  ? 1834 ILE   A CA  1 
ATOM   316 C  C   . ILE   A 1 41  ? -26.896 34.595 -28.923 1.00 42.77  ? 1834 ILE   A C   1 
ATOM   317 O  O   . ILE   A 1 41  ? -27.952 34.249 -29.470 1.00 41.11  ? 1834 ILE   A O   1 
ATOM   318 C  CB  . ILE   A 1 41  ? -28.037 35.764 -26.989 1.00 34.41  ? 1834 ILE   A CB  1 
ATOM   319 C  CG1 . ILE   A 1 41  ? -27.896 36.891 -25.964 1.00 36.74  ? 1834 ILE   A CG1 1 
ATOM   320 C  CG2 . ILE   A 1 41  ? -28.115 34.418 -26.294 1.00 32.10  ? 1834 ILE   A CG2 1 
ATOM   321 C  CD1 . ILE   A 1 41  ? -26.620 36.809 -25.129 1.00 32.36  ? 1834 ILE   A CD1 1 
ATOM   322 N  N   . LYS   A 1 42  ? -25.748 33.932 -29.086 1.00 43.80  ? 1835 LYS   A N   1 
ATOM   323 C  CA  . LYS   A 1 42  ? -25.649 32.848 -30.062 1.00 46.72  ? 1835 LYS   A CA  1 
ATOM   324 C  C   . LYS   A 1 42  ? -26.414 31.605 -29.616 1.00 48.41  ? 1835 LYS   A C   1 
ATOM   325 O  O   . LYS   A 1 42  ? -27.104 30.975 -30.428 1.00 49.28  ? 1835 LYS   A O   1 
ATOM   326 C  CB  . LYS   A 1 42  ? -24.180 32.510 -30.329 1.00 48.94  ? 1835 LYS   A CB  1 
ATOM   327 C  CG  . LYS   A 1 42  ? -23.375 33.655 -30.932 1.00 52.41  ? 1835 LYS   A CG  1 
ATOM   328 C  CD  . LYS   A 1 42  ? -24.025 34.183 -32.211 1.00 56.82  ? 1835 LYS   A CD  1 
ATOM   329 C  CE  . LYS   A 1 42  ? -23.117 35.166 -32.949 1.00 59.06  ? 1835 LYS   A CE  1 
ATOM   330 N  NZ  . LYS   A 1 42  ? -22.961 36.453 -32.220 1.00 61.60  ? 1835 LYS   A NZ  1 
ATOM   331 N  N   . ASN   A 1 43  ? -26.311 31.230 -28.340 1.00 48.59  ? 1836 ASN   A N   1 
ATOM   332 C  CA  . ASN   A 1 43  ? -26.950 30.019 -27.823 1.00 48.58  ? 1836 ASN   A CA  1 
ATOM   333 C  C   . ASN   A 1 43  ? -27.888 30.373 -26.674 1.00 47.70  ? 1836 ASN   A C   1 
ATOM   334 O  O   . ASN   A 1 43  ? -27.493 30.332 -25.497 1.00 40.44  ? 1836 ASN   A O   1 
ATOM   335 C  CB  . ASN   A 1 43  ? -25.899 29.000 -27.387 1.00 48.36  ? 1836 ASN   A CB  1 
ATOM   336 C  CG  . ASN   A 1 43  ? -24.878 28.718 -28.479 1.00 51.75  ? 1836 ASN   A CG  1 
ATOM   337 O  OD1 . ASN   A 1 43  ? -23.685 28.972 -28.312 1.00 54.56  ? 1836 ASN   A OD1 1 
ATOM   338 N  ND2 . ASN   A 1 43  ? -25.346 28.196 -29.604 1.00 56.57  ? 1836 ASN   A ND2 1 
ATOM   339 N  N   . PRO   A 1 44  ? -29.142 30.717 -26.966 1.00 51.96  ? 1837 PRO   A N   1 
ATOM   340 C  CA  . PRO   A 1 44  ? -30.092 31.026 -25.890 1.00 46.96  ? 1837 PRO   A CA  1 
ATOM   341 C  C   . PRO   A 1 44  ? -30.376 29.809 -25.025 1.00 47.22  ? 1837 PRO   A C   1 
ATOM   342 O  O   . PRO   A 1 44  ? -30.204 28.659 -25.436 1.00 48.26  ? 1837 PRO   A O   1 
ATOM   343 C  CB  . PRO   A 1 44  ? -31.352 31.483 -26.639 1.00 48.79  ? 1837 PRO   A CB  1 
ATOM   344 C  CG  . PRO   A 1 44  ? -31.219 30.884 -28.009 1.00 45.95  ? 1837 PRO   A CG  1 
ATOM   345 C  CD  . PRO   A 1 44  ? -29.741 30.890 -28.301 1.00 46.00  ? 1837 PRO   A CD  1 
ATOM   346 N  N   . MET   A 1 45  ? -30.820 30.087 -23.801 1.00 44.47  ? 1838 MET   A N   1 
ATOM   347 C  CA  . MET   A 1 45  ? -31.058 29.047 -22.813 1.00 44.30  ? 1838 MET   A CA  1 
ATOM   348 C  C   . MET   A 1 45  ? -31.943 29.623 -21.718 1.00 41.04  ? 1838 MET   A C   1 
ATOM   349 O  O   . MET   A 1 45  ? -31.906 30.824 -21.438 1.00 44.53  ? 1838 MET   A O   1 
ATOM   350 C  CB  . MET   A 1 45  ? -29.741 28.512 -22.237 1.00 38.18  ? 1838 MET   A CB  1 
ATOM   351 C  CG  . MET   A 1 45  ? -29.896 27.317 -21.312 1.00 39.51  ? 1838 MET   A CG  1 
ATOM   352 S  SD  . MET   A 1 45  ? -30.971 26.019 -21.960 1.00 49.75  ? 1838 MET   A SD  1 
ATOM   353 C  CE  . MET   A 1 45  ? -30.104 25.566 -23.469 1.00 46.38  ? 1838 MET   A CE  1 
ATOM   354 N  N   . ASP   A 1 46  ? -32.752 28.758 -21.120 1.00 41.17  ? 1839 ASP   A N   1 
ATOM   355 C  CA  . ASP   A 1 46  ? -33.660 29.159 -20.057 1.00 49.05  ? 1839 ASP   A CA  1 
ATOM   356 C  C   . ASP   A 1 46  ? -34.060 27.910 -19.283 1.00 46.72  ? 1839 ASP   A C   1 
ATOM   357 O  O   . ASP   A 1 46  ? -33.681 26.790 -19.634 1.00 45.66  ? 1839 ASP   A O   1 
ATOM   358 C  CB  . ASP   A 1 46  ? -34.884 29.882 -20.618 1.00 53.51  ? 1839 ASP   A CB  1 
ATOM   359 C  CG  . ASP   A 1 46  ? -35.789 28.957 -21.384 1.00 60.18  ? 1839 ASP   A CG  1 
ATOM   360 O  OD1 . ASP   A 1 46  ? -35.400 28.520 -22.488 1.00 65.20  ? 1839 ASP   A OD1 1 
ATOM   361 O  OD2 . ASP   A 1 46  ? -36.876 28.634 -20.863 1.00 65.54  ? 1839 ASP   A OD2 1 
ATOM   362 N  N   . PHE   A 1 47  ? -34.862 28.114 -18.234 1.00 40.20  ? 1840 PHE   A N   1 
ATOM   363 C  CA  . PHE   A 1 47  ? -35.166 27.022 -17.316 1.00 44.94  ? 1840 PHE   A CA  1 
ATOM   364 C  C   . PHE   A 1 47  ? -36.138 26.021 -17.925 1.00 49.37  ? 1840 PHE   A C   1 
ATOM   365 O  O   . PHE   A 1 47  ? -36.043 24.819 -17.653 1.00 49.73  ? 1840 PHE   A O   1 
ATOM   366 C  CB  . PHE   A 1 47  ? -35.715 27.579 -16.006 1.00 42.68  ? 1840 PHE   A CB  1 
ATOM   367 C  CG  . PHE   A 1 47  ? -34.707 28.354 -15.221 1.00 42.41  ? 1840 PHE   A CG  1 
ATOM   368 C  CD1 . PHE   A 1 47  ? -33.348 28.137 -15.413 1.00 44.90  ? 1840 PHE   A CD1 1 
ATOM   369 C  CD2 . PHE   A 1 47  ? -35.106 29.304 -14.297 1.00 43.87  ? 1840 PHE   A CD2 1 
ATOM   370 C  CE1 . PHE   A 1 47  ? -32.407 28.848 -14.696 1.00 45.42  ? 1840 PHE   A CE1 1 
ATOM   371 C  CE2 . PHE   A 1 47  ? -34.169 30.020 -13.570 1.00 48.53  ? 1840 PHE   A CE2 1 
ATOM   372 C  CZ  . PHE   A 1 47  ? -32.817 29.793 -13.770 1.00 46.18  ? 1840 PHE   A CZ  1 
ATOM   373 N  N   . SER   A 1 48  ? -37.084 26.491 -18.745 1.00 50.24  ? 1841 SER   A N   1 
ATOM   374 C  CA  . SER   A 1 48  ? -38.035 25.569 -19.362 1.00 49.32  ? 1841 SER   A CA  1 
ATOM   375 C  C   . SER   A 1 48  ? -37.342 24.660 -20.369 1.00 48.02  ? 1841 SER   A C   1 
ATOM   376 O  O   . SER   A 1 48  ? -37.665 23.471 -20.465 1.00 51.85  ? 1841 SER   A O   1 
ATOM   377 C  CB  . SER   A 1 48  ? -39.170 26.338 -20.034 1.00 51.69  ? 1841 SER   A CB  1 
ATOM   378 O  OG  . SER   A 1 48  ? -38.832 26.679 -21.369 1.00 58.16  ? 1841 SER   A OG  1 
ATOM   379 N  N   . THR   A 1 49  ? -36.391 25.206 -21.133 1.00 44.17  ? 1842 THR   A N   1 
ATOM   380 C  CA  . THR   A 1 49  ? -35.575 24.374 -22.011 1.00 48.57  ? 1842 THR   A CA  1 
ATOM   381 C  C   . THR   A 1 49  ? -34.798 23.332 -21.216 1.00 47.27  ? 1842 THR   A C   1 
ATOM   382 O  O   . THR   A 1 49  ? -34.663 22.182 -21.651 1.00 51.04  ? 1842 THR   A O   1 
ATOM   383 C  CB  . THR   A 1 49  ? -34.615 25.246 -22.820 1.00 49.98  ? 1842 THR   A CB  1 
ATOM   384 O  OG1 . THR   A 1 49  ? -35.354 26.270 -23.496 1.00 52.94  ? 1842 THR   A OG1 1 
ATOM   385 C  CG2 . THR   A 1 49  ? -33.863 24.404 -23.846 1.00 43.42  ? 1842 THR   A CG2 1 
ATOM   386 N  N   . MET   A 1 50  ? -34.284 23.710 -20.044 1.00 47.23  ? 1843 MET   A N   1 
ATOM   387 C  CA  . MET   A 1 50  ? -33.608 22.731 -19.199 1.00 49.22  ? 1843 MET   A CA  1 
ATOM   388 C  C   . MET   A 1 50  ? -34.597 21.714 -18.642 1.00 51.06  ? 1843 MET   A C   1 
ATOM   389 O  O   . MET   A 1 50  ? -34.302 20.513 -18.599 1.00 54.08  ? 1843 MET   A O   1 
ATOM   390 C  CB  . MET   A 1 50  ? -32.855 23.440 -18.072 1.00 43.46  ? 1843 MET   A CB  1 
ATOM   391 C  CG  . MET   A 1 50  ? -31.652 24.233 -18.566 1.00 48.50  ? 1843 MET   A CG  1 
ATOM   392 S  SD  . MET   A 1 50  ? -31.010 25.416 -17.367 1.00 45.72  ? 1843 MET   A SD  1 
ATOM   393 C  CE  . MET   A 1 50  ? -30.510 24.340 -16.032 1.00 40.41  ? 1843 MET   A CE  1 
ATOM   394 N  N   . ARG   A 1 51  ? -35.778 22.177 -18.222 1.00 45.43  ? 1844 ARG   A N   1 
ATOM   395 C  CA  . ARG   A 1 51  ? -36.819 21.264 -17.764 1.00 48.50  ? 1844 ARG   A CA  1 
ATOM   396 C  C   . ARG   A 1 51  ? -37.191 20.261 -18.849 1.00 50.60  ? 1844 ARG   A C   1 
ATOM   397 O  O   . ARG   A 1 51  ? -37.311 19.061 -18.580 1.00 53.76  ? 1844 ARG   A O   1 
ATOM   398 C  CB  . ARG   A 1 51  ? -38.049 22.058 -17.321 1.00 51.79  ? 1844 ARG   A CB  1 
ATOM   399 C  CG  . ARG   A 1 51  ? -39.274 21.204 -17.032 1.00 56.51  ? 1844 ARG   A CG  1 
ATOM   400 C  CD  . ARG   A 1 51  ? -39.000 20.221 -15.909 1.00 57.14  ? 1844 ARG   A CD  1 
ATOM   401 N  NE  . ARG   A 1 51  ? -38.706 20.913 -14.658 1.00 61.04  ? 1844 ARG   A NE  1 
ATOM   402 C  CZ  . ARG   A 1 51  ? -38.186 20.325 -13.585 1.00 63.30  ? 1844 ARG   A CZ  1 
ATOM   403 N  NH1 . ARG   A 1 51  ? -37.896 19.032 -13.614 1.00 65.24  ? 1844 ARG   A NH1 1 
ATOM   404 N  NH2 . ARG   A 1 51  ? -37.951 21.029 -12.488 1.00 64.55  ? 1844 ARG   A NH2 1 
ATOM   405 N  N   . HIS   A 1 52  ? -37.361 20.736 -20.085 1.00 49.11  ? 1845 HIS   A N   1 
ATOM   406 C  CA  A HIS   A 1 52  ? -37.718 19.855 -21.196 0.60 50.76  ? 1845 HIS   A CA  1 
ATOM   407 C  CA  B HIS   A 1 52  ? -37.734 19.833 -21.166 0.40 50.77  ? 1845 HIS   A CA  1 
ATOM   408 C  C   . HIS   A 1 52  ? -36.635 18.812 -21.442 1.00 53.68  ? 1845 HIS   A C   1 
ATOM   409 O  O   . HIS   A 1 52  ? -36.929 17.629 -21.657 1.00 56.70  ? 1845 HIS   A O   1 
ATOM   410 C  CB  A HIS   A 1 52  ? -37.961 20.702 -22.451 0.60 49.19  ? 1845 HIS   A CB  1 
ATOM   411 C  CB  B HIS   A 1 52  ? -38.071 20.632 -22.426 0.40 49.24  ? 1845 HIS   A CB  1 
ATOM   412 C  CG  A HIS   A 1 52  ? -38.318 19.916 -23.678 0.60 49.63  ? 1845 HIS   A CG  1 
ATOM   413 C  CG  B HIS   A 1 52  ? -39.209 21.589 -22.246 0.40 47.93  ? 1845 HIS   A CG  1 
ATOM   414 N  ND1 A HIS   A 1 52  ? -37.387 19.215 -24.414 0.60 46.58  ? 1845 HIS   A ND1 1 
ATOM   415 N  ND1 B HIS   A 1 52  ? -40.058 21.544 -21.161 0.40 48.27  ? 1845 HIS   A ND1 1 
ATOM   416 C  CD2 A HIS   A 1 52  ? -39.499 19.758 -24.322 0.60 47.88  ? 1845 HIS   A CD2 1 
ATOM   417 C  CD2 B HIS   A 1 52  ? -39.631 22.627 -23.009 0.40 47.31  ? 1845 HIS   A CD2 1 
ATOM   418 C  CE1 A HIS   A 1 52  ? -37.982 18.641 -25.445 0.60 46.36  ? 1845 HIS   A CE1 1 
ATOM   419 C  CE1 B HIS   A 1 52  ? -40.956 22.508 -21.265 0.40 47.94  ? 1845 HIS   A CE1 1 
ATOM   420 N  NE2 A HIS   A 1 52  ? -39.264 18.957 -25.413 0.60 43.80  ? 1845 HIS   A NE2 1 
ATOM   421 N  NE2 B HIS   A 1 52  ? -40.719 23.179 -22.377 0.40 47.46  ? 1845 HIS   A NE2 1 
ATOM   422 N  N   . ARG   A 1 53  ? -35.367 19.234 -21.418 1.00 56.73  ? 1846 ARG   A N   1 
ATOM   423 C  CA  . ARG   A 1 53  ? -34.282 18.298 -21.706 1.00 58.53  ? 1846 ARG   A CA  1 
ATOM   424 C  C   . ARG   A 1 53  ? -34.102 17.278 -20.588 1.00 59.69  ? 1846 ARG   A C   1 
ATOM   425 O  O   . ARG   A 1 53  ? -33.711 16.135 -20.848 1.00 63.29  ? 1846 ARG   A O   1 
ATOM   426 C  CB  . ARG   A 1 53  ? -32.978 19.059 -21.956 1.00 57.49  ? 1846 ARG   A CB  1 
ATOM   427 C  CG  . ARG   A 1 53  ? -31.815 18.160 -22.360 1.00 61.10  ? 1846 ARG   A CG  1 
ATOM   428 C  CD  . ARG   A 1 53  ? -30.552 18.949 -22.689 1.00 59.44  ? 1846 ARG   A CD  1 
ATOM   429 N  NE  . ARG   A 1 53  ? -29.413 18.060 -22.911 1.00 65.69  ? 1846 ARG   A NE  1 
ATOM   430 C  CZ  . ARG   A 1 53  ? -28.156 18.468 -23.057 1.00 70.47  ? 1846 ARG   A CZ  1 
ATOM   431 N  NH1 . ARG   A 1 53  ? -27.865 19.761 -23.008 1.00 72.05  ? 1846 ARG   A NH1 1 
ATOM   432 N  NH2 . ARG   A 1 53  ? -27.187 17.583 -23.249 1.00 71.78  ? 1846 ARG   A NH2 1 
ATOM   433 N  N   . LEU   A 1 54  ? -34.382 17.663 -19.343 1.00 57.19  ? 1847 LEU   A N   1 
ATOM   434 C  CA  . LEU   A 1 54  ? -34.314 16.700 -18.251 1.00 56.90  ? 1847 LEU   A CA  1 
ATOM   435 C  C   . LEU   A 1 54  ? -35.447 15.679 -18.345 1.00 63.90  ? 1847 LEU   A C   1 
ATOM   436 O  O   . LEU   A 1 54  ? -35.236 14.485 -18.100 1.00 67.28  ? 1847 LEU   A O   1 
ATOM   437 C  CB  . LEU   A 1 54  ? -34.350 17.443 -16.918 1.00 52.69  ? 1847 LEU   A CB  1 
ATOM   438 C  CG  . LEU   A 1 54  ? -33.772 16.746 -15.692 1.00 53.47  ? 1847 LEU   A CG  1 
ATOM   439 C  CD1 . LEU   A 1 54  ? -32.408 16.147 -15.999 1.00 49.13  ? 1847 LEU   A CD1 1 
ATOM   440 C  CD2 . LEU   A 1 54  ? -33.676 17.738 -14.549 1.00 54.39  ? 1847 LEU   A CD2 1 
ATOM   441 N  N   . SER   A 1 55  ? -36.648 16.131 -18.725 1.00 61.15  ? 1848 SER   A N   1 
ATOM   442 C  CA  . SER   A 1 55  ? -37.812 15.249 -18.789 1.00 64.06  ? 1848 SER   A CA  1 
ATOM   443 C  C   . SER   A 1 55  ? -37.641 14.155 -19.838 1.00 68.38  ? 1848 SER   A C   1 
ATOM   444 O  O   . SER   A 1 55  ? -38.054 13.008 -19.622 1.00 66.33  ? 1848 SER   A O   1 
ATOM   445 C  CB  . SER   A 1 55  ? -39.075 16.064 -19.084 1.00 61.23  ? 1848 SER   A CB  1 
ATOM   446 O  OG  . SER   A 1 55  ? -39.484 16.820 -17.957 1.00 61.76  ? 1848 SER   A OG  1 
ATOM   447 N  N   . ARG   A 1 56  ? -37.061 14.489 -20.988 1.00 66.80  ? 1849 ARG   A N   1 
ATOM   448 C  CA  . ARG   A 1 56  ? -36.865 13.517 -22.053 1.00 67.23  ? 1849 ARG   A CA  1 
ATOM   449 C  C   . ARG   A 1 56  ? -35.575 12.732 -21.895 1.00 66.97  ? 1849 ARG   A C   1 
ATOM   450 O  O   . ARG   A 1 56  ? -35.200 11.991 -22.810 1.00 69.73  ? 1849 ARG   A O   1 
ATOM   451 C  CB  . ARG   A 1 56  ? -36.893 14.204 -23.423 1.00 68.94  ? 1849 ARG   A CB  1 
ATOM   452 C  CG  . ARG   A 1 56  ? -35.783 15.215 -23.659 1.00 69.79  ? 1849 ARG   A CG  1 
ATOM   453 C  CD  . ARG   A 1 56  ? -35.747 15.634 -25.123 1.00 75.47  ? 1849 ARG   A CD  1 
ATOM   454 N  NE  . ARG   A 1 56  ? -34.632 16.530 -25.427 1.00 77.73  ? 1849 ARG   A NE  1 
ATOM   455 C  CZ  . ARG   A 1 56  ? -33.421 16.122 -25.799 1.00 76.06  ? 1849 ARG   A CZ  1 
ATOM   456 N  NH1 . ARG   A 1 56  ? -33.157 14.826 -25.914 1.00 74.84  ? 1849 ARG   A NH1 1 
ATOM   457 N  NH2 . ARG   A 1 56  ? -32.471 17.013 -26.053 1.00 72.56  ? 1849 ARG   A NH2 1 
ATOM   458 N  N   . GLY   A 1 57  ? -34.891 12.878 -20.763 1.00 62.52  ? 1850 GLY   A N   1 
ATOM   459 C  CA  . GLY   A 1 57  ? -33.674 12.128 -20.520 1.00 63.17  ? 1850 GLY   A CA  1 
ATOM   460 C  C   . GLY   A 1 57  ? -32.485 12.579 -21.336 1.00 65.23  ? 1850 GLY   A C   1 
ATOM   461 O  O   . GLY   A 1 57  ? -31.593 11.772 -21.610 1.00 70.01  ? 1850 GLY   A O   1 
ATOM   462 N  N   . GLY   A 1 58  ? -32.438 13.856 -21.719 1.00 61.98  ? 1851 GLY   A N   1 
ATOM   463 C  CA  . GLY   A 1 58  ? -31.397 14.391 -22.575 1.00 63.15  ? 1851 GLY   A CA  1 
ATOM   464 C  C   . GLY   A 1 58  ? -30.114 14.832 -21.902 1.00 67.19  ? 1851 GLY   A C   1 
ATOM   465 O  O   . GLY   A 1 58  ? -29.229 15.352 -22.588 1.00 67.98  ? 1851 GLY   A O   1 
ATOM   466 N  N   . TYR   A 1 59  ? -29.971 14.655 -20.590 1.00 66.99  ? 1852 TYR   A N   1 
ATOM   467 C  CA  . TYR   A 1 59  ? -28.735 14.992 -19.891 1.00 66.22  ? 1852 TYR   A CA  1 
ATOM   468 C  C   . TYR   A 1 59  ? -27.988 13.710 -19.553 1.00 72.94  ? 1852 TYR   A C   1 
ATOM   469 O  O   . TYR   A 1 59  ? -28.543 12.816 -18.905 1.00 74.70  ? 1852 TYR   A O   1 
ATOM   470 C  CB  . TYR   A 1 59  ? -29.001 15.791 -18.613 1.00 60.27  ? 1852 TYR   A CB  1 
ATOM   471 C  CG  . TYR   A 1 59  ? -29.325 17.252 -18.841 1.00 54.07  ? 1852 TYR   A CG  1 
ATOM   472 C  CD1 . TYR   A 1 59  ? -28.379 18.128 -19.363 1.00 52.92  ? 1852 TYR   A CD1 1 
ATOM   473 C  CD2 . TYR   A 1 59  ? -30.576 17.758 -18.521 1.00 50.97  ? 1852 TYR   A CD2 1 
ATOM   474 C  CE1 . TYR   A 1 59  ? -28.683 19.466 -19.572 1.00 50.22  ? 1852 TYR   A CE1 1 
ATOM   475 C  CE2 . TYR   A 1 59  ? -30.885 19.088 -18.722 1.00 47.00  ? 1852 TYR   A CE2 1 
ATOM   476 C  CZ  . TYR   A 1 59  ? -29.939 19.936 -19.246 1.00 48.33  ? 1852 TYR   A CZ  1 
ATOM   477 O  OH  . TYR   A 1 59  ? -30.265 21.255 -19.441 1.00 50.28  ? 1852 TYR   A OH  1 
ATOM   478 N  N   . THR   A 1 60  ? -26.730 13.632 -19.990 1.00 76.20  ? 1853 THR   A N   1 
ATOM   479 C  CA  . THR   A 1 60  ? -25.861 12.517 -19.627 1.00 78.48  ? 1853 THR   A CA  1 
ATOM   480 C  C   . THR   A 1 60  ? -25.361 12.656 -18.195 1.00 82.64  ? 1853 THR   A C   1 
ATOM   481 O  O   . THR   A 1 60  ? -25.641 11.811 -17.338 1.00 89.63  ? 1853 THR   A O   1 
ATOM   482 C  CB  . THR   A 1 60  ? -24.674 12.439 -20.589 1.00 75.57  ? 1853 THR   A CB  1 
ATOM   483 O  OG1 . THR   A 1 60  ? -25.124 11.998 -21.874 1.00 77.83  ? 1853 THR   A OG1 1 
ATOM   484 C  CG2 . THR   A 1 60  ? -23.618 11.477 -20.053 1.00 77.12  ? 1853 THR   A CG2 1 
ATOM   485 N  N   . SER   A 1 61  ? -24.614 13.718 -17.926 1.00 77.17  ? 1854 SER   A N   1 
ATOM   486 C  CA  . SER   A 1 61  ? -24.000 13.945 -16.633 1.00 72.50  ? 1854 SER   A CA  1 
ATOM   487 C  C   . SER   A 1 61  ? -24.527 15.243 -16.044 1.00 69.32  ? 1854 SER   A C   1 
ATOM   488 O  O   . SER   A 1 61  ? -25.199 16.032 -16.714 1.00 69.51  ? 1854 SER   A O   1 
ATOM   489 C  CB  . SER   A 1 61  ? -22.474 14.004 -16.754 1.00 71.83  ? 1854 SER   A CB  1 
ATOM   490 O  OG  . SER   A 1 61  ? -22.087 15.063 -17.610 1.00 67.59  ? 1854 SER   A OG  1 
ATOM   491 N  N   . SER   A 1 62  ? -24.205 15.461 -14.770 1.00 68.27  ? 1855 SER   A N   1 
ATOM   492 C  CA  . SER   A 1 62  ? -24.543 16.725 -14.136 1.00 66.93  ? 1855 SER   A CA  1 
ATOM   493 C  C   . SER   A 1 62  ? -23.716 17.878 -14.691 1.00 62.33  ? 1855 SER   A C   1 
ATOM   494 O  O   . SER   A 1 62  ? -24.109 19.036 -14.526 1.00 58.84  ? 1855 SER   A O   1 
ATOM   495 C  CB  . SER   A 1 62  ? -24.363 16.619 -12.618 1.00 70.91  ? 1855 SER   A CB  1 
ATOM   496 O  OG  . SER   A 1 62  ? -23.000 16.443 -12.272 1.00 75.38  ? 1855 SER   A OG  1 
ATOM   497 N  N   . GLU   A 1 63  ? -22.588 17.587 -15.349 1.00 67.41  ? 1856 GLU   A N   1 
ATOM   498 C  CA  . GLU   A 1 63  ? -21.780 18.647 -15.949 1.00 68.29  ? 1856 GLU   A CA  1 
ATOM   499 C  C   . GLU   A 1 63  ? -22.533 19.342 -17.075 1.00 65.05  ? 1856 GLU   A C   1 
ATOM   500 O  O   . GLU   A 1 63  ? -22.527 20.576 -17.171 1.00 61.22  ? 1856 GLU   A O   1 
ATOM   501 C  CB  . GLU   A 1 63  ? -20.455 18.082 -16.466 1.00 75.37  ? 1856 GLU   A CB  1 
ATOM   502 C  CG  . GLU   A 1 63  ? -19.353 18.007 -15.420 1.00 85.11  ? 1856 GLU   A CG  1 
ATOM   503 C  CD  . GLU   A 1 63  ? -19.404 16.736 -14.590 1.00 96.00  ? 1856 GLU   A CD  1 
ATOM   504 O  OE1 . GLU   A 1 63  ? -19.887 15.704 -15.105 1.00 100.11 ? 1856 GLU   A OE1 1 
ATOM   505 O  OE2 . GLU   A 1 63  ? -18.956 16.769 -13.423 1.00 99.13  ? 1856 GLU   A OE2 1 
ATOM   506 N  N   . GLU   A 1 64  ? -23.183 18.561 -17.946 1.00 64.78  ? 1857 GLU   A N   1 
ATOM   507 C  CA  . GLU   A 1 64  ? -23.965 19.151 -19.027 1.00 63.21  ? 1857 GLU   A CA  1 
ATOM   508 C  C   . GLU   A 1 64  ? -25.110 19.993 -18.488 1.00 54.70  ? 1857 GLU   A C   1 
ATOM   509 O  O   . GLU   A 1 64  ? -25.444 21.030 -19.073 1.00 52.13  ? 1857 GLU   A O   1 
ATOM   510 C  CB  . GLU   A 1 64  ? -24.505 18.055 -19.948 1.00 68.24  ? 1857 GLU   A CB  1 
ATOM   511 C  CG  . GLU   A 1 64  ? -23.429 17.221 -20.616 1.00 77.48  ? 1857 GLU   A CG  1 
ATOM   512 C  CD  . GLU   A 1 64  ? -24.000 16.027 -21.354 1.00 87.79  ? 1857 GLU   A CD  1 
ATOM   513 O  OE1 . GLU   A 1 64  ? -25.166 15.665 -21.085 1.00 89.00  ? 1857 GLU   A OE1 1 
ATOM   514 O  OE2 . GLU   A 1 64  ? -23.286 15.454 -22.207 1.00 93.15  ? 1857 GLU   A OE2 1 
ATOM   515 N  N   . PHE   A 1 65  ? -25.722 19.563 -17.382 1.00 49.02  ? 1858 PHE   A N   1 
ATOM   516 C  CA  . PHE   A 1 65  ? -26.772 20.363 -16.762 1.00 47.23  ? 1858 PHE   A CA  1 
ATOM   517 C  C   . PHE   A 1 65  ? -26.214 21.681 -16.249 1.00 44.11  ? 1858 PHE   A C   1 
ATOM   518 O  O   . PHE   A 1 65  ? -26.836 22.734 -16.421 1.00 42.04  ? 1858 PHE   A O   1 
ATOM   519 C  CB  . PHE   A 1 65  ? -27.435 19.572 -15.629 1.00 49.95  ? 1858 PHE   A CB  1 
ATOM   520 C  CG  . PHE   A 1 65  ? -28.490 20.344 -14.877 1.00 44.77  ? 1858 PHE   A CG  1 
ATOM   521 C  CD1 . PHE   A 1 65  ? -28.171 21.034 -13.716 1.00 41.74  ? 1858 PHE   A CD1 1 
ATOM   522 C  CD2 . PHE   A 1 65  ? -29.801 20.377 -15.328 1.00 44.55  ? 1858 PHE   A CD2 1 
ATOM   523 C  CE1 . PHE   A 1 65  ? -29.136 21.749 -13.025 1.00 42.19  ? 1858 PHE   A CE1 1 
ATOM   524 C  CE2 . PHE   A 1 65  ? -30.772 21.089 -14.639 1.00 43.19  ? 1858 PHE   A CE2 1 
ATOM   525 C  CZ  . PHE   A 1 65  ? -30.437 21.775 -13.487 1.00 41.09  ? 1858 PHE   A CZ  1 
ATOM   526 N  N   . ALA   A 1 66  ? -25.036 21.638 -15.622 1.00 40.59  ? 1859 ALA   A N   1 
ATOM   527 C  CA  . ALA   A 1 66  ? -24.421 22.855 -15.106 1.00 43.63  ? 1859 ALA   A CA  1 
ATOM   528 C  C   . ALA   A 1 66  ? -24.056 23.808 -16.235 1.00 45.62  ? 1859 ALA   A C   1 
ATOM   529 O  O   . ALA   A 1 66  ? -24.175 25.029 -16.084 1.00 49.03  ? 1859 ALA   A O   1 
ATOM   530 C  CB  . ALA   A 1 66  ? -23.187 22.504 -14.277 1.00 48.45  ? 1859 ALA   A CB  1 
ATOM   531 N  N   . ALA   A 1 67  ? -23.616 23.267 -17.373 1.00 40.16  ? 1860 ALA   A N   1 
ATOM   532 C  CA  . ALA   A 1 67  ? -23.269 24.107 -18.511 1.00 41.80  ? 1860 ALA   A CA  1 
ATOM   533 C  C   . ALA   A 1 67  ? -24.476 24.897 -19.001 1.00 42.75  ? 1860 ALA   A C   1 
ATOM   534 O  O   . ALA   A 1 67  ? -24.355 26.078 -19.344 1.00 46.16  ? 1860 ALA   A O   1 
ATOM   535 C  CB  . ALA   A 1 67  ? -22.690 23.248 -19.638 1.00 36.98  ? 1860 ALA   A CB  1 
ATOM   536 N  N   . ASP   A 1 68  ? -25.650 24.262 -19.047 1.00 42.15  ? 1861 ASP   A N   1 
ATOM   537 C  CA  . ASP   A 1 68  ? -26.849 24.971 -19.483 1.00 44.53  ? 1861 ASP   A CA  1 
ATOM   538 C  C   . ASP   A 1 68  ? -27.252 26.041 -18.479 1.00 45.54  ? 1861 ASP   A C   1 
ATOM   539 O  O   . ASP   A 1 68  ? -27.682 27.133 -18.869 1.00 48.44  ? 1861 ASP   A O   1 
ATOM   540 C  CB  . ASP   A 1 68  ? -27.998 23.989 -19.706 1.00 47.82  ? 1861 ASP   A CB  1 
ATOM   541 C  CG  . ASP   A 1 68  ? -27.999 23.395 -21.106 1.00 50.56  ? 1861 ASP   A CG  1 
ATOM   542 O  OD1 . ASP   A 1 68  ? -27.424 24.018 -22.023 1.00 50.58  ? 1861 ASP   A OD1 1 
ATOM   543 O  OD2 . ASP   A 1 68  ? -28.584 22.306 -21.290 1.00 52.41  ? 1861 ASP   A OD2 1 
ATOM   544 N  N   . ALA   A 1 69  ? -27.114 25.752 -17.182 1.00 37.18  ? 1862 ALA   A N   1 
ATOM   545 C  CA  . ALA   A 1 69  ? -27.470 26.745 -16.178 1.00 38.22  ? 1862 ALA   A CA  1 
ATOM   546 C  C   . ALA   A 1 69  ? -26.541 27.946 -16.248 1.00 38.33  ? 1862 ALA   A C   1 
ATOM   547 O  O   . ALA   A 1 69  ? -26.993 29.093 -16.169 1.00 36.85  ? 1862 ALA   A O   1 
ATOM   548 C  CB  . ALA   A 1 69  ? -27.444 26.120 -14.782 1.00 36.71  ? 1862 ALA   A CB  1 
ATOM   549 N  N   . LEU   A 1 70  ? -25.239 27.707 -16.403 1.00 36.22  ? 1863 LEU   A N   1 
ATOM   550 C  CA  . LEU   A 1 70  ? -24.308 28.823 -16.498 1.00 42.34  ? 1863 LEU   A CA  1 
ATOM   551 C  C   . LEU   A 1 70  ? -24.511 29.598 -17.792 1.00 40.16  ? 1863 LEU   A C   1 
ATOM   552 O  O   . LEU   A 1 70  ? -24.250 30.805 -17.840 1.00 37.80  ? 1863 LEU   A O   1 
ATOM   553 C  CB  . LEU   A 1 70  ? -22.870 28.325 -16.378 1.00 47.49  ? 1863 LEU   A CB  1 
ATOM   554 C  CG  . LEU   A 1 70  ? -22.572 27.572 -15.079 1.00 52.08  ? 1863 LEU   A CG  1 
ATOM   555 C  CD1 . LEU   A 1 70  ? -21.144 27.045 -15.082 1.00 55.40  ? 1863 LEU   A CD1 1 
ATOM   556 C  CD2 . LEU   A 1 70  ? -22.837 28.440 -13.845 1.00 46.15  ? 1863 LEU   A CD2 1 
ATOM   557 N  N   . LEU   A 1 71  ? -24.998 28.930 -18.839 1.00 40.70  ? 1864 LEU   A N   1 
ATOM   558 C  CA  . LEU   A 1 71  ? -25.323 29.625 -20.081 1.00 41.39  ? 1864 LEU   A CA  1 
ATOM   559 C  C   . LEU   A 1 71  ? -26.430 30.654 -19.865 1.00 40.78  ? 1864 LEU   A C   1 
ATOM   560 O  O   . LEU   A 1 71  ? -26.362 31.773 -20.391 1.00 36.49  ? 1864 LEU   A O   1 
ATOM   561 C  CB  . LEU   A 1 71  ? -25.729 28.609 -21.143 1.00 37.13  ? 1864 LEU   A CB  1 
ATOM   562 C  CG  . LEU   A 1 71  ? -25.952 29.093 -22.568 1.00 36.67  ? 1864 LEU   A CG  1 
ATOM   563 C  CD1 . LEU   A 1 71  ? -24.719 29.810 -23.100 1.00 34.08  ? 1864 LEU   A CD1 1 
ATOM   564 C  CD2 . LEU   A 1 71  ? -26.284 27.887 -23.420 1.00 35.85  ? 1864 LEU   A CD2 1 
ATOM   565 N  N   . VAL   A 1 72  ? -27.457 30.291 -19.089 1.00 32.13  ? 1865 VAL   A N   1 
ATOM   566 C  CA  . VAL   A 1 72  ? -28.546 31.223 -18.789 1.00 37.14  ? 1865 VAL   A CA  1 
ATOM   567 C  C   . VAL   A 1 72  ? -27.990 32.527 -18.231 1.00 39.27  ? 1865 VAL   A C   1 
ATOM   568 O  O   . VAL   A 1 72  ? -28.350 33.624 -18.675 1.00 39.17  ? 1865 VAL   A O   1 
ATOM   569 C  CB  . VAL   A 1 72  ? -29.548 30.588 -17.807 1.00 34.17  ? 1865 VAL   A CB  1 
ATOM   570 C  CG1 . VAL   A 1 72  ? -30.604 31.586 -17.419 1.00 30.81  ? 1865 VAL   A CG1 1 
ATOM   571 C  CG2 . VAL   A 1 72  ? -30.175 29.341 -18.413 1.00 33.14  ? 1865 VAL   A CG2 1 
ATOM   572 N  N   . PHE   A 1 73  ? -27.084 32.423 -17.258 1.00 34.22  ? 1866 PHE   A N   1 
ATOM   573 C  CA  . PHE   A 1 73  ? -26.587 33.607 -16.571 1.00 37.40  ? 1866 PHE   A CA  1 
ATOM   574 C  C   . PHE   A 1 73  ? -25.485 34.305 -17.355 1.00 34.55  ? 1866 PHE   A C   1 
ATOM   575 O  O   . PHE   A 1 73  ? -25.377 35.538 -17.296 1.00 39.50  ? 1866 PHE   A O   1 
ATOM   576 C  CB  . PHE   A 1 73  ? -26.110 33.221 -15.166 1.00 35.92  ? 1866 PHE   A CB  1 
ATOM   577 C  CG  . PHE   A 1 73  ? -27.106 32.385 -14.420 1.00 35.34  ? 1866 PHE   A CG  1 
ATOM   578 C  CD1 . PHE   A 1 73  ? -28.415 32.816 -14.279 1.00 29.30  ? 1866 PHE   A CD1 1 
ATOM   579 C  CD2 . PHE   A 1 73  ? -26.753 31.152 -13.904 1.00 40.15  ? 1866 PHE   A CD2 1 
ATOM   580 C  CE1 . PHE   A 1 73  ? -29.342 32.045 -13.616 1.00 30.82  ? 1866 PHE   A CE1 1 
ATOM   581 C  CE2 . PHE   A 1 73  ? -27.685 30.375 -13.237 1.00 37.01  ? 1866 PHE   A CE2 1 
ATOM   582 C  CZ  . PHE   A 1 73  ? -28.978 30.825 -13.095 1.00 30.89  ? 1866 PHE   A CZ  1 
ATOM   583 N  N   . ASP   A 1 74  ? -24.663 33.548 -18.085 1.00 29.54  ? 1867 ASP   A N   1 
ATOM   584 C  CA  . ASP   A 1 74  ? -23.732 34.175 -19.018 1.00 37.04  ? 1867 ASP   A CA  1 
ATOM   585 C  C   . ASP   A 1 74  ? -24.485 35.016 -20.043 1.00 40.28  ? 1867 ASP   A C   1 
ATOM   586 O  O   . ASP   A 1 74  ? -24.154 36.188 -20.265 1.00 40.30  ? 1867 ASP   A O   1 
ATOM   587 C  CB  . ASP   A 1 74  ? -22.868 33.112 -19.708 1.00 34.23  ? 1867 ASP   A CB  1 
ATOM   588 C  CG  . ASP   A 1 74  ? -21.766 32.567 -18.804 1.00 41.23  ? 1867 ASP   A CG  1 
ATOM   589 O  OD1 . ASP   A 1 74  ? -21.439 33.222 -17.788 1.00 42.57  ? 1867 ASP   A OD1 1 
ATOM   590 O  OD2 . ASP   A 1 74  ? -21.215 31.487 -19.114 1.00 47.23  ? 1867 ASP   A OD2 1 
ATOM   591 N  N   . ASN   A 1 75  ? -25.526 34.440 -20.661 1.00 36.72  ? 1868 ASN   A N   1 
ATOM   592 C  CA  . ASN   A 1 75  ? -26.324 35.192 -21.628 1.00 38.79  ? 1868 ASN   A CA  1 
ATOM   593 C  C   . ASN   A 1 75  ? -26.958 36.413 -20.982 1.00 36.35  ? 1868 ASN   A C   1 
ATOM   594 O  O   . ASN   A 1 75  ? -27.001 37.495 -21.579 1.00 34.07  ? 1868 ASN   A O   1 
ATOM   595 C  CB  . ASN   A 1 75  ? -27.408 34.298 -22.237 1.00 33.11  ? 1868 ASN   A CB  1 
ATOM   596 C  CG  . ASN   A 1 75  ? -26.836 33.223 -23.134 1.00 36.34  ? 1868 ASN   A CG  1 
ATOM   597 O  OD1 . ASN   A 1 75  ? -25.714 33.346 -23.633 1.00 42.02  ? 1868 ASN   A OD1 1 
ATOM   598 N  ND2 . ASN   A 1 75  ? -27.598 32.156 -23.339 1.00 35.40  ? 1868 ASN   A ND2 1 
ATOM   599 N  N   . CYS   A 1 76  ? -27.460 36.252 -19.757 1.00 34.62  ? 1869 CYS   A N   1 
ATOM   600 C  CA  . CYS   A 1 76  ? -28.097 37.357 -19.057 1.00 37.04  ? 1869 CYS   A CA  1 
ATOM   601 C  C   . CYS   A 1 76  ? -27.126 38.516 -18.861 1.00 41.50  ? 1869 CYS   A C   1 
ATOM   602 O  O   . CYS   A 1 76  ? -27.471 39.679 -19.103 1.00 42.88  ? 1869 CYS   A O   1 
ATOM   603 C  CB  . CYS   A 1 76  ? -28.638 36.860 -17.719 1.00 38.51  ? 1869 CYS   A CB  1 
ATOM   604 S  SG  . CYS   A 1 76  ? -29.332 38.149 -16.723 1.00 42.10  ? 1869 CYS   A SG  1 
ATOM   605 N  N   . GLN   A 1 77  ? -25.894 38.213 -18.445 1.00 37.94  ? 1870 GLN   A N   1 
ATOM   606 C  CA  . GLN   A 1 77  ? -24.883 39.247 -18.265 1.00 42.33  ? 1870 GLN   A CA  1 
ATOM   607 C  C   . GLN   A 1 77  ? -24.342 39.783 -19.589 1.00 38.64  ? 1870 GLN   A C   1 
ATOM   608 O  O   . GLN   A 1 77  ? -23.868 40.924 -19.631 1.00 39.15  ? 1870 GLN   A O   1 
ATOM   609 C  CB  . GLN   A 1 77  ? -23.736 38.707 -17.406 1.00 42.31  ? 1870 GLN   A CB  1 
ATOM   610 C  CG  . GLN   A 1 77  ? -24.146 38.372 -15.967 1.00 39.06  ? 1870 GLN   A CG  1 
ATOM   611 C  CD  . GLN   A 1 77  ? -23.039 37.673 -15.213 1.00 36.13  ? 1870 GLN   A CD  1 
ATOM   612 O  OE1 . GLN   A 1 77  ? -22.336 38.281 -14.409 1.00 41.83  ? 1870 GLN   A OE1 1 
ATOM   613 N  NE2 . GLN   A 1 77  ? -22.856 36.392 -15.495 1.00 35.03  ? 1870 GLN   A NE2 1 
ATOM   614 N  N   . THR   A 1 78  ? -24.396 38.993 -20.667 1.00 40.96  ? 1871 THR   A N   1 
ATOM   615 C  CA  . THR   A 1 78  ? -23.945 39.496 -21.964 1.00 37.98  ? 1871 THR   A CA  1 
ATOM   616 C  C   . THR   A 1 78  ? -24.923 40.520 -22.530 1.00 37.44  ? 1871 THR   A C   1 
ATOM   617 O  O   . THR   A 1 78  ? -24.511 41.534 -23.106 1.00 39.36  ? 1871 THR   A O   1 
ATOM   618 C  CB  . THR   A 1 78  ? -23.753 38.339 -22.951 1.00 41.84  ? 1871 THR   A CB  1 
ATOM   619 O  OG1 . THR   A 1 78  ? -22.696 37.480 -22.495 1.00 39.10  ? 1871 THR   A OG1 1 
ATOM   620 C  CG2 . THR   A 1 78  ? -23.401 38.867 -24.342 1.00 32.56  ? 1871 THR   A CG2 1 
ATOM   621 N  N   . PHE   A 1 79  ? -26.219 40.294 -22.356 1.00 36.45  ? 1872 PHE   A N   1 
ATOM   622 C  CA  . PHE   A 1 79  ? -27.190 41.176 -22.984 1.00 39.85  ? 1872 PHE   A CA  1 
ATOM   623 C  C   . PHE   A 1 79  ? -27.694 42.288 -22.069 1.00 39.58  ? 1872 PHE   A C   1 
ATOM   624 O  O   . PHE   A 1 79  ? -27.993 43.384 -22.555 1.00 36.59  ? 1872 PHE   A O   1 
ATOM   625 C  CB  . PHE   A 1 79  ? -28.381 40.364 -23.491 1.00 33.09  ? 1872 PHE   A CB  1 
ATOM   626 C  CG  . PHE   A 1 79  ? -29.284 41.141 -24.393 1.00 41.76  ? 1872 PHE   A CG  1 
ATOM   627 C  CD1 . PHE   A 1 79  ? -29.004 41.250 -25.747 1.00 44.55  ? 1872 PHE   A CD1 1 
ATOM   628 C  CD2 . PHE   A 1 79  ? -30.402 41.777 -23.891 1.00 41.73  ? 1872 PHE   A CD2 1 
ATOM   629 C  CE1 . PHE   A 1 79  ? -29.829 41.968 -26.579 1.00 46.27  ? 1872 PHE   A CE1 1 
ATOM   630 C  CE2 . PHE   A 1 79  ? -31.234 42.497 -24.723 1.00 44.46  ? 1872 PHE   A CE2 1 
ATOM   631 C  CZ  . PHE   A 1 79  ? -30.945 42.596 -26.067 1.00 45.94  ? 1872 PHE   A CZ  1 
ATOM   632 N  N   . ASN   A 1 80  ? -27.805 42.048 -20.766 1.00 37.83  ? 1873 ASN   A N   1 
ATOM   633 C  CA  . ASN   A 1 80  ? -28.467 42.984 -19.865 1.00 40.65  ? 1873 ASN   A CA  1 
ATOM   634 C  C   . ASN   A 1 80  ? -27.461 43.713 -18.989 1.00 44.34  ? 1873 ASN   A C   1 
ATOM   635 O  O   . ASN   A 1 80  ? -26.493 43.116 -18.506 1.00 45.90  ? 1873 ASN   A O   1 
ATOM   636 C  CB  . ASN   A 1 80  ? -29.483 42.261 -18.984 1.00 40.86  ? 1873 ASN   A CB  1 
ATOM   637 C  CG  . ASN   A 1 80  ? -30.476 41.461 -19.794 1.00 46.52  ? 1873 ASN   A CG  1 
ATOM   638 O  OD1 . ASN   A 1 80  ? -31.514 41.975 -20.206 1.00 47.44  ? 1873 ASN   A OD1 1 
ATOM   639 N  ND2 . ASN   A 1 80  ? -30.155 40.198 -20.040 1.00 43.36  ? 1873 ASN   A ND2 1 
ATOM   640 N  N   . GLU   A 1 81  ? -27.705 45.006 -18.781 1.00 52.06  ? 1874 GLU   A N   1 
ATOM   641 C  CA  . GLU   A 1 81  ? -26.909 45.776 -17.835 1.00 50.41  ? 1874 GLU   A CA  1 
ATOM   642 C  C   . GLU   A 1 81  ? -27.041 45.197 -16.433 1.00 40.79  ? 1874 GLU   A C   1 
ATOM   643 O  O   . GLU   A 1 81  ? -28.108 44.720 -16.032 1.00 39.43  ? 1874 GLU   A O   1 
ATOM   644 C  CB  . GLU   A 1 81  ? -27.356 47.241 -17.832 1.00 55.46  ? 1874 GLU   A CB  1 
ATOM   645 C  CG  . GLU   A 1 81  ? -27.291 47.923 -19.183 1.00 68.50  ? 1874 GLU   A CG  1 
ATOM   646 C  CD  . GLU   A 1 81  ? -25.908 48.457 -19.505 1.00 78.23  ? 1874 GLU   A CD  1 
ATOM   647 O  OE1 . GLU   A 1 81  ? -24.919 47.956 -18.925 1.00 79.02  ? 1874 GLU   A OE1 1 
ATOM   648 O  OE2 . GLU   A 1 81  ? -25.812 49.384 -20.338 1.00 84.13  ? 1874 GLU   A OE2 1 
ATOM   649 N  N   . ASP   A 1 82  ? -25.941 45.257 -15.681 1.00 42.34  ? 1875 ASP   A N   1 
ATOM   650 C  CA  . ASP   A 1 82  ? -25.945 44.748 -14.315 1.00 40.59  ? 1875 ASP   A CA  1 
ATOM   651 C  C   . ASP   A 1 82  ? -26.996 45.441 -13.454 1.00 47.56  ? 1875 ASP   A C   1 
ATOM   652 O  O   . ASP   A 1 82  ? -27.482 44.854 -12.478 1.00 44.50  ? 1875 ASP   A O   1 
ATOM   653 C  CB  . ASP   A 1 82  ? -24.557 44.906 -13.699 1.00 34.59  ? 1875 ASP   A CB  1 
ATOM   654 C  CG  . ASP   A 1 82  ? -23.492 44.102 -14.438 1.00 38.41  ? 1875 ASP   A CG  1 
ATOM   655 O  OD1 . ASP   A 1 82  ? -23.716 42.900 -14.721 1.00 38.78  ? 1875 ASP   A OD1 1 
ATOM   656 O  OD2 . ASP   A 1 82  ? -22.418 44.674 -14.725 1.00 35.92  ? 1875 ASP   A OD2 1 
ATOM   657 N  N   . ASP   A 1 83  ? -27.376 46.673 -13.796 1.00 47.73  ? 1876 ASP   A N   1 
ATOM   658 C  CA  . ASP   A 1 83  ? -28.386 47.389 -13.025 1.00 50.12  ? 1876 ASP   A CA  1 
ATOM   659 C  C   . ASP   A 1 83  ? -29.768 47.348 -13.659 1.00 47.17  ? 1876 ASP   A C   1 
ATOM   660 O  O   . ASP   A 1 83  ? -30.695 47.959 -13.120 1.00 48.33  ? 1876 ASP   A O   1 
ATOM   661 C  CB  . ASP   A 1 83  ? -27.962 48.848 -12.790 1.00 57.12  ? 1876 ASP   A CB  1 
ATOM   662 C  CG  . ASP   A 1 83  ? -27.617 49.577 -14.067 1.00 63.61  ? 1876 ASP   A CG  1 
ATOM   663 O  OD1 . ASP   A 1 83  ? -27.776 48.991 -15.156 1.00 62.90  ? 1876 ASP   A OD1 1 
ATOM   664 O  OD2 . ASP   A 1 83  ? -27.179 50.745 -13.974 1.00 65.06  ? 1876 ASP   A OD2 1 
ATOM   665 N  N   . SER   A 1 84  ? -29.942 46.634 -14.766 1.00 47.56  ? 1877 SER   A N   1 
ATOM   666 C  CA  . SER   A 1 84  ? -31.284 46.428 -15.288 1.00 43.16  ? 1877 SER   A CA  1 
ATOM   667 C  C   . SER   A 1 84  ? -32.055 45.481 -14.375 1.00 43.12  ? 1877 SER   A C   1 
ATOM   668 O  O   . SER   A 1 84  ? -31.478 44.763 -13.550 1.00 43.28  ? 1877 SER   A O   1 
ATOM   669 C  CB  . SER   A 1 84  ? -31.234 45.857 -16.705 1.00 39.60  ? 1877 SER   A CB  1 
ATOM   670 O  OG  . SER   A 1 84  ? -30.763 44.516 -16.690 1.00 41.80  ? 1877 SER   A OG  1 
ATOM   671 N  N   . GLU   A 1 85  ? -33.380 45.477 -14.535 1.00 47.03  ? 1878 GLU   A N   1 
ATOM   672 C  CA  . GLU   A 1 85  ? -34.211 44.573 -13.743 1.00 51.56  ? 1878 GLU   A CA  1 
ATOM   673 C  C   . GLU   A 1 85  ? -33.873 43.118 -14.046 1.00 50.88  ? 1878 GLU   A C   1 
ATOM   674 O  O   . GLU   A 1 85  ? -33.711 42.301 -13.131 1.00 53.61  ? 1878 GLU   A O   1 
ATOM   675 C  CB  . GLU   A 1 85  ? -35.693 44.846 -14.005 1.00 57.10  ? 1878 GLU   A CB  1 
ATOM   676 C  CG  . GLU   A 1 85  ? -36.200 46.184 -13.480 1.00 68.34  ? 1878 GLU   A CG  1 
ATOM   677 C  CD  . GLU   A 1 85  ? -36.260 46.233 -11.962 1.00 80.12  ? 1878 GLU   A CD  1 
ATOM   678 O  OE1 . GLU   A 1 85  ? -36.217 47.346 -11.397 1.00 85.03  ? 1878 GLU   A OE1 1 
ATOM   679 O  OE2 . GLU   A 1 85  ? -36.351 45.157 -11.333 1.00 82.75  ? 1878 GLU   A OE2 1 
ATOM   680 N  N   . VAL   A 1 86  ? -33.766 42.775 -15.335 1.00 46.15  ? 1879 VAL   A N   1 
ATOM   681 C  CA  . VAL   A 1 86  ? -33.418 41.409 -15.720 1.00 42.13  ? 1879 VAL   A CA  1 
ATOM   682 C  C   . VAL   A 1 86  ? -32.025 41.059 -15.221 1.00 41.74  ? 1879 VAL   A C   1 
ATOM   683 O  O   . VAL   A 1 86  ? -31.786 39.949 -14.729 1.00 41.54  ? 1879 VAL   A O   1 
ATOM   684 C  CB  . VAL   A 1 86  ? -33.528 41.235 -17.249 1.00 46.75  ? 1879 VAL   A CB  1 
ATOM   685 C  CG1 . VAL   A 1 86  ? -32.839 39.954 -17.696 1.00 30.57  ? 1879 VAL   A CG1 1 
ATOM   686 C  CG2 . VAL   A 1 86  ? -34.986 41.234 -17.683 1.00 41.11  ? 1879 VAL   A CG2 1 
ATOM   687 N  N   . GLY   A 1 87  ? -31.087 42.002 -15.331 1.00 40.26  ? 1880 GLY   A N   1 
ATOM   688 C  CA  . GLY   A 1 87  ? -29.731 41.740 -14.883 1.00 37.07  ? 1880 GLY   A CA  1 
ATOM   689 C  C   . GLY   A 1 87  ? -29.644 41.511 -13.386 1.00 45.98  ? 1880 GLY   A C   1 
ATOM   690 O  O   . GLY   A 1 87  ? -28.904 40.637 -12.924 1.00 43.11  ? 1880 GLY   A O   1 
ATOM   691 N  N   . LYS   A 1 88  ? -30.404 42.288 -12.608 1.00 47.02  ? 1881 LYS   A N   1 
ATOM   692 C  CA  . LYS   A 1 88  ? -30.385 42.116 -11.159 1.00 43.79  ? 1881 LYS   A CA  1 
ATOM   693 C  C   . LYS   A 1 88  ? -30.966 40.766 -10.756 1.00 45.31  ? 1881 LYS   A C   1 
ATOM   694 O  O   . LYS   A 1 88  ? -30.453 40.112 -9.839  1.00 47.20  ? 1881 LYS   A O   1 
ATOM   695 C  CB  . LYS   A 1 88  ? -31.138 43.260 -10.481 1.00 39.65  ? 1881 LYS   A CB  1 
ATOM   696 C  CG  . LYS   A 1 88  ? -30.384 44.585 -10.498 1.00 46.58  ? 1881 LYS   A CG  1 
ATOM   697 C  CD  . LYS   A 1 88  ? -31.074 45.643 -9.644  1.00 58.01  ? 1881 LYS   A CD  1 
ATOM   698 C  CE  . LYS   A 1 88  ? -32.430 46.041 -10.211 1.00 64.73  ? 1881 LYS   A CE  1 
ATOM   699 N  NZ  . LYS   A 1 88  ? -33.088 47.093 -9.376  1.00 70.23  ? 1881 LYS   A NZ  1 
ATOM   700 N  N   . ALA   A 1 89  ? -32.029 40.327 -11.437 1.00 42.59  ? 1882 ALA   A N   1 
ATOM   701 C  CA  . ALA   A 1 89  ? -32.579 39.003 -11.162 1.00 43.72  ? 1882 ALA   A CA  1 
ATOM   702 C  C   . ALA   A 1 89  ? -31.594 37.899 -11.525 1.00 44.06  ? 1882 ALA   A C   1 
ATOM   703 O  O   . ALA   A 1 89  ? -31.566 36.852 -10.865 1.00 45.99  ? 1882 ALA   A O   1 
ATOM   704 C  CB  . ALA   A 1 89  ? -33.894 38.808 -11.919 1.00 41.55  ? 1882 ALA   A CB  1 
ATOM   705 N  N   . GLY   A 1 90  ? -30.779 38.113 -12.560 1.00 41.75  ? 1883 GLY   A N   1 
ATOM   706 C  CA  . GLY   A 1 90  ? -29.826 37.091 -12.962 1.00 39.68  ? 1883 GLY   A CA  1 
ATOM   707 C  C   . GLY   A 1 90  ? -28.683 36.932 -11.976 1.00 34.71  ? 1883 GLY   A C   1 
ATOM   708 O  O   . GLY   A 1 90  ? -28.214 35.817 -11.730 1.00 33.59  ? 1883 GLY   A O   1 
ATOM   709 N  N   . HIS   A 1 91  ? -28.208 38.042 -11.409 1.00 31.74  ? 1884 HIS   A N   1 
ATOM   710 C  CA  . HIS   A 1 91  ? -27.165 37.953 -10.394 1.00 36.64  ? 1884 HIS   A CA  1 
ATOM   711 C  C   . HIS   A 1 91  ? -27.666 37.211 -9.166  1.00 35.34  ? 1884 HIS   A C   1 
ATOM   712 O  O   . HIS   A 1 91  ? -26.944 36.391 -8.589  1.00 41.26  ? 1884 HIS   A O   1 
ATOM   713 C  CB  . HIS   A 1 91  ? -26.670 39.349 -10.026 1.00 35.70  ? 1884 HIS   A CB  1 
ATOM   714 C  CG  . HIS   A 1 91  ? -25.813 39.969 -11.082 1.00 40.60  ? 1884 HIS   A CG  1 
ATOM   715 N  ND1 . HIS   A 1 91  ? -24.762 39.297 -11.670 1.00 41.28  ? 1884 HIS   A ND1 1 
ATOM   716 C  CD2 . HIS   A 1 91  ? -25.857 41.187 -11.669 1.00 42.72  ? 1884 HIS   A CD2 1 
ATOM   717 C  CE1 . HIS   A 1 91  ? -24.190 40.079 -12.567 1.00 37.56  ? 1884 HIS   A CE1 1 
ATOM   718 N  NE2 . HIS   A 1 91  ? -24.840 41.229 -12.591 1.00 42.05  ? 1884 HIS   A NE2 1 
ATOM   719 N  N   . ILE   A 1 92  ? -28.908 37.474 -8.763  1.00 37.18  ? 1885 ILE   A N   1 
ATOM   720 C  CA  . ILE   A 1 92  ? -29.508 36.722 -7.667  1.00 41.23  ? 1885 ILE   A CA  1 
ATOM   721 C  C   . ILE   A 1 92  ? -29.601 35.244 -8.023  1.00 42.41  ? 1885 ILE   A C   1 
ATOM   722 O  O   . ILE   A 1 92  ? -29.264 34.371 -7.210  1.00 36.76  ? 1885 ILE   A O   1 
ATOM   723 C  CB  . ILE   A 1 92  ? -30.887 37.309 -7.320  1.00 40.69  ? 1885 ILE   A CB  1 
ATOM   724 C  CG1 . ILE   A 1 92  ? -30.719 38.677 -6.657  1.00 37.78  ? 1885 ILE   A CG1 1 
ATOM   725 C  CG2 . ILE   A 1 92  ? -31.665 36.349 -6.442  1.00 40.65  ? 1885 ILE   A CG2 1 
ATOM   726 C  CD1 . ILE   A 1 92  ? -32.018 39.452 -6.531  1.00 39.15  ? 1885 ILE   A CD1 1 
ATOM   727 N  N   . MET   A 1 93  ? -30.046 34.937 -9.246  1.00 38.59  ? 1886 MET   A N   1 
ATOM   728 C  CA  . MET   A 1 93  ? -30.195 33.539 -9.637  1.00 36.65  ? 1886 MET   A CA  1 
ATOM   729 C  C   . MET   A 1 93  ? -28.845 32.860 -9.828  1.00 41.22  ? 1886 MET   A C   1 
ATOM   730 O  O   . MET   A 1 93  ? -28.692 31.679 -9.489  1.00 45.13  ? 1886 MET   A O   1 
ATOM   731 C  CB  . MET   A 1 93  ? -31.034 33.435 -10.909 1.00 33.71  ? 1886 MET   A CB  1 
ATOM   732 C  CG  . MET   A 1 93  ? -32.504 33.764 -10.711 1.00 41.04  ? 1886 MET   A CG  1 
ATOM   733 S  SD  . MET   A 1 93  ? -33.229 32.885 -9.310  1.00 50.43  ? 1886 MET   A SD  1 
ATOM   734 C  CE  . MET   A 1 93  ? -33.019 31.167 -9.771  1.00 40.38  ? 1886 MET   A CE  1 
ATOM   735 N  N   . ARG   A 1 94  ? -27.862 33.586 -10.366 1.00 40.54  ? 1887 ARG   A N   1 
ATOM   736 C  CA  . ARG   A 1 94  ? -26.534 33.015 -10.558 1.00 39.12  ? 1887 ARG   A CA  1 
ATOM   737 C  C   . ARG   A 1 94  ? -25.875 32.702 -9.218  1.00 36.30  ? 1887 ARG   A C   1 
ATOM   738 O  O   . ARG   A 1 94  ? -25.308 31.619 -9.032  1.00 40.01  ? 1887 ARG   A O   1 
ATOM   739 C  CB  . ARG   A 1 94  ? -25.671 33.971 -11.388 1.00 28.51  ? 1887 ARG   A CB  1 
ATOM   740 C  CG  . ARG   A 1 94  ? -24.285 33.453 -11.721 1.00 28.44  ? 1887 ARG   A CG  1 
ATOM   741 C  CD  . ARG   A 1 94  ? -23.435 34.539 -12.383 1.00 31.29  ? 1887 ARG   A CD  1 
ATOM   742 N  NE  . ARG   A 1 94  ? -23.581 35.829 -11.708 1.00 35.61  ? 1887 ARG   A NE  1 
ATOM   743 C  CZ  . ARG   A 1 94  ? -23.003 36.137 -10.547 1.00 40.68  ? 1887 ARG   A CZ  1 
ATOM   744 N  NH1 . ARG   A 1 94  ? -22.230 35.249 -9.929  1.00 32.39  ? 1887 ARG   A NH1 1 
ATOM   745 N  NH2 . ARG   A 1 94  ? -23.194 37.334 -10.000 1.00 36.81  ? 1887 ARG   A NH2 1 
ATOM   746 N  N   . ARG   A 1 95  ? -25.934 33.638 -8.268  1.00 34.27  ? 1888 ARG   A N   1 
ATOM   747 C  CA  . ARG   A 1 95  ? -25.341 33.374 -6.959  1.00 37.79  ? 1888 ARG   A CA  1 
ATOM   748 C  C   . ARG   A 1 95  ? -26.047 32.214 -6.266  1.00 40.88  ? 1888 ARG   A C   1 
ATOM   749 O  O   . ARG   A 1 95  ? -25.400 31.374 -5.628  1.00 39.59  ? 1888 ARG   A O   1 
ATOM   750 C  CB  . ARG   A 1 95  ? -25.378 34.635 -6.092  1.00 35.94  ? 1888 ARG   A CB  1 
ATOM   751 C  CG  . ARG   A 1 95  ? -24.376 35.698 -6.527  1.00 38.18  ? 1888 ARG   A CG  1 
ATOM   752 C  CD  . ARG   A 1 95  ? -24.292 36.831 -5.524  1.00 42.06  ? 1888 ARG   A CD  1 
ATOM   753 N  NE  . ARG   A 1 95  ? -25.518 37.627 -5.468  1.00 43.30  ? 1888 ARG   A NE  1 
ATOM   754 C  CZ  . ARG   A 1 95  ? -25.705 38.761 -6.137  1.00 41.86  ? 1888 ARG   A CZ  1 
ATOM   755 N  NH1 . ARG   A 1 95  ? -24.748 39.239 -6.930  1.00 36.58  ? 1888 ARG   A NH1 1 
ATOM   756 N  NH2 . ARG   A 1 95  ? -26.850 39.419 -6.016  1.00 38.50  ? 1888 ARG   A NH2 1 
ATOM   757 N  N   . PHE   A 1 96  ? -27.375 32.135 -6.408  1.00 41.33  ? 1889 PHE   A N   1 
ATOM   758 C  CA  . PHE   A 1 96  ? -28.118 31.012 -5.847  1.00 43.18  ? 1889 PHE   A CA  1 
ATOM   759 C  C   . PHE   A 1 96  ? -27.651 29.688 -6.442  1.00 46.79  ? 1889 PHE   A C   1 
ATOM   760 O  O   . PHE   A 1 96  ? -27.432 28.713 -5.714  1.00 47.70  ? 1889 PHE   A O   1 
ATOM   761 C  CB  . PHE   A 1 96  ? -29.619 31.196 -6.073  1.00 42.83  ? 1889 PHE   A CB  1 
ATOM   762 C  CG  . PHE   A 1 96  ? -30.449 30.058 -5.549  1.00 48.64  ? 1889 PHE   A CG  1 
ATOM   763 C  CD1 . PHE   A 1 96  ? -30.853 30.029 -4.219  1.00 50.27  ? 1889 PHE   A CD1 1 
ATOM   764 C  CD2 . PHE   A 1 96  ? -30.817 29.009 -6.379  1.00 47.00  ? 1889 PHE   A CD2 1 
ATOM   765 C  CE1 . PHE   A 1 96  ? -31.611 28.976 -3.731  1.00 49.82  ? 1889 PHE   A CE1 1 
ATOM   766 C  CE2 . PHE   A 1 96  ? -31.576 27.951 -5.895  1.00 51.90  ? 1889 PHE   A CE2 1 
ATOM   767 C  CZ  . PHE   A 1 96  ? -31.973 27.935 -4.571  1.00 54.43  ? 1889 PHE   A CZ  1 
ATOM   768 N  N   . PHE   A 1 97  ? -27.503 29.627 -7.770  1.00 43.02  ? 1890 PHE   A N   1 
ATOM   769 C  CA  . PHE   A 1 97  ? -27.097 28.366 -8.383  1.00 39.65  ? 1890 PHE   A CA  1 
ATOM   770 C  C   . PHE   A 1 97  ? -25.676 27.987 -7.991  1.00 39.65  ? 1890 PHE   A C   1 
ATOM   771 O  O   . PHE   A 1 97  ? -25.410 26.823 -7.672  1.00 45.98  ? 1890 PHE   A O   1 
ATOM   772 C  CB  . PHE   A 1 97  ? -27.210 28.418 -9.907  1.00 35.40  ? 1890 PHE   A CB  1 
ATOM   773 C  CG  . PHE   A 1 97  ? -26.635 27.207 -10.574 1.00 34.49  ? 1890 PHE   A CG  1 
ATOM   774 C  CD1 . PHE   A 1 97  ? -27.370 26.035 -10.665 1.00 37.70  ? 1890 PHE   A CD1 1 
ATOM   775 C  CD2 . PHE   A 1 97  ? -25.342 27.219 -11.068 1.00 35.51  ? 1890 PHE   A CD2 1 
ATOM   776 C  CE1 . PHE   A 1 97  ? -26.835 24.906 -11.258 1.00 43.19  ? 1890 PHE   A CE1 1 
ATOM   777 C  CE2 . PHE   A 1 97  ? -24.799 26.094 -11.658 1.00 37.39  ? 1890 PHE   A CE2 1 
ATOM   778 C  CZ  . PHE   A 1 97  ? -25.545 24.935 -11.758 1.00 42.58  ? 1890 PHE   A CZ  1 
ATOM   779 N  N   . GLU   A 1 98  ? -24.746 28.944 -8.032  1.00 43.30  ? 1891 GLU   A N   1 
ATOM   780 C  CA  . GLU   A 1 98  ? -23.358 28.634 -7.710  1.00 48.88  ? 1891 GLU   A CA  1 
ATOM   781 C  C   . GLU   A 1 98  ? -23.234 28.088 -6.293  1.00 52.06  ? 1891 GLU   A C   1 
ATOM   782 O  O   . GLU   A 1 98  ? -22.565 27.075 -6.064  1.00 55.70  ? 1891 GLU   A O   1 
ATOM   783 C  CB  . GLU   A 1 98  ? -22.482 29.872 -7.890  1.00 53.21  ? 1891 GLU   A CB  1 
ATOM   784 C  CG  . GLU   A 1 98  ? -22.135 30.201 -9.340  1.00 58.96  ? 1891 GLU   A CG  1 
ATOM   785 C  CD  . GLU   A 1 98  ? -21.191 31.391 -9.447  1.00 70.07  ? 1891 GLU   A CD  1 
ATOM   786 O  OE1 . GLU   A 1 98  ? -20.584 31.766 -8.417  1.00 75.04  ? 1891 GLU   A OE1 1 
ATOM   787 O  OE2 . GLU   A 1 98  ? -21.063 31.956 -10.553 1.00 70.52  ? 1891 GLU   A OE2 1 
ATOM   788 N  N   . SER   A 1 99  ? -23.889 28.735 -5.328  1.00 47.78  ? 1892 SER   A N   1 
ATOM   789 C  CA  . SER   A 1 99  ? -23.785 28.278 -3.945  1.00 55.66  ? 1892 SER   A CA  1 
ATOM   790 C  C   . SER   A 1 99  ? -24.452 26.920 -3.763  1.00 61.66  ? 1892 SER   A C   1 
ATOM   791 O  O   . SER   A 1 99  ? -23.888 26.020 -3.130  1.00 66.40  ? 1892 SER   A O   1 
ATOM   792 C  CB  . SER   A 1 99  ? -24.398 29.308 -2.997  1.00 57.31  ? 1892 SER   A CB  1 
ATOM   793 O  OG  . SER   A 1 99  ? -25.815 29.231 -3.010  1.00 64.48  ? 1892 SER   A OG  1 
ATOM   794 N  N   . ARG   A 1 100 ? -25.656 26.752 -4.317  1.00 56.53  ? 1893 ARG   A N   1 
ATOM   795 C  CA  . ARG   A 1 100 ? -26.369 25.487 -4.165  1.00 57.97  ? 1893 ARG   A CA  1 
ATOM   796 C  C   . ARG   A 1 100 ? -25.623 24.347 -4.847  1.00 56.90  ? 1893 ARG   A C   1 
ATOM   797 O  O   . ARG   A 1 100 ? -25.532 23.239 -4.305  1.00 58.85  ? 1893 ARG   A O   1 
ATOM   798 C  CB  . ARG   A 1 100 ? -27.783 25.621 -4.727  1.00 58.89  ? 1893 ARG   A CB  1 
ATOM   799 C  CG  . ARG   A 1 100 ? -28.751 24.559 -4.251  1.00 64.14  ? 1893 ARG   A CG  1 
ATOM   800 C  CD  . ARG   A 1 100 ? -29.043 24.696 -2.762  1.00 68.02  ? 1893 ARG   A CD  1 
ATOM   801 N  NE  . ARG   A 1 100 ? -30.224 23.926 -2.384  1.00 73.53  ? 1893 ARG   A NE  1 
ATOM   802 C  CZ  . ARG   A 1 100 ? -30.209 22.630 -2.092  1.00 79.81  ? 1893 ARG   A CZ  1 
ATOM   803 N  NH1 . ARG   A 1 100 ? -29.069 21.952 -2.122  1.00 84.46  ? 1893 ARG   A NH1 1 
ATOM   804 N  NH2 . ARG   A 1 100 ? -31.337 22.012 -1.769  1.00 79.14  ? 1893 ARG   A NH2 1 
ATOM   805 N  N   . TRP   A 1 101 ? -25.069 24.604 -6.032  1.00 52.04  ? 1894 TRP   A N   1 
ATOM   806 C  CA  . TRP   A 1 101 ? -24.326 23.571 -6.745  1.00 54.20  ? 1894 TRP   A CA  1 
ATOM   807 C  C   . TRP   A 1 101 ? -23.078 23.150 -5.983  1.00 62.17  ? 1894 TRP   A C   1 
ATOM   808 O  O   . TRP   A 1 101 ? -22.665 21.987 -6.063  1.00 64.57  ? 1894 TRP   A O   1 
ATOM   809 C  CB  . TRP   A 1 101 ? -23.954 24.074 -8.142  1.00 53.76  ? 1894 TRP   A CB  1 
ATOM   810 C  CG  . TRP   A 1 101 ? -23.320 23.046 -9.022  1.00 57.54  ? 1894 TRP   A CG  1 
ATOM   811 C  CD1 . TRP   A 1 101 ? -21.986 22.842 -9.216  1.00 60.84  ? 1894 TRP   A CD1 1 
ATOM   812 C  CD2 . TRP   A 1 101 ? -23.997 22.079 -9.834  1.00 56.35  ? 1894 TRP   A CD2 1 
ATOM   813 N  NE1 . TRP   A 1 101 ? -21.789 21.807 -10.099 1.00 62.57  ? 1894 TRP   A NE1 1 
ATOM   814 C  CE2 . TRP   A 1 101 ? -23.008 21.321 -10.492 1.00 60.12  ? 1894 TRP   A CE2 1 
ATOM   815 C  CE3 . TRP   A 1 101 ? -25.344 21.777 -10.065 1.00 57.67  ? 1894 TRP   A CE3 1 
ATOM   816 C  CZ2 . TRP   A 1 101 ? -23.322 20.281 -11.364 1.00 63.78  ? 1894 TRP   A CZ2 1 
ATOM   817 C  CZ3 . TRP   A 1 101 ? -25.654 20.748 -10.933 1.00 62.68  ? 1894 TRP   A CZ3 1 
ATOM   818 C  CH2 . TRP   A 1 101 ? -24.647 20.011 -11.572 1.00 63.12  ? 1894 TRP   A CH2 1 
ATOM   819 N  N   . GLU   A 1 102 ? -22.465 24.075 -5.242  1.00 68.18  ? 1895 GLU   A N   1 
ATOM   820 C  CA  . GLU   A 1 102 ? -21.238 23.758 -4.522  1.00 77.93  ? 1895 GLU   A CA  1 
ATOM   821 C  C   . GLU   A 1 102 ? -21.515 23.108 -3.172  1.00 84.40  ? 1895 GLU   A C   1 
ATOM   822 O  O   . GLU   A 1 102 ? -20.723 22.268 -2.729  1.00 86.97  ? 1895 GLU   A O   1 
ATOM   823 C  CB  . GLU   A 1 102 ? -20.385 25.018 -4.348  1.00 82.78  ? 1895 GLU   A CB  1 
ATOM   824 C  CG  . GLU   A 1 102 ? -19.805 25.564 -5.658  1.00 86.67  ? 1895 GLU   A CG  1 
ATOM   825 C  CD  . GLU   A 1 102 ? -18.843 26.729 -5.449  1.00 89.93  ? 1895 GLU   A CD  1 
ATOM   826 O  OE1 . GLU   A 1 102 ? -17.839 26.554 -4.724  1.00 93.43  ? 1895 GLU   A OE1 1 
ATOM   827 O  OE2 . GLU   A 1 102 ? -19.090 27.821 -6.009  1.00 88.03  ? 1895 GLU   A OE2 1 
ATOM   828 N  N   . GLU   A 1 103 ? -22.620 23.460 -2.507  1.00 89.05  ? 1896 GLU   A N   1 
ATOM   829 C  CA  . GLU   A 1 103 ? -23.026 22.711 -1.317  1.00 97.39  ? 1896 GLU   A CA  1 
ATOM   830 C  C   . GLU   A 1 103 ? -23.492 21.267 -1.465  1.00 95.85  ? 1896 GLU   A C   1 
ATOM   831 O  O   . GLU   A 1 103 ? -23.816 20.589 -0.484  1.00 98.46  ? 1896 GLU   A O   1 
ATOM   832 C  CB  . GLU   A 1 103 ? -23.861 23.581 -0.374  1.00 105.18 ? 1896 GLU   A CB  1 
ATOM   833 C  CG  . GLU   A 1 103 ? -25.194 24.105 -0.893  1.00 109.10 ? 1896 GLU   A CG  1 
ATOM   834 C  CD  . GLU   A 1 103 ? -25.976 24.848 0.189   1.00 114.15 ? 1896 GLU   A CD  1 
ATOM   835 O  OE1 . GLU   A 1 103 ? -25.858 24.473 1.376   1.00 119.05 ? 1896 GLU   A OE1 1 
ATOM   836 O  OE2 . GLU   A 1 103 ? -26.699 25.812 -0.142  1.00 114.14 ? 1896 GLU   A OE2 1 
ATOM   837 N  N   . PHE   A 1 104 ? -23.552 20.794 -2.709  1.00 91.47  ? 1897 PHE   A N   1 
ATOM   838 C  CA  . PHE   A 1 104 ? -23.596 19.374 -3.021  1.00 90.99  ? 1897 PHE   A CA  1 
ATOM   839 C  C   . PHE   A 1 104 ? -22.356 18.712 -3.603  1.00 91.25  ? 1897 PHE   A C   1 
ATOM   840 O  O   . PHE   A 1 104 ? -22.021 17.579 -3.243  1.00 93.29  ? 1897 PHE   A O   1 
ATOM   841 C  CB  . PHE   A 1 104 ? -24.775 19.227 -3.977  1.00 87.38  ? 1897 PHE   A CB  1 
ATOM   842 C  CG  . PHE   A 1 104 ? -25.268 17.811 -4.113  1.00 93.50  ? 1897 PHE   A CG  1 
ATOM   843 C  CD1 . PHE   A 1 104 ? -24.929 17.044 -5.216  1.00 95.91  ? 1897 PHE   A CD1 1 
ATOM   844 C  CD2 . PHE   A 1 104 ? -26.063 17.241 -3.128  1.00 95.16  ? 1897 PHE   A CD2 1 
ATOM   845 C  CE1 . PHE   A 1 104 ? -25.384 15.735 -5.344  1.00 97.99  ? 1897 PHE   A CE1 1 
ATOM   846 C  CE2 . PHE   A 1 104 ? -26.522 15.936 -3.249  1.00 96.23  ? 1897 PHE   A CE2 1 
ATOM   847 C  CZ  . PHE   A 1 104 ? -26.181 15.183 -4.357  1.00 97.33  ? 1897 PHE   A CZ  1 
ATOM   848 N  N   . TYR   A 1 105 ? -21.668 19.415 -4.498  1.00 87.72  ? 1898 TYR   A N   1 
ATOM   849 C  CA  . TYR   A 1 105 ? -20.445 18.904 -5.108  1.00 85.25  ? 1898 TYR   A CA  1 
ATOM   850 C  C   . TYR   A 1 105 ? -19.223 19.675 -4.609  1.00 82.80  ? 1898 TYR   A C   1 
ATOM   851 O  O   . TYR   A 1 105 ? -18.673 19.375 -3.550  1.00 83.73  ? 1898 TYR   A O   1 
ATOM   852 C  CB  . TYR   A 1 105 ? -20.526 18.987 -6.634  1.00 82.55  ? 1898 TYR   A CB  1 
ATOM   853 C  CG  . TYR   A 1 105 ? -21.786 18.395 -7.235  1.00 83.60  ? 1898 TYR   A CG  1 
ATOM   854 C  CD1 . TYR   A 1 105 ? -21.863 17.044 -7.550  1.00 86.47  ? 1898 TYR   A CD1 1 
ATOM   855 C  CD2 . TYR   A 1 105 ? -22.892 19.192 -7.502  1.00 81.76  ? 1898 TYR   A CD2 1 
ATOM   856 C  CE1 . TYR   A 1 105 ? -23.012 16.502 -8.107  1.00 86.02  ? 1898 TYR   A CE1 1 
ATOM   857 C  CE2 . TYR   A 1 105 ? -24.044 18.660 -8.058  1.00 80.58  ? 1898 TYR   A CE2 1 
ATOM   858 C  CZ  . TYR   A 1 105 ? -24.097 17.315 -8.360  1.00 82.52  ? 1898 TYR   A CZ  1 
ATOM   859 O  OH  . TYR   A 1 105 ? -25.241 16.781 -8.908  1.00 81.51  ? 1898 TYR   A OH  1 
HETATM 860 C  C01 A A1IAB B 2 .   ? -33.648 40.122 -23.211 0.46 43.84  ? 1901 A1IAB A C01 1 
HETATM 861 C  C01 B A1IAB B 2 .   ? -33.742 40.041 -23.231 0.41 44.13  ? 1901 A1IAB A C01 1 
HETATM 862 C  C02 A A1IAB B 2 .   ? -33.357 39.340 -21.932 0.46 41.98  ? 1901 A1IAB A C02 1 
HETATM 863 C  C02 B A1IAB B 2 .   ? -33.441 39.276 -21.943 0.41 41.98  ? 1901 A1IAB A C02 1 
HETATM 864 C  C04 A A1IAB B 2 .   ? -34.515 38.812 -21.072 0.46 42.44  ? 1901 A1IAB A C04 1 
HETATM 865 C  C04 B A1IAB B 2 .   ? -34.594 38.748 -21.076 0.41 42.44  ? 1901 A1IAB A C04 1 
HETATM 866 C  C05 A A1IAB B 2 .   ? -34.542 37.616 -20.384 0.46 42.25  ? 1901 A1IAB A C05 1 
HETATM 867 C  C05 B A1IAB B 2 .   ? -34.621 37.547 -20.398 0.41 42.58  ? 1901 A1IAB A C05 1 
HETATM 868 C  C06 A A1IAB B 2 .   ? -33.427 36.579 -20.340 0.46 39.47  ? 1901 A1IAB A C06 1 
HETATM 869 C  C06 B A1IAB B 2 .   ? -33.511 36.503 -20.374 0.41 39.87  ? 1901 A1IAB A C06 1 
HETATM 870 C  C08 A A1IAB B 2 .   ? -36.458 38.622 -20.022 0.46 44.05  ? 1901 A1IAB A C08 1 
HETATM 871 C  C08 B A1IAB B 2 .   ? -36.527 38.560 -20.009 0.41 44.33  ? 1901 A1IAB A C08 1 
HETATM 872 C  C09 A A1IAB B 2 .   ? -37.882 38.917 -19.497 0.46 49.33  ? 1901 A1IAB A C09 1 
HETATM 873 C  C09 B A1IAB B 2 .   ? -37.944 38.858 -19.467 0.41 49.38  ? 1901 A1IAB A C09 1 
HETATM 874 C  C12 A A1IAB B 2 .   ? -38.687 36.457 -20.008 0.46 52.95  ? 1901 A1IAB A C12 1 
HETATM 875 C  C12 B A1IAB B 2 .   ? -38.807 36.464 -20.153 0.41 53.05  ? 1901 A1IAB A C12 1 
HETATM 876 C  C13 A A1IAB B 2 .   ? -39.728 36.038 -21.050 0.46 54.56  ? 1901 A1IAB A C13 1 
HETATM 877 C  C13 B A1IAB B 2 .   ? -39.795 36.183 -21.288 0.41 54.46  ? 1901 A1IAB A C13 1 
HETATM 878 C  C14 A A1IAB B 2 .   ? -41.119 36.239 -20.569 0.46 56.62  ? 1901 A1IAB A C14 1 
HETATM 879 C  C14 B A1IAB B 2 .   ? -41.191 36.536 -20.923 0.41 56.58  ? 1901 A1IAB A C14 1 
HETATM 880 C  C15 A A1IAB B 2 .   ? -41.347 37.617 -20.083 0.46 59.44  ? 1901 A1IAB A C15 1 
HETATM 881 C  C15 B A1IAB B 2 .   ? -41.329 36.864 -19.487 0.41 60.41  ? 1901 A1IAB A C15 1 
HETATM 882 C  C16 A A1IAB B 2 .   ? -40.317 38.034 -19.026 0.46 55.75  ? 1901 A1IAB A C16 1 
HETATM 883 C  C16 B A1IAB B 2 .   ? -40.403 38.012 -19.064 0.41 55.69  ? 1901 A1IAB A C16 1 
HETATM 884 C  C17 A A1IAB B 2 .   ? -42.775 37.629 -19.508 0.46 65.81  ? 1901 A1IAB A C17 1 
HETATM 885 C  C17 B A1IAB B 2 .   ? -42.808 37.235 -19.282 0.41 66.27  ? 1901 A1IAB A C17 1 
HETATM 886 C  C18 A A1IAB B 2 .   ? -43.606 38.729 -19.409 0.46 68.78  ? 1901 A1IAB A C18 1 
HETATM 887 C  C18 B A1IAB B 2 .   ? -43.369 38.487 -19.451 0.41 68.79  ? 1901 A1IAB A C18 1 
HETATM 888 C  C19 A A1IAB B 2 .   ? -43.273 40.156 -19.851 0.46 72.35  ? 1901 A1IAB A C19 1 
HETATM 889 C  C19 B A1IAB B 2 .   ? -42.633 39.760 -19.876 0.41 72.52  ? 1901 A1IAB A C19 1 
HETATM 890 C  C21 A A1IAB B 2 .   ? -41.771 41.803 -19.958 0.46 73.71  ? 1901 A1IAB A C21 1 
HETATM 891 C  C21 B A1IAB B 2 .   ? -42.681 41.989 -19.973 0.41 73.99  ? 1901 A1IAB A C21 1 
HETATM 892 C  C22 A A1IAB B 2 .   ? -41.991 42.873 -18.869 0.46 73.64  ? 1901 A1IAB A C22 1 
HETATM 893 C  C22 B A1IAB B 2 .   ? -42.137 42.897 -18.850 0.41 73.64  ? 1901 A1IAB A C22 1 
HETATM 894 C  C23 A A1IAB B 2 .   ? -42.730 42.329 -18.013 0.46 73.21  ? 1901 A1IAB A C23 1 
HETATM 895 C  C23 B A1IAB B 2 .   ? -42.481 42.345 -17.777 0.41 73.19  ? 1901 A1IAB A C23 1 
HETATM 896 C  C24 A A1IAB B 2 .   ? -42.417 40.744 -18.110 0.46 73.56  ? 1901 A1IAB A C24 1 
HETATM 897 C  C24 B A1IAB B 2 .   ? -42.609 40.767 -18.118 0.41 73.56  ? 1901 A1IAB A C24 1 
HETATM 898 C  C25 A A1IAB B 2 .   ? -44.793 38.304 -18.837 0.46 68.16  ? 1901 A1IAB A C25 1 
HETATM 899 C  C25 B A1IAB B 2 .   ? -44.719 38.380 -19.164 0.41 68.59  ? 1901 A1IAB A C25 1 
HETATM 900 C  C28 A A1IAB B 2 .   ? -35.706 39.440 -20.848 0.46 43.06  ? 1901 A1IAB A C28 1 
HETATM 901 C  C28 B A1IAB B 2 .   ? -35.780 39.381 -20.835 0.41 43.04  ? 1901 A1IAB A C28 1 
HETATM 902 C  C29 A A1IAB B 2 .   ? -36.132 40.798 -21.408 0.46 42.64  ? 1901 A1IAB A C29 1 
HETATM 903 C  C29 B A1IAB B 2 .   ? -36.204 40.746 -21.379 0.41 42.60  ? 1901 A1IAB A C29 1 
HETATM 904 N  N07 A A1IAB B 2 .   ? -35.728 37.533 -19.762 0.46 43.91  ? 1901 A1IAB A N07 1 
HETATM 905 N  N07 B A1IAB B 2 .   ? -35.801 37.465 -19.765 0.41 43.51  ? 1901 A1IAB A N07 1 
HETATM 906 N  N11 A A1IAB B 2 .   ? -38.909 37.858 -19.510 0.46 51.94  ? 1901 A1IAB A N11 1 
HETATM 907 N  N11 B A1IAB B 2 .   ? -38.999 37.831 -19.557 0.41 51.96  ? 1901 A1IAB A N11 1 
HETATM 908 N  N20 A A1IAB B 2 .   ? -42.235 40.499 -19.346 0.46 74.06  ? 1901 A1IAB A N20 1 
HETATM 909 N  N20 B A1IAB B 2 .   ? -43.098 40.705 -19.291 0.41 73.96  ? 1901 A1IAB A N20 1 
HETATM 910 N  N26 A A1IAB B 2 .   ? -44.681 36.992 -18.600 0.46 67.89  ? 1901 A1IAB A N26 1 
HETATM 911 N  N26 B A1IAB B 2 .   ? -44.963 37.108 -18.834 0.41 68.43  ? 1901 A1IAB A N26 1 
HETATM 912 N  N27 A A1IAB B 2 .   ? -43.427 36.598 -19.022 0.46 67.25  ? 1901 A1IAB A N27 1 
HETATM 913 N  N27 B A1IAB B 2 .   ? -43.769 36.420 -18.913 0.41 67.95  ? 1901 A1IAB A N27 1 
HETATM 914 O  O03 A A1IAB B 2 .   ? -32.236 39.141 -21.602 0.46 41.92  ? 1901 A1IAB A O03 1 
HETATM 915 O  O03 B A1IAB B 2 .   ? -32.319 39.090 -21.612 0.41 42.40  ? 1901 A1IAB A O03 1 
HETATM 916 O  O10 A A1IAB B 2 .   ? -38.150 39.994 -19.084 0.46 51.84  ? 1901 A1IAB A O10 1 
HETATM 917 O  O10 B A1IAB B 2 .   ? -38.182 39.910 -18.980 0.41 51.95  ? 1901 A1IAB A O10 1 
HETATM 918 C  C1  . EDO   C 3 .   ? -39.958 39.314 -23.370 1.00 66.41  ? 1902 EDO   A C1  1 
HETATM 919 O  O1  . EDO   C 3 .   ? -39.985 40.735 -23.541 1.00 66.08  ? 1902 EDO   A O1  1 
HETATM 920 C  C2  . EDO   C 3 .   ? -40.121 38.652 -24.733 1.00 60.45  ? 1902 EDO   A C2  1 
HETATM 921 O  O2  . EDO   C 3 .   ? -39.657 37.296 -24.690 1.00 57.92  ? 1902 EDO   A O2  1 
HETATM 922 MG MG  . MG    D 4 .   ? -18.344 30.626 -16.043 1.00 73.30  ? 1903 MG    A MG  1 
HETATM 923 O  O   . HOH   E 5 .   ? -32.611 32.895 -20.519 1.00 45.94  ? 2001 HOH   A O   1 
HETATM 924 O  O   . HOH   E 5 .   ? -30.949 33.089 -23.324 1.00 43.59  ? 2002 HOH   A O   1 
HETATM 925 O  O   . HOH   E 5 .   ? -39.135 16.818 -15.407 1.00 50.18  ? 2003 HOH   A O   1 
HETATM 926 O  O   . HOH   E 5 .   ? -24.765 32.504 -25.933 1.00 42.04  ? 2004 HOH   A O   1 
HETATM 927 O  O   . HOH   E 5 .   ? -30.566 34.431 -19.918 1.00 43.39  ? 2005 HOH   A O   1 
HETATM 928 O  O   . HOH   E 5 .   ? -34.534 32.719 -26.906 1.00 43.25  ? 2006 HOH   A O   1 
HETATM 929 O  O   . HOH   E 5 .   ? -39.887 25.484 -16.386 1.00 58.01  ? 2007 HOH   A O   1 
HETATM 930 O  O   . HOH   E 5 .   ? -22.719 32.464 -15.476 1.00 39.90  ? 2008 HOH   A O   1 
HETATM 931 O  O   . HOH   E 5 .   ? -35.348 33.832 -20.789 1.00 52.80  ? 2009 HOH   A O   1 
HETATM 932 O  O   . HOH   E 5 .   ? -19.928 29.668 -17.488 1.00 69.20  ? 2010 HOH   A O   1 
HETATM 933 O  O   . HOH   E 5 .   ? -28.612 27.081 -27.084 1.00 55.48  ? 2011 HOH   A O   1 
HETATM 934 O  O   . HOH   E 5 .   ? -27.133 39.261 -14.578 1.00 35.03  ? 2012 HOH   A O   1 
HETATM 935 O  O   . HOH   E 5 .   ? -33.787 29.786 -24.407 1.00 49.96  ? 2013 HOH   A O   1 
HETATM 936 O  O   . HOH   E 5 .   ? -31.491 33.177 -3.104  1.00 51.57  ? 2014 HOH   A O   1 
HETATM 937 O  O   . HOH   E 5 .   ? -30.478 36.683 -21.836 1.00 40.92  ? 2015 HOH   A O   1 
HETATM 938 O  O   . HOH   E 5 .   ? -35.265 39.057 -34.284 1.00 50.21  ? 2016 HOH   A O   1 
HETATM 939 O  O   . HOH   E 5 .   ? -30.089 46.078 -20.009 1.00 36.00  ? 2017 HOH   A O   1 
HETATM 940 O  O   . HOH   E 5 .   ? -33.561 39.858 -31.849 1.00 53.43  ? 2018 HOH   A O   1 
HETATM 941 O  O   . HOH   E 5 .   ? -22.891 34.091 -23.239 1.00 59.56  ? 2019 HOH   A O   1 
HETATM 942 O  O   . HOH   E 5 .   ? -25.713 36.516 -13.631 1.00 41.19  ? 2020 HOH   A O   1 
HETATM 943 O  O   . HOH   E 5 .   ? -20.997 40.157 -19.912 1.00 58.77  ? 2021 HOH   A O   1 
HETATM 944 O  O   . HOH   E 5 .   ? -28.742 34.520 -4.273  1.00 46.71  ? 2022 HOH   A O   1 
HETATM 945 O  O   . HOH   E 5 .   ? -20.142 35.895 -18.151 1.00 60.89  ? 2023 HOH   A O   1 
HETATM 946 O  O   . HOH   E 5 .   ? -36.595 42.326 -32.777 1.00 66.18  ? 2024 HOH   A O   1 
HETATM 947 O  O   . HOH   E 5 .   ? -20.215 35.184 -7.712  1.00 33.82  ? 2025 HOH   A O   1 
HETATM 948 O  O   . HOH   E 5 .   ? -21.348 37.145 -19.791 1.00 51.06  ? 2026 HOH   A O   1 
HETATM 949 O  O   . HOH   E 5 .   ? -33.804 32.314 -24.505 1.00 50.03  ? 2027 HOH   A O   1 
HETATM 950 O  O   . HOH   E 5 .   ? -32.289 44.887 -19.891 1.00 51.70  ? 2028 HOH   A O   1 
HETATM 951 O  O   . HOH   E 5 .   ? -21.746 37.666 -27.658 0.50 54.05  ? 2029 HOH   A O   1 
HETATM 952 O  O   . HOH   E 5 .   ? -23.524 43.583 -17.965 1.00 53.44  ? 2030 HOH   A O   1 
HETATM 953 O  O   . HOH   E 5 .   ? -34.626 47.645 -16.295 1.00 46.39  ? 2031 HOH   A O   1 
HETATM 954 O  O   . HOH   E 5 .   ? -18.596 32.849 -16.706 1.00 68.87  ? 2032 HOH   A O   1 
HETATM 955 O  O   . HOH   E 5 .   ? -26.213 41.462 -15.799 1.00 38.30  ? 2033 HOH   A O   1 
HETATM 956 O  O   . HOH   E 5 .   ? -34.470 44.667 -17.660 1.00 51.20  ? 2034 HOH   A O   1 
HETATM 957 O  O   . HOH   E 5 .   ? -31.136 40.798 -33.508 1.00 44.17  ? 2035 HOH   A O   1 
HETATM 958 O  O   . HOH   E 5 .   ? -28.585 27.264 -29.992 1.00 62.73  ? 2036 HOH   A O   1 
HETATM 959 O  O   . HOH   E 5 .   ? -28.237 37.457 -3.371  1.00 27.10  ? 2037 HOH   A O   1 
HETATM 960 O  O   . HOH   E 5 .   ? -16.051 29.374 -6.624  1.00 76.20  ? 2038 HOH   A O   1 
HETATM 961 O  O   . HOH   E 5 .   ? -18.508 30.647 -3.968  1.00 66.49  ? 2039 HOH   A O   1 
HETATM 962 O  O   . HOH   E 5 .   ? -17.219 33.158 -7.947  1.00 65.30  ? 2040 HOH   A O   1 
HETATM 963 O  O   . HOH   E 5 .   ? -33.615 33.781 -29.172 1.00 53.53  ? 2041 HOH   A O   1 
HETATM 964 O  O   . HOH   E 5 .   ? -34.927 29.986 -28.073 1.00 52.57  ? 2042 HOH   A 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   . HIS A 3   ? 1.8005 1.2534 1.6541 -0.1120 -0.0217 0.2909  1796 HIS A N   
2   C CA  . HIS A 3   ? 1.7570 1.2556 1.6431 -0.0788 -0.0277 0.2929  1796 HIS A CA  
3   C C   . HIS A 3   ? 1.7063 1.2543 1.5914 -0.0934 -0.0295 0.3034  1796 HIS A C   
4   O O   . HIS A 3   ? 1.6623 1.2483 1.5469 -0.1212 -0.0185 0.2933  1796 HIS A O   
5   C CB  . HIS A 3   ? 1.7234 1.2653 1.6476 -0.0609 -0.0183 0.2670  1796 HIS A CB  
6   C CG  . HIS A 3   ? 1.7251 1.2696 1.6760 -0.0185 -0.0240 0.2673  1796 HIS A CG  
7   N ND1 . HIS A 3   ? 1.7460 1.2826 1.6995 0.0035  -0.0378 0.2886  1796 HIS A ND1 
8   C CD2 . HIS A 3   ? 1.6956 1.2516 1.6721 0.0054  -0.0173 0.2487  1796 HIS A CD2 
9   C CE1 . HIS A 3   ? 1.7264 1.2736 1.7104 0.0394  -0.0385 0.2826  1796 HIS A CE1 
10  N NE2 . HIS A 3   ? 1.7014 1.2594 1.6982 0.0408  -0.0251 0.2584  1796 HIS A NE2 
11  N N   . SER A 4   ? 1.7196 1.2669 1.6041 -0.0742 -0.0438 0.3233  1797 SER A N   
12  C CA  . SER A 4   ? 1.6961 1.2891 1.5781 -0.0854 -0.0469 0.3323  1797 SER A CA  
13  C C   . SER A 4   ? 1.6350 1.2988 1.5585 -0.0701 -0.0418 0.3152  1797 SER A C   
14  O O   . SER A 4   ? 1.6115 1.3202 1.5348 -0.0856 -0.0380 0.3127  1797 SER A O   
15  C CB  . SER A 4   ? 1.7230 1.2872 1.5859 -0.0726 -0.0669 0.3610  1797 SER A CB  
16  O OG  . SER A 4   ? 1.7199 1.2644 1.6058 -0.0336 -0.0781 0.3651  1797 SER A OG  
17  N N   . ASP A 5   ? 1.6030 1.2748 1.5594 -0.0406 -0.0410 0.3029  1798 ASP A N   
18  C CA  . ASP A 5   ? 1.5155 1.2492 1.5085 -0.0277 -0.0354 0.2862  1798 ASP A CA  
19  C C   . ASP A 5   ? 1.4155 1.1782 1.4130 -0.0496 -0.0196 0.2634  1798 ASP A C   
20  O O   . ASP A 5   ? 1.3725 1.1853 1.3806 -0.0580 -0.0154 0.2556  1798 ASP A O   
21  C CB  . ASP A 5   ? 1.5369 1.2682 1.5606 0.0082  -0.0372 0.2801  1798 ASP A CB  
22  C CG  . ASP A 5   ? 1.5909 1.3142 1.6232 0.0339  -0.0537 0.3010  1798 ASP A CG  
23  O OD1 . ASP A 5   ? 1.5504 1.3143 1.6163 0.0560  -0.0564 0.2982  1798 ASP A OD1 
24  O OD2 . ASP A 5   ? 1.6696 1.3467 1.6751 0.0311  -0.0650 0.3209  1798 ASP A OD2 
25  N N   . LEU A 6   ? 1.3277 1.0584 1.3170 -0.0587 -0.0119 0.2523  1799 LEU A N   
26  C CA  . LEU A 6   ? 1.1573 0.9151 1.1516 -0.0807 0.0008  0.2317  1799 LEU A CA  
27  C C   . LEU A 6   ? 1.0680 0.8451 1.0442 -0.1133 0.0053  0.2363  1799 LEU A C   
28  O O   . LEU A 6   ? 1.0136 0.8358 1.0031 -0.1265 0.0145  0.2204  1799 LEU A O   
29  C CB  . LEU A 6   ? 1.1582 0.8725 1.1429 -0.0871 0.0056  0.2210  1799 LEU A CB  
30  C CG  . LEU A 6   ? 1.1188 0.8210 1.1218 -0.0571 0.0059  0.2091  1799 LEU A CG  
31  C CD1 . LEU A 6   ? 1.1871 0.8274 1.1695 -0.0619 0.0075  0.2041  1799 LEU A CD1 
32  C CD2 . LEU A 6   ? 0.9810 0.7365 1.0108 -0.0530 0.0129  0.1876  1799 LEU A CD2 
33  N N   . THR A 7   ? 1.0342 0.7776 0.9792 -0.1258 -0.0007 0.2579  1800 THR A N   
34  C CA  . THR A 7   ? 1.0042 0.7638 0.9274 -0.1579 0.0054  0.2635  1800 THR A CA  
35  C C   . THR A 7   ? 0.9612 0.7807 0.8997 -0.1543 0.0072  0.2585  1800 THR A C   
36  O O   . THR A 7   ? 0.8872 0.7462 0.8304 -0.1739 0.0191  0.2453  1800 THR A O   
37  C CB  . THR A 7   ? 1.0625 0.7694 0.9447 -0.1689 -0.0037 0.2904  1800 THR A CB  
38  O OG1 . THR A 7   ? 1.1269 0.7751 0.9892 -0.1799 -0.0030 0.2934  1800 THR A OG1 
39  C CG2 . THR A 7   ? 0.9989 0.7262 0.8555 -0.2002 0.0030  0.2978  1800 THR A CG2 
40  N N   . PHE A 8   ? 0.9258 0.7532 0.8732 -0.1293 -0.0049 0.2684  1801 PHE A N   
41  C CA  . PHE A 8   ? 0.8802 0.7587 0.8381 -0.1271 -0.0047 0.2641  1801 PHE A CA  
42  C C   . PHE A 8   ? 0.8623 0.7862 0.8553 -0.1171 0.0036  0.2393  1801 PHE A C   
43  O O   . PHE A 8   ? 0.8397 0.8055 0.8383 -0.1242 0.0094  0.2294  1801 PHE A O   
44  C CB  . PHE A 8   ? 0.9930 0.8686 0.9516 -0.1055 -0.0216 0.2817  1801 PHE A CB  
45  C CG  . PHE A 8   ? 1.0807 1.0000 1.0399 -0.1085 -0.0233 0.2802  1801 PHE A CG  
46  C CD1 . PHE A 8   ? 1.1065 1.0271 1.0317 -0.1334 -0.0209 0.2885  1801 PHE A CD1 
47  C CD2 . PHE A 8   ? 1.0791 1.0360 1.0696 -0.0882 -0.0262 0.2697  1801 PHE A CD2 
48  C CE1 . PHE A 8   ? 1.0752 1.0321 0.9969 -0.1365 -0.0220 0.2855  1801 PHE A CE1 
49  C CE2 . PHE A 8   ? 1.0783 1.0704 1.0660 -0.0923 -0.0282 0.2676  1801 PHE A CE2 
50  C CZ  . PHE A 8   ? 1.0630 1.0543 1.0159 -0.1159 -0.0263 0.2749  1801 PHE A CZ  
51  N N   . CYS A 9   ? 0.8640 0.7776 0.8780 -0.1002 0.0042  0.2289  1802 CYS A N   
52  C CA  . CYS A 9   ? 0.8029 0.7544 0.8453 -0.0924 0.0112  0.2062  1802 CYS A CA  
53  C C   . CYS A 9   ? 0.7314 0.7071 0.7727 -0.1175 0.0233  0.1910  1802 CYS A C   
54  O O   . CYS A 9   ? 0.5985 0.6177 0.6552 -0.1174 0.0279  0.1773  1802 CYS A O   
55  C CB  . CYS A 9   ? 0.8041 0.7333 0.8613 -0.0736 0.0107  0.1982  1802 CYS A CB  
56  S SG  . CYS A 9   ? 0.8934 0.8075 0.9631 -0.0397 -0.0006 0.2116  1802 CYS A SG  
57  N N   . GLU A 10  ? 0.7390 0.6870 0.7628 -0.1395 0.0284  0.1936  1803 GLU A N   
58  C CA  . GLU A 10  ? 0.7516 0.7263 0.7770 -0.1660 0.0404  0.1804  1803 GLU A CA  
59  C C   . GLU A 10  ? 0.7113 0.7200 0.7278 -0.1789 0.0460  0.1832  1803 GLU A C   
60  O O   . GLU A 10  ? 0.6763 0.7286 0.7081 -0.1875 0.0555  0.1667  1803 GLU A O   
61  C CB  . GLU A 10  ? 0.8294 0.7634 0.8343 -0.1900 0.0440  0.1859  1803 GLU A CB  
62  C CG  . GLU A 10  ? 0.9687 0.9304 0.9763 -0.2213 0.0570  0.1742  1803 GLU A CG  
63  C CD  . GLU A 10  ? 1.0008 1.0130 1.0438 -0.2153 0.0614  0.1495  1803 GLU A CD  
64  O OE1 . GLU A 10  ? 1.0164 1.0771 1.0719 -0.2181 0.0681  0.1410  1803 GLU A OE1 
65  O OE2 . GLU A 10  ? 0.9488 0.9497 1.0049 -0.2073 0.0574  0.1385  1803 GLU A OE2 
66  N N   . ILE A 11  ? 0.7232 0.7123 0.7145 -0.1789 0.0395  0.2034  1804 ILE A N   
67  C CA  . ILE A 11  ? 0.7101 0.7271 0.6868 -0.1911 0.0444  0.2060  1804 ILE A CA  
68  C C   . ILE A 11  ? 0.6527 0.7131 0.6531 -0.1719 0.0430  0.1924  1804 ILE A C   
69  O O   . ILE A 11  ? 0.6173 0.7162 0.6233 -0.1807 0.0534  0.1784  1804 ILE A O   
70  C CB  . ILE A 11  ? 0.7789 0.7607 0.7194 -0.1950 0.0345  0.2322  1804 ILE A CB  
71  C CG1 . ILE A 11  ? 0.7984 0.7338 0.7094 -0.2180 0.0368  0.2462  1804 ILE A CG1 
72  C CG2 . ILE A 11  ? 0.7141 0.7241 0.6367 -0.2049 0.0380  0.2338  1804 ILE A CG2 
73  C CD1 . ILE A 11  ? 0.7995 0.6931 0.6721 -0.2207 0.0243  0.2737  1804 ILE A CD1 
74  N N   . ILE A 12  ? 0.6357 0.6897 0.6501 -0.1455 0.0306  0.1960  1805 ILE A N   
75  C CA  . ILE A 12  ? 0.6439 0.7329 0.6758 -0.1292 0.0277  0.1859  1805 ILE A CA  
76  C C   . ILE A 12  ? 0.6311 0.7499 0.6916 -0.1238 0.0353  0.1620  1805 ILE A C   
77  O O   . ILE A 12  ? 0.6571 0.8093 0.7269 -0.1200 0.0382  0.1493  1805 ILE A O   
78  C CB  . ILE A 12  ? 0.6986 0.7742 0.7376 -0.1053 0.0127  0.1982  1805 ILE A CB  
79  C CG1 . ILE A 12  ? 0.7322 0.8405 0.7814 -0.0943 0.0086  0.1916  1805 ILE A CG1 
80  C CG2 . ILE A 12  ? 0.6755 0.7342 0.7359 -0.0881 0.0106  0.1938  1805 ILE A CG2 
81  C CD1 . ILE A 12  ? 0.7983 0.8991 0.8534 -0.0759 -0.0064 0.2060  1805 ILE A CD1 
82  N N   . LEU A 13  ? 0.5986 0.7038 0.6713 -0.1233 0.0374  0.1553  1806 LEU A N   
83  C CA  . LEU A 13  ? 0.5956 0.7288 0.6927 -0.1205 0.0428  0.1333  1806 LEU A CA  
84  C C   . LEU A 13  ? 0.6150 0.7805 0.7135 -0.1409 0.0548  0.1218  1806 LEU A C   
85  O O   . LEU A 13  ? 0.5590 0.7601 0.6764 -0.1350 0.0579  0.1047  1806 LEU A O   
86  C CB  . LEU A 13  ? 0.6335 0.7425 0.7387 -0.1186 0.0416  0.1286  1806 LEU A CB  
87  C CG  . LEU A 13  ? 0.6509 0.7860 0.7794 -0.1162 0.0442  0.1068  1806 LEU A CG  
88  C CD1 . LEU A 13  ? 0.5699 0.7300 0.7132 -0.0951 0.0396  0.0981  1806 LEU A CD1 
89  C CD2 . LEU A 13  ? 0.6371 0.7427 0.7676 -0.1148 0.0416  0.1028  1806 LEU A CD2 
90  N N   . MET A 14  ? 0.6040 0.7573 0.6824 -0.1647 0.0619  0.1310  1807 MET A N   
91  C CA  . MET A 14  ? 0.6143 0.8018 0.6946 -0.1858 0.0761  0.1204  1807 MET A CA  
92  C C   . MET A 14  ? 0.6198 0.8382 0.6976 -0.1793 0.0794  0.1148  1807 MET A C   
93  O O   . MET A 14  ? 0.6057 0.8643 0.7022 -0.1799 0.0882  0.0963  1807 MET A O   
94  C CB  . MET A 14  ? 0.7163 0.8797 0.7687 -0.2143 0.0835  0.1347  1807 MET A CB  
95  C CG  . MET A 14  ? 0.7926 0.9924 0.8477 -0.2401 0.1013  0.1241  1807 MET A CG  
96  S SD  . MET A 14  ? 0.9893 1.1732 0.9981 -0.2657 0.1106  0.1430  1807 MET A SD  
97  C CE  . MET A 14  ? 0.8885 1.0972 0.8920 -0.2458 0.1081  0.1388  1807 MET A CE  
98  N N   . GLU A 15  ? 0.6172 0.8167 0.6722 -0.1723 0.0715  0.1302  1808 GLU A N   
99  C CA  . GLU A 15  ? 0.6056 0.8280 0.6518 -0.1682 0.0735  0.1256  1808 GLU A CA  
100 C C   . GLU A 15  ? 0.5193 0.7644 0.5912 -0.1447 0.0681  0.1096  1808 GLU A C   
101 O O   . GLU A 15  ? 0.5312 0.8043 0.6056 -0.1425 0.0742  0.0960  1808 GLU A O   
102 C CB  . GLU A 15  ? 0.6630 0.8573 0.6770 -0.1684 0.0634  0.1473  1808 GLU A CB  
103 C CG  . GLU A 15  ? 0.7823 0.9533 0.7623 -0.1937 0.0689  0.1638  1808 GLU A CG  
104 C CD  . GLU A 15  ? 0.9100 1.0463 0.8605 -0.1908 0.0536  0.1883  1808 GLU A CD  
105 O OE1 . GLU A 15  ? 0.9609 1.0879 0.9249 -0.1687 0.0384  0.1940  1808 GLU A OE1 
106 O OE2 . GLU A 15  ? 0.9819 1.1014 0.8958 -0.2109 0.0565  0.2021  1808 GLU A OE2 
107 N N   . MET A 16  ? 0.5105 0.7418 0.5992 -0.1271 0.0571  0.1108  1809 MET A N   
108 C CA  . MET A 16  ? 0.5029 0.7519 0.6123 -0.1068 0.0518  0.0968  1809 MET A CA  
109 C C   . MET A 16  ? 0.4707 0.7494 0.6043 -0.1073 0.0595  0.0754  1809 MET A C   
110 O O   . MET A 16  ? 0.4575 0.7598 0.6009 -0.0972 0.0602  0.0612  1809 MET A O   
111 C CB  . MET A 16  ? 0.5145 0.7410 0.6329 -0.0895 0.0399  0.1042  1809 MET A CB  
112 C CG  . MET A 16  ? 0.6118 0.8197 0.7152 -0.0829 0.0298  0.1225  1809 MET A CG  
113 S SD  . MET A 16  ? 0.6711 0.8637 0.7915 -0.0602 0.0190  0.1275  1809 MET A SD  
114 C CE  . MET A 16  ? 0.6937 0.8565 0.8157 -0.0641 0.0215  0.1331  1809 MET A CE  
115 N N   . GLU A 17  ? 0.4719 0.7490 0.6152 -0.1192 0.0642  0.0730  1810 GLU A N   
116 C CA  . GLU A 17  ? 0.5137 0.8229 0.6833 -0.1211 0.0697  0.0532  1810 GLU A CA  
117 C C   . GLU A 17  ? 0.4943 0.8409 0.6674 -0.1292 0.0824  0.0413  1810 GLU A C   
118 O O   . GLU A 17  ? 0.4838 0.8625 0.6812 -0.1202 0.0839  0.0229  1810 GLU A O   
119 C CB  . GLU A 17  ? 0.5532 0.8528 0.7289 -0.1378 0.0724  0.0543  1810 GLU A CB  
120 C CG  . GLU A 17  ? 0.6474 0.9160 0.8260 -0.1268 0.0611  0.0580  1810 GLU A CG  
121 C CD  . GLU A 17  ? 0.7074 0.9584 0.8849 -0.1458 0.0635  0.0601  1810 GLU A CD  
122 O OE1 . GLU A 17  ? 0.7241 0.9706 0.8882 -0.1682 0.0724  0.0682  1810 GLU A OE1 
123 O OE2 . GLU A 17  ? 0.7089 0.9484 0.8962 -0.1399 0.0566  0.0536  1810 GLU A OE2 
124 N N   . SER A 18  ? 0.4610 0.8030 0.6090 -0.1452 0.0915  0.0513  1811 SER A N   
125 C CA  . SER A 18  ? 0.5837 0.9595 0.7305 -0.1551 0.1070  0.0400  1811 SER A CA  
126 C C   . SER A 18  ? 0.5937 0.9726 0.7255 -0.1412 0.1054  0.0364  1811 SER A C   
127 O O   . SER A 18  ? 0.6012 1.0075 0.7311 -0.1456 0.1187  0.0241  1811 SER A O   
128 C CB  . SER A 18  ? 0.7164 1.0839 0.8384 -0.1841 0.1197  0.0524  1811 SER A CB  
129 O OG  . SER A 18  ? 0.8261 1.1489 0.9158 -0.1869 0.1100  0.0756  1811 SER A OG  
130 N N   . HIS A 19  ? 0.5072 0.8593 0.6284 -0.1255 0.0901  0.0461  1812 HIS A N   
131 C CA  . HIS A 19  ? 0.5418 0.8921 0.6457 -0.1151 0.0864  0.0441  1812 HIS A CA  
132 C C   . HIS A 19  ? 0.5405 0.9195 0.6655 -0.0992 0.0895  0.0206  1812 HIS A C   
133 O O   . HIS A 19  ? 0.5643 0.9570 0.7193 -0.0886 0.0862  0.0096  1812 HIS A O   
134 C CB  . HIS A 19  ? 0.4858 0.8057 0.5813 -0.1023 0.0686  0.0589  1812 HIS A CB  
135 C CG  . HIS A 19  ? 0.4389 0.7491 0.5078 -0.1001 0.0631  0.0643  1812 HIS A CG  
136 N ND1 . HIS A 19  ? 0.4582 0.7787 0.5272 -0.0878 0.0617  0.0497  1812 HIS A ND1 
137 C CD2 . HIS A 19  ? 0.4753 0.7643 0.5153 -0.1089 0.0569  0.0829  1812 HIS A CD2 
138 C CE1 . HIS A 19  ? 0.4642 0.7703 0.5047 -0.0910 0.0556  0.0583  1812 HIS A CE1 
139 N NE2 . HIS A 19  ? 0.4568 0.7457 0.4803 -0.1036 0.0519  0.0787  1812 HIS A NE2 
140 N N   . ASP A 20  ? 0.4833 0.8689 0.5903 -0.0972 0.0949  0.0130  1813 ASP A N   
141 C CA  . ASP A 20  ? 0.4997 0.9062 0.6226 -0.0793 0.0967  -0.0091 1813 ASP A CA  
142 C C   . ASP A 20  ? 0.5195 0.9113 0.6562 -0.0579 0.0788  -0.0103 1813 ASP A C   
143 O O   . ASP A 20  ? 0.5155 0.9242 0.6793 -0.0436 0.0766  -0.0253 1813 ASP A O   
144 C CB  . ASP A 20  ? 0.6287 1.0330 0.7215 -0.0802 0.1033  -0.0153 1813 ASP A CB  
145 C CG  . ASP A 20  ? 0.7302 1.1643 0.8204 -0.0934 0.1261  -0.0278 1813 ASP A CG  
146 O OD1 . ASP A 20  ? 0.7648 1.2317 0.8882 -0.0937 0.1361  -0.0399 1813 ASP A OD1 
147 O OD2 . ASP A 20  ? 0.7964 1.2223 0.8509 -0.1043 0.1341  -0.0257 1813 ASP A OD2 
148 N N   . ALA A 21  ? 0.4331 0.7946 0.5515 -0.0559 0.0657  0.0058  1814 ALA A N   
149 C CA  . ALA A 21  ? 0.4082 0.7542 0.5342 -0.0384 0.0504  0.0059  1814 ALA A CA  
150 C C   . ALA A 21  ? 0.3548 0.6947 0.5015 -0.0350 0.0435  0.0126  1814 ALA A C   
151 O O   . ALA A 21  ? 0.2911 0.6141 0.4391 -0.0240 0.0318  0.0172  1814 ALA A O   
152 C CB  . ALA A 21  ? 0.3320 0.6529 0.4315 -0.0392 0.0402  0.0194  1814 ALA A CB  
153 N N   . ALA A 22  ? 0.4228 0.7747 0.5835 -0.0454 0.0510  0.0127  1815 ALA A N   
154 C CA  . ALA A 22  ? 0.4005 0.7432 0.5769 -0.0434 0.0449  0.0175  1815 ALA A CA  
155 C C   . ALA A 22  ? 0.4128 0.7718 0.6143 -0.0310 0.0409  0.0009  1815 ALA A C   
156 O O   . ALA A 22  ? 0.4331 0.7837 0.6452 -0.0291 0.0350  0.0027  1815 ALA A O   
157 C CB  . ALA A 22  ? 0.3781 0.7200 0.5541 -0.0624 0.0530  0.0262  1815 ALA A CB  
158 N N   . TRP A 23  ? 0.3687 0.7487 0.5783 -0.0215 0.0429  -0.0154 1816 TRP A N   
159 C CA  . TRP A 23  ? 0.3882 0.7870 0.6239 -0.0093 0.0377  -0.0312 1816 TRP A CA  
160 C C   . TRP A 23  ? 0.4193 0.7956 0.6553 0.0045  0.0221  -0.0287 1816 TRP A C   
161 O O   . TRP A 23  ? 0.4638 0.8511 0.7193 0.0087  0.0164  -0.0369 1816 TRP A O   
162 C CB  . TRP A 23  ? 0.3337 0.7552 0.5765 0.0025  0.0417  -0.0488 1816 TRP A CB  
163 C CG  . TRP A 23  ? 0.4051 0.8035 0.6243 0.0142  0.0358  -0.0479 1816 TRP A CG  
164 C CD1 . TRP A 23  ? 0.4586 0.8470 0.6521 0.0071  0.0422  -0.0428 1816 TRP A CD1 
165 C CD2 . TRP A 23  ? 0.4403 0.8202 0.6564 0.0331  0.0213  -0.0521 1816 TRP A CD2 
166 N NE1 . TRP A 23  ? 0.4595 0.8251 0.6356 0.0198  0.0325  -0.0441 1816 TRP A NE1 
167 C CE2 . TRP A 23  ? 0.4506 0.8096 0.6398 0.0356  0.0201  -0.0494 1816 TRP A CE2 
168 C CE3 . TRP A 23  ? 0.4608 0.8373 0.6910 0.0468  0.0084  -0.0573 1816 TRP A CE3 
169 C CZ2 . TRP A 23  ? 0.4813 0.8155 0.6582 0.0502  0.0073  -0.0516 1816 TRP A CZ2 
170 C CZ3 . TRP A 23  ? 0.4820 0.8331 0.6981 0.0621  -0.0043 -0.0587 1816 TRP A CZ3 
171 C CH2 . TRP A 23  ? 0.5030 0.8329 0.6932 0.0633  -0.0042 -0.0558 1816 TRP A CH2 
172 N N   . PRO A 24  ? 0.3874 0.7346 0.6032 0.0108  0.0147  -0.0183 1817 PRO A N   
173 C CA  . PRO A 24  ? 0.3763 0.7036 0.5914 0.0216  0.0024  -0.0162 1817 PRO A CA  
174 C C   . PRO A 24  ? 0.3516 0.6657 0.5679 0.0136  0.0022  -0.0062 1817 PRO A C   
175 O O   . PRO A 24  ? 0.4084 0.7088 0.6244 0.0211  -0.0062 -0.0071 1817 PRO A O   
176 C CB  . PRO A 24  ? 0.3765 0.6805 0.5699 0.0277  -0.0029 -0.0083 1817 PRO A CB  
177 C CG  . PRO A 24  ? 0.3410 0.6545 0.5253 0.0235  0.0041  -0.0109 1817 PRO A CG  
178 C CD  . PRO A 24  ? 0.3256 0.6586 0.5184 0.0088  0.0161  -0.0098 1817 PRO A CD  
179 N N   . PHE A 25  ? 0.3371 0.6516 0.5517 -0.0012 0.0110  0.0029  1818 PHE A N   
180 C CA  . PHE A 25  ? 0.3620 0.6551 0.5722 -0.0069 0.0109  0.0144  1818 PHE A CA  
181 C C   . PHE A 25  ? 0.3948 0.6956 0.6160 -0.0204 0.0160  0.0114  1818 PHE A C   
182 O O   . PHE A 25  ? 0.4761 0.7555 0.6912 -0.0265 0.0171  0.0206  1818 PHE A O   
183 C CB  . PHE A 25  ? 0.3284 0.6055 0.5229 -0.0114 0.0139  0.0314  1818 PHE A CB  
184 C CG  . PHE A 25  ? 0.3262 0.5996 0.5104 -0.0025 0.0090  0.0343  1818 PHE A CG  
185 C CD1 . PHE A 25  ? 0.3180 0.5785 0.4998 0.0093  0.0014  0.0342  1818 PHE A CD1 
186 C CD2 . PHE A 25  ? 0.3690 0.6502 0.5428 -0.0079 0.0122  0.0366  1818 PHE A CD2 
187 C CE1 . PHE A 25  ? 0.3569 0.6127 0.5283 0.0146  -0.0033 0.0370  1818 PHE A CE1 
188 C CE2 . PHE A 25  ? 0.3570 0.6324 0.5192 -0.0017 0.0065  0.0385  1818 PHE A CE2 
189 C CZ  . PHE A 25  ? 0.3917 0.6545 0.5537 0.0090  -0.0014 0.0389  1818 PHE A CZ  
190 N N   . LEU A 26  ? 0.3919 0.7226 0.6299 -0.0253 0.0192  -0.0019 1819 LEU A N   
191 C CA  . LEU A 26  ? 0.4453 0.7871 0.6951 -0.0421 0.0246  -0.0048 1819 LEU A CA  
192 C C   . LEU A 26  ? 0.5139 0.8483 0.7721 -0.0402 0.0154  -0.0114 1819 LEU A C   
193 O O   . LEU A 26  ? 0.6039 0.9341 0.8652 -0.0557 0.0180  -0.0105 1819 LEU A O   
194 C CB  . LEU A 26  ? 0.4458 0.8287 0.7143 -0.0492 0.0328  -0.0172 1819 LEU A CB  
195 C CG  . LEU A 26  ? 0.4544 0.8420 0.7089 -0.0566 0.0447  -0.0106 1819 LEU A CG  
196 C CD1 . LEU A 26  ? 0.3574 0.7877 0.6300 -0.0615 0.0555  -0.0252 1819 LEU A CD1 
197 C CD2 . LEU A 26  ? 0.4217 0.7855 0.6580 -0.0751 0.0509  0.0062  1819 LEU A CD2 
198 N N   . GLU A 27  ? 0.4889 0.8184 0.7474 -0.0231 0.0041  -0.0176 1820 GLU A N   
199 C CA  . GLU A 27  ? 0.5119 0.8313 0.7727 -0.0210 -0.0061 -0.0238 1820 GLU A CA  
200 C C   . GLU A 27  ? 0.4753 0.7671 0.7179 -0.0043 -0.0142 -0.0200 1820 GLU A C   
201 O O   . GLU A 27  ? 0.4555 0.7451 0.6908 0.0062  -0.0140 -0.0160 1820 GLU A O   
202 C CB  . GLU A 27  ? 0.5351 0.8900 0.8214 -0.0202 -0.0133 -0.0402 1820 GLU A CB  
203 C CG  . GLU A 27  ? 0.6199 0.9913 0.9136 -0.0007 -0.0210 -0.0488 1820 GLU A CG  
204 C CD  . GLU A 27  ? 0.7620 1.1778 1.0882 0.0002  -0.0251 -0.0647 1820 GLU A CD  
205 O OE1 . GLU A 27  ? 0.7997 1.2460 1.1416 -0.0027 -0.0142 -0.0694 1820 GLU A OE1 
206 O OE2 . GLU A 27  ? 0.8026 1.2241 1.1389 0.0038  -0.0391 -0.0728 1820 GLU A OE2 
207 N N   . PRO A 28  ? 0.3957 0.6648 0.6284 -0.0033 -0.0206 -0.0210 1821 PRO A N   
208 C CA  . PRO A 28  ? 0.3887 0.6316 0.6018 0.0105  -0.0260 -0.0172 1821 PRO A CA  
209 C C   . PRO A 28  ? 0.4212 0.6748 0.6357 0.0246  -0.0368 -0.0246 1821 PRO A C   
210 O O   . PRO A 28  ? 0.4698 0.7471 0.7007 0.0263  -0.0450 -0.0361 1821 PRO A O   
211 C CB  . PRO A 28  ? 0.4407 0.6607 0.6428 0.0064  -0.0301 -0.0205 1821 PRO A CB  
212 C CG  . PRO A 28  ? 0.4751 0.6981 0.6860 -0.0109 -0.0234 -0.0201 1821 PRO A CG  
213 C CD  . PRO A 28  ? 0.4407 0.7025 0.6752 -0.0172 -0.0212 -0.0245 1821 PRO A CD  
214 N N   . VAL A 29  ? 0.4345 0.6702 0.6322 0.0346  -0.0374 -0.0177 1822 VAL A N   
215 C CA  . VAL A 29  ? 0.4875 0.7214 0.6786 0.0478  -0.0490 -0.0231 1822 VAL A CA  
216 C C   . VAL A 29  ? 0.5299 0.7535 0.7134 0.0510  -0.0617 -0.0306 1822 VAL A C   
217 O O   . VAL A 29  ? 0.5081 0.7103 0.6771 0.0461  -0.0599 -0.0280 1822 VAL A O   
218 C CB  . VAL A 29  ? 0.5418 0.7542 0.7131 0.0536  -0.0463 -0.0127 1822 VAL A CB  
219 C CG1 . VAL A 29  ? 0.4709 0.6715 0.6281 0.0655  -0.0594 -0.0169 1822 VAL A CG1 
220 C CG2 . VAL A 29  ? 0.5832 0.8073 0.7609 0.0504  -0.0374 -0.0062 1822 VAL A CG2 
221 N N   . ASN A 30  ? 0.5410 0.7788 0.7331 0.0600  -0.0754 -0.0407 1823 ASN A N   
222 C CA  . ASN A 30  ? 0.5316 0.7587 0.7136 0.0644  -0.0915 -0.0472 1823 ASN A CA  
223 C C   . ASN A 30  ? 0.4812 0.6763 0.6323 0.0749  -0.0984 -0.0416 1823 ASN A C   
224 O O   . ASN A 30  ? 0.4810 0.6779 0.6320 0.0863  -0.1057 -0.0431 1823 ASN A O   
225 C CB  . ASN A 30  ? 0.5491 0.8088 0.7579 0.0702  -0.1050 -0.0600 1823 ASN A CB  
226 C CG  . ASN A 30  ? 0.6255 0.8772 0.8258 0.0729  -0.1245 -0.0666 1823 ASN A CG  
227 O OD1 . ASN A 30  ? 0.6275 0.8438 0.7947 0.0739  -0.1295 -0.0618 1823 ASN A OD1 
228 N ND2 . ASN A 30  ? 0.6742 0.9604 0.9044 0.0736  -0.1357 -0.0779 1823 ASN A ND2 
229 N N   . PRO A 31  ? 0.5838 0.7619 0.5100 0.0282  -0.0636 -0.0280 1824 PRO A N   
230 C CA  . PRO A 31  ? 0.6433 0.7876 0.5452 0.0324  -0.0638 -0.0231 1824 PRO A CA  
231 C C   . PRO A 31  ? 0.6788 0.8269 0.5644 0.0443  -0.0783 -0.0152 1824 PRO A C   
232 O O   . PRO A 31  ? 0.7295 0.8506 0.5984 0.0541  -0.0805 -0.0089 1824 PRO A O   
233 C CB  . PRO A 31  ? 0.6661 0.7931 0.5552 0.0123  -0.0546 -0.0286 1824 PRO A CB  
234 C CG  . PRO A 31  ? 0.5991 0.7535 0.4996 -0.0006 -0.0548 -0.0349 1824 PRO A CG  
235 C CD  . PRO A 31  ? 0.5399 0.7208 0.4666 0.0076  -0.0567 -0.0350 1824 PRO A CD  
236 N N   . ARG A 32  ? 0.6349 0.8158 0.5247 0.0437  -0.0886 -0.0150 1825 ARG A N   
237 C CA  . ARG A 32  ? 0.7135 0.9026 0.5918 0.0579  -0.1046 -0.0060 1825 ARG A CA  
238 C C   . ARG A 32  ? 0.7265 0.9131 0.6159 0.0827  -0.1092 -0.0011 1825 ARG A C   
239 O O   . ARG A 32  ? 0.7371 0.9106 0.6120 0.0974  -0.1197 0.0081  1825 ARG A O   
240 C CB  . ARG A 32  ? 0.6678 0.9010 0.5548 0.0534  -0.1149 -0.0076 1825 ARG A CB  
241 C CG  . ARG A 32  ? 0.6945 0.9309 0.5653 0.0290  -0.1128 -0.0120 1825 ARG A CG  
242 C CD  . ARG A 32  ? 0.6828 0.9674 0.5676 0.0231  -0.1209 -0.0158 1825 ARG A CD  
243 N NE  . ARG A 32  ? 0.7115 1.0028 0.5799 -0.0010 -0.1199 -0.0208 1825 ARG A NE  
244 C CZ  . ARG A 32  ? 0.7502 1.0814 0.6268 -0.0123 -0.1249 -0.0259 1825 ARG A CZ  
245 N NH1 . ARG A 32  ? 0.6815 1.0507 0.5834 -0.0013 -0.1312 -0.0263 1825 ARG A NH1 
246 N NH2 . ARG A 32  ? 0.7576 1.0920 0.6168 -0.0358 -0.1228 -0.0316 1825 ARG A NH2 
247 N N   . LEU A 33  ? 0.6944 0.8921 0.6082 0.0871  -0.1013 -0.0072 1826 LEU A N   
248 C CA  . LEU A 33  ? 0.6936 0.8939 0.6209 0.1091  -0.1040 -0.0056 1826 LEU A CA  
249 C C   . LEU A 33  ? 0.7114 0.8720 0.6306 0.1129  -0.0939 -0.0051 1826 LEU A C   
250 O O   . LEU A 33  ? 0.6680 0.8240 0.5942 0.1307  -0.0951 -0.0043 1826 LEU A O   
251 C CB  . LEU A 33  ? 0.7126 0.9549 0.6713 0.1104  -0.1019 -0.0134 1826 LEU A CB  
252 C CG  . LEU A 33  ? 0.7326 1.0204 0.7022 0.1063  -0.1116 -0.0152 1826 LEU A CG  
253 C CD1 . LEU A 33  ? 0.6674 0.9929 0.6647 0.1007  -0.1062 -0.0240 1826 LEU A CD1 
254 C CD2 . LEU A 33  ? 0.7685 1.0709 0.7377 0.1277  -0.1274 -0.0085 1826 LEU A CD2 
255 N N   . VAL A 34  ? 0.7489 0.8819 0.6543 0.0966  -0.0836 -0.0064 1827 VAL A N   
256 C CA  . VAL A 34  ? 0.7187 0.8184 0.6176 0.0968  -0.0731 -0.0070 1827 VAL A CA  
257 C C   . VAL A 34  ? 0.6947 0.7573 0.5630 0.0876  -0.0713 -0.0026 1827 VAL A C   
258 O O   . VAL A 34  ? 0.6942 0.7542 0.5563 0.0698  -0.0656 -0.0059 1827 VAL A O   
259 C CB  . VAL A 34  ? 0.6423 0.7501 0.5600 0.0847  -0.0605 -0.0141 1827 VAL A CB  
260 C CG1 . VAL A 34  ? 0.5889 0.6675 0.5010 0.0859  -0.0511 -0.0143 1827 VAL A CG1 
261 C CG2 . VAL A 34  ? 0.6252 0.7723 0.5707 0.0893  -0.0623 -0.0184 1827 VAL A CG2 
262 N N   . SER A 35  ? 0.7194 0.7524 0.5684 0.0989  -0.0750 0.0039  1828 SER A N   
263 C CA  . SER A 35  ? 0.8261 0.8237 0.6427 0.0892  -0.0741 0.0088  1828 SER A CA  
264 C C   . SER A 35  ? 0.7926 0.7716 0.6062 0.0728  -0.0584 0.0025  1828 SER A C   
265 O O   . SER A 35  ? 0.7869 0.7586 0.6107 0.0762  -0.0503 -0.0007 1828 SER A O   
266 C CB  . SER A 35  ? 0.9409 0.9077 0.7369 0.1050  -0.0815 0.0179  1828 SER A CB  
267 O OG  . SER A 35  ? 1.0247 0.9577 0.7861 0.0937  -0.0815 0.0238  1828 SER A OG  
268 N N   . GLY A 36  ? 0.7659 0.7392 0.5660 0.0548  -0.0541 0.0002  1829 GLY A N   
269 C CA  . GLY A 36  ? 0.7138 0.6704 0.5107 0.0396  -0.0397 -0.0060 1829 GLY A CA  
270 C C   . GLY A 36  ? 0.7067 0.6858 0.5324 0.0314  -0.0303 -0.0148 1829 GLY A C   
271 O O   . GLY A 36  ? 0.6651 0.6341 0.4916 0.0191  -0.0187 -0.0203 1829 GLY A O   
272 N N   . TYR A 37  ? 0.7038 0.7133 0.5534 0.0376  -0.0351 -0.0160 1830 TYR A N   
273 C CA  . TYR A 37  ? 0.6659 0.6936 0.5420 0.0302  -0.0268 -0.0225 1830 TYR A CA  
274 C C   . TYR A 37  ? 0.6289 0.6552 0.5025 0.0129  -0.0200 -0.0288 1830 TYR A C   
275 O O   . TYR A 37  ? 0.6236 0.6453 0.5092 0.0047  -0.0091 -0.0340 1830 TYR A O   
276 C CB  . TYR A 37  ? 0.5840 0.6444 0.4824 0.0378  -0.0336 -0.0225 1830 TYR A CB  
277 C CG  . TYR A 37  ? 0.5887 0.6634 0.5129 0.0320  -0.0257 -0.0267 1830 TYR A CG  
278 C CD1 . TYR A 37  ? 0.6252 0.6985 0.5610 0.0379  -0.0215 -0.0257 1830 TYR A CD1 
279 C CD2 . TYR A 37  ? 0.5749 0.6625 0.5103 0.0197  -0.0226 -0.0313 1830 TYR A CD2 
280 C CE1 . TYR A 37  ? 0.6277 0.7139 0.5856 0.0319  -0.0156 -0.0276 1830 TYR A CE1 
281 C CE2 . TYR A 37  ? 0.5990 0.6961 0.5568 0.0145  -0.0163 -0.0333 1830 TYR A CE2 
282 C CZ  . TYR A 37  ? 0.6794 0.7764 0.6483 0.0208  -0.0135 -0.0306 1830 TYR A CZ  
283 O OH  . TYR A 37  ? 0.6977 0.8043 0.6873 0.0151  -0.0087 -0.0306 1830 TYR A OH  
284 N N   . ARG A 38  ? 0.5993 0.6311 0.4586 0.0073  -0.0263 -0.0289 1831 ARG A N   
285 C CA  . ARG A 38  ? 0.6415 0.6713 0.4955 -0.0104 -0.0192 -0.0366 1831 ARG A CA  
286 C C   . ARG A 38  ? 0.6584 0.6616 0.4998 -0.0195 -0.0077 -0.0405 1831 ARG A C   
287 O O   . ARG A 38  ? 0.6299 0.6316 0.4831 -0.0301 0.0038  -0.0492 1831 ARG A O   
288 C CB  . ARG A 38  ? 0.7735 0.8116 0.6073 -0.0153 -0.0292 -0.0347 1831 ARG A CB  
289 C CG  . ARG A 38  ? 0.8817 0.9233 0.7106 -0.0350 -0.0224 -0.0444 1831 ARG A CG  
290 C CD  . ARG A 38  ? 0.9585 1.0027 0.7585 -0.0424 -0.0320 -0.0414 1831 ARG A CD  
291 N NE  . ARG A 38  ? 0.9912 1.0596 0.7928 -0.0309 -0.0483 -0.0331 1831 ARG A NE  
292 C CZ  . ARG A 38  ? 0.9204 1.0191 0.7385 -0.0335 -0.0523 -0.0365 1831 ARG A CZ  
293 N NH1 . ARG A 38  ? 0.8361 0.9405 0.6692 -0.0473 -0.0411 -0.0476 1831 ARG A NH1 
294 N NH2 . ARG A 38  ? 0.8933 1.0167 0.7136 -0.0223 -0.0674 -0.0291 1831 ARG A NH2 
295 N N   . ARG A 39  ? 0.6791 0.6613 0.4976 -0.0151 -0.0104 -0.0345 1832 ARG A N   
296 C CA  . ARG A 39  ? 0.6787 0.6370 0.4814 -0.0257 0.0002  -0.0384 1832 ARG A CA  
297 C C   . ARG A 39  ? 0.6709 0.6269 0.4955 -0.0243 0.0112  -0.0424 1832 ARG A C   
298 O O   . ARG A 39  ? 0.6365 0.5840 0.4611 -0.0356 0.0229  -0.0499 1832 ARG A O   
299 C CB  . ARG A 39  ? 0.6842 0.6191 0.4540 -0.0220 -0.0070 -0.0294 1832 ARG A CB  
300 C CG  . ARG A 39  ? 0.7348 0.6434 0.4855 -0.0320 0.0032  -0.0318 1832 ARG A CG  
301 C CD  . ARG A 39  ? 0.7591 0.6414 0.4748 -0.0282 -0.0055 -0.0211 1832 ARG A CD  
302 N NE  . ARG A 39  ? 0.9320 0.8137 0.6542 -0.0077 -0.0160 -0.0119 1832 ARG A NE  
303 C CZ  . ARG A 39  ? 0.9250 0.7950 0.6533 0.0006  -0.0122 -0.0107 1832 ARG A CZ  
304 N NH1 . ARG A 39  ? 0.9505 0.8100 0.6792 -0.0097 0.0008  -0.0169 1832 ARG A NH1 
305 N NH2 . ARG A 39  ? 0.9030 0.7736 0.6374 0.0190  -0.0212 -0.0041 1832 ARG A NH2 
306 N N   . ILE A 40  ? 0.5787 0.5447 0.4229 -0.0113 0.0077  -0.0380 1833 ILE A N   
307 C CA  . ILE A 40  ? 0.6046 0.5685 0.4655 -0.0095 0.0160  -0.0393 1833 ILE A CA  
308 C C   . ILE A 40  ? 0.6299 0.6132 0.5235 -0.0115 0.0212  -0.0436 1833 ILE A C   
309 O O   . ILE A 40  ? 0.6437 0.6255 0.5511 -0.0156 0.0304  -0.0471 1833 ILE A O   
310 C CB  . ILE A 40  ? 0.5619 0.5223 0.4208 0.0041  0.0099  -0.0321 1833 ILE A CB  
311 C CG1 . ILE A 40  ? 0.5614 0.4932 0.3884 0.0036  0.0093  -0.0286 1833 ILE A CG1 
312 C CG2 . ILE A 40  ? 0.5359 0.5056 0.4187 0.0062  0.0159  -0.0330 1833 ILE A CG2 
313 C CD1 . ILE A 40  ? 0.5203 0.4445 0.3405 0.0184  0.0016  -0.0218 1833 ILE A CD1 
314 N N   . ILE A 41  ? 0.5356 0.5374 0.4418 -0.0090 0.0152  -0.0430 1834 ILE A N   
315 C CA  . ILE A 41  ? 0.5073 0.5252 0.4429 -0.0105 0.0186  -0.0450 1834 ILE A CA  
316 C C   . ILE A 41  ? 0.5559 0.5749 0.4941 -0.0219 0.0232  -0.0528 1834 ILE A C   
317 O O   . ILE A 41  ? 0.5336 0.5624 0.4660 -0.0244 0.0172  -0.0537 1834 ILE A O   
318 C CB  . ILE A 41  ? 0.4402 0.4785 0.3887 -0.0014 0.0098  -0.0395 1834 ILE A CB  
319 C CG1 . ILE A 41  ? 0.4704 0.5071 0.4183 0.0088  0.0076  -0.0341 1834 ILE A CG1 
320 C CG2 . ILE A 41  ? 0.3975 0.4502 0.3721 -0.0059 0.0127  -0.0407 1834 ILE A CG2 
321 C CD1 . ILE A 41  ? 0.4125 0.4443 0.3729 0.0062  0.0159  -0.0340 1834 ILE A CD1 
322 N N   . LYS A 42  ? 0.5683 0.5790 0.5169 -0.0291 0.0344  -0.0594 1835 LYS A N   
323 C CA  . LYS A 42  ? 0.6058 0.6138 0.5557 -0.0406 0.0412  -0.0693 1835 LYS A CA  
324 C C   . LYS A 42  ? 0.6161 0.6368 0.5864 -0.0421 0.0396  -0.0699 1835 LYS A C   
325 O O   . LYS A 42  ? 0.6284 0.6522 0.5916 -0.0507 0.0392  -0.0757 1835 LYS A O   
326 C CB  . LYS A 42  ? 0.6349 0.6314 0.5933 -0.0463 0.0545  -0.0775 1835 LYS A CB  
327 C CG  . LYS A 42  ? 0.6909 0.6744 0.6261 -0.0492 0.0579  -0.0788 1835 LYS A CG  
328 C CD  . LYS A 42  ? 0.7600 0.7368 0.6621 -0.0569 0.0535  -0.0804 1835 LYS A CD  
329 C CE  . LYS A 42  ? 0.8022 0.7629 0.6789 -0.0638 0.0588  -0.0828 1835 LYS A CE  
330 N NZ  . LYS A 42  ? 0.8397 0.7934 0.7073 -0.0545 0.0531  -0.0727 1835 LYS A NZ  
331 N N   . ASN A 43  ? 0.6080 0.6362 0.6018 -0.0355 0.0386  -0.0640 1836 ASN A N   
332 C CA  . ASN A 43  ? 0.5986 0.6360 0.6111 -0.0383 0.0375  -0.0635 1836 ASN A CA  
333 C C   . ASN A 43  ? 0.5796 0.6349 0.5977 -0.0308 0.0274  -0.0535 1836 ASN A C   
334 O O   . ASN A 43  ? 0.4810 0.5403 0.5154 -0.0256 0.0271  -0.0469 1836 ASN A O   
335 C CB  . ASN A 43  ? 0.5906 0.6191 0.6278 -0.0395 0.0467  -0.0657 1836 ASN A CB  
336 C CG  . ASN A 43  ? 0.6396 0.6525 0.6740 -0.0459 0.0584  -0.0775 1836 ASN A CG  
337 O OD1 . ASN A 43  ? 0.6744 0.6815 0.7173 -0.0424 0.0645  -0.0785 1836 ASN A OD1 
338 N ND2 . ASN A 43  ? 0.7062 0.7146 0.7286 -0.0564 0.0619  -0.0875 1836 ASN A ND2 
339 N N   . PRO A 44  ? 0.6332 0.7020 0.6388 -0.0305 0.0190  -0.0526 1837 PRO A N   
340 C CA  . PRO A 44  ? 0.5608 0.6500 0.5735 -0.0238 0.0104  -0.0453 1837 PRO A CA  
341 C C   . PRO A 44  ? 0.5543 0.6524 0.5874 -0.0295 0.0115  -0.0434 1837 PRO A C   
342 O O   . PRO A 44  ? 0.5683 0.6577 0.6078 -0.0391 0.0171  -0.0482 1837 PRO A O   
343 C CB  . PRO A 44  ? 0.5846 0.6878 0.5813 -0.0232 0.0019  -0.0468 1837 PRO A CB  
344 C CG  . PRO A 44  ? 0.5561 0.6488 0.5408 -0.0347 0.0063  -0.0549 1837 PRO A CG  
345 C CD  . PRO A 44  ? 0.5650 0.6335 0.5494 -0.0364 0.0166  -0.0583 1837 PRO A CD  
346 N N   . MET A 45  ? 0.5110 0.6253 0.5533 -0.0243 0.0065  -0.0364 1838 MET A N   
347 C CA  . MET A 45  ? 0.5004 0.6229 0.5600 -0.0304 0.0066  -0.0322 1838 MET A CA  
348 C C   . MET A 45  ? 0.4498 0.5971 0.5124 -0.0259 -0.0003 -0.0269 1838 MET A C   
349 O O   . MET A 45  ? 0.4945 0.6464 0.5510 -0.0158 -0.0030 -0.0255 1838 MET A O   
350 C CB  . MET A 45  ? 0.4233 0.5294 0.4978 -0.0305 0.0127  -0.0279 1838 MET A CB  
351 C CG  . MET A 45  ? 0.4337 0.5428 0.5247 -0.0377 0.0125  -0.0218 1838 MET A CG  
352 S SD  . MET A 45  ? 0.5638 0.6735 0.6531 -0.0517 0.0132  -0.0279 1838 MET A SD  
353 C CE  . MET A 45  ? 0.5315 0.6140 0.6165 -0.0544 0.0227  -0.0391 1838 MET A CE  
354 N N   . ASP A 46  ? 0.4434 0.6062 0.5149 -0.0343 -0.0024 -0.0251 1839 ASP A N   
355 C CA  . ASP A 46  ? 0.5327 0.7227 0.6083 -0.0327 -0.0078 -0.0219 1839 ASP A CA  
356 C C   . ASP A 46  ? 0.4970 0.6948 0.5834 -0.0460 -0.0075 -0.0179 1839 ASP A C   
357 O O   . ASP A 46  ? 0.4883 0.6682 0.5784 -0.0550 -0.0036 -0.0178 1839 ASP A O   
358 C CB  . ASP A 46  ? 0.5850 0.7967 0.6517 -0.0276 -0.0138 -0.0276 1839 ASP A CB  
359 C CG  . ASP A 46  ? 0.6669 0.8882 0.7314 -0.0390 -0.0151 -0.0328 1839 ASP A CG  
360 O OD1 . ASP A 46  ? 0.7393 0.9419 0.7963 -0.0437 -0.0120 -0.0369 1839 ASP A OD1 
361 O OD2 . ASP A 46  ? 0.7239 0.9725 0.7939 -0.0451 -0.0186 -0.0336 1839 ASP A OD2 
362 N N   . PHE A 47  ? 0.4042 0.6284 0.4949 -0.0479 -0.0112 -0.0153 1840 PHE A N   
363 C CA  . PHE A 47  ? 0.4591 0.6902 0.5580 -0.0620 -0.0112 -0.0096 1840 PHE A CA  
364 C C   . PHE A 47  ? 0.5139 0.7516 0.6103 -0.0754 -0.0114 -0.0148 1840 PHE A C   
365 O O   . PHE A 47  ? 0.5211 0.7470 0.6215 -0.0886 -0.0092 -0.0107 1840 PHE A O   
366 C CB  . PHE A 47  ? 0.4199 0.6792 0.5224 -0.0621 -0.0141 -0.0065 1840 PHE A CB  
367 C CG  . PHE A 47  ? 0.4182 0.6704 0.5229 -0.0536 -0.0131 -0.0006 1840 PHE A CG  
368 C CD1 . PHE A 47  ? 0.4585 0.6819 0.5657 -0.0504 -0.0102 0.0048  1840 PHE A CD1 
369 C CD2 . PHE A 47  ? 0.4288 0.7044 0.5335 -0.0494 -0.0145 -0.0017 1840 PHE A CD2 
370 C CE1 . PHE A 47  ? 0.4656 0.6854 0.5746 -0.0442 -0.0095 0.0099  1840 PHE A CE1 
371 C CE2 . PHE A 47  ? 0.4899 0.7592 0.5949 -0.0438 -0.0130 0.0028  1840 PHE A CE2 
372 C CZ  . PHE A 47  ? 0.4686 0.7107 0.5754 -0.0417 -0.0109 0.0090  1840 PHE A CZ  
373 N N   . SER A 48  ? 0.5210 0.7774 0.6106 -0.0727 -0.0143 -0.0236 1841 SER A N   
374 C CA  . SER A 48  ? 0.5070 0.7733 0.5934 -0.0872 -0.0146 -0.0295 1841 SER A CA  
375 C C   . SER A 48  ? 0.5031 0.7360 0.5853 -0.0940 -0.0091 -0.0322 1841 SER A C   
376 O O   . SER A 48  ? 0.5537 0.7802 0.6359 -0.1103 -0.0062 -0.0336 1841 SER A O   
377 C CB  . SER A 48  ? 0.5285 0.8257 0.6096 -0.0816 -0.0203 -0.0375 1841 SER A CB  
378 O OG  . SER A 48  ? 0.6190 0.9005 0.6901 -0.0752 -0.0204 -0.0422 1841 SER A OG  
379 N N   . THR A 49  ? 0.4631 0.6740 0.5411 -0.0829 -0.0067 -0.0338 1842 THR A N   
380 C CA  . THR A 49  ? 0.5303 0.7087 0.6064 -0.0885 0.0004  -0.0376 1842 THR A CA  
381 C C   . THR A 49  ? 0.5175 0.6729 0.6057 -0.0944 0.0051  -0.0302 1842 THR A C   
382 O O   . THR A 49  ? 0.5717 0.7066 0.6611 -0.1056 0.0106  -0.0335 1842 THR A O   
383 C CB  . THR A 49  ? 0.5558 0.7175 0.6257 -0.0757 0.0026  -0.0402 1842 THR A CB  
384 O OG1 . THR A 49  ? 0.5909 0.7722 0.6485 -0.0693 -0.0033 -0.0446 1842 THR A OG1 
385 C CG2 . THR A 49  ? 0.4833 0.6155 0.5511 -0.0827 0.0112  -0.0472 1842 THR A CG2 
386 N N   . MET A 50  ? 0.5132 0.6711 0.6103 -0.0872 0.0028  -0.0199 1843 MET A N   
387 C CA  . MET A 50  ? 0.5408 0.6797 0.6496 -0.0926 0.0050  -0.0102 1843 MET A CA  
388 C C   . MET A 50  ? 0.5615 0.7089 0.6698 -0.1099 0.0034  -0.0075 1843 MET A C   
389 O O   . MET A 50  ? 0.6063 0.7290 0.7193 -0.1193 0.0070  -0.0043 1843 MET A O   
390 C CB  . MET A 50  ? 0.4636 0.6075 0.5801 -0.0824 0.0019  0.0005  1843 MET A CB  
391 C CG  . MET A 50  ? 0.5317 0.6613 0.6498 -0.0679 0.0049  -0.0013 1843 MET A CG  
392 S SD  . MET A 50  ? 0.4906 0.6341 0.6124 -0.0572 0.0010  0.0078  1843 MET A SD  
393 C CE  . MET A 50  ? 0.4207 0.5580 0.5568 -0.0649 -0.0013 0.0233  1843 MET A CE  
394 N N   . ARG A 51  ? 0.4805 0.6623 0.5834 -0.1144 -0.0016 -0.0091 1844 ARG A N   
395 C CA  . ARG A 51  ? 0.5159 0.7103 0.6164 -0.1333 -0.0027 -0.0083 1844 ARG A CA  
396 C C   . ARG A 51  ? 0.5498 0.7285 0.6440 -0.1464 0.0021  -0.0175 1844 ARG A C   
397 O O   . ARG A 51  ? 0.5955 0.7571 0.6898 -0.1620 0.0049  -0.0142 1844 ARG A O   
398 C CB  . ARG A 51  ? 0.5438 0.7831 0.6411 -0.1344 -0.0079 -0.0120 1844 ARG A CB  
399 C CG  . ARG A 51  ? 0.5981 0.8574 0.6915 -0.1556 -0.0085 -0.0144 1844 ARG A CG  
400 C CD  . ARG A 51  ? 0.6104 0.8543 0.7062 -0.1694 -0.0077 -0.0021 1844 ARG A CD  
401 N NE  . ARG A 51  ? 0.6531 0.9120 0.7541 -0.1628 -0.0112 0.0073  1844 ARG A NE  
402 C CZ  . ARG A 51  ? 0.6857 0.9305 0.7890 -0.1704 -0.0122 0.0212  1844 ARG A CZ  
403 N NH1 . ARG A 51  ? 0.7214 0.9341 0.8234 -0.1831 -0.0102 0.0280  1844 ARG A NH1 
404 N NH2 . ARG A 51  ? 0.6949 0.9568 0.8011 -0.1657 -0.0153 0.0284  1844 ARG A NH2 
405 N N   . HIS A 52  ? 0.5321 0.7148 0.6193 -0.1413 0.0033  -0.0289 1845 HIS A N   
406 C CA  A HIS A 52  ? 0.5599 0.7299 0.6390 -0.1551 0.0083  -0.0395 1845 HIS A CA  
407 C CA  B HIS A 52  ? 0.5598 0.7301 0.6390 -0.1555 0.0083  -0.0393 1845 HIS A CA  
408 C C   . HIS A 52  ? 0.6104 0.7345 0.6946 -0.1580 0.0166  -0.0384 1845 HIS A C   
409 O O   . HIS A 52  ? 0.6555 0.7623 0.7367 -0.1749 0.0215  -0.0419 1845 HIS A O   
410 C CB  A HIS A 52  ? 0.5387 0.7221 0.6083 -0.1478 0.0070  -0.0503 1845 HIS A CB  
411 C CB  B HIS A 52  ? 0.5388 0.7240 0.6081 -0.1495 0.0068  -0.0505 1845 HIS A CB  
412 C CG  A HIS A 52  ? 0.5509 0.7248 0.6099 -0.1628 0.0121  -0.0624 1845 HIS A CG  
413 C CG  B HIS A 52  ? 0.5081 0.7385 0.5745 -0.1454 -0.0017 -0.0519 1845 HIS A CG  
414 N ND1 A HIS A 52  ? 0.5253 0.6608 0.5837 -0.1656 0.0214  -0.0678 1845 HIS A ND1 
415 N ND1 B HIS A 52  ? 0.5013 0.7602 0.5728 -0.1517 -0.0058 -0.0475 1845 HIS A ND1 
416 C CD2 A HIS A 52  ? 0.5235 0.7237 0.5721 -0.1762 0.0097  -0.0713 1845 HIS A CD2 
417 C CD2 B HIS A 52  ? 0.4951 0.7473 0.5550 -0.1351 -0.0070 -0.0572 1845 HIS A CD2 
418 C CE1 A HIS A 52  ? 0.5262 0.6626 0.5727 -0.1814 0.0250  -0.0799 1845 HIS A CE1 
419 C CE1 B HIS A 52  ? 0.4844 0.7821 0.5550 -0.1442 -0.0126 -0.0513 1845 HIS A CE1 
420 N NE2 A HIS A 52  ? 0.4827 0.6588 0.5227 -0.1885 0.0175  -0.0818 1845 HIS A NE2 
421 N NE2 B HIS A 52  ? 0.4821 0.7754 0.5458 -0.1334 -0.0141 -0.0564 1845 HIS A NE2 
422 N N   . ARG A 53  ? 0.6529 0.7568 0.7458 -0.1417 0.0186  -0.0341 1846 ARG A N   
423 C CA  . ARG A 53  ? 0.6867 0.7492 0.7882 -0.1414 0.0267  -0.0343 1846 ARG A CA  
424 C C   . ARG A 53  ? 0.7041 0.7485 0.8152 -0.1485 0.0261  -0.0214 1846 ARG A C   
425 O O   . ARG A 53  ? 0.7595 0.7700 0.8751 -0.1553 0.0327  -0.0230 1846 ARG A O   
426 C CB  . ARG A 53  ? 0.6747 0.7255 0.7841 -0.1224 0.0289  -0.0335 1846 ARG A CB  
427 C CG  . ARG A 53  ? 0.7295 0.7412 0.8509 -0.1199 0.0381  -0.0361 1846 ARG A CG  
428 C CD  . ARG A 53  ? 0.7080 0.7133 0.8372 -0.1027 0.0409  -0.0374 1846 ARG A CD  
429 N NE  . ARG A 53  ? 0.7928 0.7645 0.9385 -0.0987 0.0496  -0.0393 1846 ARG A NE  
430 C CZ  . ARG A 53  ? 0.8520 0.8156 1.0099 -0.0846 0.0533  -0.0397 1846 ARG A CZ  
431 N NH1 . ARG A 53  ? 0.8670 0.8508 1.0198 -0.0748 0.0493  -0.0380 1846 ARG A NH1 
432 N NH2 . ARG A 53  ? 0.8721 0.8072 1.0479 -0.0804 0.0613  -0.0422 1846 ARG A NH2 
433 N N   . LEU A 54  ? 0.6646 0.7300 0.7783 -0.1474 0.0183  -0.0087 1847 LEU A N   
434 C CA  . LEU A 54  ? 0.6641 0.7143 0.7834 -0.1567 0.0163  0.0052  1847 LEU A CA  
435 C C   . LEU A 54  ? 0.7570 0.8058 0.8652 -0.1801 0.0182  0.0011  1847 LEU A C   
436 O O   . LEU A 54  ? 0.8098 0.8261 0.9204 -0.1901 0.0212  0.0069  1847 LEU A O   
437 C CB  . LEU A 54  ? 0.6010 0.6776 0.7233 -0.1519 0.0079  0.0188  1847 LEU A CB  
438 C CG  . LEU A 54  ? 0.6138 0.6731 0.7445 -0.1548 0.0041  0.0374  1847 LEU A CG  
439 C CD1 . LEU A 54  ? 0.5672 0.5866 0.7129 -0.1433 0.0080  0.0418  1847 LEU A CD1 
440 C CD2 . LEU A 54  ? 0.6150 0.7042 0.7474 -0.1484 -0.0033 0.0476  1847 LEU A CD2 
441 N N   . SER A 55  ? 0.7145 0.7980 0.8109 -0.1889 0.0164  -0.0091 1848 SER A N   
442 C CA  . SER A 55  ? 0.7531 0.8427 0.8381 -0.2131 0.0180  -0.0141 1848 SER A CA  
443 C C   . SER A 55  ? 0.8217 0.8743 0.9023 -0.2238 0.0273  -0.0245 1848 SER A C   
444 O O   . SER A 55  ? 0.8041 0.8373 0.8788 -0.2435 0.0306  -0.0231 1848 SER A O   
445 C CB  . SER A 55  ? 0.7036 0.8431 0.7798 -0.2176 0.0138  -0.0241 1848 SER A CB  
446 O OG  . SER A 55  ? 0.6977 0.8717 0.7771 -0.2137 0.0066  -0.0157 1848 SER A OG  
447 N N   . ARG A 56  ? 0.8049 0.8467 0.8866 -0.2129 0.0325  -0.0359 1849 ARG A N   
448 C CA  . ARG A 56  ? 0.8231 0.8310 0.9004 -0.2231 0.0429  -0.0486 1849 ARG A CA  
449 C C   . ARG A 56  ? 0.8314 0.7898 0.9231 -0.2145 0.0492  -0.0427 1849 ARG A C   
450 O O   . ARG A 56  ? 0.8772 0.8037 0.9685 -0.2191 0.0595  -0.0546 1849 ARG A O   
451 C CB  . ARG A 56  ? 0.8427 0.8640 0.9125 -0.2182 0.0460  -0.0648 1849 ARG A CB  
452 C CG  . ARG A 56  ? 0.8511 0.8703 0.9302 -0.1939 0.0453  -0.0631 1849 ARG A CG  
453 C CD  . ARG A 56  ? 0.9253 0.9485 0.9939 -0.1936 0.0502  -0.0795 1849 ARG A CD  
454 N NE  . ARG A 56  ? 0.9534 0.9711 1.0289 -0.1730 0.0511  -0.0790 1849 ARG A NE  
455 C CZ  . ARG A 56  ? 0.9402 0.9238 1.0260 -0.1658 0.0603  -0.0828 1849 ARG A CZ  
456 N NH1 . ARG A 56  ? 0.9343 0.8835 1.0259 -0.1756 0.0695  -0.0874 1849 ARG A NH1 
457 N NH2 . ARG A 56  ? 0.8940 0.8780 0.9849 -0.1488 0.0608  -0.0826 1849 ARG A NH2 
458 N N   . GLY A 57  ? 0.7726 0.7253 0.8775 -0.2021 0.0433  -0.0251 1850 GLY A N   
459 C CA  . GLY A 57  ? 0.7899 0.6988 0.9114 -0.1922 0.0474  -0.0173 1850 GLY A CA  
460 C C   . GLY A 57  ? 0.8159 0.7125 0.9500 -0.1725 0.0535  -0.0256 1850 GLY A C   
461 O O   . GLY A 57  ? 0.8850 0.7429 1.0322 -0.1671 0.0611  -0.0274 1850 GLY A O   
462 N N   . GLY A 58  ? 0.7654 0.6936 0.8960 -0.1616 0.0505  -0.0308 1851 GLY A N   
463 C CA  . GLY A 58  ? 0.7801 0.7008 0.9186 -0.1460 0.0566  -0.0402 1851 GLY A CA  
464 C C   . GLY A 58  ? 0.8264 0.7421 0.9846 -0.1254 0.0537  -0.0282 1851 GLY A C   
465 O O   . GLY A 58  ? 0.8351 0.7481 0.9997 -0.1131 0.0589  -0.0363 1851 GLY A O   
466 N N   . TYR A 59  ? 0.8205 0.7369 0.9878 -0.1225 0.0454  -0.0092 1852 TYR A N   
467 C CA  . TYR A 59  ? 0.8053 0.7187 0.9922 -0.1043 0.0418  0.0034  1852 TYR A CA  
468 C C   . TYR A 59  ? 0.8970 0.7716 1.1028 -0.1016 0.0445  0.0117  1852 TYR A C   
469 O O   . TYR A 59  ? 0.9252 0.7854 1.1275 -0.1135 0.0411  0.0219  1852 TYR A O   
470 C CB  . TYR A 59  ? 0.7207 0.6647 0.9048 -0.1023 0.0297  0.0199  1852 TYR A CB  
471 C CG  . TYR A 59  ? 0.6342 0.6136 0.8066 -0.0972 0.0268  0.0134  1852 TYR A CG  
472 C CD1 . TYR A 59  ? 0.6166 0.5996 0.7947 -0.0823 0.0299  0.0076  1852 TYR A CD1 
473 C CD2 . TYR A 59  ? 0.5906 0.5995 0.7467 -0.1072 0.0212  0.0132  1852 TYR A CD2 
474 C CE1 . TYR A 59  ? 0.5774 0.5879 0.7430 -0.0778 0.0271  0.0025  1852 TYR A CE1 
475 C CE2 . TYR A 59  ? 0.5336 0.5719 0.6804 -0.1007 0.0184  0.0077  1852 TYR A CE2 
476 C CZ  . TYR A 59  ? 0.5496 0.5864 0.7002 -0.0861 0.0212  0.0029  1852 TYR A CZ  
477 O OH  . TYR A 59  ? 0.5696 0.6313 0.7093 -0.0799 0.0182  -0.0017 1852 TYR A OH  
478 N N   . THR A 60  ? 0.9373 0.7951 1.1629 -0.0858 0.0507  0.0075  1853 THR A N   
479 C CA  . THR A 60  ? 0.9702 0.7927 1.2191 -0.0779 0.0524  0.0165  1853 THR A CA  
480 C C   . THR A 60  ? 1.0155 0.8477 1.2769 -0.0693 0.0393  0.0416  1853 THR A C   
481 O O   . THR A 60  ? 1.1093 0.9247 1.3716 -0.0761 0.0329  0.0579  1853 THR A O   
482 C CB  . THR A 60  ? 0.9320 0.7388 1.2006 -0.0631 0.0640  0.0018  1853 THR A CB  
483 O OG1 . THR A 60  ? 0.9699 0.7601 1.2272 -0.0741 0.0771  -0.0209 1853 THR A OG1 
484 C CG2 . THR A 60  ? 0.9515 0.7284 1.2502 -0.0493 0.0635  0.0138  1853 THR A CG2 
485 N N   . SER A 61  ? 0.9347 0.7935 1.2041 -0.0558 0.0351  0.0452  1854 SER A N   
486 C CA  . SER A 61  ? 0.8670 0.7388 1.1489 -0.0474 0.0231  0.0676  1854 SER A CA  
487 C C   . SER A 61  ? 0.8190 0.7317 1.0832 -0.0518 0.0155  0.0715  1854 SER A C   
488 O O   . SER A 61  ? 0.8215 0.7517 1.0678 -0.0570 0.0196  0.0568  1854 SER A O   
489 C CB  . SER A 61  ? 0.8503 0.7178 1.1613 -0.0268 0.0254  0.0686  1854 SER A CB  
490 O OG  . SER A 61  ? 0.7909 0.6780 1.0990 -0.0206 0.0326  0.0514  1854 SER A OG  
491 N N   . SER A 62  ? 0.8941 0.6640 1.0357 -0.0140 0.0026  0.0354  1855 SER A N   
492 C CA  . SER A 62  ? 0.8628 0.6816 0.9985 -0.0248 0.0015  0.0439  1855 SER A CA  
493 C C   . SER A 62  ? 0.7818 0.6452 0.9410 -0.0068 0.0090  0.0346  1855 SER A C   
494 O O   . SER A 62  ? 0.7271 0.6293 0.8792 -0.0152 0.0116  0.0346  1855 SER A O   
495 C CB  . SER A 62  ? 0.9189 0.7294 1.0461 -0.0314 -0.0153 0.0714  1855 SER A CB  
496 O OG  . SER A 62  ? 0.9687 0.7728 1.1224 -0.0066 -0.0266 0.0819  1855 SER A OG  
497 N N   . GLU A 63  ? 0.8387 0.6967 1.0258 0.0174  0.0135  0.0258  1856 GLU A N   
498 C CA  . GLU A 63  ? 0.8285 0.7288 1.0373 0.0309  0.0234  0.0164  1856 GLU A CA  
499 C C   . GLU A 63  ? 0.7876 0.7063 0.9776 0.0210  0.0389  -0.0028 1856 GLU A C   
500 O O   . GLU A 63  ? 0.7276 0.6827 0.9157 0.0180  0.0424  -0.0033 1856 GLU A O   
501 C CB  . GLU A 63  ? 0.9082 0.8018 1.1535 0.0578  0.0280  0.0085  1856 GLU A CB  
502 C CG  . GLU A 63  ? 1.0186 0.9200 1.2951 0.0732  0.0113  0.0274  1856 GLU A CG  
503 C CD  . GLU A 63  ? 1.1747 1.0262 1.4467 0.0765  -0.0069 0.0432  1856 GLU A CD  
504 O OE1 . GLU A 63  ? 1.2461 1.0531 1.5045 0.0755  -0.0024 0.0337  1856 GLU A OE1 
505 O OE2 . GLU A 63  ? 1.2113 1.0650 1.4902 0.0790  -0.0269 0.0656  1856 GLU A OE2 
506 N N   . GLU A 64  ? 0.7990 0.6895 0.9728 0.0157  0.0464  -0.0186 1857 GLU A N   
507 C CA  . GLU A 64  ? 0.7813 0.6867 0.9335 0.0057  0.0573  -0.0360 1857 GLU A CA  
508 C C   . GLU A 64  ? 0.6719 0.6017 0.8047 -0.0136 0.0503  -0.0285 1857 GLU A C   
509 O O   . GLU A 64  ? 0.6336 0.5906 0.7564 -0.0162 0.0550  -0.0359 1857 GLU A O   
510 C CB  . GLU A 64  ? 0.8630 0.7308 0.9990 0.0009  0.0633  -0.0542 1857 GLU A CB  
511 C CG  . GLU A 64  ? 0.9826 0.8248 1.1365 0.0220  0.0731  -0.0672 1857 GLU A CG  
512 C CD  . GLU A 64  ? 1.1349 0.9311 1.2695 0.0158  0.0768  -0.0849 1857 GLU A CD  
513 O OE1 . GLU A 64  ? 1.1630 0.9434 1.2751 -0.0064 0.0682  -0.0819 1857 GLU A OE1 
514 O OE2 . GLU A 64  ? 1.2069 0.9835 1.3490 0.0320  0.0891  -0.1032 1857 GLU A OE2 
515 N N   . PHE A 65  ? 0.6056 0.5250 0.7319 -0.0269 0.0394  -0.0140 1858 PHE A N   
516 C CA  . PHE A 65  ? 0.5784 0.5257 0.6906 -0.0438 0.0349  -0.0082 1858 PHE A CA  
517 C C   . PHE A 65  ? 0.5245 0.5064 0.6452 -0.0359 0.0329  0.0002  1858 PHE A C   
518 O O   . PHE A 65  ? 0.4919 0.5018 0.6037 -0.0405 0.0343  -0.0049 1858 PHE A O   
519 C CB  . PHE A 65  ? 0.6224 0.5512 0.7245 -0.0616 0.0266  0.0059  1858 PHE A CB  
520 C CG  . PHE A 65  ? 0.5497 0.5112 0.6402 -0.0789 0.0246  0.0105  1858 PHE A CG  
521 C CD1 . PHE A 65  ? 0.5052 0.4848 0.5959 -0.0783 0.0191  0.0258  1858 PHE A CD1 
522 C CD2 . PHE A 65  ? 0.5454 0.5214 0.6260 -0.0953 0.0281  -0.0021 1858 PHE A CD2 
523 C CE1 . PHE A 65  ? 0.5044 0.5144 0.5844 -0.0927 0.0197  0.0268  1858 PHE A CE1 
524 C CE2 . PHE A 65  ? 0.5180 0.5291 0.5938 -0.1087 0.0278  -0.0005 1858 PHE A CE2 
525 C CZ  . PHE A 65  ? 0.4865 0.5136 0.5612 -0.1068 0.0249  0.0133  1858 PHE A CZ  
526 N N   . ALA A 66  ? 0.4748 0.4539 0.6135 -0.0235 0.0280  0.0126  1859 ALA A N   
527 C CA  . ALA A 66  ? 0.5004 0.5101 0.6474 -0.0181 0.0249  0.0202  1859 ALA A CA  
528 C C   . ALA A 66  ? 0.5177 0.5472 0.6684 -0.0099 0.0355  0.0068  1859 ALA A C   
529 O O   . ALA A 66  ? 0.5551 0.6082 0.6995 -0.0125 0.0346  0.0078  1859 ALA A O   
530 C CB  . ALA A 66  ? 0.5562 0.5599 0.7249 -0.0068 0.0152  0.0354  1859 ALA A CB  
531 N N   . ALA A 67  ? 0.4506 0.4673 0.6081 -0.0008 0.0461  -0.0061 1860 ALA A N   
532 C CA  . ALA A 67  ? 0.4672 0.4992 0.6217 0.0041  0.0579  -0.0183 1860 ALA A CA  
533 C C   . ALA A 67  ? 0.4858 0.5267 0.6117 -0.0069 0.0575  -0.0253 1860 ALA A C   
534 O O   . ALA A 67  ? 0.5261 0.5838 0.6442 -0.0065 0.0597  -0.0261 1860 ALA A O   
535 C CB  . ALA A 67  ? 0.4096 0.4241 0.5713 0.0141  0.0712  -0.0332 1860 ALA A CB  
536 N N   . ASP A 68  ? 0.4871 0.5163 0.5982 -0.0171 0.0537  -0.0303 1861 ASP A N   
537 C CA  . ASP A 68  ? 0.5198 0.5623 0.6097 -0.0257 0.0505  -0.0376 1861 ASP A CA  
538 C C   . ASP A 68  ? 0.5248 0.5910 0.6146 -0.0288 0.0423  -0.0278 1861 ASP A C   
539 O O   . ASP A 68  ? 0.5607 0.6412 0.6386 -0.0275 0.0403  -0.0318 1861 ASP A O   
540 C CB  . ASP A 68  ? 0.5690 0.5990 0.6490 -0.0378 0.0477  -0.0461 1861 ASP A CB  
541 C CG  . ASP A 68  ? 0.6144 0.6252 0.6813 -0.0367 0.0548  -0.0629 1861 ASP A CG  
542 O OD1 . ASP A 68  ? 0.6166 0.6302 0.6749 -0.0285 0.0619  -0.0691 1861 ASP A OD1 
543 O OD2 . ASP A 68  ? 0.6461 0.6371 0.7081 -0.0461 0.0537  -0.0702 1861 ASP A OD2 
544 N N   . ALA A 69  ? 0.4152 0.4826 0.5150 -0.0325 0.0370  -0.0151 1862 ALA A N   
545 C CA  . ALA A 69  ? 0.4224 0.5108 0.5190 -0.0359 0.0308  -0.0080 1862 ALA A CA  
546 C C   . ALA A 69  ? 0.4197 0.5175 0.5192 -0.0267 0.0310  -0.0048 1862 ALA A C   
547 O O   . ALA A 69  ? 0.3999 0.5111 0.4893 -0.0264 0.0280  -0.0073 1862 ALA A O   
548 C CB  . ALA A 69  ? 0.4035 0.4878 0.5037 -0.0440 0.0253  0.0055  1862 ALA A CB  
549 N N   . LEU A 70  ? 0.3902 0.4812 0.5050 -0.0194 0.0344  -0.0001 1863 LEU A N   
550 C CA  . LEU A 70  ? 0.4624 0.5642 0.5819 -0.0145 0.0356  0.0027  1863 LEU A CA  
551 C C   . LEU A 70  ? 0.4407 0.5416 0.5438 -0.0127 0.0425  -0.0075 1863 LEU A C   
552 O O   . LEU A 70  ? 0.4114 0.5181 0.5067 -0.0129 0.0413  -0.0056 1863 LEU A O   
553 C CB  . LEU A 70  ? 0.5187 0.6205 0.6650 -0.0074 0.0381  0.0089  1863 LEU A CB  
554 C CG  . LEU A 70  ? 0.5734 0.6721 0.7333 -0.0079 0.0271  0.0220  1863 LEU A CG  
555 C CD1 . LEU A 70  ? 0.6037 0.7051 0.7960 0.0030  0.0274  0.0267  1863 LEU A CD1 
556 C CD2 . LEU A 70  ? 0.4981 0.6085 0.6469 -0.0158 0.0160  0.0310  1863 LEU A CD2 
557 N N   . LEU A 71  ? 0.4543 0.5443 0.5478 -0.0123 0.0485  -0.0180 1864 LEU A N   
558 C CA  . LEU A 71  ? 0.4721 0.5583 0.5423 -0.0120 0.0524  -0.0268 1864 LEU A CA  
559 C C   . LEU A 71  ? 0.4677 0.5611 0.5205 -0.0136 0.0414  -0.0271 1864 LEU A C   
560 O O   . LEU A 71  ? 0.4202 0.5105 0.4559 -0.0118 0.0400  -0.0269 1864 LEU A O   
561 C CB  . LEU A 71  ? 0.4260 0.4984 0.4863 -0.0128 0.0585  -0.0390 1864 LEU A CB  
562 C CG  . LEU A 71  ? 0.4328 0.4969 0.4637 -0.0134 0.0628  -0.0485 1864 LEU A CG  
563 C CD1 . LEU A 71  ? 0.4010 0.4648 0.4292 -0.0115 0.0746  -0.0455 1864 LEU A CD1 
564 C CD2 . LEU A 71  ? 0.4301 0.4794 0.4528 -0.0156 0.0683  -0.0618 1864 LEU A CD2 
565 N N   . VAL A 72  ? 0.3538 0.4560 0.4110 -0.0171 0.0338  -0.0279 1865 VAL A N   
566 C CA  . VAL A 72  ? 0.4161 0.5309 0.4639 -0.0160 0.0242  -0.0308 1865 VAL A CA  
567 C C   . VAL A 72  ? 0.4439 0.5596 0.4884 -0.0120 0.0211  -0.0241 1865 VAL A C   
568 O O   . VAL A 72  ? 0.4493 0.5611 0.4778 -0.0068 0.0154  -0.0267 1865 VAL A O   
569 C CB  . VAL A 72  ? 0.3698 0.5001 0.4284 -0.0228 0.0206  -0.0322 1865 VAL A CB  
570 C CG1 . VAL A 72  ? 0.3221 0.4712 0.3773 -0.0193 0.0129  -0.0375 1865 VAL A CG1 
571 C CG2 . VAL A 72  ? 0.3576 0.4841 0.4175 -0.0299 0.0226  -0.0397 1865 VAL A CG2 
572 N N   . PHE A 73  ? 0.3747 0.4925 0.4330 -0.0147 0.0230  -0.0150 1866 PHE A N   
573 C CA  . PHE A 73  ? 0.4159 0.5344 0.4709 -0.0138 0.0187  -0.0097 1866 PHE A CA  
574 C C   . PHE A 73  ? 0.3854 0.4923 0.4352 -0.0135 0.0232  -0.0063 1866 PHE A C   
575 O O   . PHE A 73  ? 0.4550 0.5544 0.4915 -0.0132 0.0187  -0.0050 1866 PHE A O   
576 C CB  . PHE A 73  ? 0.3897 0.5165 0.4586 -0.0190 0.0162  -0.0014 1866 PHE A CB  
577 C CG  . PHE A 73  ? 0.3784 0.5148 0.4495 -0.0235 0.0147  -0.0029 1866 PHE A CG  
578 C CD1 . PHE A 73  ? 0.3011 0.4487 0.3635 -0.0228 0.0124  -0.0122 1866 PHE A CD1 
579 C CD2 . PHE A 73  ? 0.4365 0.5702 0.5189 -0.0289 0.0157  0.0047  1866 PHE A CD2 
580 C CE1 . PHE A 73  ? 0.3149 0.4756 0.3806 -0.0304 0.0137  -0.0143 1866 PHE A CE1 
581 C CE2 . PHE A 73  ? 0.3957 0.5348 0.4758 -0.0371 0.0154  0.0046  1866 PHE A CE2 
582 C CZ  . PHE A 73  ? 0.3156 0.4703 0.3877 -0.0394 0.0157  -0.0052 1866 PHE A CZ  
583 N N   . ASP A 74  ? 0.3196 0.4239 0.3790 -0.0143 0.0331  -0.0056 1867 ASP A N   
584 C CA  . ASP A 74  ? 0.4196 0.5160 0.4716 -0.0164 0.0412  -0.0044 1867 ASP A CA  
585 C C   . ASP A 74  ? 0.4772 0.5572 0.4959 -0.0152 0.0385  -0.0088 1867 ASP A C   
586 O O   . ASP A 74  ? 0.4871 0.5551 0.4891 -0.0182 0.0367  -0.0047 1867 ASP A O   
587 C CB  . ASP A 74  ? 0.3775 0.4769 0.4462 -0.0158 0.0550  -0.0069 1867 ASP A CB  
588 C CG  . ASP A 74  ? 0.4493 0.5639 0.5535 -0.0152 0.0561  -0.0002 1867 ASP A CG  
589 O OD1 . ASP A 74  ? 0.4612 0.5835 0.5728 -0.0186 0.0471  0.0075  1867 ASP A OD1 
590 O OD2 . ASP A 74  ? 0.5175 0.6351 0.6419 -0.0104 0.0646  -0.0033 1867 ASP A OD2 
591 N N   . ASN A 75  ? 0.4367 0.5143 0.4443 -0.0114 0.0360  -0.0167 1868 ASN A N   
592 C CA  . ASN A 75  ? 0.4784 0.5412 0.4541 -0.0085 0.0288  -0.0202 1868 ASN A CA  
593 C C   . ASN A 75  ? 0.4516 0.5107 0.4189 -0.0031 0.0148  -0.0180 1868 ASN A C   
594 O O   . ASN A 75  ? 0.4384 0.4768 0.3792 -0.0014 0.0090  -0.0151 1868 ASN A O   
595 C CB  . ASN A 75  ? 0.4070 0.4736 0.3774 -0.0061 0.0251  -0.0301 1868 ASN A CB  
596 C CG  . ASN A 75  ? 0.4503 0.5114 0.4190 -0.0107 0.0388  -0.0353 1868 ASN A CG  
597 O OD1 . ASN A 75  ? 0.5261 0.5798 0.4907 -0.0142 0.0518  -0.0325 1868 ASN A OD1 
598 N ND2 . ASN A 75  ? 0.4356 0.5009 0.4084 -0.0114 0.0370  -0.0443 1868 ASN A ND2 
599 N N   . CYS A 76  ? 0.4172 0.4937 0.4046 -0.0005 0.0097  -0.0198 1869 CYS A N   
600 C CA  . CYS A 76  ? 0.4502 0.5251 0.4320 0.0064  -0.0017 -0.0213 1869 CYS A CA  
601 C C   . CYS A 76  ? 0.5174 0.5721 0.4874 0.0027  -0.0019 -0.0137 1869 CYS A C   
602 O O   . CYS A 76  ? 0.5489 0.5827 0.4976 0.0087  -0.0113 -0.0139 1869 CYS A O   
603 C CB  . CYS A 76  ? 0.4535 0.5525 0.4572 0.0062  -0.0024 -0.0250 1869 CYS A CB  
604 S SG  . CYS A 76  ? 0.5002 0.6001 0.4992 0.0150  -0.0123 -0.0308 1869 CYS A SG  
605 N N   . GLN A 77  ? 0.4658 0.5253 0.4503 -0.0072 0.0071  -0.0069 1870 GLN A N   
606 C CA  . GLN A 77  ? 0.5292 0.5733 0.5060 -0.0149 0.0074  0.0000  1870 GLN A CA  
607 C C   . GLN A 77  ? 0.4980 0.5192 0.4508 -0.0208 0.0129  0.0047  1870 GLN A C   
608 O O   . GLN A 77  ? 0.5178 0.5166 0.4531 -0.0272 0.0100  0.0099  1870 GLN A O   
609 C CB  . GLN A 77  ? 0.5132 0.5762 0.5180 -0.0240 0.0133  0.0054  1870 GLN A CB  
610 C CG  . GLN A 77  ? 0.4619 0.5413 0.4810 -0.0218 0.0064  0.0036  1870 GLN A CG  
611 C CD  . GLN A 77  ? 0.4100 0.5071 0.4554 -0.0293 0.0089  0.0107  1870 GLN A CD  
612 O OE1 . GLN A 77  ? 0.4808 0.5789 0.5295 -0.0365 0.0035  0.0147  1870 GLN A OE1 
613 N NE2 . GLN A 77  ? 0.3858 0.4952 0.4500 -0.0272 0.0155  0.0120  1870 GLN A NE2 
614 N N   . THR A 78  ? 0.5282 0.5517 0.4762 -0.0206 0.0213  0.0027  1871 THR A N   
615 C CA  . THR A 78  ? 0.5083 0.5089 0.4260 -0.0280 0.0279  0.0070  1871 THR A CA  
616 C C   . THR A 78  ? 0.5246 0.4941 0.4039 -0.0208 0.0124  0.0080  1871 THR A C   
617 O O   . THR A 78  ? 0.5693 0.5083 0.4178 -0.0285 0.0115  0.0159  1871 THR A O   
618 C CB  . THR A 78  ? 0.5532 0.5638 0.4725 -0.0298 0.0418  0.0021  1871 THR A CB  
619 O OG1 . THR A 78  ? 0.4979 0.5336 0.4542 -0.0344 0.0559  0.0016  1871 THR A OG1 
620 C CG2 . THR A 78  ? 0.4573 0.4430 0.3368 -0.0389 0.0495  0.0058  1871 THR A CG2 
621 N N   . PHE A 79  ? 0.5090 0.4855 0.3904 -0.0063 -0.0007 0.0005  1872 PHE A N   
622 C CA  . PHE A 79  ? 0.5716 0.5218 0.4208 0.0043  -0.0180 0.0008  1872 PHE A CA  
623 C C   . PHE A 79  ? 0.5720 0.5100 0.4219 0.0150  -0.0327 -0.0004 1872 PHE A C   
624 O O   . PHE A 79  ? 0.5566 0.4587 0.3750 0.0209  -0.0459 0.0041  1872 PHE A O   
625 C CB  . PHE A 79  ? 0.4794 0.4466 0.3313 0.0147  -0.0259 -0.0084 1872 PHE A CB  
626 C CG  . PHE A 79  ? 0.6091 0.5508 0.4268 0.0256  -0.0453 -0.0072 1872 PHE A CG  
627 C CD1 . PHE A 79  ? 0.6672 0.5820 0.4436 0.0180  -0.0448 -0.0004 1872 PHE A CD1 
628 C CD2 . PHE A 79  ? 0.6051 0.5496 0.4308 0.0439  -0.0644 -0.0129 1872 PHE A CD2 
629 C CE1 . PHE A 79  ? 0.7096 0.5976 0.4506 0.0283  -0.0662 0.0029  1872 PHE A CE1 
630 C CE2 . PHE A 79  ? 0.6571 0.5781 0.4541 0.0570  -0.0857 -0.0111 1872 PHE A CE2 
631 C CZ  . PHE A 79  ? 0.7005 0.5913 0.4535 0.0491  -0.0882 -0.0020 1872 PHE A CZ  
632 N N   . ASN A 80  ? 0.5310 0.4941 0.4124 0.0180  -0.0311 -0.0067 1873 ASN A N   
633 C CA  . ASN A 80  ? 0.5686 0.5244 0.4516 0.0306  -0.0437 -0.0127 1873 ASN A CA  
634 C C   . ASN A 80  ? 0.6204 0.5616 0.5028 0.0197  -0.0398 -0.0084 1873 ASN A C   
635 O O   . ASN A 80  ? 0.6279 0.5873 0.5286 0.0054  -0.0278 -0.0045 1873 ASN A O   
636 C CB  . ASN A 80  ? 0.5477 0.5432 0.4618 0.0406  -0.0447 -0.0253 1873 ASN A CB  
637 C CG  . ASN A 80  ? 0.6112 0.6261 0.5304 0.0480  -0.0489 -0.0309 1873 ASN A CG  
638 O OD1 . ASN A 80  ? 0.6263 0.6373 0.5388 0.0638  -0.0638 -0.0367 1873 ASN A OD1 
639 N ND2 . ASN A 80  ? 0.5602 0.5952 0.4922 0.0369  -0.0372 -0.0297 1873 ASN A ND2 
640 N N   . GLU A 81  ? 0.7364 0.6435 0.5983 0.0273  -0.0519 -0.0096 1874 GLU A N   
641 C CA  . GLU A 81  ? 0.7214 0.6126 0.5812 0.0171  -0.0510 -0.0086 1874 GLU A CA  
642 C C   . GLU A 81  ? 0.5774 0.5058 0.4668 0.0177  -0.0464 -0.0182 1874 GLU A C   
643 O O   . GLU A 81  ? 0.5462 0.5009 0.4511 0.0317  -0.0482 -0.0290 1874 GLU A O   
644 C CB  . GLU A 81  ? 0.8109 0.6543 0.6419 0.0286  -0.0666 -0.0113 1874 GLU A CB  
645 C CG  . GLU A 81  ? 1.0039 0.8016 0.7972 0.0278  -0.0744 0.0005  1874 GLU A CG  
646 C CD  . GLU A 81  ? 1.1443 0.9117 0.9164 0.0012  -0.0666 0.0144  1874 GLU A CD  
647 O OE1 . GLU A 81  ? 1.1374 0.9324 0.9325 -0.0171 -0.0530 0.0158  1874 GLU A OE1 
648 O OE2 . GLU A 81  ? 1.2492 0.9655 0.9820 -0.0021 -0.0748 0.0245  1874 GLU A OE2 
649 N N   . ASP A 82  ? 0.5940 0.5249 0.4899 0.0006  -0.0410 -0.0139 1875 ASP A N   
650 C CA  . ASP A 82  ? 0.5549 0.5160 0.4714 -0.0018 -0.0383 -0.0206 1875 ASP A CA  
651 C C   . ASP A 82  ? 0.6476 0.6029 0.5567 0.0136  -0.0459 -0.0360 1875 ASP A C   
652 O O   . ASP A 82  ? 0.5937 0.5796 0.5175 0.0161  -0.0421 -0.0442 1875 ASP A O   
653 C CB  . ASP A 82  ? 0.4777 0.4380 0.3987 -0.0225 -0.0360 -0.0132 1875 ASP A CB  
654 C CG  . ASP A 82  ? 0.5150 0.4916 0.4528 -0.0359 -0.0261 -0.0007 1875 ASP A CG  
655 O OD1 . ASP A 82  ? 0.5042 0.5085 0.4609 -0.0314 -0.0192 0.0006  1875 ASP A OD1 
656 O OD2 . ASP A 82  ? 0.4899 0.4518 0.4229 -0.0516 -0.0245 0.0068  1875 ASP A OD2 
657 N N   . ASP A 83  ? 0.6708 0.5861 0.5565 0.0244  -0.0559 -0.0407 1876 ASP A N   
658 C CA  . ASP A 83  ? 0.7048 0.6137 0.5859 0.0428  -0.0624 -0.0584 1876 ASP A CA  
659 C C   . ASP A 83  ? 0.6620 0.5801 0.5500 0.0678  -0.0681 -0.0670 1876 ASP A C   
660 O O   . ASP A 83  ? 0.6768 0.5934 0.5662 0.0870  -0.0732 -0.0838 1876 ASP A O   
661 C CB  . ASP A 83  ? 0.8209 0.6762 0.6733 0.0414  -0.0719 -0.0613 1876 ASP A CB  
662 C CG  . ASP A 83  ? 0.9273 0.7351 0.7546 0.0399  -0.0800 -0.0483 1876 ASP A CG  
663 O OD1 . ASP A 83  ? 0.9139 0.7316 0.7443 0.0419  -0.0786 -0.0384 1876 ASP A OD1 
664 O OD2 . ASP A 83  ? 0.9712 0.7289 0.7720 0.0349  -0.0879 -0.0479 1876 ASP A OD2 
665 N N   . SER A 84  ? 0.6609 0.5912 0.5549 0.0685  -0.0677 -0.0578 1877 SER A N   
666 C CA  . SER A 84  ? 0.5948 0.5442 0.5010 0.0903  -0.0746 -0.0669 1877 SER A CA  
667 C C   . SER A 84  ? 0.5652 0.5700 0.5031 0.0923  -0.0645 -0.0797 1877 SER A C   
668 O O   . SER A 84  ? 0.5572 0.5833 0.5041 0.0750  -0.0525 -0.0770 1877 SER A O   
669 C CB  . SER A 84  ? 0.5525 0.4999 0.4524 0.0872  -0.0772 -0.0543 1877 SER A CB  
670 O OG  . SER A 84  ? 0.5629 0.5447 0.4807 0.0700  -0.0631 -0.0485 1877 SER A OG  
671 N N   . GLU A 85  ? 0.6010 0.6298 0.5562 0.1128  -0.0703 -0.0931 1878 GLU A N   
672 C CA  . GLU A 85  ? 0.6296 0.7139 0.6154 0.1121  -0.0592 -0.1057 1878 GLU A CA  
673 C C   . GLU A 85  ? 0.6085 0.7193 0.6056 0.0921  -0.0494 -0.0942 1878 GLU A C   
674 O O   . GLU A 85  ? 0.6306 0.7678 0.6387 0.0773  -0.0365 -0.0945 1878 GLU A O   
675 C CB  . GLU A 85  ? 0.6838 0.7942 0.6917 0.1375  -0.0680 -0.1226 1878 GLU A CB  
676 C CG  . GLU A 85  ? 0.8336 0.9251 0.8380 0.1615  -0.0757 -0.1393 1878 GLU A CG  
677 C CD  . GLU A 85  ? 0.9736 1.0864 0.9844 0.1563  -0.0596 -0.1545 1878 GLU A CD  
678 O OE1 . GLU A 85  ? 1.0503 1.1335 1.0470 0.1689  -0.0629 -0.1660 1878 GLU A OE1 
679 O OE2 . GLU A 85  ? 0.9874 1.1430 1.0136 0.1387  -0.0440 -0.1550 1878 GLU A OE2 
680 N N   . VAL A 86  ? 0.5539 0.6542 0.5452 0.0914  -0.0560 -0.0842 1879 VAL A N   
681 C CA  . VAL A 86  ? 0.4939 0.6129 0.4939 0.0740  -0.0469 -0.0752 1879 VAL A CA  
682 C C   . VAL A 86  ? 0.4961 0.6015 0.4882 0.0547  -0.0364 -0.0625 1879 VAL A C   
683 O O   . VAL A 86  ? 0.4817 0.6091 0.4874 0.0412  -0.0262 -0.0591 1879 VAL A O   
684 C CB  . VAL A 86  ? 0.5608 0.6659 0.5494 0.0773  -0.0561 -0.0689 1879 VAL A CB  
685 C CG1 . VAL A 86  ? 0.3532 0.4645 0.3438 0.0587  -0.0452 -0.0595 1879 VAL A CG1 
686 C CG2 . VAL A 86  ? 0.4751 0.6068 0.4800 0.0940  -0.0679 -0.0816 1879 VAL A CG2 
687 N N   . GLY A 87  ? 0.4969 0.5653 0.4676 0.0529  -0.0399 -0.0551 1880 GLY A N   
688 C CA  . GLY A 87  ? 0.4600 0.5204 0.4283 0.0350  -0.0319 -0.0438 1880 GLY A CA  
689 C C   . GLY A 87  ? 0.5631 0.6429 0.5412 0.0281  -0.0265 -0.0481 1880 GLY A C   
690 O O   . GLY A 87  ? 0.5194 0.6116 0.5069 0.0141  -0.0199 -0.0397 1880 GLY A O   
691 N N   . LYS A 88  ? 0.5768 0.6584 0.5513 0.0385  -0.0298 -0.0616 1881 LYS A N   
692 C CA  . LYS A 88  ? 0.5294 0.6284 0.5062 0.0306  -0.0238 -0.0671 1881 LYS A CA  
693 C C   . LYS A 88  ? 0.5296 0.6673 0.5248 0.0233  -0.0145 -0.0673 1881 LYS A C   
694 O O   . LYS A 88  ? 0.5503 0.6980 0.5452 0.0086  -0.0093 -0.0608 1881 LYS A O   
695 C CB  . LYS A 88  ? 0.4823 0.5746 0.4498 0.0448  -0.0269 -0.0851 1881 LYS A CB  
696 C CG  . LYS A 88  ? 0.5930 0.6398 0.5368 0.0463  -0.0359 -0.0844 1881 LYS A CG  
697 C CD  . LYS A 88  ? 0.7444 0.7819 0.6779 0.0602  -0.0378 -0.1048 1881 LYS A CD  
698 C CE  . LYS A 88  ? 0.8228 0.8683 0.7684 0.0868  -0.0423 -0.1193 1881 LYS A CE  
699 N NZ  . LYS A 88  ? 0.8977 0.9341 0.8366 0.1037  -0.0430 -0.1420 1881 LYS A NZ  
700 N N   . ALA A 89  ? 0.4833 0.6415 0.4934 0.0322  -0.0138 -0.0739 1882 ALA A N   
701 C CA  . ALA A 89  ? 0.4810 0.6725 0.5078 0.0217  -0.0050 -0.0733 1882 ALA A CA  
702 C C   . ALA A 89  ? 0.4874 0.6704 0.5160 0.0072  -0.0025 -0.0562 1882 ALA A C   
703 O O   . ALA A 89  ? 0.5053 0.7028 0.5394 -0.0063 0.0041  -0.0508 1882 ALA A O   
704 C CB  . ALA A 89  ? 0.4394 0.6555 0.4840 0.0327  -0.0069 -0.0847 1882 ALA A CB  
705 N N   . GLY A 90  ? 0.4683 0.6267 0.4913 0.0097  -0.0073 -0.0478 1883 GLY A N   
706 C CA  . GLY A 90  ? 0.4422 0.5946 0.4708 -0.0009 -0.0035 -0.0347 1883 GLY A CA  
707 C C   . GLY A 90  ? 0.3813 0.5286 0.4089 -0.0118 -0.0026 -0.0241 1883 GLY A C   
708 O O   . GLY A 90  ? 0.3622 0.5145 0.3994 -0.0205 0.0006  -0.0150 1883 GLY A O   
709 N N   . HIS A 91  ? 0.3519 0.4870 0.3673 -0.0112 -0.0073 -0.0251 1884 HIS A N   
710 C CA  . HIS A 91  ? 0.4150 0.5483 0.4290 -0.0225 -0.0096 -0.0160 1884 HIS A CA  
711 C C   . HIS A 91  ? 0.3932 0.5444 0.4053 -0.0304 -0.0072 -0.0159 1884 HIS A C   
712 O O   . HIS A 91  ? 0.4661 0.6195 0.4823 -0.0402 -0.0091 -0.0037 1884 HIS A O   
713 C CB  . HIS A 91  ? 0.4144 0.5293 0.4126 -0.0224 -0.0161 -0.0196 1884 HIS A CB  
714 C CG  . HIS A 91  ? 0.4835 0.5778 0.4812 -0.0220 -0.0181 -0.0143 1884 HIS A CG  
715 N ND1 . HIS A 91  ? 0.4858 0.5833 0.4994 -0.0285 -0.0151 -0.0028 1884 HIS A ND1 
716 C CD2 . HIS A 91  ? 0.5239 0.5932 0.5059 -0.0167 -0.0220 -0.0189 1884 HIS A CD2 
717 C CE1 . HIS A 91  ? 0.4470 0.5260 0.4542 -0.0296 -0.0148 -0.0007 1884 HIS A CE1 
718 N NE2 . HIS A 91  ? 0.5178 0.5764 0.5036 -0.0233 -0.0199 -0.0091 1884 HIS A NE2 
719 N N   . ILE A 92  ? 0.4140 0.5786 0.4200 -0.0263 -0.0029 -0.0293 1885 ILE A N   
720 C CA  . ILE A 92  ? 0.4604 0.6442 0.4619 -0.0369 0.0030  -0.0297 1885 ILE A CA  
721 C C   . ILE A 92  ? 0.4687 0.6593 0.4834 -0.0445 0.0067  -0.0193 1885 ILE A C   
722 O O   . ILE A 92  ? 0.3991 0.5895 0.4082 -0.0575 0.0065  -0.0077 1885 ILE A O   
723 C CB  . ILE A 92  ? 0.4481 0.6515 0.4465 -0.0300 0.0099  -0.0492 1885 ILE A CB  
724 C CG1 . ILE A 92  ? 0.4213 0.6125 0.4015 -0.0241 0.0065  -0.0600 1885 ILE A CG1 
725 C CG2 . ILE A 92  ? 0.4398 0.6681 0.4365 -0.0440 0.0201  -0.0497 1885 ILE A CG2 
726 C CD1 . ILE A 92  ? 0.4324 0.6402 0.4149 -0.0102 0.0125  -0.0825 1885 ILE A CD1 
727 N N   . MET A 93  ? 0.4148 0.6073 0.4441 -0.0371 0.0087  -0.0231 1886 MET A N   
728 C CA  . MET A 93  ? 0.3858 0.5805 0.4261 -0.0448 0.0122  -0.0160 1886 MET A CA  
729 C C   . MET A 93  ? 0.4487 0.6234 0.4940 -0.0474 0.0079  -0.0002 1886 MET A C   
730 O O   . MET A 93  ? 0.4989 0.6691 0.5468 -0.0565 0.0085  0.0098  1886 MET A O   
731 C CB  . MET A 93  ? 0.3424 0.5443 0.3942 -0.0370 0.0140  -0.0262 1886 MET A CB  
732 C CG  . MET A 93  ? 0.4243 0.6545 0.4807 -0.0350 0.0179  -0.0420 1886 MET A CG  
733 S SD  . MET A 93  ? 0.5366 0.7896 0.5900 -0.0553 0.0281  -0.0410 1886 MET A SD  
734 C CE  . MET A 93  ? 0.4120 0.6513 0.4711 -0.0703 0.0294  -0.0280 1886 MET A CE  
735 N N   . ARG A 94  ? 0.4432 0.6060 0.4912 -0.0395 0.0036  0.0020  1887 ARG A N   
736 C CA  . ARG A 94  ? 0.4251 0.5765 0.4850 -0.0403 0.0005  0.0146  1887 ARG A CA  
737 C C   . ARG A 94  ? 0.3908 0.5418 0.4466 -0.0489 -0.0069 0.0269  1887 ARG A C   
738 O O   . ARG A 94  ? 0.4366 0.5814 0.5023 -0.0515 -0.0101 0.0385  1887 ARG A O   
739 C CB  . ARG A 94  ? 0.2920 0.4356 0.3557 -0.0334 -0.0004 0.0132  1887 ARG A CB  
740 C CG  . ARG A 94  ? 0.2859 0.4258 0.3690 -0.0329 -0.0009 0.0231  1887 ARG A CG  
741 C CD  . ARG A 94  ? 0.3228 0.4587 0.4074 -0.0313 0.0000  0.0217  1887 ARG A CD  
742 N NE  . ARG A 94  ? 0.3844 0.5170 0.4515 -0.0346 -0.0064 0.0185  1887 ARG A NE  
743 C CZ  . ARG A 94  ? 0.4479 0.5843 0.5136 -0.0418 -0.0152 0.0238  1887 ARG A CZ  
744 N NH1 . ARG A 94  ? 0.3344 0.4797 0.4167 -0.0453 -0.0206 0.0346  1887 ARG A NH1 
745 N NH2 . ARG A 94  ? 0.4077 0.5368 0.4542 -0.0448 -0.0202 0.0179  1887 ARG A NH2 
746 N N   . ARG A 95  ? 0.3692 0.5243 0.4085 -0.0529 -0.0112 0.0242  1888 ARG A N   
747 C CA  . ARG A 95  ? 0.4175 0.5716 0.4466 -0.0628 -0.0204 0.0358  1888 ARG A CA  
748 C C   . ARG A 95  ? 0.4600 0.6147 0.4785 -0.0728 -0.0179 0.0426  1888 ARG A C   
749 O O   . ARG A 95  ? 0.4471 0.5930 0.4642 -0.0788 -0.0268 0.0584  1888 ARG A O   
750 C CB  . ARG A 95  ? 0.4005 0.5567 0.4082 -0.0666 -0.0243 0.0283  1888 ARG A CB  
751 C CG  . ARG A 95  ? 0.4286 0.5781 0.4438 -0.0624 -0.0305 0.0266  1888 ARG A CG  
752 C CD  . ARG A 95  ? 0.4870 0.6328 0.4781 -0.0687 -0.0368 0.0198  1888 ARG A CD  
753 N NE  . ARG A 95  ? 0.5087 0.6541 0.4823 -0.0634 -0.0282 0.0020  1888 ARG A NE  
754 C CZ  . ARG A 95  ? 0.4949 0.6291 0.4666 -0.0543 -0.0268 -0.0097 1888 ARG A CZ  
755 N NH1 . ARG A 95  ? 0.4285 0.5503 0.4112 -0.0532 -0.0315 -0.0047 1888 ARG A NH1 
756 N NH2 . ARG A 95  ? 0.4560 0.5914 0.4153 -0.0463 -0.0206 -0.0265 1888 ARG A NH2 
757 N N   . PHE A 96  ? 0.4645 0.6294 0.4765 -0.0753 -0.0066 0.0313  1889 PHE A N   
758 C CA  . PHE A 96  ? 0.4909 0.6568 0.4931 -0.0887 -0.0018 0.0373  1889 PHE A CA  
759 C C   . PHE A 96  ? 0.5374 0.6855 0.5551 -0.0882 -0.0049 0.0497  1889 PHE A C   
760 O O   . PHE A 96  ? 0.5572 0.6909 0.5643 -0.0987 -0.0102 0.0651  1889 PHE A O   
761 C CB  . PHE A 96  ? 0.4796 0.6667 0.4812 -0.0912 0.0116  0.0204  1889 PHE A CB  
762 C CG  . PHE A 96  ? 0.5549 0.7458 0.5474 -0.1092 0.0190  0.0256  1889 PHE A CG  
763 C CD1 . PHE A 96  ? 0.5819 0.7804 0.5477 -0.1258 0.0234  0.0285  1889 PHE A CD1 
764 C CD2 . PHE A 96  ? 0.5313 0.7160 0.5386 -0.1122 0.0221  0.0273  1889 PHE A CD2 
765 C CE1 . PHE A 96  ? 0.5795 0.7798 0.5336 -0.1464 0.0316  0.0348  1889 PHE A CE1 
766 C CE2 . PHE A 96  ? 0.5967 0.7812 0.5940 -0.1325 0.0288  0.0328  1889 PHE A CE2 
767 C CZ  . PHE A 96  ? 0.6349 0.8275 0.6058 -0.1503 0.0340  0.0374  1889 PHE A CZ  
768 N N   . PHE A 97  ? 0.4833 0.6285 0.5227 -0.0762 -0.0018 0.0430  1890 PHE A N   
769 C CA  . PHE A 97  ? 0.4422 0.5685 0.4957 -0.0743 -0.0029 0.0511  1890 PHE A CA  
770 C C   . PHE A 97  ? 0.4440 0.5556 0.5067 -0.0690 -0.0151 0.0670  1890 PHE A C   
771 O O   . PHE A 97  ? 0.5308 0.6225 0.5938 -0.0723 -0.0208 0.0798  1890 PHE A O   
772 C CB  . PHE A 97  ? 0.3827 0.5091 0.4531 -0.0632 0.0039  0.0385  1890 PHE A CB  
773 C CG  . PHE A 97  ? 0.3736 0.4784 0.4583 -0.0589 0.0037  0.0437  1890 PHE A CG  
774 C CD1 . PHE A 97  ? 0.4204 0.5112 0.5007 -0.0686 0.0069  0.0442  1890 PHE A CD1 
775 C CD2 . PHE A 97  ? 0.3825 0.4808 0.4860 -0.0459 0.0009  0.0471  1890 PHE A CD2 
776 C CE1 . PHE A 97  ? 0.4949 0.5598 0.5865 -0.0634 0.0063  0.0472  1890 PHE A CE1 
777 C CE2 . PHE A 97  ? 0.4078 0.4863 0.5265 -0.0393 0.0019  0.0493  1890 PHE A CE2 
778 C CZ  . PHE A 97  ? 0.4826 0.5414 0.5939 -0.0470 0.0041  0.0490  1890 PHE A CZ  
779 N N   . GLU A 98  ? 0.4842 0.6048 0.5563 -0.0607 -0.0204 0.0663  1891 GLU A N   
780 C CA  . GLU A 98  ? 0.5512 0.6661 0.6400 -0.0547 -0.0331 0.0798  1891 GLU A CA  
781 C C   . GLU A 98  ? 0.6012 0.7063 0.6705 -0.0651 -0.0468 0.0968  1891 GLU A C   
782 O O   . GLU A 98  ? 0.6492 0.7381 0.7288 -0.0612 -0.0575 0.1111  1891 GLU A O   
783 C CB  . GLU A 98  ? 0.5970 0.7275 0.6973 -0.0493 -0.0361 0.0752  1891 GLU A CB  
784 C CG  . GLU A 98  ? 0.6609 0.7960 0.7831 -0.0386 -0.0251 0.0642  1891 GLU A CG  
785 C CD  . GLU A 98  ? 0.7940 0.9421 0.9261 -0.0377 -0.0281 0.0622  1891 GLU A CD  
786 O OE1 . GLU A 98  ? 0.8557 1.0100 0.9856 -0.0434 -0.0413 0.0702  1891 GLU A OE1 
787 O OE2 . GLU A 98  ? 0.7966 0.9472 0.9357 -0.0334 -0.0178 0.0529  1891 GLU A OE2 
788 N N   . SER A 99  ? 0.5546 0.6673 0.5935 -0.0781 -0.0468 0.0952  1892 SER A N   
789 C CA  . SER A 99  ? 0.6670 0.7691 0.6787 -0.0909 -0.0595 0.1117  1892 SER A CA  
790 C C   . SER A 99  ? 0.7548 0.8349 0.7533 -0.1003 -0.0569 0.1221  1892 SER A C   
791 O O   . SER A 99  ? 0.8245 0.8824 0.8159 -0.1027 -0.0720 0.1418  1892 SER A O   
792 C CB  . SER A 99  ? 0.6945 0.8101 0.6730 -0.1035 -0.0564 0.1040  1892 SER A CB  
793 O OG  . SER A 99  ? 0.7886 0.9108 0.7504 -0.1131 -0.0390 0.0930  1892 SER A OG  
794 N N   . ARG A 100 ? 0.6893 0.7740 0.6845 -0.1062 -0.0395 0.1096  1893 ARG A N   
795 C CA  . ARG A 100 ? 0.7191 0.7826 0.7008 -0.1196 -0.0357 0.1182  1893 ARG A CA  
796 C C   . ARG A 100 ? 0.7077 0.7420 0.7124 -0.1077 -0.0437 0.1279  1893 ARG A C   
797 O O   . ARG A 100 ? 0.7477 0.7505 0.7378 -0.1156 -0.0527 0.1456  1893 ARG A O   
798 C CB  . ARG A 100 ? 0.7250 0.8066 0.7061 -0.1282 -0.0162 0.1000  1893 ARG A CB  
799 C CG  . ARG A 100 ? 0.8032 0.8713 0.7624 -0.1511 -0.0095 0.1073  1893 ARG A CG  
800 C CD  . ARG A 100 ? 0.8646 0.9353 0.7844 -0.1715 -0.0102 0.1179  1893 ARG A CD  
801 N NE  . ARG A 100 ? 0.9420 1.0109 0.8410 -0.1976 0.0029  0.1197  1893 ARG A NE  
802 C CZ  . ARG A 100 ? 1.0399 1.0709 0.9217 -0.2129 -0.0025 0.1390  1893 ARG A CZ  
803 N NH1 . ARG A 100 ? 1.1109 1.1026 0.9957 -0.2007 -0.0220 0.1577  1893 ARG A NH1 
804 N NH2 . ARG A 100 ? 1.0372 1.0696 0.9001 -0.2405 0.0115  0.1394  1893 ARG A NH2 
805 N N   . TRP A 101 ? 0.6323 0.6740 0.6708 -0.0885 -0.0404 0.1162  1894 TRP A N   
806 C CA  . TRP A 101 ? 0.6600 0.6765 0.7230 -0.0743 -0.0454 0.1210  1894 TRP A CA  
807 C C   . TRP A 101 ? 0.7635 0.7649 0.8338 -0.0654 -0.0665 0.1409  1894 TRP A C   
808 O O   . TRP A 101 ? 0.8017 0.7712 0.8806 -0.0582 -0.0749 0.1515  1894 TRP A O   
809 C CB  . TRP A 101 ? 0.6386 0.6712 0.7328 -0.0571 -0.0350 0.1027  1894 TRP A CB  
810 C CG  . TRP A 101 ? 0.6859 0.6955 0.8050 -0.0422 -0.0348 0.1015  1894 TRP A CG  
811 C CD1 . TRP A 101 ? 0.7178 0.7262 0.8677 -0.0232 -0.0429 0.1059  1894 TRP A CD1 
812 C CD2 . TRP A 101 ? 0.6794 0.6652 0.7964 -0.0448 -0.0254 0.0930  1894 TRP A CD2 
813 N NE1 . TRP A 101 ? 0.7422 0.7263 0.9090 -0.0117 -0.0377 0.0997  1894 TRP A NE1 
814 C CE2 . TRP A 101 ? 0.7243 0.6912 0.8686 -0.0255 -0.0275 0.0918  1894 TRP A CE2 
815 C CE3 . TRP A 101 ? 0.7048 0.6853 0.8012 -0.0622 -0.0156 0.0851  1894 TRP A CE3 
816 C CZ2 . TRP A 101 ? 0.7798 0.7171 0.9264 -0.0231 -0.0200 0.0823  1894 TRP A CZ2 
817 C CZ3 . TRP A 101 ? 0.7762 0.7294 0.8760 -0.0619 -0.0098 0.0769  1894 TRP A CZ3 
818 C CH2 . TRP A 101 ? 0.7823 0.7113 0.9045 -0.0425 -0.0120 0.0753  1894 TRP A CH2 
819 N N   . GLU A 102 ? 0.8335 0.8560 0.9010 -0.0651 -0.0769 0.1458  1895 GLU A N   
820 C CA  . GLU A 102 ? 0.9562 0.9706 1.0342 -0.0560 -0.1003 0.1643  1895 GLU A CA  
821 C C   . GLU A 102 ? 1.0610 1.0483 1.0977 -0.0724 -0.1158 0.1866  1895 GLU A C   
822 O O   . GLU A 102 ? 1.0997 1.0627 1.1421 -0.0639 -0.1367 0.2057  1895 GLU A O   
823 C CB  . GLU A 102 ? 1.0008 1.0497 1.0947 -0.0506 -0.1068 0.1595  1895 GLU A CB  
824 C CG  . GLU A 102 ? 1.0282 1.1002 1.1646 -0.0344 -0.0945 0.1420  1895 GLU A CG  
825 C CD  . GLU A 102 ? 1.0534 1.1564 1.2071 -0.0320 -0.1025 0.1395  1895 GLU A CD  
826 O OE1 . GLU A 102 ? 1.0917 1.1993 1.2589 -0.0277 -0.1241 0.1535  1895 GLU A OE1 
827 O OE2 . GLU A 102 ? 1.0232 1.1448 1.1766 -0.0353 -0.0888 0.1240  1895 GLU A OE2 
828 N N   . GLU A 103 ? 1.1327 1.1234 1.1273 -0.0954 -0.1060 0.1850  1896 GLU A N   
829 C CA  . GLU A 103 ? 1.2636 1.2246 1.2123 -0.1154 -0.1161 0.2063  1896 GLU A CA  
830 C C   . GLU A 103 ? 1.2590 1.1836 1.1992 -0.1235 -0.1084 0.2116  1896 GLU A C   
831 O O   . GLU A 103 ? 1.3105 1.2206 1.2099 -0.1488 -0.1013 0.2187  1896 GLU A O   
832 C CB  . GLU A 103 ? 1.3699 1.3510 1.2756 -0.1384 -0.1071 0.2016  1896 GLU A CB  
833 C CG  . GLU A 103 ? 1.4124 1.4178 1.3149 -0.1488 -0.0787 0.1784  1896 GLU A CG  
834 C CD  . GLU A 103 ? 1.4846 1.5083 1.3442 -0.1704 -0.0700 0.1740  1896 GLU A CD  
835 O OE1 . GLU A 103 ? 1.5668 1.5717 1.3848 -0.1868 -0.0815 0.1931  1896 GLU A OE1 
836 O OE2 . GLU A 103 ? 1.4717 1.5275 1.3376 -0.1702 -0.0521 0.1511  1896 GLU A OE2 
837 N N   . PHE A 104 ? 1.1956 1.1057 1.1740 -0.1035 -0.1082 0.2066  1897 PHE A N   
838 C CA  . PHE A 104 ? 1.2071 1.0701 1.1799 -0.1066 -0.1093 0.2156  1897 PHE A CA  
839 C C   . PHE A 104 ? 1.2037 1.0460 1.2173 -0.0764 -0.1245 0.2199  1897 PHE A C   
840 O O   . PHE A 104 ? 1.2483 1.0430 1.2533 -0.0729 -0.1413 0.2391  1897 PHE A O   
841 C CB  . PHE A 104 ? 1.1589 1.0269 1.1342 -0.1174 -0.0842 0.1952  1897 PHE A CB  
842 C CG  . PHE A 104 ? 1.2586 1.0751 1.2189 -0.1287 -0.0844 0.2043  1897 PHE A CG  
843 C CD1 . PHE A 104 ? 1.2876 1.0789 1.2776 -0.1107 -0.0830 0.1951  1897 PHE A CD1 
844 C CD2 . PHE A 104 ? 1.3037 1.0945 1.2173 -0.1592 -0.0852 0.2215  1897 PHE A CD2 
845 C CE1 . PHE A 104 ? 1.3372 1.0750 1.3111 -0.1221 -0.0839 0.2022  1897 PHE A CE1 
846 C CE2 . PHE A 104 ? 1.3403 1.0788 1.2374 -0.1729 -0.0856 0.2307  1897 PHE A CE2 
847 C CZ  . PHE A 104 ? 1.3535 1.0635 1.2810 -0.1540 -0.0859 0.2209  1897 PHE A CZ  
848 N N   . TYR A 105 ? 1.1327 1.0099 1.1905 -0.0545 -0.1184 0.2019  1898 TYR A N   
849 C CA  . TYR A 105 ? 1.0887 0.9579 1.1926 -0.0243 -0.1288 0.2015  1898 TYR A CA  
850 C C   . TYR A 105 ? 1.0380 0.9409 1.1672 -0.0101 -0.1465 0.2079  1898 TYR A C   
851 O O   . TYR A 105 ? 1.0586 0.9469 1.1759 -0.0096 -0.1722 0.2304  1898 TYR A O   
852 C CB  . TYR A 105 ? 1.0389 0.9218 1.1758 -0.0113 -0.1061 0.1747  1898 TYR A CB  
853 C CG  . TYR A 105 ? 1.0682 0.9263 1.1822 -0.0274 -0.0883 0.1642  1898 TYR A CG  
854 C CD1 . TYR A 105 ? 1.1219 0.9289 1.2346 -0.0233 -0.0912 0.1677  1898 TYR A CD1 
855 C CD2 . TYR A 105 ? 1.0417 0.9275 1.1373 -0.0463 -0.0700 0.1499  1898 TYR A CD2 
856 C CE1 . TYR A 105 ? 1.1303 0.9155 1.2226 -0.0410 -0.0761 0.1571  1898 TYR A CE1 
857 C CE2 . TYR A 105 ? 1.0377 0.9071 1.1169 -0.0619 -0.0557 0.1395  1898 TYR A CE2 
858 C CZ  . TYR A 105 ? 1.0796 0.8993 1.1567 -0.0608 -0.0587 0.1431  1898 TYR A CZ  
859 O OH  . TYR A 105 ? 1.0775 0.8813 1.1384 -0.0793 -0.0456 0.1320  1898 TYR A OH  
# 
