data_9F6W
# 
_entry.id   9F6W 
# 
_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   9F6W         pdb_00009f6w 10.2210/pdb9f6w/pdb 
WWPDB D_1292138322 ?            ?                   
# 
_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             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9F6W 
_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 
# 
_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)' 'First two residues SM derive from the expression tag. E1845H/L1848S.' 
2 non-polymer syn '1-(4-ethyl-2-methyl-5-piperazin-1-ylcarbonyl-1~{H}-pyrrol-3-yl)ethanone' 263.335   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    55 ? ?             ? ? 
# 
_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-(4-ethyl-2-methyl-5-piperazin-1-ylcarbonyl-1~{H}-pyrrol-3-yl)ethanone' A1IAC 
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 
A1IAC non-polymer         . '1-(4-ethyl-2-methyl-5-piperazin-1-ylcarbonyl-1~{H}-pyrrol-3-yl)ethanone' ?                 
'C14 H21 N3 O2'  263.335 
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 1795 MET MET 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        A1IAC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IAC 
_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 A1IAC 1  1901 1901 A1IAC D14 A . 
C 3 EDO   1  1902 2001 EDO   EDO A . 
D 4 MG    1  1903 1    MG    MG  A . 
E 5 HOH   1  2001 44   HOH   HOH A . 
E 5 HOH   2  2002 24   HOH   HOH A . 
E 5 HOH   3  2003 21   HOH   HOH A . 
E 5 HOH   4  2004 49   HOH   HOH A . 
E 5 HOH   5  2005 5    HOH   HOH A . 
E 5 HOH   6  2006 31   HOH   HOH A . 
E 5 HOH   7  2007 42   HOH   HOH A . 
E 5 HOH   8  2008 4    HOH   HOH A . 
E 5 HOH   9  2009 45   HOH   HOH A . 
E 5 HOH   10 2010 40   HOH   HOH A . 
E 5 HOH   11 2011 36   HOH   HOH A . 
E 5 HOH   12 2012 58   HOH   HOH A . 
E 5 HOH   13 2013 34   HOH   HOH A . 
E 5 HOH   14 2014 28   HOH   HOH A . 
E 5 HOH   15 2015 16   HOH   HOH A . 
E 5 HOH   16 2016 19   HOH   HOH A . 
E 5 HOH   17 2017 7    HOH   HOH A . 
E 5 HOH   18 2018 33   HOH   HOH A . 
E 5 HOH   19 2019 32   HOH   HOH A . 
E 5 HOH   20 2020 43   HOH   HOH A . 
E 5 HOH   21 2021 56   HOH   HOH A . 
E 5 HOH   22 2022 3    HOH   HOH A . 
E 5 HOH   23 2023 11   HOH   HOH A . 
E 5 HOH   24 2024 1    HOH   HOH A . 
E 5 HOH   25 2025 46   HOH   HOH A . 
E 5 HOH   26 2026 18   HOH   HOH A . 
E 5 HOH   27 2027 39   HOH   HOH A . 
E 5 HOH   28 2028 2    HOH   HOH A . 
E 5 HOH   29 2029 15   HOH   HOH A . 
E 5 HOH   30 2030 23   HOH   HOH A . 
E 5 HOH   31 2031 10   HOH   HOH A . 
E 5 HOH   32 2032 48   HOH   HOH A . 
E 5 HOH   33 2033 35   HOH   HOH A . 
E 5 HOH   34 2034 8    HOH   HOH A . 
E 5 HOH   35 2035 14   HOH   HOH A . 
E 5 HOH   36 2036 50   HOH   HOH A . 
E 5 HOH   37 2037 51   HOH   HOH A . 
E 5 HOH   38 2038 25   HOH   HOH A . 
E 5 HOH   39 2039 22   HOH   HOH A . 
E 5 HOH   40 2040 9    HOH   HOH A . 
E 5 HOH   41 2041 12   HOH   HOH A . 
E 5 HOH   42 2042 27   HOH   HOH A . 
E 5 HOH   43 2043 26   HOH   HOH A . 
E 5 HOH   44 2044 13   HOH   HOH A . 
E 5 HOH   45 2045 6    HOH   HOH A . 
E 5 HOH   46 2046 52   HOH   HOH A . 
E 5 HOH   47 2047 57   HOH   HOH A . 
E 5 HOH   48 2048 37   HOH   HOH A . 
E 5 HOH   49 2049 38   HOH   HOH A . 
E 5 HOH   50 2050 47   HOH   HOH A . 
E 5 HOH   51 2051 29   HOH   HOH A . 
E 5 HOH   52 2052 17   HOH   HOH A . 
E 5 HOH   53 2053 30   HOH   HOH A . 
E 5 HOH   54 2054 54   HOH   HOH A . 
E 5 HOH   55 2055 55   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                     9F6W 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     93.753 
_cell.length_a_esd                 ? 
_cell.length_b                     93.753 
_cell.length_b_esd                 ? 
_cell.length_c                     33.229 
_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                         9F6W 
_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                   9F6W 
_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             3.41 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          63.93 
_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                                       9F6W 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.20 
_reflns.d_resolution_low                               30.753 
_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                                     8667 
_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                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                18.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.99 
_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                                0.203 
_reflns.pdbx_Rpim_I_all                                0.047 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_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                              0.198 
_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                                    2.20 
_reflns_shell.d_res_low                                     2.27 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           12232 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             726 
_reflns_shell.percent_possible_obs                          98.6 
_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                               16.8 
_reflns_shell.pdbx_chi_squared                              1.04 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.4 
_reflns_shell.pdbx_Rrim_I_all                               1.637 
_reflns_shell.pdbx_Rpim_I_all                               0.396 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.846 
_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                                  1.587 
_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                                 9F6W 
_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                            2.200 
_refine.ls_d_res_low                             30.753 
_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                     8655 
_refine.ls_number_reflns_R_free                  431 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.14 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1707 
_refine.ls_R_factor_R_free                       0.1867 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1696 
_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                          1.34 
_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                 23.82 
_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                            0.18 
_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.pdbx_number_atoms_protein        860 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.number_atoms_solvent             55 
_refine_hist.number_atoms_total               939 
_refine_hist.d_res_high                       2.200 
_refine_hist.d_res_low                        30.753 
# 
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' ? 0.006  ? 913  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.791  ? 1230 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.921 ? 541  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042  ? 120  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 162  ? 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' 2.2002 2.5185 . . 142 2676 99.00  . . . . 0.1890 . . . . . . . . . . . 0.2428 
'X-RAY DIFFRACTION' 2.5185 3.1725 . . 115 2758 99.00  . . . . 0.1968 . . . . . . . . . . . 0.2175 
'X-RAY DIFFRACTION' 3.1725 30.753 . . 174 2790 100.00 . . . . 0.1540 . . . . . . . . . . . 0.1692 
# 
_struct.entry_id                     9F6W 
_struct.title                        'BAZ2A bromodomain in complex with acetylpyrrole derivative compound 1-TND14' 
_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        9F6W 
_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              9F6W 
_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 9F6W SER A 1  ? UNP Q9UIF9 ?   ?    'expression tag'      1794 1 
1 9F6W MET A 2  ? UNP Q9UIF9 ?   ?    'expression tag'      1795 2 
1 9F6W HIS A 52 ? UNP Q9UIF9 GLU 1845 'engineered mutation' 1845 3 
1 9F6W SER A 55 ? UNP Q9UIF9 LEU 1848 'engineered mutation' 1848 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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)' 860  ? 
1 MORE         -2   ? 
1 'SSA (A^2)'  6220 ? 
# 
_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 MET A 2  ? SER A 18  ? MET A 1795 SER A 1811 1 ? 17 
HELX_P HELX_P2 AA2 HIS A 19 ? TRP A 23  ? HIS A 1812 TRP A 1816 5 ? 5  
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 2001 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc2 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 1903 A HOH 2009 6_554 ? ? ? ? ? ? ? 2.304 ? ? 
metalc3 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 1903 A HOH 2021 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc4 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 1903 A HOH 2025 6_554 ? ? ? ? ? ? ? 2.432 ? ? 
metalc5 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 1903 A HOH 2047 1_555 ? ? ? ? ? ? ? 2.752 ? ? 
metalc6 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 1903 A HOH 2050 1_555 ? ? ? ? ? ? ? 2.305 ? ? 
# 
_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 2001 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2009 ? 6_554 76.8  ? 
2  O ? E HOH . ? A HOH 2001 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2021 ? 1_555 87.1  ? 
3  O ? E HOH . ? A HOH 2009 ? 6_554 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2021 ? 1_555 163.9 ? 
4  O ? E HOH . ? A HOH 2001 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2025 ? 6_554 82.4  ? 
5  O ? E HOH . ? A HOH 2009 ? 6_554 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2025 ? 6_554 91.5  ? 
6  O ? E HOH . ? A HOH 2021 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2025 ? 6_554 87.6  ? 
7  O ? E HOH . ? A HOH 2001 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2047 ? 1_555 164.6 ? 
8  O ? E HOH . ? A HOH 2009 ? 6_554 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2047 ? 1_555 107.5 ? 
9  O ? E HOH . ? A HOH 2021 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2047 ? 1_555 88.4  ? 
10 O ? E HOH . ? A HOH 2025 ? 6_554 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2047 ? 1_555 82.7  ? 
11 O ? E HOH . ? A HOH 2001 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2050 ? 1_555 78.0  ? 
12 O ? E HOH . ? A HOH 2009 ? 6_554 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2050 ? 1_555 85.8  ? 
13 O ? E HOH . ? A HOH 2021 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2050 ? 1_555 89.6  ? 
14 O ? E HOH . ? A HOH 2025 ? 6_554 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2050 ? 1_555 160.3 ? 
15 O ? E HOH . ? A HOH 2047 ? 1_555 MG ? D MG . ? A MG 1903 ? 1_555 O ? E HOH . ? A HOH 2050 ? 1_555 116.7 ? 
# 
_pdbx_entry_details.entry_id                   9F6W 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
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 -32.1776 18.9046 -9.5921  0.4650 ? -0.1385 ? 0.0617  ? 0.5328 ? 0.1307  ? 0.5165 ? 3.7124 ? 
-1.9356 ? 0.2281  ? 8.4718 ? 0.1528  ? 3.0231 ? -0.0378 ? -0.1811 ? -0.3857 ? 0.1542  ? -0.3738 ? -0.7642 ? 0.7051 ? -0.2059 ? 
0.3646  ? 
2 'X-RAY DIFFRACTION' ? refined -37.8919 36.1050 -20.5049 0.2112 ? 0.0028  ? -0.0131 ? 0.4851 ? -0.0223 ? 0.3165 ? 1.4268 ? 0.5347 
? 1.3653  ? 1.1276 ? 0.0650  ? 3.7415 ? 0.1331  ? -0.0732 ? 0.1149  ? -0.0702 ? -0.0703 ? 0.2647  ? 0.0810 ? -0.8137 ? -0.0061 ? 
3 'X-RAY DIFFRACTION' ? refined -29.3092 27.2999 -21.3216 0.2843 ? -0.0745 ? 0.0351  ? 0.3274 ? -0.0210 ? 0.3049 ? 1.9236 ? 1.1572 
? -0.8142 ? 2.8856 ? -1.5455 ? 2.3183 ? -0.1787 ? -0.0514 ? -0.3569 ? -0.3928 ? -0.0419 ? -0.3454 ? 0.3579 ? -0.1615 ? 0.2003  ? 
4 'X-RAY DIFFRACTION' ? refined -27.1113 33.7741 -9.4489  0.2130 ? -0.0645 ? -0.0135 ? 0.4583 ? -0.0236 ? 0.2713 ? 3.9705 ? 0.6184 
? 0.7066  ? 5.5590 ? -0.0874 ? 4.8195 ? 0.0096  ? -0.5929 ? -0.0737 ? 0.1636  ? -0.2314 ? -0.1864 ? 0.0702 ? -0.3662 ? 0.1308  ? 
# 
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 1795 through 1811 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1812 through 1829 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1830 through 1872 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1873 through 1898 )
;
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     SER 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      1794 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    A 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    SER 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
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 
A1IAC C12  C  N N 1   
A1IAC C16  C  N N 2   
A1IAC C18  C  N N 3   
A1IAC C19  C  N N 4   
A1IAC C01  C  N N 5   
A1IAC C02  C  N N 6   
A1IAC C03  C  Y N 7   
A1IAC C04  C  Y N 8   
A1IAC C06  C  Y N 9   
A1IAC C07  C  N N 10  
A1IAC C08  C  Y N 11  
A1IAC C09  C  N N 12  
A1IAC C11  C  N N 13  
A1IAC C15  C  N N 14  
A1IAC N05  N  Y N 15  
A1IAC N14  N  N N 16  
A1IAC N17  N  N N 17  
A1IAC O10  O  N N 18  
A1IAC O13  O  N N 19  
A1IAC H1   H  N N 20  
A1IAC H2   H  N N 21  
A1IAC H3   H  N N 22  
A1IAC H4   H  N N 23  
A1IAC H5   H  N N 24  
A1IAC H6   H  N N 25  
A1IAC H7   H  N N 26  
A1IAC H8   H  N N 27  
A1IAC H9   H  N N 28  
A1IAC H10  H  N N 29  
A1IAC H11  H  N N 30  
A1IAC H12  H  N N 31  
A1IAC H13  H  N N 32  
A1IAC H14  H  N N 33  
A1IAC H15  H  N N 34  
A1IAC H16  H  N N 35  
A1IAC H17  H  N N 36  
A1IAC H18  H  N N 37  
A1IAC H19  H  N N 38  
A1IAC H20  H  N N 39  
A1IAC H21  H  N N 40  
ALA   N    N  N N 41  
ALA   CA   C  N S 42  
ALA   C    C  N N 43  
ALA   O    O  N N 44  
ALA   CB   C  N N 45  
ALA   OXT  O  N N 46  
ALA   H    H  N N 47  
ALA   H2   H  N N 48  
ALA   HA   H  N N 49  
ALA   HB1  H  N N 50  
ALA   HB2  H  N N 51  
ALA   HB3  H  N N 52  
ALA   HXT  H  N N 53  
ARG   N    N  N N 54  
ARG   CA   C  N S 55  
ARG   C    C  N N 56  
ARG   O    O  N N 57  
ARG   CB   C  N N 58  
ARG   CG   C  N N 59  
ARG   CD   C  N N 60  
ARG   NE   N  N N 61  
ARG   CZ   C  N N 62  
ARG   NH1  N  N N 63  
ARG   NH2  N  N N 64  
ARG   OXT  O  N N 65  
ARG   H    H  N N 66  
ARG   H2   H  N N 67  
ARG   HA   H  N N 68  
ARG   HB2  H  N N 69  
ARG   HB3  H  N N 70  
ARG   HG2  H  N N 71  
ARG   HG3  H  N N 72  
ARG   HD2  H  N N 73  
ARG   HD3  H  N N 74  
ARG   HE   H  N N 75  
ARG   HH11 H  N N 76  
ARG   HH12 H  N N 77  
ARG   HH21 H  N N 78  
ARG   HH22 H  N N 79  
ARG   HXT  H  N N 80  
ASN   N    N  N N 81  
ASN   CA   C  N S 82  
ASN   C    C  N N 83  
ASN   O    O  N N 84  
ASN   CB   C  N N 85  
ASN   CG   C  N N 86  
ASN   OD1  O  N N 87  
ASN   ND2  N  N N 88  
ASN   OXT  O  N N 89  
ASN   H    H  N N 90  
ASN   H2   H  N N 91  
ASN   HA   H  N N 92  
ASN   HB2  H  N N 93  
ASN   HB3  H  N N 94  
ASN   HD21 H  N N 95  
ASN   HD22 H  N N 96  
ASN   HXT  H  N N 97  
ASP   N    N  N N 98  
ASP   CA   C  N S 99  
ASP   C    C  N N 100 
ASP   O    O  N N 101 
ASP   CB   C  N N 102 
ASP   CG   C  N N 103 
ASP   OD1  O  N N 104 
ASP   OD2  O  N N 105 
ASP   OXT  O  N N 106 
ASP   H    H  N N 107 
ASP   H2   H  N N 108 
ASP   HA   H  N N 109 
ASP   HB2  H  N N 110 
ASP   HB3  H  N N 111 
ASP   HD2  H  N N 112 
ASP   HXT  H  N N 113 
CYS   N    N  N N 114 
CYS   CA   C  N R 115 
CYS   C    C  N N 116 
CYS   O    O  N N 117 
CYS   CB   C  N N 118 
CYS   SG   S  N N 119 
CYS   OXT  O  N N 120 
CYS   H    H  N N 121 
CYS   H2   H  N N 122 
CYS   HA   H  N N 123 
CYS   HB2  H  N N 124 
CYS   HB3  H  N N 125 
CYS   HG   H  N N 126 
CYS   HXT  H  N N 127 
EDO   C1   C  N N 128 
EDO   O1   O  N N 129 
EDO   C2   C  N N 130 
EDO   O2   O  N N 131 
EDO   H11  H  N N 132 
EDO   H12  H  N N 133 
EDO   HO1  H  N N 134 
EDO   H21  H  N N 135 
EDO   H22  H  N N 136 
EDO   HO2  H  N N 137 
GLN   N    N  N N 138 
GLN   CA   C  N S 139 
GLN   C    C  N N 140 
GLN   O    O  N N 141 
GLN   CB   C  N N 142 
GLN   CG   C  N N 143 
GLN   CD   C  N N 144 
GLN   OE1  O  N N 145 
GLN   NE2  N  N N 146 
GLN   OXT  O  N N 147 
GLN   H    H  N N 148 
GLN   H2   H  N N 149 
GLN   HA   H  N N 150 
GLN   HB2  H  N N 151 
GLN   HB3  H  N N 152 
GLN   HG2  H  N N 153 
GLN   HG3  H  N N 154 
GLN   HE21 H  N N 155 
GLN   HE22 H  N N 156 
GLN   HXT  H  N N 157 
GLU   N    N  N N 158 
GLU   CA   C  N S 159 
GLU   C    C  N N 160 
GLU   O    O  N N 161 
GLU   CB   C  N N 162 
GLU   CG   C  N N 163 
GLU   CD   C  N N 164 
GLU   OE1  O  N N 165 
GLU   OE2  O  N N 166 
GLU   OXT  O  N N 167 
GLU   H    H  N N 168 
GLU   H2   H  N N 169 
GLU   HA   H  N N 170 
GLU   HB2  H  N N 171 
GLU   HB3  H  N N 172 
GLU   HG2  H  N N 173 
GLU   HG3  H  N N 174 
GLU   HE2  H  N N 175 
GLU   HXT  H  N N 176 
GLY   N    N  N N 177 
GLY   CA   C  N N 178 
GLY   C    C  N N 179 
GLY   O    O  N N 180 
GLY   OXT  O  N N 181 
GLY   H    H  N N 182 
GLY   H2   H  N N 183 
GLY   HA2  H  N N 184 
GLY   HA3  H  N N 185 
GLY   HXT  H  N N 186 
HIS   N    N  N N 187 
HIS   CA   C  N S 188 
HIS   C    C  N N 189 
HIS   O    O  N N 190 
HIS   CB   C  N N 191 
HIS   CG   C  Y N 192 
HIS   ND1  N  Y N 193 
HIS   CD2  C  Y N 194 
HIS   CE1  C  Y N 195 
HIS   NE2  N  Y N 196 
HIS   OXT  O  N N 197 
HIS   H    H  N N 198 
HIS   H2   H  N N 199 
HIS   HA   H  N N 200 
HIS   HB2  H  N N 201 
HIS   HB3  H  N N 202 
HIS   HD1  H  N N 203 
HIS   HD2  H  N N 204 
HIS   HE1  H  N N 205 
HIS   HE2  H  N N 206 
HIS   HXT  H  N N 207 
HOH   O    O  N N 208 
HOH   H1   H  N N 209 
HOH   H2   H  N N 210 
ILE   N    N  N N 211 
ILE   CA   C  N S 212 
ILE   C    C  N N 213 
ILE   O    O  N N 214 
ILE   CB   C  N S 215 
ILE   CG1  C  N N 216 
ILE   CG2  C  N N 217 
ILE   CD1  C  N N 218 
ILE   OXT  O  N N 219 
ILE   H    H  N N 220 
ILE   H2   H  N N 221 
ILE   HA   H  N N 222 
ILE   HB   H  N N 223 
ILE   HG12 H  N N 224 
ILE   HG13 H  N N 225 
ILE   HG21 H  N N 226 
ILE   HG22 H  N N 227 
ILE   HG23 H  N N 228 
ILE   HD11 H  N N 229 
ILE   HD12 H  N N 230 
ILE   HD13 H  N N 231 
ILE   HXT  H  N N 232 
LEU   N    N  N N 233 
LEU   CA   C  N S 234 
LEU   C    C  N N 235 
LEU   O    O  N N 236 
LEU   CB   C  N N 237 
LEU   CG   C  N N 238 
LEU   CD1  C  N N 239 
LEU   CD2  C  N N 240 
LEU   OXT  O  N N 241 
LEU   H    H  N N 242 
LEU   H2   H  N N 243 
LEU   HA   H  N N 244 
LEU   HB2  H  N N 245 
LEU   HB3  H  N N 246 
LEU   HG   H  N N 247 
LEU   HD11 H  N N 248 
LEU   HD12 H  N N 249 
LEU   HD13 H  N N 250 
LEU   HD21 H  N N 251 
LEU   HD22 H  N N 252 
LEU   HD23 H  N N 253 
LEU   HXT  H  N N 254 
LYS   N    N  N N 255 
LYS   CA   C  N S 256 
LYS   C    C  N N 257 
LYS   O    O  N N 258 
LYS   CB   C  N N 259 
LYS   CG   C  N N 260 
LYS   CD   C  N N 261 
LYS   CE   C  N N 262 
LYS   NZ   N  N N 263 
LYS   OXT  O  N N 264 
LYS   H    H  N N 265 
LYS   H2   H  N N 266 
LYS   HA   H  N N 267 
LYS   HB2  H  N N 268 
LYS   HB3  H  N N 269 
LYS   HG2  H  N N 270 
LYS   HG3  H  N N 271 
LYS   HD2  H  N N 272 
LYS   HD3  H  N N 273 
LYS   HE2  H  N N 274 
LYS   HE3  H  N N 275 
LYS   HZ1  H  N N 276 
LYS   HZ2  H  N N 277 
LYS   HZ3  H  N N 278 
LYS   HXT  H  N N 279 
MET   N    N  N N 280 
MET   CA   C  N S 281 
MET   C    C  N N 282 
MET   O    O  N N 283 
MET   CB   C  N N 284 
MET   CG   C  N N 285 
MET   SD   S  N N 286 
MET   CE   C  N N 287 
MET   OXT  O  N N 288 
MET   H    H  N N 289 
MET   H2   H  N N 290 
MET   HA   H  N N 291 
MET   HB2  H  N N 292 
MET   HB3  H  N N 293 
MET   HG2  H  N N 294 
MET   HG3  H  N N 295 
MET   HE1  H  N N 296 
MET   HE2  H  N N 297 
MET   HE3  H  N N 298 
MET   HXT  H  N N 299 
MG    MG   MG N N 300 
PHE   N    N  N N 301 
PHE   CA   C  N S 302 
PHE   C    C  N N 303 
PHE   O    O  N N 304 
PHE   CB   C  N N 305 
PHE   CG   C  Y N 306 
PHE   CD1  C  Y N 307 
PHE   CD2  C  Y N 308 
PHE   CE1  C  Y N 309 
PHE   CE2  C  Y N 310 
PHE   CZ   C  Y N 311 
PHE   OXT  O  N N 312 
PHE   H    H  N N 313 
PHE   H2   H  N N 314 
PHE   HA   H  N N 315 
PHE   HB2  H  N N 316 
PHE   HB3  H  N N 317 
PHE   HD1  H  N N 318 
PHE   HD2  H  N N 319 
PHE   HE1  H  N N 320 
PHE   HE2  H  N N 321 
PHE   HZ   H  N N 322 
PHE   HXT  H  N N 323 
PRO   N    N  N N 324 
PRO   CA   C  N S 325 
PRO   C    C  N N 326 
PRO   O    O  N N 327 
PRO   CB   C  N N 328 
PRO   CG   C  N N 329 
PRO   CD   C  N N 330 
PRO   OXT  O  N N 331 
PRO   H    H  N N 332 
PRO   HA   H  N N 333 
PRO   HB2  H  N N 334 
PRO   HB3  H  N N 335 
PRO   HG2  H  N N 336 
PRO   HG3  H  N N 337 
PRO   HD2  H  N N 338 
PRO   HD3  H  N N 339 
PRO   HXT  H  N N 340 
SER   N    N  N N 341 
SER   CA   C  N S 342 
SER   C    C  N N 343 
SER   O    O  N N 344 
SER   CB   C  N N 345 
SER   OG   O  N N 346 
SER   OXT  O  N N 347 
SER   H    H  N N 348 
SER   H2   H  N N 349 
SER   HA   H  N N 350 
SER   HB2  H  N N 351 
SER   HB3  H  N N 352 
SER   HG   H  N N 353 
SER   HXT  H  N N 354 
THR   N    N  N N 355 
THR   CA   C  N S 356 
THR   C    C  N N 357 
THR   O    O  N N 358 
THR   CB   C  N R 359 
THR   OG1  O  N N 360 
THR   CG2  C  N N 361 
THR   OXT  O  N N 362 
THR   H    H  N N 363 
THR   H2   H  N N 364 
THR   HA   H  N N 365 
THR   HB   H  N N 366 
THR   HG1  H  N N 367 
THR   HG21 H  N N 368 
THR   HG22 H  N N 369 
THR   HG23 H  N N 370 
THR   HXT  H  N N 371 
TRP   N    N  N N 372 
TRP   CA   C  N S 373 
TRP   C    C  N N 374 
TRP   O    O  N N 375 
TRP   CB   C  N N 376 
TRP   CG   C  Y N 377 
TRP   CD1  C  Y N 378 
TRP   CD2  C  Y N 379 
TRP   NE1  N  Y N 380 
TRP   CE2  C  Y N 381 
TRP   CE3  C  Y N 382 
TRP   CZ2  C  Y N 383 
TRP   CZ3  C  Y N 384 
TRP   CH2  C  Y N 385 
TRP   OXT  O  N N 386 
TRP   H    H  N N 387 
TRP   H2   H  N N 388 
TRP   HA   H  N N 389 
TRP   HB2  H  N N 390 
TRP   HB3  H  N N 391 
TRP   HD1  H  N N 392 
TRP   HE1  H  N N 393 
TRP   HE3  H  N N 394 
TRP   HZ2  H  N N 395 
TRP   HZ3  H  N N 396 
TRP   HH2  H  N N 397 
TRP   HXT  H  N N 398 
TYR   N    N  N N 399 
TYR   CA   C  N S 400 
TYR   C    C  N N 401 
TYR   O    O  N N 402 
TYR   CB   C  N N 403 
TYR   CG   C  Y N 404 
TYR   CD1  C  Y N 405 
TYR   CD2  C  Y N 406 
TYR   CE1  C  Y N 407 
TYR   CE2  C  Y N 408 
TYR   CZ   C  Y N 409 
TYR   OH   O  N N 410 
TYR   OXT  O  N N 411 
TYR   H    H  N N 412 
TYR   H2   H  N N 413 
TYR   HA   H  N N 414 
TYR   HB2  H  N N 415 
TYR   HB3  H  N N 416 
TYR   HD1  H  N N 417 
TYR   HD2  H  N N 418 
TYR   HE1  H  N N 419 
TYR   HE2  H  N N 420 
TYR   HH   H  N N 421 
TYR   HXT  H  N N 422 
VAL   N    N  N N 423 
VAL   CA   C  N S 424 
VAL   C    C  N N 425 
VAL   O    O  N N 426 
VAL   CB   C  N N 427 
VAL   CG1  C  N N 428 
VAL   CG2  C  N N 429 
VAL   OXT  O  N N 430 
VAL   H    H  N N 431 
VAL   H2   H  N N 432 
VAL   HA   H  N N 433 
VAL   HB   H  N N 434 
VAL   HG11 H  N N 435 
VAL   HG12 H  N N 436 
VAL   HG13 H  N N 437 
VAL   HG21 H  N N 438 
VAL   HG22 H  N N 439 
VAL   HG23 H  N N 440 
VAL   HXT  H  N N 441 
# 
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 
A1IAC C11 C09  sing N N 1   
A1IAC C09 O10  doub N N 2   
A1IAC C09 C08  sing N N 3   
A1IAC C02 C03  sing N N 4   
A1IAC C02 C01  sing N N 5   
A1IAC C18 N17  sing N N 6   
A1IAC C18 C19  sing N N 7   
A1IAC C08 C03  sing Y N 8   
A1IAC C08 C06  doub Y N 9   
A1IAC C03 C04  doub Y N 10  
A1IAC N17 C16  sing N N 11  
A1IAC C16 C15  sing N N 12  
A1IAC C06 C07  sing N N 13  
A1IAC C06 N05  sing Y N 14  
A1IAC C04 C12  sing N N 15  
A1IAC C04 N05  sing Y N 16  
A1IAC C19 N14  sing N N 17  
A1IAC C12 N14  sing N N 18  
A1IAC C12 O13  doub N N 19  
A1IAC N14 C15  sing N N 20  
A1IAC C16 H1   sing N N 21  
A1IAC C16 H2   sing N N 22  
A1IAC C18 H3   sing N N 23  
A1IAC C18 H4   sing N N 24  
A1IAC C19 H5   sing N N 25  
A1IAC C19 H6   sing N N 26  
A1IAC C01 H7   sing N N 27  
A1IAC C01 H8   sing N N 28  
A1IAC C01 H9   sing N N 29  
A1IAC C02 H10  sing N N 30  
A1IAC C02 H11  sing N N 31  
A1IAC C07 H12  sing N N 32  
A1IAC C07 H13  sing N N 33  
A1IAC C07 H14  sing N N 34  
A1IAC C11 H15  sing N N 35  
A1IAC C11 H16  sing N N 36  
A1IAC C11 H17  sing N N 37  
A1IAC C15 H18  sing N N 38  
A1IAC C15 H19  sing N N 39  
A1IAC N05 H20  sing N N 40  
A1IAC N17 H21  sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
EDO   C1  O1   sing N N 124 
EDO   C1  C2   sing N N 125 
EDO   C1  H11  sing N N 126 
EDO   C1  H12  sing N N 127 
EDO   O1  HO1  sing N N 128 
EDO   C2  O2   sing N N 129 
EDO   C2  H21  sing N N 130 
EDO   C2  H22  sing N N 131 
EDO   O2  HO2  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
PHE   N   CA   sing N N 287 
PHE   N   H    sing N N 288 
PHE   N   H2   sing N N 289 
PHE   CA  C    sing N N 290 
PHE   CA  CB   sing N N 291 
PHE   CA  HA   sing N N 292 
PHE   C   O    doub N N 293 
PHE   C   OXT  sing N N 294 
PHE   CB  CG   sing N N 295 
PHE   CB  HB2  sing N N 296 
PHE   CB  HB3  sing N N 297 
PHE   CG  CD1  doub Y N 298 
PHE   CG  CD2  sing Y N 299 
PHE   CD1 CE1  sing Y N 300 
PHE   CD1 HD1  sing N N 301 
PHE   CD2 CE2  doub Y N 302 
PHE   CD2 HD2  sing N N 303 
PHE   CE1 CZ   doub Y N 304 
PHE   CE1 HE1  sing N N 305 
PHE   CE2 CZ   sing Y N 306 
PHE   CE2 HE2  sing N N 307 
PHE   CZ  HZ   sing N N 308 
PHE   OXT HXT  sing N N 309 
PRO   N   CA   sing N N 310 
PRO   N   CD   sing N N 311 
PRO   N   H    sing N N 312 
PRO   CA  C    sing N N 313 
PRO   CA  CB   sing N N 314 
PRO   CA  HA   sing N N 315 
PRO   C   O    doub N N 316 
PRO   C   OXT  sing N N 317 
PRO   CB  CG   sing N N 318 
PRO   CB  HB2  sing N N 319 
PRO   CB  HB3  sing N N 320 
PRO   CG  CD   sing N N 321 
PRO   CG  HG2  sing N N 322 
PRO   CG  HG3  sing N N 323 
PRO   CD  HD2  sing N N 324 
PRO   CD  HD3  sing N N 325 
PRO   OXT HXT  sing N N 326 
SER   N   CA   sing N N 327 
SER   N   H    sing N N 328 
SER   N   H2   sing N N 329 
SER   CA  C    sing N N 330 
SER   CA  CB   sing N N 331 
SER   CA  HA   sing N N 332 
SER   C   O    doub N N 333 
SER   C   OXT  sing N N 334 
SER   CB  OG   sing N N 335 
SER   CB  HB2  sing N N 336 
SER   CB  HB3  sing N N 337 
SER   OG  HG   sing N N 338 
SER   OXT HXT  sing N N 339 
THR   N   CA   sing N N 340 
THR   N   H    sing N N 341 
THR   N   H2   sing N N 342 
THR   CA  C    sing N N 343 
THR   CA  CB   sing N N 344 
THR   CA  HA   sing N N 345 
THR   C   O    doub N N 346 
THR   C   OXT  sing N N 347 
THR   CB  OG1  sing N N 348 
THR   CB  CG2  sing N N 349 
THR   CB  HB   sing N N 350 
THR   OG1 HG1  sing N N 351 
THR   CG2 HG21 sing N N 352 
THR   CG2 HG22 sing N N 353 
THR   CG2 HG23 sing N N 354 
THR   OXT HXT  sing N N 355 
TRP   N   CA   sing N N 356 
TRP   N   H    sing N N 357 
TRP   N   H2   sing N N 358 
TRP   CA  C    sing N N 359 
TRP   CA  CB   sing N N 360 
TRP   CA  HA   sing N N 361 
TRP   C   O    doub N N 362 
TRP   C   OXT  sing N N 363 
TRP   CB  CG   sing N N 364 
TRP   CB  HB2  sing N N 365 
TRP   CB  HB3  sing N N 366 
TRP   CG  CD1  doub Y N 367 
TRP   CG  CD2  sing Y N 368 
TRP   CD1 NE1  sing Y N 369 
TRP   CD1 HD1  sing N N 370 
TRP   CD2 CE2  doub Y N 371 
TRP   CD2 CE3  sing Y N 372 
TRP   NE1 CE2  sing Y N 373 
TRP   NE1 HE1  sing N N 374 
TRP   CE2 CZ2  sing Y N 375 
TRP   CE3 CZ3  doub Y N 376 
TRP   CE3 HE3  sing N N 377 
TRP   CZ2 CH2  doub Y N 378 
TRP   CZ2 HZ2  sing N N 379 
TRP   CZ3 CH2  sing Y N 380 
TRP   CZ3 HZ3  sing N N 381 
TRP   CH2 HH2  sing N N 382 
TRP   OXT HXT  sing N N 383 
TYR   N   CA   sing N N 384 
TYR   N   H    sing N N 385 
TYR   N   H2   sing N N 386 
TYR   CA  C    sing N N 387 
TYR   CA  CB   sing N N 388 
TYR   CA  HA   sing N N 389 
TYR   C   O    doub N N 390 
TYR   C   OXT  sing N N 391 
TYR   CB  CG   sing N N 392 
TYR   CB  HB2  sing N N 393 
TYR   CB  HB3  sing N N 394 
TYR   CG  CD1  doub Y N 395 
TYR   CG  CD2  sing Y N 396 
TYR   CD1 CE1  sing Y N 397 
TYR   CD1 HD1  sing N N 398 
TYR   CD2 CE2  doub Y N 399 
TYR   CD2 HD2  sing N N 400 
TYR   CE1 CZ   doub Y N 401 
TYR   CE1 HE1  sing N N 402 
TYR   CE2 CZ   sing Y N 403 
TYR   CE2 HE2  sing N N 404 
TYR   CZ  OH   sing N N 405 
TYR   OH  HH   sing N N 406 
TYR   OXT HXT  sing N N 407 
VAL   N   CA   sing N N 408 
VAL   N   H    sing N N 409 
VAL   N   H2   sing N N 410 
VAL   CA  C    sing N N 411 
VAL   CA  CB   sing N N 412 
VAL   CA  HA   sing N N 413 
VAL   C   O    doub N N 414 
VAL   C   OXT  sing N N 415 
VAL   CB  CG1  sing N N 416 
VAL   CB  CG2  sing N N 417 
VAL   CB  HB   sing N N 418 
VAL   CG1 HG11 sing N N 419 
VAL   CG1 HG12 sing N N 420 
VAL   CG1 HG13 sing N N 421 
VAL   CG2 HG21 sing N N 422 
VAL   CG2 HG22 sing N N 423 
VAL   CG2 HG23 sing N N 424 
VAL   OXT HXT  sing N N 425 
# 
_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                    9F6W 
_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]   0.010666 
_atom_sites.fract_transf_matrix[1][2]   0.006158 
_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]   0.012316 
_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]   0.030094 
_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   . MET   A 1 2   ? -25.009 8.659  -11.824 1.00 83.99  ? 1795 MET   A N   1 
ATOM   2   C  CA  . MET   A 1 2   ? -25.823 9.478  -12.716 1.00 87.22  ? 1795 MET   A CA  1 
ATOM   3   C  C   . MET   A 1 2   ? -27.189 9.746  -12.096 1.00 89.59  ? 1795 MET   A C   1 
ATOM   4   O  O   . MET   A 1 2   ? -27.723 10.849 -12.211 1.00 87.74  ? 1795 MET   A O   1 
ATOM   5   C  CB  . MET   A 1 2   ? -25.985 8.809  -14.085 1.00 92.59  ? 1795 MET   A CB  1 
ATOM   6   C  CG  . MET   A 1 2   ? -26.905 9.567  -15.057 1.00 97.07  ? 1795 MET   A CG  1 
ATOM   7   S  SD  . MET   A 1 2   ? -26.965 8.853  -16.722 1.00 101.96 ? 1795 MET   A SD  1 
ATOM   8   C  CE  . MET   A 1 2   ? -28.329 9.733  -17.487 1.00 90.96  ? 1795 MET   A CE  1 
ATOM   9   N  N   . HIS   A 1 3   ? -27.760 8.729  -11.445 1.00 92.91  ? 1796 HIS   A N   1 
ATOM   10  C  CA  . HIS   A 1 3   ? -28.998 8.946  -10.700 1.00 91.68  ? 1796 HIS   A CA  1 
ATOM   11  C  C   . HIS   A 1 3   ? -28.775 9.947  -9.571  1.00 84.87  ? 1796 HIS   A C   1 
ATOM   12  O  O   . HIS   A 1 3   ? -29.647 10.776 -9.283  1.00 72.89  ? 1796 HIS   A O   1 
ATOM   13  C  CB  . HIS   A 1 3   ? -29.533 7.613  -10.165 1.00 95.80  ? 1796 HIS   A CB  1 
ATOM   14  C  CG  . HIS   A 1 3   ? -30.770 7.740  -9.326  1.00 97.30  ? 1796 HIS   A CG  1 
ATOM   15  N  ND1 . HIS   A 1 3   ? -30.728 7.885  -7.955  1.00 98.93  ? 1796 HIS   A ND1 1 
ATOM   16  C  CD2 . HIS   A 1 3   ? -32.083 7.723  -9.661  1.00 97.95  ? 1796 HIS   A CD2 1 
ATOM   17  C  CE1 . HIS   A 1 3   ? -31.960 7.960  -7.482  1.00 98.15  ? 1796 HIS   A CE1 1 
ATOM   18  N  NE2 . HIS   A 1 3   ? -32.801 7.864  -8.496  1.00 98.28  ? 1796 HIS   A NE2 1 
ATOM   19  N  N   . SER   A 1 4   ? -27.602 9.893  -8.932  1.00 88.81  ? 1797 SER   A N   1 
ATOM   20  C  CA  . SER   A 1 4   ? -27.235 10.909 -7.950  1.00 85.49  ? 1797 SER   A CA  1 
ATOM   21  C  C   . SER   A 1 4   ? -27.101 12.278 -8.608  1.00 82.80  ? 1797 SER   A C   1 
ATOM   22  O  O   . SER   A 1 4   ? -27.660 13.269 -8.120  1.00 70.32  ? 1797 SER   A O   1 
ATOM   23  C  CB  . SER   A 1 4   ? -25.934 10.509 -7.249  1.00 86.79  ? 1797 SER   A CB  1 
ATOM   24  O  OG  . SER   A 1 4   ? -24.945 10.100 -8.186  1.00 91.24  ? 1797 SER   A OG  1 
ATOM   25  N  N   . ASP   A 1 5   ? -26.366 12.344 -9.726  1.00 90.27  ? 1798 ASP   A N   1 
ATOM   26  C  CA  . ASP   A 1 5   ? -26.223 13.588 -10.483 1.00 83.67  ? 1798 ASP   A CA  1 
ATOM   27  C  C   . ASP   A 1 5   ? -27.581 14.195 -10.815 1.00 74.77  ? 1798 ASP   A C   1 
ATOM   28  O  O   . ASP   A 1 5   ? -27.830 15.378 -10.556 1.00 69.22  ? 1798 ASP   A O   1 
ATOM   29  C  CB  . ASP   A 1 5   ? -25.437 13.334 -11.778 1.00 86.97  ? 1798 ASP   A CB  1 
ATOM   30  C  CG  . ASP   A 1 5   ? -23.926 13.393 -11.588 1.00 92.37  ? 1798 ASP   A CG  1 
ATOM   31  O  OD1 . ASP   A 1 5   ? -23.456 13.417 -10.432 1.00 95.39  ? 1798 ASP   A OD1 1 
ATOM   32  O  OD2 . ASP   A 1 5   ? -23.206 13.419 -12.611 1.00 96.10  ? 1798 ASP   A OD2 1 
ATOM   33  N  N   . LEU   A 1 6   ? -28.480 13.391 -11.385 1.00 73.52  ? 1799 LEU   A N   1 
ATOM   34  C  CA  . LEU   A 1 6   ? -29.731 13.933 -11.895 1.00 70.33  ? 1799 LEU   A CA  1 
ATOM   35  C  C   . LEU   A 1 6   ? -30.729 14.230 -10.785 1.00 65.57  ? 1799 LEU   A C   1 
ATOM   36  O  O   . LEU   A 1 6   ? -31.574 15.116 -10.949 1.00 64.08  ? 1799 LEU   A O   1 
ATOM   37  C  CB  . LEU   A 1 6   ? -30.326 12.976 -12.928 1.00 75.76  ? 1799 LEU   A CB  1 
ATOM   38  C  CG  . LEU   A 1 6   ? -29.490 12.866 -14.214 1.00 76.44  ? 1799 LEU   A CG  1 
ATOM   39  C  CD1 . LEU   A 1 6   ? -30.007 11.751 -15.104 1.00 77.48  ? 1799 LEU   A CD1 1 
ATOM   40  C  CD2 . LEU   A 1 6   ? -29.450 14.190 -14.979 1.00 72.11  ? 1799 LEU   A CD2 1 
ATOM   41  N  N   . THR   A 1 7   ? -30.647 13.518 -9.657  1.00 58.95  ? 1800 THR   A N   1 
ATOM   42  C  CA  . THR   A 1 7   ? -31.455 13.875 -8.493  1.00 56.41  ? 1800 THR   A CA  1 
ATOM   43  C  C   . THR   A 1 7   ? -31.147 15.295 -8.023  1.00 54.87  ? 1800 THR   A C   1 
ATOM   44  O  O   . THR   A 1 7   ? -32.058 16.093 -7.762  1.00 48.68  ? 1800 THR   A O   1 
ATOM   45  C  CB  . THR   A 1 7   ? -31.213 12.882 -7.357  1.00 63.51  ? 1800 THR   A CB  1 
ATOM   46  O  OG1 . THR   A 1 7   ? -31.666 11.578 -7.746  1.00 65.31  ? 1800 THR   A OG1 1 
ATOM   47  C  CG2 . THR   A 1 7   ? -31.957 13.321 -6.112  1.00 61.36  ? 1800 THR   A CG2 1 
ATOM   48  N  N   . PHE   A 1 8   ? -29.858 15.625 -7.905  1.00 49.62  ? 1801 PHE   A N   1 
ATOM   49  C  CA  . PHE   A 1 8   ? -29.473 16.981 -7.539  1.00 53.38  ? 1801 PHE   A CA  1 
ATOM   50  C  C   . PHE   A 1 8   ? -29.977 17.999 -8.560  1.00 56.21  ? 1801 PHE   A C   1 
ATOM   51  O  O   . PHE   A 1 8   ? -30.430 19.087 -8.186  1.00 55.42  ? 1801 PHE   A O   1 
ATOM   52  C  CB  . PHE   A 1 8   ? -27.954 17.077 -7.406  1.00 66.48  ? 1801 PHE   A CB  1 
ATOM   53  C  CG  . PHE   A 1 8   ? -27.409 18.411 -7.826  1.00 83.62  ? 1801 PHE   A CG  1 
ATOM   54  C  CD1 . PHE   A 1 8   ? -27.514 19.508 -6.986  1.00 88.65  ? 1801 PHE   A CD1 1 
ATOM   55  C  CD2 . PHE   A 1 8   ? -26.827 18.581 -9.075  1.00 98.14  ? 1801 PHE   A CD2 1 
ATOM   56  C  CE1 . PHE   A 1 8   ? -27.035 20.748 -7.370  1.00 96.40  ? 1801 PHE   A CE1 1 
ATOM   57  C  CE2 . PHE   A 1 8   ? -26.349 19.822 -9.469  1.00 103.97 ? 1801 PHE   A CE2 1 
ATOM   58  C  CZ  . PHE   A 1 8   ? -26.453 20.907 -8.612  1.00 102.04 ? 1801 PHE   A CZ  1 
ATOM   59  N  N   . CYS   A 1 9   ? -29.887 17.670 -9.856  1.00 57.04  ? 1802 CYS   A N   1 
ATOM   60  C  CA  . CYS   A 1 9   ? -30.316 18.603 -10.899 1.00 53.57  ? 1802 CYS   A CA  1 
ATOM   61  C  C   . CYS   A 1 9   ? -31.800 18.938 -10.774 1.00 51.38  ? 1802 CYS   A C   1 
ATOM   62  O  O   . CYS   A 1 9   ? -32.205 20.092 -10.978 1.00 38.49  ? 1802 CYS   A O   1 
ATOM   63  C  CB  . CYS   A 1 9   ? -30.017 18.017 -12.282 1.00 61.26  ? 1802 CYS   A CB  1 
ATOM   64  S  SG  . CYS   A 1 9   ? -28.248 17.817 -12.658 1.00 67.32  ? 1802 CYS   A SG  1 
ATOM   65  N  N   . GLU   A 1 10  ? -32.623 17.937 -10.446 1.00 42.12  ? 1803 GLU   A N   1 
ATOM   66  C  CA  . GLU   A 1 10  ? -34.054 18.159 -10.264 1.00 46.96  ? 1803 GLU   A CA  1 
ATOM   67  C  C   . GLU   A 1 10  ? -34.329 19.042 -9.054  1.00 48.69  ? 1803 GLU   A C   1 
ATOM   68  O  O   . GLU   A 1 10  ? -35.232 19.885 -9.090  1.00 42.54  ? 1803 GLU   A O   1 
ATOM   69  C  CB  . GLU   A 1 10  ? -34.780 16.819 -10.114 1.00 51.02  ? 1803 GLU   A CB  1 
ATOM   70  C  CG  . GLU   A 1 10  ? -34.816 15.959 -11.377 1.00 61.94  ? 1803 GLU   A CG  1 
ATOM   71  C  CD  . GLU   A 1 10  ? -36.019 16.257 -12.269 1.00 65.12  ? 1803 GLU   A CD  1 
ATOM   72  O  OE1 . GLU   A 1 10  ? -36.141 15.623 -13.343 1.00 72.32  ? 1803 GLU   A OE1 1 
ATOM   73  O  OE2 . GLU   A 1 10  ? -36.843 17.120 -11.894 1.00 65.05  ? 1803 GLU   A OE2 1 
ATOM   74  N  N   . ILE   A 1 11  ? -33.577 18.853 -7.966  1.00 48.91  ? 1804 ILE   A N   1 
ATOM   75  C  CA  . ILE   A 1 11  ? -33.760 19.694 -6.784  1.00 46.10  ? 1804 ILE   A CA  1 
ATOM   76  C  C   . ILE   A 1 11  ? -33.420 21.142 -7.107  1.00 42.75  ? 1804 ILE   A C   1 
ATOM   77  O  O   . ILE   A 1 11  ? -34.186 22.062 -6.801  1.00 44.33  ? 1804 ILE   A O   1 
ATOM   78  C  CB  . ILE   A 1 11  ? -32.907 19.180 -5.612  1.00 47.03  ? 1804 ILE   A CB  1 
ATOM   79  C  CG1 . ILE   A 1 11  ? -33.325 17.767 -5.208  1.00 50.54  ? 1804 ILE   A CG1 1 
ATOM   80  C  CG2 . ILE   A 1 11  ? -33.012 20.126 -4.420  1.00 45.71  ? 1804 ILE   A CG2 1 
ATOM   81  C  CD1 . ILE   A 1 11  ? -32.544 17.239 -4.021  1.00 48.52  ? 1804 ILE   A CD1 1 
ATOM   82  N  N   . ILE   A 1 12  ? -32.270 21.367 -7.742  1.00 42.27  ? 1805 ILE   A N   1 
ATOM   83  C  CA  . ILE   A 1 12  ? -31.831 22.742 -7.927  1.00 43.52  ? 1805 ILE   A CA  1 
ATOM   84  C  C   . ILE   A 1 12  ? -32.693 23.449 -8.968  1.00 48.63  ? 1805 ILE   A C   1 
ATOM   85  O  O   . ILE   A 1 12  ? -32.967 24.650 -8.837  1.00 41.61  ? 1805 ILE   A O   1 
ATOM   86  C  CB  . ILE   A 1 12  ? -30.333 22.784 -8.278  1.00 55.16  ? 1805 ILE   A CB  1 
ATOM   87  C  CG1 . ILE   A 1 12  ? -29.795 24.203 -8.126  1.00 60.21  ? 1805 ILE   A CG1 1 
ATOM   88  C  CG2 . ILE   A 1 12  ? -30.091 22.300 -9.689  1.00 61.57  ? 1805 ILE   A CG2 1 
ATOM   89  C  CD1 . ILE   A 1 12  ? -28.298 24.245 -8.009  1.00 68.33  ? 1805 ILE   A CD1 1 
ATOM   90  N  N   . LEU   A 1 13  ? -33.169 22.726 -9.990  1.00 36.17  ? 1806 LEU   A N   1 
ATOM   91  C  CA  . LEU   A 1 13  ? -34.008 23.364 -10.998 1.00 39.80  ? 1806 LEU   A CA  1 
ATOM   92  C  C   . LEU   A 1 13  ? -35.386 23.676 -10.434 1.00 40.14  ? 1806 LEU   A C   1 
ATOM   93  O  O   . LEU   A 1 13  ? -35.950 24.741 -10.714 1.00 39.60  ? 1806 LEU   A O   1 
ATOM   94  C  CB  . LEU   A 1 13  ? -34.124 22.480 -12.246 1.00 37.46  ? 1806 LEU   A CB  1 
ATOM   95  C  CG  . LEU   A 1 13  ? -34.961 23.075 -13.386 1.00 44.69  ? 1806 LEU   A CG  1 
ATOM   96  C  CD1 . LEU   A 1 13  ? -34.436 24.461 -13.742 1.00 44.69  ? 1806 LEU   A CD1 1 
ATOM   97  C  CD2 . LEU   A 1 13  ? -34.953 22.167 -14.631 1.00 46.70  ? 1806 LEU   A CD2 1 
ATOM   98  N  N   . MET   A 1 14  ? -35.950 22.753 -9.653  1.00 37.12  ? 1807 MET   A N   1 
ATOM   99  C  CA  . MET   A 1 14  ? -37.166 23.058 -8.905  1.00 43.61  ? 1807 MET   A CA  1 
ATOM   100 C  C   . MET   A 1 14  ? -36.990 24.336 -8.087  1.00 42.08  ? 1807 MET   A C   1 
ATOM   101 O  O   . MET   A 1 14  ? -37.852 25.223 -8.093  1.00 44.44  ? 1807 MET   A O   1 
ATOM   102 C  CB  . MET   A 1 14  ? -37.520 21.878 -7.998  1.00 52.63  ? 1807 MET   A CB  1 
ATOM   103 C  CG  . MET   A 1 14  ? -38.783 22.051 -7.180  1.00 63.74  ? 1807 MET   A CG  1 
ATOM   104 S  SD  . MET   A 1 14  ? -38.589 21.336 -5.541  1.00 82.01  ? 1807 MET   A SD  1 
ATOM   105 C  CE  . MET   A 1 14  ? -37.724 22.657 -4.698  1.00 69.83  ? 1807 MET   A CE  1 
ATOM   106 N  N   . GLU   A 1 15  ? -35.857 24.459 -7.398  1.00 36.91  ? 1808 GLU   A N   1 
ATOM   107 C  CA  . GLU   A 1 15  ? -35.663 25.612 -6.525  1.00 44.20  ? 1808 GLU   A CA  1 
ATOM   108 C  C   . GLU   A 1 15  ? -35.519 26.889 -7.340  1.00 44.08  ? 1808 GLU   A C   1 
ATOM   109 O  O   . GLU   A 1 15  ? -36.012 27.950 -6.938  1.00 39.69  ? 1808 GLU   A O   1 
ATOM   110 C  CB  . GLU   A 1 15  ? -34.446 25.394 -5.625  1.00 40.48  ? 1808 GLU   A CB  1 
ATOM   111 C  CG  . GLU   A 1 15  ? -34.681 24.375 -4.507  1.00 53.19  ? 1808 GLU   A CG  1 
ATOM   112 C  CD  . GLU   A 1 15  ? -33.435 24.127 -3.668  1.00 63.11  ? 1808 GLU   A CD  1 
ATOM   113 O  OE1 . GLU   A 1 15  ? -32.387 24.737 -3.966  1.00 70.84  ? 1808 GLU   A OE1 1 
ATOM   114 O  OE2 . GLU   A 1 15  ? -33.497 23.323 -2.714  1.00 68.63  ? 1808 GLU   A OE2 1 
ATOM   115 N  N   . MET   A 1 16  ? -34.875 26.802 -8.502  1.00 38.30  ? 1809 MET   A N   1 
ATOM   116 C  CA  . MET   A 1 16  ? -34.740 27.990 -9.336  1.00 37.79  ? 1809 MET   A CA  1 
ATOM   117 C  C   . MET   A 1 16  ? -36.078 28.384 -9.950  1.00 37.43  ? 1809 MET   A C   1 
ATOM   118 O  O   . MET   A 1 16  ? -36.412 29.573 -10.000 1.00 38.04  ? 1809 MET   A O   1 
ATOM   119 C  CB  . MET   A 1 16  ? -33.684 27.757 -10.416 1.00 36.51  ? 1809 MET   A CB  1 
ATOM   120 C  CG  . MET   A 1 16  ? -32.277 27.609 -9.843  1.00 46.90  ? 1809 MET   A CG  1 
ATOM   121 S  SD  . MET   A 1 16  ? -30.996 27.882 -11.072 1.00 58.46  ? 1809 MET   A SD  1 
ATOM   122 C  CE  . MET   A 1 16  ? -31.309 26.518 -12.197 1.00 59.47  ? 1809 MET   A CE  1 
ATOM   123 N  N   . GLU   A 1 17  ? -36.868 27.400 -10.391 1.00 34.22  ? 1810 GLU   A N   1 
ATOM   124 C  CA  . GLU   A 1 17  ? -38.158 27.689 -11.015 1.00 44.40  ? 1810 GLU   A CA  1 
ATOM   125 C  C   . GLU   A 1 17  ? -39.121 28.380 -10.059 1.00 42.25  ? 1810 GLU   A C   1 
ATOM   126 O  O   . GLU   A 1 17  ? -39.996 29.136 -10.502 1.00 40.01  ? 1810 GLU   A O   1 
ATOM   127 C  CB  . GLU   A 1 17  ? -38.795 26.401 -11.533 1.00 44.03  ? 1810 GLU   A CB  1 
ATOM   128 C  CG  . GLU   A 1 17  ? -38.174 25.860 -12.803 1.00 51.06  ? 1810 GLU   A CG  1 
ATOM   129 C  CD  . GLU   A 1 17  ? -38.692 24.472 -13.136 1.00 59.54  ? 1810 GLU   A CD  1 
ATOM   130 O  OE1 . GLU   A 1 17  ? -38.985 23.718 -12.180 1.00 56.69  ? 1810 GLU   A OE1 1 
ATOM   131 O  OE2 . GLU   A 1 17  ? -38.812 24.143 -14.345 1.00 55.79  ? 1810 GLU   A OE2 1 
ATOM   132 N  N   . SER   A 1 18  ? -38.997 28.122 -8.760  1.00 39.63  ? 1811 SER   A N   1 
ATOM   133 C  CA  . SER   A 1 18  ? -39.901 28.702 -7.776  1.00 50.65  ? 1811 SER   A CA  1 
ATOM   134 C  C   . SER   A 1 18  ? -39.337 29.957 -7.116  1.00 51.31  ? 1811 SER   A C   1 
ATOM   135 O  O   . SER   A 1 18  ? -40.012 30.554 -6.274  1.00 53.93  ? 1811 SER   A O   1 
ATOM   136 C  CB  . SER   A 1 18  ? -40.253 27.662 -6.709  1.00 51.72  ? 1811 SER   A CB  1 
ATOM   137 O  OG  . SER   A 1 18  ? -39.092 27.228 -6.027  1.00 59.39  ? 1811 SER   A OG  1 
ATOM   138 N  N   . HIS   A 1 19  ? -38.134 30.380 -7.496  1.00 44.53  ? 1812 HIS   A N   1 
ATOM   139 C  CA  . HIS   A 1 19  ? -37.510 31.562 -6.908  1.00 44.09  ? 1812 HIS   A CA  1 
ATOM   140 C  C   . HIS   A 1 19  ? -38.211 32.844 -7.370  1.00 47.68  ? 1812 HIS   A C   1 
ATOM   141 O  O   . HIS   A 1 19  ? -38.639 32.949 -8.524  1.00 42.19  ? 1812 HIS   A O   1 
ATOM   142 C  CB  . HIS   A 1 19  ? -36.033 31.586 -7.309  1.00 37.75  ? 1812 HIS   A CB  1 
ATOM   143 C  CG  . HIS   A 1 19  ? -35.163 32.391 -6.404  1.00 41.88  ? 1812 HIS   A CG  1 
ATOM   144 N  ND1 . HIS   A 1 19  ? -35.219 33.767 -6.347  1.00 41.41  ? 1812 HIS   A ND1 1 
ATOM   145 C  CD2 . HIS   A 1 19  ? -34.193 32.014 -5.538  1.00 44.77  ? 1812 HIS   A CD2 1 
ATOM   146 C  CE1 . HIS   A 1 19  ? -34.324 34.203 -5.477  1.00 45.07  ? 1812 HIS   A CE1 1 
ATOM   147 N  NE2 . HIS   A 1 19  ? -33.691 33.159 -4.971  1.00 43.96  ? 1812 HIS   A NE2 1 
ATOM   148 N  N   . ASP   A 1 20  ? -38.314 33.833 -6.463  1.00 45.51  ? 1813 ASP   A N   1 
ATOM   149 C  CA  . ASP   A 1 20  ? -38.895 35.140 -6.810  1.00 38.61  ? 1813 ASP   A CA  1 
ATOM   150 C  C   . ASP   A 1 20  ? -38.185 35.808 -7.992  1.00 43.10  ? 1813 ASP   A C   1 
ATOM   151 O  O   . ASP   A 1 20  ? -38.821 36.486 -8.808  1.00 43.03  ? 1813 ASP   A O   1 
ATOM   152 C  CB  . ASP   A 1 20  ? -38.835 36.085 -5.611  1.00 48.84  ? 1813 ASP   A CB  1 
ATOM   153 C  CG  . ASP   A 1 20  ? -39.975 35.879 -4.630  1.00 59.37  ? 1813 ASP   A CG  1 
ATOM   154 O  OD1 . ASP   A 1 20  ? -40.840 35.004 -4.860  1.00 53.59  ? 1813 ASP   A OD1 1 
ATOM   155 O  OD2 . ASP   A 1 20  ? -40.000 36.621 -3.625  1.00 61.63  ? 1813 ASP   A OD2 1 
ATOM   156 N  N   . ALA   A 1 21  ? -36.867 35.663 -8.080  1.00 38.13  ? 1814 ALA   A N   1 
ATOM   157 C  CA  . ALA   A 1 21  ? -36.074 36.317 -9.117  1.00 36.27  ? 1814 ALA   A CA  1 
ATOM   158 C  C   . ALA   A 1 21  ? -36.021 35.525 -10.425 1.00 34.59  ? 1814 ALA   A C   1 
ATOM   159 O  O   . ALA   A 1 21  ? -35.281 35.906 -11.336 1.00 35.04  ? 1814 ALA   A O   1 
ATOM   160 C  CB  . ALA   A 1 21  ? -34.648 36.567 -8.607  1.00 33.53  ? 1814 ALA   A CB  1 
ATOM   161 N  N   . ALA   A 1 22  ? -36.791 34.448 -10.541 1.00 35.99  ? 1815 ALA   A N   1 
ATOM   162 C  CA  . ALA   A 1 22  ? -36.719 33.572 -11.702 1.00 38.18  ? 1815 ALA   A CA  1 
ATOM   163 C  C   . ALA   A 1 22  ? -37.551 34.066 -12.873 1.00 37.95  ? 1815 ALA   A C   1 
ATOM   164 O  O   . ALA   A 1 22  ? -37.425 33.517 -13.971 1.00 39.44  ? 1815 ALA   A O   1 
ATOM   165 C  CB  . ALA   A 1 22  ? -37.189 32.166 -11.332 1.00 28.17  ? 1815 ALA   A CB  1 
ATOM   166 N  N   . TRP   A 1 23  ? -38.379 35.087 -12.665 1.00 33.14  ? 1816 TRP   A N   1 
ATOM   167 C  CA  . TRP   A 1 23  ? -39.336 35.487 -13.689 1.00 36.37  ? 1816 TRP   A CA  1 
ATOM   168 C  C   . TRP   A 1 23  ? -38.728 35.826 -15.056 1.00 33.31  ? 1816 TRP   A C   1 
ATOM   169 O  O   . TRP   A 1 23  ? -39.432 35.622 -16.053 1.00 42.69  ? 1816 TRP   A O   1 
ATOM   170 C  CB  . TRP   A 1 23  ? -40.185 36.656 -13.158 1.00 33.74  ? 1816 TRP   A CB  1 
ATOM   171 C  CG  . TRP   A 1 23  ? -39.370 37.860 -12.816 1.00 43.35  ? 1816 TRP   A CG  1 
ATOM   172 C  CD1 . TRP   A 1 23  ? -38.821 38.164 -11.606 1.00 48.98  ? 1816 TRP   A CD1 1 
ATOM   173 C  CD2 . TRP   A 1 23  ? -38.997 38.919 -13.704 1.00 48.98  ? 1816 TRP   A CD2 1 
ATOM   174 N  NE1 . TRP   A 1 23  ? -38.135 39.351 -11.683 1.00 49.13  ? 1816 TRP   A NE1 1 
ATOM   175 C  CE2 . TRP   A 1 23  ? -38.224 39.834 -12.961 1.00 49.40  ? 1816 TRP   A CE2 1 
ATOM   176 C  CE3 . TRP   A 1 23  ? -39.245 39.186 -15.054 1.00 47.37  ? 1816 TRP   A CE3 1 
ATOM   177 C  CZ2 . TRP   A 1 23  ? -37.690 40.995 -13.523 1.00 49.46  ? 1816 TRP   A CZ2 1 
ATOM   178 C  CZ3 . TRP   A 1 23  ? -38.718 40.340 -15.610 1.00 48.97  ? 1816 TRP   A CZ3 1 
ATOM   179 C  CH2 . TRP   A 1 23  ? -37.949 41.229 -14.846 1.00 48.34  ? 1816 TRP   A CH2 1 
ATOM   180 N  N   . PRO   A 1 24  ? -37.485 36.317 -15.198 1.00 35.47  ? 1817 PRO   A N   1 
ATOM   181 C  CA  . PRO   A 1 24  ? -36.967 36.542 -16.559 1.00 33.10  ? 1817 PRO   A CA  1 
ATOM   182 C  C   . PRO   A 1 24  ? -36.493 35.292 -17.269 1.00 38.88  ? 1817 PRO   A C   1 
ATOM   183 O  O   . PRO   A 1 24  ? -36.072 35.387 -18.433 1.00 39.82  ? 1817 PRO   A O   1 
ATOM   184 C  CB  . PRO   A 1 24  ? -35.740 37.451 -16.333 1.00 39.32  ? 1817 PRO   A CB  1 
ATOM   185 C  CG  . PRO   A 1 24  ? -35.815 37.902 -14.941 1.00 35.76  ? 1817 PRO   A CG  1 
ATOM   186 C  CD  . PRO   A 1 24  ? -36.514 36.804 -14.204 1.00 31.70  ? 1817 PRO   A CD  1 
ATOM   187 N  N   . PHE   A 1 25  ? -36.529 34.130 -16.617 1.00 31.06  ? 1818 PHE   A N   1 
ATOM   188 C  CA  . PHE   A 1 25  ? -35.817 32.962 -17.121 1.00 36.85  ? 1818 PHE   A CA  1 
ATOM   189 C  C   . PHE   A 1 25  ? -36.717 31.748 -17.272 1.00 38.43  ? 1818 PHE   A C   1 
ATOM   190 O  O   . PHE   A 1 25  ? -36.243 30.695 -17.717 1.00 38.68  ? 1818 PHE   A O   1 
ATOM   191 C  CB  . PHE   A 1 25  ? -34.610 32.629 -16.236 1.00 34.48  ? 1818 PHE   A CB  1 
ATOM   192 C  CG  . PHE   A 1 25  ? -33.765 33.824 -15.936 1.00 34.91  ? 1818 PHE   A CG  1 
ATOM   193 C  CD1 . PHE   A 1 25  ? -32.973 34.387 -16.922 1.00 29.81  ? 1818 PHE   A CD1 1 
ATOM   194 C  CD2 . PHE   A 1 25  ? -33.799 34.421 -14.691 1.00 33.76  ? 1818 PHE   A CD2 1 
ATOM   195 C  CE1 . PHE   A 1 25  ? -32.210 35.501 -16.672 1.00 29.60  ? 1818 PHE   A CE1 1 
ATOM   196 C  CE2 . PHE   A 1 25  ? -33.032 35.542 -14.436 1.00 30.05  ? 1818 PHE   A CE2 1 
ATOM   197 C  CZ  . PHE   A 1 25  ? -32.237 36.079 -15.432 1.00 33.86  ? 1818 PHE   A CZ  1 
ATOM   198 N  N   . LEU   A 1 26  ? -38.007 31.877 -16.962 1.00 38.59  ? 1819 LEU   A N   1 
ATOM   199 C  CA  . LEU   A 1 26  ? -38.931 30.756 -17.009 1.00 42.70  ? 1819 LEU   A CA  1 
ATOM   200 C  C   . LEU   A 1 26  ? -39.349 30.386 -18.426 1.00 46.49  ? 1819 LEU   A C   1 
ATOM   201 O  O   . LEU   A 1 26  ? -39.783 29.251 -18.647 1.00 49.43  ? 1819 LEU   A O   1 
ATOM   202 C  CB  . LEU   A 1 26  ? -40.173 31.072 -16.162 1.00 34.08  ? 1819 LEU   A CB  1 
ATOM   203 C  CG  . LEU   A 1 26  ? -39.885 31.275 -14.674 1.00 44.62  ? 1819 LEU   A CG  1 
ATOM   204 C  CD1 . LEU   A 1 26  ? -41.159 31.577 -13.883 1.00 42.08  ? 1819 LEU   A CD1 1 
ATOM   205 C  CD2 . LEU   A 1 26  ? -39.222 30.025 -14.140 1.00 48.57  ? 1819 LEU   A CD2 1 
ATOM   206 N  N   . GLU   A 1 27  ? -39.227 31.304 -19.381 1.00 47.38  ? 1820 GLU   A N   1 
ATOM   207 C  CA  A GLU   A 1 27  ? -39.592 31.076 -20.773 0.48 42.94  ? 1820 GLU   A CA  1 
ATOM   208 C  CA  B GLU   A 1 27  ? -39.573 31.050 -20.770 0.52 42.77  ? 1820 GLU   A CA  1 
ATOM   209 C  C   . GLU   A 1 27  ? -38.518 31.682 -21.664 1.00 40.11  ? 1820 GLU   A C   1 
ATOM   210 O  O   . GLU   A 1 27  ? -37.849 32.640 -21.257 1.00 37.47  ? 1820 GLU   A O   1 
ATOM   211 C  CB  A GLU   A 1 27  ? -40.955 31.705 -21.113 0.48 46.68  ? 1820 GLU   A CB  1 
ATOM   212 C  CB  B GLU   A 1 27  ? -40.961 31.613 -21.120 0.52 46.65  ? 1820 GLU   A CB  1 
ATOM   213 C  CG  A GLU   A 1 27  ? -42.079 31.394 -20.131 0.48 51.42  ? 1820 GLU   A CG  1 
ATOM   214 C  CG  B GLU   A 1 27  ? -42.116 30.882 -20.451 0.52 51.16  ? 1820 GLU   A CG  1 
ATOM   215 C  CD  A GLU   A 1 27  ? -42.564 32.631 -19.388 0.48 57.95  ? 1820 GLU   A CD  1 
ATOM   216 C  CD  B GLU   A 1 27  ? -43.471 31.392 -20.904 0.52 58.50  ? 1820 GLU   A CD  1 
ATOM   217 O  OE1 A GLU   A 1 27  ? -42.513 32.649 -18.136 0.48 59.16  ? 1820 GLU   A OE1 1 
ATOM   218 O  OE1 B GLU   A 1 27  ? -43.526 32.139 -21.908 0.52 61.02  ? 1820 GLU   A OE1 1 
ATOM   219 O  OE2 A GLU   A 1 27  ? -42.993 33.593 -20.061 0.48 64.98  ? 1820 GLU   A OE2 1 
ATOM   220 O  OE2 B GLU   A 1 27  ? -44.482 31.042 -20.257 0.52 61.47  ? 1820 GLU   A OE2 1 
ATOM   221 N  N   . PRO   A 1 28  ? -38.330 31.153 -22.881 1.00 39.03  ? 1821 PRO   A N   1 
ATOM   222 C  CA  . PRO   A 1 28  ? -37.368 31.765 -23.813 1.00 42.04  ? 1821 PRO   A CA  1 
ATOM   223 C  C   . PRO   A 1 28  ? -37.712 33.218 -24.109 1.00 39.13  ? 1821 PRO   A C   1 
ATOM   224 O  O   . PRO   A 1 28  ? -38.880 33.587 -24.227 1.00 40.42  ? 1821 PRO   A O   1 
ATOM   225 C  CB  . PRO   A 1 28  ? -37.499 30.909 -25.084 1.00 40.52  ? 1821 PRO   A CB  1 
ATOM   226 C  CG  . PRO   A 1 28  ? -38.118 29.626 -24.636 1.00 51.26  ? 1821 PRO   A CG  1 
ATOM   227 C  CD  . PRO   A 1 28  ? -39.001 29.978 -23.474 1.00 46.13  ? 1821 PRO   A CD  1 
ATOM   228 N  N   . VAL   A 1 29  ? -36.675 34.049 -24.224 1.00 35.16  ? 1822 VAL   A N   1 
ATOM   229 C  CA  . VAL   A 1 29  ? -36.848 35.385 -24.786 1.00 35.69  ? 1822 VAL   A CA  1 
ATOM   230 C  C   . VAL   A 1 29  ? -37.457 35.270 -26.179 1.00 43.23  ? 1822 VAL   A C   1 
ATOM   231 O  O   . VAL   A 1 29  ? -37.059 34.416 -26.981 1.00 38.56  ? 1822 VAL   A O   1 
ATOM   232 C  CB  . VAL   A 1 29  ? -35.494 36.114 -24.820 1.00 39.49  ? 1822 VAL   A CB  1 
ATOM   233 C  CG1 . VAL   A 1 29  ? -35.599 37.445 -25.559 1.00 38.11  ? 1822 VAL   A CG1 1 
ATOM   234 C  CG2 . VAL   A 1 29  ? -34.966 36.318 -23.390 1.00 40.92  ? 1822 VAL   A CG2 1 
ATOM   235 N  N   . ASN   A 1 30  ? -38.448 36.113 -26.473 1.00 42.27  ? 1823 ASN   A N   1 
ATOM   236 C  CA  . ASN   A 1 30  ? -38.993 36.187 -27.821 1.00 39.39  ? 1823 ASN   A CA  1 
ATOM   237 C  C   . ASN   A 1 30  ? -38.189 37.226 -28.599 1.00 38.48  ? 1823 ASN   A C   1 
ATOM   238 O  O   . ASN   A 1 30  ? -38.347 38.432 -28.338 1.00 34.15  ? 1823 ASN   A O   1 
ATOM   239 C  CB  . ASN   A 1 30  ? -40.476 36.548 -27.802 1.00 35.93  ? 1823 ASN   A CB  1 
ATOM   240 C  CG  . ASN   A 1 30  ? -41.117 36.501 -29.202 1.00 47.22  ? 1823 ASN   A CG  1 
ATOM   241 O  OD1 . ASN   A 1 30  ? -40.421 36.521 -30.218 1.00 41.88  ? 1823 ASN   A OD1 1 
ATOM   242 N  ND2 . ASN   A 1 30  ? -42.449 36.445 -29.250 1.00 40.82  ? 1823 ASN   A ND2 1 
ATOM   243 N  N   . PRO   A 1 31  ? -37.345 36.823 -29.550 1.00 38.27  ? 1824 PRO   A N   1 
ATOM   244 C  CA  . PRO   A 1 31  ? -36.497 37.814 -30.229 1.00 35.33  ? 1824 PRO   A CA  1 
ATOM   245 C  C   . PRO   A 1 31  ? -37.282 38.802 -31.085 1.00 42.03  ? 1824 PRO   A C   1 
ATOM   246 O  O   . PRO   A 1 31  ? -36.772 39.893 -31.359 1.00 41.80  ? 1824 PRO   A O   1 
ATOM   247 C  CB  . PRO   A 1 31  ? -35.556 36.947 -31.073 1.00 36.39  ? 1824 PRO   A CB  1 
ATOM   248 C  CG  . PRO   A 1 31  ? -36.374 35.713 -31.366 1.00 46.19  ? 1824 PRO   A CG  1 
ATOM   249 C  CD  . PRO   A 1 31  ? -37.233 35.480 -30.150 1.00 38.44  ? 1824 PRO   A CD  1 
ATOM   250 N  N   . ARG   A 1 32  ? -38.509 38.474 -31.499 1.00 40.20  ? 1825 ARG   A N   1 
ATOM   251 C  CA  . ARG   A 1 32  ? -39.329 39.459 -32.199 1.00 39.90  ? 1825 ARG   A CA  1 
ATOM   252 C  C   . ARG   A 1 32  ? -39.650 40.663 -31.323 1.00 45.59  ? 1825 ARG   A C   1 
ATOM   253 O  O   . ARG   A 1 32  ? -39.920 41.750 -31.846 1.00 45.49  ? 1825 ARG   A O   1 
ATOM   254 C  CB  . ARG   A 1 32  ? -40.629 38.818 -32.683 1.00 38.81  ? 1825 ARG   A CB  1 
ATOM   255 C  CG  . ARG   A 1 32  ? -40.441 37.703 -33.712 1.00 42.76  ? 1825 ARG   A CG  1 
ATOM   256 C  CD  . ARG   A 1 32  ? -41.734 36.901 -33.858 1.00 45.08  ? 1825 ARG   A CD  1 
ATOM   257 N  NE  . ARG   A 1 32  ? -41.793 36.060 -35.053 1.00 39.08  ? 1825 ARG   A NE  1 
ATOM   258 C  CZ  . ARG   A 1 32  ? -42.784 35.203 -35.301 1.00 46.19  ? 1825 ARG   A CZ  1 
ATOM   259 N  NH1 . ARG   A 1 32  ? -43.781 35.073 -34.427 1.00 44.28  ? 1825 ARG   A NH1 1 
ATOM   260 N  NH2 . ARG   A 1 32  ? -42.789 34.475 -36.413 1.00 37.21  ? 1825 ARG   A NH2 1 
ATOM   261 N  N   . LEU   A 1 33  ? -39.629 40.495 -30.004 1.00 42.24  ? 1826 LEU   A N   1 
ATOM   262 C  CA  . LEU   A 1 33  ? -39.986 41.563 -29.085 1.00 45.83  ? 1826 LEU   A CA  1 
ATOM   263 C  C   . LEU   A 1 33  ? -38.776 42.284 -28.513 1.00 49.07  ? 1826 LEU   A C   1 
ATOM   264 O  O   . LEU   A 1 33  ? -38.943 43.311 -27.854 1.00 48.85  ? 1826 LEU   A O   1 
ATOM   265 C  CB  . LEU   A 1 33  ? -40.837 41.004 -27.936 1.00 47.79  ? 1826 LEU   A CB  1 
ATOM   266 C  CG  . LEU   A 1 33  ? -42.024 40.142 -28.387 1.00 49.82  ? 1826 LEU   A CG  1 
ATOM   267 C  CD1 . LEU   A 1 33  ? -42.745 39.495 -27.197 1.00 46.38  ? 1826 LEU   A CD1 1 
ATOM   268 C  CD2 . LEU   A 1 33  ? -42.979 40.964 -29.211 1.00 45.24  ? 1826 LEU   A CD2 1 
ATOM   269 N  N   . VAL   A 1 34  ? -37.568 41.787 -28.748 1.00 50.35  ? 1827 VAL   A N   1 
ATOM   270 C  CA  . VAL   A 1 34  ? -36.374 42.332 -28.117 1.00 43.68  ? 1827 VAL   A CA  1 
ATOM   271 C  C   . VAL   A 1 34  ? -35.391 42.679 -29.223 1.00 44.22  ? 1827 VAL   A C   1 
ATOM   272 O  O   . VAL   A 1 34  ? -34.749 41.791 -29.802 1.00 37.35  ? 1827 VAL   A O   1 
ATOM   273 C  CB  . VAL   A 1 34  ? -35.754 41.369 -27.103 1.00 38.04  ? 1827 VAL   A CB  1 
ATOM   274 C  CG1 . VAL   A 1 34  ? -34.551 42.023 -26.453 1.00 38.05  ? 1827 VAL   A CG1 1 
ATOM   275 C  CG2 . VAL   A 1 34  ? -36.794 40.973 -26.045 1.00 35.86  ? 1827 VAL   A CG2 1 
ATOM   276 N  N   . SER   A 1 35  ? -35.257 43.970 -29.504 1.00 44.53  ? 1828 SER   A N   1 
ATOM   277 C  CA  . SER   A 1 35  ? -34.365 44.411 -30.564 1.00 55.87  ? 1828 SER   A CA  1 
ATOM   278 C  C   . SER   A 1 35  ? -32.925 44.029 -30.243 1.00 53.76  ? 1828 SER   A C   1 
ATOM   279 O  O   . SER   A 1 35  ? -32.409 44.335 -29.161 1.00 54.39  ? 1828 SER   A O   1 
ATOM   280 C  CB  . SER   A 1 35  ? -34.499 45.922 -30.755 1.00 63.15  ? 1828 SER   A CB  1 
ATOM   281 O  OG  . SER   A 1 35  ? -33.643 46.378 -31.781 1.00 66.65  ? 1828 SER   A OG  1 
ATOM   282 N  N   . GLY   A 1 36  ? -32.282 43.333 -31.177 1.00 48.00  ? 1829 GLY   A N   1 
ATOM   283 C  CA  . GLY   A 1 36  ? -30.884 42.980 -31.048 1.00 46.61  ? 1829 GLY   A CA  1 
ATOM   284 C  C   . GLY   A 1 36  ? -30.599 41.638 -30.402 1.00 40.38  ? 1829 GLY   A C   1 
ATOM   285 O  O   . GLY   A 1 36  ? -29.430 41.225 -30.367 1.00 40.02  ? 1829 GLY   A O   1 
ATOM   286 N  N   . TYR   A 1 37  ? -31.620 40.927 -29.916 1.00 43.09  ? 1830 TYR   A N   1 
ATOM   287 C  CA  . TYR   A 1 37  ? -31.364 39.737 -29.109 1.00 43.91  ? 1830 TYR   A CA  1 
ATOM   288 C  C   . TYR   A 1 37  ? -30.751 38.630 -29.948 1.00 43.09  ? 1830 TYR   A C   1 
ATOM   289 O  O   . TYR   A 1 37  ? -29.752 38.008 -29.555 1.00 31.32  ? 1830 TYR   A O   1 
ATOM   290 C  CB  . TYR   A 1 37  ? -32.651 39.236 -28.463 1.00 33.66  ? 1830 TYR   A CB  1 
ATOM   291 C  CG  . TYR   A 1 37  ? -32.355 38.242 -27.379 1.00 33.94  ? 1830 TYR   A CG  1 
ATOM   292 C  CD1 . TYR   A 1 37  ? -31.901 38.674 -26.143 1.00 40.05  ? 1830 TYR   A CD1 1 
ATOM   293 C  CD2 . TYR   A 1 37  ? -32.482 36.877 -27.594 1.00 38.29  ? 1830 TYR   A CD2 1 
ATOM   294 C  CE1 . TYR   A 1 37  ? -31.602 37.787 -25.137 1.00 46.51  ? 1830 TYR   A CE1 1 
ATOM   295 C  CE2 . TYR   A 1 37  ? -32.183 35.963 -26.574 1.00 41.53  ? 1830 TYR   A CE2 1 
ATOM   296 C  CZ  . TYR   A 1 37  ? -31.739 36.432 -25.353 1.00 44.89  ? 1830 TYR   A CZ  1 
ATOM   297 O  OH  . TYR   A 1 37  ? -31.428 35.565 -24.323 1.00 42.17  ? 1830 TYR   A OH  1 
ATOM   298 N  N   . ARG   A 1 38  ? -31.357 38.379 -31.108 1.00 32.12  ? 1831 ARG   A N   1 
ATOM   299 C  CA  . ARG   A 1 38  ? -30.901 37.350 -32.026 1.00 37.80  ? 1831 ARG   A CA  1 
ATOM   300 C  C   . ARG   A 1 38  ? -29.476 37.622 -32.494 1.00 43.06  ? 1831 ARG   A C   1 
ATOM   301 O  O   . ARG   A 1 38  ? -28.656 36.702 -32.592 1.00 44.29  ? 1831 ARG   A O   1 
ATOM   302 C  CB  . ARG   A 1 38  ? -31.873 37.303 -33.212 1.00 41.09  ? 1831 ARG   A CB  1 
ATOM   303 C  CG  . ARG   A 1 38  ? -31.659 36.198 -34.231 1.00 52.31  ? 1831 ARG   A CG  1 
ATOM   304 C  CD  . ARG   A 1 38  ? -32.413 36.468 -35.565 1.00 56.18  ? 1831 ARG   A CD  1 
ATOM   305 N  NE  . ARG   A 1 38  ? -33.848 36.752 -35.425 1.00 62.58  ? 1831 ARG   A NE  1 
ATOM   306 C  CZ  . ARG   A 1 38  ? -34.798 35.848 -35.163 1.00 67.13  ? 1831 ARG   A CZ  1 
ATOM   307 N  NH1 . ARG   A 1 38  ? -34.495 34.565 -34.978 1.00 60.83  ? 1831 ARG   A NH1 1 
ATOM   308 N  NH2 . ARG   A 1 38  ? -36.069 36.230 -35.078 1.00 69.39  ? 1831 ARG   A NH2 1 
ATOM   309 N  N   . ARG   A 1 39  ? -29.174 38.884 -32.806 1.00 40.59  ? 1832 ARG   A N   1 
ATOM   310 C  CA  . ARG   A 1 39  ? -27.840 39.245 -33.270 1.00 44.42  ? 1832 ARG   A CA  1 
ATOM   311 C  C   . ARG   A 1 39  ? -26.784 38.991 -32.189 1.00 40.20  ? 1832 ARG   A C   1 
ATOM   312 O  O   . ARG   A 1 39  ? -25.681 38.515 -32.487 1.00 37.62  ? 1832 ARG   A O   1 
ATOM   313 C  CB  . ARG   A 1 39  ? -27.855 40.710 -33.717 1.00 37.16  ? 1832 ARG   A CB  1 
ATOM   314 C  CG  . ARG   A 1 39  ? -26.504 41.342 -33.977 1.00 46.41  ? 1832 ARG   A CG  1 
ATOM   315 C  CD  . ARG   A 1 39  ? -26.610 42.763 -34.575 1.00 49.30  ? 1832 ARG   A CD  1 
ATOM   316 N  NE  . ARG   A 1 39  ? -27.489 43.683 -33.840 1.00 58.39  ? 1832 ARG   A NE  1 
ATOM   317 C  CZ  . ARG   A 1 39  ? -27.120 44.412 -32.785 1.00 66.92  ? 1832 ARG   A CZ  1 
ATOM   318 N  NH1 . ARG   A 1 39  ? -25.888 44.323 -32.308 1.00 69.78  ? 1832 ARG   A NH1 1 
ATOM   319 N  NH2 . ARG   A 1 39  ? -27.984 45.229 -32.194 1.00 65.20  ? 1832 ARG   A NH2 1 
ATOM   320 N  N   . ILE   A 1 40  ? -27.114 39.252 -30.927 1.00 38.17  ? 1833 ILE   A N   1 
ATOM   321 C  CA  . ILE   A 1 40  ? -26.119 39.269 -29.853 1.00 39.97  ? 1833 ILE   A CA  1 
ATOM   322 C  C   . ILE   A 1 40  ? -26.021 37.931 -29.120 1.00 36.98  ? 1833 ILE   A C   1 
ATOM   323 O  O   . ILE   A 1 40  ? -24.922 37.497 -28.771 1.00 38.26  ? 1833 ILE   A O   1 
ATOM   324 C  CB  . ILE   A 1 40  ? -26.414 40.419 -28.868 1.00 37.52  ? 1833 ILE   A CB  1 
ATOM   325 C  CG1 . ILE   A 1 40  ? -26.042 41.759 -29.506 1.00 36.91  ? 1833 ILE   A CG1 1 
ATOM   326 C  CG2 . ILE   A 1 40  ? -25.620 40.233 -27.586 1.00 38.46  ? 1833 ILE   A CG2 1 
ATOM   327 C  CD1 . ILE   A 1 40  ? -26.505 42.955 -28.703 1.00 25.31  ? 1833 ILE   A CD1 1 
ATOM   328 N  N   . ILE   A 1 41  ? -27.141 37.261 -28.857 1.00 30.77  ? 1834 ILE   A N   1 
ATOM   329 C  CA  . ILE   A 1 41  ? -27.143 36.026 -28.075 1.00 31.82  ? 1834 ILE   A CA  1 
ATOM   330 C  C   . ILE   A 1 41  ? -27.158 34.852 -29.051 1.00 38.60  ? 1834 ILE   A C   1 
ATOM   331 O  O   . ILE   A 1 41  ? -28.192 34.560 -29.663 1.00 35.18  ? 1834 ILE   A O   1 
ATOM   332 C  CB  . ILE   A 1 41  ? -28.336 35.985 -27.109 1.00 27.71  ? 1834 ILE   A CB  1 
ATOM   333 C  CG1 . ILE   A 1 41  ? -28.221 37.119 -26.089 1.00 31.91  ? 1834 ILE   A CG1 1 
ATOM   334 C  CG2 . ILE   A 1 41  ? -28.448 34.630 -26.424 1.00 31.23  ? 1834 ILE   A CG2 1 
ATOM   335 C  CD1 . ILE   A 1 41  ? -26.917 37.100 -25.301 1.00 27.48  ? 1834 ILE   A CD1 1 
ATOM   336 N  N   . LYS   A 1 42  ? -26.013 34.167 -29.194 1.00 45.32  ? 1835 LYS   A N   1 
ATOM   337 C  CA  . LYS   A 1 42  ? -25.908 33.056 -30.147 1.00 39.82  ? 1835 LYS   A CA  1 
ATOM   338 C  C   . LYS   A 1 42  ? -26.595 31.788 -29.647 1.00 37.46  ? 1835 LYS   A C   1 
ATOM   339 O  O   . LYS   A 1 42  ? -27.131 31.018 -30.453 1.00 34.32  ? 1835 LYS   A O   1 
ATOM   340 C  CB  . LYS   A 1 42  ? -24.439 32.746 -30.457 1.00 41.39  ? 1835 LYS   A CB  1 
ATOM   341 C  CG  . LYS   A 1 42  ? -23.628 33.931 -30.946 1.00 52.65  ? 1835 LYS   A CG  1 
ATOM   342 C  CD  . LYS   A 1 42  ? -24.110 34.410 -32.309 1.00 61.67  ? 1835 LYS   A CD  1 
ATOM   343 C  CE  . LYS   A 1 42  ? -23.209 35.515 -32.850 1.00 67.50  ? 1835 LYS   A CE  1 
ATOM   344 N  NZ  . LYS   A 1 42  ? -23.184 36.684 -31.928 1.00 67.04  ? 1835 LYS   A NZ  1 
ATOM   345 N  N   . ASN   A 1 43  ? -26.564 31.516 -28.338 1.00 34.50  ? 1836 ASN   A N   1 
ATOM   346 C  CA  . ASN   A 1 43  ? -27.119 30.271 -27.788 1.00 32.49  ? 1836 ASN   A CA  1 
ATOM   347 C  C   . ASN   A 1 43  ? -28.077 30.579 -26.650 1.00 35.75  ? 1836 ASN   A C   1 
ATOM   348 O  O   . ASN   A 1 43  ? -27.713 30.472 -25.475 1.00 34.60  ? 1836 ASN   A O   1 
ATOM   349 C  CB  . ASN   A 1 43  ? -26.020 29.330 -27.304 1.00 34.77  ? 1836 ASN   A CB  1 
ATOM   350 C  CG  . ASN   A 1 43  ? -25.078 28.946 -28.408 1.00 45.85  ? 1836 ASN   A CG  1 
ATOM   351 O  OD1 . ASN   A 1 43  ? -23.903 29.312 -28.391 1.00 50.77  ? 1836 ASN   A OD1 1 
ATOM   352 N  ND2 . ASN   A 1 43  ? -25.590 28.220 -29.390 1.00 38.56  ? 1836 ASN   A ND2 1 
ATOM   353 N  N   . PRO   A 1 44  ? -29.314 30.952 -26.976 1.00 37.70  ? 1837 PRO   A N   1 
ATOM   354 C  CA  . PRO   A 1 44  ? -30.287 31.258 -25.925 1.00 31.42  ? 1837 PRO   A CA  1 
ATOM   355 C  C   . PRO   A 1 44  ? -30.514 30.058 -25.021 1.00 36.51  ? 1837 PRO   A C   1 
ATOM   356 O  O   . PRO   A 1 44  ? -30.353 28.908 -25.426 1.00 30.66  ? 1837 PRO   A O   1 
ATOM   357 C  CB  . PRO   A 1 44  ? -31.555 31.626 -26.713 1.00 38.30  ? 1837 PRO   A CB  1 
ATOM   358 C  CG  . PRO   A 1 44  ? -31.331 31.097 -28.094 1.00 37.88  ? 1837 PRO   A CG  1 
ATOM   359 C  CD  . PRO   A 1 44  ? -29.858 31.174 -28.323 1.00 30.24  ? 1837 PRO   A CD  1 
ATOM   360 N  N   . MET   A 1 45  ? -30.858 30.337 -23.765 1.00 32.91  ? 1838 MET   A N   1 
ATOM   361 C  CA  . MET   A 1 45  ? -31.158 29.262 -22.833 1.00 33.88  ? 1838 MET   A CA  1 
ATOM   362 C  C   . MET   A 1 45  ? -32.095 29.830 -21.782 1.00 34.58  ? 1838 MET   A C   1 
ATOM   363 O  O   . MET   A 1 45  ? -32.065 31.028 -21.499 1.00 35.45  ? 1838 MET   A O   1 
ATOM   364 C  CB  . MET   A 1 45  ? -29.868 28.687 -22.208 1.00 33.09  ? 1838 MET   A CB  1 
ATOM   365 C  CG  . MET   A 1 45  ? -30.068 27.457 -21.309 1.00 32.10  ? 1838 MET   A CG  1 
ATOM   366 S  SD  . MET   A 1 45  ? -31.008 26.098 -22.071 1.00 41.72  ? 1838 MET   A SD  1 
ATOM   367 C  CE  . MET   A 1 45  ? -30.041 25.763 -23.554 1.00 43.31  ? 1838 MET   A CE  1 
ATOM   368 N  N   . ASP   A 1 46  ? -32.943 28.969 -21.227 1.00 34.50  ? 1839 ASP   A N   1 
ATOM   369 C  CA  . ASP   A 1 46  ? -33.868 29.374 -20.176 1.00 34.24  ? 1839 ASP   A CA  1 
ATOM   370 C  C   . ASP   A 1 46  ? -34.283 28.133 -19.391 1.00 38.35  ? 1839 ASP   A C   1 
ATOM   371 O  O   . ASP   A 1 46  ? -33.982 27.004 -19.782 1.00 40.03  ? 1839 ASP   A O   1 
ATOM   372 C  CB  . ASP   A 1 46  ? -35.083 30.084 -20.765 1.00 39.29  ? 1839 ASP   A CB  1 
ATOM   373 C  CG  . ASP   A 1 46  ? -35.975 29.136 -21.515 1.00 49.87  ? 1839 ASP   A CG  1 
ATOM   374 O  OD1 . ASP   A 1 46  ? -35.626 28.778 -22.658 1.00 51.05  ? 1839 ASP   A OD1 1 
ATOM   375 O  OD2 . ASP   A 1 46  ? -36.997 28.715 -20.936 1.00 52.78  ? 1839 ASP   A OD2 1 
ATOM   376 N  N   . PHE   A 1 47  ? -35.014 28.352 -18.288 1.00 33.06  ? 1840 PHE   A N   1 
ATOM   377 C  CA  . PHE   A 1 47  ? -35.297 27.249 -17.368 1.00 35.65  ? 1840 PHE   A CA  1 
ATOM   378 C  C   . PHE   A 1 47  ? -36.263 26.236 -17.974 1.00 32.64  ? 1840 PHE   A C   1 
ATOM   379 O  O   . PHE   A 1 47  ? -36.135 25.032 -17.724 1.00 36.93  ? 1840 PHE   A O   1 
ATOM   380 C  CB  . PHE   A 1 47  ? -35.844 27.774 -16.030 1.00 34.09  ? 1840 PHE   A CB  1 
ATOM   381 C  CG  . PHE   A 1 47  ? -34.849 28.582 -15.234 1.00 31.90  ? 1840 PHE   A CG  1 
ATOM   382 C  CD1 . PHE   A 1 47  ? -33.489 28.484 -15.491 1.00 37.51  ? 1840 PHE   A CD1 1 
ATOM   383 C  CD2 . PHE   A 1 47  ? -35.272 29.435 -14.230 1.00 43.52  ? 1840 PHE   A CD2 1 
ATOM   384 C  CE1 . PHE   A 1 47  ? -32.570 29.223 -14.761 1.00 38.10  ? 1840 PHE   A CE1 1 
ATOM   385 C  CE2 . PHE   A 1 47  ? -34.357 30.176 -13.488 1.00 47.77  ? 1840 PHE   A CE2 1 
ATOM   386 C  CZ  . PHE   A 1 47  ? -33.005 30.072 -13.760 1.00 47.75  ? 1840 PHE   A CZ  1 
ATOM   387 N  N   . SER   A 1 48  ? -37.246 26.688 -18.759 1.00 39.09  ? 1841 SER   A N   1 
ATOM   388 C  CA  . SER   A 1 48  ? -38.178 25.734 -19.355 1.00 42.37  ? 1841 SER   A CA  1 
ATOM   389 C  C   . SER   A 1 48  ? -37.491 24.844 -20.389 1.00 40.38  ? 1841 SER   A C   1 
ATOM   390 O  O   . SER   A 1 48  ? -37.873 23.680 -20.553 1.00 40.58  ? 1841 SER   A O   1 
ATOM   391 C  CB  . SER   A 1 48  ? -39.364 26.461 -19.990 1.00 48.04  ? 1841 SER   A CB  1 
ATOM   392 O  OG  . SER   A 1 48  ? -38.989 27.085 -21.212 1.00 46.06  ? 1841 SER   A OG  1 
ATOM   393 N  N   . THR   A 1 49  ? -36.481 25.362 -21.092 1.00 34.76  ? 1842 THR   A N   1 
ATOM   394 C  CA  . THR   A 1 49  ? -35.710 24.500 -21.987 1.00 34.23  ? 1842 THR   A CA  1 
ATOM   395 C  C   . THR   A 1 49  ? -34.920 23.467 -21.192 1.00 39.19  ? 1842 THR   A C   1 
ATOM   396 O  O   . THR   A 1 49  ? -34.873 22.290 -21.571 1.00 39.45  ? 1842 THR   A O   1 
ATOM   397 C  CB  . THR   A 1 49  ? -34.781 25.340 -22.869 1.00 41.51  ? 1842 THR   A CB  1 
ATOM   398 O  OG1 . THR   A 1 49  ? -35.540 26.377 -23.498 1.00 45.51  ? 1842 THR   A OG1 1 
ATOM   399 C  CG2 . THR   A 1 49  ? -34.115 24.490 -23.961 1.00 37.51  ? 1842 THR   A CG2 1 
ATOM   400 N  N   . MET   A 1 50  ? -34.318 23.880 -20.067 1.00 37.66  ? 1843 MET   A N   1 
ATOM   401 C  CA  . MET   A 1 50  ? -33.627 22.923 -19.203 1.00 37.68  ? 1843 MET   A CA  1 
ATOM   402 C  C   . MET   A 1 50  ? -34.600 21.912 -18.615 1.00 34.49  ? 1843 MET   A C   1 
ATOM   403 O  O   . MET   A 1 50  ? -34.290 20.715 -18.525 1.00 37.99  ? 1843 MET   A O   1 
ATOM   404 C  CB  . MET   A 1 50  ? -32.878 23.659 -18.085 1.00 32.93  ? 1843 MET   A CB  1 
ATOM   405 C  CG  . MET   A 1 50  ? -31.698 24.490 -18.605 1.00 36.23  ? 1843 MET   A CG  1 
ATOM   406 S  SD  . MET   A 1 50  ? -31.072 25.666 -17.396 1.00 41.32  ? 1843 MET   A SD  1 
ATOM   407 C  CE  . MET   A 1 50  ? -30.611 24.596 -16.042 1.00 49.22  ? 1843 MET   A CE  1 
ATOM   408 N  N   . ARG   A 1 51  ? -35.779 22.374 -18.193 1.00 35.49  ? 1844 ARG   A N   1 
ATOM   409 C  CA  . ARG   A 1 51  ? -36.801 21.447 -17.713 1.00 36.52  ? 1844 ARG   A CA  1 
ATOM   410 C  C   . ARG   A 1 51  ? -37.176 20.451 -18.802 1.00 39.79  ? 1844 ARG   A C   1 
ATOM   411 O  O   . ARG   A 1 51  ? -37.224 19.240 -18.558 1.00 49.36  ? 1844 ARG   A O   1 
ATOM   412 C  CB  . ARG   A 1 51  ? -38.030 22.224 -17.232 1.00 32.16  ? 1844 ARG   A CB  1 
ATOM   413 C  CG  . ARG   A 1 51  ? -39.303 21.389 -17.101 1.00 39.26  ? 1844 ARG   A CG  1 
ATOM   414 C  CD  . ARG   A 1 51  ? -39.171 20.374 -15.985 1.00 46.06  ? 1844 ARG   A CD  1 
ATOM   415 N  NE  . ARG   A 1 51  ? -38.877 21.022 -14.702 1.00 43.04  ? 1844 ARG   A NE  1 
ATOM   416 C  CZ  . ARG   A 1 51  ? -38.298 20.409 -13.677 1.00 41.85  ? 1844 ARG   A CZ  1 
ATOM   417 N  NH1 . ARG   A 1 51  ? -37.946 19.132 -13.783 1.00 41.30  ? 1844 ARG   A NH1 1 
ATOM   418 N  NH2 . ARG   A 1 51  ? -38.070 21.069 -12.547 1.00 46.45  ? 1844 ARG   A NH2 1 
ATOM   419 N  N   . HIS   A 1 52  ? -37.429 20.942 -20.019 1.00 46.70  ? 1845 HIS   A N   1 
ATOM   420 C  CA  . HIS   A 1 52  ? -37.788 20.047 -21.119 1.00 49.22  ? 1845 HIS   A CA  1 
ATOM   421 C  C   . HIS   A 1 52  ? -36.689 19.028 -21.379 1.00 47.24  ? 1845 HIS   A C   1 
ATOM   422 O  O   . HIS   A 1 52  ? -36.962 17.831 -21.541 1.00 44.09  ? 1845 HIS   A O   1 
ATOM   423 C  CB  . HIS   A 1 52  ? -38.078 20.857 -22.385 1.00 51.39  ? 1845 HIS   A CB  1 
ATOM   424 C  CG  . HIS   A 1 52  ? -38.290 20.019 -23.613 1.00 66.12  ? 1845 HIS   A CG  1 
ATOM   425 N  ND1 . HIS   A 1 52  ? -37.250 19.564 -24.398 1.00 69.81  ? 1845 HIS   A ND1 1 
ATOM   426 C  CD2 . HIS   A 1 52  ? -39.427 19.568 -24.201 1.00 68.51  ? 1845 HIS   A CD2 1 
ATOM   427 C  CE1 . HIS   A 1 52  ? -37.735 18.864 -25.410 1.00 67.68  ? 1845 HIS   A CE1 1 
ATOM   428 N  NE2 . HIS   A 1 52  ? -39.053 18.852 -25.313 1.00 68.64  ? 1845 HIS   A NE2 1 
ATOM   429 N  N   . ARG   A 1 53  ? -35.434 19.482 -21.393 1.00 45.00  ? 1846 ARG   A N   1 
ATOM   430 C  CA  . ARG   A 1 53  ? -34.320 18.570 -21.625 1.00 44.94  ? 1846 ARG   A CA  1 
ATOM   431 C  C   . ARG   A 1 53  ? -34.220 17.516 -20.527 1.00 51.09  ? 1846 ARG   A C   1 
ATOM   432 O  O   . ARG   A 1 53  ? -33.977 16.338 -20.812 1.00 51.10  ? 1846 ARG   A O   1 
ATOM   433 C  CB  . ARG   A 1 53  ? -33.021 19.363 -21.740 1.00 48.03  ? 1846 ARG   A CB  1 
ATOM   434 C  CG  . ARG   A 1 53  ? -31.804 18.496 -21.938 1.00 65.17  ? 1846 ARG   A CG  1 
ATOM   435 C  CD  . ARG   A 1 53  ? -30.791 19.141 -22.875 1.00 71.77  ? 1846 ARG   A CD  1 
ATOM   436 N  NE  . ARG   A 1 53  ? -29.443 18.668 -22.579 1.00 79.54  ? 1846 ARG   A NE  1 
ATOM   437 C  CZ  . ARG   A 1 53  ? -28.427 18.701 -23.432 1.00 87.19  ? 1846 ARG   A CZ  1 
ATOM   438 N  NH1 . ARG   A 1 53  ? -28.601 19.173 -24.661 1.00 92.94  ? 1846 ARG   A NH1 1 
ATOM   439 N  NH2 . ARG   A 1 53  ? -27.238 18.249 -23.051 1.00 87.60  ? 1846 ARG   A NH2 1 
ATOM   440 N  N   . LEU   A 1 54  ? -34.397 17.918 -19.265 1.00 41.70  ? 1847 LEU   A N   1 
ATOM   441 C  CA  . LEU   A 1 54  ? -34.378 16.940 -18.181 1.00 50.52  ? 1847 LEU   A CA  1 
ATOM   442 C  C   . LEU   A 1 54  ? -35.488 15.908 -18.358 1.00 51.48  ? 1847 LEU   A C   1 
ATOM   443 O  O   . LEU   A 1 54  ? -35.259 14.706 -18.188 1.00 60.50  ? 1847 LEU   A O   1 
ATOM   444 C  CB  . LEU   A 1 54  ? -34.503 17.667 -16.841 1.00 50.40  ? 1847 LEU   A CB  1 
ATOM   445 C  CG  . LEU   A 1 54  ? -33.822 17.167 -15.567 1.00 47.52  ? 1847 LEU   A CG  1 
ATOM   446 C  CD1 . LEU   A 1 54  ? -32.419 16.633 -15.799 1.00 44.61  ? 1847 LEU   A CD1 1 
ATOM   447 C  CD2 . LEU   A 1 54  ? -33.776 18.317 -14.581 1.00 52.49  ? 1847 LEU   A CD2 1 
ATOM   448 N  N   . SER   A 1 55  ? -36.684 16.359 -18.752 1.00 54.99  ? 1848 SER   A N   1 
ATOM   449 C  CA  . SER   A 1 55  ? -37.828 15.462 -18.930 1.00 58.24  ? 1848 SER   A CA  1 
ATOM   450 C  C   . SER   A 1 55  ? -37.564 14.386 -19.981 1.00 63.61  ? 1848 SER   A C   1 
ATOM   451 O  O   . SER   A 1 55  ? -37.946 13.224 -19.796 1.00 66.78  ? 1848 SER   A O   1 
ATOM   452 C  CB  . SER   A 1 55  ? -39.074 16.264 -19.315 1.00 50.61  ? 1848 SER   A CB  1 
ATOM   453 O  OG  . SER   A 1 55  ? -39.572 16.999 -18.212 1.00 57.09  ? 1848 SER   A OG  1 
ATOM   454 N  N   . ARG   A 1 56  ? -36.949 14.749 -21.106 1.00 56.49  ? 1849 ARG   A N   1 
ATOM   455 C  CA  . ARG   A 1 56  ? -36.703 13.766 -22.154 1.00 62.70  ? 1849 ARG   A CA  1 
ATOM   456 C  C   . ARG   A 1 56  ? -35.409 12.990 -21.938 1.00 68.12  ? 1849 ARG   A C   1 
ATOM   457 O  O   . ARG   A 1 56  ? -35.003 12.228 -22.821 1.00 77.02  ? 1849 ARG   A O   1 
ATOM   458 C  CB  . ARG   A 1 56  ? -36.702 14.432 -23.540 1.00 62.77  ? 1849 ARG   A CB  1 
ATOM   459 C  CG  . ARG   A 1 56  ? -35.597 15.439 -23.773 1.00 68.63  ? 1849 ARG   A CG  1 
ATOM   460 C  CD  . ARG   A 1 56  ? -35.502 15.843 -25.247 1.00 81.34  ? 1849 ARG   A CD  1 
ATOM   461 N  NE  . ARG   A 1 56  ? -34.377 16.750 -25.493 1.00 78.94  ? 1849 ARG   A NE  1 
ATOM   462 C  CZ  . ARG   A 1 56  ? -33.163 16.355 -25.871 1.00 72.10  ? 1849 ARG   A CZ  1 
ATOM   463 N  NH1 . ARG   A 1 56  ? -32.909 15.065 -26.058 1.00 72.57  ? 1849 ARG   A NH1 1 
ATOM   464 N  NH2 . ARG   A 1 56  ? -32.203 17.250 -26.066 1.00 64.82  ? 1849 ARG   A NH2 1 
ATOM   465 N  N   . GLY   A 1 57  ? -34.767 13.154 -20.783 1.00 65.56  ? 1850 GLY   A N   1 
ATOM   466 C  CA  . GLY   A 1 57  ? -33.556 12.426 -20.466 1.00 65.49  ? 1850 GLY   A CA  1 
ATOM   467 C  C   . GLY   A 1 57  ? -32.293 12.951 -21.112 1.00 66.78  ? 1850 GLY   A C   1 
ATOM   468 O  O   . GLY   A 1 57  ? -31.283 12.239 -21.113 1.00 68.35  ? 1850 GLY   A O   1 
ATOM   469 N  N   . GLY   A 1 58  ? -32.304 14.183 -21.628 1.00 63.83  ? 1851 GLY   A N   1 
ATOM   470 C  CA  . GLY   A 1 58  ? -31.224 14.734 -22.438 1.00 61.50  ? 1851 GLY   A CA  1 
ATOM   471 C  C   . GLY   A 1 58  ? -29.954 15.124 -21.702 1.00 61.86  ? 1851 GLY   A C   1 
ATOM   472 O  O   . GLY   A 1 58  ? -28.991 15.534 -22.359 1.00 63.96  ? 1851 GLY   A O   1 
ATOM   473 N  N   . TYR   A 1 59  ? -29.909 15.022 -20.375 1.00 61.50  ? 1852 TYR   A N   1 
ATOM   474 C  CA  . TYR   A 1 59  ? -28.704 15.330 -19.613 1.00 62.87  ? 1852 TYR   A CA  1 
ATOM   475 C  C   . TYR   A 1 59  ? -28.056 14.032 -19.144 1.00 71.36  ? 1852 TYR   A C   1 
ATOM   476 O  O   . TYR   A 1 59  ? -28.694 13.229 -18.452 1.00 69.56  ? 1852 TYR   A O   1 
ATOM   477 C  CB  . TYR   A 1 59  ? -29.015 16.223 -18.413 1.00 61.01  ? 1852 TYR   A CB  1 
ATOM   478 C  CG  . TYR   A 1 59  ? -29.381 17.660 -18.736 1.00 54.41  ? 1852 TYR   A CG  1 
ATOM   479 C  CD1 . TYR   A 1 59  ? -28.460 18.527 -19.312 1.00 50.42  ? 1852 TYR   A CD1 1 
ATOM   480 C  CD2 . TYR   A 1 59  ? -30.639 18.158 -18.420 1.00 49.11  ? 1852 TYR   A CD2 1 
ATOM   481 C  CE1 . TYR   A 1 59  ? -28.799 19.848 -19.589 1.00 49.99  ? 1852 TYR   A CE1 1 
ATOM   482 C  CE2 . TYR   A 1 59  ? -30.985 19.469 -18.687 1.00 44.52  ? 1852 TYR   A CE2 1 
ATOM   483 C  CZ  . TYR   A 1 59  ? -30.065 20.312 -19.267 1.00 48.48  ? 1852 TYR   A CZ  1 
ATOM   484 O  OH  . TYR   A 1 59  ? -30.427 21.616 -19.528 1.00 47.80  ? 1852 TYR   A OH  1 
ATOM   485 N  N   . THR   A 1 60  ? -26.783 13.839 -19.506 1.00 72.16  ? 1853 THR   A N   1 
ATOM   486 C  CA  . THR   A 1 60  ? -26.033 12.650 -19.113 1.00 76.23  ? 1853 THR   A CA  1 
ATOM   487 C  C   . THR   A 1 60  ? -25.338 12.823 -17.767 1.00 82.80  ? 1853 THR   A C   1 
ATOM   488 O  O   . THR   A 1 60  ? -25.331 11.898 -16.947 1.00 89.55  ? 1853 THR   A O   1 
ATOM   489 C  CB  . THR   A 1 60  ? -24.996 12.302 -20.183 1.00 77.70  ? 1853 THR   A CB  1 
ATOM   490 O  OG1 . THR   A 1 60  ? -23.864 13.172 -20.057 1.00 83.48  ? 1853 THR   A OG1 1 
ATOM   491 C  CG2 . THR   A 1 60  ? -25.590 12.478 -21.570 1.00 77.72  ? 1853 THR   A CG2 1 
ATOM   492 N  N   . SER   A 1 61  ? -24.749 13.990 -17.525 1.00 78.15  ? 1854 SER   A N   1 
ATOM   493 C  CA  . SER   A 1 61  ? -24.055 14.282 -16.283 1.00 74.81  ? 1854 SER   A CA  1 
ATOM   494 C  C   . SER   A 1 61  ? -24.582 15.590 -15.717 1.00 71.98  ? 1854 SER   A C   1 
ATOM   495 O  O   . SER   A 1 61  ? -25.296 16.341 -16.388 1.00 70.91  ? 1854 SER   A O   1 
ATOM   496 C  CB  . SER   A 1 61  ? -22.539 14.374 -16.494 1.00 75.15  ? 1854 SER   A CB  1 
ATOM   497 O  OG  . SER   A 1 61  ? -22.209 15.457 -17.351 1.00 69.11  ? 1854 SER   A OG  1 
ATOM   498 N  N   . SER   A 1 62  ? -24.224 15.864 -14.464 1.00 67.14  ? 1855 SER   A N   1 
ATOM   499 C  CA  . SER   A 1 62  ? -24.607 17.133 -13.870 1.00 63.18  ? 1855 SER   A CA  1 
ATOM   500 C  C   . SER   A 1 62  ? -23.764 18.290 -14.394 1.00 60.83  ? 1855 SER   A C   1 
ATOM   501 O  O   . SER   A 1 62  ? -24.187 19.445 -14.283 1.00 62.72  ? 1855 SER   A O   1 
ATOM   502 C  CB  . SER   A 1 62  ? -24.517 17.053 -12.342 1.00 63.61  ? 1855 SER   A CB  1 
ATOM   503 O  OG  . SER   A 1 62  ? -23.173 17.050 -11.902 1.00 67.36  ? 1855 SER   A OG  1 
ATOM   504 N  N   . GLU   A 1 63  ? -22.594 18.009 -14.978 1.00 61.10  ? 1856 GLU   A N   1 
ATOM   505 C  CA  . GLU   A 1 63  ? -21.795 19.076 -15.578 1.00 57.67  ? 1856 GLU   A CA  1 
ATOM   506 C  C   . GLU   A 1 63  ? -22.477 19.650 -16.814 1.00 59.31  ? 1856 GLU   A C   1 
ATOM   507 O  O   . GLU   A 1 63  ? -22.437 20.865 -17.038 1.00 55.33  ? 1856 GLU   A O   1 
ATOM   508 C  CB  . GLU   A 1 63  ? -20.395 18.568 -15.925 1.00 64.78  ? 1856 GLU   A CB  1 
ATOM   509 C  CG  . GLU   A 1 63  ? -19.386 18.670 -14.781 1.00 75.86  ? 1856 GLU   A CG  1 
ATOM   510 C  CD  . GLU   A 1 63  ? -19.505 17.541 -13.764 1.00 86.40  ? 1856 GLU   A CD  1 
ATOM   511 O  OE1 . GLU   A 1 63  ? -20.259 16.572 -14.012 1.00 87.86  ? 1856 GLU   A OE1 1 
ATOM   512 O  OE2 . GLU   A 1 63  ? -18.832 17.626 -12.714 1.00 87.62  ? 1856 GLU   A OE2 1 
ATOM   513 N  N   . GLU   A 1 64  ? -23.092 18.791 -17.637 1.00 61.91  ? 1857 GLU   A N   1 
ATOM   514 C  CA  . GLU   A 1 64  ? -23.916 19.274 -18.743 1.00 56.79  ? 1857 GLU   A CA  1 
ATOM   515 C  C   . GLU   A 1 64  ? -25.006 20.214 -18.244 1.00 50.34  ? 1857 GLU   A C   1 
ATOM   516 O  O   . GLU   A 1 64  ? -25.238 21.281 -18.823 1.00 52.19  ? 1857 GLU   A O   1 
ATOM   517 C  CB  . GLU   A 1 64  ? -24.557 18.101 -19.487 1.00 64.82  ? 1857 GLU   A CB  1 
ATOM   518 C  CG  . GLU   A 1 64  ? -23.702 17.417 -20.527 1.00 78.85  ? 1857 GLU   A CG  1 
ATOM   519 C  CD  . GLU   A 1 64  ? -24.469 16.310 -21.233 1.00 91.27  ? 1857 GLU   A CD  1 
ATOM   520 O  OE1 . GLU   A 1 64  ? -24.252 16.101 -22.444 1.00 99.69  ? 1857 GLU   A OE1 1 
ATOM   521 O  OE2 . GLU   A 1 64  ? -25.305 15.655 -20.575 1.00 92.81  ? 1857 GLU   A OE2 1 
ATOM   522 N  N   . PHE   A 1 65  ? -25.705 19.810 -17.178 1.00 48.59  ? 1858 PHE   A N   1 
ATOM   523 C  CA  . PHE   A 1 65  ? -26.774 20.633 -16.617 1.00 40.43  ? 1858 PHE   A CA  1 
ATOM   524 C  C   . PHE   A 1 65  ? -26.246 21.993 -16.179 1.00 36.46  ? 1858 PHE   A C   1 
ATOM   525 O  O   . PHE   A 1 65  ? -26.862 23.028 -16.454 1.00 43.29  ? 1858 PHE   A O   1 
ATOM   526 C  CB  . PHE   A 1 65  ? -27.430 19.905 -15.442 1.00 39.05  ? 1858 PHE   A CB  1 
ATOM   527 C  CG  . PHE   A 1 65  ? -28.525 20.691 -14.765 1.00 40.30  ? 1858 PHE   A CG  1 
ATOM   528 C  CD1 . PHE   A 1 65  ? -28.243 21.502 -13.670 1.00 40.19  ? 1858 PHE   A CD1 1 
ATOM   529 C  CD2 . PHE   A 1 65  ? -29.837 20.599 -15.207 1.00 44.06  ? 1858 PHE   A CD2 1 
ATOM   530 C  CE1 . PHE   A 1 65  ? -29.245 22.230 -13.048 1.00 42.67  ? 1858 PHE   A CE1 1 
ATOM   531 C  CE2 . PHE   A 1 65  ? -30.850 21.316 -14.577 1.00 42.28  ? 1858 PHE   A CE2 1 
ATOM   532 C  CZ  . PHE   A 1 65  ? -30.553 22.129 -13.498 1.00 37.67  ? 1858 PHE   A CZ  1 
ATOM   533 N  N   . ALA   A 1 66  ? -25.095 22.007 -15.499 1.00 39.01  ? 1859 ALA   A N   1 
ATOM   534 C  CA  . ALA   A 1 66  ? -24.518 23.262 -15.024 1.00 46.03  ? 1859 ALA   A CA  1 
ATOM   535 C  C   . ALA   A 1 66  ? -24.152 24.184 -16.181 1.00 44.38  ? 1859 ALA   A C   1 
ATOM   536 O  O   . ALA   A 1 66  ? -24.352 25.404 -16.098 1.00 48.30  ? 1859 ALA   A O   1 
ATOM   537 C  CB  . ALA   A 1 66  ? -23.288 22.980 -14.160 1.00 48.21  ? 1859 ALA   A CB  1 
ATOM   538 N  N   . ALA   A 1 67  ? -23.625 23.618 -17.271 1.00 36.33  ? 1860 ALA   A N   1 
ATOM   539 C  CA  . ALA   A 1 67  ? -23.293 24.426 -18.441 1.00 40.60  ? 1860 ALA   A CA  1 
ATOM   540 C  C   . ALA   A 1 67  ? -24.513 25.165 -18.982 1.00 31.53  ? 1860 ALA   A C   1 
ATOM   541 O  O   . ALA   A 1 67  ? -24.408 26.324 -19.393 1.00 37.79  ? 1860 ALA   A O   1 
ATOM   542 C  CB  . ALA   A 1 67  ? -22.684 23.543 -19.534 1.00 41.47  ? 1860 ALA   A CB  1 
ATOM   543 N  N   . ASP   A 1 68  ? -25.680 24.516 -18.992 1.00 28.98  ? 1861 ASP   A N   1 
ATOM   544 C  CA  . ASP   A 1 68  ? -26.901 25.205 -19.411 1.00 33.23  ? 1861 ASP   A CA  1 
ATOM   545 C  C   . ASP   A 1 68  ? -27.298 26.298 -18.425 1.00 34.20  ? 1861 ASP   A C   1 
ATOM   546 O  O   . ASP   A 1 68  ? -27.617 27.424 -18.828 1.00 34.57  ? 1861 ASP   A O   1 
ATOM   547 C  CB  . ASP   A 1 68  ? -28.046 24.203 -19.578 1.00 39.02  ? 1861 ASP   A CB  1 
ATOM   548 C  CG  . ASP   A 1 68  ? -28.075 23.584 -20.975 1.00 44.95  ? 1861 ASP   A CG  1 
ATOM   549 O  OD1 . ASP   A 1 68  ? -27.336 24.095 -21.836 1.00 38.79  ? 1861 ASP   A OD1 1 
ATOM   550 O  OD2 . ASP   A 1 68  ? -28.820 22.600 -21.209 1.00 41.64  ? 1861 ASP   A OD2 1 
ATOM   551 N  N   . ALA   A 1 69  ? -27.322 25.974 -17.129 1.00 30.43  ? 1862 ALA   A N   1 
ATOM   552 C  CA  . ALA   A 1 69  ? -27.651 26.976 -16.119 1.00 35.57  ? 1862 ALA   A CA  1 
ATOM   553 C  C   . ALA   A 1 69  ? -26.741 28.192 -16.247 1.00 33.91  ? 1862 ALA   A C   1 
ATOM   554 O  O   . ALA   A 1 69  ? -27.209 29.339 -16.274 1.00 30.15  ? 1862 ALA   A O   1 
ATOM   555 C  CB  . ALA   A 1 69  ? -27.545 26.359 -14.714 1.00 31.18  ? 1862 ALA   A CB  1 
ATOM   556 N  N   . LEU   A 1 70  ? -25.430 27.958 -16.349 1.00 32.85  ? 1863 LEU   A N   1 
ATOM   557 C  CA  . LEU   A 1 70  ? -24.494 29.076 -16.450 1.00 34.96  ? 1863 LEU   A CA  1 
ATOM   558 C  C   . LEU   A 1 70  ? -24.671 29.844 -17.756 1.00 33.72  ? 1863 LEU   A C   1 
ATOM   559 O  O   . LEU   A 1 70  ? -24.381 31.048 -17.819 1.00 32.96  ? 1863 LEU   A O   1 
ATOM   560 C  CB  . LEU   A 1 70  ? -23.058 28.568 -16.319 1.00 37.56  ? 1863 LEU   A CB  1 
ATOM   561 C  CG  . LEU   A 1 70  ? -22.710 28.014 -14.933 1.00 48.91  ? 1863 LEU   A CG  1 
ATOM   562 C  CD1 . LEU   A 1 70  ? -21.266 27.539 -14.894 1.00 49.75  ? 1863 LEU   A CD1 1 
ATOM   563 C  CD2 . LEU   A 1 70  ? -22.963 29.071 -13.856 1.00 42.80  ? 1863 LEU   A CD2 1 
ATOM   564 N  N   . LEU   A 1 71  ? -25.128 29.168 -18.808 1.00 29.45  ? 1864 LEU   A N   1 
ATOM   565 C  CA  . LEU   A 1 71  ? -25.403 29.860 -20.063 1.00 28.73  ? 1864 LEU   A CA  1 
ATOM   566 C  C   . LEU   A 1 71  ? -26.538 30.869 -19.898 1.00 29.59  ? 1864 LEU   A C   1 
ATOM   567 O  O   . LEU   A 1 71  ? -26.481 31.972 -20.461 1.00 31.89  ? 1864 LEU   A O   1 
ATOM   568 C  CB  . LEU   A 1 71  ? -25.735 28.837 -21.146 1.00 29.90  ? 1864 LEU   A CB  1 
ATOM   569 C  CG  . LEU   A 1 71  ? -26.097 29.359 -22.532 1.00 32.88  ? 1864 LEU   A CG  1 
ATOM   570 C  CD1 . LEU   A 1 71  ? -24.934 30.148 -23.127 1.00 25.83  ? 1864 LEU   A CD1 1 
ATOM   571 C  CD2 . LEU   A 1 71  ? -26.421 28.161 -23.391 1.00 35.48  ? 1864 LEU   A CD2 1 
ATOM   572 N  N   . VAL   A 1 72  ? -27.576 30.507 -19.128 1.00 29.28  ? 1865 VAL   A N   1 
ATOM   573 C  CA  . VAL   A 1 72  ? -28.652 31.452 -18.819 1.00 31.47  ? 1865 VAL   A CA  1 
ATOM   574 C  C   . VAL   A 1 72  ? -28.073 32.755 -18.275 1.00 29.79  ? 1865 VAL   A C   1 
ATOM   575 O  O   . VAL   A 1 72  ? -28.406 33.852 -18.739 1.00 30.62  ? 1865 VAL   A O   1 
ATOM   576 C  CB  . VAL   A 1 72  ? -29.650 30.836 -17.823 1.00 26.28  ? 1865 VAL   A CB  1 
ATOM   577 C  CG1 . VAL   A 1 72  ? -30.679 31.866 -17.445 1.00 27.34  ? 1865 VAL   A CG1 1 
ATOM   578 C  CG2 . VAL   A 1 72  ? -30.336 29.595 -18.403 1.00 29.23  ? 1865 VAL   A CG2 1 
ATOM   579 N  N   . PHE   A 1 73  ? -27.174 32.650 -17.299 1.00 29.20  ? 1866 PHE   A N   1 
ATOM   580 C  CA  . PHE   A 1 73  ? -26.695 33.843 -16.607 1.00 27.23  ? 1866 PHE   A CA  1 
ATOM   581 C  C   . PHE   A 1 73  ? -25.591 34.556 -17.375 1.00 28.25  ? 1866 PHE   A C   1 
ATOM   582 O  O   . PHE   A 1 73  ? -25.439 35.773 -17.226 1.00 32.61  ? 1866 PHE   A O   1 
ATOM   583 C  CB  . PHE   A 1 73  ? -26.241 33.459 -15.197 1.00 26.95  ? 1866 PHE   A CB  1 
ATOM   584 C  CG  . PHE   A 1 73  ? -27.279 32.679 -14.447 1.00 32.45  ? 1866 PHE   A CG  1 
ATOM   585 C  CD1 . PHE   A 1 73  ? -28.590 33.140 -14.389 1.00 33.99  ? 1866 PHE   A CD1 1 
ATOM   586 C  CD2 . PHE   A 1 73  ? -26.967 31.465 -13.845 1.00 34.01  ? 1866 PHE   A CD2 1 
ATOM   587 C  CE1 . PHE   A 1 73  ? -29.566 32.414 -13.723 1.00 33.98  ? 1866 PHE   A CE1 1 
ATOM   588 C  CE2 . PHE   A 1 73  ? -27.941 30.738 -13.178 1.00 36.74  ? 1866 PHE   A CE2 1 
ATOM   589 C  CZ  . PHE   A 1 73  ? -29.241 31.216 -13.117 1.00 28.69  ? 1866 PHE   A CZ  1 
ATOM   590 N  N   . ASP   A 1 74  ? -24.818 33.832 -18.194 1.00 30.78  ? 1867 ASP   A N   1 
ATOM   591 C  CA  . ASP   A 1 74  ? -23.901 34.492 -19.130 1.00 39.06  ? 1867 ASP   A CA  1 
ATOM   592 C  C   . ASP   A 1 74  ? -24.664 35.291 -20.195 1.00 38.55  ? 1867 ASP   A C   1 
ATOM   593 O  O   . ASP   A 1 74  ? -24.329 36.449 -20.477 1.00 31.71  ? 1867 ASP   A O   1 
ATOM   594 C  CB  . ASP   A 1 74  ? -22.975 33.460 -19.791 1.00 35.63  ? 1867 ASP   A CB  1 
ATOM   595 C  CG  . ASP   A 1 74  ? -21.936 32.881 -18.819 1.00 49.29  ? 1867 ASP   A CG  1 
ATOM   596 O  OD1 . ASP   A 1 74  ? -21.641 33.519 -17.778 1.00 49.64  ? 1867 ASP   A OD1 1 
ATOM   597 O  OD2 . ASP   A 1 74  ? -21.400 31.785 -19.110 1.00 50.36  ? 1867 ASP   A OD2 1 
ATOM   598 N  N   . ASN   A 1 75  ? -25.681 34.684 -20.821 1.00 30.18  ? 1868 ASN   A N   1 
ATOM   599 C  CA  . ASN   A 1 75  ? -26.544 35.447 -21.727 1.00 25.28  ? 1868 ASN   A CA  1 
ATOM   600 C  C   . ASN   A 1 75  ? -27.117 36.682 -21.040 1.00 33.74  ? 1868 ASN   A C   1 
ATOM   601 O  O   . ASN   A 1 75  ? -27.123 37.784 -21.602 1.00 24.87  ? 1868 ASN   A O   1 
ATOM   602 C  CB  . ASN   A 1 75  ? -27.675 34.561 -22.234 1.00 29.22  ? 1868 ASN   A CB  1 
ATOM   603 C  CG  . ASN   A 1 75  ? -27.169 33.497 -23.174 1.00 33.99  ? 1868 ASN   A CG  1 
ATOM   604 O  OD1 . ASN   A 1 75  ? -26.053 33.598 -23.662 1.00 31.02  ? 1868 ASN   A OD1 1 
ATOM   605 N  ND2 . ASN   A 1 75  ? -27.976 32.476 -23.429 1.00 35.82  ? 1868 ASN   A ND2 1 
ATOM   606 N  N   . CYS   A 1 76  ? -27.608 36.510 -19.812 1.00 26.28  ? 1869 CYS   A N   1 
ATOM   607 C  CA  . CYS   A 1 76  ? -28.226 37.619 -19.097 1.00 25.26  ? 1869 CYS   A CA  1 
ATOM   608 C  C   . CYS   A 1 76  ? -27.242 38.774 -18.912 1.00 30.68  ? 1869 CYS   A C   1 
ATOM   609 O  O   . CYS   A 1 76  ? -27.565 39.935 -19.192 1.00 30.01  ? 1869 CYS   A O   1 
ATOM   610 C  CB  . CYS   A 1 76  ? -28.743 37.127 -17.746 1.00 27.27  ? 1869 CYS   A CB  1 
ATOM   611 S  SG  . CYS   A 1 76  ? -29.540 38.415 -16.810 1.00 34.01  ? 1869 CYS   A SG  1 
ATOM   612 N  N   . GLN   A 1 77  ? -26.025 38.472 -18.459 1.00 24.67  ? 1870 GLN   A N   1 
ATOM   613 C  CA  . GLN   A 1 77  ? -25.035 39.529 -18.272 1.00 27.01  ? 1870 GLN   A CA  1 
ATOM   614 C  C   . GLN   A 1 77  ? -24.506 40.079 -19.585 1.00 30.86  ? 1870 GLN   A C   1 
ATOM   615 O  O   . GLN   A 1 77  ? -24.006 41.211 -19.614 1.00 32.13  ? 1870 GLN   A O   1 
ATOM   616 C  CB  . GLN   A 1 77  ? -23.869 39.019 -17.428 1.00 26.53  ? 1870 GLN   A CB  1 
ATOM   617 C  CG  . GLN   A 1 77  ? -24.291 38.624 -16.006 1.00 25.65  ? 1870 GLN   A CG  1 
ATOM   618 C  CD  . GLN   A 1 77  ? -23.148 38.008 -15.241 1.00 31.58  ? 1870 GLN   A CD  1 
ATOM   619 O  OE1 . GLN   A 1 77  ? -22.351 38.714 -14.606 1.00 33.68  ? 1870 GLN   A OE1 1 
ATOM   620 N  NE2 . GLN   A 1 77  ? -23.042 36.683 -15.310 1.00 25.61  ? 1870 GLN   A NE2 1 
ATOM   621 N  N   . THR   A 1 78  ? -24.578 39.303 -20.666 1.00 28.03  ? 1871 THR   A N   1 
ATOM   622 C  CA  . THR   A 1 78  ? -24.134 39.817 -21.956 1.00 33.63  ? 1871 THR   A CA  1 
ATOM   623 C  C   . THR   A 1 78  ? -25.104 40.852 -22.496 1.00 34.03  ? 1871 THR   A C   1 
ATOM   624 O  O   . THR   A 1 78  ? -24.680 41.883 -23.030 1.00 32.97  ? 1871 THR   A O   1 
ATOM   625 C  CB  . THR   A 1 78  ? -23.954 38.663 -22.942 1.00 26.81  ? 1871 THR   A CB  1 
ATOM   626 O  OG1 . THR   A 1 78  ? -22.786 37.924 -22.549 1.00 29.01  ? 1871 THR   A OG1 1 
ATOM   627 C  CG2 . THR   A 1 78  ? -23.791 39.174 -24.404 1.00 22.31  ? 1871 THR   A CG2 1 
ATOM   628 N  N   . PHE   A 1 79  ? -26.407 40.616 -22.347 1.00 34.76  ? 1872 PHE   A N   1 
ATOM   629 C  CA  . PHE   A 1 79  ? -27.388 41.474 -22.999 1.00 32.37  ? 1872 PHE   A CA  1 
ATOM   630 C  C   . PHE   A 1 79  ? -27.940 42.573 -22.100 1.00 37.02  ? 1872 PHE   A C   1 
ATOM   631 O  O   . PHE   A 1 79  ? -28.324 43.634 -22.603 1.00 32.07  ? 1872 PHE   A O   1 
ATOM   632 C  CB  . PHE   A 1 79  ? -28.561 40.641 -23.530 1.00 33.06  ? 1872 PHE   A CB  1 
ATOM   633 C  CG  . PHE   A 1 79  ? -29.424 41.391 -24.512 1.00 38.99  ? 1872 PHE   A CG  1 
ATOM   634 C  CD1 . PHE   A 1 79  ? -29.142 41.352 -25.865 1.00 31.65  ? 1872 PHE   A CD1 1 
ATOM   635 C  CD2 . PHE   A 1 79  ? -30.489 42.158 -24.079 1.00 41.12  ? 1872 PHE   A CD2 1 
ATOM   636 C  CE1 . PHE   A 1 79  ? -29.919 42.046 -26.774 1.00 35.92  ? 1872 PHE   A CE1 1 
ATOM   637 C  CE2 . PHE   A 1 79  ? -31.265 42.861 -24.982 1.00 40.68  ? 1872 PHE   A CE2 1 
ATOM   638 C  CZ  . PHE   A 1 79  ? -30.977 42.806 -26.326 1.00 38.36  ? 1872 PHE   A CZ  1 
ATOM   639 N  N   . ASN   A 1 80  ? -28.001 42.358 -20.792 1.00 38.43  ? 1873 ASN   A N   1 
ATOM   640 C  CA  . ASN   A 1 80  ? -28.671 43.282 -19.889 1.00 37.74  ? 1873 ASN   A CA  1 
ATOM   641 C  C   . ASN   A 1 80  ? -27.663 43.999 -19.007 1.00 39.63  ? 1873 ASN   A C   1 
ATOM   642 O  O   . ASN   A 1 80  ? -26.660 43.410 -18.575 1.00 30.04  ? 1873 ASN   A O   1 
ATOM   643 C  CB  . ASN   A 1 80  ? -29.697 42.540 -19.031 1.00 36.00  ? 1873 ASN   A CB  1 
ATOM   644 C  CG  . ASN   A 1 80  ? -30.649 41.726 -19.880 1.00 36.05  ? 1873 ASN   A CG  1 
ATOM   645 O  OD1 . ASN   A 1 80  ? -31.634 42.251 -20.378 1.00 36.69  ? 1873 ASN   A OD1 1 
ATOM   646 N  ND2 . ASN   A 1 80  ? -30.325 40.448 -20.097 1.00 37.98  ? 1873 ASN   A ND2 1 
ATOM   647 N  N   . GLU   A 1 81  ? -27.926 45.281 -18.772 1.00 32.82  ? 1874 GLU   A N   1 
ATOM   648 C  CA  . GLU   A 1 81  ? -27.117 46.051 -17.838 1.00 34.44  ? 1874 GLU   A CA  1 
ATOM   649 C  C   . GLU   A 1 81  ? -27.242 45.456 -16.444 1.00 34.57  ? 1874 GLU   A C   1 
ATOM   650 O  O   . GLU   A 1 81  ? -28.308 44.961 -16.058 1.00 35.49  ? 1874 GLU   A O   1 
ATOM   651 C  CB  . GLU   A 1 81  ? -27.568 47.514 -17.819 1.00 41.59  ? 1874 GLU   A CB  1 
ATOM   652 C  CG  . GLU   A 1 81  ? -27.764 48.135 -19.184 1.00 65.33  ? 1874 GLU   A CG  1 
ATOM   653 C  CD  . GLU   A 1 81  ? -26.467 48.627 -19.786 1.00 85.40  ? 1874 GLU   A CD  1 
ATOM   654 O  OE1 . GLU   A 1 81  ? -26.527 49.472 -20.705 1.00 92.30  ? 1874 GLU   A OE1 1 
ATOM   655 O  OE2 . GLU   A 1 81  ? -25.387 48.179 -19.338 1.00 90.40  ? 1874 GLU   A OE2 1 
ATOM   656 N  N   . ASP   A 1 82  ? -26.141 45.508 -15.690 1.00 32.65  ? 1875 ASP   A N   1 
ATOM   657 C  CA  . ASP   A 1 82  ? -26.142 45.023 -14.311 1.00 43.75  ? 1875 ASP   A CA  1 
ATOM   658 C  C   . ASP   A 1 82  ? -27.187 45.724 -13.454 1.00 43.13  ? 1875 ASP   A C   1 
ATOM   659 O  O   . ASP   A 1 82  ? -27.667 45.144 -12.474 1.00 45.36  ? 1875 ASP   A O   1 
ATOM   660 C  CB  . ASP   A 1 82  ? -24.750 45.199 -13.698 1.00 30.77  ? 1875 ASP   A CB  1 
ATOM   661 C  CG  . ASP   A 1 82  ? -23.690 44.377 -14.427 1.00 37.34  ? 1875 ASP   A CG  1 
ATOM   662 O  OD1 . ASP   A 1 82  ? -23.949 43.182 -14.717 1.00 35.19  ? 1875 ASP   A OD1 1 
ATOM   663 O  OD2 . ASP   A 1 82  ? -22.607 44.926 -14.724 1.00 33.16  ? 1875 ASP   A OD2 1 
ATOM   664 N  N   . ASP   A 1 83  ? -27.552 46.960 -13.791 1.00 44.39  ? 1876 ASP   A N   1 
ATOM   665 C  CA  . ASP   A 1 83  ? -28.539 47.701 -13.018 1.00 48.51  ? 1876 ASP   A CA  1 
ATOM   666 C  C   . ASP   A 1 83  ? -29.922 47.692 -13.659 1.00 50.60  ? 1876 ASP   A C   1 
ATOM   667 O  O   . ASP   A 1 83  ? -30.815 48.398 -13.185 1.00 54.31  ? 1876 ASP   A O   1 
ATOM   668 C  CB  . ASP   A 1 83  ? -28.072 49.140 -12.789 1.00 60.40  ? 1876 ASP   A CB  1 
ATOM   669 C  CG  . ASP   A 1 83  ? -27.913 49.925 -14.075 1.00 68.64  ? 1876 ASP   A CG  1 
ATOM   670 O  OD1 . ASP   A 1 83  ? -28.066 49.342 -15.169 1.00 72.04  ? 1876 ASP   A OD1 1 
ATOM   671 O  OD2 . ASP   A 1 83  ? -27.626 51.140 -13.984 1.00 74.87  ? 1876 ASP   A OD2 1 
ATOM   672 N  N   . SER   A 1 84  ? -30.119 46.917 -14.723 1.00 45.84  ? 1877 SER   A N   1 
ATOM   673 C  CA  . SER   A 1 84  ? -31.453 46.749 -15.275 1.00 43.73  ? 1877 SER   A CA  1 
ATOM   674 C  C   . SER   A 1 84  ? -32.266 45.805 -14.396 1.00 37.54  ? 1877 SER   A C   1 
ATOM   675 O  O   . SER   A 1 84  ? -31.732 45.089 -13.542 1.00 40.96  ? 1877 SER   A O   1 
ATOM   676 C  CB  . SER   A 1 84  ? -31.392 46.197 -16.700 1.00 40.37  ? 1877 SER   A CB  1 
ATOM   677 O  OG  . SER   A 1 84  ? -30.859 44.887 -16.693 1.00 36.32  ? 1877 SER   A OG  1 
ATOM   678 N  N   . GLU   A 1 85  ? -33.582 45.808 -14.622 1.00 43.69  ? 1878 GLU   A N   1 
ATOM   679 C  CA  . GLU   A 1 85  ? -34.461 44.916 -13.871 1.00 41.00  ? 1878 GLU   A CA  1 
ATOM   680 C  C   . GLU   A 1 85  ? -34.106 43.452 -14.132 1.00 46.53  ? 1878 GLU   A C   1 
ATOM   681 O  O   . GLU   A 1 85  ? -34.007 42.650 -13.192 1.00 44.56  ? 1878 GLU   A O   1 
ATOM   682 C  CB  . GLU   A 1 85  ? -35.920 45.215 -14.231 1.00 48.47  ? 1878 GLU   A CB  1 
ATOM   683 C  CG  . GLU   A 1 85  ? -36.946 44.998 -13.115 1.00 62.03  ? 1878 GLU   A CG  1 
ATOM   684 C  CD  . GLU   A 1 85  ? -36.594 45.717 -11.815 1.00 80.19  ? 1878 GLU   A CD  1 
ATOM   685 O  OE1 . GLU   A 1 85  ? -36.491 45.039 -10.768 1.00 81.73  ? 1878 GLU   A OE1 1 
ATOM   686 O  OE2 . GLU   A 1 85  ? -36.420 46.957 -11.836 1.00 87.92  ? 1878 GLU   A OE2 1 
ATOM   687 N  N   . VAL   A 1 86  ? -33.879 43.091 -15.400 1.00 37.95  ? 1879 VAL   A N   1 
ATOM   688 C  CA  . VAL   A 1 86  ? -33.530 41.711 -15.717 1.00 34.09  ? 1879 VAL   A CA  1 
ATOM   689 C  C   . VAL   A 1 86  ? -32.125 41.394 -15.225 1.00 35.15  ? 1879 VAL   A C   1 
ATOM   690 O  O   . VAL   A 1 86  ? -31.875 40.312 -14.683 1.00 30.41  ? 1879 VAL   A O   1 
ATOM   691 C  CB  . VAL   A 1 86  ? -33.675 41.447 -17.226 1.00 36.71  ? 1879 VAL   A CB  1 
ATOM   692 C  CG1 . VAL   A 1 86  ? -33.004 40.120 -17.590 1.00 31.36  ? 1879 VAL   A CG1 1 
ATOM   693 C  CG2 . VAL   A 1 86  ? -35.153 41.449 -17.630 1.00 34.83  ? 1879 VAL   A CG2 1 
ATOM   694 N  N   . GLY   A 1 87  ? -31.193 42.339 -15.388 1.00 35.20  ? 1880 GLY   A N   1 
ATOM   695 C  CA  . GLY   A 1 87  ? -29.839 42.129 -14.902 1.00 36.90  ? 1880 GLY   A CA  1 
ATOM   696 C  C   . GLY   A 1 87  ? -29.779 41.916 -13.398 1.00 44.14  ? 1880 GLY   A C   1 
ATOM   697 O  O   . GLY   A 1 87  ? -29.092 41.010 -12.913 1.00 30.53  ? 1880 GLY   A O   1 
ATOM   698 N  N   . LYS   A 1 88  ? -30.496 42.747 -12.631 1.00 40.11  ? 1881 LYS   A N   1 
ATOM   699 C  CA  . LYS   A 1 88  ? -30.512 42.542 -11.184 1.00 41.59  ? 1881 LYS   A CA  1 
ATOM   700 C  C   . LYS   A 1 88  ? -31.064 41.167 -10.831 1.00 41.48  ? 1881 LYS   A C   1 
ATOM   701 O  O   . LYS   A 1 88  ? -30.499 40.462 -9.987  1.00 35.53  ? 1881 LYS   A O   1 
ATOM   702 C  CB  . LYS   A 1 88  ? -31.319 43.637 -10.484 1.00 42.45  ? 1881 LYS   A CB  1 
ATOM   703 C  CG  . LYS   A 1 88  ? -30.630 44.989 -10.450 1.00 42.84  ? 1881 LYS   A CG  1 
ATOM   704 C  CD  . LYS   A 1 88  ? -31.408 45.997 -9.638  1.00 48.03  ? 1881 LYS   A CD  1 
ATOM   705 C  CE  . LYS   A 1 88  ? -32.582 46.585 -10.397 1.00 56.43  ? 1881 LYS   A CE  1 
ATOM   706 N  NZ  . LYS   A 1 88  ? -33.223 47.666 -9.569  1.00 64.87  ? 1881 LYS   A NZ  1 
ATOM   707 N  N   . ALA   A 1 89  ? -32.155 40.754 -11.481 1.00 33.65  ? 1882 ALA   A N   1 
ATOM   708 C  CA  . ALA   A 1 89  ? -32.719 39.446 -11.166 1.00 38.05  ? 1882 ALA   A CA  1 
ATOM   709 C  C   . ALA   A 1 89  ? -31.742 38.331 -11.528 1.00 40.98  ? 1882 ALA   A C   1 
ATOM   710 O  O   . ALA   A 1 89  ? -31.634 37.327 -10.807 1.00 39.21  ? 1882 ALA   A O   1 
ATOM   711 C  CB  . ALA   A 1 89  ? -34.057 39.261 -11.882 1.00 36.41  ? 1882 ALA   A CB  1 
ATOM   712 N  N   . GLY   A 1 90  ? -30.992 38.508 -12.619 1.00 32.66  ? 1883 GLY   A N   1 
ATOM   713 C  CA  . GLY   A 1 90  ? -30.051 37.486 -13.041 1.00 31.74  ? 1883 GLY   A CA  1 
ATOM   714 C  C   . GLY   A 1 90  ? -28.888 37.318 -12.083 1.00 31.54  ? 1883 GLY   A C   1 
ATOM   715 O  O   . GLY   A 1 90  ? -28.349 36.216 -11.941 1.00 27.96  ? 1883 GLY   A O   1 
ATOM   716 N  N   . HIS   A 1 91  ? -28.460 38.400 -11.437 1.00 29.00  ? 1884 HIS   A N   1 
ATOM   717 C  CA  . HIS   A 1 91  ? -27.389 38.260 -10.459 1.00 35.33  ? 1884 HIS   A CA  1 
ATOM   718 C  C   . HIS   A 1 91  ? -27.876 37.510 -9.225  1.00 32.35  ? 1884 HIS   A C   1 
ATOM   719 O  O   . HIS   A 1 91  ? -27.153 36.672 -8.679  1.00 27.62  ? 1884 HIS   A O   1 
ATOM   720 C  CB  . HIS   A 1 91  ? -26.841 39.629 -10.085 1.00 35.82  ? 1884 HIS   A CB  1 
ATOM   721 C  CG  . HIS   A 1 91  ? -25.968 40.218 -11.139 1.00 34.51  ? 1884 HIS   A CG  1 
ATOM   722 N  ND1 . HIS   A 1 91  ? -24.858 39.565 -11.628 1.00 34.25  ? 1884 HIS   A ND1 1 
ATOM   723 C  CD2 . HIS   A 1 91  ? -26.048 41.389 -11.814 1.00 31.17  ? 1884 HIS   A CD2 1 
ATOM   724 C  CE1 . HIS   A 1 91  ? -24.287 40.313 -12.555 1.00 34.36  ? 1884 HIS   A CE1 1 
ATOM   725 N  NE2 . HIS   A 1 91  ? -24.988 41.427 -12.682 1.00 38.28  ? 1884 HIS   A NE2 1 
ATOM   726 N  N   . ILE   A 1 92  ? -29.110 37.775 -8.794  1.00 27.82  ? 1885 ILE   A N   1 
ATOM   727 C  CA  . ILE   A 1 92  ? -29.687 37.017 -7.686  1.00 40.01  ? 1885 ILE   A CA  1 
ATOM   728 C  C   . ILE   A 1 92  ? -29.752 35.529 -8.031  1.00 40.33  ? 1885 ILE   A C   1 
ATOM   729 O  O   . ILE   A 1 92  ? -29.348 34.667 -7.232  1.00 30.94  ? 1885 ILE   A O   1 
ATOM   730 C  CB  . ILE   A 1 92  ? -31.071 37.577 -7.326  1.00 37.43  ? 1885 ILE   A CB  1 
ATOM   731 C  CG1 . ILE   A 1 92  ? -30.931 39.008 -6.790  1.00 42.21  ? 1885 ILE   A CG1 1 
ATOM   732 C  CG2 . ILE   A 1 92  ? -31.749 36.682 -6.299  1.00 43.61  ? 1885 ILE   A CG2 1 
ATOM   733 C  CD1 . ILE   A 1 92  ? -32.252 39.746 -6.657  1.00 44.63  ? 1885 ILE   A CD1 1 
ATOM   734 N  N   . MET   A 1 93  ? -30.250 35.201 -9.229  1.00 33.64  ? 1886 MET   A N   1 
ATOM   735 C  CA  . MET   A 1 93  ? -30.378 33.793 -9.599  1.00 34.62  ? 1886 MET   A CA  1 
ATOM   736 C  C   . MET   A 1 93  ? -29.017 33.139 -9.786  1.00 32.78  ? 1886 MET   A C   1 
ATOM   737 O  O   . MET   A 1 93  ? -28.840 31.963 -9.444  1.00 37.73  ? 1886 MET   A O   1 
ATOM   738 C  CB  . MET   A 1 93  ? -31.211 33.643 -10.870 1.00 33.14  ? 1886 MET   A CB  1 
ATOM   739 C  CG  . MET   A 1 93  ? -32.664 34.029 -10.707 1.00 36.30  ? 1886 MET   A CG  1 
ATOM   740 S  SD  . MET   A 1 93  ? -33.456 33.094 -9.370  1.00 45.55  ? 1886 MET   A SD  1 
ATOM   741 C  CE  . MET   A 1 93  ? -33.287 31.422 -10.002 1.00 42.36  ? 1886 MET   A CE  1 
ATOM   742 N  N   . ARG   A 1 94  ? -28.043 33.886 -10.312 1.00 33.97  ? 1887 ARG   A N   1 
ATOM   743 C  CA  . ARG   A 1 94  ? -26.719 33.324 -10.547 1.00 30.93  ? 1887 ARG   A CA  1 
ATOM   744 C  C   . ARG   A 1 94  ? -26.018 33.033 -9.228  1.00 32.10  ? 1887 ARG   A C   1 
ATOM   745 O  O   . ARG   A 1 94  ? -25.392 31.978 -9.070  1.00 32.99  ? 1887 ARG   A O   1 
ATOM   746 C  CB  . ARG   A 1 94  ? -25.884 34.277 -11.423 1.00 24.45  ? 1887 ARG   A CB  1 
ATOM   747 C  CG  . ARG   A 1 94  ? -24.460 33.801 -11.727 1.00 26.79  ? 1887 ARG   A CG  1 
ATOM   748 C  CD  . ARG   A 1 94  ? -23.612 34.914 -12.382 1.00 29.17  ? 1887 ARG   A CD  1 
ATOM   749 N  NE  . ARG   A 1 94  ? -23.739 36.190 -11.670 1.00 30.14  ? 1887 ARG   A NE  1 
ATOM   750 C  CZ  . ARG   A 1 94  ? -23.118 36.481 -10.518 1.00 35.72  ? 1887 ARG   A CZ  1 
ATOM   751 N  NH1 . ARG   A 1 94  ? -22.307 35.599 -9.931  1.00 30.65  ? 1887 ARG   A NH1 1 
ATOM   752 N  NH2 . ARG   A 1 94  ? -23.304 37.664 -9.941  1.00 26.78  ? 1887 ARG   A NH2 1 
ATOM   753 N  N   . ARG   A 1 95  ? -26.100 33.962 -8.272  1.00 32.89  ? 1888 ARG   A N   1 
ATOM   754 C  CA  . ARG   A 1 95  ? -25.510 33.711 -6.964  1.00 33.19  ? 1888 ARG   A CA  1 
ATOM   755 C  C   . ARG   A 1 95  ? -26.215 32.555 -6.261  1.00 36.42  ? 1888 ARG   A C   1 
ATOM   756 O  O   . ARG   A 1 95  ? -25.560 31.728 -5.618  1.00 39.22  ? 1888 ARG   A O   1 
ATOM   757 C  CB  . ARG   A 1 95  ? -25.544 34.982 -6.112  1.00 31.21  ? 1888 ARG   A CB  1 
ATOM   758 C  CG  . ARG   A 1 95  ? -24.435 36.000 -6.432  1.00 32.05  ? 1888 ARG   A CG  1 
ATOM   759 C  CD  . ARG   A 1 95  ? -24.408 37.154 -5.383  1.00 30.11  ? 1888 ARG   A CD  1 
ATOM   760 N  NE  . ARG   A 1 95  ? -25.685 37.878 -5.361  1.00 33.06  ? 1888 ARG   A NE  1 
ATOM   761 C  CZ  . ARG   A 1 95  ? -25.943 38.990 -6.052  1.00 37.39  ? 1888 ARG   A CZ  1 
ATOM   762 N  NH1 . ARG   A 1 95  ? -25.009 39.545 -6.834  1.00 31.39  ? 1888 ARG   A NH1 1 
ATOM   763 N  NH2 . ARG   A 1 95  ? -27.141 39.550 -5.967  1.00 30.91  ? 1888 ARG   A NH2 1 
ATOM   764 N  N   . PHE   A 1 96  ? -27.546 32.471 -6.377  1.00 32.07  ? 1889 PHE   A N   1 
ATOM   765 C  CA  . PHE   A 1 96  ? -28.263 31.317 -5.826  1.00 32.88  ? 1889 PHE   A CA  1 
ATOM   766 C  C   . PHE   A 1 96  ? -27.729 30.009 -6.402  1.00 35.21  ? 1889 PHE   A C   1 
ATOM   767 O  O   . PHE   A 1 96  ? -27.385 29.088 -5.655  1.00 39.52  ? 1889 PHE   A O   1 
ATOM   768 C  CB  . PHE   A 1 96  ? -29.767 31.421 -6.105  1.00 30.27  ? 1889 PHE   A CB  1 
ATOM   769 C  CG  . PHE   A 1 96  ? -30.559 30.259 -5.558  1.00 48.35  ? 1889 PHE   A CG  1 
ATOM   770 C  CD1 . PHE   A 1 96  ? -30.973 30.247 -4.230  1.00 51.49  ? 1889 PHE   A CD1 1 
ATOM   771 C  CD2 . PHE   A 1 96  ? -30.865 29.166 -6.359  1.00 45.18  ? 1889 PHE   A CD2 1 
ATOM   772 C  CE1 . PHE   A 1 96  ? -31.691 29.173 -3.720  1.00 51.02  ? 1889 PHE   A CE1 1 
ATOM   773 C  CE2 . PHE   A 1 96  ? -31.579 28.093 -5.847  1.00 49.40  ? 1889 PHE   A CE2 1 
ATOM   774 C  CZ  . PHE   A 1 96  ? -31.990 28.097 -4.527  1.00 50.48  ? 1889 PHE   A CZ  1 
ATOM   775 N  N   . PHE   A 1 97  ? -27.659 29.908 -7.736  1.00 32.82  ? 1890 PHE   A N   1 
ATOM   776 C  CA  . PHE   A 1 97  ? -27.234 28.657 -8.367  1.00 35.64  ? 1890 PHE   A CA  1 
ATOM   777 C  C   . PHE   A 1 97  ? -25.804 28.294 -7.988  1.00 38.32  ? 1890 PHE   A C   1 
ATOM   778 O  O   . PHE   A 1 97  ? -25.519 27.143 -7.631  1.00 38.95  ? 1890 PHE   A O   1 
ATOM   779 C  CB  . PHE   A 1 97  ? -27.342 28.738 -9.888  1.00 36.09  ? 1890 PHE   A CB  1 
ATOM   780 C  CG  . PHE   A 1 97  ? -26.714 27.551 -10.581 1.00 38.74  ? 1890 PHE   A CG  1 
ATOM   781 C  CD1 . PHE   A 1 97  ? -27.396 26.339 -10.658 1.00 41.86  ? 1890 PHE   A CD1 1 
ATOM   782 C  CD2 . PHE   A 1 97  ? -25.429 27.624 -11.097 1.00 38.78  ? 1890 PHE   A CD2 1 
ATOM   783 C  CE1 . PHE   A 1 97  ? -26.822 25.233 -11.263 1.00 40.18  ? 1890 PHE   A CE1 1 
ATOM   784 C  CE2 . PHE   A 1 97  ? -24.843 26.515 -11.708 1.00 44.48  ? 1890 PHE   A CE2 1 
ATOM   785 C  CZ  . PHE   A 1 97  ? -25.541 25.318 -11.788 1.00 37.36  ? 1890 PHE   A CZ  1 
ATOM   786 N  N   . GLU   A 1 98  ? -24.882 29.256 -8.112  1.00 35.75  ? 1891 GLU   A N   1 
ATOM   787 C  CA  . GLU   A 1 98  ? -23.487 29.000 -7.783  1.00 39.81  ? 1891 GLU   A CA  1 
ATOM   788 C  C   . GLU   A 1 98  ? -23.345 28.508 -6.353  1.00 41.54  ? 1891 GLU   A C   1 
ATOM   789 O  O   . GLU   A 1 98  ? -22.646 27.522 -6.099  1.00 48.29  ? 1891 GLU   A O   1 
ATOM   790 C  CB  . GLU   A 1 98  ? -22.643 30.263 -7.987  1.00 42.75  ? 1891 GLU   A CB  1 
ATOM   791 C  CG  . GLU   A 1 98  ? -22.253 30.576 -9.431  1.00 50.88  ? 1891 GLU   A CG  1 
ATOM   792 C  CD  . GLU   A 1 98  ? -21.381 31.841 -9.560  1.00 57.04  ? 1891 GLU   A CD  1 
ATOM   793 O  OE1 . GLU   A 1 98  ? -20.660 32.181 -8.593  1.00 61.20  ? 1891 GLU   A OE1 1 
ATOM   794 O  OE2 . GLU   A 1 98  ? -21.429 32.501 -10.626 1.00 55.26  ? 1891 GLU   A OE2 1 
ATOM   795 N  N   . SER   A 1 99  ? -23.997 29.179 -5.402  1.00 42.69  ? 1892 SER   A N   1 
ATOM   796 C  CA  . SER   A 1 99  ? -23.829 28.786 -4.004  1.00 49.36  ? 1892 SER   A CA  1 
ATOM   797 C  C   . SER   A 1 99  ? -24.494 27.444 -3.731  1.00 51.93  ? 1892 SER   A C   1 
ATOM   798 O  O   . SER   A 1 99  ? -23.986 26.638 -2.941  1.00 58.72  ? 1892 SER   A O   1 
ATOM   799 C  CB  . SER   A 1 99  ? -24.386 29.865 -3.075  1.00 47.54  ? 1892 SER   A CB  1 
ATOM   800 O  OG  . SER   A 1 99  ? -25.801 29.904 -3.107  1.00 57.66  ? 1892 SER   A OG  1 
ATOM   801 N  N   . ARG   A 1 100 ? -25.623 27.181 -4.389  1.00 46.39  ? 1893 ARG   A N   1 
ATOM   802 C  CA  . ARG   A 1 100 ? -26.315 25.911 -4.196  1.00 56.39  ? 1893 ARG   A CA  1 
ATOM   803 C  C   . ARG   A 1 100 ? -25.542 24.765 -4.843  1.00 51.42  ? 1893 ARG   A C   1 
ATOM   804 O  O   . ARG   A 1 100 ? -25.358 23.708 -4.230  1.00 47.48  ? 1893 ARG   A O   1 
ATOM   805 C  CB  . ARG   A 1 100 ? -27.736 26.015 -4.752  1.00 53.08  ? 1893 ARG   A CB  1 
ATOM   806 C  CG  . ARG   A 1 100 ? -28.654 24.883 -4.374  1.00 53.87  ? 1893 ARG   A CG  1 
ATOM   807 C  CD  . ARG   A 1 100 ? -29.031 24.924 -2.896  1.00 57.63  ? 1893 ARG   A CD  1 
ATOM   808 N  NE  . ARG   A 1 100 ? -30.054 23.924 -2.600  1.00 55.16  ? 1893 ARG   A NE  1 
ATOM   809 C  CZ  . ARG   A 1 100 ? -29.852 22.831 -1.874  1.00 65.86  ? 1893 ARG   A CZ  1 
ATOM   810 N  NH1 . ARG   A 1 100 ? -28.661 22.600 -1.329  1.00 70.41  ? 1893 ARG   A NH1 1 
ATOM   811 N  NH2 . ARG   A 1 100 ? -30.852 21.982 -1.673  1.00 64.90  ? 1893 ARG   A NH2 1 
ATOM   812 N  N   . TRP   A 1 101 ? -25.050 24.967 -6.069  1.00 54.55  ? 1894 TRP   A N   1 
ATOM   813 C  CA  . TRP   A 1 101 ? -24.191 23.966 -6.695  1.00 59.67  ? 1894 TRP   A CA  1 
ATOM   814 C  C   . TRP   A 1 101 ? -22.979 23.633 -5.828  1.00 69.98  ? 1894 TRP   A C   1 
ATOM   815 O  O   . TRP   A 1 101 ? -22.509 22.490 -5.834  1.00 68.02  ? 1894 TRP   A O   1 
ATOM   816 C  CB  . TRP   A 1 101 ? -23.730 24.451 -8.071  1.00 61.62  ? 1894 TRP   A CB  1 
ATOM   817 C  CG  . TRP   A 1 101 ? -22.675 23.573 -8.704  1.00 63.57  ? 1894 TRP   A CG  1 
ATOM   818 C  CD1 . TRP   A 1 101 ? -21.326 23.594 -8.457  1.00 69.18  ? 1894 TRP   A CD1 1 
ATOM   819 C  CD2 . TRP   A 1 101 ? -22.883 22.556 -9.689  1.00 62.56  ? 1894 TRP   A CD2 1 
ATOM   820 N  NE1 . TRP   A 1 101 ? -20.689 22.648 -9.223  1.00 74.81  ? 1894 TRP   A NE1 1 
ATOM   821 C  CE2 . TRP   A 1 101 ? -21.622 22.000 -9.991  1.00 72.12  ? 1894 TRP   A CE2 1 
ATOM   822 C  CE3 . TRP   A 1 101 ? -24.010 22.060 -10.343 1.00 63.29  ? 1894 TRP   A CE3 1 
ATOM   823 C  CZ2 . TRP   A 1 101 ? -21.462 20.973 -10.916 1.00 72.42  ? 1894 TRP   A CZ2 1 
ATOM   824 C  CZ3 . TRP   A 1 101 ? -23.850 21.040 -11.259 1.00 68.43  ? 1894 TRP   A CZ3 1 
ATOM   825 C  CH2 . TRP   A 1 101 ? -22.586 20.509 -11.539 1.00 72.89  ? 1894 TRP   A CH2 1 
ATOM   826 N  N   . GLU   A 1 102 ? -22.461 24.610 -5.078  1.00 74.45  ? 1895 GLU   A N   1 
ATOM   827 C  CA  . GLU   A 1 102 ? -21.220 24.401 -4.340  1.00 74.63  ? 1895 GLU   A CA  1 
ATOM   828 C  C   . GLU   A 1 102 ? -21.441 23.698 -3.012  1.00 77.29  ? 1895 GLU   A C   1 
ATOM   829 O  O   . GLU   A 1 102 ? -20.553 22.970 -2.554  1.00 87.14  ? 1895 GLU   A O   1 
ATOM   830 C  CB  . GLU   A 1 102 ? -20.501 25.733 -4.123  1.00 77.74  ? 1895 GLU   A CB  1 
ATOM   831 C  CG  . GLU   A 1 102 ? -19.426 25.999 -5.179  1.00 89.89  ? 1895 GLU   A CG  1 
ATOM   832 C  CD  . GLU   A 1 102 ? -19.209 27.479 -5.466  1.00 96.71  ? 1895 GLU   A CD  1 
ATOM   833 O  OE1 . GLU   A 1 102 ? -18.861 28.230 -4.528  1.00 100.28 ? 1895 GLU   A OE1 1 
ATOM   834 O  OE2 . GLU   A 1 102 ? -19.391 27.891 -6.635  1.00 93.92  ? 1895 GLU   A OE2 1 
ATOM   835 N  N   . GLU   A 1 103 ? -22.597 23.884 -2.378  1.00 77.69  ? 1896 GLU   A N   1 
ATOM   836 C  CA  . GLU   A 1 103 ? -22.882 23.107 -1.178  1.00 82.62  ? 1896 GLU   A CA  1 
ATOM   837 C  C   . GLU   A 1 103 ? -23.403 21.710 -1.499  1.00 86.69  ? 1896 GLU   A C   1 
ATOM   838 O  O   . GLU   A 1 103 ? -23.868 21.011 -0.592  1.00 90.71  ? 1896 GLU   A O   1 
ATOM   839 C  CB  . GLU   A 1 103 ? -23.854 23.856 -0.253  1.00 87.24  ? 1896 GLU   A CB  1 
ATOM   840 C  CG  . GLU   A 1 103 ? -25.263 24.084 -0.777  1.00 90.76  ? 1896 GLU   A CG  1 
ATOM   841 C  CD  . GLU   A 1 103 ? -26.092 24.969 0.154   1.00 93.48  ? 1896 GLU   A CD  1 
ATOM   842 O  OE1 . GLU   A 1 103 ? -26.521 24.487 1.222   1.00 100.47 ? 1896 GLU   A OE1 1 
ATOM   843 O  OE2 . GLU   A 1 103 ? -26.301 26.155 -0.175  1.00 94.84  ? 1896 GLU   A OE2 1 
ATOM   844 N  N   . PHE   A 1 104 ? -23.330 21.294 -2.765  1.00 79.37  ? 1897 PHE   A N   1 
ATOM   845 C  CA  . PHE   A 1 104 ? -23.459 19.895 -3.159  1.00 82.81  ? 1897 PHE   A CA  1 
ATOM   846 C  C   . PHE   A 1 104 ? -22.130 19.293 -3.590  1.00 90.10  ? 1897 PHE   A C   1 
ATOM   847 O  O   . PHE   A 1 104 ? -21.760 18.210 -3.126  1.00 89.59  ? 1897 PHE   A O   1 
ATOM   848 C  CB  . PHE   A 1 104 ? -24.476 19.740 -4.299  1.00 84.59  ? 1897 PHE   A CB  1 
ATOM   849 C  CG  . PHE   A 1 104 ? -25.901 19.595 -3.839  1.00 93.89  ? 1897 PHE   A CG  1 
ATOM   850 C  CD1 . PHE   A 1 104 ? -26.345 18.410 -3.273  1.00 100.02 ? 1897 PHE   A CD1 1 
ATOM   851 C  CD2 . PHE   A 1 104 ? -26.803 20.635 -3.995  1.00 92.30  ? 1897 PHE   A CD2 1 
ATOM   852 C  CE1 . PHE   A 1 104 ? -27.663 18.272 -2.860  1.00 102.17 ? 1897 PHE   A CE1 1 
ATOM   853 C  CE2 . PHE   A 1 104 ? -28.120 20.499 -3.594  1.00 91.44  ? 1897 PHE   A CE2 1 
ATOM   854 C  CZ  . PHE   A 1 104 ? -28.549 19.320 -3.022  1.00 98.41  ? 1897 PHE   A CZ  1 
ATOM   855 N  N   . TYR   A 1 105 ? -21.396 19.976 -4.470  1.00 93.33  ? 1898 TYR   A N   1 
ATOM   856 C  CA  . TYR   A 1 105 ? -20.132 19.469 -5.008  1.00 91.18  ? 1898 TYR   A CA  1 
ATOM   857 C  C   . TYR   A 1 105 ? -18.944 20.326 -4.578  1.00 88.23  ? 1898 TYR   A C   1 
ATOM   858 O  O   . TYR   A 1 105 ? -18.644 20.441 -3.390  1.00 90.25  ? 1898 TYR   A O   1 
ATOM   859 C  CB  . TYR   A 1 105 ? -20.190 19.401 -6.538  1.00 85.28  ? 1898 TYR   A CB  1 
ATOM   860 C  CG  . TYR   A 1 105 ? -21.343 18.584 -7.084  1.00 81.42  ? 1898 TYR   A CG  1 
ATOM   861 C  CD1 . TYR   A 1 105 ? -21.287 17.196 -7.109  1.00 82.17  ? 1898 TYR   A CD1 1 
ATOM   862 C  CD2 . TYR   A 1 105 ? -22.486 19.201 -7.583  1.00 72.87  ? 1898 TYR   A CD2 1 
ATOM   863 C  CE1 . TYR   A 1 105 ? -22.337 16.445 -7.610  1.00 77.81  ? 1898 TYR   A CE1 1 
ATOM   864 C  CE2 . TYR   A 1 105 ? -23.542 18.456 -8.083  1.00 67.22  ? 1898 TYR   A CE2 1 
ATOM   865 C  CZ  . TYR   A 1 105 ? -23.459 17.080 -8.095  1.00 69.52  ? 1898 TYR   A CZ  1 
ATOM   866 O  OH  . TYR   A 1 105 ? -24.499 16.335 -8.591  1.00 72.31  ? 1898 TYR   A OH  1 
HETATM 867 C  C12 . A1IAC B 2 .   ? -38.147 38.960 -19.963 1.00 37.65  ? 1901 A1IAC A C12 1 
HETATM 868 C  C16 . A1IAC B 2 .   ? -41.360 36.918 -20.392 1.00 47.20  ? 1901 A1IAC A C16 1 
HETATM 869 C  C18 . A1IAC B 2 .   ? -39.440 35.809 -21.314 1.00 47.70  ? 1901 A1IAC A C18 1 
HETATM 870 C  C19 . A1IAC B 2 .   ? -38.561 36.390 -20.198 1.00 47.37  ? 1901 A1IAC A C19 1 
HETATM 871 C  C01 . A1IAC B 2 .   ? -36.276 42.238 -21.085 1.00 42.33  ? 1901 A1IAC A C01 1 
HETATM 872 C  C02 . A1IAC B 2 .   ? -36.470 40.927 -21.835 1.00 37.14  ? 1901 A1IAC A C02 1 
HETATM 873 C  C03 . A1IAC B 2 .   ? -35.864 39.667 -21.130 1.00 35.27  ? 1901 A1IAC A C03 1 
HETATM 874 C  C04 . A1IAC B 2 .   ? -36.627 38.820 -20.357 1.00 31.31  ? 1901 A1IAC A C04 1 
HETATM 875 C  C06 . A1IAC B 2 .   ? -34.590 37.960 -20.374 1.00 34.86  ? 1901 A1IAC A C06 1 
HETATM 876 C  C07 . A1IAC B 2 .   ? -33.466 36.964 -20.040 1.00 30.13  ? 1901 A1IAC A C07 1 
HETATM 877 C  C08 . A1IAC B 2 .   ? -34.562 39.116 -21.163 1.00 33.52  ? 1901 A1IAC A C08 1 
HETATM 878 C  C09 . A1IAC B 2 .   ? -33.303 39.605 -21.898 1.00 43.93  ? 1901 A1IAC A C09 1 
HETATM 879 C  C11 . A1IAC B 2 .   ? -33.394 40.613 -23.050 1.00 38.24  ? 1901 A1IAC A C11 1 
HETATM 880 C  C15 . A1IAC B 2 .   ? -40.430 37.737 -19.481 1.00 45.19  ? 1901 A1IAC A C15 1 
HETATM 881 N  N05 . A1IAC B 2 .   ? -35.832 37.827 -19.906 1.00 31.72  ? 1901 A1IAC A N05 1 
HETATM 882 N  N14 . A1IAC B 2 .   ? -39.005 37.738 -19.873 1.00 40.86  ? 1901 A1IAC A N14 1 
HETATM 883 N  N17 . A1IAC B 2 .   ? -40.802 35.670 -20.840 1.00 51.61  ? 1901 A1IAC A N17 1 
HETATM 884 O  O10 . A1IAC B 2 .   ? -32.223 39.181 -21.597 1.00 38.03  ? 1901 A1IAC A O10 1 
HETATM 885 O  O13 . A1IAC B 2 .   ? -38.590 40.031 -19.685 1.00 44.48  ? 1901 A1IAC A O13 1 
HETATM 886 C  C1  . EDO   C 3 .   ? -39.365 38.820 -24.325 1.00 57.08  ? 1902 EDO   A C1  1 
HETATM 887 O  O1  . EDO   C 3 .   ? -40.005 37.635 -24.802 1.00 48.52  ? 1902 EDO   A O1  1 
HETATM 888 C  C2  . EDO   C 3 .   ? -40.428 39.829 -23.903 1.00 69.59  ? 1902 EDO   A C2  1 
HETATM 889 O  O2  . EDO   C 3 .   ? -39.836 40.795 -23.025 1.00 78.39  ? 1902 EDO   A O2  1 
HETATM 890 MG MG  . MG    D 4 .   ? -17.513 31.692 -6.094  1.00 61.96  ? 1903 MG    A MG  1 
HETATM 891 O  O   . HOH   E 5 .   ? -17.955 30.330 -4.282  1.00 57.88  ? 2001 HOH   A O   1 
HETATM 892 O  O   . HOH   E 5 .   ? -21.805 47.156 -14.514 1.00 36.75  ? 2002 HOH   A O   1 
HETATM 893 O  O   . HOH   E 5 .   ? -32.925 33.135 -20.670 1.00 39.62  ? 2003 HOH   A O   1 
HETATM 894 O  O   . HOH   E 5 .   ? -35.547 42.804 -10.728 1.00 48.36  ? 2004 HOH   A O   1 
HETATM 895 O  O   . HOH   E 5 .   ? -31.145 33.338 -23.363 1.00 40.73  ? 2005 HOH   A O   1 
HETATM 896 O  O   . HOH   E 5 .   ? -21.688 30.243 -21.009 1.00 54.67  ? 2006 HOH   A O   1 
HETATM 897 O  O   . HOH   E 5 .   ? -42.189 36.866 -23.940 1.00 56.51  ? 2007 HOH   A O   1 
HETATM 898 O  O   . HOH   E 5 .   ? -39.486 25.725 -16.276 1.00 47.91  ? 2008 HOH   A O   1 
HETATM 899 O  O   . HOH   E 5 .   ? -20.079 30.097 -17.652 1.00 52.57  ? 2009 HOH   A O   1 
HETATM 900 O  O   . HOH   E 5 .   ? -39.986 34.256 -18.199 1.00 51.25  ? 2010 HOH   A O   1 
HETATM 901 O  O   . HOH   E 5 .   ? -40.265 22.588 -20.445 1.00 61.14  ? 2011 HOH   A O   1 
HETATM 902 O  O   . HOH   E 5 .   ? -35.525 33.743 -20.698 1.00 34.19  ? 2012 HOH   A O   1 
HETATM 903 O  O   . HOH   E 5 .   ? -22.129 27.482 -20.076 1.00 40.57  ? 2013 HOH   A O   1 
HETATM 904 O  O   . HOH   E 5 .   ? -22.696 32.507 -15.572 1.00 44.15  ? 2014 HOH   A O   1 
HETATM 905 O  O   . HOH   E 5 .   ? -40.765 31.601 -9.878  1.00 48.41  ? 2015 HOH   A O   1 
HETATM 906 O  O   . HOH   E 5 .   ? -34.726 33.125 -27.124 1.00 39.33  ? 2016 HOH   A O   1 
HETATM 907 O  O   . HOH   E 5 .   ? -29.240 34.873 -4.567  1.00 30.99  ? 2017 HOH   A O   1 
HETATM 908 O  O   . HOH   E 5 .   ? -33.989 30.011 -24.396 1.00 41.35  ? 2018 HOH   A O   1 
HETATM 909 O  O   . HOH   E 5 .   ? -37.626 19.096 -10.128 1.00 43.73  ? 2019 HOH   A O   1 
HETATM 910 O  O   . HOH   E 5 .   ? -33.361 45.722 -27.015 1.00 50.22  ? 2020 HOH   A O   1 
HETATM 911 O  O   . HOH   E 5 .   ? -18.967 30.625 -7.117  1.00 59.06  ? 2021 HOH   A O   1 
HETATM 912 O  O   . HOH   E 5 .   ? -30.647 34.781 -20.015 1.00 31.37  ? 2022 HOH   A O   1 
HETATM 913 O  O   . HOH   E 5 .   ? -25.131 32.902 -26.218 1.00 34.44  ? 2023 HOH   A O   1 
HETATM 914 O  O   . HOH   E 5 .   ? -27.244 39.612 -14.518 1.00 26.04  ? 2024 HOH   A O   1 
HETATM 915 O  O   . HOH   E 5 .   ? -18.939 33.231 -17.024 1.00 53.01  ? 2025 HOH   A O   1 
HETATM 916 O  O   . HOH   E 5 .   ? -44.186 36.551 -31.476 1.00 48.27  ? 2026 HOH   A O   1 
HETATM 917 O  O   . HOH   E 5 .   ? -30.561 36.912 -21.924 1.00 33.25  ? 2027 HOH   A O   1 
HETATM 918 O  O   . HOH   E 5 .   ? -20.665 35.345 -14.448 1.00 29.40  ? 2028 HOH   A O   1 
HETATM 919 O  O   . HOH   E 5 .   ? -26.174 41.858 -15.962 1.00 35.56  ? 2029 HOH   A O   1 
HETATM 920 O  O   . HOH   E 5 .   ? -23.868 43.541 -17.906 1.00 36.58  ? 2030 HOH   A O   1 
HETATM 921 O  O   . HOH   E 5 .   ? -31.444 33.718 -3.265  1.00 35.08  ? 2031 HOH   A O   1 
HETATM 922 O  O   . HOH   E 5 .   ? -32.546 44.896 -19.700 1.00 51.96  ? 2032 HOH   A O   1 
HETATM 923 O  O   . HOH   E 5 .   ? -36.458 28.977 -4.271  1.00 49.69  ? 2033 HOH   A O   1 
HETATM 924 O  O   . HOH   E 5 .   ? -34.702 47.681 -16.562 1.00 43.14  ? 2034 HOH   A O   1 
HETATM 925 O  O   . HOH   E 5 .   ? -37.502 33.485 -3.674  1.00 41.57  ? 2035 HOH   A O   1 
HETATM 926 O  O   . HOH   E 5 .   ? -38.825 16.680 -15.386 1.00 52.98  ? 2036 HOH   A O   1 
HETATM 927 O  O   . HOH   E 5 .   ? -30.476 46.359 -19.809 1.00 44.88  ? 2037 HOH   A O   1 
HETATM 928 O  O   . HOH   E 5 .   ? -29.733 22.133 -24.002 1.00 51.16  ? 2038 HOH   A O   1 
HETATM 929 O  O   . HOH   E 5 .   ? -34.107 32.524 -24.424 1.00 38.32  ? 2039 HOH   A O   1 
HETATM 930 O  O   . HOH   E 5 .   ? -33.748 40.071 -32.039 1.00 36.40  ? 2040 HOH   A O   1 
HETATM 931 O  O   . HOH   E 5 .   ? -26.072 37.089 -13.690 1.00 31.33  ? 2041 HOH   A O   1 
HETATM 932 O  O   . HOH   E 5 .   ? -37.675 38.499 -3.169  1.00 59.87  ? 2042 HOH   A O   1 
HETATM 933 O  O   . HOH   E 5 .   ? -35.421 39.078 -34.238 1.00 49.34  ? 2043 HOH   A O   1 
HETATM 934 O  O   . HOH   E 5 .   ? -35.337 37.883 -37.867 1.00 49.08  ? 2044 HOH   A O   1 
HETATM 935 O  O   . HOH   E 5 .   ? -31.427 41.055 -33.521 1.00 33.58  ? 2045 HOH   A O   1 
HETATM 936 O  O   . HOH   E 5 .   ? -34.274 45.033 -17.974 1.00 51.28  ? 2046 HOH   A O   1 
HETATM 937 O  O   . HOH   E 5 .   ? -17.639 33.605 -8.069  1.00 72.37  ? 2047 HOH   A O   1 
HETATM 938 O  O   . HOH   E 5 .   ? -20.397 25.483 -11.343 1.00 53.67  ? 2048 HOH   A O   1 
HETATM 939 O  O   . HOH   E 5 .   ? -19.661 27.953 -10.278 1.00 57.79  ? 2049 HOH   A O   1 
HETATM 940 O  O   . HOH   E 5 .   ? -16.031 29.958 -6.423  1.00 55.90  ? 2050 HOH   A O   1 
HETATM 941 O  O   . HOH   E 5 .   ? -31.041 39.964 -36.206 1.00 49.44  ? 2051 HOH   A O   1 
HETATM 942 O  O   . HOH   E 5 .   ? -19.676 28.040 -18.804 1.00 50.24  ? 2052 HOH   A O   1 
HETATM 943 O  O   . HOH   E 5 .   ? -33.624 33.945 -29.413 1.00 46.31  ? 2053 HOH   A O   1 
HETATM 944 O  O   . HOH   E 5 .   ? -35.175 30.445 -28.027 1.00 45.84  ? 2054 HOH   A O   1 
HETATM 945 O  O   . HOH   E 5 .   ? -18.958 24.427 -13.221 1.00 61.28  ? 2055 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   . MET A 2   ? 1.0945 0.8043 1.2923 -0.0026 0.1696  0.2224  1795 MET A N   
2   C CA  . MET A 2   ? 1.1392 0.8731 1.3017 -0.0138 0.1851  0.1989  1795 MET A CA  
3   C C   . MET A 2   ? 1.1832 0.9278 1.2930 -0.0486 0.1643  0.1882  1795 MET A C   
4   O O   . MET A 2   ? 1.1484 0.9356 1.2497 -0.0593 0.1593  0.1791  1795 MET A O   
5   C CB  . MET A 2   ? 1.2334 0.9243 1.3605 -0.0009 0.2192  0.1762  1795 MET A CB  
6   C CG  . MET A 2   ? 1.3017 1.0075 1.3789 -0.0100 0.2295  0.1502  1795 MET A CG  
7   S SD  . MET A 2   ? 1.4019 1.0483 1.4238 0.0128  0.2658  0.1218  1795 MET A SD  
8   C CE  . MET A 2   ? 1.2792 0.9430 1.2338 -0.0050 0.2568  0.0921  1795 MET A CE  
9   N N   . HIS A 3   ? 1.2494 0.9537 1.3272 -0.0655 0.1550  0.1904  1796 HIS A N   
10  C CA  . HIS A 3   ? 1.2428 0.9593 1.2815 -0.0982 0.1402  0.1852  1796 HIS A CA  
11  C C   . HIS A 3   ? 1.1374 0.8970 1.1904 -0.1009 0.1154  0.2033  1796 HIS A C   
12  O O   . HIS A 3   ? 0.9809 0.7753 1.0132 -0.1195 0.1084  0.1938  1796 HIS A O   
13  C CB  . HIS A 3   ? 1.3238 0.9835 1.3324 -0.1151 0.1406  0.1899  1796 HIS A CB  
14  C CG  . HIS A 3   ? 1.3506 1.0203 1.3260 -0.1486 0.1333  0.1890  1796 HIS A CG  
15  N ND1 . HIS A 3   ? 1.3750 1.0469 1.3370 -0.1547 0.1177  0.2142  1796 HIS A ND1 
16  C CD2 . HIS A 3   ? 1.3633 1.0401 1.3181 -0.1761 0.1409  0.1659  1796 HIS A CD2 
17  C CE1 . HIS A 3   ? 1.3722 1.0521 1.3049 -0.1843 0.1228  0.2081  1796 HIS A CE1 
18  N NE2 . HIS A 3   ? 1.3703 1.0572 1.3067 -0.1988 0.1361  0.1789  1796 HIS A NE2 
19  N N   . SER A 4   ? 1.1758 0.9324 1.2661 -0.0805 0.0994  0.2274  1797 SER A N   
20  C CA  . SER A 4   ? 1.1156 0.9099 1.2226 -0.0786 0.0697  0.2409  1797 SER A CA  
21  C C   . SER A 4   ? 1.0519 0.9016 1.1925 -0.0743 0.0732  0.2287  1797 SER A C   
22  O O   . SER A 4   ? 0.8883 0.7710 1.0124 -0.0874 0.0584  0.2230  1797 SER A O   
23  C CB  . SER A 4   ? 1.1235 0.9011 1.2729 -0.0548 0.0460  0.2667  1797 SER A CB  
24  O OG  . SER A 4   ? 1.1621 0.9339 1.3707 -0.0300 0.0652  0.2682  1797 SER A OG  
25  N N   . ASP A 5   ? 1.1294 0.9855 1.3148 -0.0546 0.0960  0.2254  1798 ASP A N   
26  C CA  . ASP A 5   ? 1.0216 0.9216 1.2360 -0.0494 0.1067  0.2170  1798 ASP A CA  
27  C C   . ASP A 5   ? 0.9221 0.8380 1.0806 -0.0708 0.1111  0.1946  1798 ASP A C   
28  O O   . ASP A 5   ? 0.8371 0.7914 1.0016 -0.0773 0.0977  0.1916  1798 ASP A O   
29  C CB  . ASP A 5   ? 1.0552 0.9449 1.3044 -0.0252 0.1433  0.2161  1798 ASP A CB  
30  C CG  . ASP A 5   ? 1.0888 0.9920 1.4288 -0.0009 0.1411  0.2387  1798 ASP A CG  
31  O OD1 . ASP A 5   ? 1.1133 1.0253 1.4856 -0.0015 0.1043  0.2541  1798 ASP A OD1 
32  O OD2 . ASP A 5   ? 1.1225 1.0265 1.5025 0.0205  0.1766  0.2407  1798 ASP A OD2 
33  N N   . LEU A 6   ? 0.9331 0.8187 1.0417 -0.0813 0.1271  0.1774  1799 LEU A N   
34  C CA  . LEU A 6   ? 0.9007 0.8033 0.9681 -0.0979 0.1303  0.1536  1799 LEU A CA  
35  C C   . LEU A 6   ? 0.8421 0.7638 0.8854 -0.1231 0.1097  0.1514  1799 LEU A C   
36  O O   . LEU A 6   ? 0.8171 0.7711 0.8467 -0.1332 0.1058  0.1363  1799 LEU A O   
37  C CB  . LEU A 6   ? 0.9956 0.8584 1.0247 -0.0997 0.1490  0.1327  1799 LEU A CB  
38  C CG  . LEU A 6   ? 1.0090 0.8510 1.0444 -0.0711 0.1758  0.1298  1799 LEU A CG  
39  C CD1 . LEU A 6   ? 1.0551 0.8445 1.0442 -0.0708 0.1888  0.1071  1799 LEU A CD1 
40  C CD2 . LEU A 6   ? 0.9425 0.8182 0.9793 -0.0603 0.1840  0.1254  1799 LEU A CD2 
41  N N   . THR A 7   ? 0.7684 0.6680 0.8035 -0.1311 0.0983  0.1672  1800 THR A N   
42  C CA  . THR A 7   ? 0.7403 0.6550 0.7478 -0.1504 0.0838  0.1694  1800 THR A CA  
43  C C   . THR A 7   ? 0.7009 0.6585 0.7254 -0.1435 0.0644  0.1719  1800 THR A C   
44  O O   . THR A 7   ? 0.6191 0.6059 0.6247 -0.1560 0.0609  0.1592  1800 THR A O   
45  C CB  . THR A 7   ? 0.8508 0.7242 0.8379 -0.1539 0.0761  0.1915  1800 THR A CB  
46  O OG1 . THR A 7   ? 0.8935 0.7234 0.8644 -0.1648 0.0948  0.1877  1800 THR A OG1 
47  C CG2 . THR A 7   ? 0.8330 0.7169 0.7816 -0.1693 0.0657  0.1962  1800 THR A CG2 
48  N N   . PHE A 8   ? 0.6188 0.5806 0.6858 -0.1232 0.0507  0.1873  1801 PHE A N   
49  C CA  . PHE A 8   ? 0.6453 0.6443 0.7387 -0.1169 0.0296  0.1881  1801 PHE A CA  
50  C C   . PHE A 8   ? 0.6670 0.6994 0.7691 -0.1182 0.0436  0.1700  1801 PHE A C   
51  O O   . PHE A 8   ? 0.6497 0.7104 0.7455 -0.1236 0.0303  0.1616  1801 PHE A O   
52  C CB  . PHE A 8   ? 0.7899 0.7891 0.9468 -0.0959 0.0134  0.2067  1801 PHE A CB  
53  C CG  . PHE A 8   ? 0.9759 1.0139 1.1874 -0.0876 0.0078  0.2043  1801 PHE A CG  
54  C CD1 . PHE A 8   ? 1.0326 1.0924 1.2433 -0.0922 -0.0226 0.2005  1801 PHE A CD1 
55  C CD2 . PHE A 8   ? 1.1409 1.1882 1.3998 -0.0750 0.0358  0.2056  1801 PHE A CD2 
56  C CE1 . PHE A 8   ? 1.1022 1.1934 1.3673 -0.0867 -0.0280 0.1983  1801 PHE A CE1 
57  C CE2 . PHE A 8   ? 1.1869 1.2659 1.4975 -0.0691 0.0354  0.2067  1801 PHE A CE2 
58  C CZ  . PHE A 8   ? 1.1526 1.2539 1.4705 -0.0762 0.0021  0.2031  1801 PHE A CZ  
59  N N   . CYS A 9   ? 0.6774 0.7016 0.7881 -0.1106 0.0698  0.1637  1802 CYS A N   
60  C CA  . CYS A 9   ? 0.6267 0.6734 0.7354 -0.1076 0.0825  0.1491  1802 CYS A CA  
61  C C   . CYS A 9   ? 0.6080 0.6710 0.6731 -0.1260 0.0773  0.1281  1802 CYS A C   
62  O O   . CYS A 9   ? 0.4348 0.5264 0.5014 -0.1254 0.0717  0.1190  1802 CYS A O   
63  C CB  . CYS A 9   ? 0.7335 0.7555 0.8387 -0.0934 0.1121  0.1453  1802 CYS A CB  
64  S SG  . CYS A 9   ? 0.7915 0.8029 0.9633 -0.0670 0.1294  0.1696  1802 CYS A SG  
65  N N   . GLU A 10  ? 0.5076 0.5522 0.5404 -0.1424 0.0803  0.1207  1803 GLU A N   
66  C CA  . GLU A 10  ? 0.5711 0.6354 0.5776 -0.1613 0.0780  0.1014  1803 GLU A CA  
67  C C   . GLU A 10  ? 0.5852 0.6763 0.5887 -0.1673 0.0621  0.1047  1803 GLU A C   
68  O O   . GLU A 10  ? 0.4986 0.6205 0.4970 -0.1727 0.0590  0.0888  1803 GLU A O   
69  C CB  . GLU A 10  ? 0.6388 0.6752 0.6246 -0.1797 0.0878  0.0961  1803 GLU A CB  
70  C CG  . GLU A 10  ? 0.7894 0.7956 0.7684 -0.1758 0.1002  0.0833  1803 GLU A CG  
71  C CD  . GLU A 10  ? 0.8277 0.8514 0.7953 -0.1838 0.0978  0.0543  1803 GLU A CD  
72  O OE1 . GLU A 10  ? 0.9334 0.9286 0.8857 -0.1792 0.1023  0.0389  1803 GLU A OE1 
73  O OE2 . GLU A 10  ? 0.8118 0.8753 0.7846 -0.1926 0.0890  0.0454  1803 GLU A OE2 
74  N N   . ILE A 11  ? 0.5929 0.6693 0.5960 -0.1641 0.0501  0.1239  1804 ILE A N   
75  C CA  . ILE A 11  ? 0.5572 0.6495 0.5451 -0.1659 0.0323  0.1253  1804 ILE A CA  
76  C C   . ILE A 11  ? 0.4951 0.6180 0.5113 -0.1539 0.0185  0.1185  1804 ILE A C   
77  O O   . ILE A 11  ? 0.5111 0.6584 0.5149 -0.1575 0.0134  0.1046  1804 ILE A O   
78  C CB  . ILE A 11  ? 0.5838 0.6453 0.5578 -0.1604 0.0152  0.1470  1804 ILE A CB  
79  C CG1 . ILE A 11  ? 0.6520 0.6765 0.5917 -0.1729 0.0311  0.1567  1804 ILE A CG1 
80  C CG2 . ILE A 11  ? 0.5730 0.6434 0.5205 -0.1578 -0.0074 0.1455  1804 ILE A CG2 
81  C CD1 . ILE A 11  ? 0.6477 0.6343 0.5615 -0.1647 0.0120  0.1801  1804 ILE A CD1 
82  N N   . ILE A 12  ? 0.4754 0.5961 0.5345 -0.1391 0.0153  0.1290  1805 ILE A N   
83  C CA  . ILE A 12  ? 0.4720 0.6164 0.5650 -0.1294 0.0022  0.1270  1805 ILE A CA  
84  C C   . ILE A 12  ? 0.5322 0.6970 0.6187 -0.1296 0.0167  0.1102  1805 ILE A C   
85  O O   . ILE A 12  ? 0.4343 0.6197 0.5268 -0.1272 0.0051  0.1019  1805 ILE A O   
86  C CB  . ILE A 12  ? 0.6015 0.7396 0.7548 -0.1147 -0.0012 0.1457  1805 ILE A CB  
87  C CG1 . ILE A 12  ? 0.6440 0.8029 0.8408 -0.1084 -0.0208 0.1462  1805 ILE A CG1 
88  C CG2 . ILE A 12  ? 0.6807 0.8103 0.8482 -0.1066 0.0310  0.1487  1805 ILE A CG2 
89  C CD1 . ILE A 12  ? 0.7233 0.8800 0.9928 -0.0976 -0.0336 0.1652  1805 ILE A CD1 
90  N N   . LEU A 13  ? 0.3828 0.5384 0.4532 -0.1312 0.0384  0.1035  1806 LEU A N   
91  C CA  . LEU A 13  ? 0.4282 0.5985 0.4856 -0.1284 0.0457  0.0869  1806 LEU A CA  
92  C C   . LEU A 13  ? 0.4321 0.6263 0.4668 -0.1416 0.0372  0.0673  1806 LEU A C   
93  O O   . LEU A 13  ? 0.4175 0.6337 0.4535 -0.1366 0.0306  0.0557  1806 LEU A O   
94  C CB  . LEU A 13  ? 0.4124 0.5595 0.4513 -0.1239 0.0653  0.0818  1806 LEU A CB  
95  C CG  . LEU A 13  ? 0.5095 0.6636 0.5249 -0.1170 0.0674  0.0643  1806 LEU A CG  
96  C CD1 . LEU A 13  ? 0.4999 0.6646 0.5337 -0.1015 0.0662  0.0736  1806 LEU A CD1 
97  C CD2 . LEU A 13  ? 0.5563 0.6766 0.5416 -0.1086 0.0832  0.0577  1806 LEU A CD2 
98  N N   . MET A 14  ? 0.4016 0.5906 0.4184 -0.1574 0.0403  0.0648  1807 MET A N   
99  C CA  . MET A 14  ? 0.4800 0.6936 0.4835 -0.1696 0.0384  0.0500  1807 MET A CA  
100 C C   . MET A 14  ? 0.4544 0.6844 0.4600 -0.1614 0.0226  0.0498  1807 MET A C   
101 O O   . MET A 14  ? 0.4749 0.7320 0.4816 -0.1598 0.0193  0.0333  1807 MET A O   
102 C CB  . MET A 14  ? 0.6063 0.8032 0.5905 -0.1869 0.0493  0.0560  1807 MET A CB  
103 C CG  . MET A 14  ? 0.7427 0.9632 0.7159 -0.2003 0.0576  0.0437  1807 MET A CG  
104 S SD  . MET A 14  ? 0.9974 1.1880 0.9306 -0.2089 0.0659  0.0635  1807 MET A SD  
105 C CE  . MET A 14  ? 0.8486 1.0393 0.7654 -0.1887 0.0392  0.0681  1807 MET A CE  
106 N N   . GLU A 15  ? 0.3935 0.6058 0.4030 -0.1546 0.0093  0.0664  1808 GLU A N   
107 C CA  . GLU A 15  ? 0.4838 0.7041 0.4915 -0.1473 -0.0112 0.0632  1808 GLU A CA  
108 C C   . GLU A 15  ? 0.4663 0.7037 0.5049 -0.1357 -0.0189 0.0565  1808 GLU A C   
109 O O   . GLU A 15  ? 0.4073 0.6594 0.4414 -0.1315 -0.0296 0.0431  1808 GLU A O   
110 C CB  . GLU A 15  ? 0.4452 0.6394 0.4536 -0.1422 -0.0316 0.0807  1808 GLU A CB  
111 C CG  . GLU A 15  ? 0.6301 0.8003 0.5906 -0.1503 -0.0286 0.0881  1808 GLU A CG  
112 C CD  . GLU A 15  ? 0.7663 0.9065 0.7249 -0.1414 -0.0561 0.1057  1808 GLU A CD  
113 O OE1 . GLU A 15  ? 0.8465 0.9907 0.8543 -0.1311 -0.0773 0.1107  1808 GLU A OE1 
114 O OE2 . GLU A 15  ? 0.8617 0.9733 0.7727 -0.1443 -0.0573 0.1154  1808 GLU A OE2 
115 N N   . MET A 16  ? 0.3859 0.6172 0.4521 -0.1290 -0.0104 0.0662  1809 MET A N   
116 C CA  . MET A 16  ? 0.3686 0.6089 0.4585 -0.1173 -0.0126 0.0644  1809 MET A CA  
117 C C   . MET A 16  ? 0.3646 0.6239 0.4335 -0.1164 -0.0070 0.0446  1809 MET A C   
118 O O   . MET A 16  ? 0.3661 0.6373 0.4419 -0.1084 -0.0171 0.0361  1809 MET A O   
119 C CB  . MET A 16  ? 0.3483 0.5721 0.4669 -0.1082 0.0023  0.0830  1809 MET A CB  
120 C CG  . MET A 16  ? 0.4693 0.6817 0.6310 -0.1063 -0.0071 0.1025  1809 MET A CG  
121 S SD  . MET A 16  ? 0.6007 0.8025 0.8179 -0.0925 0.0150  0.1252  1809 MET A SD  
122 C CE  . MET A 16  ? 0.6337 0.8161 0.8098 -0.0888 0.0482  0.1251  1809 MET A CE  
123 N N   . GLU A 17  ? 0.3302 0.5917 0.3782 -0.1243 0.0058  0.0358  1810 GLU A N   
124 C CA  . GLU A 17  ? 0.4557 0.7379 0.4934 -0.1231 0.0054  0.0151  1810 GLU A CA  
125 C C   . GLU A 17  ? 0.4184 0.7293 0.4575 -0.1266 -0.0028 -0.0013 1810 GLU A C   
126 O O   . GLU A 17  ? 0.3814 0.7131 0.4257 -0.1188 -0.0093 -0.0171 1810 GLU A O   
127 C CB  . GLU A 17  ? 0.4570 0.7350 0.4812 -0.1342 0.0158  0.0066  1810 GLU A CB  
128 C CG  . GLU A 17  ? 0.5603 0.8082 0.5717 -0.1247 0.0243  0.0142  1810 GLU A CG  
129 C CD  . GLU A 17  ? 0.6763 0.9118 0.6741 -0.1374 0.0310  0.0041  1810 GLU A CD  
130 O OE1 . GLU A 17  ? 0.6361 0.8769 0.6410 -0.1558 0.0355  0.0040  1810 GLU A OE1 
131 O OE2 . GLU A 17  ? 0.6426 0.8584 0.6189 -0.1284 0.0316  -0.0037 1810 GLU A OE2 
132 N N   . SER A 18  ? 0.3886 0.6981 0.4191 -0.1356 -0.0021 0.0018  1811 SER A N   
133 C CA  . SER A 18  ? 0.5234 0.8549 0.5463 -0.1368 -0.0031 -0.0138 1811 SER A CA  
134 C C   . SER A 18  ? 0.5345 0.8589 0.5562 -0.1239 -0.0213 -0.0141 1811 SER A C   
135 O O   . SER A 18  ? 0.5678 0.9045 0.5767 -0.1205 -0.0223 -0.0288 1811 SER A O   
136 C CB  . SER A 18  ? 0.5461 0.8731 0.5461 -0.1526 0.0128  -0.0111 1811 SER A CB  
137 O OG  . SER A 18  ? 0.6608 0.9544 0.6414 -0.1532 0.0061  0.0083  1811 SER A OG  
138 N N   . HIS A 19  ? 0.4563 0.7638 0.4719 -0.1852 0.0024  -0.0087 1812 HIS A N   
139 C CA  . HIS A 19  ? 0.4487 0.7538 0.4729 -0.1631 0.0141  -0.0167 1812 HIS A CA  
140 C C   . HIS A 19  ? 0.4725 0.8175 0.5218 -0.1377 0.0261  -0.0261 1812 HIS A C   
141 O O   . HIS A 19  ? 0.3957 0.7502 0.4572 -0.1276 0.0233  -0.0264 1812 HIS A O   
142 C CB  . HIS A 19  ? 0.3897 0.6379 0.4066 -0.1487 0.0079  -0.0164 1812 HIS A CB  
143 C CG  . HIS A 19  ? 0.4477 0.6810 0.4627 -0.1380 0.0150  -0.0208 1812 HIS A CG  
144 N ND1 . HIS A 19  ? 0.4314 0.6810 0.4612 -0.1154 0.0268  -0.0295 1812 HIS A ND1 
145 C CD2 . HIS A 19  ? 0.5007 0.7013 0.4990 -0.1468 0.0103  -0.0175 1812 HIS A CD2 
146 C CE1 . HIS A 19  ? 0.4877 0.7154 0.5092 -0.1124 0.0294  -0.0314 1812 HIS A CE1 
147 N NE2 . HIS A 19  ? 0.4888 0.6889 0.4925 -0.1312 0.0200  -0.0241 1812 HIS A NE2 
148 N N   . ASP A 20  ? 0.4361 0.8019 0.4913 -0.1265 0.0382  -0.0343 1813 ASP A N   
149 C CA  . ASP A 20  ? 0.3315 0.7279 0.4075 -0.0983 0.0478  -0.0447 1813 ASP A CA  
150 C C   . ASP A 20  ? 0.3980 0.7592 0.4806 -0.0734 0.0439  -0.0460 1813 ASP A C   
151 O O   . ASP A 20  ? 0.3846 0.7671 0.4833 -0.0548 0.0455  -0.0502 1813 ASP A O   
152 C CB  . ASP A 20  ? 0.4577 0.8658 0.5322 -0.0882 0.0592  -0.0544 1813 ASP A CB  
153 C CG  . ASP A 20  ? 0.5707 1.0379 0.6472 -0.1034 0.0676  -0.0578 1813 ASP A CG  
154 O OD1 . ASP A 20  ? 0.4850 0.9864 0.5647 -0.1242 0.0644  -0.0515 1813 ASP A OD1 
155 O OD2 . ASP A 20  ? 0.5957 1.0762 0.6696 -0.0950 0.0775  -0.0672 1813 ASP A OD2 
156 N N   . ALA A 21  ? 0.3561 0.6661 0.4265 -0.0728 0.0386  -0.0422 1814 ALA A N   
157 C CA  . ALA A 21  ? 0.3418 0.6202 0.4162 -0.0522 0.0357  -0.0427 1814 ALA A CA  
158 C C   . ALA A 21  ? 0.3243 0.5908 0.3992 -0.0559 0.0261  -0.0364 1814 ALA A C   
159 O O   . ALA A 21  ? 0.3383 0.5788 0.4141 -0.0422 0.0232  -0.0357 1814 ALA A O   
160 C CB  . ALA A 21  ? 0.3254 0.5608 0.3876 -0.0500 0.0350  -0.0420 1814 ALA A CB  
161 N N   . ALA A 22  ? 0.3366 0.6219 0.4091 -0.0753 0.0209  -0.0318 1815 ALA A N   
162 C CA  . ALA A 22  ? 0.3711 0.6404 0.4392 -0.0811 0.0104  -0.0264 1815 ALA A CA  
163 C C   . ALA A 22  ? 0.3546 0.6492 0.4382 -0.0679 0.0104  -0.0280 1815 ALA A C   
164 O O   . ALA A 22  ? 0.3798 0.6592 0.4596 -0.0690 0.0022  -0.0247 1815 ALA A O   
165 C CB  . ALA A 22  ? 0.2478 0.5203 0.3020 -0.1101 0.0020  -0.0200 1815 ALA A CB  
166 N N   . TRP A 23  ? 0.2759 0.6076 0.3757 -0.0541 0.0186  -0.0337 1816 TRP A N   
167 C CA  . TRP A 23  ? 0.3017 0.6632 0.4169 -0.0427 0.0170  -0.0348 1816 TRP A CA  
168 C C   . TRP A 23  ? 0.2733 0.6046 0.3876 -0.0275 0.0113  -0.0330 1816 TRP A C   
169 O O   . TRP A 23  ? 0.3844 0.7328 0.5050 -0.0271 0.0058  -0.0307 1816 TRP A O   
170 C CB  . TRP A 23  ? 0.2493 0.6514 0.3811 -0.0247 0.0262  -0.0431 1816 TRP A CB  
171 C CG  . TRP A 23  ? 0.3813 0.7550 0.5107 -0.0029 0.0313  -0.0490 1816 TRP A CG  
172 C CD1 . TRP A 23  ? 0.4594 0.8210 0.5806 -0.0041 0.0379  -0.0530 1816 TRP A CD1 
173 C CD2 . TRP A 23  ? 0.4593 0.8102 0.5915 0.0209  0.0289  -0.0505 1816 TRP A CD2 
174 N NE1 . TRP A 23  ? 0.4719 0.8042 0.5905 0.0174  0.0394  -0.0573 1816 TRP A NE1 
175 C CE2 . TRP A 23  ? 0.4760 0.8003 0.6006 0.0323  0.0337  -0.0554 1816 TRP A CE2 
176 C CE3 . TRP A 23  ? 0.4376 0.7868 0.5756 0.0321  0.0222  -0.0476 1816 TRP A CE3 
177 C CZ2 . TRP A 23  ? 0.4879 0.7823 0.6093 0.0529  0.0312  -0.0567 1816 TRP A CZ2 
178 C CZ3 . TRP A 23  ? 0.4683 0.7888 0.6035 0.0531  0.0202  -0.0488 1816 TRP A CZ3 
179 C CH2 . TRP A 23  ? 0.4725 0.7653 0.5989 0.0626  0.0244  -0.0530 1816 TRP A CH2 
180 N N   . PRO A 24  ? 0.3170 0.6075 0.4234 -0.0166 0.0120  -0.0332 1817 PRO A N   
181 C CA  . PRO A 24  ? 0.2953 0.5631 0.3994 -0.0059 0.0067  -0.0306 1817 PRO A CA  
182 C C   . PRO A 24  ? 0.3791 0.6271 0.4710 -0.0200 -0.0016 -0.0262 1817 PRO A C   
183 O O   . PRO A 24  ? 0.3962 0.6312 0.4854 -0.0127 -0.0060 -0.0245 1817 PRO A O   
184 C CB  . PRO A 24  ? 0.3868 0.6219 0.4853 0.0065  0.0105  -0.0320 1817 PRO A CB  
185 C CG  . PRO A 24  ? 0.3387 0.5814 0.4385 0.0066  0.0176  -0.0365 1817 PRO A CG  
186 C CD  . PRO A 24  ? 0.2796 0.5461 0.3789 -0.0132 0.0176  -0.0358 1817 PRO A CD  
187 N N   . PHE A 25  ? 0.2852 0.5279 0.3670 -0.0396 -0.0049 -0.0244 1818 PHE A N   
188 C CA  . PHE A 25  ? 0.3745 0.5859 0.4397 -0.0496 -0.0141 -0.0218 1818 PHE A CA  
189 C C   . PHE A 25  ? 0.3938 0.6154 0.4510 -0.0705 -0.0233 -0.0185 1818 PHE A C   
190 O O   . PHE A 25  ? 0.4127 0.6045 0.4525 -0.0789 -0.0331 -0.0172 1818 PHE A O   
191 C CB  . PHE A 25  ? 0.3588 0.5389 0.4125 -0.0529 -0.0138 -0.0222 1818 PHE A CB  
192 C CG  . PHE A 25  ? 0.3645 0.5369 0.4249 -0.0366 -0.0053 -0.0246 1818 PHE A CG  
193 C CD1 . PHE A 25  ? 0.3045 0.4623 0.3657 -0.0220 -0.0049 -0.0251 1818 PHE A CD1 
194 C CD2 . PHE A 25  ? 0.3459 0.5267 0.4101 -0.0372 0.0019  -0.0263 1818 PHE A CD2 
195 C CE1 . PHE A 25  ? 0.3034 0.4529 0.3683 -0.0104 0.0014  -0.0260 1818 PHE A CE1 
196 C CE2 . PHE A 25  ? 0.3014 0.4713 0.3688 -0.0236 0.0081  -0.0284 1818 PHE A CE2 
197 C CZ  . PHE A 25  ? 0.3551 0.5087 0.4226 -0.0111 0.0073  -0.0277 1818 PHE A CZ  
198 N N   . LEU A 26  ? 0.3780 0.6415 0.4465 -0.0788 -0.0211 -0.0174 1819 LEU A N   
199 C CA  . LEU A 26  ? 0.4281 0.7060 0.4885 -0.1032 -0.0301 -0.0128 1819 LEU A CA  
200 C C   . LEU A 26  ? 0.4772 0.7543 0.5350 -0.1030 -0.0392 -0.0112 1819 LEU A C   
201 O O   . LEU A 26  ? 0.5215 0.7924 0.5642 -0.1245 -0.0505 -0.0072 1819 LEU A O   
202 C CB  . LEU A 26  ? 0.2957 0.6281 0.3712 -0.1128 -0.0235 -0.0123 1819 LEU A CB  
203 C CG  . LEU A 26  ? 0.4285 0.7642 0.5025 -0.1177 -0.0153 -0.0138 1819 LEU A CG  
204 C CD1 . LEU A 26  ? 0.3711 0.7678 0.4600 -0.1265 -0.0077 -0.0148 1819 LEU A CD1 
205 C CD2 . LEU A 26  ? 0.5006 0.7960 0.5487 -0.1401 -0.0248 -0.0087 1819 LEU A CD2 
206 N N   . GLU A 27  ? 0.4834 0.7642 0.5526 -0.0810 -0.0358 -0.0138 1820 GLU A N   
207 C CA  A GLU A 27  ? 0.4281 0.7089 0.4945 -0.0793 -0.0439 -0.0126 1820 GLU A CA  
208 C CA  B GLU A 27  ? 0.4265 0.7063 0.4923 -0.0795 -0.0441 -0.0125 1820 GLU A CA  
209 C C   . GLU A 27  ? 0.4032 0.6545 0.4664 -0.0580 -0.0419 -0.0154 1820 GLU A C   
210 O O   . GLU A 27  ? 0.3691 0.6147 0.4399 -0.0425 -0.0330 -0.0175 1820 GLU A O   
211 C CB  A GLU A 27  ? 0.4512 0.7839 0.5384 -0.0761 -0.0427 -0.0113 1820 GLU A CB  
212 C CB  B GLU A 27  ? 0.4516 0.7833 0.5376 -0.0777 -0.0434 -0.0111 1820 GLU A CB  
213 C CG  A GLU A 27  ? 0.4933 0.8706 0.5898 -0.0946 -0.0412 -0.0092 1820 GLU A CG  
214 C CG  B GLU A 27  ? 0.4954 0.8643 0.5839 -0.1028 -0.0468 -0.0074 1820 GLU A CG  
215 C CD  A GLU A 27  ? 0.5544 0.9723 0.6750 -0.0775 -0.0291 -0.0135 1820 GLU A CD  
216 C CD  B GLU A 27  ? 0.5624 0.9879 0.6725 -0.0998 -0.0471 -0.0063 1820 GLU A CD  
217 O OE1 A GLU A 27  ? 0.5662 0.9935 0.6879 -0.0839 -0.0219 -0.0152 1820 GLU A OE1 
218 O OE1 B GLU A 27  ? 0.5906 1.0184 0.7094 -0.0798 -0.0480 -0.0076 1820 GLU A OE1 
219 O OE2 A GLU A 27  ? 0.6314 1.0697 0.7679 -0.0568 -0.0277 -0.0157 1820 GLU A OE2 
220 O OE2 B GLU A 27  ? 0.5826 1.0523 0.7007 -0.1179 -0.0470 -0.0039 1820 GLU A OE2 
221 N N   . PRO A 28  ? 0.4000 0.6328 0.4502 -0.0582 -0.0502 -0.0153 1821 PRO A N   
222 C CA  . PRO A 28  ? 0.4461 0.6581 0.4931 -0.0396 -0.0476 -0.0175 1821 PRO A CA  
223 C C   . PRO A 28  ? 0.3954 0.6307 0.4607 -0.0223 -0.0410 -0.0162 1821 PRO A C   
224 O O   . PRO A 28  ? 0.3961 0.6648 0.4749 -0.0223 -0.0425 -0.0142 1821 PRO A O   
225 C CB  . PRO A 28  ? 0.4368 0.6357 0.4672 -0.0454 -0.0583 -0.0179 1821 PRO A CB  
226 C CG  . PRO A 28  ? 0.5780 0.7734 0.5961 -0.0682 -0.0680 -0.0166 1821 PRO A CG  
227 C CD  . PRO A 28  ? 0.4955 0.7261 0.5313 -0.0768 -0.0628 -0.0132 1821 PRO A CD  
228 N N   . VAL A 29  ? 0.3514 0.5685 0.4162 -0.0078 -0.0349 -0.0172 1822 VAL A N   
229 C CA  . VAL A 29  ? 0.3516 0.5785 0.4259 0.0083  -0.0323 -0.0151 1822 VAL A CA  
230 C C   . VAL A 29  ? 0.4456 0.6810 0.5161 0.0088  -0.0404 -0.0124 1822 VAL A C   
231 O O   . VAL A 29  ? 0.3970 0.6164 0.4519 0.0022  -0.0454 -0.0133 1822 VAL A O   
232 C CB  . VAL A 29  ? 0.4104 0.6115 0.4786 0.0184  -0.0266 -0.0151 1822 VAL A CB  
233 C CG1 . VAL A 29  ? 0.3912 0.5941 0.4626 0.0323  -0.0269 -0.0113 1822 VAL A CG1 
234 C CG2 . VAL A 29  ? 0.4293 0.6237 0.5017 0.0177  -0.0194 -0.0174 1822 VAL A CG2 
235 N N   . ASN A 30  ? 0.4205 0.6812 0.5043 0.0176  -0.0425 -0.0099 1823 ASN A N   
236 C CA  . ASN A 30  ? 0.3827 0.6510 0.4628 0.0197  -0.0509 -0.0064 1823 ASN A CA  
237 C C   . ASN A 30  ? 0.3809 0.6282 0.4531 0.0330  -0.0499 -0.0033 1823 ASN A C   
238 O O   . ASN A 30  ? 0.3221 0.5722 0.4031 0.0467  -0.0484 -0.0016 1823 ASN A O   
239 C CB  . ASN A 30  ? 0.3195 0.6280 0.4179 0.0230  -0.0556 -0.0047 1823 ASN A CB  
240 C CG  . ASN A 30  ? 0.4606 0.7788 0.5548 0.0230  -0.0662 -0.0004 1823 ASN A CG  
241 O OD1 . ASN A 30  ? 0.4068 0.7002 0.4843 0.0243  -0.0689 0.0015  1823 ASN A OD1 
242 N ND2 . ASN A 30  ? 0.3612 0.7190 0.4706 0.0211  -0.0722 0.0009  1823 ASN A ND2 
243 N N   . PRO A 31  ? 0.3912 0.6174 0.4454 0.0293  -0.0514 -0.0028 1824 PRO A N   
244 C CA  . PRO A 31  ? 0.3630 0.5715 0.4079 0.0383  -0.0497 0.0012  1824 PRO A CA  
245 C C   . PRO A 31  ? 0.4440 0.6618 0.4910 0.0474  -0.0575 0.0076  1824 PRO A C   
246 O O   . PRO A 31  ? 0.4481 0.6508 0.4891 0.0554  -0.0574 0.0124  1824 PRO A O   
247 C CB  . PRO A 31  ? 0.3881 0.5809 0.4136 0.0310  -0.0494 -0.0013 1824 PRO A CB  
248 C CG  . PRO A 31  ? 0.5101 0.7125 0.5325 0.0208  -0.0565 -0.0046 1824 PRO A CG  
249 C CD  . PRO A 31  ? 0.4006 0.6198 0.4401 0.0168  -0.0560 -0.0059 1824 PRO A CD  
250 N N   . ARG A 32  ? 0.4106 0.6521 0.4649 0.0459  -0.0655 0.0085  1825 ARG A N   
251 C CA  . ARG A 32  ? 0.4017 0.6538 0.4603 0.0572  -0.0744 0.0144  1825 ARG A CA  
252 C C   . ARG A 32  ? 0.4679 0.7232 0.5409 0.0734  -0.0731 0.0145  1825 ARG A C   
253 O O   . ARG A 32  ? 0.4695 0.7186 0.5403 0.0863  -0.0805 0.0197  1825 ARG A O   
254 C CB  . ARG A 32  ? 0.3749 0.6579 0.4418 0.0519  -0.0835 0.0149  1825 ARG A CB  
255 C CG  . ARG A 32  ? 0.4333 0.7096 0.4817 0.0369  -0.0880 0.0146  1825 ARG A CG  
256 C CD  . ARG A 32  ? 0.4492 0.7569 0.5066 0.0271  -0.0965 0.0144  1825 ARG A CD  
257 N NE  . ARG A 32  ? 0.3819 0.6831 0.4198 0.0150  -0.1047 0.0152  1825 ARG A NE  
258 C CZ  . ARG A 32  ? 0.4642 0.7871 0.5038 0.0019  -0.1135 0.0152  1825 ARG A CZ  
259 N NH1 . ARG A 32  ? 0.4213 0.7783 0.4830 -0.0016 -0.1143 0.0151  1825 ARG A NH1 
260 N NH2 . ARG A 32  ? 0.3610 0.6734 0.3793 -0.0088 -0.1217 0.0153  1825 ARG A NH2 
261 N N   . LEU A 33  ? 0.4190 0.6814 0.5043 0.0734  -0.0648 0.0085  1826 LEU A N   
262 C CA  . LEU A 33  ? 0.4588 0.7257 0.5568 0.0897  -0.0631 0.0061  1826 LEU A CA  
263 C C   . LEU A 33  ? 0.5152 0.7470 0.6024 0.0931  -0.0566 0.0061  1826 LEU A C   
264 O O   . LEU A 33  ? 0.5128 0.7386 0.6046 0.1077  -0.0568 0.0042  1826 LEU A O   
265 C CB  . LEU A 33  ? 0.4652 0.7673 0.5833 0.0873  -0.0580 -0.0008 1826 LEU A CB  
266 C CG  . LEU A 33  ? 0.4742 0.8157 0.6032 0.0786  -0.0643 -0.0003 1826 LEU A CG  
267 C CD1 . LEU A 33  ? 0.4129 0.7906 0.5588 0.0705  -0.0584 -0.0060 1826 LEU A CD1 
268 C CD2 . LEU A 33  ? 0.4075 0.7671 0.5443 0.0946  -0.0754 0.0031  1826 LEU A CD2 
269 N N   . VAL A 34  ? 0.5438 0.7532 0.6162 0.0805  -0.0515 0.0077  1827 VAL A N   
270 C CA  . VAL A 34  ? 0.4714 0.6532 0.5352 0.0803  -0.0448 0.0078  1827 VAL A CA  
271 C C   . VAL A 34  ? 0.4926 0.6511 0.5363 0.0753  -0.0474 0.0152  1827 VAL A C   
272 O O   . VAL A 34  ? 0.4084 0.5670 0.4437 0.0640  -0.0445 0.0150  1827 VAL A O   
273 C CB  . VAL A 34  ? 0.3983 0.5813 0.4656 0.0694  -0.0351 0.0019  1827 VAL A CB  
274 C CG1 . VAL A 34  ? 0.4097 0.5668 0.4691 0.0694  -0.0294 0.0026  1827 VAL A CG1 
275 C CG2 . VAL A 34  ? 0.3558 0.5657 0.4410 0.0707  -0.0328 -0.0043 1827 VAL A CG2 
276 N N   . SER A 35  ? 0.5066 0.6446 0.5406 0.0835  -0.0533 0.0214  1828 SER A N   
277 C CA  . SER A 35  ? 0.6640 0.7819 0.6769 0.0761  -0.0564 0.0302  1828 SER A CA  
278 C C   . SER A 35  ? 0.6427 0.7516 0.6482 0.0636  -0.0462 0.0293  1828 SER A C   
279 O O   . SER A 35  ? 0.6529 0.7516 0.6619 0.0640  -0.0408 0.0267  1828 SER A O   
280 C CB  . SER A 35  ? 0.7688 0.8606 0.7698 0.0858  -0.0666 0.0379  1828 SER A CB  
281 O OG  . SER A 35  ? 0.8272 0.9002 0.8051 0.0752  -0.0703 0.0481  1828 SER A OG  
282 N N   . GLY A 36  ? 0.5712 0.6862 0.5664 0.0532  -0.0438 0.0306  1829 GLY A N   
283 C CA  . GLY A 36  ? 0.5567 0.6690 0.5451 0.0432  -0.0349 0.0295  1829 GLY A CA  
284 C C   . GLY A 36  ? 0.4699 0.5953 0.4691 0.0407  -0.0271 0.0192  1829 GLY A C   
285 O O   . GLY A 36  ? 0.4665 0.5932 0.4610 0.0346  -0.0204 0.0170  1829 GLY A O   
286 N N   . TYR A 37  ? 0.5493 0.6135 0.4746 -0.0552 -0.0218 -0.0114 1830 TYR A N   
287 C CA  . TYR A 37  ? 0.5578 0.6223 0.4883 -0.0577 -0.0165 -0.0194 1830 TYR A CA  
288 C C   . TYR A 37  ? 0.5604 0.6066 0.4702 -0.0685 -0.0076 -0.0248 1830 TYR A C   
289 O O   . TYR A 37  ? 0.4127 0.4485 0.3286 -0.0672 0.0035  -0.0297 1830 TYR A O   
290 C CB  . TYR A 37  ? 0.4184 0.5032 0.3574 -0.0587 -0.0249 -0.0180 1830 TYR A CB  
291 C CG  . TYR A 37  ? 0.4184 0.5043 0.3670 -0.0588 -0.0197 -0.0245 1830 TYR A CG  
292 C CD1 . TYR A 37  ? 0.4888 0.5783 0.4548 -0.0498 -0.0172 -0.0261 1830 TYR A CD1 
293 C CD2 . TYR A 37  ? 0.4788 0.5594 0.4166 -0.0692 -0.0172 -0.0287 1830 TYR A CD2 
294 C CE1 . TYR A 37  ? 0.5671 0.6588 0.5413 -0.0507 -0.0139 -0.0297 1830 TYR A CE1 
295 C CE2 . TYR A 37  ? 0.5161 0.5973 0.4647 -0.0686 -0.0123 -0.0326 1830 TYR A CE2 
296 C CZ  . TYR A 37  ? 0.5500 0.6384 0.5175 -0.0591 -0.0113 -0.0321 1830 TYR A CZ  
297 O OH  . TYR A 37  ? 0.5113 0.6019 0.4890 -0.0593 -0.0081 -0.0336 1830 TYR A OH  
298 N N   . ARG A 38  ? 0.4313 0.4729 0.3162 -0.0797 -0.0119 -0.0231 1831 ARG A N   
299 C CA  . ARG A 38  ? 0.5203 0.5386 0.3772 -0.0921 -0.0016 -0.0298 1831 ARG A CA  
300 C C   . ARG A 38  ? 0.5953 0.5927 0.4483 -0.0882 0.0143  -0.0319 1831 ARG A C   
301 O O   . ARG A 38  ? 0.6188 0.5977 0.4665 -0.0902 0.0301  -0.0385 1831 ARG A O   
302 C CB  . ARG A 38  ? 0.5723 0.5901 0.3988 -0.1073 -0.0123 -0.0259 1831 ARG A CB  
303 C CG  . ARG A 38  ? 0.7369 0.7266 0.5242 -0.1247 -0.0029 -0.0344 1831 ARG A CG  
304 C CD  . ARG A 38  ? 0.7987 0.7859 0.5500 -0.1419 -0.0148 -0.0285 1831 ARG A CD  
305 N NE  . ARG A 38  ? 0.8661 0.8846 0.6272 -0.1468 -0.0378 -0.0171 1831 ARG A NE  
306 C CZ  . ARG A 38  ? 0.9211 0.9499 0.6798 -0.1586 -0.0469 -0.0181 1831 ARG A CZ  
307 N NH1 . ARG A 38  ? 0.8533 0.8602 0.5977 -0.1669 -0.0351 -0.0312 1831 ARG A NH1 
308 N NH2 . ARG A 38  ? 0.9338 0.9956 0.7070 -0.1618 -0.0674 -0.0044 1831 ARG A NH2 
309 N N   . ARG A 39  ? 0.5616 0.5617 0.4188 -0.0823 0.0115  -0.0253 1832 ARG A N   
310 C CA  . ARG A 39  ? 0.6161 0.5995 0.4722 -0.0793 0.0262  -0.0253 1832 ARG A CA  
311 C C   . ARG A 39  ? 0.5517 0.5375 0.4383 -0.0698 0.0358  -0.0272 1832 ARG A C   
312 O O   . ARG A 39  ? 0.5235 0.4949 0.4112 -0.0695 0.0526  -0.0288 1832 ARG A O   
313 C CB  . ARG A 39  ? 0.5227 0.5100 0.3792 -0.0754 0.0190  -0.0164 1832 ARG A CB  
314 C CG  . ARG A 39  ? 0.6414 0.6170 0.5048 -0.0711 0.0317  -0.0140 1832 ARG A CG  
315 C CD  . ARG A 39  ? 0.6796 0.6552 0.5383 -0.0694 0.0246  -0.0045 1832 ARG A CD  
316 N NE  . ARG A 39  ? 0.7833 0.7754 0.6597 -0.0616 0.0091  0.0010  1832 ARG A NE  
317 C CZ  . ARG A 39  ? 0.8811 0.8783 0.7833 -0.0523 0.0079  0.0013  1832 ARG A CZ  
318 N NH1 . ARG A 39  ? 0.9144 0.9063 0.8306 -0.0510 0.0177  -0.0016 1832 ARG A NH1 
319 N NH2 . ARG A 39  ? 0.8521 0.8591 0.7660 -0.0450 -0.0027 0.0053  1832 ARG A NH2 
320 N N   . ILE A 40  ? 0.5116 0.5159 0.4229 -0.0627 0.0259  -0.0259 1833 ILE A N   
321 C CA  . ILE A 40  ? 0.5232 0.5329 0.4627 -0.0557 0.0305  -0.0247 1833 ILE A CA  
322 C C   . ILE A 40  ? 0.4813 0.4931 0.4308 -0.0561 0.0355  -0.0281 1833 ILE A C   
323 O O   . ILE A 40  ? 0.4923 0.5018 0.4596 -0.0531 0.0457  -0.0255 1833 ILE A O   
324 C CB  . ILE A 40  ? 0.4821 0.5058 0.4376 -0.0495 0.0181  -0.0217 1833 ILE A CB  
325 C CG1 . ILE A 40  ? 0.4780 0.4948 0.4297 -0.0479 0.0175  -0.0168 1833 ILE A CG1 
326 C CG2 . ILE A 40  ? 0.4834 0.5149 0.4630 -0.0465 0.0188  -0.0208 1833 ILE A CG2 
327 C CD1 . ILE A 40  ? 0.3257 0.3492 0.2869 -0.0423 0.0073  -0.0149 1833 ILE A CD1 
328 N N   . ILE A 41  ? 0.4033 0.4210 0.3448 -0.0598 0.0283  -0.0319 1834 ILE A N   
329 C CA  . ILE A 41  ? 0.4127 0.4323 0.3641 -0.0604 0.0319  -0.0341 1834 ILE A CA  
330 C C   . ILE A 41  ? 0.5134 0.5110 0.4423 -0.0685 0.0444  -0.0396 1834 ILE A C   
331 O O   . ILE A 41  ? 0.4793 0.4731 0.3841 -0.0778 0.0386  -0.0436 1834 ILE A O   
332 C CB  . ILE A 41  ? 0.3524 0.3909 0.3094 -0.0604 0.0181  -0.0346 1834 ILE A CB  
333 C CG1 . ILE A 41  ? 0.3948 0.4481 0.3695 -0.0529 0.0098  -0.0310 1834 ILE A CG1 
334 C CG2 . ILE A 41  ? 0.3949 0.4336 0.3582 -0.0630 0.0217  -0.0363 1834 ILE A CG2 
335 C CD1 . ILE A 41  ? 0.3317 0.3856 0.3266 -0.0494 0.0146  -0.0272 1834 ILE A CD1 
336 N N   . LYS A 42  ? 0.6008 0.5833 0.5377 -0.0656 0.0621  -0.0391 1835 LYS A N   
337 C CA  . LYS A 42  ? 0.5489 0.5028 0.4614 -0.0727 0.0790  -0.0458 1835 LYS A CA  
338 C C   . LYS A 42  ? 0.5216 0.4710 0.4306 -0.0779 0.0786  -0.0501 1835 LYS A C   
339 O O   . LYS A 42  ? 0.4999 0.4269 0.3772 -0.0896 0.0843  -0.0581 1835 LYS A O   
340 C CB  . LYS A 42  ? 0.5694 0.5076 0.4957 -0.0654 0.1021  -0.0424 1835 LYS A CB  
341 C CG  . LYS A 42  ? 0.7086 0.6508 0.6411 -0.0610 0.1046  -0.0369 1835 LYS A CG  
342 C CD  . LYS A 42  ? 0.8419 0.7674 0.7338 -0.0706 0.1053  -0.0428 1835 LYS A CD  
343 C CE  . LYS A 42  ? 0.9134 0.8400 0.8113 -0.0664 0.1107  -0.0364 1835 LYS A CE  
344 N NZ  . LYS A 42  ? 0.8890 0.8432 0.8151 -0.0601 0.0924  -0.0286 1835 LYS A NZ  
345 N N   . ASN A 43  ? 0.4680 0.4362 0.4065 -0.0714 0.0723  -0.0447 1836 ASN A N   
346 C CA  . ASN A 43  ? 0.4442 0.4077 0.3825 -0.0758 0.0732  -0.0470 1836 ASN A CA  
347 C C   . ASN A 43  ? 0.4715 0.4644 0.4226 -0.0757 0.0532  -0.0438 1836 ASN A C   
348 O O   . ASN A 43  ? 0.4430 0.4511 0.4207 -0.0688 0.0503  -0.0371 1836 ASN A O   
349 C CB  . ASN A 43  ? 0.4685 0.4216 0.4311 -0.0676 0.0905  -0.0414 1836 ASN A CB  
350 C CG  . ASN A 43  ? 0.6227 0.5447 0.5745 -0.0660 0.1150  -0.0443 1836 ASN A CG  
351 O OD1 . ASN A 43  ? 0.6758 0.6015 0.6516 -0.0557 0.1252  -0.0361 1836 ASN A OD1 
352 N ND2 . ASN A 43  ? 0.5534 0.4441 0.4676 -0.0773 0.1252  -0.0556 1836 ASN A ND2 
353 N N   . PRO A 44  ? 0.4993 0.5010 0.4321 -0.0839 0.0397  -0.0474 1837 PRO A N   
354 C CA  . PRO A 44  ? 0.4062 0.4356 0.3522 -0.0828 0.0239  -0.0440 1837 PRO A CA  
355 C C   . PRO A 44  ? 0.4670 0.4975 0.4227 -0.0851 0.0259  -0.0430 1837 PRO A C   
356 O O   . PRO A 44  ? 0.4040 0.4118 0.3490 -0.0914 0.0368  -0.0465 1837 PRO A O   
357 C CB  . PRO A 44  ? 0.4980 0.5340 0.4232 -0.0925 0.0124  -0.0460 1837 PRO A CB  
358 C CG  . PRO A 44  ? 0.5125 0.5197 0.4071 -0.1034 0.0217  -0.0521 1837 PRO A CG  
359 C CD  . PRO A 44  ? 0.4199 0.4086 0.3204 -0.0946 0.0383  -0.0527 1837 PRO A CD  
360 N N   . MET A 45  ? 0.4072 0.4614 0.3817 -0.0802 0.0166  -0.0381 1838 MET A N   
361 C CA  . MET A 45  ? 0.4153 0.4731 0.3988 -0.0830 0.0170  -0.0354 1838 MET A CA  
362 C C   . MET A 45  ? 0.4118 0.4977 0.4044 -0.0813 0.0045  -0.0324 1838 MET A C   
363 O O   . MET A 45  ? 0.4167 0.5156 0.4146 -0.0745 -0.0011 -0.0314 1838 MET A O   
364 C CB  . MET A 45  ? 0.4016 0.4515 0.4044 -0.0759 0.0269  -0.0291 1838 MET A CB  
365 C CG  . MET A 45  ? 0.3858 0.4357 0.3980 -0.0787 0.0288  -0.0242 1838 MET A CG  
366 S SD  . MET A 45  ? 0.5231 0.5498 0.5124 -0.0928 0.0350  -0.0316 1838 MET A SD  
367 C CE  . MET A 45  ? 0.5615 0.5497 0.5343 -0.0929 0.0541  -0.0383 1838 MET A CE  
368 N N   . ASP A 46  ? 0.4082 0.5011 0.4017 -0.0879 0.0019  -0.0310 1839 ASP A N   
369 C CA  . ASP A 46  ? 0.3932 0.5121 0.3956 -0.0863 -0.0066 -0.0277 1839 ASP A CA  
370 C C   . ASP A 46  ? 0.4431 0.5642 0.4500 -0.0929 -0.0053 -0.0242 1839 ASP A C   
371 O O   . ASP A 46  ? 0.4727 0.5738 0.4746 -0.0992 0.0014  -0.0249 1839 ASP A O   
372 C CB  . ASP A 46  ? 0.4540 0.5880 0.4507 -0.0890 -0.0144 -0.0288 1839 ASP A CB  
373 C CG  . ASP A 46  ? 0.5930 0.7236 0.5782 -0.1033 -0.0169 -0.0298 1839 ASP A CG  
374 O OD1 . ASP A 46  ? 0.6211 0.7298 0.5889 -0.1105 -0.0136 -0.0344 1839 ASP A OD1 
375 O OD2 . ASP A 46  ? 0.6217 0.7701 0.6136 -0.1087 -0.0214 -0.0259 1839 ASP A OD2 
376 N N   . PHE A 47  ? 0.3660 0.5093 0.3810 -0.0916 -0.0102 -0.0203 1840 PHE A N   
377 C CA  . PHE A 47  ? 0.3958 0.5426 0.4162 -0.0972 -0.0088 -0.0152 1840 PHE A CA  
378 C C   . PHE A 47  ? 0.3614 0.5042 0.3746 -0.1103 -0.0093 -0.0162 1840 PHE A C   
379 O O   . PHE A 47  ? 0.4200 0.5500 0.4332 -0.1169 -0.0049 -0.0136 1840 PHE A O   
380 C CB  . PHE A 47  ? 0.3660 0.5362 0.3931 -0.0934 -0.0121 -0.0112 1840 PHE A CB  
381 C CG  . PHE A 47  ? 0.3375 0.5078 0.3666 -0.0851 -0.0124 -0.0099 1840 PHE A CG  
382 C CD1 . PHE A 47  ? 0.4127 0.5674 0.4451 -0.0821 -0.0104 -0.0081 1840 PHE A CD1 
383 C CD2 . PHE A 47  ? 0.4803 0.6656 0.5075 -0.0814 -0.0138 -0.0099 1840 PHE A CD2 
384 C CE1 . PHE A 47  ? 0.4186 0.5756 0.4534 -0.0776 -0.0131 -0.0052 1840 PHE A CE1 
385 C CE2 . PHE A 47  ? 0.5363 0.7187 0.5600 -0.0776 -0.0152 -0.0095 1840 PHE A CE2 
386 C CZ  . PHE A 47  ? 0.5389 0.7086 0.5670 -0.0767 -0.0164 -0.0065 1840 PHE A CZ  
387 N N   . SER A 48  ? 0.4413 0.5949 0.4489 -0.1155 -0.0154 -0.0187 1841 SER A N   
388 C CA  . SER A 48  ? 0.4866 0.6376 0.4857 -0.1318 -0.0183 -0.0187 1841 SER A CA  
389 C C   . SER A 48  ? 0.4801 0.5942 0.4600 -0.1407 -0.0116 -0.0253 1841 SER A C   
390 O O   . SER A 48  ? 0.4904 0.5902 0.4612 -0.1547 -0.0095 -0.0261 1841 SER A O   
391 C CB  . SER A 48  ? 0.5502 0.7250 0.5501 -0.1365 -0.0284 -0.0166 1841 SER A CB  
392 O OG  . SER A 48  ? 0.5338 0.6962 0.5201 -0.1363 -0.0305 -0.0212 1841 SER A OG  
393 N N   . THR A 49  ? 0.4173 0.5135 0.3898 -0.1332 -0.0063 -0.0302 1842 THR A N   
394 C CA  . THR A 49  ? 0.4295 0.4870 0.3839 -0.1393 0.0052  -0.0367 1842 THR A CA  
395 C C   . THR A 49  ? 0.4941 0.5350 0.4599 -0.1348 0.0166  -0.0329 1842 THR A C   
396 O O   . THR A 49  ? 0.5114 0.5230 0.4645 -0.1447 0.0257  -0.0361 1842 THR A O   
397 C CB  . THR A 49  ? 0.5286 0.5732 0.4752 -0.1311 0.0101  -0.0413 1842 THR A CB  
398 O OG1 . THR A 49  ? 0.5755 0.6387 0.5149 -0.1339 -0.0018 -0.0418 1842 THR A OG1 
399 C CG2 . THR A 49  ? 0.5000 0.5022 0.4231 -0.1386 0.0247  -0.0493 1842 THR A CG2 
400 N N   . MET A 50  ? 0.4615 0.5195 0.4500 -0.1211 0.0159  -0.0252 1843 MET A N   
401 C CA  . MET A 50  ? 0.4603 0.5084 0.4632 -0.1171 0.0239  -0.0174 1843 MET A CA  
402 C C   . MET A 50  ? 0.4190 0.4703 0.4210 -0.1287 0.0213  -0.0139 1843 MET A C   
403 O O   . MET A 50  ? 0.4712 0.4985 0.4737 -0.1323 0.0311  -0.0111 1843 MET A O   
404 C CB  . MET A 50  ? 0.3858 0.4556 0.4099 -0.1039 0.0197  -0.0083 1843 MET A CB  
405 C CG  . MET A 50  ? 0.4280 0.4918 0.4569 -0.0933 0.0238  -0.0093 1843 MET A CG  
406 S SD  . MET A 50  ? 0.4774 0.5693 0.5233 -0.0834 0.0139  -0.0011 1843 MET A SD  
407 C CE  . MET A 50  ? 0.5698 0.6662 0.6340 -0.0832 0.0144  0.0142  1843 MET A CE  
408 N N   . ARG A 51  ? 0.4217 0.5023 0.4243 -0.1340 0.0096  -0.0130 1844 ARG A N   
409 C CA  . ARG A 51  ? 0.4330 0.5193 0.4352 -0.1468 0.0070  -0.0092 1844 ARG A CA  
410 C C   . ARG A 51  ? 0.4915 0.5475 0.4729 -0.1636 0.0113  -0.0163 1844 ARG A C   
411 O O   . ARG A 51  ? 0.6200 0.6561 0.5993 -0.1720 0.0178  -0.0138 1844 ARG A O   
412 C CB  . ARG A 51  ? 0.3629 0.4876 0.3715 -0.1488 -0.0044 -0.0065 1844 ARG A CB  
413 C CG  . ARG A 51  ? 0.4500 0.5842 0.4575 -0.1655 -0.0085 -0.0031 1844 ARG A CG  
414 C CD  . ARG A 51  ? 0.5346 0.6647 0.5505 -0.1672 -0.0034 0.0052  1844 ARG A CD  
415 N NE  . ARG A 51  ? 0.4842 0.6371 0.5139 -0.1539 -0.0041 0.0123  1844 ARG A NE  
416 C CZ  . ARG A 51  ? 0.4685 0.6166 0.5051 -0.1508 -0.0001 0.0209  1844 ARG A CZ  
417 N NH1 . ARG A 51  ? 0.4709 0.5921 0.5062 -0.1574 0.0062  0.0245  1844 ARG A NH1 
418 N NH2 . ARG A 51  ? 0.5179 0.6861 0.5610 -0.1418 -0.0022 0.0266  1844 ARG A NH2 
419 N N   . HIS A 52  ? 0.5871 0.6368 0.5504 -0.1701 0.0080  -0.0250 1845 HIS A N   
420 C CA  . HIS A 52  ? 0.6389 0.6565 0.5746 -0.1897 0.0114  -0.0332 1845 HIS A CA  
421 C C   . HIS A 52  ? 0.6326 0.6030 0.5593 -0.1875 0.0305  -0.0374 1845 HIS A C   
422 O O   . HIS A 52  ? 0.6071 0.5486 0.5197 -0.2020 0.0373  -0.0400 1845 HIS A O   
423 C CB  . HIS A 52  ? 0.6730 0.6914 0.5883 -0.1964 0.0042  -0.0406 1845 HIS A CB  
424 C CG  . HIS A 52  ? 0.8846 0.8643 0.7633 -0.2185 0.0083  -0.0507 1845 HIS A CG  
425 N ND1 . HIS A 52  ? 0.9545 0.8871 0.8110 -0.2174 0.0260  -0.0605 1845 HIS A ND1 
426 C CD2 . HIS A 52  ? 0.9216 0.9016 0.7798 -0.2438 -0.0028 -0.0523 1845 HIS A CD2 
427 C CE1 . HIS A 52  ? 0.9503 0.8517 0.7694 -0.2416 0.0269  -0.0698 1845 HIS A CE1 
428 N NE2 . HIS A 52  ? 0.9529 0.8830 0.7720 -0.2592 0.0079  -0.0647 1845 HIS A NE2 
429 N N   . ARG A 53  ? 0.6037 0.5656 0.5405 -0.1692 0.0405  -0.0369 1846 ARG A N   
430 C CA  . ARG A 53  ? 0.6175 0.5372 0.5526 -0.1634 0.0613  -0.0381 1846 ARG A CA  
431 C C   . ARG A 53  ? 0.6904 0.6059 0.6449 -0.1613 0.0667  -0.0272 1846 ARG A C   
432 O O   . ARG A 53  ? 0.7074 0.5823 0.6519 -0.1671 0.0823  -0.0294 1846 ARG A O   
433 C CB  . ARG A 53  ? 0.6511 0.5723 0.6014 -0.1435 0.0691  -0.0357 1846 ARG A CB  
434 C CG  . ARG A 53  ? 0.8788 0.7616 0.8357 -0.1341 0.0925  -0.0335 1846 ARG A CG  
435 C CD  . ARG A 53  ? 0.9687 0.8372 0.9212 -0.1241 0.1044  -0.0387 1846 ARG A CD  
436 N NE  . ARG A 53  ? 1.0629 0.9162 1.0429 -0.1068 0.1236  -0.0283 1846 ARG A NE  
437 C CZ  . ARG A 53  ? 1.1693 0.9963 1.1474 -0.0981 0.1438  -0.0314 1846 ARG A CZ  
438 N NH1 . ARG A 53  ? 1.2592 1.0687 1.2033 -0.1065 0.1475  -0.0463 1846 ARG A NH1 
439 N NH2 . ARG A 53  ? 1.1659 0.9852 1.1772 -0.0812 0.1606  -0.0179 1846 ARG A NH2 
440 N N   . LEU A 54  ? 0.5500 0.5043 0.5300 -0.1533 0.0550  -0.0151 1847 LEU A N   
441 C CA  . LEU A 54  ? 0.6565 0.6097 0.6533 -0.1529 0.0581  -0.0028 1847 LEU A CA  
442 C C   . LEU A 54  ? 0.6802 0.6172 0.6588 -0.1740 0.0575  -0.0068 1847 LEU A C   
443 O O   . LEU A 54  ? 0.8046 0.7105 0.7837 -0.1775 0.0697  -0.0028 1847 LEU A O   
444 C CB  . LEU A 54  ? 0.6324 0.6307 0.6517 -0.1442 0.0443  0.0091  1847 LEU A CB  
445 C CG  . LEU A 54  ? 0.5855 0.5909 0.6293 -0.1348 0.0463  0.0265  1847 LEU A CG  
446 C CD1 . LEU A 54  ? 0.5530 0.5305 0.6115 -0.1223 0.0618  0.0335  1847 LEU A CD1 
447 C CD2 . LEU A 54  ? 0.6308 0.6773 0.6862 -0.1268 0.0327  0.0329  1847 LEU A CD2 
448 N N   . SER A 55  ? 0.7230 0.6799 0.6867 -0.1887 0.0438  -0.0136 1848 SER A N   
449 C CA  . SER A 55  ? 0.7725 0.7200 0.7202 -0.2120 0.0400  -0.0159 1848 SER A CA  
450 C C   . SER A 55  ? 0.8696 0.7593 0.7879 -0.2257 0.0552  -0.0270 1848 SER A C   
451 O O   . SER A 55  ? 0.9204 0.7857 0.8314 -0.2396 0.0607  -0.0255 1848 SER A O   
452 C CB  . SER A 55  ? 0.6666 0.6492 0.6070 -0.2246 0.0219  -0.0191 1848 SER A CB  
453 O OG  . SER A 55  ? 0.7240 0.7554 0.6900 -0.2153 0.0111  -0.0085 1848 SER A OG  
454 N N   . ARG A 56  ? 0.7946 0.6590 0.6928 -0.2234 0.0633  -0.0387 1849 ARG A N   
455 C CA  . ARG A 56  ? 0.9048 0.7090 0.7685 -0.2374 0.0807  -0.0514 1849 ARG A CA  
456 C C   . ARG A 56  ? 0.9827 0.7470 0.8586 -0.2202 0.1062  -0.0479 1849 ARG A C   
457 O O   . ARG A 56  ? 1.1233 0.8317 0.9715 -0.2272 0.1266  -0.0592 1849 ARG A O   
458 C CB  . ARG A 56  ? 0.9212 0.7123 0.7516 -0.2460 0.0794  -0.0660 1849 ARG A CB  
459 C CG  . ARG A 56  ? 0.9883 0.7877 0.8316 -0.2223 0.0859  -0.0659 1849 ARG A CG  
460 C CD  . ARG A 56  ? 1.1711 0.9447 0.9748 -0.2330 0.0898  -0.0809 1849 ARG A CD  
461 N NE  . ARG A 56  ? 1.1347 0.9134 0.9514 -0.2106 0.0984  -0.0802 1849 ARG A NE  
462 C CZ  . ARG A 56  ? 1.0617 0.8008 0.8768 -0.1980 0.1244  -0.0836 1849 ARG A CZ  
463 N NH1 . ARG A 56  ? 1.0899 0.7778 0.8897 -0.2042 0.1461  -0.0888 1849 ARG A NH1 
464 N NH2 . ARG A 56  ? 0.9608 0.7110 0.7911 -0.1790 0.1300  -0.0812 1849 ARG A NH2 
465 N N   . GLY A 57  ? 0.9280 0.7188 0.8442 -0.1986 0.1062  -0.0317 1850 GLY A N   
466 C CA  . GLY A 57  ? 0.9302 0.6912 0.8668 -0.1809 0.1283  -0.0228 1850 GLY A CA  
467 C C   . GLY A 57  ? 0.9492 0.6965 0.8918 -0.1623 0.1438  -0.0254 1850 GLY A C   
468 O O   . GLY A 57  ? 0.9751 0.6897 0.9323 -0.1488 0.1668  -0.0191 1850 GLY A O   
469 N N   . GLY A 58  ? 0.9057 0.6785 0.8411 -0.1601 0.1326  -0.0324 1851 GLY A N   
470 C CA  . GLY A 58  ? 0.8813 0.6394 0.8159 -0.1465 0.1472  -0.0371 1851 GLY A CA  
471 C C   . GLY A 58  ? 0.8636 0.6436 0.8432 -0.1206 0.1523  -0.0198 1851 GLY A C   
472 O O   . GLY A 58  ? 0.8927 0.6613 0.8761 -0.1088 0.1662  -0.0217 1851 GLY A O   
473 N N   . TYR A 59  ? 0.8372 0.6492 0.8502 -0.1130 0.1412  -0.0019 1852 TYR A N   
474 C CA  . TYR A 59  ? 0.8328 0.6674 0.8885 -0.0917 0.1432  0.0175  1852 TYR A CA  
475 C C   . TYR A 59  ? 0.9411 0.7491 1.0211 -0.0829 0.1620  0.0330  1852 TYR A C   
476 O O   . TYR A 59  ? 0.9192 0.7245 0.9994 -0.0911 0.1575  0.0389  1852 TYR A O   
477 C CB  . TYR A 59  ? 0.7847 0.6746 0.8588 -0.0900 0.1167  0.0284  1852 TYR A CB  
478 C CG  . TYR A 59  ? 0.6959 0.6148 0.7566 -0.0925 0.1003  0.0178  1852 TYR A CG  
479 C CD1 . TYR A 59  ? 0.6419 0.5641 0.7096 -0.0817 0.1049  0.0164  1852 TYR A CD1 
480 C CD2 . TYR A 59  ? 0.6258 0.5700 0.6703 -0.1048 0.0813  0.0112  1852 TYR A CD2 
481 C CE1 . TYR A 59  ? 0.6323 0.5790 0.6882 -0.0838 0.0903  0.0078  1852 TYR A CE1 
482 C CE2 . TYR A 59  ? 0.5623 0.5318 0.5977 -0.1053 0.0680  0.0034  1852 TYR A CE2 
483 C CZ  . TYR A 59  ? 0.6108 0.5802 0.6509 -0.0950 0.0722  0.0014  1852 TYR A CZ  
484 O OH  . TYR A 59  ? 0.5977 0.5896 0.6287 -0.0954 0.0594  -0.0056 1852 TYR A OH  
485 N N   . THR A 60  ? 0.9495 0.7392 1.0528 -0.0656 0.1836  0.0413  1853 THR A N   
486 C CA  . THR A 60  ? 0.9995 0.7639 1.1329 -0.0533 0.2044  0.0594  1853 THR A CA  
487 C C   . THR A 60  ? 1.0510 0.8608 1.2341 -0.0398 0.1903  0.0891  1853 THR A C   
488 O O   . THR A 60  ? 1.1311 0.9373 1.3342 -0.0376 0.1920  0.1066  1853 THR A O   
489 C CB  . THR A 60  ? 1.0311 0.7526 1.1686 -0.0400 0.2383  0.0559  1853 THR A CB  
490 O OG1 . THR A 60  ? 1.0806 0.8358 1.2553 -0.0223 0.2367  0.0705  1853 THR A OG1 
491 C CG2 . THR A 60  ? 1.0622 0.7460 1.1447 -0.0552 0.2480  0.0255  1853 THR A CG2 
492 N N   . SER A 61  ? 0.9721 0.8236 1.1739 -0.0323 0.1757  0.0961  1854 SER A N   
493 C CA  . SER A 61  ? 0.9008 0.7970 1.1448 -0.0232 0.1593  0.1239  1854 SER A CA  
494 C C   . SER A 61  ? 0.8543 0.7960 1.0846 -0.0328 0.1290  0.1181  1854 SER A C   
495 O O   . SER A 61  ? 0.8525 0.7927 1.0489 -0.0420 0.1233  0.0951  1854 SER A O   
496 C CB  . SER A 61  ? 0.8889 0.7897 1.1769 -0.0035 0.1744  0.1431  1854 SER A CB  
497 O OG  . SER A 61  ? 0.8139 0.7208 1.0912 -0.0019 0.1754  0.1290  1854 SER A OG  
498 N N   . SER A 62  ? 0.7713 0.7525 1.0273 -0.0311 0.1099  0.1401  1855 SER A N   
499 C CA  . SER A 62  ? 0.7127 0.7329 0.9549 -0.0395 0.0839  0.1351  1855 SER A CA  
500 C C   . SER A 62  ? 0.6751 0.7099 0.9262 -0.0330 0.0821  0.1326  1855 SER A C   
501 O O   . SER A 62  ? 0.6988 0.7544 0.9298 -0.0402 0.0656  0.1208  1855 SER A O   
502 C CB  . SER A 62  ? 0.7014 0.7551 0.9604 -0.0432 0.0641  0.1582  1855 SER A CB  
503 O OG  . SER A 62  ? 0.7287 0.8012 1.0297 -0.0327 0.0627  0.1853  1855 SER A OG  
504 N N   . GLU A 63  ? 0.6723 0.6955 0.9538 -0.0192 0.1002  0.1439  1856 GLU A N   
505 C CA  . GLU A 63  ? 0.6219 0.6573 0.9121 -0.0136 0.1006  0.1414  1856 GLU A CA  
506 C C   . GLU A 63  ? 0.6637 0.6760 0.9136 -0.0188 0.1080  0.1113  1856 GLU A C   
507 O O   . GLU A 63  ? 0.6110 0.6407 0.8504 -0.0218 0.0967  0.1027  1856 GLU A O   
508 C CB  . GLU A 63  ? 0.6986 0.7280 1.0346 0.0032  0.1212  0.1626  1856 GLU A CB  
509 C CG  . GLU A 63  ? 0.8096 0.8801 1.1927 0.0076  0.1057  0.1965  1856 GLU A CG  
510 C CD  . GLU A 63  ? 0.9359 1.0091 1.3377 0.0081  0.1023  0.2181  1856 GLU A CD  
511 O OE1 . GLU A 63  ? 0.9721 1.0110 1.3551 0.0073  0.1163  0.2076  1856 GLU A OE1 
512 O OE2 . GLU A 63  ? 0.9284 1.0379 1.3629 0.0079  0.0848  0.2467  1856 GLU A OE2 
513 N N   . GLU A 64  ? 0.7181 0.6901 0.9440 -0.0213 0.1265  0.0958  1857 GLU A N   
514 C CA  . GLU A 64  ? 0.6744 0.6263 0.8570 -0.0305 0.1293  0.0684  1857 GLU A CA  
515 C C   . GLU A 64  ? 0.5915 0.5714 0.7498 -0.0429 0.1029  0.0580  1857 GLU A C   
516 O O   . GLU A 64  ? 0.6186 0.6058 0.7585 -0.0460 0.0962  0.0449  1857 GLU A O   
517 C CB  . GLU A 64  ? 0.8006 0.7058 0.9566 -0.0366 0.1487  0.0549  1857 GLU A CB  
518 C CG  . GLU A 64  ? 0.9908 0.8538 1.1513 -0.0267 0.1813  0.0532  1857 GLU A CG  
519 C CD  . GLU A 64  ? 1.1772 0.9894 1.3014 -0.0374 0.1986  0.0365  1857 GLU A CD  
520 O OE1 . GLU A 64  ? 1.3053 1.0770 1.4054 -0.0381 0.2218  0.0220  1857 GLU A OE1 
521 O OE2 . GLU A 64  ? 1.1992 1.0109 1.3162 -0.0471 0.1891  0.0377  1857 GLU A OE2 
522 N N   . PHE A 65  ? 0.5645 0.5591 0.7228 -0.0495 0.0896  0.0643  1858 PHE A N   
523 C CA  . PHE A 65  ? 0.4593 0.4799 0.5970 -0.0599 0.0680  0.0557  1858 PHE A CA  
524 C C   . PHE A 65  ? 0.3956 0.4474 0.5422 -0.0566 0.0533  0.0598  1858 PHE A C   
525 O O   . PHE A 65  ? 0.4859 0.5472 0.6117 -0.0611 0.0440  0.0462  1858 PHE A O   
526 C CB  . PHE A 65  ? 0.4373 0.4687 0.5777 -0.0664 0.0592  0.0654  1858 PHE A CB  
527 C CG  . PHE A 65  ? 0.4505 0.5086 0.5721 -0.0758 0.0405  0.0581  1858 PHE A CG  
528 C CD1 . PHE A 65  ? 0.4361 0.5251 0.5658 -0.0750 0.0251  0.0677  1858 PHE A CD1 
529 C CD2 . PHE A 65  ? 0.5088 0.5605 0.6047 -0.0861 0.0392  0.0428  1858 PHE A CD2 
530 C CE1 . PHE A 65  ? 0.4670 0.5763 0.5781 -0.0824 0.0123  0.0602  1858 PHE A CE1 
531 C CE2 . PHE A 65  ? 0.4818 0.5593 0.5653 -0.0925 0.0250  0.0381  1858 PHE A CE2 
532 C CZ  . PHE A 65  ? 0.4122 0.5165 0.5027 -0.0897 0.0134  0.0461  1858 PHE A CZ  
533 N N   . ALA A 66  ? 0.4122 0.4797 0.5904 -0.0493 0.0508  0.0799  1859 ALA A N   
534 C CA  . ALA A 66  ? 0.4894 0.5847 0.6748 -0.0491 0.0358  0.0850  1859 ALA A CA  
535 C C   . ALA A 66  ? 0.4735 0.5607 0.6520 -0.0453 0.0422  0.0727  1859 ALA A C   
536 O O   . ALA A 66  ? 0.5229 0.6243 0.6879 -0.0491 0.0299  0.0648  1859 ALA A O   
537 C CB  . ALA A 66  ? 0.4982 0.6123 0.7214 -0.0443 0.0314  0.1119  1859 ALA A CB  
538 N N   . ALA A 67  ? 0.3777 0.4395 0.5633 -0.0379 0.0630  0.0708  1860 ALA A N   
539 C CA  . ALA A 67  ? 0.4384 0.4900 0.6144 -0.0350 0.0711  0.0594  1860 ALA A CA  
540 C C   . ALA A 67  ? 0.3378 0.3852 0.4750 -0.0437 0.0631  0.0377  1860 ALA A C   
541 O O   . ALA A 67  ? 0.4173 0.4722 0.5463 -0.0440 0.0574  0.0313  1860 ALA A O   
542 C CB  . ALA A 67  ? 0.4581 0.4769 0.6408 -0.0269 0.0984  0.0588  1860 ALA A CB  
543 N N   . ASP A 68  ? 0.3165 0.3530 0.4317 -0.0513 0.0623  0.0281  1861 ASP A N   
544 C CA  . ASP A 68  ? 0.3798 0.4187 0.4642 -0.0597 0.0527  0.0118  1861 ASP A CA  
545 C C   . ASP A 68  ? 0.3818 0.4513 0.4665 -0.0614 0.0335  0.0133  1861 ASP A C   
546 O O   . ASP A 68  ? 0.3887 0.4645 0.4605 -0.0620 0.0271  0.0048  1861 ASP A O   
547 C CB  . ASP A 68  ? 0.4645 0.4884 0.5295 -0.0692 0.0552  0.0041  1861 ASP A CB  
548 C CG  . ASP A 68  ? 0.5586 0.5464 0.6027 -0.0731 0.0721  -0.0071 1861 ASP A CG  
549 O OD1 . ASP A 68  ? 0.4848 0.4621 0.5268 -0.0680 0.0811  -0.0102 1861 ASP A OD1 
550 O OD2 . ASP A 68  ? 0.5287 0.4972 0.5562 -0.0827 0.0769  -0.0128 1861 ASP A OD2 
551 N N   . ALA A 69  ? 0.3244 0.4105 0.4212 -0.0627 0.0251  0.0241  1862 ALA A N   
552 C CA  . ALA A 69  ? 0.3829 0.4931 0.4753 -0.0655 0.0095  0.0248  1862 ALA A CA  
553 C C   . ALA A 69  ? 0.3577 0.4749 0.4560 -0.0618 0.0052  0.0261  1862 ALA A C   
554 O O   . ALA A 69  ? 0.3130 0.4363 0.3964 -0.0631 -0.0018 0.0170  1862 ALA A O   
555 C CB  . ALA A 69  ? 0.3189 0.4432 0.4225 -0.0685 0.0025  0.0387  1862 ALA A CB  
556 N N   . LEU A 70  ? 0.3367 0.4528 0.4588 -0.0570 0.0102  0.0385  1863 LEU A N   
557 C CA  . LEU A 70  ? 0.3579 0.4822 0.4883 -0.0554 0.0056  0.0418  1863 LEU A CA  
558 C C   . LEU A 70  ? 0.3517 0.4623 0.4672 -0.0527 0.0124  0.0279  1863 LEU A C   
559 O O   . LEU A 70  ? 0.3414 0.4577 0.4530 -0.0536 0.0059  0.0253  1863 LEU A O   
560 C CB  . LEU A 70  ? 0.3773 0.5072 0.5424 -0.0507 0.0104  0.0614  1863 LEU A CB  
561 C CG  . LEU A 70  ? 0.5089 0.6579 0.6914 -0.0547 -0.0007 0.0799  1863 LEU A CG  
562 C CD1 . LEU A 70  ? 0.5029 0.6610 0.7263 -0.0489 0.0041  0.1030  1863 LEU A CD1 
563 C CD2 . LEU A 70  ? 0.4316 0.5978 0.5968 -0.0652 -0.0202 0.0781  1863 LEU A CD2 
564 N N   . LEU A 71  ? 0.3078 0.3985 0.4127 -0.0510 0.0252  0.0194  1864 LEU A N   
565 C CA  . LEU A 71  ? 0.3093 0.3870 0.3954 -0.0506 0.0302  0.0070  1864 LEU A CA  
566 C C   . LEU A 71  ? 0.3239 0.4111 0.3892 -0.0546 0.0175  -0.0031 1864 LEU A C   
567 O O   . LEU A 71  ? 0.3561 0.4424 0.4133 -0.0534 0.0152  -0.0079 1864 LEU A O   
568 C CB  . LEU A 71  ? 0.3369 0.3892 0.4098 -0.0517 0.0454  -0.0002 1864 LEU A CB  
569 C CG  . LEU A 71  ? 0.3884 0.4246 0.4361 -0.0543 0.0506  -0.0124 1864 LEU A CG  
570 C CD1 . LEU A 71  ? 0.2966 0.3304 0.3543 -0.0484 0.0574  -0.0086 1864 LEU A CD1 
571 C CD2 . LEU A 71  ? 0.4364 0.4447 0.4669 -0.0590 0.0650  -0.0192 1864 LEU A CD2 
572 N N   . VAL A 72  ? 0.3193 0.4155 0.3776 -0.0586 0.0105  -0.0050 1865 VAL A N   
573 C CA  . VAL A 72  ? 0.3481 0.4555 0.3921 -0.0602 0.0008  -0.0121 1865 VAL A CA  
574 C C   . VAL A 72  ? 0.3233 0.4384 0.3700 -0.0581 -0.0060 -0.0106 1865 VAL A C   
575 O O   . VAL A 72  ? 0.3378 0.4513 0.3745 -0.0561 -0.0082 -0.0168 1865 VAL A O   
576 C CB  . VAL A 72  ? 0.2794 0.3982 0.3209 -0.0643 -0.0039 -0.0113 1865 VAL A CB  
577 C CG1 . VAL A 72  ? 0.2923 0.4232 0.3233 -0.0637 -0.0105 -0.0170 1865 VAL A CG1 
578 C CG2 . VAL A 72  ? 0.3216 0.4312 0.3580 -0.0691 0.0019  -0.0135 1865 VAL A CG2 
579 N N   . PHE A 73  ? 0.3091 0.4316 0.3687 -0.0596 -0.0100 -0.0012 1866 PHE A N   
580 C CA  . PHE A 73  ? 0.2831 0.4114 0.3402 -0.0619 -0.0184 -0.0003 1866 PHE A CA  
581 C C   . PHE A 73  ? 0.2951 0.4174 0.3610 -0.0600 -0.0162 0.0023  1866 PHE A C   
582 O O   . PHE A 73  ? 0.3535 0.4743 0.4111 -0.0618 -0.0214 -0.0012 1866 PHE A O   
583 C CB  . PHE A 73  ? 0.2733 0.4137 0.3369 -0.0681 -0.0264 0.0099  1866 PHE A CB  
584 C CG  . PHE A 73  ? 0.3437 0.4899 0.3993 -0.0704 -0.0271 0.0088  1866 PHE A CG  
585 C CD1 . PHE A 73  ? 0.3693 0.5154 0.4068 -0.0693 -0.0261 -0.0025 1866 PHE A CD1 
586 C CD2 . PHE A 73  ? 0.3570 0.5095 0.4258 -0.0729 -0.0276 0.0207  1866 PHE A CD2 
587 C CE1 . PHE A 73  ? 0.3685 0.5219 0.4008 -0.0717 -0.0256 -0.0025 1866 PHE A CE1 
588 C CE2 . PHE A 73  ? 0.3925 0.5498 0.4536 -0.0757 -0.0278 0.0201  1866 PHE A CE2 
589 C CZ  . PHE A 73  ? 0.2963 0.4547 0.3389 -0.0756 -0.0267 0.0082  1866 PHE A CZ  
590 N N   . ASP A 74  ? 0.3236 0.4405 0.4055 -0.0564 -0.0069 0.0084  1867 ASP A N   
591 C CA  . ASP A 74  ? 0.4283 0.5385 0.5174 -0.0539 -0.0015 0.0100  1867 ASP A CA  
592 C C   . ASP A 74  ? 0.4329 0.5310 0.5007 -0.0516 0.0014  -0.0023 1867 ASP A C   
593 O O   . ASP A 74  ? 0.3484 0.4438 0.4126 -0.0519 -0.0013 -0.0038 1867 ASP A O   
594 C CB  . ASP A 74  ? 0.3795 0.4844 0.4899 -0.0492 0.0122  0.0191  1867 ASP A CB  
595 C CG  . ASP A 74  ? 0.5372 0.6579 0.6776 -0.0502 0.0087  0.0371  1867 ASP A CG  
596 O OD1 . ASP A 74  ? 0.5356 0.6714 0.6791 -0.0570 -0.0060 0.0432  1867 ASP A OD1 
597 O OD2 . ASP A 74  ? 0.5454 0.6622 0.7058 -0.0447 0.0211  0.0460  1867 ASP A OD2 
598 N N   . ASN A 75  ? 0.3341 0.4249 0.3879 -0.0506 0.0061  -0.0099 1868 ASN A N   
599 C CA  . ASN A 75  ? 0.2806 0.3647 0.3151 -0.0499 0.0054  -0.0186 1868 ASN A CA  
600 C C   . ASN A 75  ? 0.3876 0.4789 0.4153 -0.0492 -0.0044 -0.0218 1868 ASN A C   
601 O O   . ASN A 75  ? 0.2795 0.3651 0.3004 -0.0472 -0.0053 -0.0241 1868 ASN A O   
602 C CB  . ASN A 75  ? 0.3362 0.4166 0.3573 -0.0523 0.0077  -0.0240 1868 ASN A CB  
603 C CG  . ASN A 75  ? 0.4030 0.4667 0.4220 -0.0540 0.0205  -0.0241 1868 ASN A CG  
604 O OD1 . ASN A 75  ? 0.3655 0.4206 0.3926 -0.0512 0.0293  -0.0205 1868 ASN A OD1 
605 N ND2 . ASN A 75  ? 0.4319 0.4894 0.4397 -0.0590 0.0229  -0.0281 1868 ASN A ND2 
606 N N   . CYS A 76  ? 0.2896 0.3912 0.3179 -0.0509 -0.0102 -0.0218 1869 CYS A N   
607 C CA  . CYS A 76  ? 0.2789 0.3831 0.2978 -0.0498 -0.0157 -0.0263 1869 CYS A CA  
608 C C   . CYS A 76  ? 0.3499 0.4469 0.3689 -0.0515 -0.0184 -0.0251 1869 CYS A C   
609 O O   . CYS A 76  ? 0.3472 0.4360 0.3571 -0.0485 -0.0184 -0.0296 1869 CYS A O   
610 C CB  . CYS A 76  ? 0.3015 0.4159 0.3187 -0.0529 -0.0191 -0.0261 1869 CYS A CB  
611 S SG  . CYS A 76  ? 0.3926 0.5049 0.3945 -0.0512 -0.0207 -0.0330 1869 CYS A SG  
612 N N   . GLN A 77  ? 0.2687 0.3689 0.2998 -0.0568 -0.0208 -0.0176 1870 GLN A N   
613 C CA  . GLN A 77  ? 0.2996 0.3946 0.3319 -0.0616 -0.0250 -0.0150 1870 GLN A CA  
614 C C   . GLN A 77  ? 0.3500 0.4359 0.3866 -0.0582 -0.0194 -0.0141 1870 GLN A C   
615 O O   . GLN A 77  ? 0.3700 0.4479 0.4029 -0.0614 -0.0221 -0.0143 1870 GLN A O   
616 C CB  . GLN A 77  ? 0.2845 0.3908 0.3328 -0.0699 -0.0312 -0.0035 1870 GLN A CB  
617 C CG  . GLN A 77  ? 0.2736 0.3878 0.3131 -0.0761 -0.0386 -0.0032 1870 GLN A CG  
618 C CD  . GLN A 77  ? 0.3378 0.4665 0.3957 -0.0847 -0.0465 0.0121  1870 GLN A CD  
619 O OE1 . GLN A 77  ? 0.3643 0.4949 0.4203 -0.0958 -0.0564 0.0171  1870 GLN A OE1 
620 N NE2 . GLN A 77  ? 0.2526 0.3914 0.3291 -0.0806 -0.0426 0.0209  1870 GLN A NE2 
621 N N   . THR A 78  ? 0.3130 0.3976 0.3545 -0.0532 -0.0110 -0.0131 1871 THR A N   
622 C CA  . THR A 78  ? 0.3874 0.4619 0.4283 -0.0508 -0.0044 -0.0124 1871 THR A CA  
623 C C   . THR A 78  ? 0.4016 0.4671 0.4243 -0.0473 -0.0060 -0.0194 1871 THR A C   
624 O O   . THR A 78  ? 0.3921 0.4484 0.4121 -0.0474 -0.0054 -0.0184 1871 THR A O   
625 C CB  . THR A 78  ? 0.3009 0.3720 0.3460 -0.0481 0.0069  -0.0106 1871 THR A CB  
626 O OG1 . THR A 78  ? 0.3184 0.3967 0.3871 -0.0492 0.0110  -0.0006 1871 THR A OG1 
627 C CG2 . THR A 78  ? 0.2517 0.3094 0.2867 -0.0465 0.0149  -0.0120 1871 THR A CG2 
628 N N   . PHE A 79  ? 0.4129 0.4820 0.4257 -0.0442 -0.0080 -0.0247 1872 PHE A N   
629 C CA  . PHE A 79  ? 0.3882 0.4523 0.3893 -0.0394 -0.0089 -0.0276 1872 PHE A CA  
630 C C   . PHE A 79  ? 0.4497 0.5109 0.4461 -0.0363 -0.0125 -0.0310 1872 PHE A C   
631 O O   . PHE A 79  ? 0.3915 0.4442 0.3827 -0.0315 -0.0119 -0.0308 1872 PHE A O   
632 C CB  . PHE A 79  ? 0.3965 0.4680 0.3918 -0.0382 -0.0089 -0.0288 1872 PHE A CB  
633 C CG  . PHE A 79  ? 0.4751 0.5448 0.4617 -0.0346 -0.0108 -0.0272 1872 PHE A CG  
634 C CD1 . PHE A 79  ? 0.3879 0.4494 0.3652 -0.0375 -0.0083 -0.0246 1872 PHE A CD1 
635 C CD2 . PHE A 79  ? 0.4996 0.5752 0.4875 -0.0283 -0.0142 -0.0268 1872 PHE A CD2 
636 C CE1 . PHE A 79  ? 0.4447 0.5063 0.4138 -0.0355 -0.0121 -0.0203 1872 PHE A CE1 
637 C CE2 . PHE A 79  ? 0.4947 0.5714 0.4796 -0.0241 -0.0167 -0.0215 1872 PHE A CE2 
638 C CZ  . PHE A 79  ? 0.4705 0.5412 0.4457 -0.0284 -0.0171 -0.0176 1872 PHE A CZ  
639 N N   . ASN A 80  ? 0.5440 0.4833 0.4328 0.0028  -0.0570 -0.0160 1873 ASN A N   
640 C CA  . ASN A 80  ? 0.5239 0.4724 0.4376 0.0177  -0.0757 -0.0278 1873 ASN A CA  
641 C C   . ASN A 80  ? 0.5439 0.4837 0.4781 0.0103  -0.0684 -0.0281 1873 ASN A C   
642 O O   . ASN A 80  ? 0.4115 0.3680 0.3620 -0.0048 -0.0505 -0.0249 1873 ASN A O   
643 C CB  . ASN A 80  ? 0.4737 0.4763 0.4178 0.0259  -0.0812 -0.0455 1873 ASN A CB  
644 C CG  . ASN A 80  ? 0.4751 0.4902 0.4046 0.0279  -0.0899 -0.0457 1873 ASN A CG  
645 O OD1 . ASN A 80  ? 0.4867 0.4972 0.4102 0.0427  -0.1120 -0.0475 1873 ASN A OD1 
646 N ND2 . ASN A 80  ? 0.4976 0.5247 0.4209 0.0130  -0.0748 -0.0437 1873 ASN A ND2 
647 N N   . GLU A 81  ? 0.4674 0.3785 0.4012 0.0214  -0.0848 -0.0319 1874 GLU A N   
648 C CA  . GLU A 81  ? 0.4856 0.3854 0.4376 0.0139  -0.0836 -0.0369 1874 GLU A CA  
649 C C   . GLU A 81  ? 0.4600 0.4108 0.4429 0.0149  -0.0799 -0.0558 1874 GLU A C   
650 O O   . GLU A 81  ? 0.4565 0.4432 0.4485 0.0287  -0.0840 -0.0693 1874 GLU A O   
651 C CB  . GLU A 81  ? 0.5947 0.4478 0.5376 0.0292  -0.1045 -0.0417 1874 GLU A CB  
652 C CG  . GLU A 81  ? 0.9255 0.7252 0.8314 0.0331  -0.1144 -0.0216 1874 GLU A CG  
653 C CD  . GLU A 81  ? 1.2011 0.9557 1.0881 0.0077  -0.1021 0.0010  1874 GLU A CD  
654 O OE1 . GLU A 81  ? 1.3190 1.0162 1.1717 0.0087  -0.1122 0.0186  1874 GLU A OE1 
655 O OE2 . GLU A 81  ? 1.2495 1.0272 1.1578 -0.0138 -0.0829 0.0028  1874 GLU A OE2 
656 N N   . ASP A 82  ? 0.4290 0.3840 0.4275 -0.0017 -0.0729 -0.0554 1875 ASP A N   
657 C CA  . ASP A 82  ? 0.5490 0.5457 0.5677 -0.0030 -0.0720 -0.0709 1875 ASP A CA  
658 C C   . ASP A 82  ? 0.5400 0.5406 0.5581 0.0167  -0.0848 -0.0952 1875 ASP A C   
659 O O   . ASP A 82  ? 0.5516 0.5939 0.5780 0.0203  -0.0812 -0.1090 1875 ASP A O   
660 C CB  . ASP A 82  ? 0.3803 0.3745 0.4144 -0.0239 -0.0697 -0.0658 1875 ASP A CB  
661 C CG  . ASP A 82  ? 0.4566 0.4598 0.5023 -0.0404 -0.0526 -0.0439 1875 ASP A CG  
662 O OD1 . ASP A 82  ? 0.4202 0.4503 0.4665 -0.0374 -0.0412 -0.0392 1875 ASP A OD1 
663 O OD2 . ASP A 82  ? 0.4070 0.3901 0.4627 -0.0565 -0.0495 -0.0321 1875 ASP A OD2 
664 N N   . ASP A 83  ? 0.5743 0.5306 0.5816 0.0301  -0.0983 -0.1007 1876 ASP A N   
665 C CA  . ASP A 83  ? 0.6257 0.5824 0.6353 0.0538  -0.1086 -0.1267 1876 ASP A CA  
666 C C   . ASP A 83  ? 0.6468 0.6156 0.6603 0.0799  -0.1151 -0.1304 1876 ASP A C   
667 O O   . ASP A 83  ? 0.6911 0.6599 0.7125 0.1049  -0.1233 -0.1516 1876 ASP A O   
668 C CB  . ASP A 83  ? 0.8000 0.6958 0.7992 0.0551  -0.1224 -0.1350 1876 ASP A CB  
669 C CG  . ASP A 83  ? 0.9295 0.7653 0.9133 0.0560  -0.1322 -0.1147 1876 ASP A CG  
670 O OD1 . ASP A 83  ? 0.9729 0.8149 0.9495 0.0543  -0.1277 -0.0940 1876 ASP A OD1 
671 O OD2 . ASP A 83  ? 1.0312 0.8085 1.0051 0.0572  -0.1451 -0.1194 1876 ASP A OD2 
672 N N   . SER A 84  ? 0.5841 0.5641 0.5935 0.0755  -0.1125 -0.1116 1877 SER A N   
673 C CA  . SER A 84  ? 0.5470 0.5496 0.5650 0.0970  -0.1220 -0.1151 1877 SER A CA  
674 C C   . SER A 84  ? 0.4363 0.5096 0.4805 0.0999  -0.1112 -0.1311 1877 SER A C   
675 O O   . SER A 84  ? 0.4696 0.5699 0.5167 0.0825  -0.0958 -0.1336 1877 SER A O   
676 C CB  . SER A 84  ? 0.5162 0.5043 0.5135 0.0881  -0.1251 -0.0915 1877 SER A CB  
677 O OG  . SER A 84  ? 0.4549 0.4733 0.4518 0.0657  -0.1070 -0.0837 1877 SER A OG  
678 N N   . GLU A 85  ? 0.4967 0.6015 0.5618 0.1213  -0.1203 -0.1400 1878 GLU A N   
679 C CA  . GLU A 85  ? 0.4291 0.6056 0.5233 0.1214  -0.1083 -0.1532 1878 GLU A CA  
680 C C   . GLU A 85  ? 0.4933 0.6936 0.5811 0.0931  -0.0965 -0.1374 1878 GLU A C   
681 O O   . GLU A 85  ? 0.4537 0.6908 0.5487 0.0789  -0.0798 -0.1417 1878 GLU A O   
682 C CB  . GLU A 85  ? 0.5018 0.7115 0.6284 0.1487  -0.1223 -0.1633 1878 GLU A CB  
683 C CG  . GLU A 85  ? 0.6366 0.9174 0.8027 0.1603  -0.1081 -0.1869 1878 GLU A CG  
684 C CD  . GLU A 85  ? 0.8720 1.1440 1.0307 0.1687  -0.0940 -0.2088 1878 GLU A CD  
685 O OE1 . GLU A 85  ? 0.8792 1.1896 1.0364 0.1529  -0.0724 -0.2162 1878 GLU A OE1 
686 O OE2 . GLU A 85  ? 0.9895 1.2118 1.1394 0.1901  -0.1057 -0.2186 1878 GLU A OE2 
687 N N   . VAL A 86  ? 0.3997 0.5735 0.4687 0.0847  -0.1050 -0.1189 1879 VAL A N   
688 C CA  . VAL A 86  ? 0.3492 0.5364 0.4094 0.0604  -0.0939 -0.1067 1879 VAL A CA  
689 C C   . VAL A 86  ? 0.3744 0.5412 0.4199 0.0419  -0.0775 -0.0984 1879 VAL A C   
690 O O   . VAL A 86  ? 0.3041 0.4963 0.3551 0.0260  -0.0641 -0.0957 1879 VAL A O   
691 C CB  . VAL A 86  ? 0.3994 0.5595 0.4359 0.0576  -0.1069 -0.0928 1879 VAL A CB  
692 C CG1 . VAL A 86  ? 0.3390 0.4950 0.3577 0.0331  -0.0924 -0.0819 1879 VAL A CG1 
693 C CG2 . VAL A 86  ? 0.3562 0.5516 0.4155 0.0719  -0.1266 -0.1004 1879 VAL A CG2 
694 N N   . GLY A 87  ? 0.3953 0.5167 0.4253 0.0433  -0.0798 -0.0931 1880 GLY A N   
695 C CA  . GLY A 87  ? 0.4223 0.5313 0.4482 0.0262  -0.0671 -0.0854 1880 GLY A CA  
696 C C   . GLY A 87  ? 0.4978 0.6407 0.5387 0.0227  -0.0608 -0.0976 1880 GLY A C   
697 O O   . GLY A 87  ? 0.3194 0.4773 0.3633 0.0071  -0.0506 -0.0900 1880 GLY A O   
698 N N   . LYS A 88  ? 0.4409 0.5944 0.4887 0.0384  -0.0669 -0.1170 1881 LYS A N   
699 C CA  . LYS A 88  ? 0.4478 0.6330 0.4995 0.0345  -0.0593 -0.1301 1881 LYS A CA  
700 C C   . LYS A 88  ? 0.4275 0.6607 0.4877 0.0240  -0.0473 -0.1256 1881 LYS A C   
701 O O   . LYS A 88  ? 0.3493 0.5967 0.4040 0.0088  -0.0397 -0.1202 1881 LYS A O   
702 C CB  . LYS A 88  ? 0.4564 0.6454 0.5112 0.0562  -0.0638 -0.1556 1881 LYS A CB  
703 C CG  . LYS A 88  ? 0.4837 0.6185 0.5257 0.0623  -0.0759 -0.1627 1881 LYS A CG  
704 C CD  . LYS A 88  ? 0.5492 0.6841 0.5917 0.0858  -0.0785 -0.1922 1881 LYS A CD  
705 C CE  . LYS A 88  ? 0.6502 0.7835 0.7105 0.1147  -0.0868 -0.1993 1881 LYS A CE  
706 N NZ  . LYS A 88  ? 0.7584 0.8853 0.8213 0.1416  -0.0880 -0.2310 1881 LYS A NZ  
707 N N   . ALA A 89  ? 0.3160 0.5726 0.3898 0.0301  -0.0479 -0.1261 1882 ALA A N   
708 C CA  . ALA A 89  ? 0.3544 0.6534 0.4378 0.0159  -0.0371 -0.1213 1882 ALA A CA  
709 C C   . ALA A 89  ? 0.4019 0.6816 0.4735 -0.0044 -0.0324 -0.1007 1882 ALA A C   
710 O O   . ALA A 89  ? 0.3731 0.6727 0.4438 -0.0196 -0.0229 -0.0938 1882 ALA A O   
711 C CB  . ALA A 89  ? 0.3167 0.6449 0.4220 0.0238  -0.0427 -0.1260 1882 ALA A CB  
712 N N   . GLY A 90  ? 0.3137 0.5525 0.3747 -0.0041 -0.0377 -0.0904 1883 GLY A N   
713 C CA  . GLY A 90  ? 0.3107 0.5312 0.3640 -0.0188 -0.0303 -0.0739 1883 GLY A CA  
714 C C   . GLY A 90  ? 0.3084 0.5269 0.3630 -0.0271 -0.0252 -0.0668 1883 GLY A C   
715 O O   . GLY A 90  ? 0.2623 0.4815 0.3185 -0.0380 -0.0185 -0.0545 1883 GLY A O   
716 N N   . HIS A 91  ? 0.2783 0.4911 0.3324 -0.0218 -0.0310 -0.0743 1884 HIS A N   
717 C CA  . HIS A 91  ? 0.3573 0.5721 0.4129 -0.0312 -0.0317 -0.0682 1884 HIS A CA  
718 C C   . HIS A 91  ? 0.3104 0.5584 0.3604 -0.0381 -0.0284 -0.0696 1884 HIS A C   
719 O O   . HIS A 91  ? 0.2492 0.5009 0.2993 -0.0487 -0.0280 -0.0556 1884 HIS A O   
720 C CB  . HIS A 91  ? 0.3705 0.5669 0.4236 -0.0272 -0.0417 -0.0780 1884 HIS A CB  
721 C CG  . HIS A 91  ? 0.3634 0.5255 0.4224 -0.0284 -0.0431 -0.0690 1884 HIS A CG  
722 N ND1 . HIS A 91  ? 0.3574 0.5141 0.4298 -0.0382 -0.0359 -0.0512 1884 HIS A ND1 
723 C CD2 . HIS A 91  ? 0.3335 0.4643 0.3867 -0.0213 -0.0489 -0.0739 1884 HIS A CD2 
724 C CE1 . HIS A 91  ? 0.3680 0.4958 0.4419 -0.0392 -0.0344 -0.0458 1884 HIS A CE1 
725 N NE2 . HIS A 91  ? 0.4288 0.5371 0.4885 -0.0303 -0.0435 -0.0579 1884 HIS A NE2 
726 N N   . ILE A 92  ? 0.2460 0.5191 0.2919 -0.0318 -0.0253 -0.0850 1885 ILE A N   
727 C CA  . ILE A 92  ? 0.3920 0.6990 0.4292 -0.0413 -0.0172 -0.0846 1885 ILE A CA  
728 C C   . ILE A 92  ? 0.3932 0.7040 0.4352 -0.0554 -0.0108 -0.0653 1885 ILE A C   
729 O O   . ILE A 92  ? 0.2763 0.5914 0.3079 -0.0683 -0.0090 -0.0513 1885 ILE A O   
730 C CB  . ILE A 92  ? 0.3473 0.6872 0.3877 -0.0307 -0.0102 -0.1057 1885 ILE A CB  
731 C CG1 . ILE A 92  ? 0.4151 0.7434 0.4452 -0.0156 -0.0162 -0.1272 1885 ILE A CG1 
732 C CG2 . ILE A 92  ? 0.4153 0.7944 0.4472 -0.0445 0.0037  -0.1025 1885 ILE A CG2 
733 C CD1 . ILE A 92  ? 0.4330 0.7885 0.4742 0.0032  -0.0095 -0.1512 1885 ILE A CD1 
734 N N   . MET A 93  ? 0.3066 0.6106 0.3609 -0.0535 -0.0096 -0.0641 1886 MET A N   
735 C CA  . MET A 93  ? 0.3197 0.6200 0.3757 -0.0676 -0.0046 -0.0494 1886 MET A CA  
736 C C   . MET A 93  ? 0.3082 0.5756 0.3615 -0.0712 -0.0058 -0.0323 1886 MET A C   
737 O O   . MET A 93  ? 0.3736 0.6362 0.4239 -0.0828 -0.0027 -0.0177 1886 MET A O   
738 C CB  . MET A 93  ? 0.2991 0.5964 0.3637 -0.0656 -0.0065 -0.0551 1886 MET A CB  
739 C CG  . MET A 93  ? 0.3201 0.6595 0.3995 -0.0628 -0.0064 -0.0696 1886 MET A CG  
740 S SD  . MET A 93  ? 0.4211 0.8056 0.5042 -0.0833 0.0075  -0.0647 1886 MET A SD  
741 C CE  . MET A 93  ? 0.3915 0.7479 0.4702 -0.1059 0.0075  -0.0456 1886 MET A CE  
742 N N   . ARG A 94  ? 0.3294 0.5745 0.3868 -0.0613 -0.0098 -0.0329 1887 ARG A N   
743 C CA  . ARG A 94  ? 0.2958 0.5180 0.3612 -0.0621 -0.0086 -0.0179 1887 ARG A CA  
744 C C   . ARG A 94  ? 0.3065 0.5402 0.3729 -0.0677 -0.0151 -0.0069 1887 ARG A C   
745 O O   . ARG A 94  ? 0.3189 0.5428 0.3917 -0.0711 -0.0148 0.0095  1887 ARG A O   
746 C CB  . ARG A 94  ? 0.2178 0.4201 0.2911 -0.0532 -0.0086 -0.0207 1887 ARG A CB  
747 C CG  . ARG A 94  ? 0.2461 0.4338 0.3378 -0.0524 -0.0036 -0.0067 1887 ARG A CG  
748 C CD  . ARG A 94  ? 0.2767 0.4526 0.3789 -0.0485 -0.0018 -0.0082 1887 ARG A CD  
749 N NE  . ARG A 94  ? 0.2873 0.4714 0.3866 -0.0494 -0.0147 -0.0176 1887 ARG A NE  
750 C CZ  . ARG A 94  ? 0.3496 0.5485 0.4589 -0.0544 -0.0266 -0.0159 1887 ARG A CZ  
751 N NH1 . ARG A 94  ? 0.2756 0.4867 0.4023 -0.0579 -0.0296 -0.0019 1887 ARG A NH1 
752 N NH2 . ARG A 94  ? 0.2396 0.4382 0.3398 -0.0550 -0.0380 -0.0288 1887 ARG A NH2 
753 N N   . ARG A 95  ? 0.3139 0.5646 0.3714 -0.0675 -0.0229 -0.0160 1888 ARG A N   
754 C CA  . ARG A 95  ? 0.3171 0.5781 0.3656 -0.0745 -0.0327 -0.0061 1888 ARG A CA  
755 C C   . ARG A 95  ? 0.3606 0.6323 0.3911 -0.0858 -0.0278 0.0053  1888 ARG A C   
756 O O   . ARG A 95  ? 0.3992 0.6652 0.4257 -0.0917 -0.0352 0.0248  1888 ARG A O   
757 C CB  . ARG A 95  ? 0.2936 0.5654 0.3269 -0.0730 -0.0418 -0.0228 1888 ARG A CB  
758 C CG  . ARG A 95  ? 0.3034 0.5601 0.3544 -0.0689 -0.0529 -0.0267 1888 ARG A CG  
759 C CD  . ARG A 95  ? 0.2846 0.5451 0.3142 -0.0705 -0.0657 -0.0443 1888 ARG A CD  
760 N NE  . ARG A 95  ? 0.3266 0.5917 0.3380 -0.0620 -0.0566 -0.0674 1888 ARG A NE  
761 C CZ  . ARG A 95  ? 0.3848 0.6327 0.4032 -0.0514 -0.0566 -0.0833 1888 ARG A CZ  
762 N NH1 . ARG A 95  ? 0.3105 0.5333 0.3488 -0.0520 -0.0634 -0.0778 1888 ARG A NH1 
763 N NH2 . ARG A 95  ? 0.3036 0.5597 0.3110 -0.0399 -0.0494 -0.1035 1888 ARG A NH2 
764 N N   . PHE A 96  ? 0.3029 0.5906 0.3249 -0.0897 -0.0163 -0.0049 1889 PHE A N   
765 C CA  . PHE A 96  ? 0.3145 0.6118 0.3228 -0.1053 -0.0089 0.0080  1889 PHE A CA  
766 C C   . PHE A 96  ? 0.3510 0.6173 0.3694 -0.1097 -0.0098 0.0284  1889 PHE A C   
767 O O   . PHE A 96  ? 0.4130 0.6695 0.4190 -0.1191 -0.0141 0.0492  1889 PHE A O   
768 C CB  . PHE A 96  ? 0.2711 0.5958 0.2830 -0.1096 0.0041  -0.0066 1889 PHE A CB  
769 C CG  . PHE A 96  ? 0.4994 0.8369 0.5009 -0.1308 0.0139  0.0075  1889 PHE A CG  
770 C CD1 . PHE A 96  ? 0.5388 0.9032 0.5144 -0.1423 0.0212  0.0109  1889 PHE A CD1 
771 C CD2 . PHE A 96  ? 0.4614 0.7804 0.4747 -0.1415 0.0162  0.0175  1889 PHE A CD2 
772 C CE1 . PHE A 96  ? 0.5331 0.9080 0.4974 -0.1657 0.0323  0.0272  1889 PHE A CE1 
773 C CE2 . PHE A 96  ? 0.5155 0.8416 0.5199 -0.1651 0.0243  0.0322  1889 PHE A CE2 
774 C CZ  . PHE A 96  ? 0.5272 0.8825 0.5084 -0.1780 0.0332  0.0388  1889 PHE A CZ  
775 N N   . PHE A 97  ? 0.3213 0.5676 0.3580 -0.1021 -0.0061 0.0226  1890 PHE A N   
776 C CA  . PHE A 97  ? 0.3663 0.5782 0.4097 -0.1042 -0.0042 0.0366  1890 PHE A CA  
777 C C   . PHE A 97  ? 0.4027 0.5967 0.4565 -0.0957 -0.0127 0.0539  1890 PHE A C   
778 O O   . PHE A 97  ? 0.4186 0.5915 0.4697 -0.1003 -0.0158 0.0729  1890 PHE A O   
779 C CB  . PHE A 97  ? 0.3756 0.5675 0.4282 -0.0964 0.0020  0.0238  1890 PHE A CB  
780 C CG  . PHE A 97  ? 0.4215 0.5720 0.4783 -0.0941 0.0059  0.0334  1890 PHE A CG  
781 C CD1 . PHE A 97  ? 0.4713 0.6015 0.5177 -0.1087 0.0079  0.0392  1890 PHE A CD1 
782 C CD2 . PHE A 97  ? 0.4227 0.5547 0.4959 -0.0779 0.0086  0.0363  1890 PHE A CD2 
783 C CE1 . PHE A 97  ? 0.4649 0.5493 0.5124 -0.1047 0.0114  0.0454  1890 PHE A CE1 
784 C CE2 . PHE A 97  ? 0.5058 0.5995 0.5845 -0.0717 0.0151  0.0424  1890 PHE A CE2 
785 C CZ  . PHE A 97  ? 0.4300 0.4960 0.4934 -0.0839 0.0159  0.0459  1890 PHE A CZ  
786 N N   . GLU A 98  ? 0.3623 0.5636 0.4323 -0.0832 -0.0178 0.0484  1891 GLU A N   
787 C CA  . GLU A 98  ? 0.4088 0.6034 0.5004 -0.0745 -0.0278 0.0640  1891 GLU A CA  
788 C C   . GLU A 98  ? 0.4339 0.6359 0.5087 -0.0830 -0.0431 0.0827  1891 GLU A C   
789 O O   . GLU A 98  ? 0.5218 0.7060 0.6071 -0.0791 -0.0509 0.1034  1891 GLU A O   
790 C CB  . GLU A 98  ? 0.4342 0.6433 0.5469 -0.0662 -0.0323 0.0546  1891 GLU A CB  
791 C CG  . GLU A 98  ? 0.5348 0.7300 0.6682 -0.0562 -0.0175 0.0453  1891 GLU A CG  
792 C CD  . GLU A 98  ? 0.6012 0.8098 0.7564 -0.0530 -0.0217 0.0397  1891 GLU A CD  
793 O OE1 . GLU A 98  ? 0.6436 0.8700 0.8117 -0.0558 -0.0387 0.0466  1891 GLU A OE1 
794 O OE2 . GLU A 98  ? 0.5813 0.7803 0.7380 -0.0498 -0.0097 0.0293  1891 GLU A OE2 
795 N N   . SER A 99  ? 0.4502 0.6759 0.4959 -0.0935 -0.0476 0.0759  1892 SER A N   
796 C CA  . SER A 99  ? 0.5419 0.7733 0.5603 -0.1031 -0.0624 0.0940  1892 SER A CA  
797 C C   . SER A 99  ? 0.5876 0.8004 0.5851 -0.1158 -0.0565 0.1132  1892 SER A C   
798 O O   . SER A 99  ? 0.6827 0.8809 0.6676 -0.1194 -0.0707 0.1388  1892 SER A O   
799 C CB  . SER A 99  ? 0.5206 0.7797 0.5060 -0.1108 -0.0647 0.0779  1892 SER A CB  
800 O OG  . SER A 99  ? 0.6509 0.9238 0.6162 -0.1199 -0.0453 0.0652  1892 SER A OG  
801 N N   . ARG A 100 ? 0.5188 0.7303 0.5134 -0.1239 -0.0379 0.1027  1893 ARG A N   
802 C CA  . ARG A 100 ? 0.6578 0.8495 0.6352 -0.1408 -0.0318 0.1203  1893 ARG A CA  
803 C C   . ARG A 100 ? 0.6033 0.7488 0.6015 -0.1319 -0.0367 0.1366  1893 ARG A C   
804 O O   . ARG A 100 ? 0.5675 0.6853 0.5510 -0.1394 -0.0449 0.1627  1893 ARG A O   
805 C CB  . ARG A 100 ? 0.6104 0.8197 0.5866 -0.1536 -0.0132 0.1024  1893 ARG A CB  
806 C CG  . ARG A 100 ? 0.6298 0.8298 0.5874 -0.1790 -0.0053 0.1189  1893 ARG A CG  
807 C CD  . ARG A 100 ? 0.6819 0.9064 0.6014 -0.1961 -0.0035 0.1328  1893 ARG A CD  
808 N NE  . ARG A 100 ? 0.6568 0.8780 0.5609 -0.2252 0.0089  0.1482  1893 ARG A NE  
809 C CZ  . ARG A 100 ? 0.8128 1.0006 0.6890 -0.2418 0.0032  0.1807  1893 ARG A CZ  
810 N NH1 . ARG A 100 ? 0.8852 1.0431 0.7469 -0.2290 -0.0172 0.2014  1893 ARG A NH1 
811 N NH2 . ARG A 100 ? 0.8054 0.9906 0.6700 -0.2722 0.0165  0.1942  1893 ARG A NH2 
812 N N   . TRP A 101 ? 0.6365 0.7700 0.6663 -0.1145 -0.0314 0.1217  1894 TRP A N   
813 C CA  . TRP A 101 ? 0.7083 0.7991 0.7600 -0.1006 -0.0331 0.1328  1894 TRP A CA  
814 C C   . TRP A 101 ? 0.8368 0.9219 0.9004 -0.0887 -0.0528 0.1574  1894 TRP A C   
815 O O   . TRP A 101 ? 0.8224 0.8682 0.8940 -0.0816 -0.0585 0.1761  1894 TRP A O   
816 C CB  . TRP A 101 ? 0.7248 0.8116 0.8047 -0.0827 -0.0213 0.1114  1894 TRP A CB  
817 C CG  . TRP A 101 ? 0.7529 0.8025 0.8600 -0.0628 -0.0190 0.1186  1894 TRP A CG  
818 C CD1 . TRP A 101 ? 0.8101 0.8659 0.9526 -0.0427 -0.0279 0.1303  1894 TRP A CD1 
819 C CD2 . TRP A 101 ? 0.7571 0.7590 0.8610 -0.0597 -0.0068 0.1125  1894 TRP A CD2 
820 N NE1 . TRP A 101 ? 0.8867 0.9043 1.0517 -0.0244 -0.0190 0.1317  1894 TRP A NE1 
821 C CE2 . TRP A 101 ? 0.8745 0.8541 1.0118 -0.0344 -0.0057 0.1196  1894 TRP A CE2 
822 C CE3 . TRP A 101 ? 0.7836 0.7600 0.8612 -0.0763 0.0021  0.1003  1894 TRP A CE3 
823 C CZ2 . TRP A 101 ? 0.8949 0.8224 1.0342 -0.0232 0.0068  0.1127  1894 TRP A CZ2 
824 C CZ3 . TRP A 101 ? 0.8671 0.7896 0.9435 -0.0688 0.0108  0.0940  1894 TRP A CZ3 
825 C CH2 . TRP A 101 ? 0.9231 0.8189 1.0274 -0.0414 0.0145  0.0991  1894 TRP A CH2 
826 N N   . GLU A 102 ? 0.8806 1.0021 0.9461 -0.0859 -0.0660 0.1573  1895 GLU A N   
827 C CA  . GLU A 102 ? 0.8764 0.9989 0.9603 -0.0736 -0.0897 0.1792  1895 GLU A CA  
828 C C   . GLU A 102 ? 0.9279 1.0383 0.9706 -0.0879 -0.1077 0.2077  1895 GLU A C   
829 O O   . GLU A 102 ? 1.0545 1.1461 1.1103 -0.0767 -0.1285 0.2335  1895 GLU A O   
830 C CB  . GLU A 102 ? 0.8955 1.0591 0.9990 -0.0676 -0.1001 0.1669  1895 GLU A CB  
831 C CG  . GLU A 102 ? 1.0280 1.1968 1.1907 -0.0464 -0.0938 0.1582  1895 GLU A CG  
832 C CD  . GLU A 102 ? 1.0986 1.3008 1.2751 -0.0480 -0.0909 0.1364  1895 GLU A CD  
833 O OE1 . GLU A 102 ? 1.1379 1.3649 1.3074 -0.0549 -0.1118 0.1380  1895 GLU A OE1 
834 O OE2 . GLU A 102 ? 1.0600 1.2587 1.2497 -0.0434 -0.0691 0.1179  1895 GLU A OE2 
835 N N   . GLU A 103 ? 0.9456 1.0670 0.9392 -0.1117 -0.0999 0.2051  1896 GLU A N   
836 C CA  . GLU A 103 ? 1.0292 1.1340 0.9759 -0.1288 -0.1121 0.2350  1896 GLU A CA  
837 C C   . GLU A 103 ? 1.0996 1.1554 1.0388 -0.1381 -0.1034 0.2531  1896 GLU A C   
838 O O   . GLU A 103 ? 1.1715 1.2088 1.0664 -0.1584 -0.1082 0.2791  1896 GLU A O   
839 C CB  . GLU A 103 ? 1.0936 1.2330 0.9882 -0.1515 -0.1042 0.2259  1896 GLU A CB  
840 C CG  . GLU A 103 ? 1.1349 1.2911 1.0223 -0.1670 -0.0738 0.2034  1896 GLU A CG  
841 C CD  . GLU A 103 ? 1.1698 1.3677 1.0144 -0.1825 -0.0640 0.1902  1896 GLU A CD  
842 O OE1 . GLU A 103 ? 1.2753 1.4716 1.0705 -0.2029 -0.0633 0.2108  1896 GLU A OE1 
843 O OE2 . GLU A 103 ? 1.1718 1.4017 1.0299 -0.1737 -0.0561 0.1592  1896 GLU A OE2 
844 N N   . PHE A 104 ? 1.0027 1.0335 0.9795 -0.1255 -0.0906 0.2400  1897 PHE A N   
845 C CA  . PHE A 104 ? 1.0659 1.0371 1.0433 -0.1276 -0.0884 0.2564  1897 PHE A CA  
846 C C   . PHE A 104 ? 1.1550 1.0929 1.1755 -0.0952 -0.1018 0.2665  1897 PHE A C   
847 O O   . PHE A 104 ? 1.1663 1.0575 1.1800 -0.0913 -0.1174 0.2962  1897 PHE A O   
848 C CB  . PHE A 104 ? 1.0906 1.0513 1.0721 -0.1392 -0.0638 0.2313  1897 PHE A CB  
849 C CG  . PHE A 104 ? 1.2171 1.1893 1.1609 -0.1752 -0.0520 0.2338  1897 PHE A CG  
850 C CD1 . PHE A 104 ? 1.3188 1.2481 1.2336 -0.1982 -0.0552 0.2626  1897 PHE A CD1 
851 C CD2 . PHE A 104 ? 1.1798 1.2061 1.1211 -0.1861 -0.0368 0.2080  1897 PHE A CD2 
852 C CE1 . PHE A 104 ? 1.3498 1.2965 1.2358 -0.2346 -0.0410 0.2657  1897 PHE A CE1 
853 C CE2 . PHE A 104 ? 1.1704 1.2166 1.0875 -0.2179 -0.0234 0.2092  1897 PHE A CE2 
854 C CZ  . PHE A 104 ? 1.2795 1.2893 1.1702 -0.2437 -0.0241 0.2380  1897 PHE A CZ  
855 N N   . TYR A 105 ? 1.1730 1.1339 1.2392 -0.0710 -0.0949 0.2432  1898 TYR A N   
856 C CA  . TYR A 105 ? 1.1360 1.0752 1.2533 -0.0377 -0.1007 0.2479  1898 TYR A CA  
857 C C   . TYR A 105 ? 1.0692 1.0575 1.2254 -0.0193 -0.1186 0.2513  1898 TYR A C   
858 O O   . TYR A 105 ? 1.0948 1.0987 1.2354 -0.0247 -0.1453 0.2742  1898 TYR A O   
859 C CB  . TYR A 105 ? 1.0590 0.9807 1.2005 -0.0252 -0.0733 0.2179  1898 TYR A CB  
860 C CG  . TYR A 105 ? 1.0380 0.9112 1.1443 -0.0450 -0.0586 0.2104  1898 TYR A CG  
861 C CD1 . TYR A 105 ? 1.0721 0.8773 1.1726 -0.0411 -0.0633 0.2267  1898 TYR A CD1 
862 C CD2 . TYR A 105 ? 0.9309 0.8250 1.0127 -0.0676 -0.0424 0.1868  1898 TYR A CD2 
863 C CE1 . TYR A 105 ? 1.0430 0.8012 1.1121 -0.0634 -0.0522 0.2189  1898 TYR A CE1 
864 C CE2 . TYR A 105 ? 0.8813 0.7362 0.9364 -0.0885 -0.0326 0.1797  1898 TYR A CE2 
865 C CZ  . TYR A 105 ? 0.9356 0.7222 0.9836 -0.0882 -0.0375 0.1953  1898 TYR A CZ  
866 O OH  . TYR A 105 ? 0.9935 0.7385 1.0157 -0.1129 -0.0300 0.1876  1898 TYR A OH  
# 
