data_9F78
# 
_entry.id   9F78 
# 
_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   9F78         pdb_00009f78 10.2210/pdb9f78/pdb 
WWPDB D_1292138364 ?            ?                   
# 
_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                        9F78 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB '9F6W contains the same protein complexed with a similar ligand' 9F6W unspecified 
PDB '9F70 contains the same protein complexed with a similar ligand' 9F70 unspecified 
PDB '9F71 contains the same protein complexed with a similar ligand' 9F71 unspecified 
PDB '9F77 contains the same protein complexed with a similar ligand' 9F77 unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              graziano.lolli@unitn.it 
_pdbx_contact_author.name_first         Graziano 
_pdbx_contact_author.name_last          Lolli 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8536-5599 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dalle Vedove, A.' 1 ? 
'Cazzanelli, G.'   2 ? 
'Caflisch, A.'     3 ? 
'Lolli, G.'        4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Unusual backfolded binding poses of BAZ2A bromodomain binders' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dalle Vedove, A.' 1 ? 
primary 'Cazzanelli, G.'   2 ? 
primary 
;D'Agostino, V.G.
;
3 ? 
primary 'Caflisch, A.'     4 ? 
primary 'Lolli, G.'        5 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Bromodomain adjacent to zinc finger domain protein 2A' 12354.839 2   ? L1848S ? 
'Bromodomain (residues 1796-1899). First two residues SM derive from the expression tag. L1848S.' 
2 non-polymer syn 
'1-[4-ethyl-5-[4-[(5-ethyl-1,2,4-oxadiazol-3-yl)methyl]piperazin-1-yl]carbonyl-2-methyl-1~{H}-pyrrol-3-yl]ethanone' 373.449   2   
? ?      ? ?                                                                                                 
3 water       nat water 18.015    256 ? ?      ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Transcription termination factor I-interacting protein 5,TTF-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       
;SMHSDLTFCEIILMEMESHDAAWPFLEPVNPRLVSGYRRIIKNPMDFSTMRERLSRGGYTSSEEFAADALLVFDNCQTFN
EDDSEVGKAGHIMRRFFESRWEEFY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMHSDLTFCEIILMEMESHDAAWPFLEPVNPRLVSGYRRIIKNPMDFSTMRERLSRGGYTSSEEFAADALLVFDNCQTFN
EDDSEVGKAGHIMRRFFESRWEEFY
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '1-[4-ethyl-5-[4-[(5-ethyl-1,2,4-oxadiazol-3-yl)methyl]piperazin-1-yl]carbonyl-2-methyl-1~{H}-pyrrol-3-yl]ethanone' A1H98 
3 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  GLU 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 
A1H98 non-polymer         . 
'1-[4-ethyl-5-[4-[(5-ethyl-1,2,4-oxadiazol-3-yl)methyl]piperazin-1-yl]carbonyl-2-methyl-1~{H}-pyrrol-3-yl]ethanone' ? 
'C19 H27 N5 O3'  373.449 
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 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1794 ?    ?   ?   A . n 
A 1 2   MET 2   1795 ?    ?   ?   A . n 
A 1 3   HIS 3   1796 ?    ?   ?   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  GLU 52  1845 1845 GLU GLU 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 
B 1 1   SER 1   1794 ?    ?   ?   B . n 
B 1 2   MET 2   1795 ?    ?   ?   B . n 
B 1 3   HIS 3   1796 1796 HIS HIS B . n 
B 1 4   SER 4   1797 1797 SER SER B . n 
B 1 5   ASP 5   1798 1798 ASP ASP B . n 
B 1 6   LEU 6   1799 1799 LEU LEU B . n 
B 1 7   THR 7   1800 1800 THR THR B . n 
B 1 8   PHE 8   1801 1801 PHE PHE B . n 
B 1 9   CYS 9   1802 1802 CYS CYS B . n 
B 1 10  GLU 10  1803 1803 GLU GLU B . n 
B 1 11  ILE 11  1804 1804 ILE ILE B . n 
B 1 12  ILE 12  1805 1805 ILE ILE B . n 
B 1 13  LEU 13  1806 1806 LEU LEU B . n 
B 1 14  MET 14  1807 1807 MET MET B . n 
B 1 15  GLU 15  1808 1808 GLU GLU B . n 
B 1 16  MET 16  1809 1809 MET MET B . n 
B 1 17  GLU 17  1810 1810 GLU GLU B . n 
B 1 18  SER 18  1811 1811 SER SER B . n 
B 1 19  HIS 19  1812 1812 HIS HIS B . n 
B 1 20  ASP 20  1813 1813 ASP ASP B . n 
B 1 21  ALA 21  1814 1814 ALA ALA B . n 
B 1 22  ALA 22  1815 1815 ALA ALA B . n 
B 1 23  TRP 23  1816 1816 TRP TRP B . n 
B 1 24  PRO 24  1817 1817 PRO PRO B . n 
B 1 25  PHE 25  1818 1818 PHE PHE B . n 
B 1 26  LEU 26  1819 1819 LEU LEU B . n 
B 1 27  GLU 27  1820 1820 GLU GLU B . n 
B 1 28  PRO 28  1821 1821 PRO PRO B . n 
B 1 29  VAL 29  1822 1822 VAL VAL B . n 
B 1 30  ASN 30  1823 1823 ASN ASN B . n 
B 1 31  PRO 31  1824 1824 PRO PRO B . n 
B 1 32  ARG 32  1825 1825 ARG ARG B . n 
B 1 33  LEU 33  1826 1826 LEU LEU B . n 
B 1 34  VAL 34  1827 1827 VAL VAL B . n 
B 1 35  SER 35  1828 1828 SER SER B . n 
B 1 36  GLY 36  1829 1829 GLY GLY B . n 
B 1 37  TYR 37  1830 1830 TYR TYR B . n 
B 1 38  ARG 38  1831 1831 ARG ARG B . n 
B 1 39  ARG 39  1832 1832 ARG ARG B . n 
B 1 40  ILE 40  1833 1833 ILE ILE B . n 
B 1 41  ILE 41  1834 1834 ILE ILE B . n 
B 1 42  LYS 42  1835 1835 LYS LYS B . n 
B 1 43  ASN 43  1836 1836 ASN ASN B . n 
B 1 44  PRO 44  1837 1837 PRO PRO B . n 
B 1 45  MET 45  1838 1838 MET MET B . n 
B 1 46  ASP 46  1839 1839 ASP ASP B . n 
B 1 47  PHE 47  1840 1840 PHE PHE B . n 
B 1 48  SER 48  1841 1841 SER SER B . n 
B 1 49  THR 49  1842 1842 THR THR B . n 
B 1 50  MET 50  1843 1843 MET MET B . n 
B 1 51  ARG 51  1844 1844 ARG ARG B . n 
B 1 52  GLU 52  1845 1845 GLU GLU B . n 
B 1 53  ARG 53  1846 1846 ARG ARG B . n 
B 1 54  LEU 54  1847 1847 LEU LEU B . n 
B 1 55  SER 55  1848 1848 SER SER B . n 
B 1 56  ARG 56  1849 1849 ARG ARG B . n 
B 1 57  GLY 57  1850 1850 GLY GLY B . n 
B 1 58  GLY 58  1851 1851 GLY GLY B . n 
B 1 59  TYR 59  1852 1852 TYR TYR B . n 
B 1 60  THR 60  1853 1853 THR THR B . n 
B 1 61  SER 61  1854 1854 SER SER B . n 
B 1 62  SER 62  1855 1855 SER SER B . n 
B 1 63  GLU 63  1856 1856 GLU GLU B . n 
B 1 64  GLU 64  1857 1857 GLU GLU B . n 
B 1 65  PHE 65  1858 1858 PHE PHE B . n 
B 1 66  ALA 66  1859 1859 ALA ALA B . n 
B 1 67  ALA 67  1860 1860 ALA ALA B . n 
B 1 68  ASP 68  1861 1861 ASP ASP B . n 
B 1 69  ALA 69  1862 1862 ALA ALA B . n 
B 1 70  LEU 70  1863 1863 LEU LEU B . n 
B 1 71  LEU 71  1864 1864 LEU LEU B . n 
B 1 72  VAL 72  1865 1865 VAL VAL B . n 
B 1 73  PHE 73  1866 1866 PHE PHE B . n 
B 1 74  ASP 74  1867 1867 ASP ASP B . n 
B 1 75  ASN 75  1868 1868 ASN ASN B . n 
B 1 76  CYS 76  1869 1869 CYS CYS B . n 
B 1 77  GLN 77  1870 1870 GLN GLN B . n 
B 1 78  THR 78  1871 1871 THR THR B . n 
B 1 79  PHE 79  1872 1872 PHE PHE B . n 
B 1 80  ASN 80  1873 1873 ASN ASN B . n 
B 1 81  GLU 81  1874 1874 GLU GLU B . n 
B 1 82  ASP 82  1875 1875 ASP ASP B . n 
B 1 83  ASP 83  1876 1876 ASP ASP B . n 
B 1 84  SER 84  1877 1877 SER SER B . n 
B 1 85  GLU 85  1878 1878 GLU GLU B . n 
B 1 86  VAL 86  1879 1879 VAL VAL B . n 
B 1 87  GLY 87  1880 1880 GLY GLY B . n 
B 1 88  LYS 88  1881 1881 LYS LYS B . n 
B 1 89  ALA 89  1882 1882 ALA ALA B . n 
B 1 90  GLY 90  1883 1883 GLY GLY B . n 
B 1 91  HIS 91  1884 1884 HIS HIS B . n 
B 1 92  ILE 92  1885 1885 ILE ILE B . n 
B 1 93  MET 93  1886 1886 MET MET B . n 
B 1 94  ARG 94  1887 1887 ARG ARG B . n 
B 1 95  ARG 95  1888 1888 ARG ARG B . n 
B 1 96  PHE 96  1889 1889 PHE PHE B . n 
B 1 97  PHE 97  1890 1890 PHE PHE B . n 
B 1 98  GLU 98  1891 1891 GLU GLU B . n 
B 1 99  SER 99  1892 1892 SER SER B . n 
B 1 100 ARG 100 1893 1893 ARG ARG B . n 
B 1 101 TRP 101 1894 1894 TRP TRP B . n 
B 1 102 GLU 102 1895 1895 GLU GLU B . n 
B 1 103 GLU 103 1896 1896 GLU GLU B . n 
B 1 104 PHE 104 1897 1897 PHE PHE B . n 
B 1 105 TYR 105 1898 1898 TYR TYR B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H98 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H98 
_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 
C 2 A1H98 1   1901 1901 A1H98 T23 A . 
D 2 A1H98 1   1901 1901 A1H98 T23 B . 
E 3 HOH   1   2001 80   HOH   HOH A . 
E 3 HOH   2   2002 83   HOH   HOH A . 
E 3 HOH   3   2003 87   HOH   HOH A . 
E 3 HOH   4   2004 156  HOH   HOH A . 
E 3 HOH   5   2005 211  HOH   HOH A . 
E 3 HOH   6   2006 111  HOH   HOH A . 
E 3 HOH   7   2007 251  HOH   HOH A . 
E 3 HOH   8   2008 68   HOH   HOH A . 
E 3 HOH   9   2009 82   HOH   HOH A . 
E 3 HOH   10  2010 132  HOH   HOH A . 
E 3 HOH   11  2011 245  HOH   HOH A . 
E 3 HOH   12  2012 41   HOH   HOH A . 
E 3 HOH   13  2013 141  HOH   HOH A . 
E 3 HOH   14  2014 197  HOH   HOH A . 
E 3 HOH   15  2015 31   HOH   HOH A . 
E 3 HOH   16  2016 152  HOH   HOH A . 
E 3 HOH   17  2017 5    HOH   HOH A . 
E 3 HOH   18  2018 99   HOH   HOH A . 
E 3 HOH   19  2019 62   HOH   HOH A . 
E 3 HOH   20  2020 21   HOH   HOH A . 
E 3 HOH   21  2021 17   HOH   HOH A . 
E 3 HOH   22  2022 147  HOH   HOH A . 
E 3 HOH   23  2023 178  HOH   HOH A . 
E 3 HOH   24  2024 154  HOH   HOH A . 
E 3 HOH   25  2025 93   HOH   HOH A . 
E 3 HOH   26  2026 50   HOH   HOH A . 
E 3 HOH   27  2027 209  HOH   HOH A . 
E 3 HOH   28  2028 119  HOH   HOH A . 
E 3 HOH   29  2029 166  HOH   HOH A . 
E 3 HOH   30  2030 40   HOH   HOH A . 
E 3 HOH   31  2031 140  HOH   HOH A . 
E 3 HOH   32  2032 88   HOH   HOH A . 
E 3 HOH   33  2033 85   HOH   HOH A . 
E 3 HOH   34  2034 69   HOH   HOH A . 
E 3 HOH   35  2035 151  HOH   HOH A . 
E 3 HOH   36  2036 223  HOH   HOH A . 
E 3 HOH   37  2037 26   HOH   HOH A . 
E 3 HOH   38  2038 56   HOH   HOH A . 
E 3 HOH   39  2039 12   HOH   HOH A . 
E 3 HOH   40  2040 19   HOH   HOH A . 
E 3 HOH   41  2041 98   HOH   HOH A . 
E 3 HOH   42  2042 64   HOH   HOH A . 
E 3 HOH   43  2043 48   HOH   HOH A . 
E 3 HOH   44  2044 63   HOH   HOH A . 
E 3 HOH   45  2045 129  HOH   HOH A . 
E 3 HOH   46  2046 94   HOH   HOH A . 
E 3 HOH   47  2047 53   HOH   HOH A . 
E 3 HOH   48  2048 24   HOH   HOH A . 
E 3 HOH   49  2049 176  HOH   HOH A . 
E 3 HOH   50  2050 101  HOH   HOH A . 
E 3 HOH   51  2051 23   HOH   HOH A . 
E 3 HOH   52  2052 106  HOH   HOH A . 
E 3 HOH   53  2053 7    HOH   HOH A . 
E 3 HOH   54  2054 220  HOH   HOH A . 
E 3 HOH   55  2055 224  HOH   HOH A . 
E 3 HOH   56  2056 35   HOH   HOH A . 
E 3 HOH   57  2057 175  HOH   HOH A . 
E 3 HOH   58  2058 170  HOH   HOH A . 
E 3 HOH   59  2059 33   HOH   HOH A . 
E 3 HOH   60  2060 173  HOH   HOH A . 
E 3 HOH   61  2061 233  HOH   HOH A . 
E 3 HOH   62  2062 46   HOH   HOH A . 
E 3 HOH   63  2063 231  HOH   HOH A . 
E 3 HOH   64  2064 212  HOH   HOH A . 
E 3 HOH   65  2065 45   HOH   HOH A . 
E 3 HOH   66  2066 43   HOH   HOH A . 
E 3 HOH   67  2067 105  HOH   HOH A . 
E 3 HOH   68  2068 260  HOH   HOH A . 
E 3 HOH   69  2069 81   HOH   HOH A . 
E 3 HOH   70  2070 258  HOH   HOH A . 
E 3 HOH   71  2071 222  HOH   HOH A . 
E 3 HOH   72  2072 27   HOH   HOH A . 
E 3 HOH   73  2073 199  HOH   HOH A . 
E 3 HOH   74  2074 84   HOH   HOH A . 
E 3 HOH   75  2075 11   HOH   HOH A . 
E 3 HOH   76  2076 253  HOH   HOH A . 
E 3 HOH   77  2077 257  HOH   HOH A . 
E 3 HOH   78  2078 244  HOH   HOH A . 
E 3 HOH   79  2079 39   HOH   HOH A . 
E 3 HOH   80  2080 127  HOH   HOH A . 
E 3 HOH   81  2081 30   HOH   HOH A . 
E 3 HOH   82  2082 226  HOH   HOH A . 
E 3 HOH   83  2083 29   HOH   HOH A . 
E 3 HOH   84  2084 78   HOH   HOH A . 
E 3 HOH   85  2085 42   HOH   HOH A . 
E 3 HOH   86  2086 174  HOH   HOH A . 
E 3 HOH   87  2087 203  HOH   HOH A . 
E 3 HOH   88  2088 109  HOH   HOH A . 
E 3 HOH   89  2089 205  HOH   HOH A . 
E 3 HOH   90  2090 113  HOH   HOH A . 
E 3 HOH   91  2091 249  HOH   HOH A . 
E 3 HOH   92  2092 155  HOH   HOH A . 
E 3 HOH   93  2093 232  HOH   HOH A . 
E 3 HOH   94  2094 221  HOH   HOH A . 
E 3 HOH   95  2095 97   HOH   HOH A . 
E 3 HOH   96  2096 102  HOH   HOH A . 
E 3 HOH   97  2097 135  HOH   HOH A . 
E 3 HOH   98  2098 202  HOH   HOH A . 
E 3 HOH   99  2099 134  HOH   HOH A . 
E 3 HOH   100 2100 76   HOH   HOH A . 
E 3 HOH   101 2101 66   HOH   HOH A . 
E 3 HOH   102 2102 256  HOH   HOH A . 
E 3 HOH   103 2103 236  HOH   HOH A . 
E 3 HOH   104 2104 214  HOH   HOH A . 
E 3 HOH   105 2105 148  HOH   HOH A . 
E 3 HOH   106 2106 238  HOH   HOH A . 
E 3 HOH   107 2107 183  HOH   HOH A . 
E 3 HOH   108 2108 72   HOH   HOH A . 
E 3 HOH   109 2109 239  HOH   HOH A . 
E 3 HOH   110 2110 164  HOH   HOH A . 
E 3 HOH   111 2111 157  HOH   HOH A . 
E 3 HOH   112 2112 230  HOH   HOH A . 
E 3 HOH   113 2113 55   HOH   HOH A . 
E 3 HOH   114 2114 171  HOH   HOH A . 
E 3 HOH   115 2115 255  HOH   HOH A . 
E 3 HOH   116 2116 138  HOH   HOH A . 
E 3 HOH   117 2117 89   HOH   HOH A . 
E 3 HOH   118 2118 116  HOH   HOH A . 
E 3 HOH   119 2119 79   HOH   HOH A . 
E 3 HOH   120 2120 217  HOH   HOH A . 
E 3 HOH   121 2121 133  HOH   HOH A . 
E 3 HOH   122 2122 218  HOH   HOH A . 
E 3 HOH   123 2123 193  HOH   HOH A . 
E 3 HOH   124 2124 247  HOH   HOH A . 
F 3 HOH   1   2001 180  HOH   HOH B . 
F 3 HOH   2   2002 177  HOH   HOH B . 
F 3 HOH   3   2003 181  HOH   HOH B . 
F 3 HOH   4   2004 227  HOH   HOH B . 
F 3 HOH   5   2005 185  HOH   HOH B . 
F 3 HOH   6   2006 194  HOH   HOH B . 
F 3 HOH   7   2007 228  HOH   HOH B . 
F 3 HOH   8   2008 215  HOH   HOH B . 
F 3 HOH   9   2009 161  HOH   HOH B . 
F 3 HOH   10  2010 167  HOH   HOH B . 
F 3 HOH   11  2011 112  HOH   HOH B . 
F 3 HOH   12  2012 235  HOH   HOH B . 
F 3 HOH   13  2013 237  HOH   HOH B . 
F 3 HOH   14  2014 123  HOH   HOH B . 
F 3 HOH   15  2015 240  HOH   HOH B . 
F 3 HOH   16  2016 150  HOH   HOH B . 
F 3 HOH   17  2017 75   HOH   HOH B . 
F 3 HOH   18  2018 182  HOH   HOH B . 
F 3 HOH   19  2019 49   HOH   HOH B . 
F 3 HOH   20  2020 15   HOH   HOH B . 
F 3 HOH   21  2021 121  HOH   HOH B . 
F 3 HOH   22  2022 90   HOH   HOH B . 
F 3 HOH   23  2023 4    HOH   HOH B . 
F 3 HOH   24  2024 91   HOH   HOH B . 
F 3 HOH   25  2025 191  HOH   HOH B . 
F 3 HOH   26  2026 137  HOH   HOH B . 
F 3 HOH   27  2027 207  HOH   HOH B . 
F 3 HOH   28  2028 124  HOH   HOH B . 
F 3 HOH   29  2029 13   HOH   HOH B . 
F 3 HOH   30  2030 1    HOH   HOH B . 
F 3 HOH   31  2031 114  HOH   HOH B . 
F 3 HOH   32  2032 229  HOH   HOH B . 
F 3 HOH   33  2033 22   HOH   HOH B . 
F 3 HOH   34  2034 47   HOH   HOH B . 
F 3 HOH   35  2035 122  HOH   HOH B . 
F 3 HOH   36  2036 32   HOH   HOH B . 
F 3 HOH   37  2037 168  HOH   HOH B . 
F 3 HOH   38  2038 70   HOH   HOH B . 
F 3 HOH   39  2039 36   HOH   HOH B . 
F 3 HOH   40  2040 153  HOH   HOH B . 
F 3 HOH   41  2041 92   HOH   HOH B . 
F 3 HOH   42  2042 160  HOH   HOH B . 
F 3 HOH   43  2043 143  HOH   HOH B . 
F 3 HOH   44  2044 14   HOH   HOH B . 
F 3 HOH   45  2045 9    HOH   HOH B . 
F 3 HOH   46  2046 142  HOH   HOH B . 
F 3 HOH   47  2047 254  HOH   HOH B . 
F 3 HOH   48  2048 74   HOH   HOH B . 
F 3 HOH   49  2049 34   HOH   HOH B . 
F 3 HOH   50  2050 213  HOH   HOH B . 
F 3 HOH   51  2051 28   HOH   HOH B . 
F 3 HOH   52  2052 16   HOH   HOH B . 
F 3 HOH   53  2053 77   HOH   HOH B . 
F 3 HOH   54  2054 65   HOH   HOH B . 
F 3 HOH   55  2055 117  HOH   HOH B . 
F 3 HOH   56  2056 130  HOH   HOH B . 
F 3 HOH   57  2057 248  HOH   HOH B . 
F 3 HOH   58  2058 145  HOH   HOH B . 
F 3 HOH   59  2059 149  HOH   HOH B . 
F 3 HOH   60  2060 3    HOH   HOH B . 
F 3 HOH   61  2061 37   HOH   HOH B . 
F 3 HOH   62  2062 67   HOH   HOH B . 
F 3 HOH   63  2063 10   HOH   HOH B . 
F 3 HOH   64  2064 120  HOH   HOH B . 
F 3 HOH   65  2065 115  HOH   HOH B . 
F 3 HOH   66  2066 59   HOH   HOH B . 
F 3 HOH   67  2067 61   HOH   HOH B . 
F 3 HOH   68  2068 58   HOH   HOH B . 
F 3 HOH   69  2069 8    HOH   HOH B . 
F 3 HOH   70  2070 162  HOH   HOH B . 
F 3 HOH   71  2071 169  HOH   HOH B . 
F 3 HOH   72  2072 60   HOH   HOH B . 
F 3 HOH   73  2073 2    HOH   HOH B . 
F 3 HOH   74  2074 131  HOH   HOH B . 
F 3 HOH   75  2075 73   HOH   HOH B . 
F 3 HOH   76  2076 44   HOH   HOH B . 
F 3 HOH   77  2077 100  HOH   HOH B . 
F 3 HOH   78  2078 6    HOH   HOH B . 
F 3 HOH   79  2079 96   HOH   HOH B . 
F 3 HOH   80  2080 25   HOH   HOH B . 
F 3 HOH   81  2081 189  HOH   HOH B . 
F 3 HOH   82  2082 51   HOH   HOH B . 
F 3 HOH   83  2083 179  HOH   HOH B . 
F 3 HOH   84  2084 146  HOH   HOH B . 
F 3 HOH   85  2085 20   HOH   HOH B . 
F 3 HOH   86  2086 57   HOH   HOH B . 
F 3 HOH   87  2087 201  HOH   HOH B . 
F 3 HOH   88  2088 158  HOH   HOH B . 
F 3 HOH   89  2089 195  HOH   HOH B . 
F 3 HOH   90  2090 192  HOH   HOH B . 
F 3 HOH   91  2091 54   HOH   HOH B . 
F 3 HOH   92  2092 110  HOH   HOH B . 
F 3 HOH   93  2093 172  HOH   HOH B . 
F 3 HOH   94  2094 144  HOH   HOH B . 
F 3 HOH   95  2095 71   HOH   HOH B . 
F 3 HOH   96  2096 104  HOH   HOH B . 
F 3 HOH   97  2097 86   HOH   HOH B . 
F 3 HOH   98  2098 184  HOH   HOH B . 
F 3 HOH   99  2099 118  HOH   HOH B . 
F 3 HOH   100 2100 126  HOH   HOH B . 
F 3 HOH   101 2101 234  HOH   HOH B . 
F 3 HOH   102 2102 52   HOH   HOH B . 
F 3 HOH   103 2103 139  HOH   HOH B . 
F 3 HOH   104 2104 188  HOH   HOH B . 
F 3 HOH   105 2105 243  HOH   HOH B . 
F 3 HOH   106 2106 107  HOH   HOH B . 
F 3 HOH   107 2107 200  HOH   HOH B . 
F 3 HOH   108 2108 242  HOH   HOH B . 
F 3 HOH   109 2109 108  HOH   HOH B . 
F 3 HOH   110 2110 165  HOH   HOH B . 
F 3 HOH   111 2111 136  HOH   HOH B . 
F 3 HOH   112 2112 259  HOH   HOH B . 
F 3 HOH   113 2113 186  HOH   HOH B . 
F 3 HOH   114 2114 219  HOH   HOH B . 
F 3 HOH   115 2115 103  HOH   HOH B . 
F 3 HOH   116 2116 125  HOH   HOH B . 
F 3 HOH   117 2117 187  HOH   HOH B . 
F 3 HOH   118 2118 38   HOH   HOH B . 
F 3 HOH   119 2119 210  HOH   HOH B . 
F 3 HOH   120 2120 204  HOH   HOH B . 
F 3 HOH   121 2121 250  HOH   HOH B . 
F 3 HOH   122 2122 216  HOH   HOH B . 
F 3 HOH   123 2123 95   HOH   HOH B . 
F 3 HOH   124 2124 18   HOH   HOH B . 
F 3 HOH   125 2125 198  HOH   HOH B . 
F 3 HOH   126 2126 128  HOH   HOH B . 
F 3 HOH   127 2127 190  HOH   HOH B . 
F 3 HOH   128 2128 196  HOH   HOH B . 
F 3 HOH   129 2129 159  HOH   HOH B . 
F 3 HOH   130 2130 208  HOH   HOH B . 
F 3 HOH   131 2131 252  HOH   HOH B . 
F 3 HOH   132 2132 246  HOH   HOH B . 
# 
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                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F78 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     43.024 
_cell.length_a_esd                 ? 
_cell.length_b                     54.360 
_cell.length_b_esd                 ? 
_cell.length_c                     90.159 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9F78 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9F78 
_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             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.35 
_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         2019-08-07 
_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   1.000 
_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        1.000 
_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                                       9F78 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.70 
_reflns.d_resolution_low                               46.55 
_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                                     22981 
_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                           96.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.91 
_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                                0.079 
_reflns.pdbx_Rpim_I_all                                0.033 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       127373 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.071 
_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                                    1.70 
_reflns_shell.d_res_low                                     1.73 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           6749 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1148 
_reflns_shell.percent_possible_obs                          93.7 
_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                               5.9 
_reflns_shell.pdbx_chi_squared                              0.56 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     3.0 
_reflns_shell.pdbx_Rrim_I_all                               0.484 
_reflns_shell.pdbx_Rpim_I_all                               0.192 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.924 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.442 
_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                                 9F78 
_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                            1.700 
_refine.ls_d_res_low                             38.829 
_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                     22933 
_refine.ls_number_reflns_R_free                  1158 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.81 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2110 
_refine.ls_R_factor_R_free                       0.2522 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2088 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.43 
_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                            0.23 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.700 
_refine_hist.d_res_low                        38.829 
_refine_hist.number_atoms_solvent             256 
_refine_hist.number_atoms_total               2002 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1692 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005  ? 1849 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.833  ? 2507 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 21.352 ? 1116 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.045  ? 245  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 331  ? 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' 1.7000 1.7774 . . 122 2619 94.00 . . . . 0.2652 . . . . . . . . . . . 0.3283 
'X-RAY DIFFRACTION' 1.7774 1.8711 . . 152 2625 94.00 . . . . 0.2609 . . . . . . . . . . . 0.3048 
'X-RAY DIFFRACTION' 1.8711 1.9883 . . 150 2664 96.00 . . . . 0.2473 . . . . . . . . . . . 0.3043 
'X-RAY DIFFRACTION' 1.9883 2.1418 . . 148 2702 96.00 . . . . 0.2299 . . . . . . . . . . . 0.2911 
'X-RAY DIFFRACTION' 2.1418 2.3573 . . 150 2766 98.00 . . . . 0.2171 . . . . . . . . . . . 0.2816 
'X-RAY DIFFRACTION' 2.3573 2.6984 . . 143 2799 98.00 . . . . 0.2170 . . . . . . . . . . . 0.2746 
'X-RAY DIFFRACTION' 2.6984 3.3994 . . 148 2786 97.00 . . . . 0.2028 . . . . . . . . . . . 0.2245 
'X-RAY DIFFRACTION' 3.3994 38.829 . . 145 2814 93.00 . . . . 0.1804 . . . . . . . . . . . 0.2144 
# 
_struct.entry_id                     9F78 
_struct.title                        'BAZ2A bromodomain in complex with acetylpyrrole derivative compound 28-TN23' 
_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        9F78 
_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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_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 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9F78 A 3 ? 105 ? Q9UIF9 1796 ? 1898 ? 1796 1898 
2 1 9F78 B 3 ? 105 ? Q9UIF9 1796 ? 1898 ? 1796 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 9F78 SER A 1  ? UNP Q9UIF9 ?   ?    'expression tag'      1794 1 
1 9F78 MET A 2  ? UNP Q9UIF9 ?   ?    'expression tag'      1795 2 
1 9F78 SER A 55 ? UNP Q9UIF9 LEU 1848 'engineered mutation' 1848 3 
2 9F78 SER B 1  ? UNP Q9UIF9 ?   ?    'expression tag'      1794 4 
2 9F78 MET B 2  ? UNP Q9UIF9 ?   ?    'expression tag'      1795 5 
2 9F78 SER B 55 ? UNP Q9UIF9 LEU 1848 'engineered mutation' 1848 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E 
2 1 B,D,F 
# 
_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 SER A 4  ? HIS A 19  ? SER A 1797 HIS A 1812 1 ? 16 
HELX_P HELX_P2  AA2 ASP A 20 ? LEU A 26  ? ASP A 1813 LEU A 1819 5 ? 7  
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 
HELX_P HELX_P8  AA8 LEU B 6  ? SER B 18  ? LEU B 1799 SER B 1811 1 ? 13 
HELX_P HELX_P9  AA9 HIS B 19 ? TRP B 23  ? HIS B 1812 TRP B 1816 5 ? 5  
HELX_P HELX_P10 AB1 GLY B 36 ? ILE B 41  ? GLY B 1829 ILE B 1834 1 ? 6  
HELX_P HELX_P11 AB2 ASP B 46 ? ARG B 56  ? ASP B 1839 ARG B 1849 1 ? 11 
HELX_P HELX_P12 AB3 SER B 61 ? ASN B 80  ? SER B 1854 ASN B 1873 1 ? 20 
HELX_P HELX_P13 AB4 SER B 84 ? GLU B 103 ? SER B 1877 GLU B 1896 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   9F78 
_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_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 1836 ? ? -119.49 75.95  
2 1 PHE A 1897 ? ? -120.78 -57.02 
3 1 PHE B 1897 ? ? -100.57 -71.95 
# 
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 -9.8312  -7.6097 24.9452 0.1681 ? -0.0335 ? -0.0190 ? 0.2363 ? 0.0082  ? 0.1671 ? 3.9496 ? -0.6878 
? -1.3912 ? 3.2093 ? 0.4455  ? 5.5502 ? -0.2193 ? -0.3529 ? -0.0678 ? 0.0270  ? 0.1360  ? 0.2997  ? 0.2959  ? -0.5482 ? 0.0689  ? 
2 'X-RAY DIFFRACTION' ? refined -2.3981  -3.0572 26.3783 0.1311 ? 0.0159  ? -0.0192 ? 0.1646 ? 0.0167  ? 0.1788 ? 1.8247 ? -0.3389 
? -2.0110 ? 2.4272 ? 0.9185  ? 7.0888 ? -0.0317 ? 0.0083  ? 0.1334  ? 0.0051  ? -0.0220 ? -0.0738 ? -0.1729 ? -0.0040 ? 0.0058  ? 
3 'X-RAY DIFFRACTION' ? refined -12.3078 0.5068  17.7092 0.2519 ? 0.0816  ? -0.0821 ? 0.3749 ? 0.0429  ? 0.2633 ? 3.7553 ? 0.1491  
? 1.2734  ? 4.7693 ? 0.0247  ? 1.2572 ? 0.0649  ? 0.3365  ? 0.2353  ? -0.3368 ? -0.1701 ? 0.5411  ? -0.3708 ? -0.8162 ? 0.1324  ? 
4 'X-RAY DIFFRACTION' ? refined 10.0367  -4.9460 44.1121 0.1712 ? 0.0132  ? -0.0207 ? 0.1667 ? -0.0126 ? 0.1799 ? 5.2179 ? -0.5700 
? -0.4286 ? 1.7033 ? -0.0254 ? 4.1683 ? 0.1745  ? -0.1880 ? 0.1859  ? -0.0961 ? -0.0801 ? -0.1099 ? 0.0335  ? 0.4902  ? -0.0625 ? 
5 'X-RAY DIFFRACTION' ? refined 2.7538   -1.4075 44.1466 0.0873 ? 0.0046  ? -0.0136 ? 0.1317 ? -0.0060 ? 0.1570 ? 3.3153 ? 0.5717  
? -1.4815 ? 2.1661 ? -0.0704 ? 5.6276 ? 0.0906  ? -0.1386 ? 0.0505  ? 0.0114  ? 0.0337  ? 0.0112  ? -0.0207 ? 0.0586  ? -0.1013 ? 
6 'X-RAY DIFFRACTION' ? refined 14.1026  4.6797  48.2714 0.2586 ? -0.1410 ? 0.0771  ? 0.3415 ? -0.1101 ? 0.4156 ? 4.0151 ? -1.3033 
? 3.1861  ? 4.6148 ? 0.5886  ? 4.2605 ? 0.2964  ? -0.4024 ? 0.6083  ? -0.1702 ? -0.0881 ? -0.9379 ? -0.5711 ? 1.2235  ? -0.0575 ? 
# 
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 1797 through 1829 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1830 through 1872 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1873 through 1898 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 1796 through 1829 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 1830 through 1877 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 1878 through 1898 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 2123 ? 6.06 . 
2 1 O ? A HOH 2124 ? 7.81 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 1794 ? A SER 1 
2 1 Y 1 A MET 1795 ? A MET 2 
3 1 Y 1 A HIS 1796 ? A HIS 3 
4 1 Y 1 B SER 1794 ? B SER 1 
5 1 Y 1 B MET 1795 ? B MET 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1H98 C01  C N N 1   
A1H98 C02  C N N 2   
A1H98 C03  C Y N 3   
A1H98 C05  C Y N 4   
A1H98 C06  C N N 5   
A1H98 C08  C N N 6   
A1H98 C09  C N N 7   
A1H98 C11  C N N 8   
A1H98 C12  C N N 9   
A1H98 C13  C N N 10  
A1H98 C15  C Y N 11  
A1H98 C17  C Y N 12  
A1H98 C18  C N N 13  
A1H98 C19  C Y N 14  
A1H98 C20  C N N 15  
A1H98 C22  C N N 16  
A1H98 C23  C Y N 17  
A1H98 C24  C N N 18  
A1H98 C25  C N N 19  
A1H98 N04  N Y N 20  
A1H98 N07  N N N 21  
A1H98 N10  N N N 22  
A1H98 N16  N Y N 23  
A1H98 N26  N Y N 24  
A1H98 O14  O N N 25  
A1H98 O21  O N N 26  
A1H98 O27  O Y N 27  
A1H98 H1   H N N 28  
A1H98 H2   H N N 29  
A1H98 H3   H N N 30  
A1H98 H4   H N N 31  
A1H98 H5   H N N 32  
A1H98 H6   H N N 33  
A1H98 H7   H N N 34  
A1H98 H8   H N N 35  
A1H98 H9   H N N 36  
A1H98 H10  H N N 37  
A1H98 H11  H N N 38  
A1H98 H12  H N N 39  
A1H98 H13  H N N 40  
A1H98 H14  H N N 41  
A1H98 H15  H N N 42  
A1H98 H16  H N N 43  
A1H98 H17  H N N 44  
A1H98 H18  H N N 45  
A1H98 H19  H N N 46  
A1H98 H20  H N N 47  
A1H98 H21  H N N 48  
A1H98 H22  H N N 49  
A1H98 H23  H N N 50  
A1H98 H24  H N N 51  
A1H98 H25  H N N 52  
A1H98 H26  H N N 53  
A1H98 H28  H N N 54  
ALA   N    N N N 55  
ALA   CA   C N S 56  
ALA   C    C N N 57  
ALA   O    O N N 58  
ALA   CB   C N N 59  
ALA   OXT  O N N 60  
ALA   H    H N N 61  
ALA   H2   H N N 62  
ALA   HA   H N N 63  
ALA   HB1  H N N 64  
ALA   HB2  H N N 65  
ALA   HB3  H N N 66  
ALA   HXT  H N N 67  
ARG   N    N N N 68  
ARG   CA   C N S 69  
ARG   C    C N N 70  
ARG   O    O N N 71  
ARG   CB   C N N 72  
ARG   CG   C N N 73  
ARG   CD   C N N 74  
ARG   NE   N N N 75  
ARG   CZ   C N N 76  
ARG   NH1  N N N 77  
ARG   NH2  N N N 78  
ARG   OXT  O N N 79  
ARG   H    H N N 80  
ARG   H2   H N N 81  
ARG   HA   H N N 82  
ARG   HB2  H N N 83  
ARG   HB3  H N N 84  
ARG   HG2  H N N 85  
ARG   HG3  H N N 86  
ARG   HD2  H N N 87  
ARG   HD3  H N N 88  
ARG   HE   H N N 89  
ARG   HH11 H N N 90  
ARG   HH12 H N N 91  
ARG   HH21 H N N 92  
ARG   HH22 H N N 93  
ARG   HXT  H N N 94  
ASN   N    N N N 95  
ASN   CA   C N S 96  
ASN   C    C N N 97  
ASN   O    O N N 98  
ASN   CB   C N N 99  
ASN   CG   C N N 100 
ASN   OD1  O N N 101 
ASN   ND2  N N N 102 
ASN   OXT  O N N 103 
ASN   H    H N N 104 
ASN   H2   H N N 105 
ASN   HA   H N N 106 
ASN   HB2  H N N 107 
ASN   HB3  H N N 108 
ASN   HD21 H N N 109 
ASN   HD22 H N N 110 
ASN   HXT  H N N 111 
ASP   N    N N N 112 
ASP   CA   C N S 113 
ASP   C    C N N 114 
ASP   O    O N N 115 
ASP   CB   C N N 116 
ASP   CG   C N N 117 
ASP   OD1  O N N 118 
ASP   OD2  O N N 119 
ASP   OXT  O N N 120 
ASP   H    H N N 121 
ASP   H2   H N N 122 
ASP   HA   H N N 123 
ASP   HB2  H N N 124 
ASP   HB3  H N N 125 
ASP   HD2  H N N 126 
ASP   HXT  H N N 127 
CYS   N    N N N 128 
CYS   CA   C N R 129 
CYS   C    C N N 130 
CYS   O    O N N 131 
CYS   CB   C N N 132 
CYS   SG   S N N 133 
CYS   OXT  O N N 134 
CYS   H    H N N 135 
CYS   H2   H N N 136 
CYS   HA   H N N 137 
CYS   HB2  H N N 138 
CYS   HB3  H N N 139 
CYS   HG   H N N 140 
CYS   HXT  H N N 141 
GLN   N    N N N 142 
GLN   CA   C N S 143 
GLN   C    C N N 144 
GLN   O    O N N 145 
GLN   CB   C N N 146 
GLN   CG   C N N 147 
GLN   CD   C N N 148 
GLN   OE1  O N N 149 
GLN   NE2  N N N 150 
GLN   OXT  O N N 151 
GLN   H    H N N 152 
GLN   H2   H N N 153 
GLN   HA   H N N 154 
GLN   HB2  H N N 155 
GLN   HB3  H N N 156 
GLN   HG2  H N N 157 
GLN   HG3  H N N 158 
GLN   HE21 H N N 159 
GLN   HE22 H N N 160 
GLN   HXT  H N N 161 
GLU   N    N N N 162 
GLU   CA   C N S 163 
GLU   C    C N N 164 
GLU   O    O N N 165 
GLU   CB   C N N 166 
GLU   CG   C N N 167 
GLU   CD   C N N 168 
GLU   OE1  O N N 169 
GLU   OE2  O N N 170 
GLU   OXT  O N N 171 
GLU   H    H N N 172 
GLU   H2   H N N 173 
GLU   HA   H N N 174 
GLU   HB2  H N N 175 
GLU   HB3  H N N 176 
GLU   HG2  H N N 177 
GLU   HG3  H N N 178 
GLU   HE2  H N N 179 
GLU   HXT  H N N 180 
GLY   N    N N N 181 
GLY   CA   C N N 182 
GLY   C    C N N 183 
GLY   O    O N N 184 
GLY   OXT  O N N 185 
GLY   H    H N N 186 
GLY   H2   H N N 187 
GLY   HA2  H N N 188 
GLY   HA3  H N N 189 
GLY   HXT  H N N 190 
HIS   N    N N N 191 
HIS   CA   C N S 192 
HIS   C    C N N 193 
HIS   O    O N N 194 
HIS   CB   C N N 195 
HIS   CG   C Y N 196 
HIS   ND1  N Y N 197 
HIS   CD2  C Y N 198 
HIS   CE1  C Y N 199 
HIS   NE2  N Y N 200 
HIS   OXT  O N N 201 
HIS   H    H N N 202 
HIS   H2   H N N 203 
HIS   HA   H N N 204 
HIS   HB2  H N N 205 
HIS   HB3  H N N 206 
HIS   HD1  H N N 207 
HIS   HD2  H N N 208 
HIS   HE1  H N N 209 
HIS   HE2  H N N 210 
HIS   HXT  H N N 211 
HOH   O    O N N 212 
HOH   H1   H N N 213 
HOH   H2   H N N 214 
ILE   N    N N N 215 
ILE   CA   C N S 216 
ILE   C    C N N 217 
ILE   O    O N N 218 
ILE   CB   C N S 219 
ILE   CG1  C N N 220 
ILE   CG2  C N N 221 
ILE   CD1  C N N 222 
ILE   OXT  O N N 223 
ILE   H    H N N 224 
ILE   H2   H N N 225 
ILE   HA   H N N 226 
ILE   HB   H N N 227 
ILE   HG12 H N N 228 
ILE   HG13 H N N 229 
ILE   HG21 H N N 230 
ILE   HG22 H N N 231 
ILE   HG23 H N N 232 
ILE   HD11 H N N 233 
ILE   HD12 H N N 234 
ILE   HD13 H N N 235 
ILE   HXT  H N N 236 
LEU   N    N N N 237 
LEU   CA   C N S 238 
LEU   C    C N N 239 
LEU   O    O N N 240 
LEU   CB   C N N 241 
LEU   CG   C N N 242 
LEU   CD1  C N N 243 
LEU   CD2  C N N 244 
LEU   OXT  O N N 245 
LEU   H    H N N 246 
LEU   H2   H N N 247 
LEU   HA   H N N 248 
LEU   HB2  H N N 249 
LEU   HB3  H N N 250 
LEU   HG   H N N 251 
LEU   HD11 H N N 252 
LEU   HD12 H N N 253 
LEU   HD13 H N N 254 
LEU   HD21 H N N 255 
LEU   HD22 H N N 256 
LEU   HD23 H N N 257 
LEU   HXT  H N N 258 
LYS   N    N N N 259 
LYS   CA   C N S 260 
LYS   C    C N N 261 
LYS   O    O N N 262 
LYS   CB   C N N 263 
LYS   CG   C N N 264 
LYS   CD   C N N 265 
LYS   CE   C N N 266 
LYS   NZ   N N N 267 
LYS   OXT  O N N 268 
LYS   H    H N N 269 
LYS   H2   H N N 270 
LYS   HA   H N N 271 
LYS   HB2  H N N 272 
LYS   HB3  H N N 273 
LYS   HG2  H N N 274 
LYS   HG3  H N N 275 
LYS   HD2  H N N 276 
LYS   HD3  H N N 277 
LYS   HE2  H N N 278 
LYS   HE3  H N N 279 
LYS   HZ1  H N N 280 
LYS   HZ2  H N N 281 
LYS   HZ3  H N N 282 
LYS   HXT  H N N 283 
MET   N    N N N 284 
MET   CA   C N S 285 
MET   C    C N N 286 
MET   O    O N N 287 
MET   CB   C N N 288 
MET   CG   C N N 289 
MET   SD   S N N 290 
MET   CE   C N N 291 
MET   OXT  O N N 292 
MET   H    H N N 293 
MET   H2   H N N 294 
MET   HA   H N N 295 
MET   HB2  H N N 296 
MET   HB3  H N N 297 
MET   HG2  H N N 298 
MET   HG3  H N N 299 
MET   HE1  H N N 300 
MET   HE2  H N N 301 
MET   HE3  H N N 302 
MET   HXT  H N N 303 
PHE   N    N N N 304 
PHE   CA   C N S 305 
PHE   C    C N N 306 
PHE   O    O N N 307 
PHE   CB   C N N 308 
PHE   CG   C Y N 309 
PHE   CD1  C Y N 310 
PHE   CD2  C Y N 311 
PHE   CE1  C Y N 312 
PHE   CE2  C Y N 313 
PHE   CZ   C Y N 314 
PHE   OXT  O N N 315 
PHE   H    H N N 316 
PHE   H2   H N N 317 
PHE   HA   H N N 318 
PHE   HB2  H N N 319 
PHE   HB3  H N N 320 
PHE   HD1  H N N 321 
PHE   HD2  H N N 322 
PHE   HE1  H N N 323 
PHE   HE2  H N N 324 
PHE   HZ   H N N 325 
PHE   HXT  H N N 326 
PRO   N    N N N 327 
PRO   CA   C N S 328 
PRO   C    C N N 329 
PRO   O    O N N 330 
PRO   CB   C N N 331 
PRO   CG   C N N 332 
PRO   CD   C N N 333 
PRO   OXT  O N N 334 
PRO   H    H N N 335 
PRO   HA   H N N 336 
PRO   HB2  H N N 337 
PRO   HB3  H N N 338 
PRO   HG2  H N N 339 
PRO   HG3  H N N 340 
PRO   HD2  H N N 341 
PRO   HD3  H N N 342 
PRO   HXT  H N N 343 
SER   N    N N N 344 
SER   CA   C N S 345 
SER   C    C N N 346 
SER   O    O N N 347 
SER   CB   C N N 348 
SER   OG   O N N 349 
SER   OXT  O N N 350 
SER   H    H N N 351 
SER   H2   H N N 352 
SER   HA   H N N 353 
SER   HB2  H N N 354 
SER   HB3  H N N 355 
SER   HG   H N N 356 
SER   HXT  H N N 357 
THR   N    N N N 358 
THR   CA   C N S 359 
THR   C    C N N 360 
THR   O    O N N 361 
THR   CB   C N R 362 
THR   OG1  O N N 363 
THR   CG2  C N N 364 
THR   OXT  O N N 365 
THR   H    H N N 366 
THR   H2   H N N 367 
THR   HA   H N N 368 
THR   HB   H N N 369 
THR   HG1  H N N 370 
THR   HG21 H N N 371 
THR   HG22 H N N 372 
THR   HG23 H N N 373 
THR   HXT  H N N 374 
TRP   N    N N N 375 
TRP   CA   C N S 376 
TRP   C    C N N 377 
TRP   O    O N N 378 
TRP   CB   C N N 379 
TRP   CG   C Y N 380 
TRP   CD1  C Y N 381 
TRP   CD2  C Y N 382 
TRP   NE1  N Y N 383 
TRP   CE2  C Y N 384 
TRP   CE3  C Y N 385 
TRP   CZ2  C Y N 386 
TRP   CZ3  C Y N 387 
TRP   CH2  C Y N 388 
TRP   OXT  O N N 389 
TRP   H    H N N 390 
TRP   H2   H N N 391 
TRP   HA   H N N 392 
TRP   HB2  H N N 393 
TRP   HB3  H N N 394 
TRP   HD1  H N N 395 
TRP   HE1  H N N 396 
TRP   HE3  H N N 397 
TRP   HZ2  H N N 398 
TRP   HZ3  H N N 399 
TRP   HH2  H N N 400 
TRP   HXT  H N N 401 
TYR   N    N N N 402 
TYR   CA   C N S 403 
TYR   C    C N N 404 
TYR   O    O N N 405 
TYR   CB   C N N 406 
TYR   CG   C Y N 407 
TYR   CD1  C Y N 408 
TYR   CD2  C Y N 409 
TYR   CE1  C Y N 410 
TYR   CE2  C Y N 411 
TYR   CZ   C Y N 412 
TYR   OH   O N N 413 
TYR   OXT  O N N 414 
TYR   H    H N N 415 
TYR   H2   H N N 416 
TYR   HA   H N N 417 
TYR   HB2  H N N 418 
TYR   HB3  H N N 419 
TYR   HD1  H N N 420 
TYR   HD2  H N N 421 
TYR   HE1  H N N 422 
TYR   HE2  H N N 423 
TYR   HH   H N N 424 
TYR   HXT  H N N 425 
VAL   N    N N N 426 
VAL   CA   C N S 427 
VAL   C    C N N 428 
VAL   O    O N N 429 
VAL   CB   C N N 430 
VAL   CG1  C N N 431 
VAL   CG2  C N N 432 
VAL   OXT  O N N 433 
VAL   H    H N N 434 
VAL   H2   H N N 435 
VAL   HA   H N N 436 
VAL   HB   H N N 437 
VAL   HG11 H N N 438 
VAL   HG12 H N N 439 
VAL   HG13 H N N 440 
VAL   HG21 H N N 441 
VAL   HG22 H N N 442 
VAL   HG23 H N N 443 
VAL   HXT  H N N 444 
# 
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 
A1H98 C01 C02  sing N N 1   
A1H98 C24 C25  sing N N 2   
A1H98 C24 C23  sing N N 3   
A1H98 C22 C20  sing N N 4   
A1H98 C20 O21  doub N N 5   
A1H98 C20 C19  sing N N 6   
A1H98 O14 C13  doub N N 7   
A1H98 C02 C03  sing N N 8   
A1H98 C23 C19  sing Y N 9   
A1H98 C23 C15  doub Y N 10  
A1H98 C19 C17  doub Y N 11  
A1H98 C15 C13  sing N N 12  
A1H98 C15 N16  sing Y N 13  
A1H98 C13 N10  sing N N 14  
A1H98 C17 N16  sing Y N 15  
A1H98 C17 C18  sing N N 16  
A1H98 C03 N04  doub Y N 17  
A1H98 C03 O27  sing Y N 18  
A1H98 N04 C05  sing Y N 19  
A1H98 N10 C11  sing N N 20  
A1H98 N10 C09  sing N N 21  
A1H98 O27 N26  sing Y N 22  
A1H98 C11 C12  sing N N 23  
A1H98 C12 N07  sing N N 24  
A1H98 C05 N26  doub Y N 25  
A1H98 C05 C06  sing N N 26  
A1H98 C09 C08  sing N N 27  
A1H98 C08 N07  sing N N 28  
A1H98 N07 C06  sing N N 29  
A1H98 C01 H1   sing N N 30  
A1H98 C01 H2   sing N N 31  
A1H98 C01 H3   sing N N 32  
A1H98 C02 H4   sing N N 33  
A1H98 C02 H5   sing N N 34  
A1H98 C06 H6   sing N N 35  
A1H98 C06 H7   sing N N 36  
A1H98 C08 H8   sing N N 37  
A1H98 C08 H9   sing N N 38  
A1H98 C09 H10  sing N N 39  
A1H98 C09 H11  sing N N 40  
A1H98 C11 H12  sing N N 41  
A1H98 C11 H13  sing N N 42  
A1H98 C12 H14  sing N N 43  
A1H98 C12 H15  sing N N 44  
A1H98 C18 H16  sing N N 45  
A1H98 C18 H17  sing N N 46  
A1H98 C18 H18  sing N N 47  
A1H98 C22 H19  sing N N 48  
A1H98 C22 H20  sing N N 49  
A1H98 C22 H21  sing N N 50  
A1H98 C24 H22  sing N N 51  
A1H98 C24 H23  sing N N 52  
A1H98 C25 H24  sing N N 53  
A1H98 C25 H25  sing N N 54  
A1H98 C25 H26  sing N N 55  
A1H98 N16 H28  sing N N 56  
ALA   N   CA   sing N N 57  
ALA   N   H    sing N N 58  
ALA   N   H2   sing N N 59  
ALA   CA  C    sing N N 60  
ALA   CA  CB   sing N N 61  
ALA   CA  HA   sing N N 62  
ALA   C   O    doub N N 63  
ALA   C   OXT  sing N N 64  
ALA   CB  HB1  sing N N 65  
ALA   CB  HB2  sing N N 66  
ALA   CB  HB3  sing N N 67  
ALA   OXT HXT  sing N N 68  
ARG   N   CA   sing N N 69  
ARG   N   H    sing N N 70  
ARG   N   H2   sing N N 71  
ARG   CA  C    sing N N 72  
ARG   CA  CB   sing N N 73  
ARG   CA  HA   sing N N 74  
ARG   C   O    doub N N 75  
ARG   C   OXT  sing N N 76  
ARG   CB  CG   sing N N 77  
ARG   CB  HB2  sing N N 78  
ARG   CB  HB3  sing N N 79  
ARG   CG  CD   sing N N 80  
ARG   CG  HG2  sing N N 81  
ARG   CG  HG3  sing N N 82  
ARG   CD  NE   sing N N 83  
ARG   CD  HD2  sing N N 84  
ARG   CD  HD3  sing N N 85  
ARG   NE  CZ   sing N N 86  
ARG   NE  HE   sing N N 87  
ARG   CZ  NH1  sing N N 88  
ARG   CZ  NH2  doub N N 89  
ARG   NH1 HH11 sing N N 90  
ARG   NH1 HH12 sing N N 91  
ARG   NH2 HH21 sing N N 92  
ARG   NH2 HH22 sing N N 93  
ARG   OXT HXT  sing N N 94  
ASN   N   CA   sing N N 95  
ASN   N   H    sing N N 96  
ASN   N   H2   sing N N 97  
ASN   CA  C    sing N N 98  
ASN   CA  CB   sing N N 99  
ASN   CA  HA   sing N N 100 
ASN   C   O    doub N N 101 
ASN   C   OXT  sing N N 102 
ASN   CB  CG   sing N N 103 
ASN   CB  HB2  sing N N 104 
ASN   CB  HB3  sing N N 105 
ASN   CG  OD1  doub N N 106 
ASN   CG  ND2  sing N N 107 
ASN   ND2 HD21 sing N N 108 
ASN   ND2 HD22 sing N N 109 
ASN   OXT HXT  sing N N 110 
ASP   N   CA   sing N N 111 
ASP   N   H    sing N N 112 
ASP   N   H2   sing N N 113 
ASP   CA  C    sing N N 114 
ASP   CA  CB   sing N N 115 
ASP   CA  HA   sing N N 116 
ASP   C   O    doub N N 117 
ASP   C   OXT  sing N N 118 
ASP   CB  CG   sing N N 119 
ASP   CB  HB2  sing N N 120 
ASP   CB  HB3  sing N N 121 
ASP   CG  OD1  doub N N 122 
ASP   CG  OD2  sing N N 123 
ASP   OD2 HD2  sing N N 124 
ASP   OXT HXT  sing N N 125 
CYS   N   CA   sing N N 126 
CYS   N   H    sing N N 127 
CYS   N   H2   sing N N 128 
CYS   CA  C    sing N N 129 
CYS   CA  CB   sing N N 130 
CYS   CA  HA   sing N N 131 
CYS   C   O    doub N N 132 
CYS   C   OXT  sing N N 133 
CYS   CB  SG   sing N N 134 
CYS   CB  HB2  sing N N 135 
CYS   CB  HB3  sing N N 136 
CYS   SG  HG   sing N N 137 
CYS   OXT HXT  sing N N 138 
GLN   N   CA   sing N N 139 
GLN   N   H    sing N N 140 
GLN   N   H2   sing N N 141 
GLN   CA  C    sing N N 142 
GLN   CA  CB   sing N N 143 
GLN   CA  HA   sing N N 144 
GLN   C   O    doub N N 145 
GLN   C   OXT  sing N N 146 
GLN   CB  CG   sing N N 147 
GLN   CB  HB2  sing N N 148 
GLN   CB  HB3  sing N N 149 
GLN   CG  CD   sing N N 150 
GLN   CG  HG2  sing N N 151 
GLN   CG  HG3  sing N N 152 
GLN   CD  OE1  doub N N 153 
GLN   CD  NE2  sing N N 154 
GLN   NE2 HE21 sing N N 155 
GLN   NE2 HE22 sing N N 156 
GLN   OXT HXT  sing N N 157 
GLU   N   CA   sing N N 158 
GLU   N   H    sing N N 159 
GLU   N   H2   sing N N 160 
GLU   CA  C    sing N N 161 
GLU   CA  CB   sing N N 162 
GLU   CA  HA   sing N N 163 
GLU   C   O    doub N N 164 
GLU   C   OXT  sing N N 165 
GLU   CB  CG   sing N N 166 
GLU   CB  HB2  sing N N 167 
GLU   CB  HB3  sing N N 168 
GLU   CG  CD   sing N N 169 
GLU   CG  HG2  sing N N 170 
GLU   CG  HG3  sing N N 171 
GLU   CD  OE1  doub N N 172 
GLU   CD  OE2  sing N N 173 
GLU   OE2 HE2  sing N N 174 
GLU   OXT HXT  sing N N 175 
GLY   N   CA   sing N N 176 
GLY   N   H    sing N N 177 
GLY   N   H2   sing N N 178 
GLY   CA  C    sing N N 179 
GLY   CA  HA2  sing N N 180 
GLY   CA  HA3  sing N N 181 
GLY   C   O    doub N N 182 
GLY   C   OXT  sing N N 183 
GLY   OXT HXT  sing N N 184 
HIS   N   CA   sing N N 185 
HIS   N   H    sing N N 186 
HIS   N   H2   sing N N 187 
HIS   CA  C    sing N N 188 
HIS   CA  CB   sing N N 189 
HIS   CA  HA   sing N N 190 
HIS   C   O    doub N N 191 
HIS   C   OXT  sing N N 192 
HIS   CB  CG   sing N N 193 
HIS   CB  HB2  sing N N 194 
HIS   CB  HB3  sing N N 195 
HIS   CG  ND1  sing Y N 196 
HIS   CG  CD2  doub Y N 197 
HIS   ND1 CE1  doub Y N 198 
HIS   ND1 HD1  sing N N 199 
HIS   CD2 NE2  sing Y N 200 
HIS   CD2 HD2  sing N N 201 
HIS   CE1 NE2  sing Y N 202 
HIS   CE1 HE1  sing N N 203 
HIS   NE2 HE2  sing N N 204 
HIS   OXT HXT  sing N N 205 
HOH   O   H1   sing N N 206 
HOH   O   H2   sing N N 207 
ILE   N   CA   sing N N 208 
ILE   N   H    sing N N 209 
ILE   N   H2   sing N N 210 
ILE   CA  C    sing N N 211 
ILE   CA  CB   sing N N 212 
ILE   CA  HA   sing N N 213 
ILE   C   O    doub N N 214 
ILE   C   OXT  sing N N 215 
ILE   CB  CG1  sing N N 216 
ILE   CB  CG2  sing N N 217 
ILE   CB  HB   sing N N 218 
ILE   CG1 CD1  sing N N 219 
ILE   CG1 HG12 sing N N 220 
ILE   CG1 HG13 sing N N 221 
ILE   CG2 HG21 sing N N 222 
ILE   CG2 HG22 sing N N 223 
ILE   CG2 HG23 sing N N 224 
ILE   CD1 HD11 sing N N 225 
ILE   CD1 HD12 sing N N 226 
ILE   CD1 HD13 sing N N 227 
ILE   OXT HXT  sing N N 228 
LEU   N   CA   sing N N 229 
LEU   N   H    sing N N 230 
LEU   N   H2   sing N N 231 
LEU   CA  C    sing N N 232 
LEU   CA  CB   sing N N 233 
LEU   CA  HA   sing N N 234 
LEU   C   O    doub N N 235 
LEU   C   OXT  sing N N 236 
LEU   CB  CG   sing N N 237 
LEU   CB  HB2  sing N N 238 
LEU   CB  HB3  sing N N 239 
LEU   CG  CD1  sing N N 240 
LEU   CG  CD2  sing N N 241 
LEU   CG  HG   sing N N 242 
LEU   CD1 HD11 sing N N 243 
LEU   CD1 HD12 sing N N 244 
LEU   CD1 HD13 sing N N 245 
LEU   CD2 HD21 sing N N 246 
LEU   CD2 HD22 sing N N 247 
LEU   CD2 HD23 sing N N 248 
LEU   OXT HXT  sing N N 249 
LYS   N   CA   sing N N 250 
LYS   N   H    sing N N 251 
LYS   N   H2   sing N N 252 
LYS   CA  C    sing N N 253 
LYS   CA  CB   sing N N 254 
LYS   CA  HA   sing N N 255 
LYS   C   O    doub N N 256 
LYS   C   OXT  sing N N 257 
LYS   CB  CG   sing N N 258 
LYS   CB  HB2  sing N N 259 
LYS   CB  HB3  sing N N 260 
LYS   CG  CD   sing N N 261 
LYS   CG  HG2  sing N N 262 
LYS   CG  HG3  sing N N 263 
LYS   CD  CE   sing N N 264 
LYS   CD  HD2  sing N N 265 
LYS   CD  HD3  sing N N 266 
LYS   CE  NZ   sing N N 267 
LYS   CE  HE2  sing N N 268 
LYS   CE  HE3  sing N N 269 
LYS   NZ  HZ1  sing N N 270 
LYS   NZ  HZ2  sing N N 271 
LYS   NZ  HZ3  sing N N 272 
LYS   OXT HXT  sing N N 273 
MET   N   CA   sing N N 274 
MET   N   H    sing N N 275 
MET   N   H2   sing N N 276 
MET   CA  C    sing N N 277 
MET   CA  CB   sing N N 278 
MET   CA  HA   sing N N 279 
MET   C   O    doub N N 280 
MET   C   OXT  sing N N 281 
MET   CB  CG   sing N N 282 
MET   CB  HB2  sing N N 283 
MET   CB  HB3  sing N N 284 
MET   CG  SD   sing N N 285 
MET   CG  HG2  sing N N 286 
MET   CG  HG3  sing N N 287 
MET   SD  CE   sing N N 288 
MET   CE  HE1  sing N N 289 
MET   CE  HE2  sing N N 290 
MET   CE  HE3  sing N N 291 
MET   OXT HXT  sing N N 292 
PHE   N   CA   sing N N 293 
PHE   N   H    sing N N 294 
PHE   N   H2   sing N N 295 
PHE   CA  C    sing N N 296 
PHE   CA  CB   sing N N 297 
PHE   CA  HA   sing N N 298 
PHE   C   O    doub N N 299 
PHE   C   OXT  sing N N 300 
PHE   CB  CG   sing N N 301 
PHE   CB  HB2  sing N N 302 
PHE   CB  HB3  sing N N 303 
PHE   CG  CD1  doub Y N 304 
PHE   CG  CD2  sing Y N 305 
PHE   CD1 CE1  sing Y N 306 
PHE   CD1 HD1  sing N N 307 
PHE   CD2 CE2  doub Y N 308 
PHE   CD2 HD2  sing N N 309 
PHE   CE1 CZ   doub Y N 310 
PHE   CE1 HE1  sing N N 311 
PHE   CE2 CZ   sing Y N 312 
PHE   CE2 HE2  sing N N 313 
PHE   CZ  HZ   sing N N 314 
PHE   OXT HXT  sing N N 315 
PRO   N   CA   sing N N 316 
PRO   N   CD   sing N N 317 
PRO   N   H    sing N N 318 
PRO   CA  C    sing N N 319 
PRO   CA  CB   sing N N 320 
PRO   CA  HA   sing N N 321 
PRO   C   O    doub N N 322 
PRO   C   OXT  sing N N 323 
PRO   CB  CG   sing N N 324 
PRO   CB  HB2  sing N N 325 
PRO   CB  HB3  sing N N 326 
PRO   CG  CD   sing N N 327 
PRO   CG  HG2  sing N N 328 
PRO   CG  HG3  sing N N 329 
PRO   CD  HD2  sing N N 330 
PRO   CD  HD3  sing N N 331 
PRO   OXT HXT  sing N N 332 
SER   N   CA   sing N N 333 
SER   N   H    sing N N 334 
SER   N   H2   sing N N 335 
SER   CA  C    sing N N 336 
SER   CA  CB   sing N N 337 
SER   CA  HA   sing N N 338 
SER   C   O    doub N N 339 
SER   C   OXT  sing N N 340 
SER   CB  OG   sing N N 341 
SER   CB  HB2  sing N N 342 
SER   CB  HB3  sing N N 343 
SER   OG  HG   sing N N 344 
SER   OXT HXT  sing N N 345 
THR   N   CA   sing N N 346 
THR   N   H    sing N N 347 
THR   N   H2   sing N N 348 
THR   CA  C    sing N N 349 
THR   CA  CB   sing N N 350 
THR   CA  HA   sing N N 351 
THR   C   O    doub N N 352 
THR   C   OXT  sing N N 353 
THR   CB  OG1  sing N N 354 
THR   CB  CG2  sing N N 355 
THR   CB  HB   sing N N 356 
THR   OG1 HG1  sing N N 357 
THR   CG2 HG21 sing N N 358 
THR   CG2 HG22 sing N N 359 
THR   CG2 HG23 sing N N 360 
THR   OXT HXT  sing N N 361 
TRP   N   CA   sing N N 362 
TRP   N   H    sing N N 363 
TRP   N   H2   sing N N 364 
TRP   CA  C    sing N N 365 
TRP   CA  CB   sing N N 366 
TRP   CA  HA   sing N N 367 
TRP   C   O    doub N N 368 
TRP   C   OXT  sing N N 369 
TRP   CB  CG   sing N N 370 
TRP   CB  HB2  sing N N 371 
TRP   CB  HB3  sing N N 372 
TRP   CG  CD1  doub Y N 373 
TRP   CG  CD2  sing Y N 374 
TRP   CD1 NE1  sing Y N 375 
TRP   CD1 HD1  sing N N 376 
TRP   CD2 CE2  doub Y N 377 
TRP   CD2 CE3  sing Y N 378 
TRP   NE1 CE2  sing Y N 379 
TRP   NE1 HE1  sing N N 380 
TRP   CE2 CZ2  sing Y N 381 
TRP   CE3 CZ3  doub Y N 382 
TRP   CE3 HE3  sing N N 383 
TRP   CZ2 CH2  doub Y N 384 
TRP   CZ2 HZ2  sing N N 385 
TRP   CZ3 CH2  sing Y N 386 
TRP   CZ3 HZ3  sing N N 387 
TRP   CH2 HH2  sing N N 388 
TRP   OXT HXT  sing N N 389 
TYR   N   CA   sing N N 390 
TYR   N   H    sing N N 391 
TYR   N   H2   sing N N 392 
TYR   CA  C    sing N N 393 
TYR   CA  CB   sing N N 394 
TYR   CA  HA   sing N N 395 
TYR   C   O    doub N N 396 
TYR   C   OXT  sing N N 397 
TYR   CB  CG   sing N N 398 
TYR   CB  HB2  sing N N 399 
TYR   CB  HB3  sing N N 400 
TYR   CG  CD1  doub Y N 401 
TYR   CG  CD2  sing Y N 402 
TYR   CD1 CE1  sing Y N 403 
TYR   CD1 HD1  sing N N 404 
TYR   CD2 CE2  doub Y N 405 
TYR   CD2 HD2  sing N N 406 
TYR   CE1 CZ   doub Y N 407 
TYR   CE1 HE1  sing N N 408 
TYR   CE2 CZ   sing Y N 409 
TYR   CE2 HE2  sing N N 410 
TYR   CZ  OH   sing N N 411 
TYR   OH  HH   sing N N 412 
TYR   OXT HXT  sing N N 413 
VAL   N   CA   sing N N 414 
VAL   N   H    sing N N 415 
VAL   N   H2   sing N N 416 
VAL   CA  C    sing N N 417 
VAL   CA  CB   sing N N 418 
VAL   CA  HA   sing N N 419 
VAL   C   O    doub N N 420 
VAL   C   OXT  sing N N 421 
VAL   CB  CG1  sing N N 422 
VAL   CB  CG2  sing N N 423 
VAL   CB  HB   sing N N 424 
VAL   CG1 HG11 sing N N 425 
VAL   CG1 HG12 sing N N 426 
VAL   CG1 HG13 sing N N 427 
VAL   CG2 HG21 sing N N 428 
VAL   CG2 HG22 sing N N 429 
VAL   CG2 HG23 sing N N 430 
VAL   OXT HXT  sing N N 431 
# 
_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                    9F78 
_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]   0.023243 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   0.018396 
_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]   0.011092 
_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 
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   . SER   A 1 4   ? -15.782 3.679   40.599 1.00 58.88 ? 1797 SER   A N   1 
ATOM   2    C CA  . SER   A 1 4   ? -16.894 4.122   39.764 1.00 61.82 ? 1797 SER   A CA  1 
ATOM   3    C C   . SER   A 1 4   ? -16.433 4.263   38.320 1.00 61.27 ? 1797 SER   A C   1 
ATOM   4    O O   . SER   A 1 4   ? -17.049 3.715   37.407 1.00 56.94 ? 1797 SER   A O   1 
ATOM   5    C CB  . SER   A 1 4   ? -17.471 5.446   40.277 1.00 61.40 ? 1797 SER   A CB  1 
ATOM   6    O OG  . SER   A 1 4   ? -18.532 5.906   39.451 1.00 60.44 ? 1797 SER   A OG  1 
ATOM   7    N N   . ASP   A 1 5   ? -15.344 5.009   38.114 1.00 67.79 ? 1798 ASP   A N   1 
ATOM   8    C CA  . ASP   A 1 5   ? -14.731 5.059   36.790 1.00 61.80 ? 1798 ASP   A CA  1 
ATOM   9    C C   . ASP   A 1 5   ? -14.215 3.685   36.389 1.00 55.60 ? 1798 ASP   A C   1 
ATOM   10   O O   . ASP   A 1 5   ? -14.435 3.231   35.259 1.00 45.16 ? 1798 ASP   A O   1 
ATOM   11   C CB  . ASP   A 1 5   ? -13.600 6.089   36.762 1.00 62.17 ? 1798 ASP   A CB  1 
ATOM   12   C CG  . ASP   A 1 5   ? -14.099 7.513   36.923 1.00 69.37 ? 1798 ASP   A CG  1 
ATOM   13   O OD1 . ASP   A 1 5   ? -15.327 7.710   37.053 1.00 71.37 ? 1798 ASP   A OD1 1 
ATOM   14   O OD2 . ASP   A 1 5   ? -13.258 8.438   36.923 1.00 72.33 ? 1798 ASP   A OD2 1 
ATOM   15   N N   . LEU   A 1 6   ? -13.536 2.999   37.313 1.00 53.51 ? 1799 LEU   A N   1 
ATOM   16   C CA  . LEU   A 1 6   ? -13.090 1.641   37.027 1.00 47.73 ? 1799 LEU   A CA  1 
ATOM   17   C C   . LEU   A 1 6   ? -14.268 0.691   36.893 1.00 34.41 ? 1799 LEU   A C   1 
ATOM   18   O O   . LEU   A 1 6   ? -14.195 -0.271  36.123 1.00 42.26 ? 1799 LEU   A O   1 
ATOM   19   C CB  . LEU   A 1 6   ? -12.126 1.148   38.107 1.00 45.27 ? 1799 LEU   A CB  1 
ATOM   20   C CG  . LEU   A 1 6   ? -10.651 1.457   37.845 1.00 39.82 ? 1799 LEU   A CG  1 
ATOM   21   C CD1 . LEU   A 1 6   ? -10.251 0.993   36.463 1.00 40.06 ? 1799 LEU   A CD1 1 
ATOM   22   C CD2 . LEU   A 1 6   ? -10.392 2.944   38.025 1.00 45.16 ? 1799 LEU   A CD2 1 
ATOM   23   N N   . THR   A 1 7   ? -15.356 0.944   37.625 1.00 37.95 ? 1800 THR   A N   1 
ATOM   24   C CA  . THR   A 1 7   ? -16.601 0.219   37.385 1.00 45.19 ? 1800 THR   A CA  1 
ATOM   25   C C   . THR   A 1 7   ? -16.995 0.274   35.911 1.00 41.96 ? 1800 THR   A C   1 
ATOM   26   O O   . THR   A 1 7   ? -17.296 -0.757  35.298 1.00 49.45 ? 1800 THR   A O   1 
ATOM   27   C CB  . THR   A 1 7   ? -17.720 0.789   38.258 1.00 41.67 ? 1800 THR   A CB  1 
ATOM   28   O OG1 . THR   A 1 7   ? -17.489 0.443   39.634 1.00 45.00 ? 1800 THR   A OG1 1 
ATOM   29   C CG2 . THR   A 1 7   ? -19.052 0.242   37.806 1.00 40.08 ? 1800 THR   A CG2 1 
ATOM   30   N N   . PHE   A 1 8   ? -16.985 1.476   35.321 1.00 35.85 ? 1801 PHE   A N   1 
ATOM   31   C CA  . PHE   A 1 8   ? -17.264 1.594   33.893 1.00 36.16 ? 1801 PHE   A CA  1 
ATOM   32   C C   . PHE   A 1 8   ? -16.262 0.789   33.068 1.00 33.89 ? 1801 PHE   A C   1 
ATOM   33   O O   . PHE   A 1 8   ? -16.624 0.202   32.039 1.00 38.51 ? 1801 PHE   A O   1 
ATOM   34   C CB  . PHE   A 1 8   ? -17.239 3.060   33.457 1.00 39.45 ? 1801 PHE   A CB  1 
ATOM   35   C CG  . PHE   A 1 8   ? -18.239 3.937   34.164 1.00 49.82 ? 1801 PHE   A CG  1 
ATOM   36   C CD1 . PHE   A 1 8   ? -19.525 3.492   34.422 1.00 55.91 ? 1801 PHE   A CD1 1 
ATOM   37   C CD2 . PHE   A 1 8   ? -17.888 5.221   34.560 1.00 47.74 ? 1801 PHE   A CD2 1 
ATOM   38   C CE1 . PHE   A 1 8   ? -20.443 4.309   35.068 1.00 62.18 ? 1801 PHE   A CE1 1 
ATOM   39   C CE2 . PHE   A 1 8   ? -18.797 6.042   35.202 1.00 55.78 ? 1801 PHE   A CE2 1 
ATOM   40   C CZ  . PHE   A 1 8   ? -20.076 5.585   35.458 1.00 59.52 ? 1801 PHE   A CZ  1 
ATOM   41   N N   . CYS   A 1 9   ? -14.995 0.747   33.506 1.00 29.53 ? 1802 CYS   A N   1 
ATOM   42   C CA  . CYS   A 1 9   ? -13.964 0.030   32.757 1.00 26.09 ? 1802 CYS   A CA  1 
ATOM   43   C C   . CYS   A 1 9   ? -14.218 -1.475  32.733 1.00 29.09 ? 1802 CYS   A C   1 
ATOM   44   O O   . CYS   A 1 9   ? -13.967 -2.135  31.715 1.00 26.59 ? 1802 CYS   A O   1 
ATOM   45   C CB  . CYS   A 1 9   ? -12.576 0.344   33.320 1.00 25.59 ? 1802 CYS   A CB  1 
ATOM   46   S SG  . CYS   A 1 9   ? -12.023 2.055   33.022 1.00 31.51 ? 1802 CYS   A SG  1 
ATOM   47   N N   . GLU   A 1 10  ? -14.713 -2.042  33.831 1.00 29.90 ? 1803 GLU   A N   1 
ATOM   48   C CA  A GLU   A 1 10  ? -15.106 -3.447  33.825 0.58 29.51 ? 1803 GLU   A CA  1 
ATOM   49   C CA  B GLU   A 1 10  ? -15.101 -3.447  33.820 0.42 29.44 ? 1803 GLU   A CA  1 
ATOM   50   C C   . GLU   A 1 10  ? -16.155 -3.711  32.749 1.00 32.55 ? 1803 GLU   A C   1 
ATOM   51   O O   . GLU   A 1 10  ? -16.039 -4.664  31.967 1.00 28.52 ? 1803 GLU   A O   1 
ATOM   52   C CB  A GLU   A 1 10  ? -15.639 -3.850  35.202 0.58 29.53 ? 1803 GLU   A CB  1 
ATOM   53   C CB  B GLU   A 1 10  ? -15.612 -3.860  35.201 0.42 32.30 ? 1803 GLU   A CB  1 
ATOM   54   C CG  A GLU   A 1 10  ? -15.536 -5.340  35.529 0.58 39.49 ? 1803 GLU   A CG  1 
ATOM   55   C CG  B GLU   A 1 10  ? -14.823 -3.254  36.345 0.42 32.91 ? 1803 GLU   A CG  1 
ATOM   56   C CD  A GLU   A 1 10  ? -16.147 -6.247  34.466 0.58 38.22 ? 1803 GLU   A CD  1 
ATOM   57   C CD  B GLU   A 1 10  ? -14.589 -4.222  37.481 0.42 45.05 ? 1803 GLU   A CD  1 
ATOM   58   O OE1 A GLU   A 1 10  ? -15.440 -7.156  33.990 0.58 40.20 ? 1803 GLU   A OE1 1 
ATOM   59   O OE1 B GLU   A 1 10  ? -14.943 -5.411  37.332 0.42 47.55 ? 1803 GLU   A OE1 1 
ATOM   60   O OE2 A GLU   A 1 10  ? -17.329 -6.049  34.105 0.58 43.06 ? 1803 GLU   A OE2 1 
ATOM   61   O OE2 B GLU   A 1 10  ? -14.046 -3.793  38.520 0.42 47.15 ? 1803 GLU   A OE2 1 
ATOM   62   N N   . ILE   A 1 11  ? -17.191 -2.872  32.695 1.00 33.01 ? 1804 ILE   A N   1 
ATOM   63   C CA  . ILE   A 1 11  ? -18.250 -3.063  31.706 1.00 37.97 ? 1804 ILE   A CA  1 
ATOM   64   C C   . ILE   A 1 11  ? -17.693 -2.913  30.300 1.00 34.26 ? 1804 ILE   A C   1 
ATOM   65   O O   . ILE   A 1 11  ? -17.971 -3.730  29.415 1.00 30.98 ? 1804 ILE   A O   1 
ATOM   66   C CB  . ILE   A 1 11  ? -19.407 -2.084  31.958 1.00 35.90 ? 1804 ILE   A CB  1 
ATOM   67   C CG1 . ILE   A 1 11  ? -20.151 -2.476  33.230 1.00 42.77 ? 1804 ILE   A CG1 1 
ATOM   68   C CG2 . ILE   A 1 11  ? -20.357 -2.069  30.761 1.00 36.69 ? 1804 ILE   A CG2 1 
ATOM   69   C CD1 . ILE   A 1 11  ? -20.782 -3.858  33.163 1.00 40.73 ? 1804 ILE   A CD1 1 
ATOM   70   N N   . ILE   A 1 12  ? -16.885 -1.873  30.079 1.00 26.46 ? 1805 ILE   A N   1 
ATOM   71   C CA  . ILE   A 1 12  ? -16.325 -1.644  28.748 1.00 32.33 ? 1805 ILE   A CA  1 
ATOM   72   C C   . ILE   A 1 12  ? -15.493 -2.840  28.313 1.00 30.36 ? 1805 ILE   A C   1 
ATOM   73   O O   . ILE   A 1 12  ? -15.581 -3.297  27.165 1.00 31.89 ? 1805 ILE   A O   1 
ATOM   74   C CB  . ILE   A 1 12  ? -15.507 -0.340  28.726 1.00 34.46 ? 1805 ILE   A CB  1 
ATOM   75   C CG1 . ILE   A 1 12  ? -16.438 0.870   28.808 1.00 33.79 ? 1805 ILE   A CG1 1 
ATOM   76   C CG2 . ILE   A 1 12  ? -14.639 -0.263  27.476 1.00 33.56 ? 1805 ILE   A CG2 1 
ATOM   77   C CD1 . ILE   A 1 12  ? -15.702 2.196   28.859 1.00 39.11 ? 1805 ILE   A CD1 1 
ATOM   78   N N   . LEU   A 1 13  ? -14.692 -3.386  29.232 1.00 27.62 ? 1806 LEU   A N   1 
ATOM   79   C CA  . LEU   A 1 13  ? -13.849 -4.525  28.884 1.00 26.56 ? 1806 LEU   A CA  1 
ATOM   80   C C   . LEU   A 1 13  ? -14.689 -5.754  28.561 1.00 23.62 ? 1806 LEU   A C   1 
ATOM   81   O O   . LEU   A 1 13  ? -14.389 -6.480  27.604 1.00 23.03 ? 1806 LEU   A O   1 
ATOM   82   C CB  . LEU   A 1 13  ? -12.876 -4.832  30.022 1.00 25.96 ? 1806 LEU   A CB  1 
ATOM   83   C CG  . LEU   A 1 13  ? -11.846 -5.922  29.727 1.00 24.72 ? 1806 LEU   A CG  1 
ATOM   84   C CD1 . LEU   A 1 13  ? -10.882 -5.461  28.668 1.00 19.60 ? 1806 LEU   A CD1 1 
ATOM   85   C CD2 . LEU   A 1 13  ? -11.104 -6.290  30.996 1.00 26.57 ? 1806 LEU   A CD2 1 
ATOM   86   N N   . MET   A 1 14  ? -15.747 -6.001  29.347 1.00 26.96 ? 1807 MET   A N   1 
ATOM   87   C CA  A MET   A 1 14  ? -16.633 -7.131  29.080 0.45 30.54 ? 1807 MET   A CA  1 
ATOM   88   C CA  B MET   A 1 14  ? -16.611 -7.144  29.070 0.55 30.46 ? 1807 MET   A CA  1 
ATOM   89   C C   . MET   A 1 14  ? -17.249 -7.025  27.690 1.00 30.75 ? 1807 MET   A C   1 
ATOM   90   O O   . MET   A 1 14  ? -17.246 -7.988  26.917 1.00 28.15 ? 1807 MET   A O   1 
ATOM   91   C CB  A MET   A 1 14  ? -17.728 -7.203  30.149 0.45 35.05 ? 1807 MET   A CB  1 
ATOM   92   C CB  B MET   A 1 14  ? -17.683 -7.285  30.156 0.55 35.01 ? 1807 MET   A CB  1 
ATOM   93   C CG  A MET   A 1 14  ? -18.766 -8.293  29.911 0.45 40.02 ? 1807 MET   A CG  1 
ATOM   94   C CG  B MET   A 1 14  ? -18.415 -8.627  30.127 0.55 40.48 ? 1807 MET   A CG  1 
ATOM   95   S SD  A MET   A 1 14  ? -20.349 -7.950  30.708 0.45 50.59 ? 1807 MET   A SD  1 
ATOM   96   S SD  B MET   A 1 14  ? -19.578 -8.879  31.487 0.55 47.10 ? 1807 MET   A SD  1 
ATOM   97   C CE  A MET   A 1 14  ? -20.779 -6.398  29.927 0.45 45.58 ? 1807 MET   A CE  1 
ATOM   98   C CE  B MET   A 1 14  ? -20.210 -10.511 31.107 0.55 45.40 ? 1807 MET   A CE  1 
ATOM   99   N N   . GLU   A 1 15  ? -17.777 -5.844  27.352 1.00 29.58 ? 1808 GLU   A N   1 
ATOM   100  C CA  . GLU   A 1 15  ? -18.395 -5.652  26.041 1.00 30.58 ? 1808 GLU   A CA  1 
ATOM   101  C C   . GLU   A 1 15  ? -17.377 -5.806  24.918 1.00 30.44 ? 1808 GLU   A C   1 
ATOM   102  O O   . GLU   A 1 15  ? -17.704 -6.325  23.839 1.00 31.60 ? 1808 GLU   A O   1 
ATOM   103  C CB  . GLU   A 1 15  ? -19.050 -4.276  25.964 1.00 33.74 ? 1808 GLU   A CB  1 
ATOM   104  C CG  . GLU   A 1 15  ? -20.172 -4.052  26.961 1.00 42.34 ? 1808 GLU   A CG  1 
ATOM   105  C CD  . GLU   A 1 15  ? -20.848 -2.716  26.746 1.00 46.51 ? 1808 GLU   A CD  1 
ATOM   106  O OE1 . GLU   A 1 15  ? -20.324 -1.938  25.924 1.00 45.54 ? 1808 GLU   A OE1 1 
ATOM   107  O OE2 . GLU   A 1 15  ? -21.891 -2.441  27.379 1.00 43.77 ? 1808 GLU   A OE2 1 
ATOM   108  N N   . MET   A 1 16  ? -16.150 -5.328  25.142 1.00 28.30 ? 1809 MET   A N   1 
ATOM   109  C CA  . MET   A 1 16  ? -15.085 -5.506  24.159 1.00 27.25 ? 1809 MET   A CA  1 
ATOM   110  C C   . MET   A 1 16  ? -14.746 -6.978  23.999 1.00 29.57 ? 1809 MET   A C   1 
ATOM   111  O O   . MET   A 1 16  ? -14.694 -7.492  22.879 1.00 26.75 ? 1809 MET   A O   1 
ATOM   112  C CB  . MET   A 1 16  ? -13.840 -4.702  24.562 1.00 21.48 ? 1809 MET   A CB  1 
ATOM   113  C CG  . MET   A 1 16  ? -13.978 -3.200  24.293 1.00 23.21 ? 1809 MET   A CG  1 
ATOM   114  S SD  . MET   A 1 16  ? -12.412 -2.302  24.137 1.00 25.36 ? 1809 MET   A SD  1 
ATOM   115  C CE  . MET   A 1 16  ? -11.620 -2.697  25.704 1.00 21.59 ? 1809 MET   A CE  1 
ATOM   116  N N   . GLU   A 1 17  ? -14.538 -7.677  25.118 1.00 28.54 ? 1810 GLU   A N   1 
ATOM   117  C CA  . GLU   A 1 17  ? -14.330 -9.122  25.086 1.00 30.71 ? 1810 GLU   A CA  1 
ATOM   118  C C   . GLU   A 1 17  ? -15.471 -9.857  24.384 1.00 30.17 ? 1810 GLU   A C   1 
ATOM   119  O O   . GLU   A 1 17  ? -15.238 -10.891 23.752 1.00 33.00 ? 1810 GLU   A O   1 
ATOM   120  C CB  . GLU   A 1 17  ? -14.171 -9.654  26.509 1.00 21.91 ? 1810 GLU   A CB  1 
ATOM   121  C CG  . GLU   A 1 17  ? -12.844 -9.291  27.173 1.00 27.72 ? 1810 GLU   A CG  1 
ATOM   122  C CD  . GLU   A 1 17  ? -12.883 -9.488  28.683 1.00 33.07 ? 1810 GLU   A CD  1 
ATOM   123  O OE1 . GLU   A 1 17  ? -13.994 -9.688  29.235 1.00 35.28 ? 1810 GLU   A OE1 1 
ATOM   124  O OE2 . GLU   A 1 17  ? -11.803 -9.432  29.312 1.00 32.34 ? 1810 GLU   A OE2 1 
ATOM   125  N N   . SER   A 1 18  ? -16.701 -9.352  24.490 1.00 31.21 ? 1811 SER   A N   1 
ATOM   126  C CA  . SER   A 1 18  ? -17.868 -10.005 23.906 1.00 33.19 ? 1811 SER   A CA  1 
ATOM   127  C C   . SER   A 1 18  ? -18.180 -9.529  22.494 1.00 35.95 ? 1811 SER   A C   1 
ATOM   128  O O   . SER   A 1 18  ? -19.061 -10.102 21.842 1.00 39.72 ? 1811 SER   A O   1 
ATOM   129  C CB  . SER   A 1 18  ? -19.098 -9.782  24.795 1.00 29.57 ? 1811 SER   A CB  1 
ATOM   130  O OG  . SER   A 1 18  ? -18.835 -10.178 26.131 1.00 43.03 ? 1811 SER   A OG  1 
ATOM   131  N N   . HIS   A 1 19  ? -17.476 -8.514  22.005 1.00 34.16 ? 1812 HIS   A N   1 
ATOM   132  C CA  . HIS   A 1 19  ? -17.729 -7.978  20.678 1.00 30.68 ? 1812 HIS   A CA  1 
ATOM   133  C C   . HIS   A 1 19  ? -17.294 -8.977  19.607 1.00 35.21 ? 1812 HIS   A C   1 
ATOM   134  O O   . HIS   A 1 19  ? -16.362 -9.763  19.804 1.00 31.09 ? 1812 HIS   A O   1 
ATOM   135  C CB  . HIS   A 1 19  ? -16.990 -6.648  20.515 1.00 28.53 ? 1812 HIS   A CB  1 
ATOM   136  C CG  . HIS   A 1 19  ? -17.379 -5.880  19.290 1.00 35.35 ? 1812 HIS   A CG  1 
ATOM   137  N ND1 . HIS   A 1 19  ? -18.196 -4.771  19.333 1.00 37.69 ? 1812 HIS   A ND1 1 
ATOM   138  C CD2 . HIS   A 1 19  ? -17.057 -6.058  17.989 1.00 28.24 ? 1812 HIS   A CD2 1 
ATOM   139  C CE1 . HIS   A 1 19  ? -18.361 -4.301  18.110 1.00 34.61 ? 1812 HIS   A CE1 1 
ATOM   140  N NE2 . HIS   A 1 19  ? -17.687 -5.068  17.275 1.00 33.65 ? 1812 HIS   A NE2 1 
ATOM   141  N N   . ASP   A 1 20  ? -17.993 -8.943  18.464 1.00 33.82 ? 1813 ASP   A N   1 
ATOM   142  C CA  . ASP   A 1 20  ? -17.728 -9.885  17.375 1.00 39.00 ? 1813 ASP   A CA  1 
ATOM   143  C C   . ASP   A 1 20  ? -16.364 -9.656  16.737 1.00 40.42 ? 1813 ASP   A C   1 
ATOM   144  O O   . ASP   A 1 20  ? -15.794 -10.585 16.153 1.00 46.10 ? 1813 ASP   A O   1 
ATOM   145  C CB  . ASP   A 1 20  ? -18.810 -9.790  16.300 1.00 44.42 ? 1813 ASP   A CB  1 
ATOM   146  C CG  . ASP   A 1 20  ? -20.092 -10.498 16.693 1.00 54.83 ? 1813 ASP   A CG  1 
ATOM   147  O OD1 . ASP   A 1 20  ? -21.140 -10.209 16.076 1.00 61.23 ? 1813 ASP   A OD1 1 
ATOM   148  O OD2 . ASP   A 1 20  ? -20.056 -11.333 17.624 1.00 55.57 ? 1813 ASP   A OD2 1 
ATOM   149  N N   . ALA   A 1 21  ? -15.835 -8.439  16.819 1.00 31.90 ? 1814 ALA   A N   1 
ATOM   150  C CA  . ALA   A 1 21  ? -14.535 -8.122  16.243 1.00 23.33 ? 1814 ALA   A CA  1 
ATOM   151  C C   . ALA   A 1 21  ? -13.402 -8.286  17.248 1.00 20.69 ? 1814 ALA   A C   1 
ATOM   152  O O   . ALA   A 1 21  ? -12.283 -7.833  16.984 1.00 27.42 ? 1814 ALA   A O   1 
ATOM   153  C CB  . ALA   A 1 21  ? -14.535 -6.700  15.679 1.00 28.10 ? 1814 ALA   A CB  1 
ATOM   154  N N   . ALA   A 1 22  ? -13.668 -8.943  18.381 1.00 28.02 ? 1815 ALA   A N   1 
ATOM   155  C CA  . ALA   A 1 22  ? -12.679 -9.099  19.439 1.00 28.26 ? 1815 ALA   A CA  1 
ATOM   156  C C   . ALA   A 1 22  ? -11.701 -10.239 19.201 1.00 29.50 ? 1815 ALA   A C   1 
ATOM   157  O O   . ALA   A 1 22  ? -10.671 -10.292 19.880 1.00 22.56 ? 1815 ALA   A O   1 
ATOM   158  C CB  . ALA   A 1 22  ? -13.375 -9.347  20.773 1.00 24.67 ? 1815 ALA   A CB  1 
ATOM   159  N N   . TRP   A 1 23  ? -11.986 -11.143 18.249 1.00 29.27 ? 1816 TRP   A N   1 
ATOM   160  C CA  . TRP   A 1 23  ? -11.245 -12.401 18.133 1.00 31.79 ? 1816 TRP   A CA  1 
ATOM   161  C C   . TRP   A 1 23  ? -9.724  -12.249 18.013 1.00 29.92 ? 1816 TRP   A C   1 
ATOM   162  O O   . TRP   A 1 23  ? -9.010  -13.145 18.478 1.00 39.10 ? 1816 TRP   A O   1 
ATOM   163  C CB  . TRP   A 1 23  ? -11.777 -13.240 16.962 1.00 37.20 ? 1816 TRP   A CB  1 
ATOM   164  C CG  . TRP   A 1 23  ? -11.662 -12.590 15.632 1.00 35.94 ? 1816 TRP   A CG  1 
ATOM   165  C CD1 . TRP   A 1 23  ? -12.610 -11.838 15.001 1.00 42.14 ? 1816 TRP   A CD1 1 
ATOM   166  C CD2 . TRP   A 1 23  ? -10.531 -12.633 14.750 1.00 35.98 ? 1816 TRP   A CD2 1 
ATOM   167  N NE1 . TRP   A 1 23  ? -12.136 -11.404 13.786 1.00 37.30 ? 1816 TRP   A NE1 1 
ATOM   168  C CE2 . TRP   A 1 23  ? -10.862 -11.876 13.611 1.00 37.38 ? 1816 TRP   A CE2 1 
ATOM   169  C CE3 . TRP   A 1 23  ? -9.268  -13.229 14.820 1.00 36.77 ? 1816 TRP   A CE3 1 
ATOM   170  C CZ2 . TRP   A 1 23  ? -9.974  -11.700 12.550 1.00 37.12 ? 1816 TRP   A CZ2 1 
ATOM   171  C CZ3 . TRP   A 1 23  ? -8.392  -13.054 13.765 1.00 30.83 ? 1816 TRP   A CZ3 1 
ATOM   172  C CH2 . TRP   A 1 23  ? -8.748  -12.297 12.647 1.00 31.61 ? 1816 TRP   A CH2 1 
ATOM   173  N N   . PRO   A 1 24  ? -9.163  -11.173 17.438 1.00 23.43 ? 1817 PRO   A N   1 
ATOM   174  C CA  . PRO   A 1 24  ? -7.696  -11.050 17.453 1.00 19.20 ? 1817 PRO   A CA  1 
ATOM   175  C C   . PRO   A 1 24  ? -7.103  -10.583 18.777 1.00 26.99 ? 1817 PRO   A C   1 
ATOM   176  O O   . PRO   A 1 24  ? -5.871  -10.581 18.904 1.00 20.74 ? 1817 PRO   A O   1 
ATOM   177  C CB  . PRO   A 1 24  ? -7.410  -10.007 16.353 1.00 23.07 ? 1817 PRO   A CB  1 
ATOM   178  C CG  . PRO   A 1 24  ? -8.696  -9.861  15.584 1.00 24.06 ? 1817 PRO   A CG  1 
ATOM   179  C CD  . PRO   A 1 24  ? -9.753  -10.092 16.628 1.00 24.75 ? 1817 PRO   A CD  1 
ATOM   180  N N   . PHE   A 1 25  ? -7.919  -10.196 19.760 1.00 23.03 ? 1818 PHE   A N   1 
ATOM   181  C CA  . PHE   A 1 25  ? -7.429  -9.420  20.892 1.00 20.38 ? 1818 PHE   A CA  1 
ATOM   182  C C   . PHE   A 1 25  ? -7.680  -10.080 22.238 1.00 24.38 ? 1818 PHE   A C   1 
ATOM   183  O O   . PHE   A 1 25  ? -7.535  -9.413  23.265 1.00 21.72 ? 1818 PHE   A O   1 
ATOM   184  C CB  . PHE   A 1 25  ? -8.051  -8.018  20.874 1.00 17.78 ? 1818 PHE   A CB  1 
ATOM   185  C CG  . PHE   A 1 25  ? -7.968  -7.343  19.517 1.00 20.56 ? 1818 PHE   A CG  1 
ATOM   186  C CD1 . PHE   A 1 25  ? -6.729  -6.992  18.996 1.00 27.32 ? 1818 PHE   A CD1 1 
ATOM   187  C CD2 . PHE   A 1 25  ? -9.101  -7.080  18.774 1.00 22.17 ? 1818 PHE   A CD2 1 
ATOM   188  C CE1 . PHE   A 1 25  ? -6.613  -6.386  17.770 1.00 25.70 ? 1818 PHE   A CE1 1 
ATOM   189  C CE2 . PHE   A 1 25  ? -9.002  -6.466  17.523 1.00 22.69 ? 1818 PHE   A CE2 1 
ATOM   190  C CZ  . PHE   A 1 25  ? -7.759  -6.115  17.021 1.00 19.03 ? 1818 PHE   A CZ  1 
ATOM   191  N N   . LEU   A 1 26  ? -8.006  -11.376 22.254 1.00 21.10 ? 1819 LEU   A N   1 
ATOM   192  C CA  . LEU   A 1 26  ? -8.394  -12.101 23.458 1.00 18.77 ? 1819 LEU   A CA  1 
ATOM   193  C C   . LEU   A 1 26  ? -7.217  -12.759 24.163 1.00 23.39 ? 1819 LEU   A C   1 
ATOM   194  O O   . LEU   A 1 26  ? -7.343  -13.144 25.338 1.00 26.56 ? 1819 LEU   A O   1 
ATOM   195  C CB  . LEU   A 1 26  ? -9.429  -13.167 23.099 1.00 28.48 ? 1819 LEU   A CB  1 
ATOM   196  C CG  . LEU   A 1 26  ? -10.742 -12.646 22.507 1.00 32.19 ? 1819 LEU   A CG  1 
ATOM   197  C CD1 . LEU   A 1 26  ? -11.658 -13.799 22.130 1.00 27.13 ? 1819 LEU   A CD1 1 
ATOM   198  C CD2 . LEU   A 1 26  ? -11.450 -11.688 23.462 1.00 35.93 ? 1819 LEU   A CD2 1 
ATOM   199  N N   . GLU   A 1 27  ? -6.091  -12.919 23.469 1.00 22.39 ? 1820 GLU   A N   1 
ATOM   200  C CA  . GLU   A 1 27  ? -4.904  -13.534 24.038 1.00 22.89 ? 1820 GLU   A CA  1 
ATOM   201  C C   . GLU   A 1 27  ? -3.693  -12.834 23.444 1.00 16.54 ? 1820 GLU   A C   1 
ATOM   202  O O   . GLU   A 1 27  ? -3.798  -12.244 22.361 1.00 20.13 ? 1820 GLU   A O   1 
ATOM   203  C CB  . GLU   A 1 27  ? -4.851  -15.047 23.757 1.00 22.98 ? 1820 GLU   A CB  1 
ATOM   204  C CG  . GLU   A 1 27  ? -4.721  -15.415 22.309 1.00 33.13 ? 1820 GLU   A CG  1 
ATOM   205  C CD  . GLU   A 1 27  ? -4.576  -16.911 22.108 1.00 41.34 ? 1820 GLU   A CD  1 
ATOM   206  O OE1 . GLU   A 1 27  ? -3.600  -17.506 22.623 1.00 34.63 ? 1820 GLU   A OE1 1 
ATOM   207  O OE2 . GLU   A 1 27  ? -5.451  -17.493 21.442 1.00 45.08 ? 1820 GLU   A OE2 1 
ATOM   208  N N   . PRO   A 1 28  ? -2.554  -12.844 24.136 1.00 22.62 ? 1821 PRO   A N   1 
ATOM   209  C CA  . PRO   A 1 28  ? -1.374  -12.138 23.622 1.00 21.77 ? 1821 PRO   A CA  1 
ATOM   210  C C   . PRO   A 1 28  ? -0.877  -12.747 22.316 1.00 17.54 ? 1821 PRO   A C   1 
ATOM   211  O O   . PRO   A 1 28  ? -0.947  -13.960 22.100 1.00 22.97 ? 1821 PRO   A O   1 
ATOM   212  C CB  . PRO   A 1 28  ? -0.340  -12.305 24.745 1.00 27.04 ? 1821 PRO   A CB  1 
ATOM   213  C CG  . PRO   A 1 28  ? -1.117  -12.703 25.967 1.00 25.74 ? 1821 PRO   A CG  1 
ATOM   214  C CD  . PRO   A 1 28  ? -2.324  -13.430 25.471 1.00 20.53 ? 1821 PRO   A CD  1 
ATOM   215  N N   . VAL   A 1 29  ? -0.394  -11.877 21.427 1.00 17.55 ? 1822 VAL   A N   1 
ATOM   216  C CA  . VAL   A 1 29  ? 0.363   -12.331 20.268 1.00 16.80 ? 1822 VAL   A CA  1 
ATOM   217  C C   . VAL   A 1 29  ? 1.602   -13.049 20.768 1.00 23.04 ? 1822 VAL   A C   1 
ATOM   218  O O   . VAL   A 1 29  ? 2.342   -12.513 21.602 1.00 25.14 ? 1822 VAL   A O   1 
ATOM   219  C CB  . VAL   A 1 29  ? 0.744   -11.131 19.390 1.00 20.40 ? 1822 VAL   A CB  1 
ATOM   220  C CG1 . VAL   A 1 29  ? 1.604   -11.576 18.199 1.00 19.66 ? 1822 VAL   A CG1 1 
ATOM   221  C CG2 . VAL   A 1 29  ? -0.494  -10.371 18.947 1.00 33.09 ? 1822 VAL   A CG2 1 
ATOM   222  N N   . ASN   A 1 30  ? 1.845   -14.263 20.268 1.00 21.41 ? 1823 ASN   A N   1 
ATOM   223  C CA  . ASN   A 1 30  ? 3.048   -14.985 20.655 1.00 23.75 ? 1823 ASN   A CA  1 
ATOM   224  C C   . ASN   A 1 30  ? 4.177   -14.569 19.725 1.00 26.70 ? 1823 ASN   A C   1 
ATOM   225  O O   . ASN   A 1 30  ? 4.196   -14.995 18.558 1.00 23.01 ? 1823 ASN   A O   1 
ATOM   226  C CB  . ASN   A 1 30  ? 2.844   -16.488 20.603 1.00 22.78 ? 1823 ASN   A CB  1 
ATOM   227  C CG  . ASN   A 1 30  ? 3.979   -17.243 21.272 1.00 36.15 ? 1823 ASN   A CG  1 
ATOM   228  O OD1 . ASN   A 1 30  ? 5.144   -16.831 21.211 1.00 35.63 ? 1823 ASN   A OD1 1 
ATOM   229  N ND2 . ASN   A 1 30  ? 3.644   -18.342 21.943 1.00 51.54 ? 1823 ASN   A ND2 1 
ATOM   230  N N   . PRO   A 1 31  ? 5.137   -13.766 20.187 1.00 27.96 ? 1824 PRO   A N   1 
ATOM   231  C CA  . PRO   A 1 31  ? 6.155   -13.229 19.271 1.00 27.69 ? 1824 PRO   A CA  1 
ATOM   232  C C   . PRO   A 1 31  ? 6.952   -14.293 18.524 1.00 29.20 ? 1824 PRO   A C   1 
ATOM   233  O O   . PRO   A 1 31  ? 7.414   -14.025 17.408 1.00 28.89 ? 1824 PRO   A O   1 
ATOM   234  C CB  . PRO   A 1 31  ? 7.048   -12.396 20.204 1.00 25.40 ? 1824 PRO   A CB  1 
ATOM   235  C CG  . PRO   A 1 31  ? 6.794   -12.941 21.567 1.00 34.54 ? 1824 PRO   A CG  1 
ATOM   236  C CD  . PRO   A 1 31  ? 5.358   -13.339 21.577 1.00 31.83 ? 1824 PRO   A CD  1 
ATOM   237  N N   . ARG   A 1 32  ? 7.067   -15.497 19.090 1.00 30.27 ? 1825 ARG   A N   1 
ATOM   238  C CA  . ARG   A 1 32  ? 7.837   -16.594 18.439 1.00 34.06 ? 1825 ARG   A CA  1 
ATOM   239  C C   . ARG   A 1 32  ? 7.057   -17.154 17.243 1.00 31.25 ? 1825 ARG   A C   1 
ATOM   240  O O   . ARG   A 1 32  ? 7.689   -17.732 16.343 1.00 33.20 ? 1825 ARG   A O   1 
ATOM   241  C CB  . ARG   A 1 32  ? 8.110   -17.712 19.451 1.00 40.15 ? 1825 ARG   A CB  1 
ATOM   242  C CG  . ARG   A 1 32  ? 9.576   -18.094 19.595 1.00 50.13 ? 1825 ARG   A CG  1 
ATOM   243  C CD  . ARG   A 1 32  ? 9.792   -19.188 20.624 1.00 52.78 ? 1825 ARG   A CD  1 
ATOM   244  N NE  . ARG   A 1 32  ? 10.668  -18.770 21.709 1.00 53.00 ? 1825 ARG   A NE  1 
ATOM   245  C CZ  . ARG   A 1 32  ? 10.244  -18.359 22.897 1.00 56.51 ? 1825 ARG   A CZ  1 
ATOM   246  N NH1 . ARG   A 1 32  ? 8.948   -18.306 23.155 1.00 52.69 ? 1825 ARG   A NH1 1 
ATOM   247  N NH2 . ARG   A 1 32  ? 11.114  -18.000 23.821 1.00 62.12 ? 1825 ARG   A NH2 1 
ATOM   248  N N   . LEU   A 1 33  ? 5.739   -16.955 17.222 1.00 25.64 ? 1826 LEU   A N   1 
ATOM   249  C CA  . LEU   A 1 33  ? 4.871   -17.504 16.187 1.00 28.96 ? 1826 LEU   A CA  1 
ATOM   250  C C   . LEU   A 1 33  ? 4.542   -16.504 15.077 1.00 25.61 ? 1826 LEU   A C   1 
ATOM   251  O O   . LEU   A 1 33  ? 3.849   -16.862 14.114 1.00 26.28 ? 1826 LEU   A O   1 
ATOM   252  C CB  . LEU   A 1 33  ? 3.575   -18.014 16.836 1.00 31.93 ? 1826 LEU   A CB  1 
ATOM   253  C CG  . LEU   A 1 33  ? 3.559   -19.470 17.305 1.00 44.71 ? 1826 LEU   A CG  1 
ATOM   254  C CD1 . LEU   A 1 33  ? 4.665   -19.764 18.315 1.00 45.49 ? 1826 LEU   A CD1 1 
ATOM   255  C CD2 . LEU   A 1 33  ? 2.197   -19.820 17.881 1.00 46.92 ? 1826 LEU   A CD2 1 
ATOM   256  N N   . VAL   A 1 34  ? 5.026   -15.269 15.174 1.00 23.56 ? 1827 VAL   A N   1 
ATOM   257  C CA  . VAL   A 1 34  ? 4.724   -14.219 14.207 1.00 22.22 ? 1827 VAL   A CA  1 
ATOM   258  C C   . VAL   A 1 34  ? 6.041   -13.557 13.839 1.00 28.19 ? 1827 VAL   A C   1 
ATOM   259  O O   . VAL   A 1 34  ? 6.643   -12.852 14.661 1.00 26.46 ? 1827 VAL   A O   1 
ATOM   260  C CB  . VAL   A 1 34  ? 3.726   -13.185 14.745 1.00 22.48 ? 1827 VAL   A CB  1 
ATOM   261  C CG1 . VAL   A 1 34  ? 3.477   -12.098 13.693 1.00 23.62 ? 1827 VAL   A CG1 1 
ATOM   262  C CG2 . VAL   A 1 34  ? 2.426   -13.867 15.169 1.00 22.84 ? 1827 VAL   A CG2 1 
ATOM   263  N N   . SER   A 1 35  ? 6.485   -13.780 12.613 1.00 32.00 ? 1828 SER   A N   1 
ATOM   264  C CA  . SER   A 1 35  ? 7.723   -13.174 12.159 1.00 25.55 ? 1828 SER   A CA  1 
ATOM   265  C C   . SER   A 1 35  ? 7.638   -11.660 12.251 1.00 24.19 ? 1828 SER   A C   1 
ATOM   266  O O   . SER   A 1 35  ? 6.664   -11.051 11.797 1.00 27.11 ? 1828 SER   A O   1 
ATOM   267  C CB  . SER   A 1 35  ? 8.020   -13.592 10.724 1.00 27.44 ? 1828 SER   A CB  1 
ATOM   268  O OG  . SER   A 1 35  ? 9.288   -13.084 10.365 1.00 29.10 ? 1828 SER   A OG  1 
ATOM   269  N N   . GLY   A 1 36  ? 8.655   -11.058 12.862 1.00 27.12 ? 1829 GLY   A N   1 
ATOM   270  C CA  . GLY   A 1 36  ? 8.782   -9.618  12.917 1.00 24.78 ? 1829 GLY   A CA  1 
ATOM   271  C C   . GLY   A 1 36  ? 8.034   -8.924  14.040 1.00 25.65 ? 1829 GLY   A C   1 
ATOM   272  O O   . GLY   A 1 36  ? 8.231   -7.717  14.229 1.00 22.42 ? 1829 GLY   A O   1 
ATOM   273  N N   . TYR   A 1 37  ? 7.184   -9.630  14.797 1.00 24.37 ? 1830 TYR   A N   1 
ATOM   274  C CA  . TYR   A 1 37  ? 6.340   -8.937  15.765 1.00 20.31 ? 1830 TYR   A CA  1 
ATOM   275  C C   . TYR   A 1 37  ? 7.163   -8.337  16.900 1.00 33.39 ? 1830 TYR   A C   1 
ATOM   276  O O   . TYR   A 1 37  ? 6.950   -7.183  17.292 1.00 33.13 ? 1830 TYR   A O   1 
ATOM   277  C CB  . TYR   A 1 37  ? 5.272   -9.880  16.312 1.00 18.57 ? 1830 TYR   A CB  1 
ATOM   278  C CG  . TYR   A 1 37  ? 4.163   -9.128  17.021 1.00 23.48 ? 1830 TYR   A CG  1 
ATOM   279  C CD1 . TYR   A 1 37  ? 3.220   -8.414  16.295 1.00 22.94 ? 1830 TYR   A CD1 1 
ATOM   280  C CD2 . TYR   A 1 37  ? 4.079   -9.108  18.418 1.00 25.22 ? 1830 TYR   A CD2 1 
ATOM   281  C CE1 . TYR   A 1 37  ? 2.219   -7.709  16.920 1.00 18.55 ? 1830 TYR   A CE1 1 
ATOM   282  C CE2 . TYR   A 1 37  ? 3.079   -8.410  19.060 1.00 17.21 ? 1830 TYR   A CE2 1 
ATOM   283  C CZ  . TYR   A 1 37  ? 2.144   -7.714  18.318 1.00 15.45 ? 1830 TYR   A CZ  1 
ATOM   284  O OH  . TYR   A 1 37  ? 1.126   -6.997  18.900 1.00 19.94 ? 1830 TYR   A OH  1 
ATOM   285  N N   . ARG   A 1 38  ? 8.099   -9.115  17.454 1.00 35.22 ? 1831 ARG   A N   1 
ATOM   286  C CA  . ARG   A 1 38  ? 8.933   -8.614  18.544 1.00 38.17 ? 1831 ARG   A CA  1 
ATOM   287  C C   . ARG   A 1 38  ? 9.750   -7.402  18.114 1.00 33.75 ? 1831 ARG   A C   1 
ATOM   288  O O   . ARG   A 1 38  ? 9.955   -6.481  18.911 1.00 38.03 ? 1831 ARG   A O   1 
ATOM   289  C CB  . ARG   A 1 38  ? 9.856   -9.726  19.051 1.00 34.60 ? 1831 ARG   A CB  1 
ATOM   290  C CG  . ARG   A 1 38  ? 10.777  -9.315  20.191 1.00 43.03 ? 1831 ARG   A CG  1 
ATOM   291  C CD  . ARG   A 1 38  ? 11.493  -10.519 20.790 1.00 52.76 ? 1831 ARG   A CD  1 
ATOM   292  N NE  . ARG   A 1 38  ? 12.033  -10.228 22.117 1.00 59.16 ? 1831 ARG   A NE  1 
ATOM   293  C CZ  . ARG   A 1 38  ? 11.354  -10.369 23.254 1.00 58.01 ? 1831 ARG   A CZ  1 
ATOM   294  N NH1 . ARG   A 1 38  ? 11.929  -10.077 24.414 1.00 55.85 ? 1831 ARG   A NH1 1 
ATOM   295  N NH2 . ARG   A 1 38  ? 10.101  -10.805 23.235 1.00 51.39 ? 1831 ARG   A NH2 1 
ATOM   296  N N   . ARG   A 1 39  ? 10.194  -7.373  16.859 1.00 27.43 ? 1832 ARG   A N   1 
ATOM   297  C CA  . ARG   A 1 39  ? 11.058  -6.258  16.384 1.00 35.27 ? 1832 ARG   A CA  1 
ATOM   298  C C   . ARG   A 1 39  ? 10.268  -4.962  16.169 1.00 35.68 ? 1832 ARG   A C   1 
ATOM   299  O O   . ARG   A 1 39  ? 10.897  -3.900  16.177 1.00 41.21 ? 1832 ARG   A O   1 
ATOM   300  C CB  . ARG   A 1 39  ? 11.727  -6.655  15.065 1.00 29.89 ? 1832 ARG   A CB  1 
ATOM   301  C CG  . ARG   A 1 39  ? 12.934  -7.563  15.237 1.00 43.13 ? 1832 ARG   A CG  1 
ATOM   302  C CD  . ARG   A 1 39  ? 13.331  -8.259  13.952 1.00 48.45 ? 1832 ARG   A CD  1 
ATOM   303  N NE  . ARG   A 1 39  ? 14.063  -9.474  14.264 1.00 51.94 ? 1832 ARG   A NE  1 
ATOM   304  C CZ  . ARG   A 1 39  ? 15.340  -9.500  14.610 1.00 58.14 ? 1832 ARG   A CZ  1 
ATOM   305  N NH1 . ARG   A 1 39  ? 16.033  -8.376  14.668 1.00 57.94 ? 1832 ARG   A NH1 1 
ATOM   306  N NH2 . ARG   A 1 39  ? 15.923  -10.653 14.880 1.00 63.31 ? 1832 ARG   A NH2 1 
ATOM   307  N N   . ILE   A 1 40  ? 8.945   -5.044  16.026 1.00 25.53 ? 1833 ILE   A N   1 
ATOM   308  C CA  . ILE   A 1 40  ? 8.144   -3.883  15.678 1.00 29.23 ? 1833 ILE   A CA  1 
ATOM   309  C C   . ILE   A 1 40  ? 7.323   -3.377  16.861 1.00 27.01 ? 1833 ILE   A C   1 
ATOM   310  O O   . ILE   A 1 40  ? 7.144   -2.167  17.016 1.00 29.84 ? 1833 ILE   A O   1 
ATOM   311  C CB  . ILE   A 1 40  ? 7.237   -4.197  14.467 1.00 23.72 ? 1833 ILE   A CB  1 
ATOM   312  C CG1 . ILE   A 1 40  ? 8.090   -4.355  13.197 1.00 22.49 ? 1833 ILE   A CG1 1 
ATOM   313  C CG2 . ILE   A 1 40  ? 6.192   -3.111  14.268 1.00 27.00 ? 1833 ILE   A CG2 1 
ATOM   314  C CD1 . ILE   A 1 40  ? 7.265   -4.554  11.924 1.00 22.23 ? 1833 ILE   A CD1 1 
ATOM   315  N N   . ILE   A 1 41  ? 6.815   -4.280  17.700 1.00 22.37 ? 1834 ILE   A N   1 
ATOM   316  C CA  . ILE   A 1 41  ? 5.905   -3.930  18.787 1.00 22.85 ? 1834 ILE   A CA  1 
ATOM   317  C C   . ILE   A 1 41  ? 6.663   -4.088  20.097 1.00 23.13 ? 1834 ILE   A C   1 
ATOM   318  O O   . ILE   A 1 41  ? 6.956   -5.211  20.519 1.00 23.03 ? 1834 ILE   A O   1 
ATOM   319  C CB  . ILE   A 1 41  ? 4.638   -4.796  18.771 1.00 20.01 ? 1834 ILE   A CB  1 
ATOM   320  C CG1 . ILE   A 1 41  ? 3.880   -4.589  17.467 1.00 17.88 ? 1834 ILE   A CG1 1 
ATOM   321  C CG2 . ILE   A 1 41  ? 3.701   -4.425  19.939 1.00 16.08 ? 1834 ILE   A CG2 1 
ATOM   322  C CD1 . ILE   A 1 41  ? 3.383   -3.171  17.312 1.00 18.94 ? 1834 ILE   A CD1 1 
ATOM   323  N N   . LYS   A 1 42  ? 6.986   -2.967  20.741 1.00 20.40 ? 1835 LYS   A N   1 
ATOM   324  C CA  . LYS   A 1 42  ? 7.763   -3.010  22.009 1.00 30.20 ? 1835 LYS   A CA  1 
ATOM   325  C C   . LYS   A 1 42  ? 6.829   -3.144  23.216 1.00 24.40 ? 1835 LYS   A C   1 
ATOM   326  O O   . LYS   A 1 42  ? 7.259   -3.718  24.219 1.00 24.31 ? 1835 LYS   A O   1 
ATOM   327  C CB  . LYS   A 1 42  ? 8.587   -1.729  22.169 1.00 38.94 ? 1835 LYS   A CB  1 
ATOM   328  C CG  . LYS   A 1 42  ? 9.774   -1.592  21.227 1.00 46.55 ? 1835 LYS   A CG  1 
ATOM   329  C CD  . LYS   A 1 42  ? 10.154  -2.889  20.549 1.00 50.86 ? 1835 LYS   A CD  1 
ATOM   330  C CE  . LYS   A 1 42  ? 10.970  -3.808  21.431 1.00 56.97 ? 1835 LYS   A CE  1 
ATOM   331  N NZ  . LYS   A 1 42  ? 10.642  -5.232  21.184 1.00 56.94 ? 1835 LYS   A NZ  1 
ATOM   332  N N   . ASN   A 1 43  ? 5.600   -2.638  23.100 1.00 19.49 ? 1836 ASN   A N   1 
ATOM   333  C CA  . ASN   A 1 43  ? 4.650   -2.635  24.209 1.00 17.65 ? 1836 ASN   A CA  1 
ATOM   334  C C   . ASN   A 1 43  ? 3.421   -3.436  23.812 1.00 15.07 ? 1836 ASN   A C   1 
ATOM   335  O O   . ASN   A 1 43  ? 2.372   -2.852  23.504 1.00 16.44 ? 1836 ASN   A O   1 
ATOM   336  C CB  . ASN   A 1 43  ? 4.260   -1.204  24.561 1.00 17.44 ? 1836 ASN   A CB  1 
ATOM   337  C CG  . ASN   A 1 43  ? 5.439   -0.380  24.980 1.00 24.77 ? 1836 ASN   A CG  1 
ATOM   338  O OD1 . ASN   A 1 43  ? 6.180   -0.748  25.901 1.00 35.42 ? 1836 ASN   A OD1 1 
ATOM   339  N ND2 . ASN   A 1 43  ? 5.642   0.742   24.300 1.00 24.82 ? 1836 ASN   A ND2 1 
ATOM   340  N N   . PRO   A 1 44  ? 3.497   -4.765  23.804 1.00 16.45 ? 1837 PRO   A N   1 
ATOM   341  C CA  . PRO   A 1 44  ? 2.306   -5.555  23.464 1.00 21.08 ? 1837 PRO   A CA  1 
ATOM   342  C C   . PRO   A 1 44  ? 1.201   -5.447  24.515 1.00 23.73 ? 1837 PRO   A C   1 
ATOM   343  O O   . PRO   A 1 44  ? 1.445   -5.238  25.711 1.00 18.54 ? 1837 PRO   A O   1 
ATOM   344  C CB  . PRO   A 1 44  ? 2.839   -6.989  23.355 1.00 18.75 ? 1837 PRO   A CB  1 
ATOM   345  C CG  . PRO   A 1 44  ? 4.140   -6.984  24.003 1.00 28.22 ? 1837 PRO   A CG  1 
ATOM   346  C CD  . PRO   A 1 44  ? 4.697   -5.603  23.938 1.00 21.45 ? 1837 PRO   A CD  1 
ATOM   347  N N   . MET   A 1 45  ? -0.036  -5.587  24.042 1.00 19.17 ? 1838 MET   A N   1 
ATOM   348  C CA  . MET   A 1 45  ? -1.220  -5.503  24.888 1.00 17.81 ? 1838 MET   A CA  1 
ATOM   349  C C   . MET   A 1 45  ? -2.362  -6.275  24.241 1.00 20.92 ? 1838 MET   A C   1 
ATOM   350  O O   . MET   A 1 45  ? -2.447  -6.390  23.014 1.00 19.04 ? 1838 MET   A O   1 
ATOM   351  C CB  . MET   A 1 45  ? -1.628  -4.044  25.141 1.00 18.52 ? 1838 MET   A CB  1 
ATOM   352  C CG  . MET   A 1 45  ? -2.703  -3.854  26.216 1.00 23.44 ? 1838 MET   A CG  1 
ATOM   353  S SD  . MET   A 1 45  ? -2.395  -4.756  27.749 1.00 20.75 ? 1838 MET   A SD  1 
ATOM   354  C CE  . MET   A 1 45  ? -0.810  -4.116  28.262 1.00 19.63 ? 1838 MET   A CE  1 
ATOM   355  N N   . ASP   A 1 46  ? -3.236  -6.811  25.087 1.00 18.74 ? 1839 ASP   A N   1 
ATOM   356  C CA  . ASP   A 1 46  ? -4.419  -7.540  24.658 1.00 16.69 ? 1839 ASP   A CA  1 
ATOM   357  C C   . ASP   A 1 46  ? -5.411  -7.492  25.811 1.00 20.91 ? 1839 ASP   A C   1 
ATOM   358  O O   . ASP   A 1 46  ? -5.051  -7.095  26.922 1.00 17.11 ? 1839 ASP   A O   1 
ATOM   359  C CB  . ASP   A 1 46  ? -4.085  -8.990  24.302 1.00 21.48 ? 1839 ASP   A CB  1 
ATOM   360  C CG  . ASP   A 1 46  ? -3.813  -9.841  25.541 1.00 14.03 ? 1839 ASP   A CG  1 
ATOM   361  O OD1 . ASP   A 1 46  ? -2.748  -9.680  26.161 1.00 19.56 ? 1839 ASP   A OD1 1 
ATOM   362  O OD2 . ASP   A 1 46  ? -4.689  -10.666 25.882 1.00 21.82 ? 1839 ASP   A OD2 1 
ATOM   363  N N   . PHE   A 1 47  ? -6.648  -7.949  25.546 1.00 19.58 ? 1840 PHE   A N   1 
ATOM   364  C CA  . PHE   A 1 47  ? -7.729  -7.848  26.536 1.00 18.35 ? 1840 PHE   A CA  1 
ATOM   365  C C   . PHE   A 1 47  ? -7.508  -8.768  27.738 1.00 17.85 ? 1840 PHE   A C   1 
ATOM   366  O O   . PHE   A 1 47  ? -7.879  -8.412  28.861 1.00 24.34 ? 1840 PHE   A O   1 
ATOM   367  C CB  . PHE   A 1 47  ? -9.098  -8.166  25.902 1.00 17.73 ? 1840 PHE   A CB  1 
ATOM   368  C CG  . PHE   A 1 47  ? -9.537  -7.197  24.828 1.00 22.80 ? 1840 PHE   A CG  1 
ATOM   369  C CD1 . PHE   A 1 47  ? -8.994  -5.923  24.733 1.00 16.58 ? 1840 PHE   A CD1 1 
ATOM   370  C CD2 . PHE   A 1 47  ? -10.514 -7.578  23.909 1.00 24.37 ? 1840 PHE   A CD2 1 
ATOM   371  C CE1 . PHE   A 1 47  ? -9.431  -5.047  23.739 1.00 21.97 ? 1840 PHE   A CE1 1 
ATOM   372  C CE2 . PHE   A 1 47  ? -10.936 -6.712  22.905 1.00 25.60 ? 1840 PHE   A CE2 1 
ATOM   373  C CZ  . PHE   A 1 47  ? -10.395 -5.450  22.818 1.00 21.62 ? 1840 PHE   A CZ  1 
ATOM   374  N N   . SER   A 1 48  ? -6.949  -9.968  27.542 1.00 19.56 ? 1841 SER   A N   1 
ATOM   375  C CA  . SER   A 1 48  ? -6.732  -10.823 28.714 1.00 21.80 ? 1841 SER   A CA  1 
ATOM   376  C C   . SER   A 1 48  ? -5.695  -10.220 29.655 1.00 23.77 ? 1841 SER   A C   1 
ATOM   377  O O   . SER   A 1 48  ? -5.803  -10.370 30.879 1.00 19.31 ? 1841 SER   A O   1 
ATOM   378  C CB  . SER   A 1 48  ? -6.311  -12.235 28.314 1.00 17.18 ? 1841 SER   A CB  1 
ATOM   379  O OG  . SER   A 1 48  ? -4.971  -12.267 27.848 1.00 18.04 ? 1841 SER   A OG  1 
ATOM   380  N N   . THR   A 1 49  ? -4.708  -9.512  29.106 1.00 21.20 ? 1842 THR   A N   1 
ATOM   381  C CA  . THR   A 1 49  ? -3.715  -8.846  29.949 1.00 14.80 ? 1842 THR   A CA  1 
ATOM   382  C C   . THR   A 1 49  ? -4.333  -7.671  30.690 1.00 13.57 ? 1842 THR   A C   1 
ATOM   383  O O   . THR   A 1 49  ? -4.013  -7.426  31.865 1.00 20.74 ? 1842 THR   A O   1 
ATOM   384  C CB  . THR   A 1 49  ? -2.534  -8.403  29.081 1.00 20.86 ? 1842 THR   A CB  1 
ATOM   385  O OG1 . THR   A 1 49  ? -1.967  -9.565  28.458 1.00 19.40 ? 1842 THR   A OG1 1 
ATOM   386  C CG2 . THR   A 1 49  ? -1.456  -7.714  29.928 1.00 17.91 ? 1842 THR   A CG2 1 
ATOM   387  N N   . MET   A 1 50  ? -5.251  -6.953  30.030 1.00 13.29 ? 1843 MET   A N   1 
ATOM   388  C CA  . MET   A 1 50  ? -6.017  -5.901  30.687 1.00 13.39 ? 1843 MET   A CA  1 
ATOM   389  C C   . MET   A 1 50  ? -6.926  -6.493  31.756 1.00 16.92 ? 1843 MET   A C   1 
ATOM   390  O O   . MET   A 1 50  ? -7.070  -5.924  32.841 1.00 22.00 ? 1843 MET   A O   1 
ATOM   391  C CB  . MET   A 1 50  ? -6.834  -5.115  29.662 1.00 16.98 ? 1843 MET   A CB  1 
ATOM   392  C CG  . MET   A 1 50  ? -5.948  -4.381  28.668 1.00 16.92 ? 1843 MET   A CG  1 
ATOM   393  S SD  . MET   A 1 50  ? -6.906  -3.668  27.310 1.00 20.92 ? 1843 MET   A SD  1 
ATOM   394  C CE  . MET   A 1 50  ? -7.899  -2.495  28.222 1.00 22.88 ? 1843 MET   A CE  1 
ATOM   395  N N   . ARG   A 1 51  ? -7.534  -7.641  31.454 1.00 14.88 ? 1844 ARG   A N   1 
ATOM   396  C CA  . ARG   A 1 51  ? -8.410  -8.301  32.418 1.00 16.04 ? 1844 ARG   A CA  1 
ATOM   397  C C   . ARG   A 1 51  ? -7.637  -8.728  33.663 1.00 17.67 ? 1844 ARG   A C   1 
ATOM   398  O O   . ARG   A 1 51  ? -8.119  -8.556  34.795 1.00 20.39 ? 1844 ARG   A O   1 
ATOM   399  C CB  . ARG   A 1 51  ? -9.085  -9.502  31.753 1.00 20.37 ? 1844 ARG   A CB  1 
ATOM   400  C CG  . ARG   A 1 51  ? -9.840  -10.421 32.720 1.00 23.46 ? 1844 ARG   A CG  1 
ATOM   401  C CD  . ARG   A 1 51  ? -11.018 -9.723  33.350 1.00 28.63 ? 1844 ARG   A CD  1 
ATOM   402  N NE  . ARG   A 1 51  ? -12.048 -9.392  32.371 1.00 39.44 ? 1844 ARG   A NE  1 
ATOM   403  C CZ  . ARG   A 1 51  ? -13.227 -8.868  32.685 1.00 40.95 ? 1844 ARG   A CZ  1 
ATOM   404  N NH1 . ARG   A 1 51  ? -13.521 -8.623  33.956 1.00 41.87 ? 1844 ARG   A NH1 1 
ATOM   405  N NH2 . ARG   A 1 51  ? -14.107 -8.589  31.734 1.00 33.17 ? 1844 ARG   A NH2 1 
ATOM   406  N N   . GLU   A 1 52  ? -6.444  -9.293  33.477 1.00 21.75 ? 1845 GLU   A N   1 
ATOM   407  C CA  . GLU   A 1 52  ? -5.630  -9.696  34.621 1.00 28.10 ? 1845 GLU   A CA  1 
ATOM   408  C C   . GLU   A 1 52  ? -5.308  -8.496  35.502 1.00 18.76 ? 1845 GLU   A C   1 
ATOM   409  O O   . GLU   A 1 52  ? -5.452  -8.550  36.733 1.00 24.15 ? 1845 GLU   A O   1 
ATOM   410  C CB  . GLU   A 1 52  ? -4.351  -10.374 34.120 1.00 32.77 ? 1845 GLU   A CB  1 
ATOM   411  C CG  . GLU   A 1 52  ? -3.571  -11.140 35.184 1.00 29.09 ? 1845 GLU   A CG  1 
ATOM   412  C CD  . GLU   A 1 52  ? -2.802  -10.223 36.114 1.00 34.92 ? 1845 GLU   A CD  1 
ATOM   413  O OE1 . GLU   A 1 52  ? -2.284  -9.187  35.631 1.00 27.34 ? 1845 GLU   A OE1 1 
ATOM   414  O OE2 . GLU   A 1 52  ? -2.743  -10.528 37.329 1.00 33.19 ? 1845 GLU   A OE2 1 
ATOM   415  N N   . ARG   A 1 53  ? -4.847  -7.408  34.884 1.00 17.72 ? 1846 ARG   A N   1 
ATOM   416  C CA  . ARG   A 1 53  ? -4.492  -6.212  35.638 1.00 18.73 ? 1846 ARG   A CA  1 
ATOM   417  C C   . ARG   A 1 53  ? -5.708  -5.607  36.338 1.00 16.68 ? 1846 ARG   A C   1 
ATOM   418  O O   . ARG   A 1 53  ? -5.617  -5.206  37.498 1.00 20.71 ? 1846 ARG   A O   1 
ATOM   419  C CB  . ARG   A 1 53  ? -3.840  -5.191  34.706 1.00 15.60 ? 1846 ARG   A CB  1 
ATOM   420  C CG  . ARG   A 1 53  ? -3.469  -3.890  35.405 1.00 17.79 ? 1846 ARG   A CG  1 
ATOM   421  C CD  . ARG   A 1 53  ? -2.612  -3.030  34.470 1.00 20.35 ? 1846 ARG   A CD  1 
ATOM   422  N NE  . ARG   A 1 53  ? -2.371  -1.718  35.065 1.00 20.96 ? 1846 ARG   A NE  1 
ATOM   423  C CZ  . ARG   A 1 53  ? -1.844  -0.684  34.418 1.00 22.43 ? 1846 ARG   A CZ  1 
ATOM   424  N NH1 . ARG   A 1 53  ? -1.490  -0.814  33.146 1.00 25.67 ? 1846 ARG   A NH1 1 
ATOM   425  N NH2 . ARG   A 1 53  ? -1.672  0.475   35.044 1.00 22.63 ? 1846 ARG   A NH2 1 
ATOM   426  N N   . LEU   A 1 54  ? -6.857  -5.544  35.656 1.00 16.35 ? 1847 LEU   A N   1 
ATOM   427  C CA  . LEU   A 1 54  ? -8.041  -4.949  36.257 1.00 18.66 ? 1847 LEU   A CA  1 
ATOM   428  C C   . LEU   A 1 54  ? -8.507  -5.751  37.473 1.00 19.41 ? 1847 LEU   A C   1 
ATOM   429  O O   . LEU   A 1 54  ? -8.878  -5.174  38.510 1.00 23.24 ? 1847 LEU   A O   1 
ATOM   430  C CB  . LEU   A 1 54  ? -9.141  -4.835  35.200 1.00 23.15 ? 1847 LEU   A CB  1 
ATOM   431  C CG  . LEU   A 1 54  ? -10.443 -4.125  35.538 1.00 28.42 ? 1847 LEU   A CG  1 
ATOM   432  C CD1 . LEU   A 1 54  ? -10.218 -2.681  35.995 1.00 22.67 ? 1847 LEU   A CD1 1 
ATOM   433  C CD2 . LEU   A 1 54  ? -11.350 -4.174  34.314 1.00 27.96 ? 1847 LEU   A CD2 1 
ATOM   434  N N   . SER   A 1 55  ? -8.403  -7.082  37.401 1.00 19.80 ? 1848 SER   A N   1 
ATOM   435  C CA  A SER   A 1 55  ? -8.964  -7.920  38.455 0.41 20.70 ? 1848 SER   A CA  1 
ATOM   436  C CA  B SER   A 1 55  ? -8.956  -7.933  38.452 0.59 19.10 ? 1848 SER   A CA  1 
ATOM   437  C C   . SER   A 1 55  ? -8.226  -7.756  39.777 1.00 25.61 ? 1848 SER   A C   1 
ATOM   438  O O   . SER   A 1 55  ? -8.843  -7.870  40.838 1.00 27.05 ? 1848 SER   A O   1 
ATOM   439  C CB  A SER   A 1 55  ? -8.964  -9.384  38.022 0.41 22.45 ? 1848 SER   A CB  1 
ATOM   440  C CB  B SER   A 1 55  ? -8.917  -9.402  38.029 0.59 22.14 ? 1848 SER   A CB  1 
ATOM   441  O OG  A SER   A 1 55  ? -9.869  -9.583  36.948 0.41 23.65 ? 1848 SER   A OG  1 
ATOM   442  O OG  B SER   A 1 55  ? -7.616  -9.950  38.150 0.59 26.42 ? 1848 SER   A OG  1 
ATOM   443  N N   . ARG   A 1 56  ? -6.919  -7.489  39.744 1.00 25.45 ? 1849 ARG   A N   1 
ATOM   444  C CA  . ARG   A 1 56  ? -6.155  -7.310  40.980 1.00 25.59 ? 1849 ARG   A CA  1 
ATOM   445  C C   . ARG   A 1 56  ? -5.994  -5.844  41.367 1.00 24.46 ? 1849 ARG   A C   1 
ATOM   446  O O   . ARG   A 1 56  ? -5.063  -5.502  42.106 1.00 25.16 ? 1849 ARG   A O   1 
ATOM   447  C CB  . ARG   A 1 56  ? -4.784  -7.960  40.848 1.00 28.68 ? 1849 ARG   A CB  1 
ATOM   448  C CG  . ARG   A 1 56  ? -3.998  -7.398  39.698 1.00 22.79 ? 1849 ARG   A CG  1 
ATOM   449  C CD  . ARG   A 1 56  ? -2.559  -7.845  39.731 1.00 29.63 ? 1849 ARG   A CD  1 
ATOM   450  N NE  . ARG   A 1 56  ? -1.950  -7.604  38.431 1.00 26.69 ? 1849 ARG   A NE  1 
ATOM   451  C CZ  . ARG   A 1 56  ? -1.548  -6.415  38.003 1.00 30.72 ? 1849 ARG   A CZ  1 
ATOM   452  N NH1 . ARG   A 1 56  ? -1.681  -5.339  38.775 1.00 25.47 ? 1849 ARG   A NH1 1 
ATOM   453  N NH2 . ARG   A 1 56  ? -1.013  -6.302  36.795 1.00 37.07 ? 1849 ARG   A NH2 1 
ATOM   454  N N   . GLY   A 1 57  ? -6.881  -4.975  40.891 1.00 18.95 ? 1850 GLY   A N   1 
ATOM   455  C CA  . GLY   A 1 57  ? -6.781  -3.552  41.161 1.00 18.99 ? 1850 GLY   A CA  1 
ATOM   456  C C   . GLY   A 1 57  ? -5.526  -2.873  40.657 1.00 18.51 ? 1850 GLY   A C   1 
ATOM   457  O O   . GLY   A 1 57  ? -5.033  -1.935  41.297 1.00 21.22 ? 1850 GLY   A O   1 
ATOM   458  N N   . GLY   A 1 58  ? -5.002  -3.300  39.503 1.00 17.56 ? 1851 GLY   A N   1 
ATOM   459  C CA  . GLY   A 1 58  ? -3.792  -2.699  38.984 1.00 20.16 ? 1851 GLY   A CA  1 
ATOM   460  C C   . GLY   A 1 58  ? -3.980  -1.463  38.125 1.00 19.76 ? 1851 GLY   A C   1 
ATOM   461  O O   . GLY   A 1 58  ? -3.001  -0.960  37.567 1.00 20.55 ? 1851 GLY   A O   1 
ATOM   462  N N   . TYR   A 1 59  ? -5.203  -0.955  38.009 1.00 19.37 ? 1852 TYR   A N   1 
ATOM   463  C CA  . TYR   A 1 59  ? -5.494  0.314   37.343 1.00 25.54 ? 1852 TYR   A CA  1 
ATOM   464  C C   . TYR   A 1 59  ? -5.915  1.326   38.395 1.00 18.48 ? 1852 TYR   A C   1 
ATOM   465  O O   . TYR   A 1 59  ? -6.999  1.199   38.979 1.00 22.10 ? 1852 TYR   A O   1 
ATOM   466  C CB  . TYR   A 1 59  ? -6.607  0.165   36.316 1.00 18.53 ? 1852 TYR   A CB  1 
ATOM   467  C CG  . TYR   A 1 59  ? -6.219  -0.625  35.104 1.00 16.48 ? 1852 TYR   A CG  1 
ATOM   468  C CD1 . TYR   A 1 59  ? -5.241  -0.150  34.252 1.00 17.90 ? 1852 TYR   A CD1 1 
ATOM   469  C CD2 . TYR   A 1 59  ? -6.839  -1.834  34.812 1.00 17.30 ? 1852 TYR   A CD2 1 
ATOM   470  C CE1 . TYR   A 1 59  ? -4.887  -0.859  33.120 1.00 19.14 ? 1852 TYR   A CE1 1 
ATOM   471  C CE2 . TYR   A 1 59  ? -6.500  -2.552  33.697 1.00 16.44 ? 1852 TYR   A CE2 1 
ATOM   472  C CZ  . TYR   A 1 59  ? -5.512  -2.056  32.855 1.00 16.92 ? 1852 TYR   A CZ  1 
ATOM   473  O OH  . TYR   A 1 59  ? -5.143  -2.761  31.738 1.00 18.74 ? 1852 TYR   A OH  1 
ATOM   474  N N   . THR   A 1 60  ? -5.088  2.360   38.609 1.00 19.72 ? 1853 THR   A N   1 
ATOM   475  C CA  . THR   A 1 60  ? -5.425  3.358   39.624 1.00 21.03 ? 1853 THR   A CA  1 
ATOM   476  C C   . THR   A 1 60  ? -6.412  4.397   39.106 1.00 21.80 ? 1853 THR   A C   1 
ATOM   477  O O   . THR   A 1 60  ? -7.082  5.058   39.905 1.00 23.18 ? 1853 THR   A O   1 
ATOM   478  C CB  . THR   A 1 60  ? -4.165  4.073   40.151 1.00 24.77 ? 1853 THR   A CB  1 
ATOM   479  O OG1 . THR   A 1 60  ? -3.407  4.628   39.057 1.00 28.39 ? 1853 THR   A OG1 1 
ATOM   480  C CG2 . THR   A 1 60  ? -3.288  3.116   40.960 1.00 26.37 ? 1853 THR   A CG2 1 
ATOM   481  N N   . SER   A 1 61  ? -6.533  4.536   37.789 1.00 21.22 ? 1854 SER   A N   1 
ATOM   482  C CA  . SER   A 1 61  ? -7.421  5.517   37.189 1.00 22.54 ? 1854 SER   A CA  1 
ATOM   483  C C   . SER   A 1 61  ? -7.947  4.942   35.886 1.00 23.39 ? 1854 SER   A C   1 
ATOM   484  O O   . SER   A 1 61  ? -7.375  4.005   35.328 1.00 22.53 ? 1854 SER   A O   1 
ATOM   485  C CB  . SER   A 1 61  ? -6.701  6.837   36.900 1.00 26.86 ? 1854 SER   A CB  1 
ATOM   486  O OG  . SER   A 1 61  ? -5.812  6.663   35.801 1.00 31.92 ? 1854 SER   A OG  1 
ATOM   487  N N   . SER   A 1 62  ? -9.047  5.525   35.405 1.00 23.49 ? 1855 SER   A N   1 
ATOM   488  C CA  . SER   A 1 62  ? -9.576  5.128   34.104 1.00 27.24 ? 1855 SER   A CA  1 
ATOM   489  C C   . SER   A 1 62  ? -8.618  5.490   32.978 1.00 26.54 ? 1855 SER   A C   1 
ATOM   490  O O   . SER   A 1 62  ? -8.575  4.794   31.955 1.00 22.15 ? 1855 SER   A O   1 
ATOM   491  C CB  . SER   A 1 62  ? -10.942 5.777   33.881 1.00 24.01 ? 1855 SER   A CB  1 
ATOM   492  O OG  . SER   A 1 62  ? -10.877 7.184   34.060 1.00 30.66 ? 1855 SER   A OG  1 
ATOM   493  N N   . GLU   A 1 63  ? -7.847  6.565   33.149 1.00 28.37 ? 1856 GLU   A N   1 
ATOM   494  C CA  . GLU   A 1 63  ? -6.829  6.930   32.167 1.00 29.91 ? 1856 GLU   A CA  1 
ATOM   495  C C   . GLU   A 1 63  ? -5.840  5.790   31.936 1.00 27.40 ? 1856 GLU   A C   1 
ATOM   496  O O   . GLU   A 1 63  ? -5.445  5.524   30.797 1.00 25.35 ? 1856 GLU   A O   1 
ATOM   497  C CB  . GLU   A 1 63  ? -6.094  8.190   32.631 1.00 30.82 ? 1856 GLU   A CB  1 
ATOM   498  C CG  . GLU   A 1 63  ? -6.844  9.501   32.416 1.00 37.46 ? 1856 GLU   A CG  1 
ATOM   499  C CD  . GLU   A 1 63  ? -8.051  9.662   33.317 1.00 37.08 ? 1856 GLU   A CD  1 
ATOM   500  O OE1 . GLU   A 1 63  ? -9.026  10.309  32.881 1.00 33.70 ? 1856 GLU   A OE1 1 
ATOM   501  O OE2 . GLU   A 1 63  ? -8.026  9.156   34.460 1.00 33.22 ? 1856 GLU   A OE2 1 
ATOM   502  N N   . GLU   A 1 64  ? -5.426  5.096   33.003 1.00 21.93 ? 1857 GLU   A N   1 
ATOM   503  C CA  . GLU   A 1 64  ? -4.472  4.010   32.804 1.00 22.27 ? 1857 GLU   A CA  1 
ATOM   504  C C   . GLU   A 1 64  ? -5.099  2.840   32.055 1.00 23.02 ? 1857 GLU   A C   1 
ATOM   505  O O   . GLU   A 1 64  ? -4.416  2.168   31.273 1.00 23.19 ? 1857 GLU   A O   1 
ATOM   506  C CB  . GLU   A 1 64  ? -3.897  3.570   34.159 1.00 23.40 ? 1857 GLU   A CB  1 
ATOM   507  C CG  . GLU   A 1 64  ? -2.987  4.630   34.774 1.00 27.21 ? 1857 GLU   A CG  1 
ATOM   508  C CD  . GLU   A 1 64  ? -2.411  4.206   36.106 1.00 39.66 ? 1857 GLU   A CD  1 
ATOM   509  O OE1 . GLU   A 1 64  ? -2.930  3.232   36.691 1.00 43.22 ? 1857 GLU   A OE1 1 
ATOM   510  O OE2 . GLU   A 1 64  ? -1.432  4.837   36.567 1.00 40.46 ? 1857 GLU   A OE2 1 
ATOM   511  N N   . PHE   A 1 65  ? -6.393  2.592   32.274 1.00 20.76 ? 1858 PHE   A N   1 
ATOM   512  C CA  . PHE   A 1 65  ? -7.117  1.594   31.493 1.00 18.78 ? 1858 PHE   A CA  1 
ATOM   513  C C   . PHE   A 1 65  ? -7.160  1.984   30.022 1.00 18.26 ? 1858 PHE   A C   1 
ATOM   514  O O   . PHE   A 1 65  ? -6.907  1.153   29.140 1.00 20.64 ? 1858 PHE   A O   1 
ATOM   515  C CB  . PHE   A 1 65  ? -8.536  1.438   32.056 1.00 22.07 ? 1858 PHE   A CB  1 
ATOM   516  C CG  . PHE   A 1 65  ? -9.398  0.477   31.289 1.00 20.60 ? 1858 PHE   A CG  1 
ATOM   517  C CD1 . PHE   A 1 65  ? -10.248 0.931   30.286 1.00 22.03 ? 1858 PHE   A CD1 1 
ATOM   518  C CD2 . PHE   A 1 65  ? -9.370  -0.877  31.574 1.00 20.07 ? 1858 PHE   A CD2 1 
ATOM   519  C CE1 . PHE   A 1 65  ? -11.049 0.058   29.593 1.00 23.08 ? 1858 PHE   A CE1 1 
ATOM   520  C CE2 . PHE   A 1 65  ? -10.168 -1.759  30.863 1.00 25.89 ? 1858 PHE   A CE2 1 
ATOM   521  C CZ  . PHE   A 1 65  ? -11.011 -1.285  29.872 1.00 20.10 ? 1858 PHE   A CZ  1 
ATOM   522  N N   . ALA   A 1 66  ? -7.458  3.252   29.747 1.00 20.36 ? 1859 ALA   A N   1 
ATOM   523  C CA  . ALA   A 1 66  ? -7.554  3.717   28.366 1.00 19.91 ? 1859 ALA   A CA  1 
ATOM   524  C C   . ALA   A 1 66  ? -6.217  3.619   27.655 1.00 25.31 ? 1859 ALA   A C   1 
ATOM   525  O O   . ALA   A 1 66  ? -6.186  3.354   26.451 1.00 25.24 ? 1859 ALA   A O   1 
ATOM   526  C CB  . ALA   A 1 66  ? -8.056  5.151   28.319 1.00 22.20 ? 1859 ALA   A CB  1 
ATOM   527  N N   . ALA   A 1 67  ? -5.105  3.832   28.373 1.00 21.20 ? 1860 ALA   A N   1 
ATOM   528  C CA  . ALA   A 1 67  ? -3.795  3.686   27.736 1.00 18.23 ? 1860 ALA   A CA  1 
ATOM   529  C C   . ALA   A 1 67  ? -3.603  2.267   27.224 1.00 25.80 ? 1860 ALA   A C   1 
ATOM   530  O O   . ALA   A 1 67  ? -3.104  2.062   26.110 1.00 22.70 ? 1860 ALA   A O   1 
ATOM   531  C CB  . ALA   A 1 67  ? -2.668  4.060   28.704 1.00 18.00 ? 1860 ALA   A CB  1 
ATOM   532  N N   . ASP   A 1 68  ? -4.025  1.269   28.008 1.00 17.70 ? 1861 ASP   A N   1 
ATOM   533  C CA  . ASP   A 1 68  ? -3.847  -0.108  27.571 1.00 13.92 ? 1861 ASP   A CA  1 
ATOM   534  C C   . ASP   A 1 68  ? -4.742  -0.426  26.379 1.00 19.83 ? 1861 ASP   A C   1 
ATOM   535  O O   . ASP   A 1 68  ? -4.304  -1.098  25.437 1.00 17.93 ? 1861 ASP   A O   1 
ATOM   536  C CB  . ASP   A 1 68  ? -4.113  -1.080  28.716 1.00 29.12 ? 1861 ASP   A CB  1 
ATOM   537  C CG  . ASP   A 1 68  ? -2.880  -1.310  29.578 1.00 20.57 ? 1861 ASP   A CG  1 
ATOM   538  O OD1 . ASP   A 1 68  ? -2.971  -2.058  30.574 1.00 17.33 ? 1861 ASP   A OD1 1 
ATOM   539  O OD2 . ASP   A 1 68  ? -1.816  -0.741  29.260 1.00 20.51 ? 1861 ASP   A OD2 1 
ATOM   540  N N   . ALA   A 1 69  ? -5.993  0.042   26.409 1.00 21.01 ? 1862 ALA   A N   1 
ATOM   541  C CA  . ALA   A 1 69  ? -6.914  -0.210  25.302 1.00 17.71 ? 1862 ALA   A CA  1 
ATOM   542  C C   . ALA   A 1 69  ? -6.364  0.348   23.989 1.00 24.79 ? 1862 ALA   A C   1 
ATOM   543  O O   . ALA   A 1 69  ? -6.376  -0.333  22.951 1.00 20.97 ? 1862 ALA   A O   1 
ATOM   544  C CB  . ALA   A 1 69  ? -8.288  0.386   25.616 1.00 20.87 ? 1862 ALA   A CB  1 
ATOM   545  N N   . LEU   A 1 70  ? -5.866  1.588   24.015 1.00 25.24 ? 1863 LEU   A N   1 
ATOM   546  C CA  . LEU   A 1 70  ? -5.350  2.176   22.780 1.00 18.67 ? 1863 LEU   A CA  1 
ATOM   547  C C   . LEU   A 1 70  ? -4.075  1.481   22.319 1.00 18.54 ? 1863 LEU   A C   1 
ATOM   548  O O   . LEU   A 1 70  ? -3.804  1.421   21.112 1.00 21.76 ? 1863 LEU   A O   1 
ATOM   549  C CB  . LEU   A 1 70  ? -5.123  3.676   22.961 1.00 21.92 ? 1863 LEU   A CB  1 
ATOM   550  C CG  . LEU   A 1 70  ? -6.376  4.510   23.293 1.00 27.98 ? 1863 LEU   A CG  1 
ATOM   551  C CD1 . LEU   A 1 70  ? -6.070  6.008   23.326 1.00 30.54 ? 1863 LEU   A CD1 1 
ATOM   552  C CD2 . LEU   A 1 70  ? -7.558  4.229   22.363 1.00 25.96 ? 1863 LEU   A CD2 1 
ATOM   553  N N   . LEU   A 1 71  ? -3.279  0.952   23.256 1.00 17.77 ? 1864 LEU   A N   1 
ATOM   554  C CA  . LEU   A 1 71  ? -2.123  0.156   22.865 1.00 21.64 ? 1864 LEU   A CA  1 
ATOM   555  C C   . LEU   A 1 71  ? -2.536  -1.030  22.020 1.00 19.13 ? 1864 LEU   A C   1 
ATOM   556  O O   . LEU   A 1 71  ? -1.840  -1.381  21.067 1.00 17.91 ? 1864 LEU   A O   1 
ATOM   557  C CB  . LEU   A 1 71  ? -1.365  -0.346  24.092 1.00 23.21 ? 1864 LEU   A CB  1 
ATOM   558  C CG  . LEU   A 1 71  ? -0.063  0.331   24.483 1.00 22.15 ? 1864 LEU   A CG  1 
ATOM   559  C CD1 . LEU   A 1 71  ? 0.544   -0.419  25.666 1.00 20.72 ? 1864 LEU   A CD1 1 
ATOM   560  C CD2 . LEU   A 1 71  ? 0.911   0.399   23.293 1.00 22.30 ? 1864 LEU   A CD2 1 
ATOM   561  N N   . VAL   A 1 72  ? -3.644  -1.687  22.381 1.00 15.63 ? 1865 VAL   A N   1 
ATOM   562  C CA  . VAL   A 1 72  ? -4.113  -2.834  21.610 1.00 13.73 ? 1865 VAL   A CA  1 
ATOM   563  C C   . VAL   A 1 72  ? -4.369  -2.415  20.173 1.00 14.64 ? 1865 VAL   A C   1 
ATOM   564  O O   . VAL   A 1 72  ? -3.921  -3.077  19.228 1.00 20.16 ? 1865 VAL   A O   1 
ATOM   565  C CB  . VAL   A 1 72  ? -5.377  -3.437  22.237 1.00 16.43 ? 1865 VAL   A CB  1 
ATOM   566  C CG1 . VAL   A 1 72  ? -5.860  -4.621  21.420 1.00 23.86 ? 1865 VAL   A CG1 1 
ATOM   567  C CG2 . VAL   A 1 72  ? -5.080  -3.873  23.652 1.00 19.70 ? 1865 VAL   A CG2 1 
ATOM   568  N N   . PHE   A 1 73  ? -5.077  -1.293  19.994 1.00 15.68 ? 1866 PHE   A N   1 
ATOM   569  C CA  . PHE   A 1 73  ? -5.433  -0.839  18.647 1.00 19.45 ? 1866 PHE   A CA  1 
ATOM   570  C C   . PHE   A 1 73  ? -4.275  -0.160  17.932 1.00 21.10 ? 1866 PHE   A C   1 
ATOM   571  O O   . PHE   A 1 73  ? -4.183  -0.227  16.690 1.00 19.03 ? 1866 PHE   A O   1 
ATOM   572  C CB  . PHE   A 1 73  ? -6.613  0.131   18.705 1.00 19.40 ? 1866 PHE   A CB  1 
ATOM   573  C CG  . PHE   A 1 73  ? -7.713  -0.308  19.622 1.00 22.78 ? 1866 PHE   A CG  1 
ATOM   574  C CD1 . PHE   A 1 73  ? -8.216  -1.593  19.558 1.00 22.96 ? 1866 PHE   A CD1 1 
ATOM   575  C CD2 . PHE   A 1 73  ? -8.219  0.561   20.565 1.00 23.45 ? 1866 PHE   A CD2 1 
ATOM   576  C CE1 . PHE   A 1 73  ? -9.218  -2.004  20.415 1.00 25.40 ? 1866 PHE   A CE1 1 
ATOM   577  C CE2 . PHE   A 1 73  ? -9.227  0.162   21.424 1.00 30.16 ? 1866 PHE   A CE2 1 
ATOM   578  C CZ  . PHE   A 1 73  ? -9.725  -1.128  21.348 1.00 25.55 ? 1866 PHE   A CZ  1 
ATOM   579  N N   . ASP   A 1 74  ? -3.421  0.550   18.666 1.00 17.14 ? 1867 ASP   A N   1 
ATOM   580  C CA  . ASP   A 1 74  ? -2.271  1.176   18.024 1.00 19.17 ? 1867 ASP   A CA  1 
ATOM   581  C C   . ASP   A 1 74  ? -1.274  0.129   17.551 1.00 20.58 ? 1867 ASP   A C   1 
ATOM   582  O O   . ASP   A 1 74  ? -0.759  0.229   16.437 1.00 19.09 ? 1867 ASP   A O   1 
ATOM   583  C CB  . ASP   A 1 74  ? -1.599  2.166   18.967 1.00 28.78 ? 1867 ASP   A CB  1 
ATOM   584  C CG  . ASP   A 1 74  ? -2.324  3.495   19.045 1.00 29.47 ? 1867 ASP   A CG  1 
ATOM   585  O OD1 . ASP   A 1 74  ? -3.214  3.797   18.206 1.00 23.39 ? 1867 ASP   A OD1 1 
ATOM   586  O OD2 . ASP   A 1 74  ? -1.982  4.257   19.961 1.00 26.06 ? 1867 ASP   A OD2 1 
ATOM   587  N N   . ASN   A 1 75  ? -0.982  -0.875  18.383 1.00 15.80 ? 1868 ASN   A N   1 
ATOM   588  C CA  . ASN   A 1 75  ? -0.151  -1.991  17.937 1.00 15.39 ? 1868 ASN   A CA  1 
ATOM   589  C C   . ASN   A 1 75  ? -0.741  -2.651  16.697 1.00 15.70 ? 1868 ASN   A C   1 
ATOM   590  O O   . ASN   A 1 75  ? -0.006  -3.015  15.769 1.00 17.73 ? 1868 ASN   A O   1 
ATOM   591  C CB  . ASN   A 1 75  ? -0.018  -3.033  19.041 1.00 20.44 ? 1868 ASN   A CB  1 
ATOM   592  C CG  . ASN   A 1 75  ? 0.803   -2.542  20.182 1.00 15.95 ? 1868 ASN   A CG  1 
ATOM   593  O OD1 . ASN   A 1 75  ? 1.535   -1.566  20.039 1.00 19.79 ? 1868 ASN   A OD1 1 
ATOM   594  N ND2 . ASN   A 1 75  ? 0.682   -3.203  21.336 1.00 14.97 ? 1868 ASN   A ND2 1 
ATOM   595  N N   . CYS   A 1 76  ? -2.067  -2.818  16.675 1.00 16.30 ? 1869 CYS   A N   1 
ATOM   596  C CA  . CYS   A 1 76  ? -2.703  -3.531  15.574 1.00 25.74 ? 1869 CYS   A CA  1 
ATOM   597  C C   . CYS   A 1 76  ? -2.593  -2.741  14.277 1.00 21.30 ? 1869 CYS   A C   1 
ATOM   598  O O   . CYS   A 1 76  ? -2.344  -3.322  13.213 1.00 24.08 ? 1869 CYS   A O   1 
ATOM   599  C CB  . CYS   A 1 76  ? -4.168  -3.827  15.911 1.00 26.54 ? 1869 CYS   A CB  1 
ATOM   600  S SG  . CYS   A 1 76  ? -5.076  -4.656  14.571 1.00 18.97 ? 1869 CYS   A SG  1 
ATOM   601  N N   . GLN   A 1 77  ? -2.765  -1.420  14.342 1.00 18.53 ? 1870 GLN   A N   1 
ATOM   602  C CA  . GLN   A 1 77  ? -2.663  -0.599  13.126 1.00 20.21 ? 1870 GLN   A CA  1 
ATOM   603  C C   . GLN   A 1 77  ? -1.220  -0.484  12.649 1.00 22.62 ? 1870 GLN   A C   1 
ATOM   604  O O   . GLN   A 1 77  ? -0.971  -0.317  11.447 1.00 21.62 ? 1870 GLN   A O   1 
ATOM   605  C CB  . GLN   A 1 77  ? -3.257  0.800   13.382 1.00 22.93 ? 1870 GLN   A CB  1 
ATOM   606  C CG  . GLN   A 1 77  ? -3.208  1.769   12.189 1.00 35.08 ? 1870 GLN   A CG  1 
ATOM   607  C CD  . GLN   A 1 77  ? -4.068  3.022   12.378 1.00 41.12 ? 1870 GLN   A CD  1 
ATOM   608  O OE1 . GLN   A 1 77  ? -4.225  3.819   11.454 1.00 46.84 ? 1870 GLN   A OE1 1 
ATOM   609  N NE2 . GLN   A 1 77  ? -4.623  3.195   13.568 1.00 28.94 ? 1870 GLN   A NE2 1 
ATOM   610  N N   . THR   A 1 78  ? -0.262  -0.550  13.574 1.00 23.71 ? 1871 THR   A N   1 
ATOM   611  C CA  . THR   A 1 78  ? 1.145   -0.411  13.210 1.00 21.86 ? 1871 THR   A CA  1 
ATOM   612  C C   . THR   A 1 78  ? 1.633   -1.627  12.425 1.00 19.73 ? 1871 THR   A C   1 
ATOM   613  O O   . THR   A 1 78  ? 2.355   -1.487  11.423 1.00 20.90 ? 1871 THR   A O   1 
ATOM   614  C CB  . THR   A 1 78  ? 1.974   -0.206  14.482 1.00 26.50 ? 1871 THR   A CB  1 
ATOM   615  O OG1 . THR   A 1 78  ? 1.739   1.111   15.012 1.00 21.98 ? 1871 THR   A OG1 1 
ATOM   616  C CG2 . THR   A 1 78  ? 3.461   -0.387  14.196 1.00 30.83 ? 1871 THR   A CG2 1 
ATOM   617  N N   . PHE   A 1 79  ? 1.209   -2.821  12.837 1.00 24.85 ? 1872 PHE   A N   1 
ATOM   618  C CA  . PHE   A 1 79  ? 1.763   -4.072  12.337 1.00 28.69 ? 1872 PHE   A CA  1 
ATOM   619  C C   . PHE   A 1 79  ? 0.941   -4.707  11.227 1.00 28.98 ? 1872 PHE   A C   1 
ATOM   620  O O   . PHE   A 1 79  ? 1.489   -5.511  10.466 1.00 26.22 ? 1872 PHE   A O   1 
ATOM   621  C CB  . PHE   A 1 79  ? 1.890   -5.083  13.492 1.00 20.46 ? 1872 PHE   A CB  1 
ATOM   622  C CG  . PHE   A 1 79  ? 2.605   -6.359  13.117 1.00 19.38 ? 1872 PHE   A CG  1 
ATOM   623  C CD1 . PHE   A 1 79  ? 1.891   -7.503  12.776 1.00 17.80 ? 1872 PHE   A CD1 1 
ATOM   624  C CD2 . PHE   A 1 79  ? 3.996   -6.412  13.109 1.00 25.40 ? 1872 PHE   A CD2 1 
ATOM   625  C CE1 . PHE   A 1 79  ? 2.550   -8.675  12.461 1.00 18.47 ? 1872 PHE   A CE1 1 
ATOM   626  C CE2 . PHE   A 1 79  ? 4.661   -7.579  12.772 1.00 22.68 ? 1872 PHE   A CE2 1 
ATOM   627  C CZ  . PHE   A 1 79  ? 3.934   -8.710  12.460 1.00 22.43 ? 1872 PHE   A CZ  1 
ATOM   628  N N   . ASN   A 1 80  ? -0.341  -4.368  11.106 1.00 29.95 ? 1873 ASN   A N   1 
ATOM   629  C CA  . ASN   A 1 80  ? -1.247  -5.021  10.169 1.00 31.37 ? 1873 ASN   A CA  1 
ATOM   630  C C   . ASN   A 1 80  ? -1.826  -4.026  9.172  1.00 26.15 ? 1873 ASN   A C   1 
ATOM   631  O O   . ASN   A 1 80  ? -2.124  -2.880  9.514  1.00 25.75 ? 1873 ASN   A O   1 
ATOM   632  C CB  . ASN   A 1 80  ? -2.400  -5.713  10.913 1.00 28.22 ? 1873 ASN   A CB  1 
ATOM   633  C CG  . ASN   A 1 80  ? -1.919  -6.749  11.889 1.00 23.34 ? 1873 ASN   A CG  1 
ATOM   634  O OD1 . ASN   A 1 80  ? -1.532  -7.846  11.501 1.00 24.72 ? 1873 ASN   A OD1 1 
ATOM   635  N ND2 . ASN   A 1 80  ? -1.961  -6.415  13.175 1.00 21.14 ? 1873 ASN   A ND2 1 
ATOM   636  N N   . GLU   A 1 81  ? -1.995  -4.481  7.928  1.00 28.68 ? 1874 GLU   A N   1 
ATOM   637  C CA  . GLU   A 1 81  ? -2.616  -3.642  6.911  1.00 34.73 ? 1874 GLU   A CA  1 
ATOM   638  C C   . GLU   A 1 81  ? -4.107  -3.460  7.181  1.00 30.78 ? 1874 GLU   A C   1 
ATOM   639  O O   . GLU   A 1 81  ? -4.766  -4.318  7.776  1.00 30.57 ? 1874 GLU   A O   1 
ATOM   640  C CB  . GLU   A 1 81  ? -2.402  -4.248  5.528  1.00 42.07 ? 1874 GLU   A CB  1 
ATOM   641  C CG  . GLU   A 1 81  ? -0.961  -4.634  5.252  1.00 51.15 ? 1874 GLU   A CG  1 
ATOM   642  C CD  . GLU   A 1 81  ? -0.033  -3.436  5.238  1.00 57.09 ? 1874 GLU   A CD  1 
ATOM   643  O OE1 . GLU   A 1 81  ? -0.505  -2.325  4.910  1.00 64.59 ? 1874 GLU   A OE1 1 
ATOM   644  O OE2 . GLU   A 1 81  ? 1.165   -3.604  5.558  1.00 56.31 ? 1874 GLU   A OE2 1 
ATOM   645  N N   . ASP   A 1 82  ? -4.640  -2.317  6.736  1.00 32.24 ? 1875 ASP   A N   1 
ATOM   646  C CA  . ASP   A 1 82  ? -6.059  -2.034  6.942  1.00 39.71 ? 1875 ASP   A CA  1 
ATOM   647  C C   . ASP   A 1 82  ? -6.936  -3.091  6.285  1.00 42.20 ? 1875 ASP   A C   1 
ATOM   648  O O   . ASP   A 1 82  ? -8.041  -3.373  6.766  1.00 45.07 ? 1875 ASP   A O   1 
ATOM   649  C CB  . ASP   A 1 82  ? -6.416  -0.648  6.394  1.00 40.80 ? 1875 ASP   A CB  1 
ATOM   650  C CG  . ASP   A 1 82  ? -5.680  0.481   7.100  1.00 40.94 ? 1875 ASP   A CG  1 
ATOM   651  O OD1 . ASP   A 1 82  ? -4.987  0.225   8.108  1.00 40.44 ? 1875 ASP   A OD1 1 
ATOM   652  O OD2 . ASP   A 1 82  ? -5.794  1.637   6.639  1.00 46.54 ? 1875 ASP   A OD2 1 
ATOM   653  N N   . ASP   A 1 83  ? -6.453  -3.693  5.199  1.00 37.50 ? 1876 ASP   A N   1 
ATOM   654  C CA  . ASP   A 1 83  ? -7.231  -4.653  4.435  1.00 41.65 ? 1876 ASP   A CA  1 
ATOM   655  C C   . ASP   A 1 83  ? -7.188  -6.057  5.019  1.00 36.61 ? 1876 ASP   A C   1 
ATOM   656  O O   . ASP   A 1 83  ? -8.014  -6.887  4.627  1.00 38.01 ? 1876 ASP   A O   1 
ATOM   657  C CB  . ASP   A 1 83  ? -6.745  -4.671  2.980  1.00 55.88 ? 1876 ASP   A CB  1 
ATOM   658  C CG  . ASP   A 1 83  ? -5.239  -4.836  2.866  1.00 72.43 ? 1876 ASP   A CG  1 
ATOM   659  O OD1 . ASP   A 1 83  ? -4.750  -5.978  3.000  1.00 77.88 ? 1876 ASP   A OD1 1 
ATOM   660  O OD2 . ASP   A 1 83  ? -4.544  -3.823  2.637  1.00 78.24 ? 1876 ASP   A OD2 1 
ATOM   661  N N   . SER   A 1 84  ? -6.268  -6.337  5.946  1.00 33.98 ? 1877 SER   A N   1 
ATOM   662  C CA  . SER   A 1 84  ? -6.207  -7.652  6.569  1.00 33.98 ? 1877 SER   A CA  1 
ATOM   663  C C   . SER   A 1 84  ? -7.387  -7.834  7.520  1.00 31.10 ? 1877 SER   A C   1 
ATOM   664  O O   . SER   A 1 84  ? -8.011  -6.869  7.961  1.00 31.19 ? 1877 SER   A O   1 
ATOM   665  C CB  . SER   A 1 84  ? -4.895  -7.836  7.334  1.00 30.45 ? 1877 SER   A CB  1 
ATOM   666  O OG  . SER   A 1 84  ? -4.930  -7.110  8.553  1.00 27.82 ? 1877 SER   A OG  1 
ATOM   667  N N   . GLU   A 1 85  ? -7.710  -9.097  7.810  1.00 31.84 ? 1878 GLU   A N   1 
ATOM   668  C CA  . GLU   A 1 85  ? -8.806  -9.374  8.733  1.00 33.84 ? 1878 GLU   A CA  1 
ATOM   669  C C   . GLU   A 1 85  ? -8.506  -8.826  10.124 1.00 31.86 ? 1878 GLU   A C   1 
ATOM   670  O O   . GLU   A 1 85  ? -9.401  -8.295  10.794 1.00 26.46 ? 1878 GLU   A O   1 
ATOM   671  C CB  . GLU   A 1 85  ? -9.077  -10.876 8.796  1.00 30.35 ? 1878 GLU   A CB  1 
ATOM   672  C CG  . GLU   A 1 85  ? -9.574  -11.478 7.481  1.00 33.55 ? 1878 GLU   A CG  1 
ATOM   673  C CD  . GLU   A 1 85  ? -10.831 -10.797 6.969  1.00 36.75 ? 1878 GLU   A CD  1 
ATOM   674  O OE1 . GLU   A 1 85  ? -10.832 -10.356 5.803  1.00 39.01 ? 1878 GLU   A OE1 1 
ATOM   675  O OE2 . GLU   A 1 85  ? -11.811 -10.688 7.738  1.00 38.42 ? 1878 GLU   A OE2 1 
ATOM   676  N N   . VAL   A 1 86  ? -7.253  -8.941  10.573 1.00 25.63 ? 1879 VAL   A N   1 
ATOM   677  C CA  . VAL   A 1 86  ? -6.883  -8.416  11.892 1.00 22.96 ? 1879 VAL   A CA  1 
ATOM   678  C C   . VAL   A 1 86  ? -6.865  -6.890  11.879 1.00 22.80 ? 1879 VAL   A C   1 
ATOM   679  O O   . VAL   A 1 86  ? -7.350  -6.246  12.816 1.00 23.32 ? 1879 VAL   A O   1 
ATOM   680  C CB  . VAL   A 1 86  ? -5.537  -9.004  12.343 1.00 21.70 ? 1879 VAL   A CB  1 
ATOM   681  C CG1 . VAL   A 1 86  ? -5.013  -8.269  13.589 1.00 19.57 ? 1879 VAL   A CG1 1 
ATOM   682  C CG2 . VAL   A 1 86  ? -5.700  -10.488 12.621 1.00 23.29 ? 1879 VAL   A CG2 1 
ATOM   683  N N   . GLY   A 1 87  ? -6.347  -6.286  10.804 1.00 24.23 ? 1880 GLY   A N   1 
ATOM   684  C CA  . GLY   A 1 87  ? -6.399  -4.836  10.693 1.00 24.53 ? 1880 GLY   A CA  1 
ATOM   685  C C   . GLY   A 1 87  ? -7.820  -4.306  10.688 1.00 25.45 ? 1880 GLY   A C   1 
ATOM   686  O O   . GLY   A 1 87  ? -8.140  -3.335  11.379 1.00 24.74 ? 1880 GLY   A O   1 
ATOM   687  N N   . LYS   A 1 88  ? -8.691  -4.960  9.923  1.00 27.36 ? 1881 LYS   A N   1 
ATOM   688  C CA  . LYS   A 1 88  ? -10.107 -4.519  9.877  1.00 28.48 ? 1881 LYS   A CA  1 
ATOM   689  C C   . LYS   A 1 88  ? -10.682 -4.574  11.297 1.00 26.67 ? 1881 LYS   A C   1 
ATOM   690  O O   . LYS   A 1 88  ? -11.366 -3.623  11.699 1.00 27.59 ? 1881 LYS   A O   1 
ATOM   691  C CB  . LYS   A 1 88  ? -10.917 -5.453  8.973  1.00 32.08 ? 1881 LYS   A CB  1 
ATOM   692  C CG  . LYS   A 1 88  ? -10.749 -5.239  7.476  1.00 42.57 ? 1881 LYS   A CG  1 
ATOM   693  C CD  . LYS   A 1 88  ? -11.898 -5.802  6.660  1.00 44.65 ? 1881 LYS   A CD  1 
ATOM   694  C CE  . LYS   A 1 88  ? -11.453 -6.526  5.405  1.00 51.38 ? 1881 LYS   A CE  1 
ATOM   695  N NZ  . LYS   A 1 88  ? -11.917 -7.934  5.369  1.00 43.95 ? 1881 LYS   A NZ  1 
ATOM   696  N N   . ALA   A 1 89  ? -10.326 -5.616  12.049 1.00 25.18 ? 1882 ALA   A N   1 
ATOM   697  C CA  . ALA   A 1 89  ? -10.913 -5.818  13.368 1.00 23.97 ? 1882 ALA   A CA  1 
ATOM   698  C C   . ALA   A 1 89  ? -10.450 -4.750  14.353 1.00 26.87 ? 1882 ALA   A C   1 
ATOM   699  O O   . ALA   A 1 89  ? -11.235 -4.287  15.195 1.00 24.01 ? 1882 ALA   A O   1 
ATOM   700  C CB  . ALA   A 1 89  ? -10.568 -7.217  13.874 1.00 27.13 ? 1882 ALA   A CB  1 
ATOM   701  N N   . GLY   A 1 90  ? -9.186  -4.331  14.249 1.00 26.73 ? 1883 GLY   A N   1 
ATOM   702  C CA  . GLY   A 1 90  ? -8.681  -3.305  15.148 1.00 25.63 ? 1883 GLY   A CA  1 
ATOM   703  C C   . GLY   A 1 90  ? -9.325  -1.953  14.909 1.00 21.46 ? 1883 GLY   A C   1 
ATOM   704  O O   . GLY   A 1 90  ? -9.598  -1.205  15.840 1.00 21.07 ? 1883 GLY   A O   1 
ATOM   705  N N   . HIS   A 1 91  ? -9.554  -1.601  13.646 1.00 23.24 ? 1884 HIS   A N   1 
ATOM   706  C CA  . HIS   A 1 91  ? -10.263 -0.357  13.383 1.00 24.76 ? 1884 HIS   A CA  1 
ATOM   707  C C   . HIS   A 1 91  ? -11.687 -0.399  13.938 1.00 25.55 ? 1884 HIS   A C   1 
ATOM   708  O O   . HIS   A 1 91  ? -12.185 0.603   14.447 1.00 26.08 ? 1884 HIS   A O   1 
ATOM   709  C CB  . HIS   A 1 91  ? -10.275 -0.079  11.886 1.00 34.58 ? 1884 HIS   A CB  1 
ATOM   710  C CG  . HIS   A 1 91  ? -8.931  0.280   11.330 1.00 34.09 ? 1884 HIS   A CG  1 
ATOM   711  N ND1 . HIS   A 1 91  ? -8.200  1.354   11.789 1.00 29.49 ? 1884 HIS   A ND1 1 
ATOM   712  C CD2 . HIS   A 1 91  ? -8.194  -0.282  10.341 1.00 27.59 ? 1884 HIS   A CD2 1 
ATOM   713  C CE1 . HIS   A 1 91  ? -7.072  1.443   11.104 1.00 30.37 ? 1884 HIS   A CE1 1 
ATOM   714  N NE2 . HIS   A 1 91  ? -7.043  0.458   10.224 1.00 27.44 ? 1884 HIS   A NE2 1 
ATOM   715  N N   . ILE   A 1 92  ? -12.353 -1.551  13.849 1.00 25.90 ? 1885 ILE   A N   1 
ATOM   716  C CA  . ILE   A 1 92  ? -13.723 -1.660  14.344 1.00 29.05 ? 1885 ILE   A CA  1 
ATOM   717  C C   . ILE   A 1 92  ? -13.747 -1.574  15.864 1.00 25.65 ? 1885 ILE   A C   1 
ATOM   718  O O   . ILE   A 1 92  ? -14.600 -0.893  16.457 1.00 27.52 ? 1885 ILE   A O   1 
ATOM   719  C CB  . ILE   A 1 92  ? -14.360 -2.968  13.850 1.00 27.96 ? 1885 ILE   A CB  1 
ATOM   720  C CG1 . ILE   A 1 92  ? -14.685 -2.854  12.355 1.00 30.23 ? 1885 ILE   A CG1 1 
ATOM   721  C CG2 . ILE   A 1 92  ? -15.600 -3.312  14.667 1.00 35.79 ? 1885 ILE   A CG2 1 
ATOM   722  C CD1 . ILE   A 1 92  ? -15.151 -4.141  11.716 1.00 39.45 ? 1885 ILE   A CD1 1 
ATOM   723  N N   . MET   A 1 93  ? -12.820 -2.273  16.523 1.00 27.97 ? 1886 MET   A N   1 
ATOM   724  C CA  . MET   A 1 93  ? -12.808 -2.246  17.978 1.00 25.35 ? 1886 MET   A CA  1 
ATOM   725  C C   . MET   A 1 93  ? -12.383 -0.887  18.509 1.00 26.46 ? 1886 MET   A C   1 
ATOM   726  O O   . MET   A 1 93  ? -12.791 -0.507  19.611 1.00 23.91 ? 1886 MET   A O   1 
ATOM   727  C CB  . MET   A 1 93  ? -11.887 -3.339  18.525 1.00 28.09 ? 1886 MET   A CB  1 
ATOM   728  C CG  . MET   A 1 93  ? -12.352 -4.739  18.182 1.00 27.34 ? 1886 MET   A CG  1 
ATOM   729  S SD  . MET   A 1 93  ? -13.945 -5.131  18.931 1.00 28.51 ? 1886 MET   A SD  1 
ATOM   730  C CE  . MET   A 1 93  ? -13.637 -4.713  20.653 1.00 26.45 ? 1886 MET   A CE  1 
ATOM   731  N N   . ARG   A 1 94  ? -11.568 -0.138  17.756 1.00 22.16 ? 1887 ARG   A N   1 
ATOM   732  C CA  . ARG   A 1 94  ? -11.207 1.197   18.226 1.00 34.55 ? 1887 ARG   A CA  1 
ATOM   733  C C   . ARG   A 1 94  ? -12.423 2.109   18.241 1.00 31.17 ? 1887 ARG   A C   1 
ATOM   734  O O   . ARG   A 1 94  ? -12.648 2.841   19.211 1.00 33.02 ? 1887 ARG   A O   1 
ATOM   735  C CB  . ARG   A 1 94  ? -10.101 1.819   17.374 1.00 26.95 ? 1887 ARG   A CB  1 
ATOM   736  C CG  . ARG   A 1 94  ? -9.621  3.168   17.932 1.00 32.74 ? 1887 ARG   A CG  1 
ATOM   737  C CD  . ARG   A 1 94  ? -8.843  4.006   16.930 1.00 22.67 ? 1887 ARG   A CD  1 
ATOM   738  N NE  . ARG   A 1 94  ? -7.618  3.350   16.502 1.00 21.48 ? 1887 ARG   A NE  1 
ATOM   739  C CZ  . ARG   A 1 94  ? -6.447  3.454   17.124 1.00 25.67 ? 1887 ARG   A CZ  1 
ATOM   740  N NH1 . ARG   A 1 94  ? -6.329  4.208   18.209 1.00 20.93 ? 1887 ARG   A NH1 1 
ATOM   741  N NH2 . ARG   A 1 94  ? -5.389  2.821   16.647 1.00 24.54 ? 1887 ARG   A NH2 1 
ATOM   742  N N   . ARG   A 1 95  ? -13.225 2.038   17.178 1.00 25.92 ? 1888 ARG   A N   1 
ATOM   743  C CA  . ARG   A 1 95  ? -14.446 2.881   17.101 1.00 31.59 ? 1888 ARG   A CA  1 
ATOM   744  C C   . ARG   A 1 95  ? -15.390 2.483   18.236 1.00 29.99 ? 1888 ARG   A C   1 
ATOM   745  O O   . ARG   A 1 95  ? -15.965 3.383   18.858 1.00 30.19 ? 1888 ARG   A O   1 
ATOM   746  C CB  . ARG   A 1 95  ? -15.129 2.745   15.737 1.00 33.29 ? 1888 ARG   A CB  1 
ATOM   747  C CG  . ARG   A 1 95  ? -16.539 3.320   15.697 1.00 38.24 ? 1888 ARG   A CG  1 
ATOM   748  C CD  . ARG   A 1 95  ? -16.605 4.682   15.032 1.00 43.84 ? 1888 ARG   A CD  1 
ATOM   749  N NE  . ARG   A 1 95  ? -17.949 5.248   15.043 1.00 43.08 ? 1888 ARG   A NE  1 
ATOM   750  C CZ  . ARG   A 1 95  ? -19.035 4.602   14.642 1.00 46.96 ? 1888 ARG   A CZ  1 
ATOM   751  N NH1 . ARG   A 1 95  ? -18.938 3.367   14.188 1.00 46.79 ? 1888 ARG   A NH1 1 
ATOM   752  N NH2 . ARG   A 1 95  ? -20.214 5.190   14.690 1.00 53.40 ? 1888 ARG   A NH2 1 
ATOM   753  N N   . PHE   A 1 96  ? -15.536 1.179   18.488 1.00 34.75 ? 1889 PHE   A N   1 
ATOM   754  C CA  . PHE   A 1 96  ? -16.416 0.734   19.564 1.00 37.23 ? 1889 PHE   A CA  1 
ATOM   755  C C   . PHE   A 1 96  ? -15.925 1.252   20.908 1.00 33.86 ? 1889 PHE   A C   1 
ATOM   756  O O   . PHE   A 1 96  ? -16.698 1.819   21.689 1.00 31.85 ? 1889 PHE   A O   1 
ATOM   757  C CB  . PHE   A 1 96  ? -16.522 -0.791  19.584 1.00 30.81 ? 1889 PHE   A CB  1 
ATOM   758  C CG  . PHE   A 1 96  ? -17.412 -1.315  20.680 1.00 31.27 ? 1889 PHE   A CG  1 
ATOM   759  C CD1 . PHE   A 1 96  ? -16.871 -1.890  21.826 1.00 27.99 ? 1889 PHE   A CD1 1 
ATOM   760  C CD2 . PHE   A 1 96  ? -18.790 -1.215  20.577 1.00 41.28 ? 1889 PHE   A CD2 1 
ATOM   761  C CE1 . PHE   A 1 96  ? -17.690 -2.363  22.834 1.00 29.43 ? 1889 PHE   A CE1 1 
ATOM   762  C CE2 . PHE   A 1 96  ? -19.612 -1.690  21.580 1.00 39.65 ? 1889 PHE   A CE2 1 
ATOM   763  C CZ  . PHE   A 1 96  ? -19.057 -2.266  22.715 1.00 35.95 ? 1889 PHE   A CZ  1 
ATOM   764  N N   . PHE   A 1 97  ? -14.632 1.076   21.182 1.00 30.40 ? 1890 PHE   A N   1 
ATOM   765  C CA  . PHE   A 1 97  ? -14.054 1.604   22.410 1.00 27.49 ? 1890 PHE   A CA  1 
ATOM   766  C C   . PHE   A 1 97  ? -14.238 3.106   22.499 1.00 26.53 ? 1890 PHE   A C   1 
ATOM   767  O O   . PHE   A 1 97  ? -14.662 3.629   23.531 1.00 27.76 ? 1890 PHE   A O   1 
ATOM   768  C CB  . PHE   A 1 97  ? -12.566 1.258   22.501 1.00 22.82 ? 1890 PHE   A CB  1 
ATOM   769  C CG  . PHE   A 1 97  ? -11.849 1.992   23.613 1.00 22.45 ? 1890 PHE   A CG  1 
ATOM   770  C CD1 . PHE   A 1 97  ? -11.889 1.515   24.922 1.00 23.71 ? 1890 PHE   A CD1 1 
ATOM   771  C CD2 . PHE   A 1 97  ? -11.154 3.165   23.358 1.00 29.65 ? 1890 PHE   A CD2 1 
ATOM   772  C CE1 . PHE   A 1 97  ? -11.244 2.185   25.949 1.00 31.13 ? 1890 PHE   A CE1 1 
ATOM   773  C CE2 . PHE   A 1 97  ? -10.503 3.839   24.387 1.00 32.05 ? 1890 PHE   A CE2 1 
ATOM   774  C CZ  . PHE   A 1 97  ? -10.547 3.343   25.681 1.00 27.58 ? 1890 PHE   A CZ  1 
ATOM   775  N N   . GLU   A 1 98  ? -13.884 3.825   21.437 1.00 28.90 ? 1891 GLU   A N   1 
ATOM   776  C CA  . GLU   A 1 98  ? -14.083 5.268   21.447 1.00 37.67 ? 1891 GLU   A CA  1 
ATOM   777  C C   . GLU   A 1 98  ? -15.546 5.655   21.621 1.00 36.99 ? 1891 GLU   A C   1 
ATOM   778  O O   . GLU   A 1 98  ? -15.826 6.736   22.143 1.00 34.66 ? 1891 GLU   A O   1 
ATOM   779  C CB  . GLU   A 1 98  ? -13.531 5.888   20.168 1.00 36.64 ? 1891 GLU   A CB  1 
ATOM   780  C CG  . GLU   A 1 98  ? -12.017 5.914   20.096 1.00 36.09 ? 1891 GLU   A CG  1 
ATOM   781  C CD  . GLU   A 1 98  ? -11.534 6.526   18.806 1.00 37.26 ? 1891 GLU   A CD  1 
ATOM   782  O OE1 . GLU   A 1 98  ? -12.367 6.693   17.898 1.00 47.36 ? 1891 GLU   A OE1 1 
ATOM   783  O OE2 . GLU   A 1 98  ? -10.335 6.837   18.702 1.00 44.13 ? 1891 GLU   A OE2 1 
ATOM   784  N N   . SER   A 1 99  ? -16.489 4.808   21.207 1.00 36.78 ? 1892 SER   A N   1 
ATOM   785  C CA  . SER   A 1 99  ? -17.888 5.185   21.362 1.00 41.55 ? 1892 SER   A CA  1 
ATOM   786  C C   . SER   A 1 99  ? -18.356 4.977   22.795 1.00 41.81 ? 1892 SER   A C   1 
ATOM   787  O O   . SER   A 1 99  ? -19.034 5.845   23.357 1.00 45.40 ? 1892 SER   A O   1 
ATOM   788  C CB  . SER   A 1 99  ? -18.767 4.402   20.385 1.00 48.72 ? 1892 SER   A CB  1 
ATOM   789  O OG  . SER   A 1 99  ? -19.013 3.082   20.838 1.00 57.53 ? 1892 SER   A OG  1 
ATOM   790  N N   . ARG   A 1 100 ? -17.996 3.840   23.400 1.00 36.07 ? 1893 ARG   A N   1 
ATOM   791  C CA  . ARG   A 1 100 ? -18.383 3.584   24.782 1.00 34.83 ? 1893 ARG   A CA  1 
ATOM   792  C C   . ARG   A 1 100 ? -17.658 4.522   25.735 1.00 45.70 ? 1893 ARG   A C   1 
ATOM   793  O O   . ARG   A 1 100 ? -18.237 4.978   26.731 1.00 49.30 ? 1893 ARG   A O   1 
ATOM   794  C CB  . ARG   A 1 100 ? -18.102 2.124   25.138 1.00 38.53 ? 1893 ARG   A CB  1 
ATOM   795  C CG  . ARG   A 1 100 ? -18.953 1.135   24.348 1.00 39.55 ? 1893 ARG   A CG  1 
ATOM   796  C CD  . ARG   A 1 100 ? -20.430 1.405   24.580 1.00 40.82 ? 1893 ARG   A CD  1 
ATOM   797  N NE  . ARG   A 1 100 ? -20.971 0.669   25.720 1.00 42.52 ? 1893 ARG   A NE  1 
ATOM   798  C CZ  . ARG   A 1 100 ? -22.002 1.085   26.449 1.00 45.65 ? 1893 ARG   A CZ  1 
ATOM   799  N NH1 . ARG   A 1 100 ? -22.593 2.238   26.169 1.00 50.20 ? 1893 ARG   A NH1 1 
ATOM   800  N NH2 . ARG   A 1 100 ? -22.438 0.353   27.466 1.00 43.41 ? 1893 ARG   A NH2 1 
ATOM   801  N N   . TRP   A 1 101 ? -16.396 4.836   25.431 1.00 38.46 ? 1894 TRP   A N   1 
ATOM   802  C CA  . TRP   A 1 101 ? -15.600 5.678   26.317 1.00 35.50 ? 1894 TRP   A CA  1 
ATOM   803  C C   . TRP   A 1 101 ? -16.142 7.097   26.380 1.00 39.49 ? 1894 TRP   A C   1 
ATOM   804  O O   . TRP   A 1 101 ? -16.021 7.764   27.414 1.00 47.79 ? 1894 TRP   A O   1 
ATOM   805  C CB  . TRP   A 1 101 ? -14.149 5.695   25.848 1.00 31.13 ? 1894 TRP   A CB  1 
ATOM   806  C CG  . TRP   A 1 101 ? -13.214 6.319   26.835 1.00 30.87 ? 1894 TRP   A CG  1 
ATOM   807  C CD1 . TRP   A 1 101 ? -12.739 7.598   26.822 1.00 36.03 ? 1894 TRP   A CD1 1 
ATOM   808  C CD2 . TRP   A 1 101 ? -12.648 5.693   27.988 1.00 28.74 ? 1894 TRP   A CD2 1 
ATOM   809  N NE1 . TRP   A 1 101 ? -11.901 7.803   27.892 1.00 37.83 ? 1894 TRP   A NE1 1 
ATOM   810  C CE2 . TRP   A 1 101 ? -11.825 6.646   28.620 1.00 33.20 ? 1894 TRP   A CE2 1 
ATOM   811  C CE3 . TRP   A 1 101 ? -12.745 4.412   28.541 1.00 31.90 ? 1894 TRP   A CE3 1 
ATOM   812  C CZ2 . TRP   A 1 101 ? -11.113 6.362   29.792 1.00 31.84 ? 1894 TRP   A CZ2 1 
ATOM   813  C CZ3 . TRP   A 1 101 ? -12.037 4.132   29.701 1.00 35.01 ? 1894 TRP   A CZ3 1 
ATOM   814  C CH2 . TRP   A 1 101 ? -11.235 5.104   30.311 1.00 28.30 ? 1894 TRP   A CH2 1 
ATOM   815  N N   . GLU   A 1 102 ? -16.738 7.571   25.292 1.00 40.72 ? 1895 GLU   A N   1 
ATOM   816  C CA  . GLU   A 1 102 ? -17.218 8.943   25.220 1.00 45.93 ? 1895 GLU   A CA  1 
ATOM   817  C C   . GLU   A 1 102 ? -18.644 9.097   25.723 1.00 51.61 ? 1895 GLU   A C   1 
ATOM   818  O O   . GLU   A 1 102 ? -19.018 10.194  26.154 1.00 53.94 ? 1895 GLU   A O   1 
ATOM   819  C CB  . GLU   A 1 102 ? -17.095 9.459   23.781 1.00 55.27 ? 1895 GLU   A CB  1 
ATOM   820  C CG  . GLU   A 1 102 ? -15.736 10.119  23.436 1.00 64.22 ? 1895 GLU   A CG  1 
ATOM   821  C CD  . GLU   A 1 102 ? -14.509 9.209   23.607 1.00 67.68 ? 1895 GLU   A CD  1 
ATOM   822  O OE1 . GLU   A 1 102 ? -14.645 8.030   23.983 1.00 66.71 ? 1895 GLU   A OE1 1 
ATOM   823  O OE2 . GLU   A 1 102 ? -13.383 9.688   23.362 1.00 70.18 ? 1895 GLU   A OE2 1 
ATOM   824  N N   . GLU   A 1 103 ? -19.451 8.035   25.698 1.00 56.36 ? 1896 GLU   A N   1 
ATOM   825  C CA  . GLU   A 1 103 ? -20.751 8.069   26.354 1.00 63.36 ? 1896 GLU   A CA  1 
ATOM   826  C C   . GLU   A 1 103 ? -20.668 7.648   27.816 1.00 58.97 ? 1896 GLU   A C   1 
ATOM   827  O O   . GLU   A 1 103 ? -21.704 7.379   28.435 1.00 63.50 ? 1896 GLU   A O   1 
ATOM   828  C CB  . GLU   A 1 103 ? -21.778 7.219   25.591 1.00 71.83 ? 1896 GLU   A CB  1 
ATOM   829  C CG  . GLU   A 1 103 ? -21.396 5.778   25.302 1.00 73.09 ? 1896 GLU   A CG  1 
ATOM   830  C CD  . GLU   A 1 103 ? -22.150 5.216   24.099 1.00 68.96 ? 1896 GLU   A CD  1 
ATOM   831  O OE1 . GLU   A 1 103 ? -23.137 5.852   23.665 1.00 70.28 ? 1896 GLU   A OE1 1 
ATOM   832  O OE2 . GLU   A 1 103 ? -21.751 4.149   23.582 1.00 63.14 ? 1896 GLU   A OE2 1 
ATOM   833  N N   . PHE   A 1 104 ? -19.456 7.587   28.372 1.00 55.81 ? 1897 PHE   A N   1 
ATOM   834  C CA  . PHE   A 1 104 ? -19.233 7.523   29.814 1.00 51.78 ? 1897 PHE   A CA  1 
ATOM   835  C C   . PHE   A 1 104 ? -18.392 8.699   30.292 1.00 55.30 ? 1897 PHE   A C   1 
ATOM   836  O O   . PHE   A 1 104 ? -18.836 9.463   31.155 1.00 57.19 ? 1897 PHE   A O   1 
ATOM   837  C CB  . PHE   A 1 104 ? -18.554 6.203   30.204 1.00 53.83 ? 1897 PHE   A CB  1 
ATOM   838  C CG  . PHE   A 1 104 ? -19.382 4.981   29.931 1.00 59.76 ? 1897 PHE   A CG  1 
ATOM   839  C CD1 . PHE   A 1 104 ? -20.759 5.010   30.078 1.00 69.56 ? 1897 PHE   A CD1 1 
ATOM   840  C CD2 . PHE   A 1 104 ? -18.781 3.798   29.531 1.00 50.94 ? 1897 PHE   A CD2 1 
ATOM   841  C CE1 . PHE   A 1 104 ? -21.521 3.886   29.827 1.00 68.45 ? 1897 PHE   A CE1 1 
ATOM   842  C CE2 . PHE   A 1 104 ? -19.535 2.672   29.277 1.00 52.53 ? 1897 PHE   A CE2 1 
ATOM   843  C CZ  . PHE   A 1 104 ? -20.908 2.715   29.425 1.00 62.02 ? 1897 PHE   A CZ  1 
ATOM   844  N N   . TYR   A 1 105 ? -17.193 8.880   29.740 1.00 60.82 ? 1898 TYR   A N   1 
ATOM   845  C CA  . TYR   A 1 105 ? -16.280 9.944   30.163 1.00 55.93 ? 1898 TYR   A CA  1 
ATOM   846  C C   . TYR   A 1 105 ? -16.343 11.145  29.225 1.00 51.36 ? 1898 TYR   A C   1 
ATOM   847  O O   . TYR   A 1 105 ? -17.254 11.964  29.305 1.00 54.55 ? 1898 TYR   A O   1 
ATOM   848  C CB  . TYR   A 1 105 ? -14.852 9.408   30.233 1.00 49.95 ? 1898 TYR   A CB  1 
ATOM   849  C CG  . TYR   A 1 105 ? -14.723 8.167   31.083 1.00 53.38 ? 1898 TYR   A CG  1 
ATOM   850  C CD1 . TYR   A 1 105 ? -14.464 8.260   32.446 1.00 62.34 ? 1898 TYR   A CD1 1 
ATOM   851  C CD2 . TYR   A 1 105 ? -14.888 6.905   30.533 1.00 50.68 ? 1898 TYR   A CD2 1 
ATOM   852  C CE1 . TYR   A 1 105 ? -14.359 7.128   33.234 1.00 56.77 ? 1898 TYR   A CE1 1 
ATOM   853  C CE2 . TYR   A 1 105 ? -14.783 5.766   31.314 1.00 53.51 ? 1898 TYR   A CE2 1 
ATOM   854  C CZ  . TYR   A 1 105 ? -14.519 5.886   32.660 1.00 54.40 ? 1898 TYR   A CZ  1 
ATOM   855  O OH  . TYR   A 1 105 ? -14.414 4.762   33.443 1.00 61.84 ? 1898 TYR   A OH  1 
ATOM   856  N N   . HIS   B 1 3   ? 12.652  9.426   28.144 1.00 59.86 ? 1796 HIS   B N   1 
ATOM   857  C CA  . HIS   B 1 3   ? 12.116  8.612   29.231 1.00 58.45 ? 1796 HIS   B CA  1 
ATOM   858  C C   . HIS   B 1 3   ? 11.541  7.306   28.701 1.00 56.72 ? 1796 HIS   B C   1 
ATOM   859  O O   . HIS   B 1 3   ? 10.832  6.595   29.414 1.00 53.70 ? 1796 HIS   B O   1 
ATOM   860  C CB  . HIS   B 1 3   ? 11.038  9.379   30.004 1.00 60.12 ? 1796 HIS   B CB  1 
ATOM   861  C CG  . HIS   B 1 3   ? 11.576  10.483  30.860 1.00 65.16 ? 1796 HIS   B CG  1 
ATOM   862  N ND1 . HIS   B 1 3   ? 10.835  11.075  31.860 1.00 66.06 ? 1796 HIS   B ND1 1 
ATOM   863  C CD2 . HIS   B 1 3   ? 12.780  11.102  30.868 1.00 68.89 ? 1796 HIS   B CD2 1 
ATOM   864  C CE1 . HIS   B 1 3   ? 11.559  12.010  32.448 1.00 69.13 ? 1796 HIS   B CE1 1 
ATOM   865  N NE2 . HIS   B 1 3   ? 12.744  12.048  31.864 1.00 70.86 ? 1796 HIS   B NE2 1 
ATOM   866  N N   . SER   B 1 4   ? 11.843  6.998   27.441 1.00 61.21 ? 1797 SER   B N   1 
ATOM   867  C CA  . SER   B 1 4   ? 11.371  5.770   26.819 1.00 62.03 ? 1797 SER   B CA  1 
ATOM   868  C C   . SER   B 1 4   ? 12.308  4.596   27.054 1.00 62.51 ? 1797 SER   B C   1 
ATOM   869  O O   . SER   B 1 4   ? 11.903  3.449   26.836 1.00 69.33 ? 1797 SER   B O   1 
ATOM   870  C CB  . SER   B 1 4   ? 11.181  5.973   25.308 1.00 62.18 ? 1797 SER   B CB  1 
ATOM   871  O OG  . SER   B 1 4   ? 12.374  5.687   24.596 1.00 67.93 ? 1797 SER   B OG  1 
ATOM   872  N N   . ASP   B 1 5   ? 13.544  4.853   27.479 1.00 55.25 ? 1798 ASP   B N   1 
ATOM   873  C CA  . ASP   B 1 5   ? 14.495  3.794   27.793 1.00 50.04 ? 1798 ASP   B CA  1 
ATOM   874  C C   . ASP   B 1 5   ? 14.239  3.345   29.226 1.00 49.36 ? 1798 ASP   B C   1 
ATOM   875  O O   . ASP   B 1 5   ? 14.486  4.095   30.175 1.00 49.86 ? 1798 ASP   B O   1 
ATOM   876  C CB  . ASP   B 1 5   ? 15.931  4.275   27.606 1.00 58.61 ? 1798 ASP   B CB  1 
ATOM   877  C CG  . ASP   B 1 5   ? 16.925  3.127   27.533 1.00 63.94 ? 1798 ASP   B CG  1 
ATOM   878  O OD1 . ASP   B 1 5   ? 16.600  2.030   28.031 1.00 61.78 ? 1798 ASP   B OD1 1 
ATOM   879  O OD2 . ASP   B 1 5   ? 18.029  3.317   26.979 1.00 62.32 ? 1798 ASP   B OD2 1 
ATOM   880  N N   . LEU   B 1 6   ? 13.728  2.124   29.376 1.00 47.00 ? 1799 LEU   B N   1 
ATOM   881  C CA  . LEU   B 1 6   ? 13.422  1.548   30.674 1.00 37.71 ? 1799 LEU   B CA  1 
ATOM   882  C C   . LEU   B 1 6   ? 14.629  0.861   31.307 1.00 34.23 ? 1799 LEU   B C   1 
ATOM   883  O O   . LEU   B 1 6   ? 14.457  0.056   32.232 1.00 44.86 ? 1799 LEU   B O   1 
ATOM   884  C CB  . LEU   B 1 6   ? 12.255  0.565   30.542 1.00 35.64 ? 1799 LEU   B CB  1 
ATOM   885  C CG  . LEU   B 1 6   ? 10.819  1.089   30.664 1.00 39.50 ? 1799 LEU   B CG  1 
ATOM   886  C CD1 . LEU   B 1 6   ? 10.424  1.268   32.126 1.00 43.21 ? 1799 LEU   B CD1 1 
ATOM   887  C CD2 . LEU   B 1 6   ? 10.599  2.376   29.888 1.00 38.91 ? 1799 LEU   B CD2 1 
ATOM   888  N N   . THR   B 1 7   ? 15.841  1.176   30.842 1.00 32.17 ? 1800 THR   B N   1 
ATOM   889  C CA  . THR   B 1 7   ? 17.041  0.515   31.352 1.00 33.79 ? 1800 THR   B CA  1 
ATOM   890  C C   . THR   B 1 7   ? 17.282  0.857   32.816 1.00 30.83 ? 1800 THR   B C   1 
ATOM   891  O O   . THR   B 1 7   ? 17.567  -0.031  33.626 1.00 34.23 ? 1800 THR   B O   1 
ATOM   892  C CB  . THR   B 1 7   ? 18.264  0.893   30.508 1.00 35.65 ? 1800 THR   B CB  1 
ATOM   893  O OG1 . THR   B 1 7   ? 18.117  0.361   29.188 1.00 41.44 ? 1800 THR   B OG1 1 
ATOM   894  C CG2 . THR   B 1 7   ? 19.550  0.338   31.130 1.00 35.67 ? 1800 THR   B CG2 1 
ATOM   895  N N   . PHE   B 1 8   ? 17.178  2.143   33.173 1.00 31.30 ? 1801 PHE   B N   1 
ATOM   896  C CA  . PHE   B 1 8   ? 17.338  2.549   34.568 1.00 33.87 ? 1801 PHE   B CA  1 
ATOM   897  C C   . PHE   B 1 8   ? 16.351  1.818   35.468 1.00 32.47 ? 1801 PHE   B C   1 
ATOM   898  O O   . PHE   B 1 8   ? 16.697  1.408   36.580 1.00 27.71 ? 1801 PHE   B O   1 
ATOM   899  C CB  . PHE   B 1 8   ? 17.143  4.062   34.719 1.00 43.23 ? 1801 PHE   B CB  1 
ATOM   900  C CG  . PHE   B 1 8   ? 18.094  4.898   33.898 1.00 60.79 ? 1801 PHE   B CG  1 
ATOM   901  C CD1 . PHE   B 1 8   ? 19.268  4.363   33.394 1.00 66.84 ? 1801 PHE   B CD1 1 
ATOM   902  C CD2 . PHE   B 1 8   ? 17.809  6.230   33.640 1.00 66.97 ? 1801 PHE   B CD2 1 
ATOM   903  C CE1 . PHE   B 1 8   ? 20.133  5.138   32.643 1.00 67.40 ? 1801 PHE   B CE1 1 
ATOM   904  C CE2 . PHE   B 1 8   ? 18.672  7.010   32.891 1.00 72.53 ? 1801 PHE   B CE2 1 
ATOM   905  C CZ  . PHE   B 1 8   ? 19.835  6.462   32.392 1.00 70.26 ? 1801 PHE   B CZ  1 
ATOM   906  N N   . CYS   B 1 9   ? 15.112  1.651   34.995 1.00 39.69 ? 1802 CYS   B N   1 
ATOM   907  C CA  . CYS   B 1 9   ? 14.087  0.965   35.777 1.00 37.57 ? 1802 CYS   B CA  1 
ATOM   908  C C   . CYS   B 1 9   ? 14.437  -0.500  35.998 1.00 21.96 ? 1802 CYS   B C   1 
ATOM   909  O O   . CYS   B 1 9   ? 14.192  -1.046  37.078 1.00 20.73 ? 1802 CYS   B O   1 
ATOM   910  C CB  . CYS   B 1 9   ? 12.734  1.090   35.076 1.00 22.77 ? 1802 CYS   B CB  1 
ATOM   911  S SG  . CYS   B 1 9   ? 12.070  2.758   35.101 1.00 31.19 ? 1802 CYS   B SG  1 
ATOM   912  N N   . GLU   B 1 10  ? 14.979  -1.161  34.973 1.00 22.82 ? 1803 GLU   B N   1 
ATOM   913  C CA  . GLU   B 1 10  ? 15.463  -2.526  35.140 1.00 28.07 ? 1803 GLU   B CA  1 
ATOM   914  C C   . GLU   B 1 10  ? 16.534  -2.587  36.218 1.00 22.52 ? 1803 GLU   B C   1 
ATOM   915  O O   . GLU   B 1 10  ? 16.532  -3.499  37.048 1.00 25.56 ? 1803 GLU   B O   1 
ATOM   916  C CB  . GLU   B 1 10  ? 16.000  -3.056  33.807 1.00 30.12 ? 1803 GLU   B CB  1 
ATOM   917  C CG  . GLU   B 1 10  ? 14.915  -3.133  32.751 1.00 23.83 ? 1803 GLU   B CG  1 
ATOM   918  C CD  . GLU   B 1 10  ? 15.429  -3.469  31.362 1.00 43.64 ? 1803 GLU   B CD  1 
ATOM   919  O OE1 . GLU   B 1 10  ? 14.591  -3.754  30.485 1.00 42.89 ? 1803 GLU   B OE1 1 
ATOM   920  O OE2 . GLU   B 1 10  ? 16.657  -3.445  31.145 1.00 45.39 ? 1803 GLU   B OE2 1 
ATOM   921  N N   . ILE   B 1 11  ? 17.426  -1.593  36.234 1.00 24.18 ? 1804 ILE   B N   1 
ATOM   922  C CA  A ILE   B 1 11  ? 18.507  -1.549  37.215 0.71 25.70 ? 1804 ILE   B CA  1 
ATOM   923  C CA  B ILE   B 1 11  ? 18.503  -1.557  37.218 0.29 25.50 ? 1804 ILE   B CA  1 
ATOM   924  C C   . ILE   B 1 11  ? 17.940  -1.367  38.619 1.00 23.55 ? 1804 ILE   B C   1 
ATOM   925  O O   . ILE   B 1 11  ? 18.262  -2.122  39.551 1.00 24.87 ? 1804 ILE   B O   1 
ATOM   926  C CB  A ILE   B 1 11  ? 19.489  -0.418  36.866 0.71 27.43 ? 1804 ILE   B CB  1 
ATOM   927  C CB  B ILE   B 1 11  ? 19.508  -0.449  36.861 0.29 27.84 ? 1804 ILE   B CB  1 
ATOM   928  C CG1 A ILE   B 1 11  ? 20.199  -0.708  35.540 0.71 29.17 ? 1804 ILE   B CG1 1 
ATOM   929  C CG1 B ILE   B 1 11  ? 20.395  -0.928  35.721 0.29 29.14 ? 1804 ILE   B CG1 1 
ATOM   930  C CG2 A ILE   B 1 11  ? 20.475  -0.208  38.004 0.71 31.16 ? 1804 ILE   B CG2 1 
ATOM   931  C CG2 B ILE   B 1 11  ? 20.344  -0.074  38.075 0.29 30.23 ? 1804 ILE   B CG2 1 
ATOM   932  C CD1 A ILE   B 1 11  ? 21.076  0.432   35.060 0.71 32.00 ? 1804 ILE   B CD1 1 
ATOM   933  C CD1 B ILE   B 1 11  ? 20.911  -2.310  35.974 0.29 28.72 ? 1804 ILE   B CD1 1 
ATOM   934  N N   . ILE   B 1 12  ? 17.095  -0.354  38.791 1.00 23.24 ? 1805 ILE   B N   1 
ATOM   935  C CA  . ILE   B 1 12  ? 16.599  -0.035  40.126 1.00 22.43 ? 1805 ILE   B CA  1 
ATOM   936  C C   . ILE   B 1 12  ? 15.726  -1.161  40.669 1.00 21.41 ? 1805 ILE   B C   1 
ATOM   937  O O   . ILE   B 1 12  ? 15.762  -1.454  41.874 1.00 24.23 ? 1805 ILE   B O   1 
ATOM   938  C CB  . ILE   B 1 12  ? 15.890  1.333   40.082 1.00 35.28 ? 1805 ILE   B CB  1 
ATOM   939  C CG1 . ILE   B 1 12  ? 15.783  1.954   41.471 1.00 32.29 ? 1805 ILE   B CG1 1 
ATOM   940  C CG2 . ILE   B 1 12  ? 14.537  1.236   39.427 1.00 41.55 ? 1805 ILE   B CG2 1 
ATOM   941  C CD1 . ILE   B 1 12  ? 15.450  3.426   41.430 1.00 34.94 ? 1805 ILE   B CD1 1 
ATOM   942  N N   . LEU   B 1 13  ? 14.967  -1.840  39.802 1.00 24.68 ? 1806 LEU   B N   1 
ATOM   943  C CA  . LEU   B 1 13  ? 14.123  -2.944  40.246 1.00 18.26 ? 1806 LEU   B CA  1 
ATOM   944  C C   . LEU   B 1 13  ? 14.965  -4.094  40.790 1.00 18.95 ? 1806 LEU   B C   1 
ATOM   945  O O   . LEU   B 1 13  ? 14.697  -4.631  41.879 1.00 17.75 ? 1806 LEU   B O   1 
ATOM   946  C CB  . LEU   B 1 13  ? 13.245  -3.422  39.081 1.00 19.23 ? 1806 LEU   B CB  1 
ATOM   947  C CG  . LEU   B 1 13  ? 12.301  -4.569  39.435 1.00 16.53 ? 1806 LEU   B CG  1 
ATOM   948  C CD1 . LEU   B 1 13  ? 11.312  -4.090  40.513 1.00 16.76 ? 1806 LEU   B CD1 1 
ATOM   949  C CD2 . LEU   B 1 13  ? 11.536  -5.105  38.232 1.00 17.05 ? 1806 LEU   B CD2 1 
ATOM   950  N N   . MET   B 1 14  ? 15.991  -4.489  40.040 1.00 19.30 ? 1807 MET   B N   1 
ATOM   951  C CA  . MET   B 1 14  ? 16.889  -5.538  40.503 1.00 19.77 ? 1807 MET   B CA  1 
ATOM   952  C C   . MET   B 1 14  ? 17.518  -5.160  41.832 1.00 27.94 ? 1807 MET   B C   1 
ATOM   953  O O   . MET   B 1 14  ? 17.562  -5.969  42.767 1.00 27.23 ? 1807 MET   B O   1 
ATOM   954  C CB  . MET   B 1 14  ? 17.976  -5.799  39.462 1.00 24.68 ? 1807 MET   B CB  1 
ATOM   955  C CG  . MET   B 1 14  ? 19.034  -6.792  39.898 1.00 34.58 ? 1807 MET   B CG  1 
ATOM   956  S SD  . MET   B 1 14  ? 20.448  -6.758  38.772 1.00 42.02 ? 1807 MET   B SD  1 
ATOM   957  C CE  . MET   B 1 14  ? 19.632  -6.504  37.191 1.00 42.14 ? 1807 MET   B CE  1 
ATOM   958  N N   . GLU   B 1 15  ? 17.996  -3.920  41.942 1.00 21.25 ? 1808 GLU   B N   1 
ATOM   959  C CA  . GLU   B 1 15  ? 18.581  -3.477  43.204 1.00 29.54 ? 1808 GLU   B CA  1 
ATOM   960  C C   . GLU   B 1 15  ? 17.556  -3.458  44.328 1.00 28.99 ? 1808 GLU   B C   1 
ATOM   961  O O   . GLU   B 1 15  ? 17.901  -3.755  45.479 1.00 29.50 ? 1808 GLU   B O   1 
ATOM   962  C CB  . GLU   B 1 15  ? 19.208  -2.096  43.036 1.00 27.65 ? 1808 GLU   B CB  1 
ATOM   963  C CG  . GLU   B 1 15  ? 20.353  -2.088  42.033 1.00 25.52 ? 1808 GLU   B CG  1 
ATOM   964  C CD  . GLU   B 1 15  ? 20.891  -0.703  41.787 1.00 40.08 ? 1808 GLU   B CD  1 
ATOM   965  O OE1 . GLU   B 1 15  ? 22.000  -0.577  41.222 1.00 42.00 ? 1808 GLU   B OE1 1 
ATOM   966  O OE2 . GLU   B 1 15  ? 20.204  0.268   42.165 1.00 39.92 ? 1808 GLU   B OE2 1 
ATOM   967  N N   . MET   B 1 16  ? 16.299  -3.112  44.021 1.00 22.63 ? 1809 MET   B N   1 
ATOM   968  C CA  . MET   B 1 16  ? 15.258  -3.127  45.046 1.00 19.94 ? 1809 MET   B CA  1 
ATOM   969  C C   . MET   B 1 16  ? 14.935  -4.553  45.480 1.00 27.52 ? 1809 MET   B C   1 
ATOM   970  O O   . MET   B 1 16  ? 14.801  -4.825  46.674 1.00 26.57 ? 1809 MET   B O   1 
ATOM   971  C CB  . MET   B 1 16  ? 14.000  -2.406  44.539 1.00 17.54 ? 1809 MET   B CB  1 
ATOM   972  C CG  . MET   B 1 16  ? 14.104  -0.902  44.609 1.00 21.59 ? 1809 MET   B CG  1 
ATOM   973  S SD  . MET   B 1 16  ? 12.538  -0.015  44.506 1.00 24.12 ? 1809 MET   B SD  1 
ATOM   974  C CE  . MET   B 1 16  ? 11.985  -0.569  42.898 1.00 20.66 ? 1809 MET   B CE  1 
ATOM   975  N N   . GLU   B 1 17  ? 14.797  -5.477  44.521 1.00 19.58 ? 1810 GLU   B N   1 
ATOM   976  C CA  . GLU   B 1 17  ? 14.530  -6.873  44.856 1.00 17.10 ? 1810 GLU   B CA  1 
ATOM   977  C C   . GLU   B 1 17  ? 15.634  -7.463  45.732 1.00 22.43 ? 1810 GLU   B C   1 
ATOM   978  O O   . GLU   B 1 17  ? 15.354  -8.231  46.661 1.00 26.30 ? 1810 GLU   B O   1 
ATOM   979  C CB  . GLU   B 1 17  ? 14.374  -7.700  43.574 1.00 28.20 ? 1810 GLU   B CB  1 
ATOM   980  C CG  . GLU   B 1 17  ? 13.183  -7.309  42.706 1.00 20.79 ? 1810 GLU   B CG  1 
ATOM   981  C CD  . GLU   B 1 17  ? 13.276  -7.878  41.298 1.00 24.62 ? 1810 GLU   B CD  1 
ATOM   982  O OE1 . GLU   B 1 17  ? 12.219  -8.063  40.655 1.00 22.41 ? 1810 GLU   B OE1 1 
ATOM   983  O OE2 . GLU   B 1 17  ? 14.407  -8.122  40.831 1.00 25.19 ? 1810 GLU   B OE2 1 
ATOM   984  N N   . SER   B 1 18  ? 16.888  -7.099  45.475 1.00 26.07 ? 1811 SER   B N   1 
ATOM   985  C CA  A SER   B 1 18  ? 18.025  -7.666  46.189 0.32 27.66 ? 1811 SER   B CA  1 
ATOM   986  C CA  B SER   B 1 18  ? 18.019  -7.672  46.190 0.68 27.65 ? 1811 SER   B CA  1 
ATOM   987  C C   . SER   B 1 18  ? 18.367  -6.913  47.468 1.00 26.66 ? 1811 SER   B C   1 
ATOM   988  O O   . SER   B 1 18  ? 19.352  -7.259  48.124 1.00 34.84 ? 1811 SER   B O   1 
ATOM   989  C CB  A SER   B 1 18  ? 19.260  -7.707  45.281 0.32 27.90 ? 1811 SER   B CB  1 
ATOM   990  C CB  B SER   B 1 18  ? 19.243  -7.738  45.266 0.68 28.59 ? 1811 SER   B CB  1 
ATOM   991  O OG  A SER   B 1 18  ? 19.874  -6.433  45.189 0.32 26.48 ? 1811 SER   B OG  1 
ATOM   992  O OG  B SER   B 1 18  ? 18.978  -8.541  44.121 0.68 22.61 ? 1811 SER   B OG  1 
ATOM   993  N N   . HIS   B 1 19  ? 17.581  -5.904  47.843 1.00 24.37 ? 1812 HIS   B N   1 
ATOM   994  C CA  . HIS   B 1 19  ? 17.871  -5.094  49.015 1.00 27.02 ? 1812 HIS   B CA  1 
ATOM   995  C C   . HIS   B 1 19  ? 17.500  -5.865  50.274 1.00 25.93 ? 1812 HIS   B C   1 
ATOM   996  O O   . HIS   B 1 19  ? 16.558  -6.663  50.278 1.00 27.78 ? 1812 HIS   B O   1 
ATOM   997  C CB  . HIS   B 1 19  ? 17.099  -3.771  48.954 1.00 22.58 ? 1812 HIS   B CB  1 
ATOM   998  C CG  . HIS   B 1 19  ? 17.592  -2.725  49.903 1.00 26.97 ? 1812 HIS   B CG  1 
ATOM   999  N ND1 . HIS   B 1 19  ? 17.314  -2.756  51.255 1.00 25.29 ? 1812 HIS   B ND1 1 
ATOM   1000 C CD2 . HIS   B 1 19  ? 18.328  -1.608  49.696 1.00 29.36 ? 1812 HIS   B CD2 1 
ATOM   1001 C CE1 . HIS   B 1 19  ? 17.866  -1.710  51.841 1.00 30.89 ? 1812 HIS   B CE1 1 
ATOM   1002 N NE2 . HIS   B 1 19  ? 18.491  -0.998  50.921 1.00 29.90 ? 1812 HIS   B NE2 1 
ATOM   1003 N N   . ASP   B 1 20  ? 18.271  -5.626  51.340 1.00 30.09 ? 1813 ASP   B N   1 
ATOM   1004 C CA  . ASP   B 1 20  ? 18.052  -6.331  52.601 1.00 32.06 ? 1813 ASP   B CA  1 
ATOM   1005 C C   . ASP   B 1 20  ? 16.650  -6.101  53.154 1.00 29.38 ? 1813 ASP   B C   1 
ATOM   1006 O O   . ASP   B 1 20  ? 16.099  -6.986  53.820 1.00 25.49 ? 1813 ASP   B O   1 
ATOM   1007 C CB  . ASP   B 1 20  ? 19.099  -5.905  53.636 1.00 37.60 ? 1813 ASP   B CB  1 
ATOM   1008 C CG  . ASP   B 1 20  ? 20.411  -6.668  53.499 1.00 45.03 ? 1813 ASP   B CG  1 
ATOM   1009 O OD1 . ASP   B 1 20  ? 20.492  -7.561  52.634 1.00 44.93 ? 1813 ASP   B OD1 1 
ATOM   1010 O OD2 . ASP   B 1 20  ? 21.355  -6.387  54.272 1.00 44.63 ? 1813 ASP   B OD2 1 
ATOM   1011 N N   . ALA   B 1 21  ? 16.051  -4.938  52.889 1.00 24.49 ? 1814 ALA   B N   1 
ATOM   1012 C CA  . ALA   B 1 21  ? 14.733  -4.603  53.419 1.00 27.69 ? 1814 ALA   B CA  1 
ATOM   1013 C C   . ALA   B 1 21  ? 13.608  -4.934  52.448 1.00 30.10 ? 1814 ALA   B C   1 
ATOM   1014 O O   . ALA   B 1 21  ? 12.494  -4.424  52.605 1.00 28.49 ? 1814 ALA   B O   1 
ATOM   1015 C CB  . ALA   B 1 21  ? 14.664  -3.123  53.793 1.00 29.48 ? 1814 ALA   B CB  1 
ATOM   1016 N N   . ALA   B 1 22  ? 13.872  -5.768  51.453 1.00 26.73 ? 1815 ALA   B N   1 
ATOM   1017 C CA  . ALA   B 1 22  ? 12.891  -6.047  50.414 1.00 27.25 ? 1815 ALA   B CA  1 
ATOM   1018 C C   . ALA   B 1 22  ? 12.011  -7.245  50.727 1.00 21.83 ? 1815 ALA   B C   1 
ATOM   1019 O O   . ALA   B 1 22  ? 11.076  -7.513  49.965 1.00 26.68 ? 1815 ALA   B O   1 
ATOM   1020 C CB  . ALA   B 1 22  ? 13.588  -6.284  49.078 1.00 24.57 ? 1815 ALA   B CB  1 
ATOM   1021 N N   . TRP   B 1 23  ? 12.288  -7.961  51.818 1.00 25.52 ? 1816 TRP   B N   1 
ATOM   1022 C CA  . TRP   B 1 23  ? 11.586  -9.192  52.167 1.00 28.60 ? 1816 TRP   B CA  1 
ATOM   1023 C C   . TRP   B 1 23  ? 10.059  -9.057  52.253 1.00 25.80 ? 1816 TRP   B C   1 
ATOM   1024 O O   . TRP   B 1 23  ? 9.372   -10.054 52.000 1.00 29.14 ? 1816 TRP   B O   1 
ATOM   1025 C CB  . TRP   B 1 23  ? 12.162  -9.758  53.474 1.00 21.76 ? 1816 TRP   B CB  1 
ATOM   1026 C CG  . TRP   B 1 23  ? 12.029  -8.836  54.650 1.00 34.22 ? 1816 TRP   B CG  1 
ATOM   1027 C CD1 . TRP   B 1 23  ? 12.916  -7.882  55.053 1.00 34.39 ? 1816 TRP   B CD1 1 
ATOM   1028 C CD2 . TRP   B 1 23  ? 10.931  -8.775  55.562 1.00 27.07 ? 1816 TRP   B CD2 1 
ATOM   1029 N NE1 . TRP   B 1 23  ? 12.437  -7.227  56.163 1.00 32.40 ? 1816 TRP   B NE1 1 
ATOM   1030 C CE2 . TRP   B 1 23  ? 11.216  -7.756  56.493 1.00 26.75 ? 1816 TRP   B CE2 1 
ATOM   1031 C CE3 . TRP   B 1 23  ? 9.729   -9.477  55.676 1.00 30.29 ? 1816 TRP   B CE3 1 
ATOM   1032 C CZ2 . TRP   B 1 23  ? 10.344  -7.426  57.530 1.00 29.88 ? 1816 TRP   B CZ2 1 
ATOM   1033 C CZ3 . TRP   B 1 23  ? 8.861   -9.144  56.694 1.00 34.07 ? 1816 TRP   B CZ3 1 
ATOM   1034 C CH2 . TRP   B 1 23  ? 9.177   -8.133  57.617 1.00 35.54 ? 1816 TRP   B CH2 1 
ATOM   1035 N N   . PRO   B 1 24  ? 9.468   -7.897  52.577 1.00 24.38 ? 1817 PRO   B N   1 
ATOM   1036 C CA  . PRO   B 1 24  ? 8.003   -7.797  52.533 1.00 17.80 ? 1817 PRO   B CA  1 
ATOM   1037 C C   . PRO   B 1 24  ? 7.406   -7.590  51.145 1.00 20.38 ? 1817 PRO   B C   1 
ATOM   1038 O O   . PRO   B 1 24  ? 6.176   -7.596  51.033 1.00 19.35 ? 1817 PRO   B O   1 
ATOM   1039 C CB  . PRO   B 1 24  ? 7.707   -6.573  53.424 1.00 22.98 ? 1817 PRO   B CB  1 
ATOM   1040 C CG  . PRO   B 1 24  ? 8.957   -6.317  54.195 1.00 25.31 ? 1817 PRO   B CG  1 
ATOM   1041 C CD  . PRO   B 1 24  ? 10.033  -6.703  53.231 1.00 27.27 ? 1817 PRO   B CD  1 
ATOM   1042 N N   . PHE   B 1 25  ? 8.219   -7.422  50.092 1.00 20.13 ? 1818 PHE   B N   1 
ATOM   1043 C CA  . PHE   B 1 25  ? 7.746   -6.883  48.819 1.00 20.74 ? 1818 PHE   B CA  1 
ATOM   1044 C C   . PHE   B 1 25  ? 8.041   -7.771  47.614 1.00 20.53 ? 1818 PHE   B C   1 
ATOM   1045 O O   . PHE   B 1 25  ? 7.857   -7.324  46.475 1.00 18.72 ? 1818 PHE   B O   1 
ATOM   1046 C CB  . PHE   B 1 25  ? 8.342   -5.484  48.610 1.00 19.20 ? 1818 PHE   B CB  1 
ATOM   1047 C CG  . PHE   B 1 25  ? 8.155   -4.577  49.798 1.00 22.68 ? 1818 PHE   B CG  1 
ATOM   1048 C CD1 . PHE   B 1 25  ? 6.885   -4.180  50.180 1.00 19.40 ? 1818 PHE   B CD1 1 
ATOM   1049 C CD2 . PHE   B 1 25  ? 9.242   -4.135  50.535 1.00 29.76 ? 1818 PHE   B CD2 1 
ATOM   1050 C CE1 . PHE   B 1 25  ? 6.702   -3.361  51.292 1.00 23.93 ? 1818 PHE   B CE1 1 
ATOM   1051 C CE2 . PHE   B 1 25  ? 9.068   -3.311  51.645 1.00 23.70 ? 1818 PHE   B CE2 1 
ATOM   1052 C CZ  . PHE   B 1 25  ? 7.797   -2.924  52.019 1.00 25.78 ? 1818 PHE   B CZ  1 
ATOM   1053 N N   . LEU   B 1 26  ? 8.459   -9.017  47.859 1.00 20.05 ? 1819 LEU   B N   1 
ATOM   1054 C CA  . LEU   B 1 26  ? 8.866   -9.956  46.776 1.00 22.49 ? 1819 LEU   B CA  1 
ATOM   1055 C C   . LEU   B 1 26  ? 7.670   -10.710 46.173 1.00 18.27 ? 1819 LEU   B C   1 
ATOM   1056 O O   . LEU   B 1 26  ? 7.848   -11.321 45.114 1.00 23.76 ? 1819 LEU   B O   1 
ATOM   1057 C CB  . LEU   B 1 26  ? 9.906   -10.928 47.340 1.00 23.41 ? 1819 LEU   B CB  1 
ATOM   1058 C CG  . LEU   B 1 26  ? 11.344  -10.412 47.378 1.00 36.77 ? 1819 LEU   B CG  1 
ATOM   1059 C CD1 . LEU   B 1 26  ? 11.444  -9.011  46.806 1.00 44.31 ? 1819 LEU   B CD1 1 
ATOM   1060 C CD2 . LEU   B 1 26  ? 11.908  -10.450 48.786 1.00 36.51 ? 1819 LEU   B CD2 1 
ATOM   1061 N N   . GLU   B 1 27  ? 6.516   -10.698 46.841 1.00 23.24 ? 1820 GLU   B N   1 
ATOM   1062 C CA  . GLU   B 1 27  ? 5.321   -11.358 46.340 1.00 23.97 ? 1820 GLU   B CA  1 
ATOM   1063 C C   . GLU   B 1 27  ? 4.114   -10.568 46.810 1.00 20.31 ? 1820 GLU   B C   1 
ATOM   1064 O O   . GLU   B 1 27  ? 4.207   -9.821  47.792 1.00 18.73 ? 1820 GLU   B O   1 
ATOM   1065 C CB  . GLU   B 1 27  ? 5.229   -12.813 46.812 1.00 18.52 ? 1820 GLU   B CB  1 
ATOM   1066 C CG  . GLU   B 1 27  ? 5.018   -13.008 48.291 1.00 26.89 ? 1820 GLU   B CG  1 
ATOM   1067 C CD  . GLU   B 1 27  ? 4.933   -14.477 48.641 1.00 33.59 ? 1820 GLU   B CD  1 
ATOM   1068 O OE1 . GLU   B 1 27  ? 3.857   -15.082 48.423 1.00 36.29 ? 1820 GLU   B OE1 1 
ATOM   1069 O OE2 . GLU   B 1 27  ? 5.951   -15.029 49.105 1.00 33.14 ? 1820 GLU   B OE2 1 
ATOM   1070 N N   . PRO   B 1 28  ? 2.981   -10.678 46.126 1.00 16.65 ? 1821 PRO   B N   1 
ATOM   1071 C CA  . PRO   B 1 28  ? 1.815   -9.882  46.526 1.00 18.43 ? 1821 PRO   B CA  1 
ATOM   1072 C C   . PRO   B 1 28  ? 1.289   -10.316 47.894 1.00 16.65 ? 1821 PRO   B C   1 
ATOM   1073 O O   . PRO   B 1 28  ? 1.436   -11.470 48.313 1.00 20.47 ? 1821 PRO   B O   1 
ATOM   1074 C CB  . PRO   B 1 28  ? 0.791   -10.149 45.411 1.00 19.60 ? 1821 PRO   B CB  1 
ATOM   1075 C CG  . PRO   B 1 28  ? 1.554   -10.845 44.318 1.00 19.54 ? 1821 PRO   B CG  1 
ATOM   1076 C CD  . PRO   B 1 28  ? 2.694   -11.541 44.965 1.00 15.86 ? 1821 PRO   B CD  1 
ATOM   1077 N N   . VAL   B 1 29  ? 0.730   -9.349  48.620 1.00 16.11 ? 1822 VAL   B N   1 
ATOM   1078 C CA  . VAL   B 1 29  ? 0.004   -9.674  49.844 1.00 27.86 ? 1822 VAL   B CA  1 
ATOM   1079 C C   . VAL   B 1 29  ? -1.215  -10.510 49.487 1.00 26.50 ? 1822 VAL   B C   1 
ATOM   1080 O O   . VAL   B 1 29  ? -1.984  -10.155 48.588 1.00 22.22 ? 1822 VAL   B O   1 
ATOM   1081 C CB  . VAL   B 1 29  ? -0.391  -8.390  50.591 1.00 26.93 ? 1822 VAL   B CB  1 
ATOM   1082 C CG1 . VAL   B 1 29  ? -1.203  -8.718  51.843 1.00 30.42 ? 1822 VAL   B CG1 1 
ATOM   1083 C CG2 . VAL   B 1 29  ? 0.841   -7.602  50.940 1.00 21.10 ? 1822 VAL   B CG2 1 
ATOM   1084 N N   . ASN   B 1 30  ? -1.391  -11.639 50.187 1.00 23.44 ? 1823 ASN   B N   1 
ATOM   1085 C CA  . ASN   B 1 30  ? -2.532  -12.528 49.966 1.00 27.07 ? 1823 ASN   B CA  1 
ATOM   1086 C C   . ASN   B 1 30  ? -3.730  -11.989 50.736 1.00 20.94 ? 1823 ASN   B C   1 
ATOM   1087 O O   . ASN   B 1 30  ? -3.797  -12.153 51.959 1.00 27.48 ? 1823 ASN   B O   1 
ATOM   1088 C CB  . ASN   B 1 30  ? -2.220  -13.961 50.419 1.00 29.96 ? 1823 ASN   B CB  1 
ATOM   1089 C CG  . ASN   B 1 30  ? -3.221  -14.990 49.889 1.00 27.27 ? 1823 ASN   B CG  1 
ATOM   1090 O OD1 . ASN   B 1 30  ? -4.417  -14.702 49.771 1.00 32.30 ? 1823 ASN   B OD1 1 
ATOM   1091 N ND2 . ASN   B 1 30  ? -2.741  -16.175 49.553 1.00 29.71 ? 1823 ASN   B ND2 1 
ATOM   1092 N N   . PRO   B 1 31  ? -4.696  -11.361 50.058 1.00 24.72 ? 1824 PRO   B N   1 
ATOM   1093 C CA  . PRO   B 1 31  ? -5.804  -10.728 50.785 1.00 30.97 ? 1824 PRO   B CA  1 
ATOM   1094 C C   . PRO   B 1 31  ? -6.672  -11.722 51.533 1.00 35.44 ? 1824 PRO   B C   1 
ATOM   1095 O O   . PRO   B 1 31  ? -7.280  -11.354 52.547 1.00 39.43 ? 1824 PRO   B O   1 
ATOM   1096 C CB  . PRO   B 1 31  ? -6.588  -10.017 49.675 1.00 30.25 ? 1824 PRO   B CB  1 
ATOM   1097 C CG  . PRO   B 1 31  ? -6.314  -10.833 48.454 1.00 28.47 ? 1824 PRO   B CG  1 
ATOM   1098 C CD  . PRO   B 1 31  ? -4.891  -11.316 48.595 1.00 26.54 ? 1824 PRO   B CD  1 
ATOM   1099 N N   . ARG   B 1 32  ? -6.730  -12.975 51.085 1.00 35.06 ? 1825 ARG   B N   1 
ATOM   1100 C CA  . ARG   B 1 32  ? -7.521  -13.984 51.781 1.00 32.18 ? 1825 ARG   B CA  1 
ATOM   1101 C C   . ARG   B 1 32  ? -6.869  -14.461 53.075 1.00 37.45 ? 1825 ARG   B C   1 
ATOM   1102 O O   . ARG   B 1 32  ? -7.524  -15.159 53.857 1.00 44.91 ? 1825 ARG   B O   1 
ATOM   1103 C CB  . ARG   B 1 32  ? -7.784  -15.165 50.840 1.00 38.82 ? 1825 ARG   B CB  1 
ATOM   1104 C CG  . ARG   B 1 32  ? -8.403  -14.730 49.506 1.00 38.66 ? 1825 ARG   B CG  1 
ATOM   1105 C CD  . ARG   B 1 32  ? -8.278  -15.777 48.407 1.00 41.41 ? 1825 ARG   B CD  1 
ATOM   1106 N NE  . ARG   B 1 32  ? -6.896  -16.065 48.038 1.00 40.20 ? 1825 ARG   B NE  1 
ATOM   1107 C CZ  . ARG   B 1 32  ? -6.139  -15.275 47.281 1.00 39.08 ? 1825 ARG   B CZ  1 
ATOM   1108 N NH1 . ARG   B 1 32  ? -6.621  -14.125 46.826 1.00 39.32 ? 1825 ARG   B NH1 1 
ATOM   1109 N NH2 . ARG   B 1 32  ? -4.892  -15.627 46.989 1.00 38.93 ? 1825 ARG   B NH2 1 
ATOM   1110 N N   . LEU   B 1 33  ? -5.609  -14.103 53.319 1.00 31.16 ? 1826 LEU   B N   1 
ATOM   1111 C CA  . LEU   B 1 33  ? -4.916  -14.442 54.554 1.00 38.10 ? 1826 LEU   B CA  1 
ATOM   1112 C C   . LEU   B 1 33  ? -4.707  -13.249 55.480 1.00 41.57 ? 1826 LEU   B C   1 
ATOM   1113 O O   . LEU   B 1 33  ? -4.260  -13.445 56.616 1.00 57.03 ? 1826 LEU   B O   1 
ATOM   1114 C CB  . LEU   B 1 33  ? -3.547  -15.073 54.247 1.00 33.31 ? 1826 LEU   B CB  1 
ATOM   1115 C CG  . LEU   B 1 33  ? -3.489  -16.384 53.454 1.00 33.67 ? 1826 LEU   B CG  1 
ATOM   1116 C CD1 . LEU   B 1 33  ? -2.036  -16.788 53.201 1.00 36.95 ? 1826 LEU   B CD1 1 
ATOM   1117 C CD2 . LEU   B 1 33  ? -4.243  -17.497 54.156 1.00 37.62 ? 1826 LEU   B CD2 1 
ATOM   1118 N N   . VAL   B 1 34  ? -5.022  -12.031 55.040 1.00 29.36 ? 1827 VAL   B N   1 
ATOM   1119 C CA  . VAL   B 1 34  ? -4.756  -10.806 55.790 1.00 25.67 ? 1827 VAL   B CA  1 
ATOM   1120 C C   . VAL   B 1 34  ? -6.089  -10.090 55.968 1.00 31.48 ? 1827 VAL   B C   1 
ATOM   1121 O O   . VAL   B 1 34  ? -6.604  -9.482  55.022 1.00 33.37 ? 1827 VAL   B O   1 
ATOM   1122 C CB  . VAL   B 1 34  ? -3.732  -9.908  55.086 1.00 31.46 ? 1827 VAL   B CB  1 
ATOM   1123 C CG1 . VAL   B 1 34  ? -3.287  -8.773  56.006 1.00 27.89 ? 1827 VAL   B CG1 1 
ATOM   1124 C CG2 . VAL   B 1 34  ? -2.527  -10.725 54.630 1.00 37.38 ? 1827 VAL   B CG2 1 
ATOM   1125 N N   . SER   B 1 35  ? -6.659  -10.155 57.173 1.00 41.12 ? 1828 SER   B N   1 
ATOM   1126 C CA  . SER   B 1 35  ? -7.982  -9.581  57.386 1.00 42.69 ? 1828 SER   B CA  1 
ATOM   1127 C C   . SER   B 1 35  ? -7.953  -8.073  57.155 1.00 43.07 ? 1828 SER   B C   1 
ATOM   1128 O O   . SER   B 1 35  ? -7.116  -7.361  57.714 1.00 36.41 ? 1828 SER   B O   1 
ATOM   1129 C CB  . SER   B 1 35  ? -8.481  -9.898  58.795 1.00 49.68 ? 1828 SER   B CB  1 
ATOM   1130 O OG  . SER   B 1 35  ? -7.824  -9.098  59.763 1.00 51.06 ? 1828 SER   B OG  1 
ATOM   1131 N N   . GLY   B 1 36  ? -8.855  -7.592  56.296 1.00 43.54 ? 1829 GLY   B N   1 
ATOM   1132 C CA  . GLY   B 1 36  ? -9.020  -6.173  56.058 1.00 41.64 ? 1829 GLY   B CA  1 
ATOM   1133 C C   . GLY   B 1 36  ? -8.176  -5.590  54.939 1.00 34.00 ? 1829 GLY   B C   1 
ATOM   1134 O O   . GLY   B 1 36  ? -8.358  -4.412  54.602 1.00 31.54 ? 1829 GLY   B O   1 
ATOM   1135 N N   . TYR   B 1 37  ? -7.262  -6.367  54.353 1.00 28.58 ? 1830 TYR   B N   1 
ATOM   1136 C CA  . TYR   B 1 37  ? -6.310  -5.796  53.408 1.00 20.78 ? 1830 TYR   B CA  1 
ATOM   1137 C C   . TYR   B 1 37  ? -7.019  -5.220  52.186 1.00 22.18 ? 1830 TYR   B C   1 
ATOM   1138 O O   . TYR   B 1 37  ? -6.694  -4.120  51.723 1.00 29.22 ? 1830 TYR   B O   1 
ATOM   1139 C CB  . TYR   B 1 37  ? -5.279  -6.850  52.987 1.00 23.68 ? 1830 TYR   B CB  1 
ATOM   1140 C CG  . TYR   B 1 37  ? -4.105  -6.218  52.298 1.00 26.90 ? 1830 TYR   B CG  1 
ATOM   1141 C CD1 . TYR   B 1 37  ? -4.025  -6.186  50.912 1.00 21.26 ? 1830 TYR   B CD1 1 
ATOM   1142 C CD2 . TYR   B 1 37  ? -3.107  -5.589  53.031 1.00 19.37 ? 1830 TYR   B CD2 1 
ATOM   1143 C CE1 . TYR   B 1 37  ? -2.964  -5.579  50.276 1.00 22.12 ? 1830 TYR   B CE1 1 
ATOM   1144 C CE2 . TYR   B 1 37  ? -2.036  -4.990  52.416 1.00 22.25 ? 1830 TYR   B CE2 1 
ATOM   1145 C CZ  . TYR   B 1 37  ? -1.979  -4.974  51.029 1.00 18.16 ? 1830 TYR   B CZ  1 
ATOM   1146 O OH  . TYR   B 1 37  ? -0.914  -4.365  50.419 1.00 19.06 ? 1830 TYR   B OH  1 
ATOM   1147 N N   . ARG   B 1 38  ? -7.977  -5.963  51.637 1.00 27.81 ? 1831 ARG   B N   1 
ATOM   1148 C CA  . ARG   B 1 38  ? -8.690  -5.492  50.453 1.00 28.19 ? 1831 ARG   B CA  1 
ATOM   1149 C C   . ARG   B 1 38  ? -9.599  -4.313  50.775 1.00 31.16 ? 1831 ARG   B C   1 
ATOM   1150 O O   . ARG   B 1 38  ? -9.891  -3.495  49.898 1.00 35.37 ? 1831 ARG   B O   1 
ATOM   1151 C CB  . ARG   B 1 38  ? -9.511  -6.632  49.859 1.00 37.37 ? 1831 ARG   B CB  1 
ATOM   1152 C CG  . ARG   B 1 38  ? -9.118  -7.048  48.440 1.00 43.97 ? 1831 ARG   B CG  1 
ATOM   1153 C CD  . ARG   B 1 38  ? -10.054 -8.136  47.899 1.00 54.59 ? 1831 ARG   B CD  1 
ATOM   1154 N NE  . ARG   B 1 38  ? -9.980  -9.381  48.670 1.00 64.63 ? 1831 ARG   B NE  1 
ATOM   1155 C CZ  . ARG   B 1 38  ? -10.787 -9.700  49.682 1.00 69.09 ? 1831 ARG   B CZ  1 
ATOM   1156 N NH1 . ARG   B 1 38  ? -11.748 -8.869  50.065 1.00 71.76 ? 1831 ARG   B NH1 1 
ATOM   1157 N NH2 . ARG   B 1 38  ? -10.630 -10.854 50.318 1.00 67.89 ? 1831 ARG   B NH2 1 
ATOM   1158 N N   . ARG   B 1 39  ? -10.079 -4.226  52.015 1.00 27.94 ? 1832 ARG   B N   1 
ATOM   1159 C CA  . ARG   B 1 39  ? -10.933 -3.109  52.395 1.00 36.80 ? 1832 ARG   B CA  1 
ATOM   1160 C C   . ARG   B 1 39  ? -10.151 -1.806  52.430 1.00 30.87 ? 1832 ARG   B C   1 
ATOM   1161 O O   . ARG   B 1 39  ? -10.708 -0.735  52.168 1.00 35.95 ? 1832 ARG   B O   1 
ATOM   1162 C CB  . ARG   B 1 39  ? -11.577 -3.386  53.754 1.00 40.23 ? 1832 ARG   B CB  1 
ATOM   1163 C CG  . ARG   B 1 39  ? -12.668 -4.439  53.716 1.00 40.06 ? 1832 ARG   B CG  1 
ATOM   1164 C CD  . ARG   B 1 39  ? -14.021 -3.777  53.768 1.00 41.20 ? 1832 ARG   B CD  1 
ATOM   1165 N NE  . ARG   B 1 39  ? -15.114 -4.733  53.652 1.00 53.81 ? 1832 ARG   B NE  1 
ATOM   1166 C CZ  . ARG   B 1 39  ? -15.530 -5.516  54.640 1.00 55.32 ? 1832 ARG   B CZ  1 
ATOM   1167 N NH1 . ARG   B 1 39  ? -14.928 -5.469  55.819 1.00 50.13 ? 1832 ARG   B NH1 1 
ATOM   1168 N NH2 . ARG   B 1 39  ? -16.537 -6.356  54.445 1.00 63.35 ? 1832 ARG   B NH2 1 
ATOM   1169 N N   . ILE   B 1 40  ? -8.864  -1.885  52.740 1.00 24.71 ? 1833 ILE   B N   1 
ATOM   1170 C CA  . ILE   B 1 40  ? -8.030  -0.713  52.950 1.00 27.28 ? 1833 ILE   B CA  1 
ATOM   1171 C C   . ILE   B 1 40  ? -7.187  -0.383  51.719 1.00 25.61 ? 1833 ILE   B C   1 
ATOM   1172 O O   . ILE   B 1 40  ? -7.007  0.786   51.382 1.00 36.55 ? 1833 ILE   B O   1 
ATOM   1173 C CB  . ILE   B 1 40  ? -7.153  -0.939  54.203 1.00 22.21 ? 1833 ILE   B CB  1 
ATOM   1174 C CG1 . ILE   B 1 40  ? -8.039  -0.930  55.466 1.00 21.39 ? 1833 ILE   B CG1 1 
ATOM   1175 C CG2 . ILE   B 1 40  ? -6.036  0.090   54.289 1.00 25.84 ? 1833 ILE   B CG2 1 
ATOM   1176 C CD1 . ILE   B 1 40  ? -7.306  -1.347  56.779 1.00 22.52 ? 1833 ILE   B CD1 1 
ATOM   1177 N N   . ILE   B 1 41  ? -6.677  -1.388  51.025 1.00 18.72 ? 1834 ILE   B N   1 
ATOM   1178 C CA  . ILE   B 1 41  ? -5.710  -1.185  49.948 1.00 20.74 ? 1834 ILE   B CA  1 
ATOM   1179 C C   . ILE   B 1 41  ? -6.427  -1.441  48.628 1.00 24.37 ? 1834 ILE   B C   1 
ATOM   1180 O O   . ILE   B 1 41  ? -6.625  -2.593  48.231 1.00 22.47 ? 1834 ILE   B O   1 
ATOM   1181 C CB  . ILE   B 1 41  ? -4.488  -2.094  50.101 1.00 23.84 ? 1834 ILE   B CB  1 
ATOM   1182 C CG1 . ILE   B 1 41  ? -3.835  -1.856  51.466 1.00 14.49 ? 1834 ILE   B CG1 1 
ATOM   1183 C CG2 . ILE   B 1 41  ? -3.510  -1.858  48.959 1.00 21.09 ? 1834 ILE   B CG2 1 
ATOM   1184 C CD1 . ILE   B 1 41  ? -3.340  -0.431  51.651 1.00 15.02 ? 1834 ILE   B CD1 1 
ATOM   1185 N N   . LYS   B 1 42  ? -6.804  -0.367  47.933 1.00 21.18 ? 1835 LYS   B N   1 
ATOM   1186 C CA  . LYS   B 1 42  ? -7.587  -0.530  46.720 1.00 26.59 ? 1835 LYS   B CA  1 
ATOM   1187 C C   . LYS   B 1 42  ? -6.725  -0.947  45.538 1.00 18.82 ? 1835 LYS   B C   1 
ATOM   1188 O O   . LYS   B 1 42  ? -7.228  -1.634  44.645 1.00 24.04 ? 1835 LYS   B O   1 
ATOM   1189 C CB  . LYS   B 1 42  ? -8.348  0.757   46.402 1.00 28.18 ? 1835 LYS   B CB  1 
ATOM   1190 C CG  . LYS   B 1 42  ? -9.474  1.043   47.400 1.00 35.97 ? 1835 LYS   B CG  1 
ATOM   1191 C CD  . LYS   B 1 42  ? -10.112 -0.264  47.912 1.00 40.38 ? 1835 LYS   B CD  1 
ATOM   1192 C CE  . LYS   B 1 42  ? -11.230 -0.017  48.924 1.00 43.27 ? 1835 LYS   B CE  1 
ATOM   1193 N NZ  . LYS   B 1 42  ? -12.495 0.415   48.268 1.00 55.16 ? 1835 LYS   B NZ  1 
ATOM   1194 N N   . ASN   B 1 43  ? -5.443  -0.562  45.532 1.00 17.32 ? 1836 ASN   B N   1 
ATOM   1195 C CA  . ASN   B 1 43  ? -4.524  -0.859  44.425 1.00 21.90 ? 1836 ASN   B CA  1 
ATOM   1196 C C   . ASN   B 1 43  ? -3.251  -1.512  44.965 1.00 15.99 ? 1836 ASN   B C   1 
ATOM   1197 O O   . ASN   B 1 43  ? -2.233  -0.841  45.170 1.00 14.98 ? 1836 ASN   B O   1 
ATOM   1198 C CB  . ASN   B 1 43  ? -4.187  0.410   43.633 1.00 24.56 ? 1836 ASN   B CB  1 
ATOM   1199 C CG  . ASN   B 1 43  ? -5.432  1.186   43.181 1.00 24.28 ? 1836 ASN   B CG  1 
ATOM   1200 O OD1 . ASN   B 1 43  ? -5.665  2.324   43.607 1.00 24.89 ? 1836 ASN   B OD1 1 
ATOM   1201 N ND2 . ASN   B 1 43  ? -6.226  0.580   42.301 1.00 22.49 ? 1836 ASN   B ND2 1 
ATOM   1202 N N   . PRO   B 1 44  ? -3.264  -2.829  45.182 1.00 12.57 ? 1837 PRO   B N   1 
ATOM   1203 C CA  . PRO   B 1 44  ? -2.041  -3.504  45.647 1.00 16.29 ? 1837 PRO   B CA  1 
ATOM   1204 C C   . PRO   B 1 44  ? -0.934  -3.463  44.599 1.00 17.22 ? 1837 PRO   B C   1 
ATOM   1205 O O   . PRO   B 1 44  ? -1.192  -3.396  43.395 1.00 17.34 ? 1837 PRO   B O   1 
ATOM   1206 C CB  . PRO   B 1 44  ? -2.500  -4.942  45.912 1.00 16.89 ? 1837 PRO   B CB  1 
ATOM   1207 C CG  . PRO   B 1 44  ? -3.742  -5.110  45.100 1.00 24.71 ? 1837 PRO   B CG  1 
ATOM   1208 C CD  . PRO   B 1 44  ? -4.393  -3.755  45.027 1.00 15.19 ? 1837 PRO   B CD  1 
ATOM   1209 N N   . MET   B 1 45  ? 0.307   -3.509  45.077 1.00 14.32 ? 1838 MET   B N   1 
ATOM   1210 C CA  . MET   B 1 45  ? 1.510   -3.569  44.245 1.00 17.06 ? 1838 MET   B CA  1 
ATOM   1211 C C   . MET   B 1 45  ? 2.660   -4.192  45.038 1.00 20.67 ? 1838 MET   B C   1 
ATOM   1212 O O   . MET   B 1 45  ? 2.763   -4.027  46.260 1.00 20.65 ? 1838 MET   B O   1 
ATOM   1213 C CB  . MET   B 1 45  ? 1.909   -2.182  43.727 1.00 18.34 ? 1838 MET   B CB  1 
ATOM   1214 C CG  . MET   B 1 45  ? 3.067   -2.178  42.689 1.00 13.11 ? 1838 MET   B CG  1 
ATOM   1215 S SD  . MET   B 1 45  ? 2.705   -3.296  41.296 1.00 18.97 ? 1838 MET   B SD  1 
ATOM   1216 C CE  . MET   B 1 45  ? 1.198   -2.612  40.642 1.00 21.38 ? 1838 MET   B CE  1 
ATOM   1217 N N   . ASP   B 1 46  ? 3.513   -4.931  44.328 1.00 17.76 ? 1839 ASP   B N   1 
ATOM   1218 C CA  . ASP   B 1 46  ? 4.703   -5.554  44.888 1.00 15.87 ? 1839 ASP   B CA  1 
ATOM   1219 C C   . ASP   B 1 46  ? 5.723   -5.709  43.762 1.00 15.77 ? 1839 ASP   B C   1 
ATOM   1220 O O   . ASP   B 1 46  ? 5.384   -5.579  42.572 1.00 20.95 ? 1839 ASP   B O   1 
ATOM   1221 C CB  . ASP   B 1 46  ? 4.387   -6.907  45.525 1.00 18.75 ? 1839 ASP   B CB  1 
ATOM   1222 C CG  . ASP   B 1 46  ? 4.225   -8.013  44.489 1.00 21.35 ? 1839 ASP   B CG  1 
ATOM   1223 O OD1 . ASP   B 1 46  ? 5.141   -8.857  44.339 1.00 23.13 ? 1839 ASP   B OD1 1 
ATOM   1224 O OD2 . ASP   B 1 46  ? 3.187   -8.018  43.806 1.00 20.58 ? 1839 ASP   B OD2 1 
ATOM   1225 N N   . PHE   B 1 47  ? 6.975   -5.999  44.135 1.00 16.92 ? 1840 PHE   B N   1 
ATOM   1226 C CA  . PHE   B 1 47  ? 8.060   -6.030  43.144 1.00 20.20 ? 1840 PHE   B CA  1 
ATOM   1227 C C   . PHE   B 1 47  ? 7.855   -7.117  42.084 1.00 22.42 ? 1840 PHE   B C   1 
ATOM   1228 O O   . PHE   B 1 47  ? 8.220   -6.924  40.917 1.00 24.09 ? 1840 PHE   B O   1 
ATOM   1229 C CB  . PHE   B 1 47  ? 9.419   -6.220  43.831 1.00 22.60 ? 1840 PHE   B CB  1 
ATOM   1230 C CG  . PHE   B 1 47  ? 9.822   -5.078  44.739 1.00 23.60 ? 1840 PHE   B CG  1 
ATOM   1231 C CD1 . PHE   B 1 47  ? 9.231   -3.818  44.629 1.00 20.94 ? 1840 PHE   B CD1 1 
ATOM   1232 C CD2 . PHE   B 1 47  ? 10.808  -5.263  45.693 1.00 31.28 ? 1840 PHE   B CD2 1 
ATOM   1233 C CE1 . PHE   B 1 47  ? 9.624   -2.773  45.487 1.00 20.25 ? 1840 PHE   B CE1 1 
ATOM   1234 C CE2 . PHE   B 1 47  ? 11.205  -4.230  46.535 1.00 25.77 ? 1840 PHE   B CE2 1 
ATOM   1235 C CZ  . PHE   B 1 47  ? 10.609  -2.990  46.438 1.00 20.89 ? 1840 PHE   B CZ  1 
ATOM   1236 N N   . SER   B 1 48  ? 7.278   -8.266  42.455 1.00 20.79 ? 1841 SER   B N   1 
ATOM   1237 C CA  . SER   B 1 48  ? 7.113   -9.323  41.451 1.00 18.81 ? 1841 SER   B CA  1 
ATOM   1238 C C   . SER   B 1 48  ? 6.073   -8.945  40.408 1.00 18.89 ? 1841 SER   B C   1 
ATOM   1239 O O   . SER   B 1 48  ? 6.163   -9.384  39.253 1.00 23.72 ? 1841 SER   B O   1 
ATOM   1240 C CB  . SER   B 1 48  ? 6.739   -10.661 42.091 1.00 21.11 ? 1841 SER   B CB  1 
ATOM   1241 O OG  . SER   B 1 48  ? 5.460   -10.623 42.710 1.00 23.10 ? 1841 SER   B OG  1 
ATOM   1242 N N   . THR   B 1 49  ? 5.082   -8.145  40.795 1.00 18.39 ? 1842 THR   B N   1 
ATOM   1243 C CA  . THR   B 1 49  ? 4.105   -7.671  39.822 1.00 14.58 ? 1842 THR   B CA  1 
ATOM   1244 C C   . THR   B 1 49  ? 4.725   -6.621  38.911 1.00 14.50 ? 1842 THR   B C   1 
ATOM   1245 O O   . THR   B 1 49  ? 4.479   -6.620  37.695 1.00 20.18 ? 1842 THR   B O   1 
ATOM   1246 C CB  . THR   B 1 49  ? 2.877   -7.129  40.560 1.00 15.41 ? 1842 THR   B CB  1 
ATOM   1247 O OG1 . THR   B 1 49  ? 2.283   -8.190  41.327 1.00 22.46 ? 1842 THR   B OG1 1 
ATOM   1248 C CG2 . THR   B 1 49  ? 1.844   -6.561  39.586 1.00 20.96 ? 1842 THR   B CG2 1 
ATOM   1249 N N   . MET   B 1 50  ? 5.531   -5.709  39.473 1.00 12.78 ? 1843 MET   B N   1 
ATOM   1250 C CA  . MET   B 1 50  ? 6.302   -4.807  38.613 1.00 13.38 ? 1843 MET   B CA  1 
ATOM   1251 C C   . MET   B 1 50  ? 7.254   -5.592  37.719 1.00 20.01 ? 1843 MET   B C   1 
ATOM   1252 O O   . MET   B 1 50  ? 7.440   -5.239  36.547 1.00 22.42 ? 1843 MET   B O   1 
ATOM   1253 C CB  . MET   B 1 50  ? 7.069   -3.769  39.432 1.00 13.12 ? 1843 MET   B CB  1 
ATOM   1254 C CG  . MET   B 1 50  ? 6.188   -2.960  40.388 1.00 16.44 ? 1843 MET   B CG  1 
ATOM   1255 S SD  . MET   B 1 50  ? 7.135   -2.063  41.634 1.00 22.96 ? 1843 MET   B SD  1 
ATOM   1256 C CE  . MET   B 1 50  ? 7.951   -0.823  40.626 1.00 19.30 ? 1843 MET   B CE  1 
ATOM   1257 N N   . ARG   B 1 51  ? 7.866   -6.660  38.250 1.00 15.86 ? 1844 ARG   B N   1 
ATOM   1258 C CA  . ARG   B 1 51  ? 8.770   -7.483  37.441 1.00 19.71 ? 1844 ARG   B CA  1 
ATOM   1259 C C   . ARG   B 1 51  ? 8.047   -8.101  36.245 1.00 19.54 ? 1844 ARG   B C   1 
ATOM   1260 O O   . ARG   B 1 51  ? 8.579   -8.121  35.123 1.00 23.48 ? 1844 ARG   B O   1 
ATOM   1261 C CB  . ARG   B 1 51  ? 9.410   -8.570  38.316 1.00 20.05 ? 1844 ARG   B CB  1 
ATOM   1262 C CG  . ARG   B 1 51  ? 10.229  -9.623  37.571 1.00 30.73 ? 1844 ARG   B CG  1 
ATOM   1263 C CD  . ARG   B 1 51  ? 11.440  -9.031  36.874 1.00 33.08 ? 1844 ARG   B CD  1 
ATOM   1264 N NE  . ARG   B 1 51  ? 12.453  -8.516  37.804 1.00 27.75 ? 1844 ARG   B NE  1 
ATOM   1265 C CZ  . ARG   B 1 51  ? 13.619  -8.006  37.412 1.00 24.30 ? 1844 ARG   B CZ  1 
ATOM   1266 N NH1 . ARG   B 1 51  ? 13.922  -7.958  36.120 1.00 32.71 ? 1844 ARG   B NH1 1 
ATOM   1267 N NH2 . ARG   B 1 51  ? 14.482  -7.549  38.305 1.00 37.18 ? 1844 ARG   B NH2 1 
ATOM   1268 N N   . GLU   B 1 52  ? 6.838   -8.614  36.464 1.00 19.70 ? 1845 GLU   B N   1 
ATOM   1269 C CA  . GLU   B 1 52  ? 6.105   -9.275  35.389 1.00 26.63 ? 1845 GLU   B CA  1 
ATOM   1270 C C   . GLU   B 1 52  ? 5.724   -8.280  34.301 1.00 15.99 ? 1845 GLU   B C   1 
ATOM   1271 O O   . GLU   B 1 52  ? 5.799   -8.588  33.107 1.00 22.27 ? 1845 GLU   B O   1 
ATOM   1272 C CB  . GLU   B 1 52  ? 4.857   -9.953  35.955 1.00 27.31 ? 1845 GLU   B CB  1 
ATOM   1273 C CG  . GLU   B 1 52  ? 4.134   -10.903 34.984 1.00 29.23 ? 1845 GLU   B CG  1 
ATOM   1274 C CD  . GLU   B 1 52  ? 3.242   -10.197 33.955 1.00 28.54 ? 1845 GLU   B CD  1 
ATOM   1275 O OE1 . GLU   B 1 52  ? 2.859   -9.020  34.155 1.00 26.93 ? 1845 GLU   B OE1 1 
ATOM   1276 O OE2 . GLU   B 1 52  ? 2.914   -10.837 32.936 1.00 36.36 ? 1845 GLU   B OE2 1 
ATOM   1277 N N   . ARG   B 1 53  ? 5.256   -7.104  34.704 1.00 16.56 ? 1846 ARG   B N   1 
ATOM   1278 C CA  . ARG   B 1 53  ? 4.868   -6.083  33.743 1.00 18.62 ? 1846 ARG   B CA  1 
ATOM   1279 C C   . ARG   B 1 53  ? 6.081   -5.547  33.000 1.00 19.58 ? 1846 ARG   B C   1 
ATOM   1280 O O   . ARG   B 1 53  ? 6.018   -5.319  31.788 1.00 23.85 ? 1846 ARG   B O   1 
ATOM   1281 C CB  . ARG   B 1 53  ? 4.133   -4.959  34.456 1.00 25.67 ? 1846 ARG   B CB  1 
ATOM   1282 C CG  . ARG   B 1 53  ? 3.786   -3.769  33.575 1.00 18.28 ? 1846 ARG   B CG  1 
ATOM   1283 C CD  . ARG   B 1 53  ? 2.881   -2.841  34.377 1.00 21.08 ? 1846 ARG   B CD  1 
ATOM   1284 N NE  . ARG   B 1 53  ? 2.568   -1.622  33.655 1.00 18.38 ? 1846 ARG   B NE  1 
ATOM   1285 C CZ  . ARG   B 1 53  ? 1.973   -0.556  34.183 1.00 21.78 ? 1846 ARG   B CZ  1 
ATOM   1286 N NH1 . ARG   B 1 53  ? 1.623   -0.537  35.462 1.00 24.12 ? 1846 ARG   B NH1 1 
ATOM   1287 N NH2 . ARG   B 1 53  ? 1.751   0.511   33.428 1.00 26.73 ? 1846 ARG   B NH2 1 
ATOM   1288 N N   . LEU   B 1 54  ? 7.201   -5.347  33.706 1.00 20.32 ? 1847 LEU   B N   1 
ATOM   1289 C CA  . LEU   B 1 54  ? 8.417   -4.903  33.031 1.00 19.97 ? 1847 LEU   B CA  1 
ATOM   1290 C C   . LEU   B 1 54  ? 8.882   -5.922  31.991 1.00 26.22 ? 1847 LEU   B C   1 
ATOM   1291 O O   . LEU   B 1 54  ? 9.301   -5.546  30.888 1.00 31.52 ? 1847 LEU   B O   1 
ATOM   1292 C CB  . LEU   B 1 54  ? 9.515   -4.636  34.062 1.00 18.06 ? 1847 LEU   B CB  1 
ATOM   1293 C CG  . LEU   B 1 54  ? 10.911  -4.213  33.597 1.00 22.84 ? 1847 LEU   B CG  1 
ATOM   1294 C CD1 . LEU   B 1 54  ? 10.892  -2.861  32.882 1.00 26.49 ? 1847 LEU   B CD1 1 
ATOM   1295 C CD2 . LEU   B 1 54  ? 11.884  -4.169  34.783 1.00 25.75 ? 1847 LEU   B CD2 1 
ATOM   1296 N N   . SER   B 1 55  ? 8.769   -7.220  32.303 1.00 25.34 ? 1848 SER   B N   1 
ATOM   1297 C CA  A SER   B 1 55  ? 9.319   -8.256  31.434 0.63 31.03 ? 1848 SER   B CA  1 
ATOM   1298 C CA  B SER   B 1 55  ? 9.318   -8.256  31.434 0.37 31.20 ? 1848 SER   B CA  1 
ATOM   1299 C C   . SER   B 1 55  ? 8.538   -8.424  30.135 1.00 34.38 ? 1848 SER   B C   1 
ATOM   1300 O O   . SER   B 1 55  ? 9.104   -8.898  29.144 1.00 34.63 ? 1848 SER   B O   1 
ATOM   1301 C CB  A SER   B 1 55  ? 9.378   -9.590  32.180 0.63 33.63 ? 1848 SER   B CB  1 
ATOM   1302 C CB  B SER   B 1 55  ? 9.374   -9.593  32.176 0.37 33.21 ? 1848 SER   B CB  1 
ATOM   1303 O OG  A SER   B 1 55  ? 10.265  -9.521  33.285 0.63 35.87 ? 1848 SER   B OG  1 
ATOM   1304 O OG  B SER   B 1 55  ? 8.079   -10.126 32.392 0.37 27.95 ? 1848 SER   B OG  1 
ATOM   1305 N N   . ARG   B 1 56  ? 7.253   -8.063  30.102 1.00 35.94 ? 1849 ARG   B N   1 
ATOM   1306 C CA  A ARG   B 1 56  ? 6.466   -8.165  28.877 0.66 34.81 ? 1849 ARG   B CA  1 
ATOM   1307 C CA  B ARG   B 1 56  ? 6.452   -8.160  28.888 0.34 34.24 ? 1849 ARG   B CA  1 
ATOM   1308 C C   . ARG   B 1 56  ? 6.304   -6.816  28.187 1.00 32.65 ? 1849 ARG   B C   1 
ATOM   1309 O O   . ARG   B 1 56  ? 5.353   -6.620  27.421 1.00 30.26 ? 1849 ARG   B O   1 
ATOM   1310 C CB  A ARG   B 1 56  ? 5.099   -8.788  29.160 0.66 31.08 ? 1849 ARG   B CB  1 
ATOM   1311 C CB  B ARG   B 1 56  ? 5.076   -8.748  29.205 0.34 32.02 ? 1849 ARG   B CB  1 
ATOM   1312 C CG  A ARG   B 1 56  ? 4.329   -8.069  30.243 0.66 28.89 ? 1849 ARG   B CG  1 
ATOM   1313 C CG  B ARG   B 1 56  ? 4.310   -7.959  30.247 0.34 30.15 ? 1849 ARG   B CG  1 
ATOM   1314 C CD  A ARG   B 1 56  ? 2.862   -8.457  30.246 0.66 35.29 ? 1849 ARG   B CD  1 
ATOM   1315 C CD  B ARG   B 1 56  ? 2.816   -8.226  30.165 0.34 34.46 ? 1849 ARG   B CD  1 
ATOM   1316 N NE  A ARG   B 1 56  ? 2.136   -7.754  31.300 0.66 34.25 ? 1849 ARG   B NE  1 
ATOM   1317 N NE  B ARG   B 1 56  ? 2.048   -7.010  30.411 0.34 33.35 ? 1849 ARG   B NE  1 
ATOM   1318 C CZ  A ARG   B 1 56  ? 1.668   -6.514  31.190 0.66 33.63 ? 1849 ARG   B CZ  1 
ATOM   1319 C CZ  B ARG   B 1 56  ? 1.523   -6.677  31.586 0.34 33.93 ? 1849 ARG   B CZ  1 
ATOM   1320 N NH1 A ARG   B 1 56  ? 1.027   -5.959  32.210 0.66 38.45 ? 1849 ARG   B NH1 1 
ATOM   1321 N NH1 B ARG   B 1 56  ? 0.844   -5.543  31.709 0.34 35.06 ? 1849 ARG   B NH1 1 
ATOM   1322 N NH2 A ARG   B 1 56  ? 1.847   -5.824  30.071 0.66 28.08 ? 1849 ARG   B NH2 1 
ATOM   1323 N NH2 B ARG   B 1 56  ? 1.671   -7.475  32.637 0.34 30.41 ? 1849 ARG   B NH2 1 
ATOM   1324 N N   . GLY   B 1 57  ? 7.226   -5.890  28.432 1.00 22.81 ? 1850 GLY   B N   1 
ATOM   1325 C CA  . GLY   B 1 57  ? 7.123   -4.560  27.872 1.00 19.68 ? 1850 GLY   B CA  1 
ATOM   1326 C C   . GLY   B 1 57  ? 5.900   -3.794  28.324 1.00 28.06 ? 1850 GLY   B C   1 
ATOM   1327 O O   . GLY   B 1 57  ? 5.403   -2.944  27.581 1.00 25.74 ? 1850 GLY   B O   1 
ATOM   1328 N N   . GLY   B 1 58  ? 5.404   -4.059  29.543 1.00 17.33 ? 1851 GLY   B N   1 
ATOM   1329 C CA  . GLY   B 1 58  ? 4.179   -3.425  30.004 1.00 16.67 ? 1851 GLY   B CA  1 
ATOM   1330 C C   . GLY   B 1 58  ? 4.310   -1.994  30.451 1.00 24.25 ? 1851 GLY   B C   1 
ATOM   1331 O O   . GLY   B 1 58  ? 3.291   -1.358  30.722 1.00 33.53 ? 1851 GLY   B O   1 
ATOM   1332 N N   . TYR   B 1 59  ? 5.529   -1.470  30.540 1.00 23.34 ? 1852 TYR   B N   1 
ATOM   1333 C CA  . TYR   B 1 59  ? 5.767   -0.085  30.919 1.00 26.49 ? 1852 TYR   B CA  1 
ATOM   1334 C C   . TYR   B 1 59  ? 6.168   0.719   29.693 1.00 22.04 ? 1852 TYR   B C   1 
ATOM   1335 O O   . TYR   B 1 59  ? 7.211   0.451   29.085 1.00 24.24 ? 1852 TYR   B O   1 
ATOM   1336 C CB  . TYR   B 1 59  ? 6.866   0.008   31.971 1.00 21.03 ? 1852 TYR   B CB  1 
ATOM   1337 C CG  . TYR   B 1 59  ? 6.482   -0.515  33.335 1.00 21.40 ? 1852 TYR   B CG  1 
ATOM   1338 C CD1 . TYR   B 1 59  ? 5.508   0.125   34.099 1.00 21.34 ? 1852 TYR   B CD1 1 
ATOM   1339 C CD2 . TYR   B 1 59  ? 7.127   -1.625  33.877 1.00 22.49 ? 1852 TYR   B CD2 1 
ATOM   1340 C CE1 . TYR   B 1 59  ? 5.174   -0.337  35.359 1.00 20.75 ? 1852 TYR   B CE1 1 
ATOM   1341 C CE2 . TYR   B 1 59  ? 6.790   -2.097  35.151 1.00 19.59 ? 1852 TYR   B CE2 1 
ATOM   1342 C CZ  . TYR   B 1 59  ? 5.818   -1.452  35.875 1.00 20.63 ? 1852 TYR   B CZ  1 
ATOM   1343 O OH  . TYR   B 1 59  ? 5.490   -1.925  37.135 1.00 22.18 ? 1852 TYR   B OH  1 
ATOM   1344 N N   . THR   B 1 60  ? 5.358   1.716   29.340 1.00 27.02 ? 1853 THR   B N   1 
ATOM   1345 C CA  . THR   B 1 60  ? 5.716   2.574   28.222 1.00 27.18 ? 1853 THR   B CA  1 
ATOM   1346 C C   . THR   B 1 60  ? 6.621   3.732   28.630 1.00 23.34 ? 1853 THR   B C   1 
ATOM   1347 O O   . THR   B 1 60  ? 7.268   4.325   27.765 1.00 26.03 ? 1853 THR   B O   1 
ATOM   1348 C CB  . THR   B 1 60  ? 4.458   3.124   27.528 1.00 29.17 ? 1853 THR   B CB  1 
ATOM   1349 O OG1 . THR   B 1 60  ? 3.741   3.973   28.432 1.00 27.95 ? 1853 THR   B OG1 1 
ATOM   1350 C CG2 . THR   B 1 60  ? 3.548   1.991   27.075 1.00 31.83 ? 1853 THR   B CG2 1 
ATOM   1351 N N   . SER   B 1 61  ? 6.710   4.054   29.921 1.00 27.67 ? 1854 SER   B N   1 
ATOM   1352 C CA  . SER   B 1 61  ? 7.543   5.164   30.367 1.00 24.13 ? 1854 SER   B CA  1 
ATOM   1353 C C   . SER   B 1 61  ? 8.033   4.884   31.779 1.00 22.55 ? 1854 SER   B C   1 
ATOM   1354 O O   . SER   B 1 61  ? 7.468   4.057   32.495 1.00 20.62 ? 1854 SER   B O   1 
ATOM   1355 C CB  . SER   B 1 61  ? 6.791   6.504   30.333 1.00 25.84 ? 1854 SER   B CB  1 
ATOM   1356 O OG  . SER   B 1 61  ? 5.767   6.552   31.312 1.00 30.25 ? 1854 SER   B OG  1 
ATOM   1357 N N   . SER   B 1 62  ? 9.103   5.584   32.167 1.00 19.38 ? 1855 SER   B N   1 
ATOM   1358 C CA  . SER   B 1 62  ? 9.608   5.460   33.536 1.00 23.94 ? 1855 SER   B CA  1 
ATOM   1359 C C   . SER   B 1 62  ? 8.605   5.995   34.550 1.00 22.26 ? 1855 SER   B C   1 
ATOM   1360 O O   . SER   B 1 62  ? 8.596   5.551   35.710 1.00 25.32 ? 1855 SER   B O   1 
ATOM   1361 C CB  . SER   B 1 62  ? 10.945  6.186   33.674 1.00 26.99 ? 1855 SER   B CB  1 
ATOM   1362 O OG  . SER   B 1 62  ? 10.858  7.525   33.206 1.00 32.30 ? 1855 SER   B OG  1 
ATOM   1363 N N   . GLU   B 1 63  ? 7.743   6.924   34.121 1.00 26.49 ? 1856 GLU   B N   1 
ATOM   1364 C CA  . GLU   B 1 63  ? 6.717   7.487   34.998 1.00 28.41 ? 1856 GLU   B CA  1 
ATOM   1365 C C   . GLU   B 1 63  ? 5.775   6.412   35.540 1.00 26.58 ? 1856 GLU   B C   1 
ATOM   1366 O O   . GLU   B 1 63  ? 5.384   6.455   36.715 1.00 27.25 ? 1856 GLU   B O   1 
ATOM   1367 C CB  . GLU   B 1 63  ? 5.923   8.567   34.254 1.00 22.77 ? 1856 GLU   B CB  1 
ATOM   1368 C CG  . GLU   B 1 63  ? 6.571   9.948   34.235 1.00 39.62 ? 1856 GLU   B CG  1 
ATOM   1369 C CD  . GLU   B 1 63  ? 7.824   10.020  33.367 1.00 49.87 ? 1856 GLU   B CD  1 
ATOM   1370 O OE1 . GLU   B 1 63  ? 7.943   9.238   32.399 1.00 47.93 ? 1856 GLU   B OE1 1 
ATOM   1371 O OE2 . GLU   B 1 63  ? 8.695   10.866  33.661 1.00 55.44 ? 1856 GLU   B OE2 1 
ATOM   1372 N N   . GLU   B 1 64  ? 5.382   5.446   34.700 1.00 22.17 ? 1857 GLU   B N   1 
ATOM   1373 C CA  . GLU   B 1 64  ? 4.507   4.381   35.184 1.00 26.93 ? 1857 GLU   B CA  1 
ATOM   1374 C C   . GLU   B 1 64  ? 5.239   3.464   36.158 1.00 21.48 ? 1857 GLU   B C   1 
ATOM   1375 O O   . GLU   B 1 64  ? 4.675   3.049   37.182 1.00 21.72 ? 1857 GLU   B O   1 
ATOM   1376 C CB  . GLU   B 1 64  ? 3.956   3.587   34.006 1.00 24.94 ? 1857 GLU   B CB  1 
ATOM   1377 C CG  . GLU   B 1 64  ? 3.310   4.456   32.937 1.00 35.08 ? 1857 GLU   B CG  1 
ATOM   1378 C CD  . GLU   B 1 64  ? 3.060   3.677   31.678 1.00 44.19 ? 1857 GLU   B CD  1 
ATOM   1379 O OE1 . GLU   B 1 64  ? 2.148   4.054   30.908 1.00 57.28 ? 1857 GLU   B OE1 1 
ATOM   1380 O OE2 . GLU   B 1 64  ? 3.772   2.669   31.476 1.00 35.14 ? 1857 GLU   B OE2 1 
ATOM   1381 N N   . PHE   B 1 65  ? 6.495   3.138   35.859 1.00 22.83 ? 1858 PHE   B N   1 
ATOM   1382 C CA  . PHE   B 1 65  ? 7.289   2.347   36.792 1.00 22.26 ? 1858 PHE   B CA  1 
ATOM   1383 C C   . PHE   B 1 65  ? 7.385   3.039   38.146 1.00 24.45 ? 1858 PHE   B C   1 
ATOM   1384 O O   . PHE   B 1 65  ? 7.147   2.425   39.199 1.00 20.15 ? 1858 PHE   B O   1 
ATOM   1385 C CB  . PHE   B 1 65  ? 8.677   2.104   36.200 1.00 19.90 ? 1858 PHE   B CB  1 
ATOM   1386 C CG  . PHE   B 1 65  ? 9.580   1.306   37.087 1.00 19.92 ? 1858 PHE   B CG  1 
ATOM   1387 C CD1 . PHE   B 1 65  ? 10.389  1.938   38.010 1.00 16.66 ? 1858 PHE   B CD1 1 
ATOM   1388 C CD2 . PHE   B 1 65  ? 9.632   -0.078  36.987 1.00 24.26 ? 1858 PHE   B CD2 1 
ATOM   1389 C CE1 . PHE   B 1 65  ? 11.222  1.210   38.838 1.00 23.73 ? 1858 PHE   B CE1 1 
ATOM   1390 C CE2 . PHE   B 1 65  ? 10.469  -0.816  37.807 1.00 32.75 ? 1858 PHE   B CE2 1 
ATOM   1391 C CZ  . PHE   B 1 65  ? 11.270  -0.168  38.736 1.00 23.63 ? 1858 PHE   B CZ  1 
ATOM   1392 N N   . ALA   B 1 66  ? 7.718   4.329   38.136 1.00 20.63 ? 1859 ALA   B N   1 
ATOM   1393 C CA  . ALA   B 1 66  ? 7.848   5.080   39.385 1.00 19.86 ? 1859 ALA   B CA  1 
ATOM   1394 C C   . ALA   B 1 66  ? 6.544   5.098   40.173 1.00 22.24 ? 1859 ALA   B C   1 
ATOM   1395 O O   . ALA   B 1 66  ? 6.553   4.981   41.408 1.00 24.27 ? 1859 ALA   B O   1 
ATOM   1396 C CB  . ALA   B 1 66  ? 8.314   6.504   39.086 1.00 24.30 ? 1859 ALA   B CB  1 
ATOM   1397 N N   . ALA   B 1 67  ? 5.412   5.260   39.486 1.00 23.41 ? 1860 ALA   B N   1 
ATOM   1398 C CA  . ALA   B 1 67  ? 4.123   5.221   40.169 1.00 26.01 ? 1860 ALA   B CA  1 
ATOM   1399 C C   . ALA   B 1 67  ? 3.920   3.887   40.863 1.00 29.84 ? 1860 ALA   B C   1 
ATOM   1400 O O   . ALA   B 1 67  ? 3.441   3.845   42.002 1.00 22.21 ? 1860 ALA   B O   1 
ATOM   1401 C CB  . ALA   B 1 67  ? 2.977   5.490   39.189 1.00 28.86 ? 1860 ALA   B CB  1 
ATOM   1402 N N   . ASP   B 1 68  ? 4.285   2.782   40.201 1.00 18.64 ? 1861 ASP   B N   1 
ATOM   1403 C CA  . ASP   B 1 68  ? 4.107   1.479   40.832 1.00 20.07 ? 1861 ASP   B CA  1 
ATOM   1404 C C   . ASP   B 1 68  ? 4.998   1.328   42.059 1.00 18.56 ? 1861 ASP   B C   1 
ATOM   1405 O O   . ASP   B 1 68  ? 4.559   0.795   43.082 1.00 18.78 ? 1861 ASP   B O   1 
ATOM   1406 C CB  . ASP   B 1 68  ? 4.378   0.353   39.841 1.00 20.02 ? 1861 ASP   B CB  1 
ATOM   1407 C CG  . ASP   B 1 68  ? 3.127   -0.093  39.119 1.00 23.31 ? 1861 ASP   B CG  1 
ATOM   1408 O OD1 . ASP   B 1 68  ? 2.031   0.367   39.511 1.00 29.19 ? 1861 ASP   B OD1 1 
ATOM   1409 O OD2 . ASP   B 1 68  ? 3.235   -0.906  38.175 1.00 24.88 ? 1861 ASP   B OD2 1 
ATOM   1410 N N   . ALA   B 1 69  ? 6.258   1.767   41.963 1.00 22.83 ? 1862 ALA   B N   1 
ATOM   1411 C CA  . ALA   B 1 69  ? 7.166   1.694   43.107 1.00 18.87 ? 1862 ALA   B CA  1 
ATOM   1412 C C   . ALA   B 1 69  ? 6.586   2.429   44.308 1.00 23.86 ? 1862 ALA   B C   1 
ATOM   1413 O O   . ALA   B 1 69  ? 6.535   1.884   45.415 1.00 21.83 ? 1862 ALA   B O   1 
ATOM   1414 C CB  . ALA   B 1 69  ? 8.531   2.277   42.741 1.00 24.27 ? 1862 ALA   B CB  1 
ATOM   1415 N N   . LEU   B 1 70  ? 6.132   3.667   44.098 1.00 24.90 ? 1863 LEU   B N   1 
ATOM   1416 C CA  . LEU   B 1 70  ? 5.612   4.476   45.197 1.00 23.71 ? 1863 LEU   B CA  1 
ATOM   1417 C C   . LEU   B 1 70  ? 4.353   3.868   45.789 1.00 25.72 ? 1863 LEU   B C   1 
ATOM   1418 O O   . LEU   B 1 70  ? 4.128   3.956   47.008 1.00 21.64 ? 1863 LEU   B O   1 
ATOM   1419 C CB  . LEU   B 1 70  ? 5.342   5.900   44.711 1.00 22.95 ? 1863 LEU   B CB  1 
ATOM   1420 C CG  . LEU   B 1 70  ? 6.617   6.702   44.459 1.00 26.83 ? 1863 LEU   B CG  1 
ATOM   1421 C CD1 . LEU   B 1 70  ? 6.302   8.120   43.993 1.00 31.89 ? 1863 LEU   B CD1 1 
ATOM   1422 C CD2 . LEU   B 1 70  ? 7.486   6.709   45.715 1.00 30.41 ? 1863 LEU   B CD2 1 
ATOM   1423 N N   . LEU   B 1 71  ? 3.532   3.242   44.940 1.00 20.58 ? 1864 LEU   B N   1 
ATOM   1424 C CA  . LEU   B 1 71  ? 2.357   2.522   45.401 1.00 19.91 ? 1864 LEU   B CA  1 
ATOM   1425 C C   . LEU   B 1 71  ? 2.722   1.445   46.416 1.00 19.05 ? 1864 LEU   B C   1 
ATOM   1426 O O   . LEU   B 1 71  ? 2.041   1.300   47.441 1.00 17.04 ? 1864 LEU   B O   1 
ATOM   1427 C CB  . LEU   B 1 71  ? 1.646   1.917   44.190 1.00 21.34 ? 1864 LEU   B CB  1 
ATOM   1428 C CG  . LEU   B 1 71  ? 0.210   1.444   44.297 1.00 27.33 ? 1864 LEU   B CG  1 
ATOM   1429 C CD1 . LEU   B 1 71  ? -0.612  2.425   45.101 1.00 24.71 ? 1864 LEU   B CD1 1 
ATOM   1430 C CD2 . LEU   B 1 71  ? -0.357  1.288   42.890 1.00 17.68 ? 1864 LEU   B CD2 1 
ATOM   1431 N N   . VAL   B 1 72  ? 3.788   0.676   46.154 1.00 20.17 ? 1865 VAL   B N   1 
ATOM   1432 C CA  . VAL   B 1 72  ? 4.219   -0.356  47.107 1.00 18.57 ? 1865 VAL   B CA  1 
ATOM   1433 C C   . VAL   B 1 72  ? 4.411   0.252   48.485 1.00 21.61 ? 1865 VAL   B C   1 
ATOM   1434 O O   . VAL   B 1 72  ? 3.857   -0.224  49.480 1.00 19.65 ? 1865 VAL   B O   1 
ATOM   1435 C CB  . VAL   B 1 72  ? 5.509   -1.044  46.627 1.00 19.81 ? 1865 VAL   B CB  1 
ATOM   1436 C CG1 . VAL   B 1 72  ? 5.980   -2.063  47.645 1.00 18.55 ? 1865 VAL   B CG1 1 
ATOM   1437 C CG2 . VAL   B 1 72  ? 5.268   -1.704  45.287 1.00 17.86 ? 1865 VAL   B CG2 1 
ATOM   1438 N N   . PHE   B 1 73  ? 5.175   1.335   48.553 1.00 20.66 ? 1866 PHE   B N   1 
ATOM   1439 C CA  . PHE   B 1 73  ? 5.480   1.940   49.839 1.00 22.11 ? 1866 PHE   B CA  1 
ATOM   1440 C C   . PHE   B 1 73  ? 4.289   2.700   50.405 1.00 23.06 ? 1866 PHE   B C   1 
ATOM   1441 O O   . PHE   B 1 73  ? 4.111   2.733   51.627 1.00 15.84 ? 1866 PHE   B O   1 
ATOM   1442 C CB  . PHE   B 1 73  ? 6.693   2.853   49.702 1.00 19.85 ? 1866 PHE   B CB  1 
ATOM   1443 C CG  . PHE   B 1 73  ? 7.801   2.241   48.915 1.00 22.52 ? 1866 PHE   B CG  1 
ATOM   1444 C CD1 . PHE   B 1 73  ? 8.239   0.954   49.196 1.00 21.89 ? 1866 PHE   B CD1 1 
ATOM   1445 C CD2 . PHE   B 1 73  ? 8.377   2.928   47.853 1.00 18.38 ? 1866 PHE   B CD2 1 
ATOM   1446 C CE1 . PHE   B 1 73  ? 9.252   0.379   48.436 1.00 32.94 ? 1866 PHE   B CE1 1 
ATOM   1447 C CE2 . PHE   B 1 73  ? 9.403   2.361   47.096 1.00 24.42 ? 1866 PHE   B CE2 1 
ATOM   1448 C CZ  . PHE   B 1 73  ? 9.838   1.087   47.391 1.00 22.64 ? 1866 PHE   B CZ  1 
ATOM   1449 N N   . ASP   B 1 74  ? 3.457   3.305   49.553 1.00 22.30 ? 1867 ASP   B N   1 
ATOM   1450 C CA  . ASP   B 1 74  ? 2.290   4.002   50.085 1.00 20.66 ? 1867 ASP   B CA  1 
ATOM   1451 C C   . ASP   B 1 74  ? 1.272   3.024   50.662 1.00 15.91 ? 1867 ASP   B C   1 
ATOM   1452 O O   . ASP   B 1 74  ? 0.656   3.307   51.697 1.00 18.76 ? 1867 ASP   B O   1 
ATOM   1453 C CB  . ASP   B 1 74  ? 1.662   4.889   49.020 1.00 21.13 ? 1867 ASP   B CB  1 
ATOM   1454 C CG  . ASP   B 1 74  ? 2.485   6.134   48.732 1.00 23.39 ? 1867 ASP   B CG  1 
ATOM   1455 O OD1 . ASP   B 1 74  ? 3.270   6.577   49.607 1.00 26.05 ? 1867 ASP   B OD1 1 
ATOM   1456 O OD2 . ASP   B 1 74  ? 2.351   6.675   47.610 1.00 30.09 ? 1867 ASP   B OD2 1 
ATOM   1457 N N   . ASN   B 1 75  ? 1.090   1.863   50.031 1.00 20.96 ? 1868 ASN   B N   1 
ATOM   1458 C CA  . ASN   B 1 75  ? 0.239   0.839   50.624 1.00 25.87 ? 1868 ASN   B CA  1 
ATOM   1459 C C   . ASN   B 1 75  ? 0.834   0.341   51.927 1.00 24.50 ? 1868 ASN   B C   1 
ATOM   1460 O O   . ASN   B 1 75  ? 0.127   0.189   52.938 1.00 19.94 ? 1868 ASN   B O   1 
ATOM   1461 C CB  . ASN   B 1 75  ? 0.062   -0.333  49.668 1.00 16.30 ? 1868 ASN   B CB  1 
ATOM   1462 C CG  . ASN   B 1 75  ? -0.710  0.037   48.431 1.00 15.05 ? 1868 ASN   B CG  1 
ATOM   1463 O OD1 . ASN   B 1 75  ? -1.474  1.009   48.415 1.00 16.07 ? 1868 ASN   B OD1 1 
ATOM   1464 N ND2 . ASN   B 1 75  ? -0.517  -0.746  47.380 1.00 18.22 ? 1868 ASN   B ND2 1 
ATOM   1465 N N   . CYS   B 1 76  ? 2.139   0.071   51.922 1.00 17.23 ? 1869 CYS   B N   1 
ATOM   1466 C CA  . CYS   B 1 76  ? 2.762   -0.385  53.160 1.00 17.21 ? 1869 CYS   B CA  1 
ATOM   1467 C C   . CYS   B 1 76  ? 2.484   0.592   54.294 1.00 20.73 ? 1869 CYS   B C   1 
ATOM   1468 O O   . CYS   B 1 76  ? 2.062   0.189   55.380 1.00 20.95 ? 1869 CYS   B O   1 
ATOM   1469 C CB  . CYS   B 1 76  ? 4.263   -0.582  52.963 1.00 16.91 ? 1869 CYS   B CB  1 
ATOM   1470 S SG  . CYS   B 1 76  ? 5.080   -1.302  54.370 1.00 22.25 ? 1869 CYS   B SG  1 
ATOM   1471 N N   . GLN   B 1 77  ? 2.669   1.890   54.040 1.00 20.63 ? 1870 GLN   B N   1 
ATOM   1472 C CA  . GLN   B 1 77  ? 2.532   2.890   55.097 1.00 20.28 ? 1870 GLN   B CA  1 
ATOM   1473 C C   . GLN   B 1 77  ? 1.093   3.022   55.593 1.00 21.10 ? 1870 GLN   B C   1 
ATOM   1474 O O   . GLN   B 1 77  ? 0.864   3.291   56.778 1.00 28.16 ? 1870 GLN   B O   1 
ATOM   1475 C CB  . GLN   B 1 77  ? 3.047   4.235   54.589 1.00 22.46 ? 1870 GLN   B CB  1 
ATOM   1476 C CG  . GLN   B 1 77  ? 2.895   5.379   55.560 1.00 24.37 ? 1870 GLN   B CG  1 
ATOM   1477 C CD  . GLN   B 1 77  ? 3.714   6.574   55.149 1.00 36.16 ? 1870 GLN   B CD  1 
ATOM   1478 O OE1 . GLN   B 1 77  ? 3.899   7.515   55.922 1.00 49.41 ? 1870 GLN   B OE1 1 
ATOM   1479 N NE2 . GLN   B 1 77  ? 4.219   6.544   53.931 1.00 37.40 ? 1870 GLN   B NE2 1 
ATOM   1480 N N   . THR   B 1 78  ? 0.114   2.860   54.703 1.00 18.93 ? 1871 THR   B N   1 
ATOM   1481 C CA  . THR   B 1 78  ? -1.279  2.911   55.127 1.00 28.05 ? 1871 THR   B CA  1 
ATOM   1482 C C   . THR   B 1 78  ? -1.640  1.710   55.990 1.00 22.82 ? 1871 THR   B C   1 
ATOM   1483 O O   . THR   B 1 78  ? -2.299  1.858   57.026 1.00 25.62 ? 1871 THR   B O   1 
ATOM   1484 C CB  . THR   B 1 78  ? -2.190  2.977   53.903 1.00 30.12 ? 1871 THR   B CB  1 
ATOM   1485 O OG1 . THR   B 1 78  ? -1.871  4.143   53.134 1.00 36.07 ? 1871 THR   B OG1 1 
ATOM   1486 C CG2 . THR   B 1 78  ? -3.661  3.016   54.327 1.00 29.95 ? 1871 THR   B CG2 1 
ATOM   1487 N N   . PHE   B 1 79  ? -1.201  0.516   55.599 1.00 21.92 ? 1872 PHE   B N   1 
ATOM   1488 C CA  . PHE   B 1 79  ? -1.675  -0.687  56.262 1.00 19.08 ? 1872 PHE   B CA  1 
ATOM   1489 C C   . PHE   B 1 79  ? -0.893  -0.952  57.541 1.00 23.47 ? 1872 PHE   B C   1 
ATOM   1490 O O   . PHE   B 1 79  ? -1.475  -1.448  58.509 1.00 27.64 ? 1872 PHE   B O   1 
ATOM   1491 C CB  . PHE   B 1 79  ? -1.658  -1.865  55.294 1.00 21.59 ? 1872 PHE   B CB  1 
ATOM   1492 C CG  . PHE   B 1 79  ? -2.541  -3.012  55.717 1.00 24.65 ? 1872 PHE   B CG  1 
ATOM   1493 C CD1 . PHE   B 1 79  ? -3.914  -2.924  55.588 1.00 21.56 ? 1872 PHE   B CD1 1 
ATOM   1494 C CD2 . PHE   B 1 79  ? -1.995  -4.173  56.238 1.00 23.36 ? 1872 PHE   B CD2 1 
ATOM   1495 C CE1 . PHE   B 1 79  ? -4.732  -3.964  55.974 1.00 29.44 ? 1872 PHE   B CE1 1 
ATOM   1496 C CE2 . PHE   B 1 79  ? -2.810  -5.231  56.620 1.00 35.33 ? 1872 PHE   B CE2 1 
ATOM   1497 C CZ  . PHE   B 1 79  ? -4.181  -5.126  56.491 1.00 35.46 ? 1872 PHE   B CZ  1 
ATOM   1498 N N   . ASN   B 1 80  ? 0.403   -0.656  57.528 1.00 25.24 ? 1873 ASN   B N   1 
ATOM   1499 C CA  . ASN   B 1 80  ? 1.230   -1.005  58.706 1.00 27.14 ? 1873 ASN   B CA  1 
ATOM   1500 C C   . ASN   B 1 80  ? 1.700   0.191   59.526 1.00 28.93 ? 1873 ASN   B C   1 
ATOM   1501 O O   . ASN   B 1 80  ? 1.884   1.277   58.963 1.00 32.37 ? 1873 ASN   B O   1 
ATOM   1502 C CB  . ASN   B 1 80  ? 2.428   -1.810  58.205 1.00 21.42 ? 1873 ASN   B CB  1 
ATOM   1503 C CG  . ASN   B 1 80  ? 2.010   -2.983  57.351 1.00 22.09 ? 1873 ASN   B CG  1 
ATOM   1504 O OD1 . ASN   B 1 80  ? 1.799   -4.080  57.857 1.00 30.30 ? 1873 ASN   B OD1 1 
ATOM   1505 N ND2 . ASN   B 1 80  ? 1.880   -2.757  56.058 1.00 23.83 ? 1873 ASN   B ND2 1 
ATOM   1506 N N   . GLU   B 1 81  ? 1.854   -0.031  60.827 1.00 35.98 ? 1874 GLU   B N   1 
ATOM   1507 C CA  . GLU   B 1 81  ? 2.379   1.003   61.706 1.00 33.81 ? 1874 GLU   B CA  1 
ATOM   1508 C C   . GLU   B 1 81  ? 3.896   1.135   61.531 1.00 31.06 ? 1874 GLU   B C   1 
ATOM   1509 O O   . GLU   B 1 81  ? 4.579   0.211   61.084 1.00 32.60 ? 1874 GLU   B O   1 
ATOM   1510 C CB  . GLU   B 1 81  ? 2.020   0.702   63.162 1.00 46.60 ? 1874 GLU   B CB  1 
ATOM   1511 C CG  . GLU   B 1 81  ? 0.511   0.612   63.426 1.00 44.97 ? 1874 GLU   B CG  1 
ATOM   1512 C CD  . GLU   B 1 81  ? -0.193  1.961   63.341 1.00 37.09 ? 1874 GLU   B CD  1 
ATOM   1513 O OE1 . GLU   B 1 81  ? 0.279   2.920   63.982 1.00 45.00 ? 1874 GLU   B OE1 1 
ATOM   1514 O OE2 . GLU   B 1 81  ? -1.211  2.070   62.623 1.00 41.30 ? 1874 GLU   B OE2 1 
ATOM   1515 N N   . ASP   B 1 82  ? 4.412   2.313   61.893 1.00 29.60 ? 1875 ASP   B N   1 
ATOM   1516 C CA  . ASP   B 1 82  ? 5.819   2.642   61.652 1.00 35.59 ? 1875 ASP   B CA  1 
ATOM   1517 C C   . ASP   B 1 82  ? 6.771   1.740   62.428 1.00 38.03 ? 1875 ASP   B C   1 
ATOM   1518 O O   . ASP   B 1 82  ? 7.862   1.416   61.941 1.00 35.28 ? 1875 ASP   B O   1 
ATOM   1519 C CB  . ASP   B 1 82  ? 6.091   4.102   62.016 1.00 31.13 ? 1875 ASP   B CB  1 
ATOM   1520 C CG  . ASP   B 1 82  ? 5.498   5.073   61.016 1.00 48.07 ? 1875 ASP   B CG  1 
ATOM   1521 O OD1 . ASP   B 1 82  ? 4.996   4.610   59.971 1.00 38.50 ? 1875 ASP   B OD1 1 
ATOM   1522 O OD2 . ASP   B 1 82  ? 5.537   6.288   61.285 1.00 49.28 ? 1875 ASP   B OD2 1 
ATOM   1523 N N   . ASP   B 1 83  ? 6.406   1.354   63.647 1.00 34.71 ? 1876 ASP   B N   1 
ATOM   1524 C CA  . ASP   B 1 83  ? 7.336   0.550   64.429 1.00 49.06 ? 1876 ASP   B CA  1 
ATOM   1525 C C   . ASP   B 1 83  ? 7.237   -0.935  64.107 1.00 50.60 ? 1876 ASP   B C   1 
ATOM   1526 O O   . ASP   B 1 83  ? 8.021   -1.726  64.644 1.00 55.82 ? 1876 ASP   B O   1 
ATOM   1527 C CB  . ASP   B 1 83  ? 7.129   0.794   65.928 1.00 57.53 ? 1876 ASP   B CB  1 
ATOM   1528 C CG  . ASP   B 1 83  ? 5.683   0.645   66.355 1.00 68.08 ? 1876 ASP   B CG  1 
ATOM   1529 O OD1 . ASP   B 1 83  ? 4.790   0.712   65.483 1.00 68.66 ? 1876 ASP   B OD1 1 
ATOM   1530 O OD2 . ASP   B 1 83  ? 5.445   0.473   67.571 1.00 69.24 ? 1876 ASP   B OD2 1 
ATOM   1531 N N   . SER   B 1 84  ? 6.317   -1.327  63.230 1.00 46.10 ? 1877 SER   B N   1 
ATOM   1532 C CA  . SER   B 1 84  ? 6.240   -2.711  62.788 1.00 45.26 ? 1877 SER   B CA  1 
ATOM   1533 C C   . SER   B 1 84  ? 7.383   -3.035  61.828 1.00 43.06 ? 1877 SER   B C   1 
ATOM   1534 O O   . SER   B 1 84  ? 7.945   -2.154  61.168 1.00 30.96 ? 1877 SER   B O   1 
ATOM   1535 C CB  . SER   B 1 84  ? 4.895   -2.984  62.112 1.00 43.40 ? 1877 SER   B CB  1 
ATOM   1536 O OG  . SER   B 1 84  ? 4.680   -2.105  61.023 1.00 40.16 ? 1877 SER   B OG  1 
ATOM   1537 N N   . GLU   B 1 85  ? 7.734   -4.321  61.769 1.00 42.88 ? 1878 GLU   B N   1 
ATOM   1538 C CA  . GLU   B 1 85  ? 8.857   -4.730  60.938 1.00 34.76 ? 1878 GLU   B CA  1 
ATOM   1539 C C   . GLU   B 1 85  ? 8.563   -4.450  59.480 1.00 34.81 ? 1878 GLU   B C   1 
ATOM   1540 O O   . GLU   B 1 85  ? 9.431   -3.972  58.744 1.00 28.91 ? 1878 GLU   B O   1 
ATOM   1541 C CB  . GLU   B 1 85  ? 9.158   -6.210  61.129 1.00 35.72 ? 1878 GLU   B CB  1 
ATOM   1542 C CG  . GLU   B 1 85  ? 10.619  -6.506  61.301 1.00 49.45 ? 1878 GLU   B CG  1 
ATOM   1543 C CD  . GLU   B 1 85  ? 11.196  -5.814  62.521 1.00 56.09 ? 1878 GLU   B CD  1 
ATOM   1544 O OE1 . GLU   B 1 85  ? 11.774  -4.715  62.382 1.00 57.66 ? 1878 GLU   B OE1 1 
ATOM   1545 O OE2 . GLU   B 1 85  ? 11.053  -6.364  63.630 1.00 65.50 ? 1878 GLU   B OE2 1 
ATOM   1546 N N   . VAL   B 1 86  ? 7.336   -4.729  59.051 1.00 28.59 ? 1879 VAL   B N   1 
ATOM   1547 C CA  . VAL   B 1 86  ? 6.974   -4.419  57.668 1.00 25.53 ? 1879 VAL   B CA  1 
ATOM   1548 C C   . VAL   B 1 86  ? 6.886   -2.914  57.478 1.00 24.74 ? 1879 VAL   B C   1 
ATOM   1549 O O   . VAL   B 1 86  ? 7.268   -2.388  56.431 1.00 22.89 ? 1879 VAL   B O   1 
ATOM   1550 C CB  . VAL   B 1 86  ? 5.673   -5.133  57.268 1.00 24.76 ? 1879 VAL   B CB  1 
ATOM   1551 C CG1 . VAL   B 1 86  ? 5.175   -4.616  55.911 1.00 21.89 ? 1879 VAL   B CG1 1 
ATOM   1552 C CG2 . VAL   B 1 86  ? 5.939   -6.624  57.148 1.00 36.45 ? 1879 VAL   B CG2 1 
ATOM   1553 N N   . GLY   B 1 87  ? 6.386   -2.197  58.481 1.00 28.56 ? 1880 GLY   B N   1 
ATOM   1554 C CA  . GLY   B 1 87  ? 6.405   -0.739  58.435 1.00 38.49 ? 1880 GLY   B CA  1 
ATOM   1555 C C   . GLY   B 1 87  ? 7.791   -0.143  58.236 1.00 28.99 ? 1880 GLY   B C   1 
ATOM   1556 O O   . GLY   B 1 87  ? 7.989   0.745   57.396 1.00 25.42 ? 1880 GLY   B O   1 
ATOM   1557 N N   . LYS   B 1 88  ? 8.772   -0.621  59.000 1.00 32.26 ? 1881 LYS   B N   1 
ATOM   1558 C CA  . LYS   B 1 88  ? 10.116  -0.077  58.896 1.00 29.41 ? 1881 LYS   B CA  1 
ATOM   1559 C C   . LYS   B 1 88  ? 10.728  -0.394  57.539 1.00 27.62 ? 1881 LYS   B C   1 
ATOM   1560 O O   . LYS   B 1 88  ? 11.410  0.452   56.957 1.00 27.36 ? 1881 LYS   B O   1 
ATOM   1561 C CB  . LYS   B 1 88  ? 10.982  -0.619  60.042 1.00 32.26 ? 1881 LYS   B CB  1 
ATOM   1562 C CG  . LYS   B 1 88  ? 12.491  -0.365  59.916 1.00 38.53 ? 1881 LYS   B CG  1 
ATOM   1563 C CD  . LYS   B 1 88  ? 13.241  -0.932  61.124 1.00 45.88 ? 1881 LYS   B CD  1 
ATOM   1564 C CE  . LYS   B 1 88  ? 14.742  -0.880  60.924 1.00 51.69 ? 1881 LYS   B CE  1 
ATOM   1565 N NZ  . LYS   B 1 88  ? 15.458  -2.084  61.446 1.00 53.34 ? 1881 LYS   B NZ  1 
ATOM   1566 N N   . ALA   B 1 89  ? 10.483  -1.599  57.015 1.00 26.06 ? 1882 ALA   B N   1 
ATOM   1567 C CA  . ALA   B 1 89  ? 11.147  -2.017  55.776 1.00 37.52 ? 1882 ALA   B CA  1 
ATOM   1568 C C   . ALA   B 1 89  ? 10.713  -1.157  54.586 1.00 22.72 ? 1882 ALA   B C   1 
ATOM   1569 O O   . ALA   B 1 89  ? 11.523  -0.818  53.708 1.00 26.70 ? 1882 ALA   B O   1 
ATOM   1570 C CB  . ALA   B 1 89  ? 10.861  -3.498  55.510 1.00 27.86 ? 1882 ALA   B CB  1 
ATOM   1571 N N   . GLY   B 1 90  ? 9.436   -0.798  54.540 1.00 37.51 ? 1883 GLY   B N   1 
ATOM   1572 C CA  . GLY   B 1 90  ? 8.938   0.011   53.435 1.00 27.85 ? 1883 GLY   B CA  1 
ATOM   1573 C C   . GLY   B 1 90  ? 9.387   1.450   53.547 1.00 20.95 ? 1883 GLY   B C   1 
ATOM   1574 O O   . GLY   B 1 90  ? 9.597   2.126   52.538 1.00 34.23 ? 1883 GLY   B O   1 
ATOM   1575 N N   . HIS   B 1 91  ? 9.534   1.939   54.777 1.00 26.43 ? 1884 HIS   B N   1 
ATOM   1576 C CA  . HIS   B 1 91  ? 10.208  3.211   54.972 1.00 24.71 ? 1884 HIS   B CA  1 
ATOM   1577 C C   . HIS   B 1 91  ? 11.629  3.148   54.435 1.00 32.65 ? 1884 HIS   B C   1 
ATOM   1578 O O   . HIS   B 1 91  ? 12.088  4.073   53.753 1.00 30.46 ? 1884 HIS   B O   1 
ATOM   1579 C CB  . HIS   B 1 91  ? 10.204  3.564   56.462 1.00 27.15 ? 1884 HIS   B CB  1 
ATOM   1580 C CG  . HIS   B 1 91  ? 8.878   4.024   56.974 1.00 30.17 ? 1884 HIS   B CG  1 
ATOM   1581 N ND1 . HIS   B 1 91  ? 8.082   4.913   56.287 1.00 28.23 ? 1884 HIS   B ND1 1 
ATOM   1582 C CD2 . HIS   B 1 91  ? 8.224   3.748   58.130 1.00 33.31 ? 1884 HIS   B CD2 1 
ATOM   1583 C CE1 . HIS   B 1 91  ? 6.984   5.147   56.983 1.00 33.46 ? 1884 HIS   B CE1 1 
ATOM   1584 N NE2 . HIS   B 1 91  ? 7.048   4.458   58.110 1.00 35.56 ? 1884 HIS   B NE2 1 
ATOM   1585 N N   . ILE   B 1 92  ? 12.328  2.042   54.705 1.00 26.12 ? 1885 ILE   B N   1 
ATOM   1586 C CA  . ILE   B 1 92  ? 13.710  1.903   54.262 1.00 28.38 ? 1885 ILE   B CA  1 
ATOM   1587 C C   . ILE   B 1 92  ? 13.764  1.828   52.744 1.00 26.08 ? 1885 ILE   B C   1 
ATOM   1588 O O   . ILE   B 1 92  ? 14.620  2.458   52.112 1.00 27.50 ? 1885 ILE   B O   1 
ATOM   1589 C CB  . ILE   B 1 92  ? 14.356  0.661   54.907 1.00 28.57 ? 1885 ILE   B CB  1 
ATOM   1590 C CG1 . ILE   B 1 92  ? 14.657  0.896   56.394 1.00 31.02 ? 1885 ILE   B CG1 1 
ATOM   1591 C CG2 . ILE   B 1 92  ? 15.612  0.249   54.149 1.00 29.69 ? 1885 ILE   B CG2 1 
ATOM   1592 C CD1 . ILE   B 1 92  ? 15.221  -0.326  57.078 1.00 32.32 ? 1885 ILE   B CD1 1 
ATOM   1593 N N   . MET   B 1 93  ? 12.835  1.075   52.143 1.00 24.10 ? 1886 MET   B N   1 
ATOM   1594 C CA  . MET   B 1 93  ? 12.850  0.860   50.696 1.00 27.40 ? 1886 MET   B CA  1 
ATOM   1595 C C   . MET   B 1 93  ? 12.427  2.113   49.936 1.00 27.37 ? 1886 MET   B C   1 
ATOM   1596 O O   . MET   B 1 93  ? 12.934  2.375   48.835 1.00 28.47 ? 1886 MET   B O   1 
ATOM   1597 C CB  . MET   B 1 93  ? 11.950  -0.324  50.330 1.00 20.31 ? 1886 MET   B CB  1 
ATOM   1598 C CG  . MET   B 1 93  ? 12.456  -1.705  50.789 1.00 21.00 ? 1886 MET   B CG  1 
ATOM   1599 S SD  . MET   B 1 93  ? 14.131  -2.109  50.270 1.00 24.64 ? 1886 MET   B SD  1 
ATOM   1600 C CE  . MET   B 1 93  ? 14.051  -1.810  48.494 1.00 22.47 ? 1886 MET   B CE  1 
ATOM   1601 N N   . ARG   B 1 94  ? 11.488  2.891   50.492 1.00 28.67 ? 1887 ARG   B N   1 
ATOM   1602 C CA  . ARG   B 1 94  ? 11.110  4.152   49.854 1.00 25.30 ? 1887 ARG   B CA  1 
ATOM   1603 C C   . ARG   B 1 94  ? 12.285  5.112   49.804 1.00 28.84 ? 1887 ARG   B C   1 
ATOM   1604 O O   . ARG   B 1 94  ? 12.461  5.843   48.823 1.00 26.67 ? 1887 ARG   B O   1 
ATOM   1605 C CB  . ARG   B 1 94  ? 9.943   4.824   50.591 1.00 24.24 ? 1887 ARG   B CB  1 
ATOM   1606 C CG  . ARG   B 1 94  ? 9.511   6.140   49.914 1.00 24.51 ? 1887 ARG   B CG  1 
ATOM   1607 C CD  . ARG   B 1 94  ? 8.751   7.097   50.828 1.00 25.20 ? 1887 ARG   B CD  1 
ATOM   1608 N NE  . ARG   B 1 94  ? 7.537   6.497   51.361 1.00 33.99 ? 1887 ARG   B NE  1 
ATOM   1609 C CZ  . ARG   B 1 94  ? 6.369   6.479   50.726 1.00 30.39 ? 1887 ARG   B CZ  1 
ATOM   1610 N NH1 . ARG   B 1 94  ? 6.255   7.025   49.516 1.00 27.58 ? 1887 ARG   B NH1 1 
ATOM   1611 N NH2 . ARG   B 1 94  ? 5.319   5.909   51.304 1.00 20.97 ? 1887 ARG   B NH2 1 
ATOM   1612 N N   . ARG   B 1 95  ? 13.079  5.158   50.874 1.00 32.76 ? 1888 ARG   B N   1 
ATOM   1613 C CA  A ARG   B 1 95  ? 14.258  6.014   50.873 0.68 32.67 ? 1888 ARG   B CA  1 
ATOM   1614 C CA  B ARG   B 1 95  ? 14.254  6.019   50.869 0.32 33.89 ? 1888 ARG   B CA  1 
ATOM   1615 C C   . ARG   B 1 95  ? 15.302  5.507   49.891 1.00 35.78 ? 1888 ARG   B C   1 
ATOM   1616 O O   . ARG   B 1 95  ? 15.938  6.300   49.188 1.00 35.69 ? 1888 ARG   B O   1 
ATOM   1617 C CB  A ARG   B 1 95  ? 14.842  6.106   52.279 0.68 36.55 ? 1888 ARG   B CB  1 
ATOM   1618 C CB  B ARG   B 1 95  ? 14.827  6.138   52.282 0.32 37.08 ? 1888 ARG   B CB  1 
ATOM   1619 C CG  A ARG   B 1 95  ? 14.020  6.957   53.225 0.68 39.20 ? 1888 ARG   B CG  1 
ATOM   1620 C CG  B ARG   B 1 95  ? 13.880  6.834   53.258 0.32 38.52 ? 1888 ARG   B CG  1 
ATOM   1621 C CD  A ARG   B 1 95  ? 14.695  7.053   54.586 0.68 42.69 ? 1888 ARG   B CD  1 
ATOM   1622 C CD  B ARG   B 1 95  ? 14.576  7.213   54.562 0.32 42.04 ? 1888 ARG   B CD  1 
ATOM   1623 N NE  A ARG   B 1 95  ? 16.076  7.513   54.474 0.68 44.89 ? 1888 ARG   B NE  1 
ATOM   1624 N NE  B ARG   B 1 95  ? 15.590  8.251   54.389 0.32 44.45 ? 1888 ARG   B NE  1 
ATOM   1625 C CZ  A ARG   B 1 95  ? 16.423  8.794   54.414 0.68 45.58 ? 1888 ARG   B CZ  1 
ATOM   1626 C CZ  B ARG   B 1 95  ? 16.901  8.030   54.401 0.32 46.46 ? 1888 ARG   B CZ  1 
ATOM   1627 N NH1 A ARG   B 1 95  ? 15.481  9.728   54.459 0.68 44.84 ? 1888 ARG   B NH1 1 
ATOM   1628 N NH1 B ARG   B 1 95  ? 17.374  6.804   54.583 0.32 47.65 ? 1888 ARG   B NH1 1 
ATOM   1629 N NH2 A ARG   B 1 95  ? 17.700  9.139   54.304 0.68 43.73 ? 1888 ARG   B NH2 1 
ATOM   1630 N NH2 B ARG   B 1 95  ? 17.744  9.041   54.238 0.32 44.91 ? 1888 ARG   B NH2 1 
ATOM   1631 N N   . PHE   B 1 96  ? 15.488  4.188   49.823 1.00 30.97 ? 1889 PHE   B N   1 
ATOM   1632 C CA  . PHE   B 1 96  ? 16.412  3.637   48.843 1.00 33.31 ? 1889 PHE   B CA  1 
ATOM   1633 C C   . PHE   B 1 96  ? 15.947  3.970   47.432 1.00 29.82 ? 1889 PHE   B C   1 
ATOM   1634 O O   . PHE   B 1 96  ? 16.740  4.407   46.594 1.00 32.87 ? 1889 PHE   B O   1 
ATOM   1635 C CB  . PHE   B 1 96  ? 16.547  2.127   49.034 1.00 29.68 ? 1889 PHE   B CB  1 
ATOM   1636 C CG  . PHE   B 1 96  ? 17.451  1.477   48.033 1.00 35.54 ? 1889 PHE   B CG  1 
ATOM   1637 C CD1 . PHE   B 1 96  ? 18.779  1.865   47.921 1.00 44.39 ? 1889 PHE   B CD1 1 
ATOM   1638 C CD2 . PHE   B 1 96  ? 16.973  0.491   47.190 1.00 29.36 ? 1889 PHE   B CD2 1 
ATOM   1639 C CE1 . PHE   B 1 96  ? 19.616  1.276   46.998 1.00 41.26 ? 1889 PHE   B CE1 1 
ATOM   1640 C CE2 . PHE   B 1 96  ? 17.817  -0.105  46.264 1.00 39.98 ? 1889 PHE   B CE2 1 
ATOM   1641 C CZ  . PHE   B 1 96  ? 19.131  0.288   46.172 1.00 38.15 ? 1889 PHE   B CZ  1 
ATOM   1642 N N   . PHE   B 1 97  ? 14.647  3.815   47.169 1.00 32.45 ? 1890 PHE   B N   1 
ATOM   1643 C CA  . PHE   B 1 97  ? 14.136  4.071   45.826 1.00 27.20 ? 1890 PHE   B CA  1 
ATOM   1644 C C   . PHE   B 1 97  ? 14.276  5.543   45.448 1.00 28.07 ? 1890 PHE   B C   1 
ATOM   1645 O O   . PHE   B 1 97  ? 14.715  5.868   44.341 1.00 29.77 ? 1890 PHE   B O   1 
ATOM   1646 C CB  . PHE   B 1 97  ? 12.679  3.625   45.707 1.00 22.71 ? 1890 PHE   B CB  1 
ATOM   1647 C CG  . PHE   B 1 97  ? 12.023  4.087   44.438 1.00 23.27 ? 1890 PHE   B CG  1 
ATOM   1648 C CD1 . PHE   B 1 97  ? 12.266  3.422   43.247 1.00 25.13 ? 1890 PHE   B CD1 1 
ATOM   1649 C CD2 . PHE   B 1 97  ? 11.200  5.210   44.426 1.00 27.61 ? 1890 PHE   B CD2 1 
ATOM   1650 C CE1 . PHE   B 1 97  ? 11.687  3.851   42.066 1.00 24.05 ? 1890 PHE   B CE1 1 
ATOM   1651 C CE2 . PHE   B 1 97  ? 10.613  5.644   43.241 1.00 30.75 ? 1890 PHE   B CE2 1 
ATOM   1652 C CZ  . PHE   B 1 97  ? 10.862  4.961   42.062 1.00 29.41 ? 1890 PHE   B CZ  1 
ATOM   1653 N N   . GLU   B 1 98  ? 13.871  6.449   46.339 1.00 31.61 ? 1891 GLU   B N   1 
ATOM   1654 C CA  A GLU   B 1 98  ? 13.966  7.870   46.022 0.52 35.41 ? 1891 GLU   B CA  1 
ATOM   1655 C CA  B GLU   B 1 98  ? 13.968  7.875   46.041 0.48 35.33 ? 1891 GLU   B CA  1 
ATOM   1656 C C   . GLU   B 1 98  ? 15.420  8.307   45.866 1.00 36.00 ? 1891 GLU   B C   1 
ATOM   1657 O O   . GLU   B 1 98  ? 15.728  9.152   45.019 1.00 36.92 ? 1891 GLU   B O   1 
ATOM   1658 C CB  A GLU   B 1 98  ? 13.251  8.698   47.092 0.52 36.40 ? 1891 GLU   B CB  1 
ATOM   1659 C CB  B GLU   B 1 98  ? 13.293  8.686   47.147 0.48 36.33 ? 1891 GLU   B CB  1 
ATOM   1660 C CG  A GLU   B 1 98  ? 11.732  8.579   47.031 0.52 34.12 ? 1891 GLU   B CG  1 
ATOM   1661 C CG  B GLU   B 1 98  ? 11.785  8.532   47.167 0.48 34.06 ? 1891 GLU   B CG  1 
ATOM   1662 C CD  A GLU   B 1 98  ? 11.027  9.495   48.010 0.52 37.44 ? 1891 GLU   B CD  1 
ATOM   1663 C CD  B GLU   B 1 98  ? 11.165  8.923   45.844 0.48 34.10 ? 1891 GLU   B CD  1 
ATOM   1664 O OE1 A GLU   B 1 98  ? 11.481  9.593   49.170 0.52 39.84 ? 1891 GLU   B OE1 1 
ATOM   1665 O OE1 B GLU   B 1 98  ? 11.566  9.969   45.292 0.48 39.19 ? 1891 GLU   B OE1 1 
ATOM   1666 O OE2 A GLU   B 1 98  ? 10.021  10.122  47.617 0.52 38.84 ? 1891 GLU   B OE2 1 
ATOM   1667 O OE2 B GLU   B 1 98  ? 10.296  8.182   45.342 0.48 36.96 ? 1891 GLU   B OE2 1 
ATOM   1668 N N   . SER   B 1 99  ? 16.327  7.736   46.662 1.00 37.12 ? 1892 SER   B N   1 
ATOM   1669 C CA  . SER   B 1 99  ? 17.739  8.088   46.543 1.00 41.14 ? 1892 SER   B CA  1 
ATOM   1670 C C   . SER   B 1 99  ? 18.316  7.625   45.211 1.00 44.84 ? 1892 SER   B C   1 
ATOM   1671 O O   . SER   B 1 99  ? 19.088  8.352   44.568 1.00 47.88 ? 1892 SER   B O   1 
ATOM   1672 C CB  . SER   B 1 99  ? 18.530  7.485   47.703 1.00 40.79 ? 1892 SER   B CB  1 
ATOM   1673 O OG  . SER   B 1 99  ? 19.924  7.678   47.518 1.00 47.63 ? 1892 SER   B OG  1 
ATOM   1674 N N   . ARG   B 1 100 ? 17.948  6.418   44.777 1.00 42.16 ? 1893 ARG   B N   1 
ATOM   1675 C CA  . ARG   B 1 100 ? 18.465  5.871   43.531 1.00 45.26 ? 1893 ARG   B CA  1 
ATOM   1676 C C   . ARG   B 1 100 ? 17.796  6.511   42.321 1.00 43.58 ? 1893 ARG   B C   1 
ATOM   1677 O O   . ARG   B 1 100 ? 18.448  6.748   41.300 1.00 56.95 ? 1893 ARG   B O   1 
ATOM   1678 C CB  . ARG   B 1 100 ? 18.276  4.355   43.516 1.00 44.88 ? 1893 ARG   B CB  1 
ATOM   1679 C CG  . ARG   B 1 100 ? 19.091  3.656   42.460 1.00 48.53 ? 1893 ARG   B CG  1 
ATOM   1680 C CD  . ARG   B 1 100 ? 20.560  4.009   42.623 1.00 54.65 ? 1893 ARG   B CD  1 
ATOM   1681 N NE  . ARG   B 1 100 ? 21.307  3.813   41.381 1.00 63.84 ? 1893 ARG   B NE  1 
ATOM   1682 C CZ  . ARG   B 1 100 ? 22.129  2.795   41.157 1.00 60.18 ? 1893 ARG   B CZ  1 
ATOM   1683 N NH1 . ARG   B 1 100 ? 22.761  2.696   39.999 1.00 57.49 ? 1893 ARG   B NH1 1 
ATOM   1684 N NH2 . ARG   B 1 100 ? 22.322  1.881   42.097 1.00 57.85 ? 1893 ARG   B NH2 1 
ATOM   1685 N N   . TRP   B 1 101 ? 16.501  6.808   42.425 1.00 40.05 ? 1894 TRP   B N   1 
ATOM   1686 C CA  . TRP   B 1 101 ? 15.798  7.489   41.342 1.00 42.51 ? 1894 TRP   B CA  1 
ATOM   1687 C C   . TRP   B 1 101 ? 16.320  8.903   41.155 1.00 45.01 ? 1894 TRP   B C   1 
ATOM   1688 O O   . TRP   B 1 101 ? 16.368  9.411   40.029 1.00 45.99 ? 1894 TRP   B O   1 
ATOM   1689 C CB  . TRP   B 1 101 ? 14.299  7.519   41.637 1.00 40.27 ? 1894 TRP   B CB  1 
ATOM   1690 C CG  . TRP   B 1 101 ? 13.437  7.910   40.470 1.00 32.11 ? 1894 TRP   B CG  1 
ATOM   1691 C CD1 . TRP   B 1 101 ? 12.960  9.154   40.186 1.00 36.24 ? 1894 TRP   B CD1 1 
ATOM   1692 C CD2 . TRP   B 1 101 ? 12.924  7.039   39.450 1.00 37.63 ? 1894 TRP   B CD2 1 
ATOM   1693 N NE1 . TRP   B 1 101 ? 12.187  9.116   39.047 1.00 41.81 ? 1894 TRP   B NE1 1 
ATOM   1694 C CE2 . TRP   B 1 101 ? 12.151  7.829   38.577 1.00 39.86 ? 1894 TRP   B CE2 1 
ATOM   1695 C CE3 . TRP   B 1 101 ? 13.049  5.670   39.189 1.00 36.31 ? 1894 TRP   B CE3 1 
ATOM   1696 C CZ2 . TRP   B 1 101 ? 11.512  7.299   37.457 1.00 37.82 ? 1894 TRP   B CZ2 1 
ATOM   1697 C CZ3 . TRP   B 1 101 ? 12.413  5.144   38.080 1.00 46.25 ? 1894 TRP   B CZ3 1 
ATOM   1698 C CH2 . TRP   B 1 101 ? 11.653  5.959   37.227 1.00 45.51 ? 1894 TRP   B CH2 1 
ATOM   1699 N N   . GLU   B 1 102 ? 16.694  9.563   42.253 1.00 50.23 ? 1895 GLU   B N   1 
ATOM   1700 C CA  . GLU   B 1 102 ? 17.251  10.906  42.167 1.00 61.27 ? 1895 GLU   B CA  1 
ATOM   1701 C C   . GLU   B 1 102 ? 18.651  10.909  41.568 1.00 60.49 ? 1895 GLU   B C   1 
ATOM   1702 O O   . GLU   B 1 102 ? 19.085  11.938  41.044 1.00 65.08 ? 1895 GLU   B O   1 
ATOM   1703 C CB  . GLU   B 1 102 ? 17.268  11.553  43.555 1.00 67.65 ? 1895 GLU   B CB  1 
ATOM   1704 C CG  . GLU   B 1 102 ? 17.541  13.054  43.558 1.00 75.46 ? 1895 GLU   B CG  1 
ATOM   1705 C CD  . GLU   B 1 102 ? 16.515  13.840  42.760 1.00 77.60 ? 1895 GLU   B CD  1 
ATOM   1706 O OE1 . GLU   B 1 102 ? 16.895  14.863  42.147 1.00 77.71 ? 1895 GLU   B OE1 1 
ATOM   1707 O OE2 . GLU   B 1 102 ? 15.330  13.433  42.746 1.00 76.85 ? 1895 GLU   B OE2 1 
ATOM   1708 N N   . GLU   B 1 103 ? 19.363  9.785   41.624 1.00 61.82 ? 1896 GLU   B N   1 
ATOM   1709 C CA  . GLU   B 1 103 ? 20.712  9.719   41.077 1.00 70.24 ? 1896 GLU   B CA  1 
ATOM   1710 C C   . GLU   B 1 103 ? 20.739  9.468   39.575 1.00 76.49 ? 1896 GLU   B C   1 
ATOM   1711 O O   . GLU   B 1 103 ? 21.823  9.492   38.980 1.00 80.00 ? 1896 GLU   B O   1 
ATOM   1712 C CB  . GLU   B 1 103 ? 21.523  8.637   41.792 1.00 70.30 ? 1896 GLU   B CB  1 
ATOM   1713 C CG  . GLU   B 1 103 ? 21.913  9.010   43.208 1.00 73.97 ? 1896 GLU   B CG  1 
ATOM   1714 C CD  . GLU   B 1 103 ? 22.987  8.098   43.771 1.00 78.96 ? 1896 GLU   B CD  1 
ATOM   1715 O OE1 . GLU   B 1 103 ? 24.056  8.612   44.161 1.00 85.50 ? 1896 GLU   B OE1 1 
ATOM   1716 O OE2 . GLU   B 1 103 ? 22.758  6.873   43.810 1.00 76.62 ? 1896 GLU   B OE2 1 
ATOM   1717 N N   . PHE   B 1 104 ? 19.588  9.221   38.952 1.00 74.18 ? 1897 PHE   B N   1 
ATOM   1718 C CA  . PHE   B 1 104 ? 19.514  9.117   37.500 1.00 69.57 ? 1897 PHE   B CA  1 
ATOM   1719 C C   . PHE   B 1 104 ? 18.980  10.418  36.924 1.00 69.11 ? 1897 PHE   B C   1 
ATOM   1720 O O   . PHE   B 1 104 ? 19.723  11.201  36.324 1.00 71.34 ? 1897 PHE   B O   1 
ATOM   1721 C CB  . PHE   B 1 104 ? 18.610  7.959   37.073 1.00 66.54 ? 1897 PHE   B CB  1 
ATOM   1722 C CG  . PHE   B 1 104 ? 19.097  6.609   37.509 1.00 67.41 ? 1897 PHE   B CG  1 
ATOM   1723 C CD1 . PHE   B 1 104 ? 20.446  6.371   37.708 1.00 76.38 ? 1897 PHE   B CD1 1 
ATOM   1724 C CD2 . PHE   B 1 104 ? 18.202  5.575   37.709 1.00 67.38 ? 1897 PHE   B CD2 1 
ATOM   1725 C CE1 . PHE   B 1 104 ? 20.898  5.122   38.110 1.00 77.80 ? 1897 PHE   B CE1 1 
ATOM   1726 C CE2 . PHE   B 1 104 ? 18.638  4.325   38.107 1.00 68.10 ? 1897 PHE   B CE2 1 
ATOM   1727 C CZ  . PHE   B 1 104 ? 19.987  4.101   38.304 1.00 72.54 ? 1897 PHE   B CZ  1 
ATOM   1728 N N   . TYR   B 1 105 ? 17.690  10.653  37.130 1.00 69.12 ? 1898 TYR   B N   1 
ATOM   1729 C CA  . TYR   B 1 105 ? 16.980  11.778  36.540 1.00 70.72 ? 1898 TYR   B CA  1 
ATOM   1730 C C   . TYR   B 1 105 ? 17.255  13.072  37.302 1.00 71.87 ? 1898 TYR   B C   1 
ATOM   1731 O O   . TYR   B 1 105 ? 17.973  13.950  36.820 1.00 79.15 ? 1898 TYR   B O   1 
ATOM   1732 C CB  . TYR   B 1 105 ? 15.474  11.487  36.515 1.00 66.02 ? 1898 TYR   B CB  1 
ATOM   1733 C CG  . TYR   B 1 105 ? 15.117  10.078  36.080 1.00 56.33 ? 1898 TYR   B CG  1 
ATOM   1734 C CD1 . TYR   B 1 105 ? 14.799  9.795   34.754 1.00 52.45 ? 1898 TYR   B CD1 1 
ATOM   1735 C CD2 . TYR   B 1 105 ? 15.097  9.032   36.995 1.00 49.52 ? 1898 TYR   B CD2 1 
ATOM   1736 C CE1 . TYR   B 1 105 ? 14.467  8.513   34.356 1.00 48.75 ? 1898 TYR   B CE1 1 
ATOM   1737 C CE2 . TYR   B 1 105 ? 14.772  7.745   36.604 1.00 49.31 ? 1898 TYR   B CE2 1 
ATOM   1738 C CZ  . TYR   B 1 105 ? 14.457  7.494   35.283 1.00 46.20 ? 1898 TYR   B CZ  1 
ATOM   1739 O OH  . TYR   B 1 105 ? 14.129  6.217   34.899 1.00 52.97 ? 1898 TYR   B OH  1 
HETATM 1740 C C01 . A1H98 C 2 .   ? -0.561  -16.959 14.280 1.00 35.87 ? 1901 A1H98 A C01 1 
HETATM 1741 C C02 . A1H98 C 2 .   ? 0.369   -17.423 15.408 1.00 35.85 ? 1901 A1H98 A C02 1 
HETATM 1742 C C03 . A1H98 C 2 .   ? -0.096  -16.930 16.783 1.00 30.88 ? 1901 A1H98 A C03 1 
HETATM 1743 C C05 . A1H98 C 2 .   ? -1.261  -16.550 18.566 1.00 23.38 ? 1901 A1H98 A C05 1 
HETATM 1744 C C06 . A1H98 C 2 .   ? -2.386  -16.541 19.626 1.00 17.59 ? 1901 A1H98 A C06 1 
HETATM 1745 C C08 . A1H98 C 2 .   ? -2.902  -14.422 19.236 1.00 25.61 ? 1901 A1H98 A C08 1 
HETATM 1746 C C09 . A1H98 C 2 .   ? -3.983  -13.477 18.696 1.00 24.26 ? 1901 A1H98 A C09 1 
HETATM 1747 C C11 . A1H98 C 2 .   ? -5.097  -15.254 17.721 1.00 22.41 ? 1901 A1H98 A C11 1 
HETATM 1748 C C12 . A1H98 C 2 .   ? -4.023  -16.226 18.210 1.00 30.76 ? 1901 A1H98 A C12 1 
HETATM 1749 C C13 . A1H98 C 2 .   ? -4.425  -13.314 16.176 1.00 26.10 ? 1901 A1H98 A C13 1 
HETATM 1750 C C15 . A1H98 C 2 .   ? -3.723  -11.925 16.161 1.00 21.50 ? 1901 A1H98 A C15 1 
HETATM 1751 C C17 . A1H98 C 2 .   ? -3.270  -9.840  16.645 1.00 16.75 ? 1901 A1H98 A C17 1 
HETATM 1752 C C18 . A1H98 C 2 .   ? -3.350  -8.441  17.265 1.00 14.69 ? 1901 A1H98 A C18 1 
HETATM 1753 C C19 . A1H98 C 2 .   ? -2.324  -10.269 15.741 1.00 13.78 ? 1901 A1H98 A C19 1 
HETATM 1754 C C20 . A1H98 C 2 .   ? -1.178  -9.407  15.201 1.00 18.29 ? 1901 A1H98 A C20 1 
HETATM 1755 C C22 . A1H98 C 2 .   ? 0.000   -10.077 14.481 1.00 23.66 ? 1901 A1H98 A C22 1 
HETATM 1756 C C23 . A1H98 C 2 .   ? -2.595  -11.578 15.434 1.00 21.41 ? 1901 A1H98 A C23 1 
HETATM 1757 C C24 . A1H98 C 2 .   ? -1.826  -12.493 14.470 1.00 27.59 ? 1901 A1H98 A C24 1 
HETATM 1758 C C25 . A1H98 C 2 .   ? -1.432  -13.820 15.103 1.00 30.27 ? 1901 A1H98 A C25 1 
HETATM 1759 N N04 . A1H98 C 2 .   ? -1.267  -17.187 17.378 1.00 29.68 ? 1901 A1H98 A N04 1 
HETATM 1760 N N07 . A1H98 C 2 .   ? -3.317  -15.750 19.312 1.00 29.50 ? 1901 A1H98 A N07 1 
HETATM 1761 N N10 . A1H98 C 2 .   ? -4.517  -13.994 17.489 1.00 25.47 ? 1901 A1H98 A N10 1 
HETATM 1762 N N16 . A1H98 C 2 .   ? -4.099  -10.871 16.881 1.00 20.48 ? 1901 A1H98 A N16 1 
HETATM 1763 N N26 . A1H98 C 2 .   ? -0.102  -15.931 18.679 1.00 25.11 ? 1901 A1H98 A N26 1 
HETATM 1764 O O14 . A1H98 C 2 .   ? -4.867  -13.800 15.205 1.00 27.02 ? 1901 A1H98 A O14 1 
HETATM 1765 O O21 . A1H98 C 2 .   ? -1.206  -8.242  15.357 1.00 23.08 ? 1901 A1H98 A O21 1 
HETATM 1766 O O27 . A1H98 C 2 .   ? 0.604   -16.167 17.581 1.00 24.30 ? 1901 A1H98 A O27 1 
HETATM 1767 C C01 . A1H98 D 2 .   ? -0.773  -13.570 56.171 1.00 39.03 ? 1901 A1H98 B C01 1 
HETATM 1768 C C02 . A1H98 D 2 .   ? 0.234   -14.510 55.498 1.00 32.06 ? 1901 A1H98 B C02 1 
HETATM 1769 C C03 . A1H98 D 2 .   ? 0.608   -14.008 54.095 1.00 30.60 ? 1901 A1H98 B C03 1 
HETATM 1770 C C05 . A1H98 D 2 .   ? 1.712   -13.632 52.252 1.00 30.87 ? 1901 A1H98 B C05 1 
HETATM 1771 C C06 . A1H98 D 2 .   ? 2.823   -13.656 51.170 1.00 27.43 ? 1901 A1H98 B C06 1 
HETATM 1772 C C08 . A1H98 D 2 .   ? 4.482   -13.150 52.554 1.00 27.65 ? 1901 A1H98 B C08 1 
HETATM 1773 C C09 . A1H98 D 2 .   ? 5.546   -12.106 52.903 1.00 29.95 ? 1901 A1H98 B C09 1 
HETATM 1774 C C11 . A1H98 D 2 .   ? 4.484   -10.514 51.599 1.00 27.35 ? 1901 A1H98 B C11 1 
HETATM 1775 C C12 . A1H98 D 2 .   ? 3.343   -11.498 51.261 1.00 22.08 ? 1901 A1H98 B C12 1 
HETATM 1776 C C13 . A1H98 D 2 .   ? 4.752   -9.965  54.103 1.00 23.01 ? 1901 A1H98 B C13 1 
HETATM 1777 C C15 . A1H98 D 2 .   ? 4.012   -8.607  53.909 1.00 18.83 ? 1901 A1H98 B C15 1 
HETATM 1778 C C17 . A1H98 D 2 .   ? 3.462   -6.604  53.230 1.00 16.95 ? 1901 A1H98 B C17 1 
HETATM 1779 C C18 . A1H98 D 2 .   ? 3.507   -5.277  52.464 1.00 16.63 ? 1901 A1H98 B C18 1 
HETATM 1780 C C19 . A1H98 D 2 .   ? 2.479   -6.988  54.136 1.00 16.99 ? 1901 A1H98 B C19 1 
HETATM 1781 C C20 . A1H98 D 2 .   ? 1.265   -6.114  54.541 1.00 21.63 ? 1901 A1H98 B C20 1 
HETATM 1782 C C22 . A1H98 D 2 .   ? 0.093   -6.698  55.358 1.00 29.01 ? 1901 A1H98 B C22 1 
HETATM 1783 C C23 . A1H98 D 2 .   ? 2.834   -8.258  54.576 1.00 17.20 ? 1901 A1H98 B C23 1 
HETATM 1784 C C24 . A1H98 D 2 .   ? 2.158   -9.201  55.604 1.00 18.74 ? 1901 A1H98 B C24 1 
HETATM 1785 C C25 . A1H98 D 2 .   ? 1.609   -10.511 55.040 1.00 24.78 ? 1901 A1H98 B C25 1 
HETATM 1786 N N04 . A1H98 D 2 .   ? 1.754   -14.255 53.459 1.00 30.70 ? 1901 A1H98 B N04 1 
HETATM 1787 N N07 . A1H98 D 2 .   ? 3.758   -12.831 51.387 1.00 25.09 ? 1901 A1H98 B N07 1 
HETATM 1788 N N10 . A1H98 D 2 .   ? 4.940   -10.827 52.909 1.00 31.62 ? 1901 A1H98 B N10 1 
HETATM 1789 N N16 . A1H98 D 2 .   ? 4.370   -7.598  53.114 1.00 18.57 ? 1901 A1H98 B N16 1 
HETATM 1790 N N26 . A1H98 D 2 .   ? 0.536   -13.020 52.160 1.00 25.83 ? 1901 A1H98 B N26 1 
HETATM 1791 O O14 . A1H98 D 2 .   ? 5.118   -10.336 55.170 1.00 27.26 ? 1901 A1H98 B O14 1 
HETATM 1792 O O21 . A1H98 D 2 .   ? 1.174   -4.969  54.226 1.00 20.42 ? 1901 A1H98 B O21 1 
HETATM 1793 O O27 . A1H98 D 2 .   ? -0.135  -13.252 53.301 1.00 33.55 ? 1901 A1H98 B O27 1 
HETATM 1794 O O   . HOH   E 3 .   ? 9.941   -17.869 16.277 1.00 44.59 ? 2001 HOH   A O   1 
HETATM 1795 O O   . HOH   E 3 .   ? -11.343 -7.862  36.494 1.00 37.23 ? 2002 HOH   A O   1 
HETATM 1796 O O   . HOH   E 3 .   ? -0.898  3.536   21.907 1.00 42.87 ? 2003 HOH   A O   1 
HETATM 1797 O O   . HOH   E 3 .   ? -1.767  -16.588 23.756 1.00 32.53 ? 2004 HOH   A O   1 
HETATM 1798 O O   . HOH   E 3 .   ? 0.011   -16.130 22.176 1.00 39.93 ? 2005 HOH   A O   1 
HETATM 1799 O O   . HOH   E 3 .   ? -2.114  1.261   37.800 1.00 27.00 ? 2006 HOH   A O   1 
HETATM 1800 O O   . HOH   E 3 .   ? 0.734   -5.412  35.402 1.00 60.94 ? 2007 HOH   A O   1 
HETATM 1801 O O   . HOH   E 3 .   ? 2.487   -6.486  27.544 1.00 25.14 ? 2008 HOH   A O   1 
HETATM 1802 O O   . HOH   E 3 .   ? 10.996  -14.868 10.656 1.00 38.62 ? 2009 HOH   A O   1 
HETATM 1803 O O   . HOH   E 3 .   ? -12.498 10.056  35.185 1.00 27.79 ? 2010 HOH   A O   1 
HETATM 1804 O O   . HOH   E 3 .   ? -15.297 2.804   42.887 1.00 48.43 ? 2011 HOH   A O   1 
HETATM 1805 O O   . HOH   E 3 .   ? -3.040  -7.333  20.762 1.00 18.55 ? 2012 HOH   A O   1 
HETATM 1806 O O   . HOH   E 3 .   ? -0.473  1.399   29.112 1.00 30.02 ? 2013 HOH   A O   1 
HETATM 1807 O O   . HOH   E 3 .   ? -21.149 -9.202  13.750 1.00 46.85 ? 2014 HOH   A O   1 
HETATM 1808 O O   . HOH   E 3 .   ? -10.108 -11.283 28.958 1.00 27.73 ? 2015 HOH   A O   1 
HETATM 1809 O O   . HOH   E 3 .   ? 6.692   -17.124 23.236 1.00 50.16 ? 2016 HOH   A O   1 
HETATM 1810 O O   . HOH   E 3 .   ? -0.149  -6.440  21.039 1.00 19.39 ? 2017 HOH   A O   1 
HETATM 1811 O O   . HOH   E 3 .   ? -3.077  -12.736 29.512 1.00 34.19 ? 2018 HOH   A O   1 
HETATM 1812 O O   . HOH   E 3 .   ? 8.623   -11.867 16.722 1.00 28.41 ? 2019 HOH   A O   1 
HETATM 1813 O O   . HOH   E 3 .   ? -7.203  -13.692 20.218 1.00 27.65 ? 2020 HOH   A O   1 
HETATM 1814 O O   . HOH   E 3 .   ? -3.910  -10.213 20.546 1.00 18.15 ? 2021 HOH   A O   1 
HETATM 1815 O O   . HOH   E 3 .   ? -2.112  0.560   9.295  1.00 32.44 ? 2022 HOH   A O   1 
HETATM 1816 O O   . HOH   E 3 .   ? -22.761 -3.993  29.270 1.00 36.20 ? 2023 HOH   A O   1 
HETATM 1817 O O   . HOH   E 3 .   ? -19.544 -6.818  32.989 1.00 45.53 ? 2024 HOH   A O   1 
HETATM 1818 O O   . HOH   E 3 .   ? -7.960  6.336   19.630 1.00 35.99 ? 2025 HOH   A O   1 
HETATM 1819 O O   . HOH   E 3 .   ? -1.894  -8.237  33.190 1.00 20.89 ? 2026 HOH   A O   1 
HETATM 1820 O O   . HOH   E 3 .   ? -21.301 -10.877 26.720 1.00 35.00 ? 2027 HOH   A O   1 
HETATM 1821 O O   . HOH   E 3 .   ? -0.817  4.259   39.422 1.00 36.54 ? 2028 HOH   A O   1 
HETATM 1822 O O   . HOH   E 3 .   ? 9.486   -3.539  25.636 1.00 36.51 ? 2029 HOH   A O   1 
HETATM 1823 O O   . HOH   E 3 .   ? 2.820   -10.137 22.702 1.00 25.79 ? 2030 HOH   A O   1 
HETATM 1824 O O   . HOH   E 3 .   ? 2.573   -2.996  26.644 1.00 31.71 ? 2031 HOH   A O   1 
HETATM 1825 O O   . HOH   E 3 .   ? -5.057  -14.127 12.554 1.00 31.96 ? 2032 HOH   A O   1 
HETATM 1826 O O   . HOH   E 3 .   ? 2.401   -16.371 11.909 1.00 29.21 ? 2033 HOH   A O   1 
HETATM 1827 O O   . HOH   E 3 .   ? -2.439  -5.098  41.691 1.00 24.02 ? 2034 HOH   A O   1 
HETATM 1828 O O   . HOH   E 3 .   ? 2.407   -20.732 21.833 1.00 35.15 ? 2035 HOH   A O   1 
HETATM 1829 O O   . HOH   E 3 .   ? -6.210  10.363  36.044 1.00 40.43 ? 2036 HOH   A O   1 
HETATM 1830 O O   . HOH   E 3 .   ? -2.850  -5.554  18.959 1.00 17.87 ? 2037 HOH   A O   1 
HETATM 1831 O O   . HOH   E 3 .   ? -0.877  -6.250  17.224 1.00 15.10 ? 2038 HOH   A O   1 
HETATM 1832 O O   . HOH   E 3 .   ? 4.055   -1.100  20.952 1.00 20.55 ? 2039 HOH   A O   1 
HETATM 1833 O O   . HOH   E 3 .   ? -6.427  5.149   14.147 1.00 34.80 ? 2040 HOH   A O   1 
HETATM 1834 O O   . HOH   E 3 .   ? 7.227   2.924   24.689 1.00 32.45 ? 2041 HOH   A O   1 
HETATM 1835 O O   . HOH   E 3 .   ? -9.644  9.532   36.623 1.00 28.00 ? 2042 HOH   A O   1 
HETATM 1836 O O   . HOH   E 3 .   ? -7.026  -12.627 31.835 1.00 30.19 ? 2043 HOH   A O   1 
HETATM 1837 O O   . HOH   E 3 .   ? -15.678 -12.081 21.099 1.00 34.45 ? 2044 HOH   A O   1 
HETATM 1838 O O   . HOH   E 3 .   ? -20.303 -6.181  22.964 1.00 27.74 ? 2045 HOH   A O   1 
HETATM 1839 O O   . HOH   E 3 .   ? -7.878  -1.436  38.883 1.00 23.71 ? 2046 HOH   A O   1 
HETATM 1840 O O   . HOH   E 3 .   ? -11.673 3.337   14.297 1.00 25.62 ? 2047 HOH   A O   1 
HETATM 1841 O O   . HOH   E 3 .   ? -1.651  1.756   31.541 1.00 21.10 ? 2048 HOH   A O   1 
HETATM 1842 O O   . HOH   E 3 .   ? -7.464  1.378   14.502 1.00 32.12 ? 2049 HOH   A O   1 
HETATM 1843 O O   . HOH   E 3 .   ? -3.367  6.460   21.032 1.00 32.31 ? 2050 HOH   A O   1 
HETATM 1844 O O   . HOH   E 3 .   ? -4.539  -1.609  10.206 1.00 23.02 ? 2051 HOH   A O   1 
HETATM 1845 O O   . HOH   E 3 .   ? -12.099 -9.084  10.590 1.00 34.62 ? 2052 HOH   A O   1 
HETATM 1846 O O   . HOH   E 3 .   ? -6.311  -1.102  15.056 1.00 20.98 ? 2053 HOH   A O   1 
HETATM 1847 O O   . HOH   E 3 .   ? 1.946   0.982   18.896 1.00 42.85 ? 2054 HOH   A O   1 
HETATM 1848 O O   . HOH   E 3 .   ? -12.960 3.670   40.683 1.00 49.37 ? 2055 HOH   A O   1 
HETATM 1849 O O   . HOH   E 3 .   ? 4.097   1.787   22.167 1.00 35.46 ? 2056 HOH   A O   1 
HETATM 1850 O O   . HOH   E 3 .   ? -15.789 -13.228 15.125 1.00 37.63 ? 2057 HOH   A O   1 
HETATM 1851 O O   . HOH   E 3 .   ? 0.048   -3.689  37.238 1.00 29.63 ? 2058 HOH   A O   1 
HETATM 1852 O O   . HOH   E 3 .   ? -0.346  -8.752  24.954 1.00 16.82 ? 2059 HOH   A O   1 
HETATM 1853 O O   . HOH   E 3 .   ? -19.491 2.454   18.094 1.00 37.40 ? 2060 HOH   A O   1 
HETATM 1854 O O   . HOH   E 3 .   ? 9.389   -10.373 9.424  1.00 46.08 ? 2061 HOH   A O   1 
HETATM 1855 O O   . HOH   E 3 .   ? -2.038  -9.199  9.017  1.00 27.17 ? 2062 HOH   A O   1 
HETATM 1856 O O   . HOH   E 3 .   ? -10.457 7.290   37.196 1.00 29.33 ? 2063 HOH   A O   1 
HETATM 1857 O O   . HOH   E 3 .   ? -9.326  11.814  30.428 1.00 30.29 ? 2064 HOH   A O   1 
HETATM 1858 O O   . HOH   E 3 .   ? -9.374  -16.022 18.746 1.00 36.71 ? 2065 HOH   A O   1 
HETATM 1859 O O   . HOH   E 3 .   ? -5.798  -1.936  12.425 1.00 19.16 ? 2066 HOH   A O   1 
HETATM 1860 O O   . HOH   E 3 .   ? -3.956  -4.173  -0.220 1.00 42.71 ? 2067 HOH   A O   1 
HETATM 1861 O O   . HOH   E 3 .   ? -4.930  -10.419 9.392  1.00 30.00 ? 2068 HOH   A O   1 
HETATM 1862 O O   . HOH   E 3 .   ? 0.850   -10.523 28.852 1.00 23.51 ? 2069 HOH   A O   1 
HETATM 1863 O O   . HOH   E 3 .   ? -20.646 -12.450 22.836 1.00 51.31 ? 2070 HOH   A O   1 
HETATM 1864 O O   . HOH   E 3 .   ? 2.938   1.097   9.982  1.00 32.88 ? 2071 HOH   A O   1 
HETATM 1865 O O   . HOH   E 3 .   ? -0.599  3.039   15.036 1.00 33.52 ? 2072 HOH   A O   1 
HETATM 1866 O O   . HOH   E 3 .   ? -3.798  7.621   38.611 1.00 38.84 ? 2073 HOH   A O   1 
HETATM 1867 O O   . HOH   E 3 .   ? -9.492  3.924   12.829 1.00 33.72 ? 2074 HOH   A O   1 
HETATM 1868 O O   . HOH   E 3 .   ? -1.474  3.993   24.371 1.00 26.21 ? 2075 HOH   A O   1 
HETATM 1869 O O   . HOH   E 3 .   ? -14.580 -7.777  39.263 1.00 37.73 ? 2076 HOH   A O   1 
HETATM 1870 O O   . HOH   E 3 .   ? -8.243  -16.195 21.332 1.00 42.34 ? 2077 HOH   A O   1 
HETATM 1871 O O   . HOH   E 3 .   ? -15.310 7.102   17.053 1.00 48.49 ? 2078 HOH   A O   1 
HETATM 1872 O O   . HOH   E 3 .   ? 0.035   -9.012  22.517 1.00 22.33 ? 2079 HOH   A O   1 
HETATM 1873 O O   . HOH   E 3 .   ? -6.557  -15.695 26.927 1.00 37.23 ? 2080 HOH   A O   1 
HETATM 1874 O O   . HOH   E 3 .   ? 4.266   -14.982 10.793 1.00 28.23 ? 2081 HOH   A O   1 
HETATM 1875 O O   . HOH   E 3 .   ? -11.611 -13.166 9.654  1.00 42.77 ? 2082 HOH   A O   1 
HETATM 1876 O O   . HOH   E 3 .   ? -10.077 -12.005 26.383 1.00 40.66 ? 2083 HOH   A O   1 
HETATM 1877 O O   . HOH   E 3 .   ? 10.750  -10.151 15.476 1.00 30.62 ? 2084 HOH   A O   1 
HETATM 1878 O O   . HOH   E 3 .   ? 6.250   -0.152  19.289 1.00 35.91 ? 2085 HOH   A O   1 
HETATM 1879 O O   . HOH   E 3 .   ? -6.705  8.173   40.382 1.00 43.52 ? 2086 HOH   A O   1 
HETATM 1880 O O   . HOH   E 3 .   ? -22.787 -8.471  18.212 1.00 45.58 ? 2087 HOH   A O   1 
HETATM 1881 O O   . HOH   E 3 .   ? -0.884  -7.605  7.665  1.00 27.01 ? 2088 HOH   A O   1 
HETATM 1882 O O   . HOH   E 3 .   ? -1.742  -0.659  2.307  1.00 47.36 ? 2089 HOH   A O   1 
HETATM 1883 O O   . HOH   E 3 .   ? -2.486  7.004   31.455 1.00 38.01 ? 2090 HOH   A O   1 
HETATM 1884 O O   . HOH   E 3 .   ? -3.335  -19.887 17.371 1.00 37.35 ? 2091 HOH   A O   1 
HETATM 1885 O O   . HOH   E 3 .   ? 10.668  -13.350 18.379 1.00 34.82 ? 2092 HOH   A O   1 
HETATM 1886 O O   . HOH   E 3 .   ? -20.836 8.441   13.629 1.00 38.44 ? 2093 HOH   A O   1 
HETATM 1887 O O   . HOH   E 3 .   ? -24.370 -4.885  27.762 1.00 41.09 ? 2094 HOH   A O   1 
HETATM 1888 O O   . HOH   E 3 .   ? -22.296 1.753   20.663 1.00 45.88 ? 2095 HOH   A O   1 
HETATM 1889 O O   . HOH   E 3 .   ? -0.883  -10.710 32.745 1.00 32.48 ? 2096 HOH   A O   1 
HETATM 1890 O O   . HOH   E 3 .   ? 5.680   -19.462 24.862 1.00 40.33 ? 2097 HOH   A O   1 
HETATM 1891 O O   . HOH   E 3 .   ? -8.154  -5.983  44.273 1.00 34.27 ? 2098 HOH   A O   1 
HETATM 1892 O O   . HOH   E 3 .   ? 0.178   3.901   25.992 1.00 40.30 ? 2099 HOH   A O   1 
HETATM 1893 O O   . HOH   E 3 .   ? 1.547   3.118   21.058 1.00 37.66 ? 2100 HOH   A O   1 
HETATM 1894 O O   . HOH   E 3 .   ? 1.608   -8.998  26.633 1.00 21.61 ? 2101 HOH   A O   1 
HETATM 1895 O O   . HOH   E 3 .   ? -11.032 -10.256 42.979 1.00 43.99 ? 2102 HOH   A O   1 
HETATM 1896 O O   . HOH   E 3 .   ? -14.858 0.462   42.606 1.00 44.89 ? 2103 HOH   A O   1 
HETATM 1897 O O   . HOH   E 3 .   ? -6.034  -8.219  44.751 1.00 28.38 ? 2104 HOH   A O   1 
HETATM 1898 O O   . HOH   E 3 .   ? 3.201   -13.078 25.447 1.00 36.43 ? 2105 HOH   A O   1 
HETATM 1899 O O   . HOH   E 3 .   ? -20.441 8.848   16.248 1.00 55.18 ? 2106 HOH   A O   1 
HETATM 1900 O O   . HOH   E 3 .   ? 10.098  -1.095  26.611 1.00 41.98 ? 2107 HOH   A O   1 
HETATM 1901 O O   . HOH   E 3 .   ? -0.979  5.569   42.154 1.00 43.13 ? 2108 HOH   A O   1 
HETATM 1902 O O   . HOH   E 3 .   ? -3.531  -20.872 20.120 1.00 40.53 ? 2109 HOH   A O   1 
HETATM 1903 O O   . HOH   E 3 .   ? -6.077  -13.601 36.974 1.00 34.65 ? 2110 HOH   A O   1 
HETATM 1904 O O   . HOH   E 3 .   ? -7.823  -14.008 38.932 1.00 36.92 ? 2111 HOH   A O   1 
HETATM 1905 O O   . HOH   E 3 .   ? -7.301  11.269  38.062 1.00 51.81 ? 2112 HOH   A O   1 
HETATM 1906 O O   . HOH   E 3 .   ? 3.379   -10.258 25.049 1.00 28.12 ? 2113 HOH   A O   1 
HETATM 1907 O O   . HOH   E 3 .   ? 5.460   -9.548  21.829 1.00 35.61 ? 2114 HOH   A O   1 
HETATM 1908 O O   . HOH   E 3 .   ? -7.442  -10.292 44.208 1.00 47.25 ? 2115 HOH   A O   1 
HETATM 1909 O O   . HOH   E 3 .   ? -23.856 3.242   19.842 1.00 38.01 ? 2116 HOH   A O   1 
HETATM 1910 O O   . HOH   E 3 .   ? -24.932 5.812   19.491 1.00 41.71 ? 2117 HOH   A O   1 
HETATM 1911 O O   . HOH   E 3 .   ? -8.766  -13.874 30.938 1.00 35.34 ? 2118 HOH   A O   1 
HETATM 1912 O O   . HOH   E 3 .   ? -1.358  -11.715 41.721 1.00 41.33 ? 2119 HOH   A O   1 
HETATM 1913 O O   . HOH   E 3 .   ? -2.548  -15.850 11.285 1.00 40.99 ? 2120 HOH   A O   1 
HETATM 1914 O O   . HOH   E 3 .   ? 0.160   -14.581 11.554 1.00 42.40 ? 2121 HOH   A O   1 
HETATM 1915 O O   . HOH   E 3 .   ? -4.628  -17.164 29.662 1.00 41.68 ? 2122 HOH   A O   1 
HETATM 1916 O O   . HOH   E 3 .   ? -3.033  -18.461 28.580 1.00 45.25 ? 2123 HOH   A O   1 
HETATM 1917 O O   . HOH   E 3 .   ? -1.400  -16.307 8.358  1.00 55.67 ? 2124 HOH   A O   1 
HETATM 1918 O O   . HOH   F 3 .   ? -9.919  -11.458 47.868 1.00 46.04 ? 2001 HOH   B O   1 
HETATM 1919 O O   . HOH   F 3 .   ? -1.125  -5.503  33.003 1.00 32.56 ? 2002 HOH   B O   1 
HETATM 1920 O O   . HOH   F 3 .   ? -2.685  0.366   61.959 1.00 28.60 ? 2003 HOH   B O   1 
HETATM 1921 O O   . HOH   F 3 .   ? -2.962  -13.098 58.573 1.00 43.34 ? 2004 HOH   B O   1 
HETATM 1922 O O   . HOH   F 3 .   ? -1.370  5.292   51.110 1.00 56.13 ? 2005 HOH   B O   1 
HETATM 1923 O O   . HOH   F 3 .   ? 18.835  14.049  39.966 1.00 44.74 ? 2006 HOH   B O   1 
HETATM 1924 O O   . HOH   F 3 .   ? 8.661   12.766  35.129 1.00 33.81 ? 2007 HOH   B O   1 
HETATM 1925 O O   . HOH   F 3 .   ? 1.175   4.376   58.904 1.00 36.97 ? 2008 HOH   B O   1 
HETATM 1926 O O   . HOH   F 3 .   ? -0.696  -3.682  31.585 1.00 38.77 ? 2009 HOH   B O   1 
HETATM 1927 O O   . HOH   F 3 .   ? 4.477   1.924   69.255 1.00 48.42 ? 2010 HOH   B O   1 
HETATM 1928 O O   . HOH   F 3 .   ? 8.485   0.568   27.024 1.00 24.78 ? 2011 HOH   B O   1 
HETATM 1929 O O   . HOH   F 3 .   ? 12.603  -9.861  33.901 1.00 37.68 ? 2012 HOH   B O   1 
HETATM 1930 O O   . HOH   F 3 .   ? 20.357  -8.718  50.482 1.00 34.58 ? 2013 HOH   B O   1 
HETATM 1931 O O   . HOH   F 3 .   ? 0.822   3.817   28.855 1.00 41.79 ? 2014 HOH   B O   1 
HETATM 1932 O O   . HOH   F 3 .   ? 17.485  -1.904  28.481 1.00 42.35 ? 2015 HOH   B O   1 
HETATM 1933 O O   . HOH   F 3 .   ? 5.488   -10.415 57.603 1.00 36.74 ? 2016 HOH   B O   1 
HETATM 1934 O O   . HOH   F 3 .   ? -1.914  3.422   48.709 1.00 36.08 ? 2017 HOH   B O   1 
HETATM 1935 O O   . HOH   F 3 .   ? 23.691  5.656   45.747 1.00 71.23 ? 2018 HOH   B O   1 
HETATM 1936 O O   . HOH   F 3 .   ? 10.104  -1.188  65.871 1.00 39.49 ? 2019 HOH   B O   1 
HETATM 1937 O O   . HOH   F 3 .   ? 19.177  1.224   51.779 1.00 32.04 ? 2020 HOH   B O   1 
HETATM 1938 O O   . HOH   F 3 .   ? 1.134   -11.123 31.231 1.00 34.87 ? 2021 HOH   B O   1 
HETATM 1939 O O   . HOH   F 3 .   ? 0.328   2.171   39.448 1.00 34.68 ? 2022 HOH   B O   1 
HETATM 1940 O O   . HOH   F 3 .   ? -2.223  -8.127  47.177 1.00 19.62 ? 2023 HOH   B O   1 
HETATM 1941 O O   . HOH   F 3 .   ? 2.184   -7.951  36.294 1.00 30.11 ? 2024 HOH   B O   1 
HETATM 1942 O O   . HOH   F 3 .   ? 10.210  9.804   43.196 1.00 46.79 ? 2025 HOH   B O   1 
HETATM 1943 O O   . HOH   F 3 .   ? 15.876  -9.440  53.319 1.00 33.92 ? 2026 HOH   B O   1 
HETATM 1944 O O   . HOH   F 3 .   ? -15.602 -7.727  52.519 1.00 46.18 ? 2027 HOH   B O   1 
HETATM 1945 O O   . HOH   F 3 .   ? 16.564  -9.156  48.702 1.00 35.80 ? 2028 HOH   B O   1 
HETATM 1946 O O   . HOH   F 3 .   ? 3.571   -4.786  48.582 1.00 22.02 ? 2029 HOH   B O   1 
HETATM 1947 O O   . HOH   F 3 .   ? 0.418   -3.758  48.280 1.00 18.23 ? 2030 HOH   B O   1 
HETATM 1948 O O   . HOH   F 3 .   ? 3.559   8.912   47.101 1.00 38.87 ? 2031 HOH   B O   1 
HETATM 1949 O O   . HOH   F 3 .   ? 5.535   9.516   55.665 1.00 55.71 ? 2032 HOH   B O   1 
HETATM 1950 O O   . HOH   F 3 .   ? 13.470  9.845   50.829 1.00 42.84 ? 2033 HOH   B O   1 
HETATM 1951 O O   . HOH   F 3 .   ? 2.048   1.141   30.224 1.00 32.95 ? 2034 HOH   B O   1 
HETATM 1952 O O   . HOH   F 3 .   ? 20.310  -3.829  46.512 1.00 37.62 ? 2035 HOH   B O   1 
HETATM 1953 O O   . HOH   F 3 .   ? 4.354   2.517   58.510 1.00 29.32 ? 2036 HOH   B O   1 
HETATM 1954 O O   . HOH   F 3 .   ? -9.587  -1.956  43.507 1.00 33.55 ? 2037 HOH   B O   1 
HETATM 1955 O O   . HOH   F 3 .   ? 20.229  8.175   54.041 1.00 29.86 ? 2038 HOH   B O   1 
HETATM 1956 O O   . HOH   F 3 .   ? -2.122  -1.628  41.643 1.00 20.13 ? 2039 HOH   B O   1 
HETATM 1957 O O   . HOH   F 3 .   ? 1.349   -1.240  28.868 1.00 25.13 ? 2040 HOH   B O   1 
HETATM 1958 O O   . HOH   F 3 .   ? 0.662   5.871   45.677 1.00 30.79 ? 2041 HOH   B O   1 
HETATM 1959 O O   . HOH   F 3 .   ? -11.161 1.902   52.473 1.00 39.43 ? 2042 HOH   B O   1 
HETATM 1960 O O   . HOH   F 3 .   ? -8.398  -8.478  52.529 1.00 31.04 ? 2043 HOH   B O   1 
HETATM 1961 O O   . HOH   F 3 .   ? 0.982   -3.248  52.143 1.00 17.35 ? 2044 HOH   B O   1 
HETATM 1962 O O   . HOH   F 3 .   ? 0.065   2.544   34.049 1.00 27.08 ? 2045 HOH   B O   1 
HETATM 1963 O O   . HOH   F 3 .   ? -6.892  4.674   42.999 1.00 35.49 ? 2046 HOH   B O   1 
HETATM 1964 O O   . HOH   F 3 .   ? 9.227   11.545  49.798 1.00 48.01 ? 2047 HOH   B O   1 
HETATM 1965 O O   . HOH   F 3 .   ? 1.154   -2.425  61.995 1.00 29.53 ? 2048 HOH   B O   1 
HETATM 1966 O O   . HOH   F 3 .   ? 16.319  -6.080  36.107 1.00 24.45 ? 2049 HOH   B O   1 
HETATM 1967 O O   . HOH   F 3 .   ? 3.337   6.446   58.742 1.00 37.27 ? 2050 HOH   B O   1 
HETATM 1968 O O   . HOH   F 3 .   ? -4.038  1.193   47.398 1.00 26.05 ? 2051 HOH   B O   1 
HETATM 1969 O O   . HOH   F 3 .   ? 3.887   -7.581  49.387 1.00 25.28 ? 2052 HOH   B O   1 
HETATM 1970 O O   . HOH   F 3 .   ? 8.224   -13.443 49.152 1.00 33.26 ? 2053 HOH   B O   1 
HETATM 1971 O O   . HOH   F 3 .   ? 1.393   -14.132 47.530 1.00 38.37 ? 2054 HOH   B O   1 
HETATM 1972 O O   . HOH   F 3 .   ? 12.162  -4.287  59.132 1.00 31.36 ? 2055 HOH   B O   1 
HETATM 1973 O O   . HOH   F 3 .   ? -2.796  3.839   58.907 1.00 35.47 ? 2056 HOH   B O   1 
HETATM 1974 O O   . HOH   F 3 .   ? 11.008  6.581   53.211 1.00 47.32 ? 2057 HOH   B O   1 
HETATM 1975 O O   . HOH   F 3 .   ? -13.369 -7.620  54.983 1.00 35.22 ? 2058 HOH   B O   1 
HETATM 1976 O O   . HOH   F 3 .   ? 17.292  3.217   52.366 1.00 29.56 ? 2059 HOH   B O   1 
HETATM 1977 O O   . HOH   F 3 .   ? 10.292  -9.970  41.321 1.00 24.80 ? 2060 HOH   B O   1 
HETATM 1978 O O   . HOH   F 3 .   ? 5.886   1.953   56.013 1.00 24.89 ? 2061 HOH   B O   1 
HETATM 1979 O O   . HOH   F 3 .   ? 17.010  -8.650  41.695 1.00 21.52 ? 2062 HOH   B O   1 
HETATM 1980 O O   . HOH   F 3 .   ? 7.642   -10.837 49.947 1.00 21.60 ? 2063 HOH   B O   1 
HETATM 1981 O O   . HOH   F 3 .   ? 7.222   -11.880 38.514 1.00 24.70 ? 2064 HOH   B O   1 
HETATM 1982 O O   . HOH   F 3 .   ? -8.652  1.597   41.281 1.00 29.07 ? 2065 HOH   B O   1 
HETATM 1983 O O   . HOH   F 3 .   ? 6.196   2.263   53.478 1.00 27.67 ? 2066 HOH   B O   1 
HETATM 1984 O O   . HOH   F 3 .   ? -8.693  -11.821 54.953 1.00 28.42 ? 2067 HOH   B O   1 
HETATM 1985 O O   . HOH   F 3 .   ? -10.470 -9.474  54.930 1.00 39.75 ? 2068 HOH   B O   1 
HETATM 1986 O O   . HOH   F 3 .   ? 2.974   -2.800  50.259 1.00 22.00 ? 2069 HOH   B O   1 
HETATM 1987 O O   . HOH   F 3 .   ? -10.385 -3.532  47.098 1.00 45.21 ? 2070 HOH   B O   1 
HETATM 1988 O O   . HOH   F 3 .   ? 0.129   -1.302  37.761 1.00 21.62 ? 2071 HOH   B O   1 
HETATM 1989 O O   . HOH   F 3 .   ? 7.209   4.677   53.586 1.00 28.64 ? 2072 HOH   B O   1 
HETATM 1990 O O   . HOH   F 3 .   ? 0.783   -6.690  44.596 1.00 25.49 ? 2073 HOH   B O   1 
HETATM 1991 O O   . HOH   F 3 .   ? -10.887 -13.307 51.764 1.00 34.37 ? 2074 HOH   B O   1 
HETATM 1992 O O   . HOH   F 3 .   ? 0.463   -1.650  31.059 1.00 35.09 ? 2075 HOH   B O   1 
HETATM 1993 O O   . HOH   F 3 .   ? 10.220  -11.195 43.507 1.00 30.03 ? 2076 HOH   B O   1 
HETATM 1994 O O   . HOH   F 3 .   ? 8.899   7.040   54.513 1.00 26.74 ? 2077 HOH   B O   1 
HETATM 1995 O O   . HOH   F 3 .   ? 0.397   -6.756  47.387 1.00 22.57 ? 2078 HOH   B O   1 
HETATM 1996 O O   . HOH   F 3 .   ? 20.774  -4.184  51.232 1.00 31.50 ? 2079 HOH   B O   1 
HETATM 1997 O O   . HOH   F 3 .   ? 1.556   5.717   43.145 1.00 32.85 ? 2080 HOH   B O   1 
HETATM 1998 O O   . HOH   F 3 .   ? 8.182   -2.356  29.781 1.00 31.57 ? 2081 HOH   B O   1 
HETATM 1999 O O   . HOH   F 3 .   ? 1.815   2.565   36.941 1.00 27.87 ? 2082 HOH   B O   1 
HETATM 2000 O O   . HOH   F 3 .   ? -17.049 -6.861  57.299 1.00 45.87 ? 2083 HOH   B O   1 
HETATM 2001 O O   . HOH   F 3 .   ? 2.962   7.181   30.696 1.00 42.49 ? 2084 HOH   B O   1 
HETATM 2002 O O   . HOH   F 3 .   ? -0.873  -0.132  39.589 1.00 26.89 ? 2085 HOH   B O   1 
HETATM 2003 O O   . HOH   F 3 .   ? -0.294  -9.633  41.238 1.00 34.75 ? 2086 HOH   B O   1 
HETATM 2004 O O   . HOH   F 3 .   ? -8.165  -4.194  45.799 1.00 39.67 ? 2087 HOH   B O   1 
HETATM 2005 O O   . HOH   F 3 .   ? 2.351   4.577   62.640 1.00 35.44 ? 2088 HOH   B O   1 
HETATM 2006 O O   . HOH   F 3 .   ? 16.047  -3.653  58.989 1.00 32.92 ? 2089 HOH   B O   1 
HETATM 2007 O O   . HOH   F 3 .   ? 10.233  -12.217 34.546 1.00 35.89 ? 2090 HOH   B O   1 
HETATM 2008 O O   . HOH   F 3 .   ? -4.262  3.694   45.894 1.00 39.59 ? 2091 HOH   B O   1 
HETATM 2009 O O   . HOH   F 3 .   ? 7.166   -14.118 44.147 1.00 32.10 ? 2092 HOH   B O   1 
HETATM 2010 O O   . HOH   F 3 .   ? 0.544   5.989   53.132 1.00 34.79 ? 2093 HOH   B O   1 
HETATM 2011 O O   . HOH   F 3 .   ? 15.437  9.283   49.750 1.00 29.03 ? 2094 HOH   B O   1 
HETATM 2012 O O   . HOH   F 3 .   ? -5.657  2.450   48.863 1.00 41.96 ? 2095 HOH   B O   1 
HETATM 2013 O O   . HOH   F 3 .   ? -0.262  6.067   30.398 1.00 31.28 ? 2096 HOH   B O   1 
HETATM 2014 O O   . HOH   F 3 .   ? 6.175   -6.350  63.684 1.00 38.61 ? 2097 HOH   B O   1 
HETATM 2015 O O   . HOH   F 3 .   ? 0.470   7.161   51.069 1.00 42.79 ? 2098 HOH   B O   1 
HETATM 2016 O O   . HOH   F 3 .   ? 14.654  -10.048 51.049 1.00 34.53 ? 2099 HOH   B O   1 
HETATM 2017 O O   . HOH   F 3 .   ? 14.168  -4.675  57.208 1.00 35.50 ? 2100 HOH   B O   1 
HETATM 2018 O O   . HOH   F 3 .   ? 15.989  12.238  52.433 1.00 44.91 ? 2101 HOH   B O   1 
HETATM 2019 O O   . HOH   F 3 .   ? -9.511  -14.646 45.382 1.00 39.71 ? 2102 HOH   B O   1 
HETATM 2020 O O   . HOH   F 3 .   ? -10.878 -7.251  53.733 1.00 33.54 ? 2103 HOH   B O   1 
HETATM 2021 O O   . HOH   F 3 .   ? 19.637  -11.580 45.365 1.00 44.22 ? 2104 HOH   B O   1 
HETATM 2022 O O   . HOH   F 3 .   ? 11.859  12.306  37.946 1.00 43.99 ? 2105 HOH   B O   1 
HETATM 2023 O O   . HOH   F 3 .   ? 0.749   -12.018 35.265 1.00 50.02 ? 2106 HOH   B O   1 
HETATM 2024 O O   . HOH   F 3 .   ? -2.070  -13.781 46.600 1.00 33.58 ? 2107 HOH   B O   1 
HETATM 2025 O O   . HOH   F 3 .   ? 18.951  12.156  53.091 1.00 57.59 ? 2108 HOH   B O   1 
HETATM 2026 O O   . HOH   F 3 .   ? -1.016  4.756   32.245 1.00 38.35 ? 2109 HOH   B O   1 
HETATM 2027 O O   . HOH   F 3 .   ? 2.254   7.502   61.031 1.00 40.53 ? 2110 HOH   B O   1 
HETATM 2028 O O   . HOH   F 3 .   ? -8.893  3.440   44.535 1.00 36.62 ? 2111 HOH   B O   1 
HETATM 2029 O O   . HOH   F 3 .   ? 23.448  -4.198  52.389 1.00 54.46 ? 2112 HOH   B O   1 
HETATM 2030 O O   . HOH   F 3 .   ? -12.426 -13.072 48.054 1.00 40.44 ? 2113 HOH   B O   1 
HETATM 2031 O O   . HOH   F 3 .   ? 7.026   7.963   27.055 1.00 38.87 ? 2114 HOH   B O   1 
HETATM 2032 O O   . HOH   F 3 .   ? 1.278   -10.193 37.409 1.00 31.79 ? 2115 HOH   B O   1 
HETATM 2033 O O   . HOH   F 3 .   ? 7.930   -12.265 35.885 1.00 39.20 ? 2116 HOH   B O   1 
HETATM 2034 O O   . HOH   F 3 .   ? 18.448  -11.045 48.223 1.00 36.71 ? 2117 HOH   B O   1 
HETATM 2035 O O   . HOH   F 3 .   ? -1.398  -7.397  42.933 1.00 22.77 ? 2118 HOH   B O   1 
HETATM 2036 O O   . HOH   F 3 .   ? 10.906  -13.273 31.924 1.00 44.33 ? 2119 HOH   B O   1 
HETATM 2037 O O   . HOH   F 3 .   ? 8.556   9.584   27.824 1.00 47.44 ? 2120 HOH   B O   1 
HETATM 2038 O O   . HOH   F 3 .   ? 3.198   -11.992 38.102 1.00 41.66 ? 2121 HOH   B O   1 
HETATM 2039 O O   . HOH   F 3 .   ? -5.105  -7.680  47.467 1.00 35.80 ? 2122 HOH   B O   1 
HETATM 2040 O O   . HOH   F 3 .   ? -2.936  -8.651  44.760 1.00 27.55 ? 2123 HOH   B O   1 
HETATM 2041 O O   . HOH   F 3 .   ? -12.219 -14.853 50.038 1.00 30.22 ? 2124 HOH   B O   1 
HETATM 2042 O O   . HOH   F 3 .   ? 10.382  -14.417 47.000 1.00 41.46 ? 2125 HOH   B O   1 
HETATM 2043 O O   . HOH   F 3 .   ? -1.671  5.250   46.410 1.00 31.13 ? 2126 HOH   B O   1 
HETATM 2044 O O   . HOH   F 3 .   ? 2.744   8.400   41.902 1.00 42.60 ? 2127 HOH   B O   1 
HETATM 2045 O O   . HOH   F 3 .   ? 21.861  -1.445  46.351 1.00 43.65 ? 2128 HOH   B O   1 
HETATM 2046 O O   . HOH   F 3 .   ? 2.123   -12.627 28.662 1.00 46.59 ? 2129 HOH   B O   1 
HETATM 2047 O O   . HOH   F 3 .   ? 4.897   -13.864 38.468 1.00 47.11 ? 2130 HOH   B O   1 
HETATM 2048 O O   . HOH   F 3 .   ? 7.973   -11.174 59.382 1.00 42.22 ? 2131 HOH   B O   1 
HETATM 2049 O O   . HOH   F 3 .   ? 6.989   -9.831  61.826 1.00 44.45 ? 2132 HOH   B 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   . SER A 4   ? 0.6778 0.9752 0.5843 0.1865  0.0869  -0.1757 1797 SER A N   
2    C CA  . SER A 4   ? 0.7011 1.0047 0.6430 0.1990  0.0946  -0.1698 1797 SER A CA  
3    C C   . SER A 4   ? 0.6954 0.9731 0.6595 0.1938  0.0807  -0.1656 1797 SER A C   
4    O O   . SER A 4   ? 0.6230 0.9236 0.6168 0.1918  0.0803  -0.1465 1797 SER A O   
5    C CB  . SER A 4   ? 0.7033 0.9884 0.6410 0.2200  0.1056  -0.1905 1797 SER A CB  
6    O OG  . SER A 4   ? 0.6771 0.9694 0.6500 0.2357  0.1116  -0.1828 1797 SER A OG  
7    N N   . ASP A 5   ? 0.7985 1.0287 0.7486 0.1896  0.0696  -0.1840 1798 ASP A N   
8    C CA  . ASP A 5   ? 0.7266 0.9288 0.6927 0.1818  0.0569  -0.1797 1798 ASP A CA  
9    C C   . ASP A 5   ? 0.6389 0.8660 0.6077 0.1639  0.0488  -0.1617 1798 ASP A C   
10   O O   . ASP A 5   ? 0.4965 0.7302 0.4893 0.1609  0.0449  -0.1462 1798 ASP A O   
11   C CB  . ASP A 5   ? 0.7554 0.9013 0.7054 0.1751  0.0490  -0.2030 1798 ASP A CB  
12   C CG  . ASP A 5   ? 0.8601 0.9678 0.8077 0.1924  0.0597  -0.2191 1798 ASP A CG  
13   O OD1 . ASP A 5   ? 0.8744 1.0029 0.8343 0.2127  0.0719  -0.2123 1798 ASP A OD1 
14   O OD2 . ASP A 5   ? 0.9191 0.9757 0.8533 0.1844  0.0571  -0.2383 1798 ASP A OD2 
15   N N   . LEU A 6   ? 0.6164 0.8571 0.5595 0.1529  0.0464  -0.1622 1799 LEU A N   
16   C CA  . LEU A 6   ? 0.5372 0.7980 0.4785 0.1383  0.0420  -0.1422 1799 LEU A CA  
17   C C   . LEU A 6   ? 0.3493 0.6501 0.3081 0.1376  0.0553  -0.1176 1799 LEU A C   
18   O O   . LEU A 6   ? 0.4430 0.7480 0.4147 0.1225  0.0518  -0.0972 1799 LEU A O   
19   C CB  . LEU A 6   ? 0.5154 0.7806 0.4240 0.1309  0.0359  -0.1445 1799 LEU A CB  
20   C CG  . LEU A 6   ? 0.4578 0.6956 0.3597 0.1198  0.0180  -0.1585 1799 LEU A CG  
21   C CD1 . LEU A 6   ? 0.4591 0.6831 0.3800 0.1094  0.0109  -0.1474 1799 LEU A CD1 
22   C CD2 . LEU A 6   ? 0.5358 0.7420 0.4379 0.1226  0.0151  -0.1869 1799 LEU A CD2 
23   N N   . THR A 7   ? 0.3853 0.7093 0.3473 0.1482  0.0691  -0.1172 1800 THR A N   
24   C CA  . THR A 7   ? 0.4550 0.8186 0.4436 0.1444  0.0817  -0.0962 1800 THR A CA  
25   C C   . THR A 7   ? 0.4001 0.7668 0.4273 0.1421  0.0743  -0.0885 1800 THR A C   
26   O O   . THR A 7   ? 0.4813 0.8704 0.5273 0.1250  0.0752  -0.0692 1800 THR A O   
27   C CB  . THR A 7   ? 0.4020 0.7878 0.3937 0.1595  0.0969  -0.1020 1800 THR A CB  
28   O OG1 . THR A 7   ? 0.4540 0.8454 0.4102 0.1588  0.1056  -0.1031 1800 THR A OG1 
29   C CG2 . THR A 7   ? 0.3550 0.7835 0.3844 0.1545  0.1072  -0.0839 1800 THR A CG2 
30   N N   . PHE A 8   ? 0.3281 0.6684 0.3656 0.1581  0.0666  -0.1027 1801 PHE A N   
31   C CA  . PHE A 8   ? 0.3221 0.6606 0.3911 0.1587  0.0564  -0.0938 1801 PHE A CA  
32   C C   . PHE A 8   ? 0.3048 0.6150 0.3678 0.1332  0.0415  -0.0818 1801 PHE A C   
33   O O   . PHE A 8   ? 0.3529 0.6729 0.4375 0.1204  0.0343  -0.0656 1801 PHE A O   
34   C CB  . PHE A 8   ? 0.3769 0.6749 0.4471 0.1806  0.0512  -0.1080 1801 PHE A CB  
35   C CG  . PHE A 8   ? 0.5044 0.8113 0.5774 0.2018  0.0634  -0.1157 1801 PHE A CG  
36   C CD1 . PHE A 8   ? 0.5559 0.9166 0.6518 0.2040  0.0733  -0.1037 1801 PHE A CD1 
37   C CD2 . PHE A 8   ? 0.5001 0.7599 0.5540 0.2178  0.0662  -0.1361 1801 PHE A CD2 
38   C CE1 . PHE A 8   ? 0.6303 1.0015 0.7306 0.2255  0.0857  -0.1115 1801 PHE A CE1 
39   C CE2 . PHE A 8   ? 0.5993 0.8646 0.6554 0.2388  0.0793  -0.1439 1801 PHE A CE2 
40   C CZ  . PHE A 8   ? 0.6196 0.9426 0.6993 0.2444  0.0889  -0.1315 1801 PHE A CZ  
41   N N   . CYS A 9   ? 0.2708 0.5471 0.3041 0.1249  0.0361  -0.0905 1802 CYS A N   
42   C CA  . CYS A 9   ? 0.2386 0.4865 0.2660 0.1032  0.0230  -0.0797 1802 CYS A CA  
43   C C   . CYS A 9   ? 0.2684 0.5391 0.2977 0.0842  0.0271  -0.0578 1802 CYS A C   
44   O O   . CYS A 9   ? 0.2390 0.4949 0.2765 0.0679  0.0187  -0.0451 1802 CYS A O   
45   C CB  . CYS A 9   ? 0.2512 0.4696 0.2514 0.1007  0.0165  -0.0954 1802 CYS A CB  
46   S SG  . CYS A 9   ? 0.3418 0.5148 0.3408 0.1118  0.0109  -0.1216 1802 CYS A SG  
47   N N   . GLU A 10  ? 0.2714 0.5740 0.2906 0.0854  0.0419  -0.0532 1803 GLU A N   
48   C CA  A GLU A 10  ? 0.2603 0.5793 0.2818 0.0658  0.0504  -0.0312 1803 GLU A CA  
49   C CA  B GLU A 10  ? 0.2594 0.5782 0.2809 0.0658  0.0503  -0.0312 1803 GLU A CA  
50   C C   . GLU A 10  ? 0.2792 0.6195 0.3382 0.0544  0.0492  -0.0219 1803 GLU A C   
51   O O   . GLU A 10  ? 0.2307 0.5583 0.2947 0.0328  0.0446  -0.0091 1803 GLU A O   
52   C CB  A GLU A 10  ? 0.2552 0.6069 0.2598 0.0707  0.0708  -0.0267 1803 GLU A CB  
53   C CB  B GLU A 10  ? 0.2908 0.6416 0.2949 0.0705  0.0705  -0.0266 1803 GLU A CB  
54   C CG  A GLU A 10  ? 0.3882 0.7364 0.3760 0.0514  0.0815  -0.0031 1803 GLU A CG  
55   C CG  B GLU A 10  ? 0.3133 0.6563 0.2810 0.0884  0.0703  -0.0425 1803 GLU A CG  
56   C CD  A GLU A 10  ? 0.3623 0.7111 0.3787 0.0259  0.0823  0.0122  1803 GLU A CD  
57   C CD  B GLU A 10  ? 0.4759 0.8280 0.4076 0.0862  0.0831  -0.0282 1803 GLU A CD  
58   O OE1 A GLU A 10  ? 0.4038 0.7163 0.4074 0.0108  0.0771  0.0238  1803 GLU A OE1 
59   O OE1 B GLU A 10  ? 0.5061 0.8601 0.4404 0.0690  0.0934  -0.0042 1803 GLU A OE1 
60   O OE2 A GLU A 10  ? 0.3988 0.7864 0.4509 0.0215  0.0878  0.0109  1803 GLU A OE2 
61   O OE2 B GLU A 10  ? 0.5144 0.8609 0.4162 0.0990  0.0796  -0.0399 1803 GLU A OE2 
62   N N   . ILE A 11  ? 0.2647 0.6397 0.3498 0.0702  0.0529  -0.0298 1804 ILE A N   
63   C CA  . ILE A 11  ? 0.3034 0.7119 0.4272 0.0620  0.0491  -0.0225 1804 ILE A CA  
64   C C   . ILE A 11  ? 0.2674 0.6403 0.3940 0.0562  0.0282  -0.0213 1804 ILE A C   
65   O O   . ILE A 11  ? 0.2190 0.5989 0.3593 0.0346  0.0218  -0.0117 1804 ILE A O   
66   C CB  . ILE A 11  ? 0.2520 0.7084 0.4037 0.0877  0.0563  -0.0312 1804 ILE A CB  
67   C CG1 . ILE A 11  ? 0.3309 0.8164 0.4779 0.0850  0.0774  -0.0282 1804 ILE A CG1 
68   C CG2 . ILE A 11  ? 0.2420 0.7232 0.4290 0.0830  0.0441  -0.0250 1804 ILE A CG2 
69   C CD1 . ILE A 11  ? 0.2909 0.8034 0.4533 0.0527  0.0866  -0.0116 1804 ILE A CD1 
70   N N   . ILE A 12  ? 0.1871 0.5196 0.2986 0.0734  0.0186  -0.0320 1805 ILE A N   
71   C CA  . ILE A 12  ? 0.2736 0.5706 0.3842 0.0692  0.0017  -0.0294 1805 ILE A CA  
72   C C   . ILE A 12  ? 0.2625 0.5331 0.3578 0.0425  -0.0026 -0.0202 1805 ILE A C   
73   O O   . ILE A 12  ? 0.2814 0.5468 0.3835 0.0290  -0.0124 -0.0132 1805 ILE A O   
74   C CB  . ILE A 12  ? 0.3207 0.5732 0.4154 0.0884  -0.0029 -0.0423 1805 ILE A CB  
75   C CG1 . ILE A 12  ? 0.3015 0.5705 0.4120 0.1180  0.0005  -0.0496 1805 ILE A CG1 
76   C CG2 . ILE A 12  ? 0.3269 0.5358 0.4126 0.0792  -0.0162 -0.0376 1805 ILE A CG2 
77   C CD1 . ILE A 12  ? 0.3922 0.6087 0.4852 0.1355  -0.0001 -0.0638 1805 ILE A CD1 
78   N N   . LEU A 13  ? 0.2407 0.4955 0.3130 0.0365  0.0048  -0.0201 1806 LEU A N   
79   C CA  . LEU A 13  ? 0.2422 0.4686 0.2983 0.0166  0.0025  -0.0106 1806 LEU A CA  
80   C C   . LEU A 13  ? 0.1948 0.4402 0.2627 -0.0056 0.0085  0.0018  1806 LEU A C   
81   O O   . LEU A 13  ? 0.1960 0.4185 0.2607 -0.0224 0.0022  0.0069  1806 LEU A O   
82   C CB  . LEU A 13  ? 0.2485 0.4606 0.2772 0.0205  0.0086  -0.0115 1806 LEU A CB  
83   C CG  . LEU A 13  ? 0.2498 0.4296 0.2598 0.0078  0.0066  -0.0014 1806 LEU A CG  
84   C CD1 . LEU A 13  ? 0.1952 0.3441 0.2054 0.0076  -0.0065 -0.0076 1806 LEU A CD1 
85   C CD2 . LEU A 13  ? 0.2824 0.4611 0.2660 0.0162  0.0127  0.0010  1806 LEU A CD2 
86   N N   . MET A 14  ? 0.2185 0.5057 0.3001 -0.0077 0.0221  0.0052  1807 MET A N   
87   C CA  A MET A 14  ? 0.2513 0.5600 0.3490 -0.0339 0.0301  0.0151  1807 MET A CA  
88   C CA  B MET A 14  ? 0.2508 0.5585 0.3481 -0.0341 0.0300  0.0151  1807 MET A CA  
89   C C   . MET A 14  ? 0.2400 0.5647 0.3636 -0.0437 0.0149  0.0114  1807 MET A C   
90   O O   . MET A 14  ? 0.2125 0.5221 0.3351 -0.0687 0.0117  0.0151  1807 MET A O   
91   C CB  A MET A 14  ? 0.2862 0.6459 0.3998 -0.0335 0.0492  0.0181  1807 MET A CB  
92   C CB  B MET A 14  ? 0.2871 0.6441 0.3991 -0.0349 0.0496  0.0189  1807 MET A CB  
93   C CG  A MET A 14  ? 0.3311 0.7209 0.4688 -0.0651 0.0600  0.0265  1807 MET A CG  
94   C CG  B MET A 14  ? 0.3480 0.7187 0.4714 -0.0683 0.0638  0.0305  1807 MET A CG  
95   S SD  A MET A 14  ? 0.4244 0.8966 0.6012 -0.0615 0.0778  0.0253  1807 MET A SD  
96   S SD  B MET A 14  ? 0.4081 0.8354 0.5460 -0.0724 0.0930  0.0380  1807 MET A SD  
97   C CE  A MET A 14  ? 0.3427 0.8431 0.5460 -0.0294 0.0558  0.0101  1807 MET A CE  
98   C CE  B MET A 14  ? 0.3881 0.8018 0.5353 -0.1177 0.1050  0.0493  1807 MET A CE  
99   N N   . GLU A 15  ? 0.2088 0.5624 0.3526 -0.0221 0.0053  0.0038  1808 GLU A N   
100  C CA  . GLU A 15  ? 0.2071 0.5823 0.3726 -0.0257 -0.0115 0.0019  1808 GLU A CA  
101  C C   . GLU A 15  ? 0.2313 0.5531 0.3720 -0.0323 -0.0257 0.0021  1808 GLU A C   
102  O O   . GLU A 15  ? 0.2417 0.5705 0.3884 -0.0496 -0.0367 0.0020  1808 GLU A O   
103  C CB  . GLU A 15  ? 0.2292 0.6379 0.4150 0.0066  -0.0179 -0.0032 1808 GLU A CB  
104  C CG  . GLU A 15  ? 0.3087 0.7776 0.5226 0.0168  -0.0031 -0.0049 1808 GLU A CG  
105  C CD  . GLU A 15  ? 0.3532 0.8351 0.5788 0.0510  -0.0094 -0.0093 1808 GLU A CD  
106  O OE1 . GLU A 15  ? 0.3548 0.8061 0.5694 0.0679  -0.0237 -0.0099 1808 GLU A OE1 
107  O OE2 . GLU A 15  ? 0.2998 0.8192 0.5439 0.0612  0.0010  -0.0111 1808 GLU A OE2 
108  N N   . MET A 16  ? 0.2296 0.5024 0.3433 -0.0190 -0.0256 0.0007  1809 MET A N   
109  C CA  . MET A 16  ? 0.2403 0.4642 0.3310 -0.0253 -0.0350 0.0013  1809 MET A CA  
110  C C   . MET A 16  ? 0.2813 0.4834 0.3588 -0.0524 -0.0296 0.0055  1809 MET A C   
111  O O   . MET A 16  ? 0.2521 0.4405 0.3236 -0.0669 -0.0379 0.0048  1809 MET A O   
112  C CB  . MET A 16  ? 0.1870 0.3715 0.2578 -0.0083 -0.0337 -0.0026 1809 MET A CB  
113  C CG  . MET A 16  ? 0.2073 0.3908 0.2839 0.0159  -0.0400 -0.0076 1809 MET A CG  
114  S SD  . MET A 16  ? 0.2606 0.3882 0.3149 0.0244  -0.0411 -0.0134 1809 MET A SD  
115  C CE  . MET A 16  ? 0.2165 0.3429 0.2608 0.0222  -0.0305 -0.0204 1809 MET A CE  
116  N N   . GLU A 17  ? 0.2730 0.4693 0.3423 -0.0580 -0.0146 0.0102  1810 GLU A N   
117  C CA  . GLU A 17  ? 0.3138 0.4839 0.3692 -0.0818 -0.0056 0.0166  1810 GLU A CA  
118  C C   . GLU A 17  ? 0.2922 0.4871 0.3669 -0.1090 -0.0069 0.0148  1810 GLU A C   
119  O O   . GLU A 17  ? 0.3435 0.5058 0.4046 -0.1307 -0.0055 0.0145  1810 GLU A O   
120  C CB  . GLU A 17  ? 0.2074 0.3740 0.2510 -0.0798 0.0123  0.0256  1810 GLU A CB  
121  C CG  . GLU A 17  ? 0.2985 0.4373 0.3173 -0.0581 0.0122  0.0265  1810 GLU A CG  
122  C CD  . GLU A 17  ? 0.3663 0.5173 0.3730 -0.0493 0.0269  0.0342  1810 GLU A CD  
123  O OE1 . GLU A 17  ? 0.3788 0.5626 0.3989 -0.0577 0.0388  0.0384  1810 GLU A OE1 
124  O OE2 . GLU A 17  ? 0.3707 0.5033 0.3546 -0.0339 0.0264  0.0358  1810 GLU A OE2 
125  N N   . SER A 18  ? 0.2749 0.5290 0.3821 -0.1085 -0.0092 0.0117  1811 SER A N   
126  C CA  . SER A 18  ? 0.2784 0.5714 0.4115 -0.1366 -0.0116 0.0075  1811 SER A CA  
127  C C   . SER A 18  ? 0.3040 0.6159 0.4459 -0.1352 -0.0350 -0.0013 1811 SER A C   
128  O O   . SER A 18  ? 0.3432 0.6703 0.4957 -0.1518 -0.0393 -0.0077 1811 SER A O   
129  C CB  . SER A 18  ? 0.1983 0.5581 0.3673 -0.1370 -0.0006 0.0091  1811 SER A CB  
130  O OG  . SER A 18  ? 0.3787 0.7225 0.5339 -0.1361 0.0221  0.0189  1811 SER A OG  
131  N N   . HIS A 19  ? 0.2935 0.5843 0.4200 -0.1078 -0.0472 -0.0014 1812 HIS A N   
132  C CA  . HIS A 19  ? 0.2446 0.5492 0.3718 -0.1012 -0.0683 -0.0059 1812 HIS A CA  
133  C C   . HIS A 19  ? 0.3246 0.5877 0.4256 -0.1242 -0.0728 -0.0116 1812 HIS A C   
134  O O   . HIS A 19  ? 0.2965 0.5106 0.3741 -0.1381 -0.0627 -0.0107 1812 HIS A O   
135  C CB  . HIS A 19  ? 0.2306 0.5106 0.3428 -0.0668 -0.0745 -0.0019 1812 HIS A CB  
136  C CG  . HIS A 19  ? 0.3110 0.6092 0.4230 -0.0522 -0.0943 -0.0015 1812 HIS A CG  
137  N ND1 . HIS A 19  ? 0.3221 0.6560 0.4538 -0.0239 -0.1000 0.0016  1812 HIS A ND1 
138  C CD2 . HIS A 19  ? 0.2366 0.5119 0.3245 -0.0579 -0.1066 -0.0028 1812 HIS A CD2 
139  C CE1 . HIS A 19  ? 0.2886 0.6188 0.4075 -0.0126 -0.1155 0.0044  1812 HIS A CE1 
140  N NE2 . HIS A 19  ? 0.2963 0.5939 0.3883 -0.0333 -0.1200 0.0013  1812 HIS A NE2 
141  N N   . ASP A 20  ? 0.3001 0.5814 0.4033 -0.1249 -0.0871 -0.0178 1813 ASP A N   
142  C CA  . ASP A 20  ? 0.3851 0.6330 0.4636 -0.1448 -0.0913 -0.0264 1813 ASP A CA  
143  C C   . ASP A 20  ? 0.4333 0.6282 0.4741 -0.1360 -0.0941 -0.0244 1813 ASP A C   
144  O O   . ASP A 20  ? 0.5281 0.6806 0.5431 -0.1517 -0.0897 -0.0309 1813 ASP A O   
145  C CB  . ASP A 20  ? 0.4368 0.7247 0.5263 -0.1452 -0.1082 -0.0341 1813 ASP A CB  
146  C CG  . ASP A 20  ? 0.5433 0.8744 0.6657 -0.1660 -0.1038 -0.0405 1813 ASP A CG  
147  O OD1 . ASP A 20  ? 0.6016 0.9815 0.7433 -0.1623 -0.1182 -0.0451 1813 ASP A OD1 
148  O OD2 . ASP A 20  ? 0.5554 0.8721 0.6838 -0.1856 -0.0854 -0.0398 1813 ASP A OD2 
149  N N   . ALA A 21  ? 0.3270 0.5216 0.3636 -0.1105 -0.0999 -0.0159 1814 ALA A N   
150  C CA  . ALA A 21  ? 0.2468 0.3908 0.2490 -0.1012 -0.1001 -0.0125 1814 ALA A CA  
151  C C   . ALA A 21  ? 0.2300 0.3309 0.2251 -0.0963 -0.0814 -0.0082 1814 ALA A C   
152  O O   . ALA A 21  ? 0.3344 0.3981 0.3095 -0.0834 -0.0776 -0.0048 1814 ALA A O   
153  C CB  . ALA A 21  ? 0.3060 0.4582 0.3034 -0.0718 -0.1111 -0.0042 1814 ALA A CB  
154  N N   . ALA A 22  ? 0.3151 0.4237 0.3258 -0.1067 -0.0694 -0.0077 1815 ALA A N   
155  C CA  . ALA A 22  ? 0.3311 0.4081 0.3345 -0.0987 -0.0541 -0.0025 1815 ALA A CA  
156  C C   . ALA A 22  ? 0.3725 0.3989 0.3496 -0.1102 -0.0443 -0.0036 1815 ALA A C   
157  O O   . ALA A 22  ? 0.2960 0.2971 0.2640 -0.0985 -0.0345 0.0013  1815 ALA A O   
158  C CB  . ALA A 22  ? 0.2692 0.3744 0.2938 -0.1021 -0.0438 0.0011  1815 ALA A CB  
159  N N   . TRP A 23  ? 0.3786 0.3909 0.3426 -0.1315 -0.0470 -0.0113 1816 TRP A N   
160  C CA  . TRP A 23  ? 0.4361 0.3965 0.3753 -0.1431 -0.0342 -0.0134 1816 TRP A CA  
161  C C   . TRP A 23  ? 0.4320 0.3540 0.3506 -0.1231 -0.0277 -0.0098 1816 TRP A C   
162  O O   . TRP A 23  ? 0.5649 0.4506 0.4700 -0.1217 -0.0139 -0.0062 1816 TRP A O   
163  C CB  . TRP A 23  ? 0.5121 0.4627 0.4386 -0.1638 -0.0384 -0.0261 1816 TRP A CB  
164  C CG  . TRP A 23  ? 0.4983 0.4561 0.4113 -0.1564 -0.0527 -0.0324 1816 TRP A CG  
165  C CD1 . TRP A 23  ? 0.5569 0.5612 0.4830 -0.1545 -0.0699 -0.0351 1816 TRP A CD1 
166  C CD2 . TRP A 23  ? 0.5223 0.4407 0.4041 -0.1474 -0.0497 -0.0350 1816 TRP A CD2 
167  N NE1 . TRP A 23  ? 0.5080 0.5006 0.4087 -0.1455 -0.0782 -0.0378 1816 TRP A NE1 
168  C CE2 . TRP A 23  ? 0.5354 0.4759 0.4088 -0.1428 -0.0651 -0.0383 1816 TRP A CE2 
169  C CE3 . TRP A 23  ? 0.5555 0.4252 0.4162 -0.1402 -0.0344 -0.0338 1816 TRP A CE3 
170  C CZ2 . TRP A 23  ? 0.5521 0.4648 0.3934 -0.1349 -0.0643 -0.0405 1816 TRP A CZ2 
171  C CZ3 . TRP A 23  ? 0.4968 0.3436 0.3312 -0.1315 -0.0334 -0.0376 1816 TRP A CZ3 
172  C CH2 . TRP A 23  ? 0.5038 0.3704 0.3270 -0.1307 -0.0475 -0.0409 1816 TRP A CH2 
173  N N   . PRO A 24  ? 0.3486 0.2769 0.2648 -0.1068 -0.0354 -0.0095 1817 PRO A N   
174  C CA  . PRO A 24  ? 0.3083 0.2087 0.2124 -0.0907 -0.0267 -0.0066 1817 PRO A CA  
175  C C   . PRO A 24  ? 0.3978 0.3098 0.3178 -0.0744 -0.0215 0.0006  1817 PRO A C   
176  O O   . PRO A 24  ? 0.3252 0.2226 0.2402 -0.0622 -0.0149 0.0020  1817 PRO A O   
177  C CB  . PRO A 24  ? 0.3586 0.2628 0.2553 -0.0834 -0.0347 -0.0081 1817 PRO A CB  
178  C CG  . PRO A 24  ? 0.3638 0.2907 0.2597 -0.0949 -0.0488 -0.0122 1817 PRO A CG  
179  C CD  . PRO A 24  ? 0.3542 0.3109 0.2754 -0.1024 -0.0505 -0.0110 1817 PRO A CD  
180  N N   . PHE A 25  ? 0.3313 0.2734 0.2703 -0.0735 -0.0243 0.0038  1818 PHE A N   
181  C CA  . PHE A 25  ? 0.2879 0.2470 0.2394 -0.0571 -0.0229 0.0067  1818 PHE A CA  
182  C C   . PHE A 25  ? 0.3353 0.3021 0.2888 -0.0559 -0.0149 0.0131  1818 PHE A C   
183  O O   . PHE A 25  ? 0.2916 0.2798 0.2538 -0.0435 -0.0153 0.0135  1818 PHE A O   
184  C CB  . PHE A 25  ? 0.2403 0.2270 0.2083 -0.0504 -0.0322 0.0037  1818 PHE A CB  
185  C CG  . PHE A 25  ? 0.2810 0.2580 0.2422 -0.0504 -0.0393 0.0016  1818 PHE A CG  
186  C CD1 . PHE A 25  ? 0.3773 0.3319 0.3289 -0.0452 -0.0356 0.0007  1818 PHE A CD1 
187  C CD2 . PHE A 25  ? 0.2949 0.2887 0.2588 -0.0548 -0.0491 0.0017  1818 PHE A CD2 
188  C CE1 . PHE A 25  ? 0.3647 0.3070 0.3049 -0.0449 -0.0389 0.0016  1818 PHE A CE1 
189  C CE2 . PHE A 25  ? 0.3092 0.2928 0.2600 -0.0516 -0.0557 0.0027  1818 PHE A CE2 
190  C CZ  . PHE A 25  ? 0.2773 0.2317 0.2139 -0.0469 -0.0494 0.0036  1818 PHE A CZ  
191  N N   . LEU A 26  ? 0.3048 0.2504 0.2465 -0.0686 -0.0062 0.0179  1819 LEU A N   
192  C CA  . LEU A 26  ? 0.2757 0.2230 0.2145 -0.0700 0.0047  0.0277  1819 LEU A CA  
193  C C   . LEU A 26  ? 0.3487 0.2711 0.2688 -0.0532 0.0135  0.0370  1819 LEU A C   
194  O O   . LEU A 26  ? 0.3897 0.3165 0.3029 -0.0468 0.0218  0.0479  1819 LEU A O   
195  C CB  . LEU A 26  ? 0.4044 0.3375 0.3403 -0.0960 0.0119  0.0287  1819 LEU A CB  
196  C CG  . LEU A 26  ? 0.4312 0.4021 0.3898 -0.1129 0.0019  0.0199  1819 LEU A CG  
197  C CD1 . LEU A 26  ? 0.3714 0.3303 0.3292 -0.1437 0.0090  0.0174  1819 LEU A CD1 
198  C CD2 . LEU A 26  ? 0.4543 0.4749 0.4359 -0.1030 -0.0001 0.0222  1819 LEU A CD2 
199  N N   . GLU A 27  ? 0.3471 0.2460 0.2577 -0.0441 0.0126  0.0340  1820 GLU A N   
200  C CA  . GLU A 27  ? 0.3639 0.2458 0.2601 -0.0237 0.0194  0.0427  1820 GLU A CA  
201  C C   . GLU A 27  ? 0.2772 0.1693 0.1819 -0.0109 0.0125  0.0340  1820 GLU A C   
202  O O   . GLU A 27  ? 0.3203 0.2125 0.2319 -0.0212 0.0072  0.0239  1820 GLU A O   
203  C CB  . GLU A 27  ? 0.3910 0.2197 0.2626 -0.0279 0.0341  0.0510  1820 GLU A CB  
204  C CG  . GLU A 27  ? 0.5328 0.3295 0.3966 -0.0397 0.0353  0.0399  1820 GLU A CG  
205  C CD  . GLU A 27  ? 0.6661 0.4022 0.5025 -0.0418 0.0519  0.0457  1820 GLU A CD  
206  O OE1 . GLU A 27  ? 0.5925 0.3081 0.4151 -0.0167 0.0607  0.0570  1820 GLU A OE1 
207  O OE2 . GLU A 27  ? 0.7226 0.4366 0.5536 -0.0669 0.0552  0.0375  1820 GLU A OE2 
208  N N   . PRO A 28  ? 0.3498 0.2550 0.2548 0.0110  0.0123  0.0379  1821 PRO A N   
209  C CA  . PRO A 28  ? 0.3281 0.2514 0.2477 0.0198  0.0072  0.0284  1821 PRO A CA  
210  C C   . PRO A 28  ? 0.2888 0.1789 0.1989 0.0176  0.0153  0.0258  1821 PRO A C   
211  O O   . PRO A 28  ? 0.3777 0.2285 0.2668 0.0200  0.0259  0.0326  1821 PRO A O   
212  C CB  . PRO A 28  ? 0.3855 0.3350 0.3069 0.0441  0.0053  0.0341  1821 PRO A CB  
213  C CG  . PRO A 28  ? 0.3733 0.3246 0.2802 0.0478  0.0065  0.0457  1821 PRO A CG  
214  C CD  . PRO A 28  ? 0.3253 0.2363 0.2182 0.0287  0.0162  0.0515  1821 PRO A CD  
215  N N   . VAL A 29  ? 0.2806 0.1826 0.2036 0.0125  0.0123  0.0156  1822 VAL A N   
216  C CA  . VAL A 29  ? 0.2814 0.1611 0.1958 0.0151  0.0216  0.0121  1822 VAL A CA  
217  C C   . VAL A 29  ? 0.3575 0.2439 0.2740 0.0403  0.0286  0.0176  1822 VAL A C   
218  O O   . VAL A 29  ? 0.3629 0.2919 0.3004 0.0526  0.0222  0.0173  1822 VAL A O   
219  C CB  . VAL A 29  ? 0.3166 0.2135 0.2451 0.0062  0.0191  0.0030  1822 VAL A CB  
220  C CG1 . VAL A 29  ? 0.3168 0.1952 0.2350 0.0102  0.0316  -0.0004 1822 VAL A CG1 
221  C CG2 . VAL A 29  ? 0.4799 0.3723 0.4050 -0.0123 0.0109  0.0005  1822 VAL A CG2 
222  N N   . ASN A 30  ? 0.3577 0.2033 0.2523 0.0495  0.0413  0.0214  1823 ASN A N   
223  C CA  . ASN A 30  ? 0.3850 0.2362 0.2811 0.0795  0.0490  0.0280  1823 ASN A CA  
224  C C   . ASN A 30  ? 0.4097 0.2825 0.3224 0.0851  0.0551  0.0183  1823 ASN A C   
225  O O   . ASN A 30  ? 0.3807 0.2180 0.2755 0.0803  0.0668  0.0125  1823 ASN A O   
226  C CB  . ASN A 30  ? 0.4037 0.1946 0.2670 0.0905  0.0631  0.0372  1823 ASN A CB  
227  C CG  . ASN A 30  ? 0.5708 0.3687 0.4340 0.1288  0.0697  0.0491  1823 ASN A CG  
228  O OD1 . ASN A 30  ? 0.5404 0.3848 0.4286 0.1467  0.0679  0.0452  1823 ASN A OD1 
229  N ND2 . ASN A 30  ? 0.7894 0.5435 0.6255 0.1421  0.0777  0.0648  1823 ASN A ND2 
230  N N   . PRO A 31  ? 0.3950 0.3265 0.3407 0.0939  0.0487  0.0151  1824 PRO A N   
231  C CA  . PRO A 31  ? 0.3761 0.3336 0.3425 0.0930  0.0567  0.0055  1824 PRO A CA  
232  C C   . PRO A 31  ? 0.4066 0.3419 0.3609 0.1149  0.0749  0.0066  1824 PRO A C   
233  O O   . PRO A 31  ? 0.4020 0.3372 0.3586 0.1083  0.0867  -0.0015 1824 PRO A O   
234  C CB  . PRO A 31  ? 0.3101 0.3384 0.3167 0.0994  0.0458  0.0016  1824 PRO A CB  
235  C CG  . PRO A 31  ? 0.4260 0.4617 0.4248 0.1174  0.0349  0.0119  1824 PRO A CG  
236  C CD  . PRO A 31  ? 0.4217 0.4008 0.3867 0.1037  0.0346  0.0186  1824 PRO A CD  
237  N N   . ARG A 32  ? 0.4327 0.3461 0.3712 0.1428  0.0796  0.0172  1825 ARG A N   
238  C CA  . ARG A 32  ? 0.4958 0.3792 0.4190 0.1674  0.0991  0.0177  1825 ARG A CA  
239  C C   . ARG A 32  ? 0.4972 0.3094 0.3808 0.1494  0.1114  0.0101  1825 ARG A C   
240  O O   . ARG A 32  ? 0.5328 0.3244 0.4044 0.1612  0.1291  0.0033  1825 ARG A O   
241  C CB  . ARG A 32  ? 0.5825 0.4497 0.4932 0.2042  0.1019  0.0334  1825 ARG A CB  
242  C CG  . ARG A 32  ? 0.6777 0.6071 0.6199 0.2381  0.1020  0.0372  1825 ARG A CG  
243  C CD  . ARG A 32  ? 0.7259 0.6331 0.6465 0.2631  0.1008  0.0545  1825 ARG A CD  
244  N NE  . ARG A 32  ? 0.6946 0.6755 0.6436 0.2836  0.0849  0.0617  1825 ARG A NE  
245  C CZ  . ARG A 32  ? 0.7308 0.7361 0.6802 0.2816  0.0681  0.0692  1825 ARG A CZ  
246  N NH1 . ARG A 32  ? 0.7042 0.6671 0.6306 0.2617  0.0660  0.0724  1825 ARG A NH1 
247  N NH2 . ARG A 32  ? 0.7717 0.8453 0.7431 0.2979  0.0531  0.0722  1825 ARG A NH2 
248  N N   . LEU A 33  ? 0.4437 0.2229 0.3075 0.1213  0.1024  0.0095  1826 LEU A N   
249  C CA  . LEU A 33  ? 0.5193 0.2360 0.3452 0.1013  0.1100  0.0003  1826 LEU A CA  
250  C C   . LEU A 33  ? 0.4724 0.2026 0.2981 0.0746  0.1061  -0.0116 1826 LEU A C   
251  O O   . LEU A 33  ? 0.5060 0.1934 0.2992 0.0575  0.1098  -0.0215 1826 LEU A O   
252  C CB  . LEU A 33  ? 0.5761 0.2545 0.3828 0.0850  0.1028  0.0064  1826 LEU A CB  
253  C CG  . LEU A 33  ? 0.7600 0.3937 0.5451 0.0991  0.1132  0.0153  1826 LEU A CG  
254  C CD1 . LEU A 33  ? 0.7560 0.4160 0.5564 0.1380  0.1160  0.0307  1826 LEU A CD1 
255  C CD2 . LEU A 33  ? 0.7986 0.4112 0.5731 0.0738  0.1063  0.0197  1826 LEU A CD2 
256  N N   . VAL A 34  ? 0.4168 0.2032 0.2751 0.0704  0.0991  -0.0112 1827 VAL A N   
257  C CA  . VAL A 34  ? 0.3972 0.1936 0.2535 0.0474  0.0963  -0.0178 1827 VAL A CA  
258  C C   . VAL A 34  ? 0.4497 0.2889 0.3326 0.0563  0.1076  -0.0196 1827 VAL A C   
259  O O   . VAL A 34  ? 0.3982 0.2874 0.3199 0.0600  0.1015  -0.0164 1827 VAL A O   
260  C CB  . VAL A 34  ? 0.3900 0.2051 0.2591 0.0267  0.0769  -0.0143 1827 VAL A CB  
261  C CG1 . VAL A 34  ? 0.4049 0.2248 0.2678 0.0083  0.0759  -0.0178 1827 VAL A CG1 
262  C CG2 . VAL A 34  ? 0.4122 0.1945 0.2613 0.0169  0.0677  -0.0124 1827 VAL A CG2 
263  N N   . SER A 35  ? 0.5104 0.3325 0.3728 0.0578  0.1247  -0.0262 1828 SER A N   
264  C CA  . SER A 35  ? 0.4063 0.2703 0.2943 0.0635  0.1397  -0.0278 1828 SER A CA  
265  C C   . SER A 35  ? 0.3693 0.2675 0.2824 0.0408  0.1312  -0.0247 1828 SER A C   
266  O O   . SER A 35  ? 0.4213 0.2962 0.3125 0.0209  0.1225  -0.0232 1828 SER A O   
267  C CB  . SER A 35  ? 0.4516 0.2864 0.3044 0.0657  0.1609  -0.0353 1828 SER A CB  
268  O OG  . SER A 35  ? 0.4477 0.3283 0.3296 0.0723  0.1790  -0.0358 1828 SER A OG  
269  N N   . GLY A 36  ? 0.3722 0.3263 0.3320 0.0445  0.1334  -0.0245 1829 GLY A N   
270  C CA  . GLY A 36  ? 0.3242 0.3070 0.3101 0.0218  0.1304  -0.0241 1829 GLY A CA  
271  C C   . GLY A 36  ? 0.3275 0.3185 0.3285 0.0107  0.1075  -0.0228 1829 GLY A C   
272  O O   . GLY A 36  ? 0.2710 0.2844 0.2966 -0.0071 0.1058  -0.0247 1829 GLY A O   
273  N N   . TYR A 37  ? 0.2830 0.3473 0.2956 0.0568  0.0877  0.0374  1830 TYR A N   
274  C CA  . TYR A 37  ? 0.2285 0.2922 0.2508 0.0458  0.0714  0.0371  1830 TYR A CA  
275  C C   . TYR A 37  ? 0.3690 0.4753 0.4244 0.0474  0.0649  0.0375  1830 TYR A C   
276  O O   . TYR A 37  ? 0.3585 0.4736 0.4269 0.0310  0.0564  0.0367  1830 TYR A O   
277  C CB  . TYR A 37  ? 0.2251 0.2552 0.2254 0.0504  0.0672  0.0346  1830 TYR A CB  
278  C CG  . TYR A 37  ? 0.2862 0.3137 0.2924 0.0372  0.0523  0.0334  1830 TYR A CG  
279  C CD1 . TYR A 37  ? 0.2853 0.3035 0.2829 0.0234  0.0468  0.0322  1830 TYR A CD1 
280  C CD2 . TYR A 37  ? 0.3010 0.3376 0.3195 0.0419  0.0442  0.0337  1830 TYR A CD2 
281  C CE1 . TYR A 37  ? 0.2276 0.2470 0.2304 0.0165  0.0345  0.0314  1830 TYR A CE1 
282  C CE2 . TYR A 37  ? 0.1988 0.2332 0.2218 0.0314  0.0327  0.0321  1830 TYR A CE2 
283  C CZ  . TYR A 37  ? 0.1813 0.2081 0.1977 0.0197  0.0283  0.0309  1830 TYR A CZ  
284  O OH  . TYR A 37  ? 0.2366 0.2642 0.2568 0.0141  0.0181  0.0295  1830 TYR A OH  
285  N N   . ARG A 38  ? 0.3800 0.5124 0.4456 0.0685  0.0688  0.0382  1831 ARG A N   
286  C CA  . ARG A 38  ? 0.3896 0.5737 0.4870 0.0708  0.0607  0.0367  1831 ARG A CA  
287  C C   . ARG A 38  ? 0.3113 0.5357 0.4353 0.0485  0.0642  0.0328  1831 ARG A C   
288  O O   . ARG A 38  ? 0.3499 0.6012 0.4939 0.0328  0.0554  0.0284  1831 ARG A O   
289  C CB  . ARG A 38  ? 0.3344 0.5456 0.4346 0.1042  0.0649  0.0391  1831 ARG A CB  
290  C CG  . ARG A 38  ? 0.4080 0.6855 0.5413 0.1101  0.0542  0.0364  1831 ARG A CG  
291  C CD  . ARG A 38  ? 0.5326 0.8188 0.6534 0.1463  0.0538  0.0400  1831 ARG A CD  
292  N NE  . ARG A 38  ? 0.5964 0.9210 0.7305 0.1473  0.0371  0.0365  1831 ARG A NE  
293  C CZ  . ARG A 38  ? 0.5945 0.8966 0.7132 0.1522  0.0263  0.0388  1831 ARG A CZ  
294  N NH1 . ARG A 38  ? 0.5516 0.8908 0.6798 0.1529  0.0127  0.0348  1831 ARG A NH1 
295  N NH2 . ARG A 38  ? 0.5395 0.7818 0.6312 0.1555  0.0305  0.0442  1831 ARG A NH2 
296  N N   . ARG A 39  ? 0.2326 0.4569 0.3527 0.0441  0.0791  0.0333  1832 ARG A N   
297  C CA  . ARG A 39  ? 0.3141 0.5718 0.4543 0.0199  0.0877  0.0293  1832 ARG A CA  
298  C C   . ARG A 39  ? 0.3362 0.5565 0.4629 -0.0090 0.0845  0.0293  1832 ARG A C   
299  O O   . ARG A 39  ? 0.3947 0.6361 0.5350 -0.0339 0.0902  0.0245  1832 ARG A O   
300  C CB  . ARG A 39  ? 0.2469 0.5083 0.3803 0.0249  0.1072  0.0307  1832 ARG A CB  
301  C CG  . ARG A 39  ? 0.3862 0.7084 0.5443 0.0495  0.1154  0.0285  1832 ARG A CG  
302  C CD  . ARG A 39  ? 0.4654 0.7716 0.6039 0.0651  0.1346  0.0313  1832 ARG A CD  
303  N NE  . ARG A 39  ? 0.4897 0.8390 0.6447 0.0896  0.1379  0.0274  1832 ARG A NE  
304  C CZ  . ARG A 39  ? 0.5730 0.9170 0.7189 0.1222  0.1292  0.0300  1832 ARG A CZ  
305  N NH1 . ARG A 39  ? 0.5922 0.8935 0.7156 0.1329  0.1200  0.0352  1832 ARG A NH1 
306  N NH2 . ARG A 39  ? 0.6236 1.0026 0.7793 0.1442  0.1310  0.0280  1832 ARG A NH2 
307  N N   . ILE A 40  ? 0.2352 0.4014 0.3332 -0.0059 0.0769  0.0340  1833 ILE A N   
308  C CA  . ILE A 40  ? 0.3022 0.4286 0.3797 -0.0241 0.0754  0.0364  1833 ILE A CA  
309  C C   . ILE A 40  ? 0.2778 0.3920 0.3565 -0.0267 0.0600  0.0350  1833 ILE A C   
310  O O   . ILE A 40  ? 0.3222 0.4182 0.3934 -0.0436 0.0605  0.0344  1833 ILE A O   
311  C CB  . ILE A 40  ? 0.2583 0.3416 0.3015 -0.0173 0.0782  0.0420  1833 ILE A CB  
312  C CG1 . ILE A 40  ? 0.2434 0.3317 0.2792 -0.0199 0.0965  0.0434  1833 ILE A CG1 
313  C CG2 . ILE A 40  ? 0.3212 0.3649 0.3397 -0.0254 0.0725  0.0462  1833 ILE A CG2 
314  C CD1 . ILE A 40  ? 0.2667 0.3141 0.2640 -0.0153 0.0992  0.0480  1833 ILE A CD1 
315  N N   . ILE A 41  ? 0.2163 0.3343 0.2993 -0.0102 0.0488  0.0344  1834 ILE A N   
316  C CA  . ILE A 41  ? 0.2276 0.3319 0.3086 -0.0106 0.0355  0.0332  1834 ILE A CA  
317  C C   . ILE A 41  ? 0.2102 0.3533 0.3154 -0.0082 0.0291  0.0281  1834 ILE A C   
318  O O   . ILE A 41  ? 0.2013 0.3618 0.3119 0.0106  0.0272  0.0289  1834 ILE A O   
319  C CB  . ILE A 41  ? 0.2062 0.2844 0.2697 0.0026  0.0292  0.0352  1834 ILE A CB  
320  C CG1 . ILE A 41  ? 0.1962 0.2469 0.2362 0.0003  0.0327  0.0385  1834 ILE A CG1 
321  C CG2 . ILE A 41  ? 0.1593 0.2288 0.2229 0.0022  0.0176  0.0334  1834 ILE A CG2 
322  C CD1 . ILE A 41  ? 0.2199 0.2510 0.2487 -0.0084 0.0306  0.0413  1834 ILE A CD1 
323  N N   . LYS A 42  ? 0.1690 0.3226 0.2833 -0.0264 0.0266  0.0228  1835 LYS A N   
324  C CA  . LYS A 42  ? 0.2712 0.4688 0.4075 -0.0267 0.0186  0.0160  1835 LYS A CA  
325  C C   . LYS A 42  ? 0.2063 0.3868 0.3340 -0.0182 0.0057  0.0158  1835 LYS A C   
326  O O   . LYS A 42  ? 0.1915 0.4027 0.3294 -0.0061 -0.0024 0.0136  1835 LYS A O   
327  C CB  . LYS A 42  ? 0.3703 0.5907 0.5187 -0.0566 0.0235  0.0065  1835 LYS A CB  
328  C CG  . LYS A 42  ? 0.4498 0.7051 0.6138 -0.0679 0.0379  0.0040  1835 LYS A CG  
329  C CD  . LYS A 42  ? 0.4726 0.7949 0.6650 -0.0466 0.0348  0.0024  1835 LYS A CD  
330  C CE  . LYS A 42  ? 0.5558 0.8680 0.7410 -0.0244 0.0447  0.0112  1835 LYS A CE  
331  N NZ  . LYS A 42  ? 0.5483 0.8793 0.7360 0.0121  0.0379  0.0158  1835 LYS A NZ  
332  N N   . ASN A 43  ? 0.1662 0.3006 0.2736 -0.0214 0.0043  0.0184  1836 ASN A N   
333  C CA  . ASN A 43  ? 0.1514 0.2692 0.2501 -0.0153 -0.0053 0.0175  1836 ASN A CA  
334  C C   . ASN A 43  ? 0.1329 0.2230 0.2167 -0.0014 -0.0054 0.0232  1836 ASN A C   
335  O O   . ASN A 43  ? 0.1634 0.2269 0.2342 -0.0037 -0.0057 0.0245  1836 ASN A O   
336  C CB  . ASN A 43  ? 0.1604 0.2537 0.2485 -0.0320 -0.0053 0.0131  1836 ASN A CB  
337  C CG  . ASN A 43  ? 0.2413 0.3595 0.3405 -0.0536 -0.0033 0.0038  1836 ASN A CG  
338  O OD1 . ASN A 43  ? 0.3565 0.5169 0.4724 -0.0531 -0.0108 -0.0022 1836 ASN A OD1 
339  N ND2 . ASN A 43  ? 0.2543 0.3475 0.3412 -0.0738 0.0077  0.0020  1836 ASN A ND2 
340  N N   . PRO A 44  ? 0.1491 0.2447 0.2313 0.0131  -0.0041 0.0258  1837 PRO A N   
341  C CA  . PRO A 44  ? 0.2220 0.2913 0.2875 0.0190  -0.0022 0.0277  1837 PRO A CA  
342  C C   . PRO A 44  ? 0.2616 0.3192 0.3208 0.0189  -0.0079 0.0253  1837 PRO A C   
343  O O   . PRO A 44  ? 0.1919 0.2576 0.2547 0.0206  -0.0131 0.0234  1837 PRO A O   
344  C CB  . PRO A 44  ? 0.1949 0.2643 0.2532 0.0330  0.0043  0.0300  1837 PRO A CB  
345  C CG  . PRO A 44  ? 0.2992 0.4009 0.3723 0.0415  0.0020  0.0304  1837 PRO A CG  
346  C CD  . PRO A 44  ? 0.1993 0.3242 0.2914 0.0249  -0.0018 0.0267  1837 PRO A CD  
347  N N   . MET A 45  ? 0.2118 0.2552 0.2614 0.0165  -0.0069 0.0242  1838 MET A N   
348  C CA  . MET A 45  ? 0.1975 0.2359 0.2432 0.0157  -0.0099 0.0209  1838 MET A CA  
349  C C   . MET A 45  ? 0.2413 0.2758 0.2778 0.0117  -0.0060 0.0175  1838 MET A C   
350  O O   . MET A 45  ? 0.2183 0.2540 0.2512 0.0093  -0.0043 0.0176  1838 MET A O   
351  C CB  . MET A 45  ? 0.2053 0.2437 0.2549 0.0141  -0.0152 0.0201  1838 MET A CB  
352  C CG  . MET A 45  ? 0.2686 0.3060 0.3158 0.0162  -0.0173 0.0163  1838 MET A CG  
353  S SD  . MET A 45  ? 0.2368 0.2721 0.2794 0.0177  -0.0164 0.0145  1838 MET A SD  
354  C CE  . MET A 45  ? 0.2177 0.2615 0.2667 0.0174  -0.0219 0.0153  1838 MET A CE  
355  N N   . ASP A 46  ? 0.2164 0.2482 0.2475 0.0087  -0.0036 0.0131  1839 ASP A N   
356  C CA  . ASP A 46  ? 0.1917 0.2269 0.2156 -0.0016 0.0014  0.0060  1839 ASP A CA  
357  C C   . ASP A 46  ? 0.2425 0.2841 0.2678 -0.0053 0.0027  0.0010  1839 ASP A C   
358  O O   . ASP A 46  ? 0.1963 0.2313 0.2225 0.0016  0.0007  0.0041  1839 ASP A O   
359  C CB  . ASP A 46  ? 0.2673 0.2784 0.2707 -0.0075 0.0130  0.0043  1839 ASP A CB  
360  C CG  . ASP A 46  ? 0.1875 0.1721 0.1735 -0.0042 0.0216  0.0060  1839 ASP A CG  
361  O OD1 . ASP A 46  ? 0.2586 0.2388 0.2457 0.0106  0.0183  0.0135  1839 ASP A OD1 
362  O OD2 . ASP A 46  ? 0.2967 0.2665 0.2657 -0.0174 0.0321  -0.0007 1839 ASP A OD2 
363  N N   . PHE A 47  ? 0.2205 0.2784 0.2452 -0.0180 0.0070  -0.0082 1840 PHE A N   
364  C CA  . PHE A 47  ? 0.1980 0.2715 0.2276 -0.0232 0.0102  -0.0146 1840 PHE A CA  
365  C C   . PHE A 47  ? 0.2093 0.2502 0.2188 -0.0288 0.0221  -0.0142 1840 PHE A C   
366  O O   . PHE A 47  ? 0.2902 0.3334 0.3011 -0.0259 0.0233  -0.0147 1840 PHE A O   
367  C CB  . PHE A 47  ? 0.1750 0.2863 0.2122 -0.0388 0.0126  -0.0271 1840 PHE A CB  
368  C CG  . PHE A 47  ? 0.2209 0.3709 0.2744 -0.0275 -0.0004 -0.0269 1840 PHE A CG  
369  C CD1 . PHE A 47  ? 0.1424 0.2866 0.2010 -0.0050 -0.0104 -0.0161 1840 PHE A CD1 
370  C CD2 . PHE A 47  ? 0.2254 0.4163 0.2841 -0.0401 -0.0017 -0.0382 1840 PHE A CD2 
371  C CE1 . PHE A 47  ? 0.2002 0.3706 0.2639 0.0091  -0.0201 -0.0140 1840 PHE A CE1 
372  C CE2 . PHE A 47  ? 0.2253 0.4535 0.2938 -0.0248 -0.0148 -0.0367 1840 PHE A CE2 
373  C CZ  . PHE A 47  ? 0.1798 0.3936 0.2483 0.0020  -0.0234 -0.0233 1840 PHE A CZ  
374  N N   . SER A 48  ? 0.2508 0.2565 0.2359 -0.0349 0.0329  -0.0131 1841 SER A N   
375  C CA  . SER A 48  ? 0.3017 0.2684 0.2585 -0.0350 0.0455  -0.0104 1841 SER A CA  
376  C C   . SER A 48  ? 0.3283 0.2883 0.2864 -0.0126 0.0360  0.0003  1841 SER A C   
377  O O   . SER A 48  ? 0.2821 0.2268 0.2249 -0.0093 0.0407  0.0020  1841 SER A O   
378  C CB  . SER A 48  ? 0.2706 0.1905 0.1915 -0.0410 0.0615  -0.0100 1841 SER A CB  
379  O OG  . SER A 48  ? 0.2866 0.1940 0.2048 -0.0204 0.0557  0.0000  1841 SER A OG  
380  N N   . THR A 49  ? 0.2855 0.2596 0.2605 0.0005  0.0233  0.0061  1842 THR A N   
381  C CA  . THR A 49  ? 0.2012 0.1799 0.1810 0.0163  0.0133  0.0126  1842 THR A CA  
382  C C   . THR A 49  ? 0.1748 0.1718 0.1688 0.0147  0.0061  0.0088  1842 THR A C   
383  O O   . THR A 49  ? 0.2700 0.2622 0.2558 0.0215  0.0031  0.0103  1842 THR A O   
384  C CB  . THR A 49  ? 0.2681 0.2611 0.2632 0.0244  0.0048  0.0170  1842 THR A CB  
385  O OG1 . THR A 49  ? 0.2618 0.2353 0.2401 0.0296  0.0137  0.0205  1842 THR A OG1 
386  C CG2 . THR A 49  ? 0.2235 0.2310 0.2259 0.0352  -0.0056 0.0202  1842 THR A CG2 
387  N N   . MET A 50  ? 0.1588 0.1762 0.1701 0.0081  0.0038  0.0037  1843 MET A N   
388  C CA  . MET A 50  ? 0.1527 0.1833 0.1725 0.0102  0.0005  -0.0001 1843 MET A CA  
389  C C   . MET A 50  ? 0.2032 0.2289 0.2108 0.0042  0.0109  -0.0048 1843 MET A C   
390  O O   . MET A 50  ? 0.2701 0.2929 0.2730 0.0092  0.0102  -0.0059 1843 MET A O   
391  C CB  . MET A 50  ? 0.1846 0.2394 0.2210 0.0112  -0.0033 -0.0030 1843 MET A CB  
392  C CG  . MET A 50  ? 0.1831 0.2349 0.2250 0.0169  -0.0111 0.0026  1843 MET A CG  
393  S SD  . MET A 50  ? 0.2230 0.2979 0.2739 0.0230  -0.0149 0.0018  1843 MET A SD  
394  C CE  . MET A 50  ? 0.2451 0.3273 0.2969 0.0364  -0.0152 -0.0009 1843 MET A CE  
395  N N   . ARG A 51  ? 0.1817 0.2032 0.1803 -0.0092 0.0227  -0.0088 1844 ARG A N   
396  C CA  . ARG A 51  ? 0.2045 0.2175 0.1874 -0.0203 0.0372  -0.0142 1844 ARG A CA  
397  C C   . ARG A 51  ? 0.2477 0.2229 0.2009 -0.0115 0.0409  -0.0070 1844 ARG A C   
398  O O   . ARG A 51  ? 0.2868 0.2579 0.2299 -0.0115 0.0464  -0.0090 1844 ARG A O   
399  C CB  . ARG A 51  ? 0.2640 0.2729 0.2370 -0.0423 0.0518  -0.0216 1844 ARG A CB  
400  C CG  . ARG A 51  ? 0.3190 0.3063 0.2661 -0.0598 0.0726  -0.0273 1844 ARG A CG  
401  C CD  . ARG A 51  ? 0.3644 0.3920 0.3315 -0.0647 0.0751  -0.0359 1844 ARG A CD  
402  N NE  . ARG A 51  ? 0.4708 0.5569 0.4707 -0.0756 0.0718  -0.0474 1844 ARG A NE  
403  C CZ  . ARG A 51  ? 0.4659 0.6018 0.4882 -0.0792 0.0749  -0.0571 1844 ARG A CZ  
404  N NH1 . ARG A 51  ? 0.4830 0.6110 0.4969 -0.0751 0.0833  -0.0569 1844 ARG A NH1 
405  N NH2 . ARG A 51  ? 0.3369 0.5342 0.3890 -0.0845 0.0695  -0.0672 1844 ARG A NH2 
406  N N   . GLU A 52  ? 0.3128 0.2633 0.2503 -0.0013 0.0380  0.0014  1845 GLU A N   
407  C CA  . GLU A 52  ? 0.4127 0.3345 0.3204 0.0134  0.0388  0.0093  1845 GLU A CA  
408  C C   . GLU A 52  ? 0.2842 0.2255 0.2030 0.0233  0.0248  0.0090  1845 GLU A C   
409  O O   . GLU A 52  ? 0.3647 0.2917 0.2612 0.0274  0.0284  0.0097  1845 GLU A O   
410  C CB  . GLU A 52  ? 0.4813 0.3871 0.3766 0.0284  0.0358  0.0182  1845 GLU A CB  
411  C CG  . GLU A 52  ? 0.4588 0.3324 0.3142 0.0486  0.0393  0.0279  1845 GLU A CG  
412  C CD  . GLU A 52  ? 0.5208 0.4213 0.3849 0.0635  0.0214  0.0298  1845 GLU A CD  
413  O OE1 . GLU A 52  ? 0.4002 0.3391 0.2996 0.0621  0.0060  0.0262  1845 GLU A OE1 
414  O OE2 . GLU A 52  ? 0.5162 0.3970 0.3480 0.0742  0.0241  0.0339  1845 GLU A OE2 
415  N N   . ARG A 53  ? 0.2522 0.2209 0.2002 0.0258  0.0104  0.0075  1846 ARG A N   
416  C CA  . ARG A 53  ? 0.2591 0.2397 0.2130 0.0307  -0.0009 0.0048  1846 ARG A CA  
417  C C   . ARG A 53  ? 0.2332 0.2147 0.1860 0.0258  0.0055  -0.0020 1846 ARG A C   
418  O O   . ARG A 53  ? 0.2918 0.2661 0.2292 0.0298  0.0037  -0.0040 1846 ARG A O   
419  C CB  . ARG A 53  ? 0.2045 0.2045 0.1837 0.0296  -0.0122 0.0037  1846 ARG A CB  
420  C CG  . ARG A 53  ? 0.2305 0.2349 0.2105 0.0290  -0.0208 -0.0016 1846 ARG A CG  
421  C CD  . ARG A 53  ? 0.2533 0.2690 0.2508 0.0241  -0.0283 -0.0024 1846 ARG A CD  
422  N NE  . ARG A 53  ? 0.2646 0.2750 0.2568 0.0181  -0.0326 -0.0099 1846 ARG A NE  
423  C CZ  . ARG A 53  ? 0.2817 0.2899 0.2805 0.0092  -0.0346 -0.0129 1846 ARG A CZ  
424  N NH1 . ARG A 53  ? 0.3156 0.3308 0.3290 0.0072  -0.0338 -0.0081 1846 ARG A NH1 
425  N NH2 . ARG A 53  ? 0.2936 0.2870 0.2794 0.0007  -0.0351 -0.0214 1846 ARG A NH2 
426  N N   . LEU A 54  ? 0.2193 0.2143 0.1878 0.0183  0.0129  -0.0065 1847 LEU A N   
427  C CA  . LEU A 54  ? 0.2441 0.2495 0.2155 0.0174  0.0198  -0.0134 1847 LEU A CA  
428  C C   . LEU A 54  ? 0.2680 0.2560 0.2133 0.0126  0.0334  -0.0146 1847 LEU A C   
429  O O   . LEU A 54  ? 0.3209 0.3057 0.2562 0.0167  0.0363  -0.0182 1847 LEU A O   
430  C CB  . LEU A 54  ? 0.2823 0.3188 0.2783 0.0128  0.0236  -0.0183 1847 LEU A CB  
431  C CG  . LEU A 54  ? 0.3366 0.3996 0.3438 0.0172  0.0300  -0.0258 1847 LEU A CG  
432  C CD1 . LEU A 54  ? 0.2685 0.3210 0.2719 0.0338  0.0231  -0.0256 1847 LEU A CD1 
433  C CD2 . LEU A 54  ? 0.3084 0.4130 0.3410 0.0147  0.0301  -0.0301 1847 LEU A CD2 
434  N N   . SER A 55  ? 0.2858 0.2539 0.2126 0.0046  0.0434  -0.0109 1848 SER A N   
435  C CA  A SER A 55  ? 0.3160 0.2594 0.2112 -0.0027 0.0612  -0.0117 1848 SER A CA  
436  C CA  B SER A 55  ? 0.2958 0.2389 0.1908 -0.0027 0.0613  -0.0116 1848 SER A CA  
437  C C   . SER A 55  ? 0.3968 0.3151 0.2610 0.0116  0.0565  -0.0062 1848 SER A C   
438  O O   . SER A 55  ? 0.4271 0.3320 0.2688 0.0087  0.0689  -0.0086 1848 SER A O   
439  C CB  A SER A 55  ? 0.3556 0.2696 0.2279 -0.0147 0.0761  -0.0087 1848 SER A CB  
440  C CB  B SER A 55  ? 0.3524 0.2652 0.2237 -0.0141 0.0759  -0.0083 1848 SER A CB  
441  O OG  A SER A 55  ? 0.3531 0.2948 0.2506 -0.0338 0.0829  -0.0178 1848 SER A OG  
442  O OG  B SER A 55  ? 0.4261 0.3066 0.2713 0.0024  0.0694  0.0031  1848 SER A OG  
443  N N   . ARG A 56  ? 0.3961 0.3125 0.2584 0.0261  0.0391  0.0001  1849 ARG A N   
444  C CA  . ARG A 56  ? 0.4119 0.3151 0.2455 0.0396  0.0312  0.0035  1849 ARG A CA  
445  C C   . ARG A 56  ? 0.3852 0.3096 0.2346 0.0412  0.0177  -0.0044 1849 ARG A C   
446  O O   . ARG A 56  ? 0.3988 0.3243 0.2329 0.0498  0.0049  -0.0041 1849 ARG A O   
447  C CB  . ARG A 56  ? 0.4579 0.3545 0.2772 0.0554  0.0206  0.0133  1849 ARG A CB  
448  C CG  . ARG A 56  ? 0.3605 0.2881 0.2174 0.0555  0.0055  0.0123  1849 ARG A CG  
449  C CD  . ARG A 56  ? 0.4476 0.3832 0.2949 0.0737  -0.0068 0.0199  1849 ARG A CD  
450  N NE  . ARG A 56  ? 0.3907 0.3511 0.2722 0.0708  -0.0142 0.0196  1849 ARG A NE  
451  C CZ  . ARG A 56  ? 0.4213 0.4122 0.3339 0.0619  -0.0264 0.0124  1849 ARG A CZ  
452  N NH1 . ARG A 56  ? 0.3523 0.3504 0.2651 0.0549  -0.0327 0.0041  1849 ARG A NH1 
453  N NH2 . ARG A 56  ? 0.4873 0.4956 0.4257 0.0589  -0.0298 0.0133  1849 ARG A NH2 
454  N N   . GLY A 57  ? 0.3013 0.2418 0.1770 0.0338  0.0211  -0.0121 1850 GLY A N   
455  C CA  . GLY A 57  ? 0.2969 0.2445 0.1800 0.0359  0.0123  -0.0196 1850 GLY A CA  
456  C C   . GLY A 57  ? 0.2841 0.2406 0.1787 0.0360  -0.0049 -0.0199 1850 GLY A C   
457  O O   . GLY A 57  ? 0.3232 0.2760 0.2073 0.0346  -0.0125 -0.0268 1850 GLY A O   
458  N N   . GLY A 58  ? 0.2612 0.2297 0.1761 0.0348  -0.0097 -0.0144 1851 GLY A N   
459  C CA  . GLY A 58  ? 0.2857 0.2671 0.2132 0.0321  -0.0233 -0.0154 1851 GLY A CA  
460  C C   . GLY A 58  ? 0.2749 0.2559 0.2200 0.0258  -0.0239 -0.0202 1851 GLY A C   
461  O O   . GLY A 58  ? 0.2790 0.2679 0.2338 0.0192  -0.0317 -0.0216 1851 GLY A O   
462  N N   . TYR A 59  ? 0.2723 0.2444 0.2190 0.0291  -0.0144 -0.0226 1852 TYR A N   
463  C CA  . TYR A 59  ? 0.3524 0.3141 0.3041 0.0302  -0.0127 -0.0258 1852 TYR A CA  
464  C C   . TYR A 59  ? 0.2784 0.2168 0.2068 0.0330  -0.0076 -0.0343 1852 TYR A C   
465  O O   . TYR A 59  ? 0.3259 0.2650 0.2489 0.0418  0.0016  -0.0359 1852 TYR A O   
466  C CB  . TYR A 59  ? 0.2535 0.2279 0.2227 0.0387  -0.0062 -0.0217 1852 TYR A CB  
467  C CG  . TYR A 59  ? 0.2156 0.2068 0.2036 0.0347  -0.0102 -0.0151 1852 TYR A CG  
468  C CD1 . TYR A 59  ? 0.2338 0.2197 0.2265 0.0300  -0.0163 -0.0126 1852 TYR A CD1 
469  C CD2 . TYR A 59  ? 0.2170 0.2260 0.2143 0.0331  -0.0054 -0.0127 1852 TYR A CD2 
470  C CE1 . TYR A 59  ? 0.2400 0.2398 0.2475 0.0275  -0.0186 -0.0069 1852 TYR A CE1 
471  C CE2 . TYR A 59  ? 0.1988 0.2177 0.2081 0.0289  -0.0076 -0.0081 1852 TYR A CE2 
472  C CZ  . TYR A 59  ? 0.2044 0.2193 0.2191 0.0279  -0.0147 -0.0047 1852 TYR A CZ  
473  O OH  . TYR A 59  ? 0.2215 0.2448 0.2457 0.0248  -0.0157 -0.0004 1852 TYR A OH  
474  N N   . THR A 60  ? 0.3064 0.2235 0.2194 0.0236  -0.0114 -0.0411 1853 THR A N   
475  C CA  . THR A 60  ? 0.3432 0.2294 0.2265 0.0245  -0.0049 -0.0510 1853 THR A CA  
476  C C   . THR A 60  ? 0.3650 0.2237 0.2398 0.0396  0.0073  -0.0508 1853 THR A C   
477  O O   . THR A 60  ? 0.3985 0.2328 0.2495 0.0489  0.0169  -0.0572 1853 THR A O   
478  C CB  . THR A 60  ? 0.4020 0.2736 0.2658 0.0039  -0.0119 -0.0619 1853 THR A CB  
479  O OG1 . THR A 60  ? 0.4470 0.3124 0.3194 -0.0083 -0.0135 -0.0615 1853 THR A OG1 
480  C CG2 . THR A 60  ? 0.4105 0.3150 0.2764 -0.0035 -0.0250 -0.0631 1853 THR A CG2 
481  N N   . SER A 61  ? 0.3512 0.2133 0.2417 0.0458  0.0077  -0.0431 1854 SER A N   
482  C CA  . SER A 61  ? 0.3803 0.2174 0.2587 0.0666  0.0181  -0.0405 1854 SER A CA  
483  C C   . SER A 61  ? 0.3700 0.2412 0.2774 0.0787  0.0151  -0.0299 1854 SER A C   
484  O O   . SER A 61  ? 0.3419 0.2412 0.2728 0.0659  0.0063  -0.0257 1854 SER A O   
485  C CB  . SER A 61  ? 0.4648 0.2454 0.3103 0.0583  0.0237  -0.0444 1854 SER A CB  
486  O OG  . SER A 61  ? 0.5218 0.3094 0.3815 0.0442  0.0174  -0.0389 1854 SER A OG  
487  N N   . SER A 62  ? 0.3733 0.2430 0.2763 0.1055  0.0225  -0.0262 1855 SER A N   
488  C CA  . SER A 62  ? 0.4014 0.3060 0.3278 0.1182  0.0184  -0.0175 1855 SER A CA  
489  C C   . SER A 62  ? 0.4037 0.2825 0.3223 0.1097  0.0146  -0.0111 1855 SER A C   
490  O O   . SER A 62  ? 0.3302 0.2405 0.2711 0.1075  0.0076  -0.0051 1855 SER A O   
491  C CB  . SER A 62  ? 0.3588 0.2740 0.2797 0.1538  0.0260  -0.0152 1855 SER A CB  
492  O OG  . SER A 62  ? 0.4786 0.3300 0.3564 0.1707  0.0364  -0.0149 1855 SER A OG  
493  N N   . GLU A 63  ? 0.4578 0.2779 0.3422 0.1019  0.0209  -0.0135 1856 GLU A N   
494  C CA  . GLU A 63  ? 0.4896 0.2826 0.3642 0.0874  0.0206  -0.0091 1856 GLU A CA  
495  C C   . GLU A 63  ? 0.4336 0.2666 0.3409 0.0613  0.0093  -0.0096 1856 GLU A C   
496  O O   . GLU A 63  ? 0.4011 0.2434 0.3185 0.0579  0.0064  -0.0027 1856 GLU A O   
497  C CB  . GLU A 63  ? 0.5390 0.2624 0.3697 0.0732  0.0320  -0.0162 1856 GLU A CB  
498  C CG  . GLU A 63  ? 0.6598 0.3203 0.4434 0.1016  0.0477  -0.0122 1856 GLU A CG  
499  C CD  . GLU A 63  ? 0.6549 0.3214 0.4325 0.1302  0.0523  -0.0150 1856 GLU A CD  
500  O OE1 . GLU A 63  ? 0.6211 0.2776 0.3816 0.1641  0.0593  -0.0066 1856 GLU A OE1 
501  O OE2 . GLU A 63  ? 0.5932 0.2838 0.3851 0.1171  0.0483  -0.0248 1856 GLU A OE2 
502  N N   . GLU A 64  ? 0.3525 0.2080 0.2729 0.0459  0.0035  -0.0170 1857 GLU A N   
503  C CA  . GLU A 64  ? 0.3362 0.2273 0.2826 0.0281  -0.0061 -0.0161 1857 GLU A CA  
504  C C   . GLU A 64  ? 0.3238 0.2542 0.2967 0.0384  -0.0103 -0.0086 1857 GLU A C   
505  O O   . GLU A 64  ? 0.3151 0.2628 0.3032 0.0300  -0.0146 -0.0045 1857 GLU A O   
506  C CB  . GLU A 64  ? 0.3463 0.2498 0.2929 0.0151  -0.0115 -0.0245 1857 GLU A CB  
507  C CG  . GLU A 64  ? 0.4126 0.2861 0.3353 -0.0042 -0.0095 -0.0352 1857 GLU A CG  
508  C CD  . GLU A 64  ? 0.5642 0.4575 0.4852 -0.0152 -0.0174 -0.0442 1857 GLU A CD  
509  O OE1 . GLU A 64  ? 0.5988 0.5148 0.5284 -0.0033 -0.0211 -0.0407 1857 GLU A OE1 
510  O OE2 . GLU A 64  ? 0.5809 0.4673 0.4890 -0.0370 -0.0194 -0.0553 1857 GLU A OE2 
511  N N   . PHE A 65  ? 0.2884 0.2346 0.2659 0.0547  -0.0076 -0.0083 1858 PHE A N   
512  C CA  . PHE A 65  ? 0.2433 0.2273 0.2428 0.0601  -0.0098 -0.0043 1858 PHE A CA  
513  C C   . PHE A 65  ? 0.2372 0.2199 0.2366 0.0684  -0.0112 0.0025  1858 PHE A C   
514  O O   . PHE A 65  ? 0.2560 0.2589 0.2693 0.0615  -0.0150 0.0056  1858 PHE A O   
515  C CB  . PHE A 65  ? 0.2752 0.2832 0.2801 0.0733  -0.0048 -0.0083 1858 PHE A CB  
516  C CG  . PHE A 65  ? 0.2343 0.2872 0.2613 0.0738  -0.0058 -0.0082 1858 PHE A CG  
517  C CD1 . PHE A 65  ? 0.2430 0.3188 0.2753 0.0916  -0.0074 -0.0058 1858 PHE A CD1 
518  C CD2 . PHE A 65  ? 0.2182 0.2888 0.2556 0.0565  -0.0042 -0.0112 1858 PHE A CD2 
519  C CE1 . PHE A 65  ? 0.2332 0.3579 0.2859 0.0881  -0.0092 -0.0089 1858 PHE A CE1 
520  C CE2 . PHE A 65  ? 0.2740 0.3823 0.3274 0.0508  -0.0028 -0.0142 1858 PHE A CE2 
521  C CZ  . PHE A 65  ? 0.1867 0.3268 0.2503 0.0647  -0.0063 -0.0144 1858 PHE A CZ  
522  N N   . ALA A 66  ? 0.2812 0.2340 0.2586 0.0845  -0.0066 0.0054  1859 ALA A N   
523  C CA  . ALA A 66  ? 0.2810 0.2260 0.2493 0.0970  -0.0068 0.0137  1859 ALA A CA  
524  C C   . ALA A 66  ? 0.3562 0.2831 0.3222 0.0768  -0.0075 0.0169  1859 ALA A C   
525  O O   . ALA A 66  ? 0.3509 0.2884 0.3199 0.0799  -0.0099 0.0230  1859 ALA A O   
526  C CB  . ALA A 66  ? 0.3358 0.2381 0.2695 0.1217  0.0014  0.0176  1859 ALA A CB  
527  N N   . ALA A 67  ? 0.3131 0.2182 0.2742 0.0557  -0.0053 0.0117  1860 ALA A N   
528  C CA  . ALA A 67  ? 0.2756 0.1765 0.2406 0.0352  -0.0052 0.0130  1860 ALA A CA  
529  C C   . ALA A 67  ? 0.3476 0.2918 0.3410 0.0310  -0.0122 0.0150  1860 ALA A C   
530  O O   . ALA A 67  ? 0.3066 0.2534 0.3023 0.0271  -0.0113 0.0199  1860 ALA A O   
531  C CB  . ALA A 67  ? 0.2785 0.1664 0.2391 0.0120  -0.0035 0.0039  1860 ALA A CB  
532  N N   . ASP A 68  ? 0.2301 0.2026 0.2399 0.0318  -0.0168 0.0113  1861 ASP A N   
533  C CA  . ASP A 68  ? 0.1669 0.1677 0.1943 0.0274  -0.0199 0.0126  1861 ASP A CA  
534  C C   . ASP A 68  ? 0.2363 0.2512 0.2661 0.0365  -0.0204 0.0162  1861 ASP A C   
535  O O   . ASP A 68  ? 0.2080 0.2310 0.2424 0.0314  -0.0205 0.0187  1861 ASP A O   
536  C CB  . ASP A 68  ? 0.3524 0.3678 0.3864 0.0256  -0.0210 0.0083  1861 ASP A CB  
537  C CG  . ASP A 68  ? 0.2442 0.2591 0.2784 0.0171  -0.0236 0.0063  1861 ASP A CG  
538  O OD1 . ASP A 68  ? 0.2021 0.2224 0.2341 0.0183  -0.0242 0.0044  1861 ASP A OD1 
539  O OD2 . ASP A 68  ? 0.2443 0.2558 0.2793 0.0092  -0.0246 0.0063  1861 ASP A OD2 
540  N N   . ALA A 69  ? 0.2499 0.2723 0.2760 0.0510  -0.0207 0.0154  1862 ALA A N   
541  C CA  . ALA A 69  ? 0.1985 0.2465 0.2277 0.0607  -0.0235 0.0170  1862 ALA A CA  
542  C C   . ALA A 69  ? 0.2991 0.3288 0.3139 0.0651  -0.0237 0.0249  1862 ALA A C   
543  O O   . ALA A 69  ? 0.2440 0.2907 0.2620 0.0617  -0.0261 0.0258  1862 ALA A O   
544  C CB  . ALA A 69  ? 0.2325 0.2996 0.2610 0.0805  -0.0242 0.0149  1862 ALA A CB  
545  N N   . LEU A 70  ? 0.3254 0.3148 0.3189 0.0707  -0.0190 0.0300  1863 LEU A N   
546  C CA  . LEU A 70  ? 0.2576 0.2215 0.2304 0.0738  -0.0155 0.0383  1863 LEU A CA  
547  C C   . LEU A 70  ? 0.2522 0.2171 0.2351 0.0519  -0.0132 0.0380  1863 LEU A C   
548  O O   . LEU A 70  ? 0.2975 0.2584 0.2707 0.0526  -0.0114 0.0434  1863 LEU A O   
549  C CB  . LEU A 70  ? 0.3279 0.2374 0.2675 0.0816  -0.0064 0.0430  1863 LEU A CB  
550  C CG  . LEU A 70  ? 0.4138 0.3144 0.3350 0.1117  -0.0061 0.0454  1863 LEU A CG  
551  C CD1 . LEU A 70  ? 0.4853 0.3143 0.3606 0.1201  0.0072  0.0511  1863 LEU A CD1 
552  C CD2 . LEU A 70  ? 0.3738 0.3149 0.2975 0.1379  -0.0147 0.0499  1863 LEU A CD2 
553  N N   . LEU A 71  ? 0.2341 0.2066 0.2344 0.0354  -0.0129 0.0320  1864 LEU A N   
554  C CA  . LEU A 71  ? 0.2751 0.2590 0.2880 0.0207  -0.0110 0.0315  1864 LEU A CA  
555  C C   . LEU A 71  ? 0.2335 0.2403 0.2532 0.0239  -0.0137 0.0319  1864 LEU A C   
556  O O   . LEU A 71  ? 0.2186 0.2253 0.2365 0.0190  -0.0098 0.0346  1864 LEU A O   
557  C CB  . LEU A 71  ? 0.2851 0.2824 0.3145 0.0102  -0.0127 0.0254  1864 LEU A CB  
558  C CG  . LEU A 71  ? 0.2734 0.2643 0.3038 -0.0052 -0.0088 0.0223  1864 LEU A CG  
559  C CD1 . LEU A 71  ? 0.2408 0.2584 0.2881 -0.0090 -0.0143 0.0167  1864 LEU A CD1 
560  C CD2 . LEU A 71  ? 0.2752 0.2665 0.3056 -0.0144 -0.0015 0.0256  1864 LEU A CD2 
561  N N   . VAL A 72  ? 0.1803 0.2070 0.2066 0.0292  -0.0184 0.0277  1865 VAL A N   
562  C CA  . VAL A 72  ? 0.1491 0.1952 0.1775 0.0264  -0.0192 0.0247  1865 VAL A CA  
563  C C   . VAL A 72  ? 0.1654 0.2115 0.1796 0.0334  -0.0207 0.0292  1865 VAL A C   
564  O O   . VAL A 72  ? 0.2368 0.2831 0.2460 0.0275  -0.0178 0.0294  1865 VAL A O   
565  C CB  . VAL A 72  ? 0.1728 0.2427 0.2089 0.0260  -0.0219 0.0170  1865 VAL A CB  
566  C CG1 . VAL A 72  ? 0.2617 0.3489 0.2958 0.0163  -0.0206 0.0106  1865 VAL A CG1 
567  C CG2 . VAL A 72  ? 0.2142 0.2772 0.2571 0.0202  -0.0188 0.0140  1865 VAL A CG2 
568  N N   . PHE A 73  ? 0.1837 0.2259 0.1862 0.0491  -0.0242 0.0336  1866 PHE A N   
569  C CA  . PHE A 73  ? 0.2384 0.2801 0.2204 0.0617  -0.0267 0.0396  1866 PHE A CA  
570  C C   . PHE A 73  ? 0.2791 0.2815 0.2411 0.0589  -0.0180 0.0486  1866 PHE A C   
571  O O   . PHE A 73  ? 0.2596 0.2591 0.2043 0.0621  -0.0172 0.0529  1866 PHE A O   
572  C CB  . PHE A 73  ? 0.2387 0.2888 0.2095 0.0867  -0.0326 0.0429  1866 PHE A CB  
573  C CG  . PHE A 73  ? 0.2605 0.3513 0.2536 0.0887  -0.0382 0.0334  1866 PHE A CG  
574  C CD1 . PHE A 73  ? 0.2430 0.3746 0.2548 0.0728  -0.0414 0.0223  1866 PHE A CD1 
575  C CD2 . PHE A 73  ? 0.2719 0.3555 0.2637 0.1041  -0.0373 0.0346  1866 PHE A CD2 
576  C CE1 . PHE A 73  ? 0.2551 0.4239 0.2862 0.0700  -0.0432 0.0124  1866 PHE A CE1 
577  C CE2 . PHE A 73  ? 0.3365 0.4602 0.3493 0.1052  -0.0401 0.0254  1866 PHE A CE2 
578  C CZ  . PHE A 73  ? 0.2563 0.4246 0.2901 0.0867  -0.0428 0.0142  1866 PHE A CZ  
579  N N   . ASP A 74  ? 0.2391 0.2120 0.2002 0.0513  -0.0105 0.0504  1867 ASP A N   
580  C CA  . ASP A 74  ? 0.2818 0.2212 0.2255 0.0418  0.0008  0.0563  1867 ASP A CA  
581  C C   . ASP A 74  ? 0.2884 0.2453 0.2482 0.0260  0.0048  0.0533  1867 ASP A C   
582  O O   . ASP A 74  ? 0.2791 0.2233 0.2227 0.0236  0.0121  0.0582  1867 ASP A O   
583  C CB  . ASP A 74  ? 0.4151 0.3240 0.3544 0.0313  0.0088  0.0551  1867 ASP A CB  
584  C CG  . ASP A 74  ? 0.4492 0.3165 0.3540 0.0487  0.0123  0.0612  1867 ASP A CG  
585  O OD1 . ASP A 74  ? 0.3824 0.2431 0.2633 0.0726  0.0093  0.0693  1867 ASP A OD1 
586  O OD2 . ASP A 74  ? 0.4173 0.2574 0.3154 0.0398  0.0186  0.0577  1867 ASP A OD2 
587  N N   . ASN A 75  ? 0.2101 0.1927 0.1974 0.0179  0.0017  0.0459  1868 ASN A N   
588  C CA  . ASN A 75  ? 0.1962 0.1940 0.1944 0.0102  0.0062  0.0435  1868 ASN A CA  
589  C C   . ASN A 75  ? 0.2036 0.2056 0.1872 0.0155  0.0051  0.0441  1868 ASN A C   
590  O O   . ASN A 75  ? 0.2329 0.2312 0.2094 0.0115  0.0131  0.0457  1868 ASN A O   
591  C CB  . ASN A 75  ? 0.2465 0.2639 0.2660 0.0082  0.0030  0.0372  1868 ASN A CB  
592  C CG  . ASN A 75  ? 0.1837 0.2050 0.2174 0.0021  0.0034  0.0353  1868 ASN A CG  
593  O OD1 . ASN A 75  ? 0.2362 0.2486 0.2672 -0.0066 0.0088  0.0367  1868 ASN A OD1 
594  N ND2 . ASN A 75  ? 0.1633 0.1968 0.2086 0.0046  -0.0014 0.0313  1868 ASN A ND2 
595  N N   . CYS A 76  ? 0.2086 0.2228 0.1877 0.0234  -0.0044 0.0413  1869 CYS A N   
596  C CA  . CYS A 76  ? 0.3284 0.3551 0.2943 0.0245  -0.0073 0.0380  1869 CYS A CA  
597  C C   . CYS A 76  ? 0.2866 0.2977 0.2250 0.0327  -0.0053 0.0465  1869 CYS A C   
598  O O   . CYS A 76  ? 0.3268 0.3372 0.2510 0.0291  -0.0016 0.0455  1869 CYS A O   
599  C CB  . CYS A 76  ? 0.3271 0.3831 0.2984 0.0281  -0.0182 0.0305  1869 CYS A CB  
600  S SG  . CYS A 76  ? 0.2277 0.3105 0.1825 0.0243  -0.0239 0.0220  1869 CYS A SG  
601  N N   . GLN A 77  ? 0.2627 0.2544 0.1869 0.0447  -0.0058 0.0553  1870 GLN A N   
602  C CA  . GLN A 77  ? 0.3046 0.2706 0.1928 0.0551  -0.0014 0.0656  1870 GLN A CA  
603  C C   . GLN A 77  ? 0.3463 0.2851 0.2279 0.0403  0.0151  0.0696  1870 GLN A C   
604  O O   . GLN A 77  ? 0.3489 0.2710 0.2017 0.0430  0.0215  0.0757  1870 GLN A O   
605  C CB  . GLN A 77  ? 0.3550 0.2956 0.2206 0.0750  -0.0030 0.0749  1870 GLN A CB  
606  C CG  . GLN A 77  ? 0.5383 0.4395 0.3550 0.0907  0.0037  0.0884  1870 GLN A CG  
607  C CD  . GLN A 77  ? 0.6339 0.5088 0.4196 0.1199  0.0012  0.0983  1870 GLN A CD  
608  O OE1 . GLN A 77  ? 0.7326 0.5737 0.4733 0.1388  0.0059  0.1098  1870 GLN A OE1 
609  N NE2 . GLN A 77  ? 0.4679 0.3563 0.2755 0.1249  -0.0045 0.0932  1870 GLN A NE2 
610  N N   . THR A 78  ? 0.3515 0.2904 0.2588 0.0249  0.0223  0.0658  1871 THR A N   
611  C CA  . THR A 78  ? 0.3320 0.2588 0.2399 0.0091  0.0385  0.0673  1871 THR A CA  
612  C C   . THR A 78  ? 0.2968 0.2425 0.2102 0.0056  0.0428  0.0635  1871 THR A C   
613  O O   . THR A 78  ? 0.3217 0.2543 0.2180 0.0006  0.0559  0.0675  1871 THR A O   
614  C CB  . THR A 78  ? 0.3777 0.3141 0.3150 -0.0052 0.0419  0.0618  1871 THR A CB  
615  O OG1 . THR A 78  ? 0.3364 0.2412 0.2574 -0.0062 0.0440  0.0650  1871 THR A OG1 
616  C CG2 . THR A 78  ? 0.4242 0.3724 0.3748 -0.0221 0.0569  0.0594  1871 THR A CG2 
617  N N   . PHE A 79  ? 0.3474 0.3180 0.2788 0.0082  0.0343  0.0557  1872 PHE A N   
618  C CA  . PHE A 79  ? 0.3914 0.3725 0.3263 0.0053  0.0412  0.0506  1872 PHE A CA  
619  C C   . PHE A 79  ? 0.4048 0.3830 0.3131 0.0093  0.0375  0.0477  1872 PHE A C   
620  O O   . PHE A 79  ? 0.3745 0.3490 0.2726 0.0068  0.0474  0.0448  1872 PHE A O   
621  C CB  . PHE A 79  ? 0.2726 0.2712 0.2336 0.0051  0.0383  0.0434  1872 PHE A CB  
622  C CG  . PHE A 79  ? 0.2588 0.2593 0.2185 0.0068  0.0490  0.0393  1872 PHE A CG  
623  C CD1 . PHE A 79  ? 0.2474 0.2391 0.1898 0.0073  0.0483  0.0323  1872 PHE A CD1 
624  C CD2 . PHE A 79  ? 0.3266 0.3383 0.3003 0.0076  0.0614  0.0412  1872 PHE A CD2 
625  C CE1 . PHE A 79  ? 0.2623 0.2441 0.1953 0.0111  0.0611  0.0286  1872 PHE A CE1 
626  C CE2 . PHE A 79  ? 0.2932 0.3057 0.2628 0.0155  0.0727  0.0383  1872 PHE A CE2 
627  C CZ  . PHE A 79  ? 0.3049 0.2963 0.2511 0.0185  0.0732  0.0327  1872 PHE A CZ  
628  N N   . ASN A 80  ? 0.4332 0.3723 0.3326 -0.0059 0.0359  0.0348  1873 ASN A N   
629  C CA  . ASN A 80  ? 0.4550 0.4172 0.3195 -0.0014 0.0264  0.0184  1873 ASN A CA  
630  C C   . ASN A 80  ? 0.4067 0.3714 0.2155 0.0134  0.0256  0.0341  1873 ASN A C   
631  O O   . ASN A 80  ? 0.4059 0.3623 0.2100 0.0214  0.0206  0.0559  1873 ASN A O   
632  C CB  . ASN A 80  ? 0.4016 0.3841 0.2865 -0.0058 0.0006  0.0058  1873 ASN A CB  
633  C CG  . ASN A 80  ? 0.3238 0.3029 0.2600 -0.0219 -0.0021 -0.0070 1873 ASN A CG  
634  O OD1 . ASN A 80  ? 0.3358 0.3184 0.2849 -0.0293 0.0003  -0.0270 1873 ASN A OD1 
635  N ND2 . ASN A 80  ? 0.2892 0.2601 0.2537 -0.0271 -0.0087 0.0039  1873 ASN A ND2 
636  N N   . GLU A 81  ? 0.4501 0.4244 0.2151 0.0175  0.0284  0.0222  1874 GLU A N   
637  C CA  . GLU A 81  ? 0.5462 0.5219 0.2517 0.0308  0.0229  0.0371  1874 GLU A CA  
638  C C   . GLU A 81  ? 0.4908 0.4844 0.1944 0.0382  -0.0095 0.0374  1874 GLU A C   
639  O O   . GLU A 81  ? 0.4713 0.4830 0.2073 0.0323  -0.0264 0.0188  1874 GLU A O   
640  C CB  . GLU A 81  ? 0.6553 0.6351 0.3082 0.0326  0.0333  0.0218  1874 GLU A CB  
641  C CG  . GLU A 81  ? 0.7708 0.7388 0.4337 0.0251  0.0682  0.0151  1874 GLU A CG  
642  C CD  . GLU A 81  ? 0.8535 0.8008 0.5149 0.0266  0.0933  0.0468  1874 GLU A CD  
643  O OE1 . GLU A 81  ? 0.9627 0.9033 0.5881 0.0357  0.0862  0.0732  1874 GLU A OE1 
644  O OE2 . GLU A 81  ? 0.8336 0.7710 0.5349 0.0183  0.1184  0.0459  1874 GLU A OE2 
645  N N   . ASP A 82  ? 0.5220 0.5110 0.1919 0.0510  -0.0182 0.0601  1875 ASP A N   
646  C CA  . ASP A 82  ? 0.6093 0.6163 0.2832 0.0601  -0.0489 0.0614  1875 ASP A CA  
647  C C   . ASP A 82  ? 0.6387 0.6691 0.2958 0.0594  -0.0700 0.0370  1875 ASP A C   
648  O O   . ASP A 82  ? 0.6578 0.7104 0.3443 0.0606  -0.0938 0.0283  1875 ASP A O   
649  C CB  . ASP A 82  ? 0.6387 0.6338 0.2775 0.0748  -0.0566 0.0900  1875 ASP A CB  
650  C CG  . ASP A 82  ? 0.6408 0.6118 0.3027 0.0764  -0.0411 0.1143  1875 ASP A CG  
651  O OD1 . ASP A 82  ? 0.6221 0.5866 0.3279 0.0667  -0.0273 0.1084  1875 ASP A OD1 
652  O OD2 . ASP A 82  ? 0.7190 0.6770 0.3721 0.0801  -0.0447 0.1342  1875 ASP A OD2 
653  N N   . ASP A 83  ? 0.5954 0.6215 0.2078 0.0573  -0.0611 0.0245  1876 ASP A N   
654  C CA  . ASP A 83  ? 0.6500 0.6935 0.2389 0.0578  -0.0835 -0.0003 1876 ASP A CA  
655  C C   . ASP A 83  ? 0.5653 0.6227 0.2031 0.0444  -0.0860 -0.0304 1876 ASP A C   
656  O O   . ASP A 83  ? 0.5781 0.6526 0.2136 0.0436  -0.1106 -0.0518 1876 ASP A O   
657  C CB  . ASP A 83  ? 0.8577 0.8871 0.3783 0.0591  -0.0716 -0.0023 1876 ASP A CB  
658  C CG  . ASP A 83  ? 1.0771 1.0905 0.5846 0.0551  -0.0322 -0.0041 1876 ASP A CG  
659  O OD1 . ASP A 83  ? 1.1360 1.1541 0.6689 0.0458  -0.0228 -0.0321 1876 ASP A OD1 
660  O OD2 . ASP A 83  ? 1.1646 1.1598 0.6485 0.0585  -0.0103 0.0232  1876 ASP A OD2 
661  N N   . SER A 84  ? 0.5194 0.5683 0.2033 0.0335  -0.0644 -0.0316 1877 SER A N   
662  C CA  . SER A 84  ? 0.4993 0.5584 0.2333 0.0198  -0.0690 -0.0566 1877 SER A CA  
663  C C   . SER A 84  ? 0.4399 0.5213 0.2203 0.0163  -0.0941 -0.0562 1877 SER A C   
664  O O   . SER A 84  ? 0.4381 0.5245 0.2227 0.0241  -0.1009 -0.0363 1877 SER A O   
665  C CB  . SER A 84  ? 0.4476 0.4894 0.2198 0.0091  -0.0424 -0.0548 1877 SER A CB  
666  O OG  . SER A 84  ? 0.4039 0.4414 0.2119 0.0072  -0.0414 -0.0338 1877 SER A OG  
667  N N   . GLU A 85  ? 0.4323 0.5277 0.2498 0.0046  -0.1074 -0.0789 1878 GLU A N   
668  C CA  . GLU A 85  ? 0.4335 0.5527 0.2995 -0.0012 -0.1277 -0.0778 1878 GLU A CA  
669  C C   . GLU A 85  ? 0.3983 0.5116 0.3008 -0.0066 -0.1137 -0.0587 1878 GLU A C   
670  O O   . GLU A 85  ? 0.3181 0.4474 0.2398 -0.0031 -0.1224 -0.0470 1878 GLU A O   
671  C CB  . GLU A 85  ? 0.3729 0.5047 0.2754 -0.0153 -0.1433 -0.1035 1878 GLU A CB  
672  C CG  . GLU A 85  ? 0.4231 0.5578 0.2940 -0.0105 -0.1605 -0.1230 1878 GLU A CG  
673  C CD  . GLU A 85  ? 0.4661 0.6111 0.3193 -0.0003 -0.1776 -0.1091 1878 GLU A CD  
674  O OE1 . GLU A 85  ? 0.5169 0.6521 0.3132 0.0107  -0.1807 -0.1096 1878 GLU A OE1 
675  O OE2 . GLU A 85  ? 0.4670 0.6288 0.3639 -0.0041 -0.1864 -0.0970 1878 GLU A OE2 
676  N N   . VAL A 86  ? 0.3236 0.4136 0.2367 -0.0146 -0.0926 -0.0565 1879 VAL A N   
677  C CA  . VAL A 86  ? 0.2837 0.3631 0.2257 -0.0198 -0.0819 -0.0394 1879 VAL A CA  
678  C C   . VAL A 86  ? 0.2944 0.3631 0.2090 -0.0047 -0.0734 -0.0171 1879 VAL A C   
679  O O   . VAL A 86  ? 0.2939 0.3669 0.2252 -0.0022 -0.0756 -0.0049 1879 VAL A O   
680  C CB  . VAL A 86  ? 0.2676 0.3237 0.2332 -0.0328 -0.0667 -0.0438 1879 VAL A CB  
681  C CG1 . VAL A 86  ? 0.2404 0.2786 0.2246 -0.0362 -0.0570 -0.0246 1879 VAL A CG1 
682  C CG2 . VAL A 86  ? 0.2716 0.3379 0.2756 -0.0488 -0.0796 -0.0631 1879 VAL A CG2 
683  N N   . GLY A 87  ? 0.3314 0.3862 0.2030 0.0058  -0.0637 -0.0115 1880 GLY A N   
684  C CA  . GLY A 87  ? 0.3471 0.3908 0.1940 0.0201  -0.0592 0.0114  1880 GLY A CA  
685  C C   . GLY A 87  ? 0.3521 0.4180 0.1967 0.0317  -0.0804 0.0164  1880 GLY A C   
686  O O   . GLY A 87  ? 0.3401 0.4034 0.1965 0.0394  -0.0811 0.0310  1880 GLY A O   
687  N N   . LYS A 88  ? 0.3736 0.4610 0.2048 0.0341  -0.0994 0.0031  1881 LYS A N   
688  C CA  . LYS A 88  ? 0.3763 0.4885 0.2171 0.0444  -0.1222 0.0063  1881 LYS A CA  
689  C C   . LYS A 88  ? 0.3304 0.4584 0.2245 0.0388  -0.1219 0.0069  1881 LYS A C   
690  O O   . LYS A 88  ? 0.3356 0.4711 0.2417 0.0502  -0.1261 0.0182  1881 LYS A O   
691  C CB  . LYS A 88  ? 0.4177 0.5519 0.2494 0.0436  -0.1459 -0.0122 1881 LYS A CB  
692  C CG  . LYS A 88  ? 0.5761 0.6967 0.3446 0.0529  -0.1511 -0.0113 1881 LYS A CG  
693  C CD  . LYS A 88  ? 0.5977 0.7302 0.3687 0.0552  -0.1759 -0.0131 1881 LYS A CD  
694  C CE  . LYS A 88  ? 0.6733 0.8120 0.4667 0.0658  -0.1837 0.0067  1881 LYS A CE  
695  N NZ  . LYS A 88  ? 0.5580 0.7223 0.3896 0.0644  -0.2072 0.0006  1881 LYS A NZ  
696  N N   . ALA A 89  ? 0.2996 0.4318 0.2252 0.0213  -0.1163 -0.0052 1882 ALA A N   
697  C CA  . ALA A 89  ? 0.2633 0.4131 0.2343 0.0134  -0.1160 -0.0048 1882 ALA A CA  
698  C C   . ALA A 89  ? 0.3060 0.4364 0.2784 0.0185  -0.1001 0.0105  1882 ALA A C   
699  O O   . ALA A 89  ? 0.2570 0.4034 0.2518 0.0230  -0.1006 0.0143  1882 ALA A O   
700  C CB  . ALA A 89  ? 0.2927 0.4454 0.2927 -0.0080 -0.1148 -0.0178 1882 ALA A CB  
701  N N   . GLY A 90  ? 0.3228 0.4191 0.2736 0.0183  -0.0857 0.0181  1883 GLY A N   
702  C CA  . GLY A 90  ? 0.3157 0.3895 0.2685 0.0231  -0.0741 0.0314  1883 GLY A CA  
703  C C   . GLY A 90  ? 0.2666 0.3416 0.2072 0.0438  -0.0792 0.0431  1883 GLY A C   
704  O O   . GLY A 90  ? 0.2579 0.3304 0.2124 0.0502  -0.0762 0.0478  1883 GLY A O   
705  N N   . HIS A 91  ? 0.2979 0.3746 0.2105 0.0551  -0.0879 0.0478  1884 HIS A N   
706  C CA  . HIS A 91  ? 0.3190 0.3973 0.2246 0.0750  -0.0976 0.0600  1884 HIS A CA  
707  C C   . HIS A 91  ? 0.3054 0.4197 0.2456 0.0810  -0.1101 0.0518  1884 HIS A C   
708  O O   . HIS A 91  ? 0.3070 0.4222 0.2618 0.0950  -0.1117 0.0578  1884 HIS A O   
709  C CB  . HIS A 91  ? 0.4589 0.5317 0.3233 0.0841  -0.1075 0.0682  1884 HIS A CB  
710  C CG  . HIS A 91  ? 0.4753 0.5135 0.3065 0.0815  -0.0910 0.0810  1884 HIS A CG  
711  N ND1 . HIS A 91  ? 0.4258 0.4349 0.2598 0.0863  -0.0796 0.0978  1884 HIS A ND1 
712  C CD2 . HIS A 91  ? 0.4073 0.4363 0.2047 0.0748  -0.0829 0.0789  1884 HIS A CD2 
713  C CE1 . HIS A 91  ? 0.4540 0.4391 0.2610 0.0816  -0.0647 0.1079  1884 HIS A CE1 
714  N NE2 . HIS A 91  ? 0.4207 0.4181 0.2037 0.0749  -0.0645 0.0961  1884 HIS A NE2 
715  N N   . ILE A 92  ? 0.2938 0.4384 0.2520 0.0708  -0.1189 0.0374  1885 ILE A N   
716  C CA  . ILE A 92  ? 0.3073 0.4905 0.3059 0.0749  -0.1290 0.0302  1885 ILE A CA  
717  C C   . ILE A 92  ? 0.2532 0.4402 0.2810 0.0691  -0.1118 0.0282  1885 ILE A C   
718  O O   . ILE A 92  ? 0.2625 0.4674 0.3156 0.0810  -0.1112 0.0281  1885 ILE A O   
719  C CB  . ILE A 92  ? 0.2783 0.4912 0.2927 0.0631  -0.1436 0.0162  1885 ILE A CB  
720  C CG1 . ILE A 92  ? 0.3190 0.5259 0.3037 0.0709  -0.1627 0.0172  1885 ILE A CG1 
721  C CG2 . ILE A 92  ? 0.3458 0.6001 0.4140 0.0603  -0.1470 0.0091  1885 ILE A CG2 
722  C CD1 . ILE A 92  ? 0.4286 0.6489 0.4215 0.0570  -0.1758 0.0027  1885 ILE A CD1 
723  N N   . MET A 93  ? 0.2895 0.4593 0.3139 0.0509  -0.0980 0.0258  1886 MET A N   
724  C CA  . MET A 93  ? 0.2501 0.4202 0.2929 0.0437  -0.0833 0.0246  1886 MET A CA  
725  C C   . MET A 93  ? 0.2780 0.4202 0.3072 0.0585  -0.0747 0.0324  1886 MET A C   
726  O O   . MET A 93  ? 0.2387 0.3878 0.2821 0.0614  -0.0654 0.0292  1886 MET A O   
727  C CB  . MET A 93  ? 0.2903 0.4449 0.3321 0.0201  -0.0756 0.0220  1886 MET A CB  
728  C CG  . MET A 93  ? 0.2647 0.4462 0.3278 0.0042  -0.0849 0.0129  1886 MET A CG  
729  S SD  . MET A 93  ? 0.2475 0.4800 0.3558 0.0006  -0.0858 0.0082  1886 MET A SD  
730  C CE  . MET A 93  ? 0.2269 0.4457 0.3325 -0.0053 -0.0639 0.0138  1886 MET A CE  
731  N N   . ARG A 94  ? 0.2432 0.3534 0.2453 0.0676  -0.0770 0.0423  1887 ARG A N   
732  C CA  . ARG A 94  ? 0.4117 0.4942 0.4068 0.0820  -0.0722 0.0500  1887 ARG A CA  
733  C C   . ARG A 94  ? 0.3553 0.4598 0.3691 0.1034  -0.0797 0.0485  1887 ARG A C   
734  O O   . ARG A 94  ? 0.3763 0.4764 0.4018 0.1125  -0.0727 0.0445  1887 ARG A O   
735  C CB  . ARG A 94  ? 0.3373 0.3821 0.3048 0.0861  -0.0728 0.0641  1887 ARG A CB  
736  C CG  . ARG A 94  ? 0.4222 0.4338 0.3880 0.0987  -0.0696 0.0726  1887 ARG A CG  
737  C CD  . ARG A 94  ? 0.3120 0.2927 0.2569 0.1065  -0.0724 0.0909  1887 ARG A CD  
738  N NE  . ARG A 94  ? 0.3081 0.2699 0.2380 0.0902  -0.0629 0.0958  1887 ARG A NE  
739  C CZ  . ARG A 94  ? 0.3704 0.3005 0.3046 0.0807  -0.0535 0.0990  1887 ARG A CZ  
740  N NH1 . ARG A 94  ? 0.3103 0.2242 0.2608 0.0823  -0.0535 0.0955  1887 ARG A NH1 
741  N NH2 . ARG A 94  ? 0.3624 0.2799 0.2902 0.0670  -0.0444 0.1024  1887 ARG A NH2 
742  N N   . ARG A 95  ? 0.2796 0.4076 0.2976 0.1122  -0.0953 0.0502  1888 ARG A N   
743  C CA  . ARG A 95  ? 0.3349 0.4860 0.3793 0.1330  -0.1056 0.0486  1888 ARG A CA  
744  C C   . ARG A 95  ? 0.2889 0.4779 0.3727 0.1304  -0.0958 0.0338  1888 ARG A C   
745  O O   . ARG A 95  ? 0.2802 0.4787 0.3881 0.1469  -0.0924 0.0288  1888 ARG A O   
746  C CB  . ARG A 95  ? 0.3520 0.5202 0.3927 0.1409  -0.1285 0.0537  1888 ARG A CB  
747  C CG  . ARG A 95  ? 0.3920 0.5879 0.4729 0.1552  -0.1395 0.0492  1888 ARG A CG  
748  C CD  . ARG A 95  ? 0.4758 0.6440 0.5461 0.1672  -0.1521 0.0633  1888 ARG A CD  
749  N NE  . ARG A 95  ? 0.4428 0.6356 0.5582 0.1817  -0.1623 0.0596  1888 ARG A NE  
750  C CZ  . ARG A 95  ? 0.4693 0.6993 0.6157 0.1805  -0.1750 0.0532  1888 ARG A CZ  
751  N NH1 . ARG A 95  ? 0.4657 0.7109 0.6013 0.1648  -0.1802 0.0485  1888 ARG A NH1 
752  N NH2 . ARG A 95  ? 0.5288 0.7798 0.7204 0.1942  -0.1827 0.0512  1888 ARG A NH2 
753  N N   . PHE A 96  ? 0.3385 0.5503 0.4316 0.1099  -0.0907 0.0265  1889 PHE A N   
754  C CA  . PHE A 96  ? 0.3456 0.5940 0.4750 0.1041  -0.0778 0.0156  1889 PHE A CA  
755  C C   . PHE A 96  ? 0.3136 0.5406 0.4322 0.1039  -0.0570 0.0124  1889 PHE A C   
756  O O   . PHE A 96  ? 0.2740 0.5206 0.4157 0.1158  -0.0463 0.0040  1889 PHE A O   
757  C CB  . PHE A 96  ? 0.2530 0.5240 0.3935 0.0794  -0.0775 0.0117  1889 PHE A CB  
758  C CG  . PHE A 96  ? 0.2336 0.5432 0.4115 0.0703  -0.0622 0.0044  1889 PHE A CG  
759  C CD1 . PHE A 96  ? 0.1995 0.4984 0.3656 0.0512  -0.0436 0.0045  1889 PHE A CD1 
760  C CD2 . PHE A 96  ? 0.3285 0.6853 0.5545 0.0806  -0.0662 -0.0013 1889 PHE A CD2 
761  C CE1 . PHE A 96  ? 0.1960 0.5306 0.3914 0.0415  -0.0270 0.0005  1889 PHE A CE1 
762  C CE2 . PHE A 96  ? 0.2827 0.6780 0.5457 0.0714  -0.0480 -0.0067 1889 PHE A CE2 
763  C CZ  . PHE A 96  ? 0.2458 0.6298 0.4903 0.0513  -0.0269 -0.0051 1889 PHE A CZ  
764  N N   . PHE A 97  ? 0.2949 0.4813 0.3790 0.0912  -0.0516 0.0176  1890 PHE A N   
765  C CA  . PHE A 97  ? 0.2725 0.4314 0.3404 0.0909  -0.0370 0.0146  1890 PHE A CA  
766  C C   . PHE A 97  ? 0.2650 0.4084 0.3346 0.1171  -0.0387 0.0126  1890 PHE A C   
767  O O   . PHE A 97  ? 0.2766 0.4251 0.3532 0.1257  -0.0262 0.0017  1890 PHE A O   
768  C CB  . PHE A 97  ? 0.2388 0.3532 0.2751 0.0747  -0.0371 0.0221  1890 PHE A CB  
769  C CG  . PHE A 97  ? 0.2531 0.3303 0.2696 0.0772  -0.0290 0.0199  1890 PHE A CG  
770  C CD1 . PHE A 97  ? 0.2708 0.3503 0.2798 0.0640  -0.0166 0.0132  1890 PHE A CD1 
771  C CD2 . PHE A 97  ? 0.3612 0.4000 0.3655 0.0921  -0.0353 0.0251  1890 PHE A CD2 
772  C CE1 . PHE A 97  ? 0.3849 0.4277 0.3703 0.0665  -0.0124 0.0093  1890 PHE A CE1 
773  C CE2 . PHE A 97  ? 0.4089 0.4116 0.3971 0.0944  -0.0315 0.0211  1890 PHE A CE2 
774  C CZ  . PHE A 97  ? 0.3558 0.3598 0.3323 0.0820  -0.0209 0.0120  1890 PHE A CZ  
775  N N   . GLU A 98  ? 0.3047 0.4269 0.3664 0.1299  -0.0537 0.0230  1891 GLU A N   
776  C CA  . GLU A 98  ? 0.4189 0.5245 0.4878 0.1550  -0.0589 0.0230  1891 GLU A CA  
777  C C   . GLU A 98  ? 0.3828 0.5307 0.4920 0.1733  -0.0588 0.0113  1891 GLU A C   
778  O O   . GLU A 98  ? 0.3521 0.4911 0.4739 0.1930  -0.0565 0.0035  1891 GLU A O   
779  C CB  . GLU A 98  ? 0.4199 0.4982 0.4740 0.1635  -0.0761 0.0407  1891 GLU A CB  
780  C CG  . GLU A 98  ? 0.4391 0.4705 0.4616 0.1511  -0.0734 0.0521  1891 GLU A CG  
781  C CD  . GLU A 98  ? 0.4663 0.4748 0.4746 0.1563  -0.0855 0.0712  1891 GLU A CD  
782  O OE1 . GLU A 98  ? 0.5846 0.6136 0.6013 0.1626  -0.0967 0.0749  1891 GLU A OE1 
783  O OE2 . GLU A 98  ? 0.5707 0.5419 0.5643 0.1442  -0.0804 0.0807  1891 GLU A OE2 
784  N N   . SER A 99  ? 0.3563 0.5502 0.4910 0.1677  -0.0620 0.0087  1892 SER A N   
785  C CA  . SER A 99  ? 0.3864 0.6233 0.5691 0.1852  -0.0619 -0.0023 1892 SER A CA  
786  C C   . SER A 99  ? 0.3769 0.6370 0.5748 0.1813  -0.0349 -0.0190 1892 SER A C   
787  O O   . SER A 99  ? 0.4095 0.6816 0.6339 0.2017  -0.0268 -0.0317 1892 SER A O   
788  C CB  . SER A 99  ? 0.4541 0.7323 0.6647 0.1811  -0.0780 0.0010  1892 SER A CB  
789  O OG  . SER A 99  ? 0.5522 0.8610 0.7727 0.1580  -0.0656 -0.0042 1892 SER A OG  
790  N N   . ARG A 100 ? 0.3082 0.5737 0.4886 0.1555  -0.0206 -0.0190 1893 ARG A N   
791  C CA  . ARG A 100 ? 0.2846 0.5696 0.4694 0.1488  0.0065  -0.0316 1893 ARG A CA  
792  C C   . ARG A 100 ? 0.4479 0.6901 0.5983 0.1580  0.0169  -0.0395 1893 ARG A C   
793  O O   . ARG A 100 ? 0.4857 0.7426 0.6450 0.1684  0.0367  -0.0555 1893 ARG A O   
794  C CB  . ARG A 100 ? 0.3321 0.6277 0.5042 0.1171  0.0149  -0.0255 1893 ARG A CB  
795  C CG  . ARG A 100 ? 0.3161 0.6578 0.5289 0.1072  0.0052  -0.0213 1893 ARG A CG  
796  C CD  . ARG A 100 ? 0.2949 0.6915 0.5648 0.1214  0.0154  -0.0320 1893 ARG A CD  
797  N NE  . ARG A 100 ? 0.3003 0.7308 0.5846 0.1047  0.0434  -0.0364 1893 ARG A NE  
798  C CZ  . ARG A 100 ? 0.3146 0.7844 0.6354 0.1167  0.0662  -0.0487 1893 ARG A CZ  
799  N NH1 . ARG A 100 ? 0.3594 0.8380 0.7101 0.1467  0.0619  -0.0595 1893 ARG A NH1 
800  N NH2 . ARG A 100 ? 0.2735 0.7737 0.6023 0.0987  0.0942  -0.0497 1893 ARG A NH2 
801  N N   . TRP A 101 ? 0.3864 0.5757 0.4993 0.1549  0.0038  -0.0297 1894 TRP A N   
802  C CA  . TRP A 101 ? 0.3748 0.5184 0.4558 0.1615  0.0089  -0.0368 1894 TRP A CA  
803  C C   . TRP A 101 ? 0.4194 0.5588 0.5222 0.1929  0.0065  -0.0492 1894 TRP A C   
804  O O   . TRP A 101 ? 0.5359 0.6559 0.6240 0.2023  0.0176  -0.0649 1894 TRP A O   
805  C CB  . TRP A 101 ? 0.3479 0.4390 0.3959 0.1510  -0.0065 -0.0216 1894 TRP A CB  
806  C CG  . TRP A 101 ? 0.3716 0.4141 0.3871 0.1516  -0.0040 -0.0279 1894 TRP A CG  
807  C CD1 . TRP A 101 ? 0.4513 0.4540 0.4635 0.1705  -0.0144 -0.0302 1894 TRP A CD1 
808  C CD2 . TRP A 101 ? 0.3612 0.3874 0.3434 0.1321  0.0064  -0.0323 1894 TRP A CD2 
809  N NE1 . TRP A 101 ? 0.4984 0.4610 0.4782 0.1642  -0.0119 -0.0378 1894 TRP A NE1 
810  C CE2 . TRP A 101 ? 0.4425 0.4182 0.4008 0.1407  0.0003  -0.0388 1894 TRP A CE2 
811  C CE3 . TRP A 101 ? 0.3980 0.4452 0.3687 0.1073  0.0178  -0.0300 1894 TRP A CE3 
812  C CZ2 . TRP A 101 ? 0.4483 0.3937 0.3679 0.1260  0.0040  -0.0442 1894 TRP A CZ2 
813  C CZ3 . TRP A 101 ? 0.4604 0.4775 0.3922 0.0923  0.0224  -0.0330 1894 TRP A CZ3 
814  C CH2 . TRP A 101 ? 0.4012 0.3679 0.3062 0.1019  0.0149  -0.0405 1894 TRP A CH2 
815  N N   . GLU A 102 ? 0.4182 0.5735 0.5556 0.2097  -0.0098 -0.0431 1895 GLU A N   
816  C CA  . GLU A 102 ? 0.4775 0.6254 0.6420 0.2404  -0.0174 -0.0524 1895 GLU A CA  
817  C C   . GLU A 102 ? 0.5163 0.7164 0.7281 0.2564  -0.0018 -0.0725 1895 GLU A C   
818  O O   . GLU A 102 ? 0.5416 0.7347 0.7734 0.2811  0.0006  -0.0887 1895 GLU A O   
819  C CB  . GLU A 102 ? 0.5968 0.7304 0.7730 0.2508  -0.0458 -0.0328 1895 GLU A CB  
820  C CG  . GLU A 102 ? 0.7427 0.8135 0.8837 0.2477  -0.0594 -0.0171 1895 GLU A CG  
821  C CD  . GLU A 102 ? 0.8093 0.8553 0.9070 0.2212  -0.0537 -0.0076 1895 GLU A CD  
822  O OE1 . GLU A 102 ? 0.7907 0.8633 0.8806 0.2013  -0.0405 -0.0114 1895 GLU A OE1 
823  O OE2 . GLU A 102 ? 0.8641 0.8627 0.9398 0.2186  -0.0630 0.0050  1895 GLU A OE2 
824  N N   . GLU A 103 ? 0.5514 0.8039 0.7863 0.2429  0.0094  -0.0726 1896 GLU A N   
825  C CA  . GLU A 103 ? 0.6065 0.9122 0.8885 0.2544  0.0310  -0.0922 1896 GLU A CA  
826  C C   . GLU A 103 ? 0.5589 0.8701 0.8117 0.2416  0.0650  -0.1069 1896 GLU A C   
827  O O   . GLU A 103 ? 0.5884 0.9497 0.8748 0.2437  0.0901  -0.1205 1896 GLU A O   
828  C CB  . GLU A 103 ? 0.6782 1.0408 1.0103 0.2477  0.0249  -0.0848 1896 GLU A CB  
829  C CG  . GLU A 103 ? 0.6988 1.0699 1.0085 0.2151  0.0234  -0.0691 1896 GLU A CG  
830  C CD  . GLU A 103 ? 0.6197 1.0275 0.9728 0.2133  0.0009  -0.0590 1896 GLU A CD  
831  O OE1 . GLU A 103 ? 0.6148 1.0405 1.0150 0.2303  -0.0087 -0.0622 1896 GLU A OE1 
832  O OE2 . GLU A 103 ? 0.5527 0.9594 0.8872 0.1900  -0.0085 -0.0462 1896 GLU A OE2 
833  N N   . PHE A 104 ? 0.5563 0.8169 0.7474 0.2279  0.0660  -0.1035 1897 PHE A N   
834  C CA  . PHE A 104 ? 0.5220 0.7722 0.6732 0.2210  0.0928  -0.1190 1897 PHE A CA  
835  C C   . PHE A 104 ? 0.5980 0.7889 0.7144 0.2374  0.0847  -0.1309 1897 PHE A C   
836  O O   . PHE A 104 ? 0.6208 0.8137 0.7386 0.2565  0.1017  -0.1558 1897 PHE A O   
837  C CB  . PHE A 104 ? 0.5646 0.8078 0.6727 0.1855  0.0990  -0.1040 1897 PHE A CB  
838  C CG  . PHE A 104 ? 0.6095 0.9095 0.7516 0.1669  0.1087  -0.0941 1897 PHE A CG  
839  C CD1 . PHE A 104 ? 0.6956 1.0554 0.8919 0.1782  0.1282  -0.1058 1897 PHE A CD1 
840  C CD2 . PHE A 104 ? 0.5054 0.7990 0.6310 0.1382  0.0978  -0.0740 1897 PHE A CD2 
841  C CE1 . PHE A 104 ? 0.6517 1.0635 0.8857 0.1600  0.1353  -0.0959 1897 PHE A CE1 
842  C CE2 . PHE A 104 ? 0.4974 0.8405 0.6579 0.1208  0.1038  -0.0655 1897 PHE A CE2 
843  C CZ  . PHE A 104 ? 0.5798 0.9819 0.7947 0.1310  0.1220  -0.0757 1897 PHE A CZ  
844  N N   . TYR A 105 ? 0.6947 0.8333 0.7831 0.2309  0.0594  -0.1147 1898 TYR A N   
845  C CA  . TYR A 105 ? 0.6627 0.7409 0.7214 0.2432  0.0480  -0.1233 1898 TYR A CA  
846  C C   . TYR A 105 ? 0.5986 0.6588 0.6941 0.2696  0.0244  -0.1203 1898 TYR A C   
847  O O   . TYR A 105 ? 0.6199 0.6992 0.7537 0.2948  0.0284  -0.1374 1898 TYR A O   
848  C CB  . TYR A 105 ? 0.6191 0.6495 0.6292 0.2181  0.0355  -0.1063 1898 TYR A CB  
849  C CG  . TYR A 105 ? 0.6699 0.7138 0.6444 0.1900  0.0533  -0.1045 1898 TYR A CG  
850  C CD1 . TYR A 105 ? 0.8058 0.8280 0.7347 0.1862  0.0669  -0.1211 1898 TYR A CD1 
851  C CD2 . TYR A 105 ? 0.6212 0.6979 0.6064 0.1673  0.0552  -0.0864 1898 TYR A CD2 
852  C CE1 . TYR A 105 ? 0.7437 0.7762 0.6371 0.1594  0.0817  -0.1162 1898 TYR A CE1 
853  C CE2 . TYR A 105 ? 0.6632 0.7505 0.6196 0.1408  0.0695  -0.0825 1898 TYR A CE2 
854  C CZ  . TYR A 105 ? 0.6973 0.7623 0.6074 0.1366  0.0827  -0.0957 1898 TYR A CZ  
855  O OH  . TYR A 105 ? 0.7994 0.8724 0.6778 0.1092  0.0953  -0.0885 1898 TYR A OH  
856  N N   . HIS B 3   ? 0.7765 0.6985 0.7994 -0.0100 0.1453  0.3070  1796 HIS B N   
857  C CA  . HIS B 3   ? 0.7608 0.6741 0.7859 -0.0062 0.1331  0.2784  1796 HIS B CA  
858  C C   . HIS B 3   ? 0.7370 0.6881 0.7299 0.0188  0.1216  0.2726  1796 HIS B C   
859  O O   . HIS B 3   ? 0.7029 0.6460 0.6915 0.0269  0.1095  0.2528  1796 HIS B O   
860  C CB  . HIS B 3   ? 0.7950 0.6559 0.8332 -0.0037 0.1259  0.2692  1796 HIS B CB  
861  C CG  . HIS B 3   ? 0.8619 0.6827 0.9313 -0.0293 0.1335  0.2617  1796 HIS B CG  
862  N ND1 . HIS B 3   ? 0.8828 0.6603 0.9669 -0.0307 0.1274  0.2431  1796 HIS B ND1 
863  C CD2 . HIS B 3   ? 0.9030 0.7236 0.9909 -0.0551 0.1461  0.2676  1796 HIS B CD2 
864  C CE1 . HIS B 3   ? 0.9225 0.6730 1.0311 -0.0556 0.1350  0.2364  1796 HIS B CE1 
865  N NE2 . HIS B 3   ? 0.9350 0.7103 1.0472 -0.0721 0.1461  0.2515  1796 HIS B NE2 
866  N N   . SER B 4   ? 0.7876 0.7806 0.7575 0.0304  0.1250  0.2880  1797 SER B N   
867  C CA  . SER B 4   ? 0.7959 0.8280 0.7330 0.0533  0.1133  0.2778  1797 SER B CA  
868  C C   . SER B 4   ? 0.7922 0.8612 0.7219 0.0512  0.1146  0.2596  1797 SER B C   
869  O O   . SER B 4   ? 0.8792 0.9717 0.7831 0.0687  0.1027  0.2417  1797 SER B O   
870  C CB  . SER B 4   ? 0.7948 0.8584 0.7093 0.0689  0.1149  0.2980  1797 SER B CB  
871  O OG  . SER B 4   ? 0.8556 0.9621 0.7632 0.0653  0.1261  0.3040  1797 SER B OG  
872  N N   . ASP B 5   ? 0.6900 0.7665 0.6427 0.0305  0.1280  0.2611  1798 ASP B N   
873  C CA  . ASP B 5   ? 0.6115 0.7274 0.5625 0.0293  0.1301  0.2428  1798 ASP B CA  
874  C C   . ASP B 5   ? 0.6064 0.6939 0.5750 0.0217  0.1164  0.2101  1798 ASP B C   
875  O O   . ASP B 5   ? 0.6118 0.6710 0.6117 -0.0001 0.1204  0.2078  1798 ASP B O   
876  C CB  . ASP B 5   ? 0.7034 0.8470 0.6766 0.0099  0.1464  0.2523  1798 ASP B CB  
877  C CG  . ASP B 5   ? 0.7547 0.9533 0.7214 0.0172  0.1479  0.2339  1798 ASP B CG  
878  O OD1 . ASP B 5   ? 0.7307 0.9312 0.6854 0.0310  0.1342  0.2061  1798 ASP B OD1 
879  O OD2 . ASP B 5   ? 0.7192 0.9541 0.6944 0.0099  0.1592  0.2415  1798 ASP B OD2 
880  N N   . LEU B 6   ? 0.5808 0.6754 0.5295 0.0389  0.0996  0.1829  1799 LEU B N   
881  C CA  . LEU B 6   ? 0.4667 0.5383 0.4278 0.0345  0.0854  0.1527  1799 LEU B CA  
882  C C   . LEU B 6   ? 0.4088 0.5080 0.3837 0.0279  0.0865  0.1339  1799 LEU B C   
883  O O   . LEU B 6   ? 0.5455 0.6361 0.5231 0.0304  0.0737  0.1093  1799 LEU B O   
884  C CB  . LEU B 6   ? 0.4515 0.5150 0.3875 0.0541  0.0674  0.1354  1799 LEU B CB  
885  C CG  . LEU B 6   ? 0.5126 0.5419 0.4465 0.0578  0.0590  0.1413  1799 LEU B CG  
886  C CD1 . LEU B 6   ? 0.5629 0.5584 0.5204 0.0452  0.0525  0.1247  1799 LEU B CD1 
887  C CD2 . LEU B 6   ? 0.5075 0.5287 0.4422 0.0576  0.0711  0.1758  1799 LEU B CD2 
888  N N   . THR B 7   ? 0.3673 0.5026 0.3524 0.0198  0.1019  0.1471  1800 THR B N   
889  C CA  . THR B 7   ? 0.3709 0.5426 0.3704 0.0167  0.1033  0.1308  1800 THR B CA  
890  C C   . THR B 7   ? 0.3288 0.4832 0.3593 -0.0041 0.0983  0.1166  1800 THR B C   
891  O O   . THR B 7   ? 0.3672 0.5326 0.4010 0.0016  0.0879  0.0947  1800 THR B O   
892  C CB  . THR B 7   ? 0.3753 0.5964 0.3826 0.0109  0.1226  0.1503  1800 THR B CB  
893  O OG1 . THR B 7   ? 0.4511 0.6985 0.4248 0.0343  0.1261  0.1582  1800 THR B OG1 
894  C CG2 . THR B 7   ? 0.3539 0.6184 0.3830 0.0066  0.1242  0.1345  1800 THR B CG2 
895  N N   . PHE B 8   ? 0.3363 0.4637 0.3892 -0.0274 0.1057  0.1285  1801 PHE B N   
896  C CA  . PHE B 8   ? 0.3650 0.4764 0.4455 -0.0480 0.1005  0.1110  1801 PHE B CA  
897  C C   . PHE B 8   ? 0.3603 0.4452 0.4283 -0.0358 0.0824  0.0889  1801 PHE B C   
898  O O   . PHE B 8   ? 0.2925 0.3882 0.3722 -0.0411 0.0741  0.0690  1801 PHE B O   
899  C CB  . PHE B 8   ? 0.4885 0.5624 0.5918 -0.0724 0.1110  0.1247  1801 PHE B CB  
900  C CG  . PHE B 8   ? 0.6981 0.7929 0.8185 -0.0898 0.1308  0.1505  1801 PHE B CG  
901  C CD1 . PHE B 8   ? 0.7538 0.9088 0.8770 -0.0888 0.1384  0.1546  1801 PHE B CD1 
902  C CD2 . PHE B 8   ? 0.7851 0.8389 0.9205 -0.1067 0.1431  0.1721  1801 PHE B CD2 
903  C CE1 . PHE B 8   ? 0.7471 0.9262 0.8876 -0.1067 0.1582  0.1805  1801 PHE B CE1 
904  C CE2 . PHE B 8   ? 0.8453 0.9149 0.9955 -0.1243 0.1612  0.1971  1801 PHE B CE2 
905  C CZ  . PHE B 8   ? 0.7949 0.9281 0.9465 -0.1250 0.1682  0.2001  1801 PHE B CZ  
906  N N   . CYS B 9   ? 0.4694 0.5244 0.5142 -0.0196 0.0762  0.0936  1802 CYS B N   
907  C CA  . CYS B 9   ? 0.4538 0.4857 0.4881 -0.0096 0.0603  0.0753  1802 CYS B CA  
908  C C   . CYS B 9   ? 0.2519 0.3087 0.2739 0.0054  0.0504  0.0592  1802 CYS B C   
909  O O   . CYS B 9   ? 0.2375 0.2874 0.2627 0.0053  0.0399  0.0431  1802 CYS B O   
910  C CB  . CYS B 9   ? 0.2822 0.2862 0.2968 0.0041  0.0563  0.0851  1802 CYS B CB  
911  S SG  . CYS B 9   ? 0.3971 0.3602 0.4279 -0.0081 0.0654  0.1024  1802 CYS B SG  
912  N N   . GLU B 10  ? 0.2584 0.3433 0.2654 0.0199  0.0541  0.0640  1803 GLU B N   
913  C CA  . GLU B 10  ? 0.3207 0.4267 0.3190 0.0360  0.0467  0.0487  1803 GLU B CA  
914  C C   . GLU B 10  ? 0.2340 0.3653 0.2562 0.0261  0.0469  0.0405  1803 GLU B C   
915  O O   . GLU B 10  ? 0.2731 0.4039 0.2942 0.0344  0.0363  0.0273  1803 GLU B O   
916  C CB  . GLU B 10  ? 0.3427 0.4789 0.3229 0.0534  0.0536  0.0536  1803 GLU B CB  
917  C CG  . GLU B 10  ? 0.2780 0.3966 0.2310 0.0653  0.0505  0.0585  1803 GLU B CG  
918  C CD  . GLU B 10  ? 0.5240 0.6777 0.4565 0.0815  0.0589  0.0637  1803 GLU B CD  
919  O OE1 . GLU B 10  ? 0.5253 0.6724 0.4319 0.0941  0.0539  0.0627  1803 GLU B OE1 
920  O OE2 . GLU B 10  ? 0.5299 0.7226 0.4720 0.0816  0.0705  0.0678  1803 GLU B OE2 
921  N N   . ILE B 11  ? 0.2398 0.3942 0.2848 0.0070  0.0586  0.0494  1804 ILE B N   
922  C CA  A ILE B 11  ? 0.2391 0.4276 0.3097 -0.0050 0.0584  0.0407  1804 ILE B CA  
923  C CA  B ILE B 11  ? 0.2367 0.4251 0.3072 -0.0049 0.0583  0.0406  1804 ILE B CA  
924  C C   . ILE B 11  ? 0.2170 0.3819 0.2961 -0.0162 0.0473  0.0271  1804 ILE B C   
925  O O   . ILE B 11  ? 0.2268 0.4096 0.3085 -0.0098 0.0377  0.0154  1804 ILE B O   
926  C CB  A ILE B 11  ? 0.2430 0.4599 0.3394 -0.0282 0.0739  0.0529  1804 ILE B CB  
927  C CB  B ILE B 11  ? 0.2478 0.4659 0.3440 -0.0277 0.0738  0.0527  1804 ILE B CB  
928  C CG1 A ILE B 11  ? 0.2554 0.5095 0.3435 -0.0155 0.0862  0.0669  1804 ILE B CG1 
929  C CG1 B ILE B 11  ? 0.2512 0.5144 0.3415 -0.0134 0.0844  0.0630  1804 ILE B CG1 
930  C CG2 A ILE B 11  ? 0.2682 0.5209 0.3948 -0.0462 0.0714  0.0406  1804 ILE B CG2 
931  C CG2 B ILE B 11  ? 0.2586 0.5043 0.3856 -0.0488 0.0712  0.0403  1804 ILE B CG2 
932  C CD1 A ILE B 11  ? 0.2738 0.5551 0.3870 -0.0402 0.1041  0.0843  1804 ILE B CD1 
933  C CD1 B ILE B 11  ? 0.2383 0.5317 0.3211 0.0117  0.0759  0.0491  1804 ILE B CD1 
934  N N   . ILE B 12  ? 0.2248 0.3510 0.3074 -0.0311 0.0492  0.0294  1805 ILE B N   
935  C CA  . ILE B 12  ? 0.2174 0.3260 0.3088 -0.0427 0.0409  0.0144  1805 ILE B CA  
936  C C   . ILE B 12  ? 0.2163 0.3101 0.2872 -0.0240 0.0274  0.0063  1805 ILE B C   
937  O O   . ILE B 12  ? 0.2473 0.3509 0.3225 -0.0268 0.0191  -0.0059 1805 ILE B O   
938  C CB  . ILE B 12  ? 0.3905 0.4587 0.4914 -0.0596 0.0478  0.0182  1805 ILE B CB  
939  C CG1 . ILE B 12  ? 0.3495 0.4105 0.4670 -0.0774 0.0434  -0.0014 1805 ILE B CG1 
940  C CG2 . ILE B 12  ? 0.4902 0.5191 0.5693 -0.0438 0.0456  0.0275  1805 ILE B CG2 
941  C CD1 . ILE B 12  ? 0.3898 0.4136 0.5244 -0.0966 0.0531  -0.0002 1805 ILE B CD1 
942  N N   . LEU B 13  ? 0.2718 0.3458 0.3203 -0.0057 0.0249  0.0132  1806 LEU B N   
943  C CA  . LEU B 13  ? 0.2015 0.2590 0.2334 0.0090  0.0130  0.0065  1806 LEU B CA  
944  C C   . LEU B 13  ? 0.2009 0.2863 0.2325 0.0206  0.0070  0.0012  1806 LEU B C   
945  O O   . LEU B 13  ? 0.1867 0.2702 0.2174 0.0223  -0.0016 -0.0046 1806 LEU B O   
946  C CB  . LEU B 13  ? 0.2282 0.2636 0.2388 0.0237  0.0115  0.0124  1806 LEU B CB  
947  C CG  . LEU B 13  ? 0.2054 0.2208 0.2017 0.0351  -0.0003 0.0054  1806 LEU B CG  
948  C CD1 . LEU B 13  ? 0.2125 0.2090 0.2154 0.0239  -0.0046 0.0015  1806 LEU B CD1 
949  C CD2 . LEU B 13  ? 0.2236 0.2238 0.2003 0.0478  -0.0032 0.0067  1806 LEU B CD2 
950  N N   . MET B 14  ? 0.1958 0.3095 0.2280 0.0307  0.0122  0.0047  1807 MET B N   
951  C CA  . MET B 14  ? 0.1912 0.3341 0.2259 0.0456  0.0075  0.0012  1807 MET B CA  
952  C C   . MET B 14  ? 0.2783 0.4511 0.3322 0.0325  0.0040  -0.0035 1807 MET B C   
953  O O   . MET B 14  ? 0.2679 0.4475 0.3192 0.0423  -0.0051 -0.0057 1807 MET B O   
954  C CB  . MET B 14  ? 0.2415 0.4183 0.2779 0.0579  0.0162  0.0048  1807 MET B CB  
955  C CG  . MET B 14  ? 0.3527 0.5657 0.3956 0.0764  0.0127  0.0019  1807 MET B CG  
956  S SD  . MET B 14  ? 0.4254 0.6933 0.4780 0.0866  0.0263  0.0057  1807 MET B SD  
957  C CE  . MET B 14  ? 0.4452 0.6821 0.4739 0.0893  0.0344  0.0097  1807 MET B CE  
958  N N   . GLU B 15  ? 0.1810 0.3721 0.2545 0.0096  0.0111  -0.0049 1808 GLU B N   
959  C CA  . GLU B 15  ? 0.2690 0.4923 0.3612 -0.0059 0.0067  -0.0142 1808 GLU B CA  
960  C C   . GLU B 15  ? 0.2735 0.4710 0.3571 -0.0104 -0.0022 -0.0218 1808 GLU B C   
961  O O   . GLU B 15  ? 0.2690 0.4955 0.3564 -0.0103 -0.0103 -0.0281 1808 GLU B O   
962  C CB  . GLU B 15  ? 0.2312 0.4715 0.3480 -0.0336 0.0167  -0.0169 1808 GLU B CB  
963  C CG  . GLU B 15  ? 0.1873 0.4660 0.3165 -0.0317 0.0270  -0.0076 1808 GLU B CG  
964  C CD  . GLU B 15  ? 0.3594 0.6487 0.5147 -0.0625 0.0387  -0.0067 1808 GLU B CD  
965  O OE1 . GLU B 15  ? 0.3629 0.6972 0.5356 -0.0674 0.0477  -0.0001 1808 GLU B OE1 
966  O OE2 . GLU B 15  ? 0.3683 0.6203 0.5283 -0.0820 0.0398  -0.0124 1808 GLU B OE2 
967  N N   . MET B 16  ? 0.2129 0.3622 0.2848 -0.0130 -0.0007 -0.0207 1809 MET B N   
968  C CA  . MET B 16  ? 0.1883 0.3171 0.2521 -0.0156 -0.0076 -0.0275 1809 MET B CA  
969  C C   . MET B 16  ? 0.2903 0.4177 0.3376 0.0044  -0.0168 -0.0216 1809 MET B C   
970  O O   . MET B 16  ? 0.2743 0.4159 0.3193 0.0038  -0.0234 -0.0250 1809 MET B O   
971  C CB  . MET B 16  ? 0.1751 0.2580 0.2335 -0.0210 -0.0032 -0.0265 1809 MET B CB  
972  C CG  . MET B 16  ? 0.2227 0.2985 0.2991 -0.0424 0.0048  -0.0340 1809 MET B CG  
973  S SD  . MET B 16  ? 0.2729 0.2983 0.3454 -0.0452 0.0082  -0.0355 1809 MET B SD  
974  C CE  . MET B 16  ? 0.2418 0.2452 0.2978 -0.0276 0.0101  -0.0157 1809 MET B CE  
975  N N   . GLU B 17  ? 0.1997 0.3092 0.2349 0.0219  -0.0169 -0.0128 1810 GLU B N   
976  C CA  . GLU B 17  ? 0.1759 0.2759 0.1980 0.0403  -0.0245 -0.0068 1810 GLU B CA  
977  C C   . GLU B 17  ? 0.2275 0.3689 0.2559 0.0496  -0.0292 -0.0040 1810 GLU B C   
978  O O   . GLU B 17  ? 0.2791 0.4198 0.3004 0.0574  -0.0361 0.0021  1810 GLU B O   
979  C CB  . GLU B 17  ? 0.3287 0.4038 0.3390 0.0567  -0.0232 -0.0031 1810 GLU B CB  
980  C CG  . GLU B 17  ? 0.2498 0.2889 0.2511 0.0509  -0.0213 -0.0045 1810 GLU B CG  
981  C CD  . GLU B 17  ? 0.3059 0.3339 0.2958 0.0651  -0.0191 -0.0048 1810 GLU B CD  
982  O OE1 . GLU B 17  ? 0.2913 0.2906 0.2697 0.0659  -0.0216 -0.0066 1810 GLU B OE1 
983  O OE2 . GLU B 17  ? 0.3037 0.3569 0.2965 0.0757  -0.0149 -0.0047 1810 GLU B OE2 
984  N N   . SER B 18  ? 0.2553 0.4372 0.2981 0.0489  -0.0255 -0.0063 1811 SER B N   
985  C CA  A SER B 18  ? 0.2564 0.4867 0.3077 0.0609  -0.0305 -0.0030 1811 SER B CA  
986  C CA  B SER B 18  ? 0.2565 0.4865 0.3076 0.0609  -0.0305 -0.0029 1811 SER B CA  
987  C C   . SER B 18  ? 0.2262 0.4979 0.2889 0.0434  -0.0351 -0.0108 1811 SER B C   
988  O O   . SER B 18  ? 0.3100 0.6325 0.3812 0.0517  -0.0405 -0.0086 1811 SER B O   
989  C CB  A SER B 18  ? 0.2440 0.5083 0.3079 0.0699  -0.0242 -0.0024 1811 SER B CB  
990  C CB  B SER B 18  ? 0.2532 0.5164 0.3166 0.0706  -0.0243 -0.0022 1811 SER B CB  
991  O OG  A SER B 18  ? 0.2085 0.5053 0.2924 0.0458  -0.0180 -0.0103 1811 SER B OG  
992  O OG  B SER B 18  ? 0.1932 0.4227 0.2431 0.0900  -0.0206 0.0018  1811 SER B OG  
993  N N   . HIS B 19  ? 0.2030 0.4569 0.2660 0.0211  -0.0335 -0.0212 1812 HIS B N   
994  C CA  . HIS B 19  ? 0.2206 0.5123 0.2937 0.0027  -0.0374 -0.0348 1812 HIS B CA  
995  C C   . HIS B 19  ? 0.2071 0.5127 0.2652 0.0137  -0.0470 -0.0291 1812 HIS B C   
996  O O   . HIS B 19  ? 0.2490 0.5168 0.2898 0.0262  -0.0482 -0.0169 1812 HIS B O   
997  C CB  . HIS B 19  ? 0.1729 0.4341 0.2509 -0.0217 -0.0312 -0.0496 1812 HIS B CB  
998  C CG  . HIS B 19  ? 0.2110 0.5092 0.3046 -0.0446 -0.0331 -0.0703 1812 HIS B CG  
999  N ND1 . HIS B 19  ? 0.1844 0.5069 0.2696 -0.0468 -0.0411 -0.0803 1812 HIS B ND1 
1000 C CD2 . HIS B 19  ? 0.2278 0.5428 0.3450 -0.0679 -0.0278 -0.0845 1812 HIS B CD2 
1001 C CE1 . HIS B 19  ? 0.2407 0.5914 0.3415 -0.0691 -0.0411 -0.1025 1812 HIS B CE1 
1002 N NE2 . HIS B 19  ? 0.2224 0.5686 0.3452 -0.0838 -0.0335 -0.1059 1812 HIS B NE2 
1003 N N   . ASP B 20  ? 0.2378 0.6021 0.3034 0.0081  -0.0538 -0.0371 1813 ASP B N   
1004 C CA  . ASP B 20  ? 0.2612 0.6466 0.3105 0.0195  -0.0618 -0.0285 1813 ASP B CA  
1005 C C   . ASP B 20  ? 0.2429 0.5970 0.2766 0.0116  -0.0613 -0.0322 1813 ASP B C   
1006 O O   . ASP B 20  ? 0.2004 0.5515 0.2168 0.0253  -0.0651 -0.0157 1813 ASP B O   
1007 C CB  . ASP B 20  ? 0.3135 0.7483 0.3671 0.0113  -0.0623 -0.0390 1813 ASP B CB  
1008 C CG  . ASP B 20  ? 0.3946 0.8626 0.4540 0.0291  -0.0634 -0.0262 1813 ASP B CG  
1009 O OD1 . ASP B 20  ? 0.3999 0.8482 0.4590 0.0493  -0.0627 -0.0098 1813 ASP B OD1 
1010 O OD2 . ASP B 20  ? 0.3728 0.8866 0.4364 0.0240  -0.0647 -0.0337 1813 ASP B OD2 
1011 N N   . ALA B 21  ? 0.1876 0.5153 0.2277 -0.0095 -0.0548 -0.0516 1814 ALA B N   
1012 C CA  . ALA B 21  ? 0.2414 0.5419 0.2690 -0.0161 -0.0523 -0.0578 1814 ALA B CA  
1013 C C   . ALA B 21  ? 0.2950 0.5327 0.3161 -0.0101 -0.0461 -0.0458 1814 ALA B C   
1014 O O   . ALA B 21  ? 0.2845 0.4968 0.3013 -0.0174 -0.0419 -0.0532 1814 ALA B O   
1015 C CB  . ALA B 21  ? 0.2579 0.5654 0.2970 -0.0398 -0.0488 -0.0879 1814 ALA B CB  
1016 N N   . ALA B 22  ? 0.2597 0.4756 0.2803 0.0038  -0.0456 -0.0294 1815 ALA B N   
1017 C CA  . ALA B 22  ? 0.2861 0.4477 0.3014 0.0079  -0.0411 -0.0217 1815 ALA B CA  
1018 C C   . ALA B 22  ? 0.2293 0.3702 0.2298 0.0199  -0.0442 -0.0045 1815 ALA B C   
1019 O O   . ALA B 22  ? 0.3057 0.4055 0.3025 0.0210  -0.0418 -0.0002 1815 ALA B O   
1020 C CB  . ALA B 22  ? 0.2544 0.4032 0.2759 0.0157  -0.0382 -0.0170 1815 ALA B CB  
1021 N N   . TRP B 23  ? 0.2689 0.4392 0.2617 0.0279  -0.0495 0.0066  1816 TRP B N   
1022 C CA  . TRP B 23  ? 0.3186 0.4689 0.2993 0.0386  -0.0516 0.0279  1816 TRP B CA  
1023 C C   . TRP B 23  ? 0.2942 0.4160 0.2703 0.0282  -0.0476 0.0277  1816 TRP B C   
1024 O O   . TRP B 23  ? 0.3487 0.4384 0.3203 0.0333  -0.0478 0.0433  1816 TRP B O   
1025 C CB  . TRP B 23  ? 0.2196 0.4147 0.1924 0.0479  -0.0570 0.0418  1816 TRP B CB  
1026 C CG  . TRP B 23  ? 0.3636 0.6039 0.3327 0.0351  -0.0575 0.0281  1816 TRP B CG  
1027 C CD1 . TRP B 23  ? 0.3479 0.6342 0.3244 0.0269  -0.0602 0.0076  1816 TRP B CD1 
1028 C CD2 . TRP B 23  ? 0.2750 0.5209 0.2327 0.0284  -0.0548 0.0310  1816 TRP B CD2 
1029 N NE1 . TRP B 23  ? 0.3149 0.6324 0.2836 0.0161  -0.0600 -0.0054 1816 TRP B NE1 
1030 C CE2 . TRP B 23  ? 0.2549 0.5502 0.2112 0.0182  -0.0561 0.0094  1816 TRP B CE2 
1031 C CE3 . TRP B 23  ? 0.3280 0.5447 0.2782 0.0287  -0.0510 0.0486  1816 TRP B CE3 
1032 C CZ2 . TRP B 23  ? 0.2911 0.6086 0.2358 0.0115  -0.0531 0.0042  1816 TRP B CZ2 
1033 C CZ3 . TRP B 23  ? 0.3708 0.6118 0.3118 0.0208  -0.0473 0.0465  1816 TRP B CZ3 
1034 C CH2 . TRP B 23  ? 0.3739 0.6657 0.3108 0.0139  -0.0481 0.0244  1816 TRP B CH2 
1035 N N   . PRO B 24  ? 0.2720 0.4034 0.2511 0.0141  -0.0437 0.0101  1817 PRO B N   
1036 C CA  . PRO B 24  ? 0.1971 0.3047 0.1747 0.0072  -0.0395 0.0104  1817 PRO B CA  
1037 C C   . PRO B 24  ? 0.2413 0.3068 0.2262 0.0054  -0.0373 0.0059  1817 PRO B C   
1038 O O   . PRO B 24  ? 0.2333 0.2828 0.2191 0.0008  -0.0350 0.0072  1817 PRO B O   
1039 C CB  . PRO B 24  ? 0.2525 0.3895 0.2312 -0.0032 -0.0359 -0.0095 1817 PRO B CB  
1040 C CG  . PRO B 24  ? 0.2679 0.4486 0.2450 -0.0028 -0.0400 -0.0168 1817 PRO B CG  
1041 C CD  . PRO B 24  ? 0.2943 0.4635 0.2782 0.0042  -0.0432 -0.0109 1817 PRO B CD  
1042 N N   . PHE B 25  ? 0.2408 0.2936 0.2305 0.0093  -0.0378 0.0015  1818 PHE B N   
1043 C CA  . PHE B 25  ? 0.2564 0.2801 0.2514 0.0070  -0.0350 -0.0051 1818 PHE B CA  
1044 C C   . PHE B 25  ? 0.2631 0.2622 0.2546 0.0170  -0.0376 0.0021  1818 PHE B C   
1045 O O   . PHE B 25  ? 0.2452 0.2277 0.2386 0.0169  -0.0357 -0.0027 1818 PHE B O   
1046 C CB  . PHE B 25  ? 0.2304 0.2639 0.2351 -0.0005 -0.0302 -0.0199 1818 PHE B CB  
1047 C CG  . PHE B 25  ? 0.2657 0.3219 0.2740 -0.0100 -0.0278 -0.0331 1818 PHE B CG  
1048 C CD1 . PHE B 25  ? 0.2267 0.2756 0.2349 -0.0132 -0.0248 -0.0377 1818 PHE B CD1 
1049 C CD2 . PHE B 25  ? 0.3431 0.4323 0.3553 -0.0154 -0.0287 -0.0432 1818 PHE B CD2 
1050 C CE1 . PHE B 25  ? 0.2760 0.3472 0.2860 -0.0199 -0.0218 -0.0534 1818 PHE B CE1 
1051 C CE2 . PHE B 25  ? 0.2582 0.3702 0.2721 -0.0245 -0.0270 -0.0602 1818 PHE B CE2 
1052 C CZ  . PHE B 25  ? 0.2888 0.3900 0.3006 -0.0259 -0.0231 -0.0660 1818 PHE B CZ  
1053 N N   . LEU B 26  ? 0.2599 0.2561 0.2457 0.0269  -0.0417 0.0133  1819 LEU B N   
1054 C CA  . LEU B 26  ? 0.2998 0.2725 0.2820 0.0387  -0.0439 0.0160  1819 LEU B CA  
1055 C C   . LEU B 26  ? 0.2595 0.1967 0.2381 0.0369  -0.0468 0.0182  1819 LEU B C   
1056 O O   . LEU B 26  ? 0.3376 0.2527 0.3123 0.0453  -0.0488 0.0147  1819 LEU B O   
1057 C CB  . LEU B 26  ? 0.3088 0.2920 0.2888 0.0534  -0.0467 0.0262  1819 LEU B CB  
1058 C CG  . LEU B 26  ? 0.4638 0.4840 0.4494 0.0601  -0.0454 0.0227  1819 LEU B CG  
1059 C CD1 . LEU B 26  ? 0.5533 0.5841 0.5460 0.0496  -0.0402 0.0092  1819 LEU B CD1 
1060 C CD2 . LEU B 26  ? 0.4470 0.5062 0.4339 0.0594  -0.0479 0.0290  1819 LEU B CD2 
1061 N N   . GLU B 27  ? 0.3225 0.2575 0.3032 0.0259  -0.0469 0.0224  1820 GLU B N   
1062 C CA  . GLU B 27  ? 0.3402 0.2484 0.3220 0.0198  -0.0499 0.0232  1820 GLU B CA  
1063 C C   . GLU B 27  ? 0.2869 0.2095 0.2752 0.0069  -0.0473 0.0214  1820 GLU B C   
1064 O O   . GLU B 27  ? 0.2577 0.2064 0.2474 0.0039  -0.0432 0.0217  1820 GLU B O   
1065 C CB  . GLU B 27  ? 0.2789 0.1652 0.2594 0.0218  -0.0526 0.0369  1820 GLU B CB  
1066 C CG  . GLU B 27  ? 0.3786 0.2834 0.3596 0.0169  -0.0500 0.0537  1820 GLU B CG  
1067 C CD  . GLU B 27  ? 0.4731 0.3494 0.4539 0.0192  -0.0517 0.0717  1820 GLU B CD  
1068 O OE1 . GLU B 27  ? 0.5131 0.3654 0.5004 0.0067  -0.0525 0.0744  1820 GLU B OE1 
1069 O OE2 . GLU B 27  ? 0.4685 0.3461 0.4444 0.0336  -0.0521 0.0836  1820 GLU B OE2 
1070 N N   . PRO B 28  ? 0.2431 0.1535 0.2361 0.0001  -0.0499 0.0174  1821 PRO B N   
1071 C CA  . PRO B 28  ? 0.2565 0.1856 0.2581 -0.0089 -0.0470 0.0155  1821 PRO B CA  
1072 C C   . PRO B 28  ? 0.2278 0.1723 0.2326 -0.0170 -0.0437 0.0274  1821 PRO B C   
1073 O O   . PRO B 28  ? 0.2810 0.2131 0.2835 -0.0190 -0.0451 0.0404  1821 PRO B O   
1074 C CB  . PRO B 28  ? 0.2737 0.1907 0.2804 -0.0133 -0.0525 0.0098  1821 PRO B CB  
1075 C CG  . PRO B 28  ? 0.2842 0.1765 0.2817 -0.0056 -0.0577 0.0045  1821 PRO B CG  
1076 C CD  . PRO B 28  ? 0.2427 0.1258 0.2340 0.0010  -0.0560 0.0123  1821 PRO B CD  
1077 N N   . VAL B 29  ? 0.2100 0.1823 0.2196 -0.0202 -0.0381 0.0237  1822 VAL B N   
1078 C CA  . VAL B 29  ? 0.3503 0.3454 0.3627 -0.0282 -0.0336 0.0345  1822 VAL B CA  
1079 C C   . VAL B 29  ? 0.3321 0.3189 0.3559 -0.0398 -0.0358 0.0419  1822 VAL B C   
1080 O O   . VAL B 29  ? 0.2754 0.2603 0.3085 -0.0417 -0.0388 0.0323  1822 VAL B O   
1081 C CB  . VAL B 29  ? 0.3267 0.3546 0.3420 -0.0271 -0.0265 0.0237  1822 VAL B CB  
1082 C CG1 . VAL B 29  ? 0.3598 0.4193 0.3767 -0.0344 -0.0203 0.0344  1822 VAL B CG1 
1083 C CG2 . VAL B 29  ? 0.2534 0.2883 0.2601 -0.0199 -0.0252 0.0135  1822 VAL B CG2 
1084 N N   . ASN B 30  ? 0.2944 0.2777 0.3185 -0.0481 -0.0345 0.0602  1823 ASN B N   
1085 C CA  . ASN B 30  ? 0.3383 0.3136 0.3767 -0.0640 -0.0359 0.0686  1823 ASN B CA  
1086 C C   . ASN B 30  ? 0.2422 0.2612 0.2922 -0.0727 -0.0284 0.0713  1823 ASN B C   
1087 O O   . ASN B 30  ? 0.3181 0.3617 0.3643 -0.0758 -0.0206 0.0863  1823 ASN B O   
1088 C CB  . ASN B 30  ? 0.3845 0.3331 0.4209 -0.0702 -0.0359 0.0901  1823 ASN B CB  
1089 C CG  . ASN B 30  ? 0.3522 0.2781 0.4058 -0.0894 -0.0391 0.0944  1823 ASN B CG  
1090 O OD1 . ASN B 30  ? 0.4304 0.3131 0.4840 -0.0922 -0.0429 0.1013  1823 ASN B OD1 
1091 N ND2 . ASN B 30  ? 0.3678 0.3232 0.4379 -0.1027 -0.0377 0.0895  1823 ASN B ND2 
1092 N N   . PRO B 31  ? 0.2806 0.3143 0.3444 -0.0752 -0.0301 0.0580  1824 PRO B N   
1093 C CA  . PRO B 31  ? 0.3399 0.4206 0.4161 -0.0790 -0.0219 0.0584  1824 PRO B CA  
1094 C C   . PRO B 31  ? 0.3864 0.4852 0.4751 -0.0982 -0.0165 0.0786  1824 PRO B C   
1095 O O   . PRO B 31  ? 0.4209 0.5637 0.5136 -0.0999 -0.0063 0.0845  1824 PRO B O   
1096 C CB  . PRO B 31  ? 0.3238 0.4118 0.4139 -0.0751 -0.0274 0.0422  1824 PRO B CB  
1097 C CG  . PRO B 31  ? 0.3143 0.3637 0.4037 -0.0804 -0.0390 0.0392  1824 PRO B CG  
1098 C CD  . PRO B 31  ? 0.3087 0.3216 0.3780 -0.0740 -0.0399 0.0438  1824 PRO B CD  
1099 N N   . ARG B 32  ? 0.3904 0.4563 0.4856 -0.1132 -0.0221 0.0892  1825 ARG B N   
1100 C CA  . ARG B 32  ? 0.3453 0.4224 0.4549 -0.1350 -0.0159 0.1118  1825 ARG B CA  
1101 C C   . ARG B 32  ? 0.4165 0.4961 0.5103 -0.1331 -0.0068 0.1369  1825 ARG B C   
1102 O O   . ARG B 32  ? 0.5018 0.5991 0.6055 -0.1499 0.0016  0.1606  1825 ARG B O   
1103 C CB  . ARG B 32  ? 0.4391 0.4732 0.5627 -0.1532 -0.0250 0.1124  1825 ARG B CB  
1104 C CG  . ARG B 32  ? 0.4314 0.4696 0.5680 -0.1542 -0.0360 0.0869  1825 ARG B CG  
1105 C CD  . ARG B 32  ? 0.4810 0.4699 0.6225 -0.1659 -0.0478 0.0779  1825 ARG B CD  
1106 N NE  . ARG B 32  ? 0.4902 0.4288 0.6083 -0.1492 -0.0520 0.0740  1825 ARG B NE  
1107 C CZ  . ARG B 32  ? 0.4836 0.4163 0.5849 -0.1277 -0.0574 0.0562  1825 ARG B CZ  
1108 N NH1 . ARG B 32  ? 0.4738 0.4423 0.5780 -0.1193 -0.0593 0.0425  1825 ARG B NH1 
1109 N NH2 . ARG B 32  ? 0.5013 0.3936 0.5842 -0.1136 -0.0600 0.0541  1825 ARG B NH2 
1110 N N   . LEU B 33  ? 0.3489 0.4160 0.4192 -0.1136 -0.0083 0.1337  1826 LEU B N   
1111 C CA  . LEU B 33  ? 0.4386 0.5176 0.4914 -0.1079 -0.0014 0.1563  1826 LEU B CA  
1112 C C   . LEU B 33  ? 0.4701 0.6008 0.5085 -0.0943 0.0053  0.1463  1826 LEU B C   
1113 O O   . LEU B 33  ? 0.6631 0.8182 0.6857 -0.0899 0.0112  0.1640  1826 LEU B O   
1114 C CB  . LEU B 33  ? 0.3989 0.4303 0.4365 -0.0955 -0.0088 0.1617  1826 LEU B CB  
1115 C CG  . LEU B 33  ? 0.4202 0.3918 0.4676 -0.1047 -0.0149 0.1710  1826 LEU B CG  
1116 C CD1 . LEU B 33  ? 0.4797 0.4134 0.5108 -0.0852 -0.0211 0.1724  1826 LEU B CD1 
1117 C CD2 . LEU B 33  ? 0.4675 0.4350 0.5270 -0.1249 -0.0073 0.2030  1826 LEU B CD2 
1118 N N   . VAL B 34  ? 0.3080 0.4561 0.3513 -0.0869 0.0044  0.1184  1827 VAL B N   
1119 C CA  . VAL B 34  ? 0.2522 0.4397 0.2834 -0.0733 0.0100  0.1016  1827 VAL B CA  
1120 C C   . VAL B 34  ? 0.3066 0.5357 0.3540 -0.0764 0.0180  0.0912  1827 VAL B C   
1121 O O   . VAL B 34  ? 0.3286 0.5485 0.3908 -0.0735 0.0141  0.0735  1827 VAL B O   
1122 C CB  . VAL B 34  ? 0.3366 0.4992 0.3596 -0.0587 0.0025  0.0769  1827 VAL B CB  
1123 C CG1 . VAL B 34  ? 0.2837 0.4823 0.2937 -0.0477 0.0079  0.0593  1827 VAL B CG1 
1124 C CG2 . VAL B 34  ? 0.4288 0.5498 0.4417 -0.0555 -0.0061 0.0867  1827 VAL B CG2 
1125 N N   . SER B 35  ? 0.4128 0.6922 0.4574 -0.0803 0.0297  0.1031  1828 SER B N   
1126 C CA  . SER B 35  ? 0.4114 0.7368 0.4738 -0.0822 0.0389  0.0950  1828 SER B CA  
1127 C C   . SER B 35  ? 0.4136 0.7469 0.4761 -0.0633 0.0392  0.0606  1828 SER B C   
1128 O O   . SER B 35  ? 0.3341 0.6719 0.3775 -0.0510 0.0404  0.0451  1828 SER B O   
1129 C CB  . SER B 35  ? 0.4827 0.8664 0.5386 -0.0879 0.0531  0.1141  1828 SER B CB  
1130 O OG  . SER B 35  ? 0.4983 0.9119 0.5298 -0.0722 0.0579  0.0993  1828 SER B OG  
1131 N N   . GLY B 36  ? 0.4119 0.7455 0.4970 -0.0610 0.0374  0.0487  1829 GLY B N   
1132 C CA  . GLY B 36  ? 0.3845 0.7236 0.4740 -0.0418 0.0394  0.0200  1829 GLY B CA  
1133 C C   . GLY B 36  ? 0.3069 0.5921 0.3928 -0.0321 0.0285  0.0053  1829 GLY B C   
1134 O O   . GLY B 36  ? 0.2746 0.5566 0.3671 -0.0164 0.0302  -0.0153 1829 GLY B O   
1135 N N   . TYR B 37  ? 0.3026 0.4515 0.3319 -0.0751 0.0405  0.0376  1830 TYR B N   
1136 C CA  . TYR B 37  ? 0.2063 0.3402 0.2432 -0.0598 0.0297  0.0316  1830 TYR B CA  
1137 C C   . TYR B 37  ? 0.2078 0.3624 0.2726 -0.0555 0.0279  0.0256  1830 TYR B C   
1138 O O   . TYR B 37  ? 0.2925 0.4499 0.3678 -0.0398 0.0260  0.0185  1830 TYR B O   
1139 C CB  . TYR B 37  ? 0.2610 0.3573 0.2816 -0.0610 0.0202  0.0394  1830 TYR B CB  
1140 C CG  . TYR B 37  ? 0.3038 0.3893 0.3290 -0.0453 0.0111  0.0333  1830 TYR B CG  
1141 C CD1 . TYR B 37  ? 0.2297 0.3094 0.2686 -0.0427 0.0054  0.0293  1830 TYR B CD1 
1142 C CD2 . TYR B 37  ? 0.2115 0.2975 0.2269 -0.0357 0.0089  0.0305  1830 TYR B CD2 
1143 C CE1 . TYR B 37  ? 0.2422 0.3139 0.2846 -0.0303 -0.0009 0.0241  1830 TYR B CE1 
1144 C CE2 . TYR B 37  ? 0.2480 0.3287 0.2688 -0.0253 0.0019  0.0243  1830 TYR B CE2 
1145 C CZ  . TYR B 37  ? 0.1942 0.2669 0.2290 -0.0223 -0.0021 0.0216  1830 TYR B CZ  
1146 O OH  . TYR B 37  ? 0.2054 0.2741 0.2447 -0.0138 -0.0071 0.0158  1830 TYR B OH  
1147 N N   . ARG B 38  ? 0.2707 0.4401 0.3457 -0.0707 0.0283  0.0288  1831 ARG B N   
1148 C CA  . ARG B 38  ? 0.2576 0.4553 0.3582 -0.0672 0.0243  0.0250  1831 ARG B CA  
1149 C C   . ARG B 38  ? 0.2737 0.5137 0.3966 -0.0532 0.0330  0.0215  1831 ARG B C   
1150 O O   . ARG B 38  ? 0.3144 0.5730 0.4565 -0.0384 0.0295  0.0198  1831 ARG B O   
1151 C CB  . ARG B 38  ? 0.3689 0.5778 0.4731 -0.0918 0.0223  0.0276  1831 ARG B CB  
1152 C CG  . ARG B 38  ? 0.4587 0.6504 0.5615 -0.0956 0.0108  0.0249  1831 ARG B CG  
1153 C CD  . ARG B 38  ? 0.5884 0.7933 0.6923 -0.1247 0.0103  0.0239  1831 ARG B CD  
1154 N NE  . ARG B 38  ? 0.7359 0.9049 0.8149 -0.1464 0.0181  0.0283  1831 ARG B NE  
1155 C CZ  . ARG B 38  ? 0.7894 0.9705 0.8654 -0.1565 0.0280  0.0317  1831 ARG B CZ  
1156 N NH1 . ARG B 38  ? 0.7992 1.0299 0.8974 -0.1471 0.0317  0.0298  1831 ARG B NH1 
1157 N NH2 . ARG B 38  ? 0.7969 0.9369 0.8458 -0.1741 0.0351  0.0378  1831 ARG B NH2 
1158 N N   . ARG B 39  ? 0.2291 0.4843 0.3483 -0.0563 0.0455  0.0213  1832 ARG B N   
1159 C CA  . ARG B 39  ? 0.3220 0.6149 0.4612 -0.0399 0.0572  0.0166  1832 ARG B CA  
1160 C C   . ARG B 39  ? 0.2571 0.5250 0.3910 -0.0155 0.0590  0.0092  1832 ARG B C   
1161 O O   . ARG B 39  ? 0.3090 0.5956 0.4612 0.0050  0.0658  0.0061  1832 ARG B O   
1162 C CB  . ARG B 39  ? 0.3629 0.6721 0.4936 -0.0502 0.0716  0.0164  1832 ARG B CB  
1163 C CG  . ARG B 39  ? 0.3532 0.6803 0.4885 -0.0712 0.0710  0.0216  1832 ARG B CG  
1164 C CD  . ARG B 39  ? 0.3459 0.7140 0.5056 -0.0594 0.0781  0.0183  1832 ARG B CD  
1165 N NE  . ARG B 39  ? 0.4952 0.8877 0.6618 -0.0807 0.0772  0.0216  1832 ARG B NE  
1166 C CZ  . ARG B 39  ? 0.5181 0.9124 0.6713 -0.1006 0.0865  0.0241  1832 ARG B CZ  
1167 N NH1 . ARG B 39  ? 0.4669 0.8406 0.5971 -0.1011 0.0963  0.0248  1832 ARG B NH1 
1168 N NH2 . ARG B 39  ? 0.6101 1.0267 0.7702 -0.1212 0.0860  0.0261  1832 ARG B NH2 
1169 N N   . ILE B 40  ? 0.2014 0.4274 0.3101 -0.0176 0.0537  0.0067  1833 ILE B N   
1170 C CA  . ILE B 40  ? 0.2457 0.4463 0.3444 -0.0023 0.0570  -0.0026 1833 ILE B CA  
1171 C C   . ILE B 40  ? 0.2318 0.4081 0.3332 0.0052  0.0454  -0.0020 1833 ILE B C   
1172 O O   . ILE B 40  ? 0.3733 0.5373 0.4780 0.0207  0.0500  -0.0074 1833 ILE B O   
1173 C CB  . ILE B 40  ? 0.1976 0.3792 0.2670 -0.0119 0.0589  -0.0066 1833 ILE B CB  
1174 C CG1 . ILE B 40  ? 0.1811 0.3870 0.2447 -0.0165 0.0743  -0.0093 1833 ILE B CG1 
1175 C CG2 . ILE B 40  ? 0.2572 0.4111 0.3133 -0.0041 0.0585  -0.0176 1833 ILE B CG2 
1176 C CD1 . ILE B 40  ? 0.2103 0.4047 0.2406 -0.0287 0.0751  -0.0100 1833 ILE B CD1 
1177 N N   . ILE B 41  ? 0.1490 0.3151 0.2472 -0.0054 0.0325  0.0044  1834 ILE B N   
1178 C CA  . ILE B 41  ? 0.1829 0.3257 0.2794 -0.0005 0.0227  0.0042  1834 ILE B CA  
1179 C C   . ILE B 41  ? 0.2175 0.3774 0.3312 0.0005  0.0161  0.0101  1834 ILE B C   
1180 O O   . ILE B 41  ? 0.1923 0.3563 0.3051 -0.0138 0.0094  0.0142  1834 ILE B O   
1181 C CB  . ILE B 41  ? 0.2359 0.3552 0.3147 -0.0099 0.0143  0.0058  1834 ILE B CB  
1182 C CG1 . ILE B 41  ? 0.1255 0.2386 0.1866 -0.0117 0.0187  0.0013  1834 ILE B CG1 
1183 C CG2 . ILE B 41  ? 0.2070 0.3082 0.2863 -0.0047 0.0064  0.0046  1834 ILE B CG2 
1184 C CD1 . ILE B 41  ? 0.1358 0.2405 0.1943 -0.0036 0.0248  -0.0101 1834 ILE B CD1 
1185 N N   . LYS B 42  ? 0.1701 0.3379 0.2965 0.0168  0.0182  0.0106  1835 LYS B N   
1186 C CA  . LYS B 42  ? 0.2246 0.4188 0.3669 0.0189  0.0107  0.0176  1835 LYS B CA  
1187 C C   . LYS B 42  ? 0.1364 0.3097 0.2691 0.0133  -0.0007 0.0187  1835 LYS B C   
1188 O O   . LYS B 42  ? 0.1943 0.3869 0.3322 0.0042  -0.0091 0.0220  1835 LYS B O   
1189 C CB  . LYS B 42  ? 0.2333 0.4457 0.3915 0.0428  0.0172  0.0216  1835 LYS B CB  
1190 C CG  . LYS B 42  ? 0.3160 0.5615 0.4893 0.0501  0.0296  0.0206  1835 LYS B CG  
1191 C CD  . LYS B 42  ? 0.3606 0.6356 0.5381 0.0261  0.0275  0.0206  1835 LYS B CD  
1192 C CE  . LYS B 42  ? 0.3858 0.6861 0.5721 0.0297  0.0402  0.0183  1835 LYS B CE  
1193 N NZ  . LYS B 42  ? 0.5203 0.8511 0.7243 0.0415  0.0379  0.0231  1835 LYS B NZ  
1194 N N   . ASN B 43  ? 0.1342 0.2716 0.2523 0.0166  -0.0004 0.0147  1836 ASN B N   
1195 C CA  . ASN B 43  ? 0.2014 0.3201 0.3104 0.0132  -0.0084 0.0149  1836 ASN B CA  
1196 C C   . ASN B 43  ? 0.1398 0.2332 0.2345 0.0050  -0.0094 0.0098  1836 ASN B C   
1197 O O   . ASN B 43  ? 0.1349 0.2110 0.2232 0.0093  -0.0066 0.0058  1836 ASN B O   
1198 C CB  . ASN B 43  ? 0.2393 0.3462 0.3475 0.0277  -0.0063 0.0175  1836 ASN B CB  
1199 C CG  . ASN B 43  ? 0.2227 0.3550 0.3450 0.0431  -0.0046 0.0260  1836 ASN B CG  
1200 O OD1 . ASN B 43  ? 0.2323 0.3562 0.3571 0.0590  0.0056  0.0271  1836 ASN B OD1 
1201 N ND2 . ASN B 43  ? 0.1866 0.3507 0.3171 0.0390  -0.0141 0.0319  1836 ASN B ND2 
1202 N N   . PRO B 44  ? 0.0992 0.1903 0.1882 -0.0068 -0.0129 0.0104  1837 PRO B N   
1203 C CA  . PRO B 44  ? 0.1579 0.2270 0.2339 -0.0090 -0.0142 0.0088  1837 PRO B CA  
1204 C C   . PRO B 44  ? 0.1757 0.2307 0.2478 -0.0050 -0.0178 0.0062  1837 PRO B C   
1205 O O   . PRO B 44  ? 0.1760 0.2331 0.2498 -0.0055 -0.0205 0.0061  1837 PRO B O   
1206 C CB  . PRO B 44  ? 0.1701 0.2330 0.2386 -0.0210 -0.0152 0.0123  1837 PRO B CB  
1207 C CG  . PRO B 44  ? 0.2599 0.3416 0.3373 -0.0299 -0.0169 0.0125  1837 PRO B CG  
1208 C CD  . PRO B 44  ? 0.1253 0.2334 0.2185 -0.0191 -0.0149 0.0131  1837 PRO B CD  
1209 N N   . MET B 45  ? 0.1438 0.1899 0.2105 -0.0013 -0.0178 0.0044  1838 MET B N   
1210 C CA  . MET B 45  ? 0.1817 0.2201 0.2464 0.0027  -0.0193 0.0015  1838 MET B CA  
1211 C C   . MET B 45  ? 0.2292 0.2664 0.2897 0.0072  -0.0207 0.0025  1838 MET B C   
1212 O O   . MET B 45  ? 0.2267 0.2724 0.2853 0.0070  -0.0209 0.0040  1838 MET B O   
1213 C CB  . MET B 45  ? 0.1953 0.2372 0.2644 0.0048  -0.0163 -0.0020 1838 MET B CB  
1214 C CG  . MET B 45  ? 0.1306 0.1692 0.1983 0.0063  -0.0161 -0.0049 1838 MET B CG  
1215 S SD  . MET B 45  ? 0.2102 0.2398 0.2709 0.0054  -0.0188 -0.0043 1838 MET B SD  
1216 C CE  . MET B 45  ? 0.2378 0.2749 0.2998 0.0025  -0.0207 0.0002  1838 MET B CE  
1217 N N   . ASP B 46  ? 0.1959 0.2250 0.2541 0.0126  -0.0215 0.0021  1839 ASP B N   
1218 C CA  . ASP B 46  ? 0.1708 0.2041 0.2280 0.0225  -0.0229 0.0051  1839 ASP B CA  
1219 C C   . ASP B 46  ? 0.1680 0.2021 0.2292 0.0295  -0.0207 0.0006  1839 ASP B C   
1220 O O   . ASP B 46  ? 0.2375 0.2621 0.2966 0.0250  -0.0181 -0.0041 1839 ASP B O   
1221 C CB  . ASP B 46  ? 0.2178 0.2313 0.2632 0.0267  -0.0232 0.0137  1839 ASP B CB  
1222 C CG  . ASP B 46  ? 0.2639 0.2471 0.3001 0.0282  -0.0194 0.0124  1839 ASP B CG  
1223 O OD1 . ASP B 46  ? 0.2922 0.2628 0.3240 0.0423  -0.0171 0.0149  1839 ASP B OD1 
1224 O OD2 . ASP B 46  ? 0.2584 0.2322 0.2914 0.0154  -0.0183 0.0081  1839 ASP B OD2 
1225 N N   . PHE B 47  ? 0.1752 0.2258 0.2421 0.0410  -0.0217 0.0025  1840 PHE B N   
1226 C CA  . PHE B 47  ? 0.2107 0.2718 0.2851 0.0483  -0.0177 -0.0025 1840 PHE B CA  
1227 C C   . PHE B 47  ? 0.2528 0.2828 0.3164 0.0548  -0.0121 -0.0045 1840 PHE B C   
1228 O O   . PHE B 47  ? 0.2733 0.3045 0.3375 0.0537  -0.0069 -0.0117 1840 PHE B O   
1229 C CB  . PHE B 47  ? 0.2259 0.3205 0.3121 0.0618  -0.0202 0.0010  1840 PHE B CB  
1230 C CG  . PHE B 47  ? 0.2237 0.3543 0.3189 0.0505  -0.0251 -0.0015 1840 PHE B CG  
1231 C CD1 . PHE B 47  ? 0.1919 0.3183 0.2853 0.0314  -0.0231 -0.0088 1840 PHE B CD1 
1232 C CD2 . PHE B 47  ? 0.3055 0.4740 0.4092 0.0594  -0.0312 0.0033  1840 PHE B CD2 
1233 C CE1 . PHE B 47  ? 0.1735 0.3256 0.2705 0.0186  -0.0252 -0.0142 1840 PHE B CE1 
1234 C CE2 . PHE B 47  ? 0.2223 0.4258 0.3311 0.0446  -0.0358 -0.0020 1840 PHE B CE2 
1235 C CZ  . PHE B 47  ? 0.1661 0.3576 0.2701 0.0228  -0.0317 -0.0122 1840 PHE B CZ  
1236 N N   . SER B 48  ? 0.2469 0.2460 0.2971 0.0593  -0.0116 0.0010  1841 SER B N   
1237 C CA  . SER B 48  ? 0.2386 0.2018 0.2741 0.0623  -0.0042 -0.0041 1841 SER B CA  
1238 C C   . SER B 48  ? 0.2454 0.1993 0.2729 0.0428  -0.0040 -0.0128 1841 SER B C   
1239 O O   . SER B 48  ? 0.3155 0.2533 0.3323 0.0416  0.0020  -0.0216 1841 SER B O   
1240 C CB  . SER B 48  ? 0.2865 0.2103 0.3052 0.0687  -0.0013 0.0035  1841 SER B CB  
1241 O OG  . SER B 48  ? 0.3175 0.2313 0.3288 0.0510  -0.0052 0.0074  1841 SER B OG  
1242 N N   . THR B 49  ? 0.2335 0.1999 0.2652 0.0289  -0.0101 -0.0102 1842 THR B N   
1243 C CA  . THR B 49  ? 0.1860 0.1544 0.2134 0.0140  -0.0117 -0.0153 1842 THR B CA  
1244 C C   . THR B 49  ? 0.1765 0.1645 0.2098 0.0152  -0.0105 -0.0189 1842 THR B C   
1245 O O   . THR B 49  ? 0.2530 0.2376 0.2762 0.0090  -0.0091 -0.0243 1842 THR B O   
1246 C CB  . THR B 49  ? 0.1909 0.1709 0.2238 0.0037  -0.0171 -0.0099 1842 THR B CB  
1247 O OG1 . THR B 49  ? 0.2895 0.2500 0.3140 -0.0010 -0.0163 -0.0064 1842 THR B OG1 
1248 C CG2 . THR B 49  ? 0.2576 0.2494 0.2895 -0.0076 -0.0204 -0.0121 1842 THR B CG2 
1249 N N   . MET B 50  ? 0.1433 0.1522 0.1902 0.0205  -0.0105 -0.0162 1843 MET B N   
1250 C CA  . MET B 50  ? 0.1449 0.1683 0.1951 0.0196  -0.0064 -0.0194 1843 MET B CA  
1251 C C   . MET B 50  ? 0.2317 0.2517 0.2770 0.0272  0.0006  -0.0259 1843 MET B C   
1252 O O   . MET B 50  ? 0.2639 0.2861 0.3018 0.0227  0.0052  -0.0300 1843 MET B O   
1253 C CB  . MET B 50  ? 0.1296 0.1749 0.1938 0.0192  -0.0061 -0.0179 1843 MET B CB  
1254 C CG  . MET B 50  ? 0.1711 0.2160 0.2377 0.0130  -0.0101 -0.0139 1843 MET B CG  
1255 S SD  . MET B 50  ? 0.2426 0.3096 0.3200 0.0095  -0.0096 -0.0162 1843 MET B SD  
1256 C CE  . MET B 50  ? 0.1942 0.2668 0.2723 -0.0004 -0.0013 -0.0206 1843 MET B CE  
1257 N N   . ARG B 51  ? 0.1805 0.1941 0.2280 0.0406  0.0029  -0.0261 1844 ARG B N   
1258 C CA  . ARG B 51  ? 0.2328 0.2404 0.2756 0.0526  0.0123  -0.0329 1844 ARG B CA  
1259 C C   . ARG B 51  ? 0.2482 0.2262 0.2678 0.0443  0.0165  -0.0416 1844 ARG B C   
1260 O O   . ARG B 51  ? 0.3000 0.2804 0.3119 0.0450  0.0247  -0.0499 1844 ARG B O   
1261 C CB  . ARG B 51  ? 0.2380 0.2383 0.2854 0.0731  0.0141  -0.0284 1844 ARG B CB  
1262 C CG  . ARG B 51  ? 0.3807 0.3656 0.4213 0.0913  0.0264  -0.0352 1844 ARG B CG  
1263 C CD  . ARG B 51  ? 0.3923 0.4165 0.4482 0.0971  0.0337  -0.0406 1844 ARG B CD  
1264 N NE  . ARG B 51  ? 0.2997 0.3721 0.3827 0.1068  0.0293  -0.0331 1844 ARG B NE  
1265 C CZ  . ARG B 51  ? 0.2349 0.3520 0.3365 0.1106  0.0354  -0.0368 1844 ARG B CZ  
1266 N NH1 . ARG B 51  ? 0.3442 0.4601 0.4386 0.1076  0.0473  -0.0469 1844 ARG B NH1 
1267 N NH2 . ARG B 51  ? 0.3733 0.5399 0.4996 0.1153  0.0299  -0.0311 1844 ARG B NH2 
1268 N N   . GLU B 52  ? 0.2627 0.2160 0.2697 0.0340  0.0115  -0.0408 1845 GLU B N   
1269 C CA  . GLU B 52  ? 0.3668 0.2953 0.3499 0.0215  0.0144  -0.0511 1845 GLU B CA  
1270 C C   . GLU B 52  ? 0.2263 0.1767 0.2043 0.0085  0.0110  -0.0529 1845 GLU B C   
1271 O O   . GLU B 52  ? 0.3147 0.2579 0.2737 0.0030  0.0164  -0.0632 1845 GLU B O   
1272 C CB  . GLU B 52  ? 0.3861 0.2919 0.3598 0.0086  0.0092  -0.0494 1845 GLU B CB  
1273 C CG  . GLU B 52  ? 0.4295 0.3057 0.3755 -0.0082 0.0132  -0.0629 1845 GLU B CG  
1274 C CD  . GLU B 52  ? 0.4142 0.3167 0.3535 -0.0275 0.0052  -0.0665 1845 GLU B CD  
1275 O OE1 . GLU B 52  ? 0.3767 0.3137 0.3327 -0.0280 -0.0040 -0.0557 1845 GLU B OE1 
1276 O OE2 . GLU B 52  ? 0.5266 0.4137 0.4413 -0.0416 0.0086  -0.0802 1845 GLU B OE2 
1277 N N   . ARG B 53  ? 0.2211 0.1954 0.2127 0.0040  0.0026  -0.0427 1846 ARG B N   
1278 C CA  . ARG B 53  ? 0.2433 0.2353 0.2289 -0.0044 -0.0005 -0.0398 1846 ARG B CA  
1279 C C   . ARG B 53  ? 0.2524 0.2546 0.2369 0.0007  0.0086  -0.0420 1846 ARG B C   
1280 O O   . ARG B 53  ? 0.3111 0.3171 0.2782 -0.0060 0.0109  -0.0445 1846 ARG B O   
1281 C CB  . ARG B 53  ? 0.3226 0.3302 0.3225 -0.0058 -0.0085 -0.0275 1846 ARG B CB  
1282 C CG  . ARG B 53  ? 0.2264 0.2480 0.2202 -0.0092 -0.0106 -0.0198 1846 ARG B CG  
1283 C CD  . ARG B 53  ? 0.2545 0.2850 0.2616 -0.0069 -0.0167 -0.0086 1846 ARG B CD  
1284 N NE  . ARG B 53  ? 0.2199 0.2576 0.2208 -0.0050 -0.0173 0.0023  1846 ARG B NE  
1285 C CZ  . ARG B 53  ? 0.2594 0.2992 0.2692 0.0014  -0.0185 0.0131  1846 ARG B CZ  
1286 N NH1 . ARG B 53  ? 0.2838 0.3231 0.3095 0.0045  -0.0192 0.0125  1846 ARG B NH1 
1287 N NH2 . ARG B 53  ? 0.3253 0.3648 0.3254 0.0060  -0.0173 0.0251  1846 ARG B NH2 
1288 N N   . LEU B 54  ? 0.2526 0.2643 0.2551 0.0109  0.0139  -0.0409 1847 LEU B N   
1289 C CA  . LEU B 54  ? 0.2421 0.2700 0.2466 0.0134  0.0242  -0.0440 1847 LEU B CA  
1290 C C   . LEU B 54  ? 0.3303 0.3480 0.3179 0.0176  0.0344  -0.0564 1847 LEU B C   
1291 O O   . LEU B 54  ? 0.3985 0.4253 0.3738 0.0126  0.0421  -0.0598 1847 LEU B O   
1292 C CB  . LEU B 54  ? 0.2025 0.2514 0.2321 0.0220  0.0268  -0.0419 1847 LEU B CB  
1293 C CG  . LEU B 54  ? 0.2505 0.3273 0.2899 0.0233  0.0382  -0.0456 1847 LEU B CG  
1294 C CD1 . LEU B 54  ? 0.2974 0.3803 0.3288 0.0071  0.0417  -0.0408 1847 LEU B CD1 
1295 C CD2 . LEU B 54  ? 0.2688 0.3745 0.3352 0.0315  0.0373  -0.0441 1847 LEU B CD2 
1296 N N   . SER B 55  ? 0.3286 0.3228 0.3113 0.0261  0.0361  -0.0635 1848 SER B N   
1297 C CA  A SER B 55  ? 0.4120 0.3892 0.3777 0.0333  0.0493  -0.0776 1848 SER B CA  
1298 C CA  B SER B 55  ? 0.4141 0.3914 0.3798 0.0333  0.0493  -0.0776 1848 SER B CA  
1299 C C   . SER B 55  ? 0.4698 0.4332 0.4032 0.0163  0.0499  -0.0870 1848 SER B C   
1300 O O   . SER B 55  ? 0.4810 0.4380 0.3966 0.0185  0.0629  -0.0999 1848 SER B O   
1301 C CB  A SER B 55  ? 0.4557 0.4012 0.4210 0.0479  0.0528  -0.0812 1848 SER B CB  
1302 C CB  B SER B 55  ? 0.4505 0.3958 0.4156 0.0479  0.0528  -0.0813 1848 SER B CB  
1303 O OG  A SER B 55  ? 0.4682 0.4333 0.4613 0.0669  0.0526  -0.0720 1848 SER B OG  
1304 O OG  B SER B 55  ? 0.3993 0.3144 0.3482 0.0339  0.0448  -0.0821 1848 SER B OG  
1305 N N   . ARG B 56  ? 0.4926 0.4553 0.4175 -0.0001 0.0364  -0.0814 1849 ARG B N   
1306 C CA  A ARG B 56  ? 0.4892 0.4496 0.3839 -0.0176 0.0339  -0.0889 1849 ARG B CA  
1307 C CA  B ARG B 56  ? 0.4819 0.4424 0.3767 -0.0177 0.0337  -0.0888 1849 ARG B CA  
1308 C C   . ARG B 56  ? 0.4529 0.4433 0.3445 -0.0245 0.0283  -0.0768 1849 ARG B C   
1309 O O   . ARG B 56  ? 0.4264 0.4255 0.2980 -0.0383 0.0195  -0.0752 1849 ARG B O   
1310 C CB  A ARG B 56  ? 0.4498 0.3959 0.3351 -0.0324 0.0227  -0.0913 1849 ARG B CB  
1311 C CB  B ARG B 56  ? 0.4609 0.4080 0.3475 -0.0323 0.0222  -0.0905 1849 ARG B CB  
1312 C CG  A ARG B 56  ? 0.4083 0.3710 0.3184 -0.0324 0.0092  -0.0746 1849 ARG B CG  
1313 C CG  B ARG B 56  ? 0.4230 0.3883 0.3343 -0.0323 0.0085  -0.0733 1849 ARG B CG  
1314 C CD  A ARG B 56  ? 0.4915 0.4564 0.3929 -0.0510 -0.0023 -0.0759 1849 ARG B CD  
1315 C CD  B ARG B 56  ? 0.4786 0.4497 0.3810 -0.0509 -0.0037 -0.0736 1849 ARG B CD  
1316 N NE  A ARG B 56  ? 0.4637 0.4474 0.3902 -0.0484 -0.0127 -0.0604 1849 ARG B NE  
1317 N NE  B ARG B 56  ? 0.4480 0.4525 0.3666 -0.0503 -0.0161 -0.0562 1849 ARG B NE  
1318 C CZ  A ARG B 56  ? 0.4422 0.4564 0.3790 -0.0458 -0.0212 -0.0461 1849 ARG B CZ  
1319 C CZ  B ARG B 56  ? 0.4454 0.4566 0.3873 -0.0459 -0.0218 -0.0459 1849 ARG B CZ  
1320 N NH1 A ARG B 56  ? 0.4919 0.5187 0.4505 -0.0415 -0.0276 -0.0345 1849 ARG B NH1 
1321 N NH1 B ARG B 56  ? 0.4464 0.4849 0.4008 -0.0423 -0.0303 -0.0311 1849 ARG B NH1 
1322 N NH2 A ARG B 56  ? 0.3715 0.4008 0.2945 -0.0463 -0.0216 -0.0428 1849 ARG B NH2 
1323 N NH2 B ARG B 56  ? 0.4053 0.3942 0.3558 -0.0435 -0.0180 -0.0495 1849 ARG B NH2 
1324 N N   . GLY B 57  ? 0.3168 0.3235 0.2263 -0.0157 0.0338  -0.0676 1850 GLY B N   
1325 C CA  . GLY B 57  ? 0.2726 0.2979 0.1772 -0.0217 0.0312  -0.0537 1850 GLY B CA  
1326 C C   . GLY B 57  ? 0.3750 0.4055 0.2856 -0.0251 0.0159  -0.0382 1850 GLY B C   
1327 O O   . GLY B 57  ? 0.3472 0.3878 0.2430 -0.0297 0.0114  -0.0264 1850 GLY B O   
1328 N N   . GLY B 58  ? 0.2341 0.2589 0.1655 -0.0209 0.0087  -0.0366 1851 GLY B N   
1329 C CA  . GLY B 58  ? 0.2204 0.2534 0.1593 -0.0222 -0.0040 -0.0236 1851 GLY B CA  
1330 C C   . GLY B 58  ? 0.3110 0.3478 0.2625 -0.0160 -0.0031 -0.0082 1851 GLY B C   
1331 O O   . GLY B 58  ? 0.4250 0.4679 0.3811 -0.0133 -0.0115 0.0036  1851 GLY B O   
1332 N N   . TYR B 59  ? 0.2988 0.3324 0.2557 -0.0143 0.0080  -0.0087 1852 TYR B N   
1333 C CA  . TYR B 59  ? 0.3378 0.3672 0.3016 -0.0133 0.0121  0.0032  1852 TYR B CA  
1334 C C   . TYR B 59  ? 0.2893 0.3170 0.2310 -0.0184 0.0200  0.0116  1852 TYR B C   
1335 O O   . TYR B 59  ? 0.3175 0.3509 0.2526 -0.0236 0.0303  0.0037  1852 TYR B O   
1336 C CB  . TYR B 59  ? 0.2612 0.2918 0.2462 -0.0132 0.0193  -0.0036 1852 TYR B CB  
1337 C CG  . TYR B 59  ? 0.2594 0.2902 0.2636 -0.0078 0.0121  -0.0074 1852 TYR B CG  
1338 C CD1 . TYR B 59  ? 0.2588 0.2830 0.2689 -0.0053 0.0062  0.0005  1852 TYR B CD1 
1339 C CD2 . TYR B 59  ? 0.2675 0.3043 0.2825 -0.0033 0.0128  -0.0177 1852 TYR B CD2 
1340 C CE1 . TYR B 59  ? 0.2459 0.2718 0.2709 -0.0018 0.0011  -0.0028 1852 TYR B CE1 
1341 C CE2 . TYR B 59  ? 0.2267 0.2623 0.2554 0.0014  0.0066  -0.0185 1852 TYR B CE2 
1342 C CZ  . TYR B 59  ? 0.2400 0.2710 0.2728 0.0005  0.0008  -0.0116 1852 TYR B CZ  
1343 O OH  . TYR B 59  ? 0.2559 0.2872 0.2994 0.0038  -0.0040 -0.0124 1852 TYR B OH  
1344 N N   . THR B 60  ? 0.3588 0.3792 0.2886 -0.0153 0.0163  0.0287  1853 THR B N   
1345 C CA  . THR B 60  ? 0.3714 0.3850 0.2763 -0.0195 0.0246  0.0409  1853 THR B CA  
1346 C C   . THR B 60  ? 0.3283 0.3218 0.2368 -0.0254 0.0391  0.0460  1853 THR B C   
1347 O O   . THR B 60  ? 0.3713 0.3578 0.2599 -0.0338 0.0505  0.0528  1853 THR B O   
1348 C CB  . THR B 60  ? 0.4025 0.4174 0.2886 -0.0109 0.0145  0.0607  1853 THR B CB  
1349 O OG1 . THR B 60  ? 0.3870 0.3878 0.2872 0.0007  0.0118  0.0724  1853 THR B OG1 
1350 C CG2 . THR B 60  ? 0.4289 0.4702 0.3101 -0.0111 -0.0003 0.0536  1853 THR B CG2 
1351 N N   . SER B 61  ? 0.3786 0.3630 0.3097 -0.0243 0.0399  0.0416  1854 SER B N   
1352 C CA  . SER B 61  ? 0.3401 0.3043 0.2725 -0.0349 0.0540  0.0433  1854 SER B CA  
1353 C C   . SER B 61  ? 0.3077 0.2812 0.2681 -0.0385 0.0532  0.0279  1854 SER B C   
1354 O O   . SER B 61  ? 0.2739 0.2597 0.2498 -0.0290 0.0418  0.0216  1854 SER B O   
1355 C CB  . SER B 61  ? 0.3794 0.3067 0.2955 -0.0287 0.0579  0.0625  1854 SER B CB  
1356 O OG  . SER B 61  ? 0.4323 0.3542 0.3629 -0.0147 0.0489  0.0635  1854 SER B OG  
1357 N N   . SER B 62  ? 0.2674 0.2369 0.2322 -0.0546 0.0657  0.0223  1855 SER B N   
1358 C CA  . SER B 62  ? 0.3128 0.2956 0.3013 -0.0602 0.0643  0.0085  1855 SER B CA  
1359 C C   . SER B 62  ? 0.2993 0.2570 0.2894 -0.0526 0.0596  0.0115  1855 SER B C   
1360 O O   . SER B 62  ? 0.3274 0.2996 0.3351 -0.0508 0.0530  0.0015  1855 SER B O   
1361 C CB  . SER B 62  ? 0.3482 0.3378 0.3397 -0.0837 0.0787  0.0010  1855 SER B CB  
1362 O OG  . SER B 62  ? 0.4374 0.3851 0.4047 -0.0955 0.0921  0.0116  1855 SER B OG  
1363 N N   . GLU B 63  ? 0.3715 0.2927 0.3421 -0.0458 0.0636  0.0263  1856 GLU B N   
1364 C CA  . GLU B 63  ? 0.4037 0.3004 0.3753 -0.0343 0.0619  0.0299  1856 GLU B CA  
1365 C C   . GLU B 63  ? 0.3661 0.2889 0.3549 -0.0184 0.0460  0.0273  1856 GLU B C   
1366 O O   . GLU B 63  ? 0.3716 0.2927 0.3712 -0.0153 0.0441  0.0207  1856 GLU B O   
1367 C CB  . GLU B 63  ? 0.3536 0.2101 0.3015 -0.0229 0.0690  0.0500  1856 GLU B CB  
1368 C CG  . GLU B 63  ? 0.5896 0.3985 0.5172 -0.0383 0.0889  0.0525  1856 GLU B CG  
1369 C CD  . GLU B 63  ? 0.7208 0.5362 0.6380 -0.0610 0.0984  0.0511  1856 GLU B CD  
1370 O OE1 . GLU B 63  ? 0.6864 0.5320 0.6028 -0.0575 0.0914  0.0556  1856 GLU B OE1 
1371 O OE2 . GLU B 63  ? 0.8021 0.5932 0.7111 -0.0844 0.1143  0.0441  1856 GLU B OE2 
1372 N N   . GLU B 64  ? 0.3026 0.2484 0.2913 -0.0106 0.0357  0.0315  1857 GLU B N   
1373 C CA  . GLU B 64  ? 0.3508 0.3188 0.3535 -0.0007 0.0222  0.0282  1857 GLU B CA  
1374 C C   . GLU B 64  ? 0.2700 0.2564 0.2896 -0.0072 0.0194  0.0129  1857 GLU B C   
1375 O O   . GLU B 64  ? 0.2671 0.2598 0.2982 -0.0026 0.0136  0.0093  1857 GLU B O   
1376 C CB  . GLU B 64  ? 0.3228 0.3078 0.3168 0.0041  0.0133  0.0339  1857 GLU B CB  
1377 C CG  . GLU B 64  ? 0.4613 0.4355 0.4360 0.0119  0.0142  0.0520  1857 GLU B CG  
1378 C CD  . GLU B 64  ? 0.5741 0.5696 0.5354 0.0106  0.0061  0.0545  1857 GLU B CD  
1379 O OE1 . GLU B 64  ? 0.7421 0.7436 0.6908 0.0200  0.0001  0.0700  1857 GLU B OE1 
1380 O OE2 . GLU B 64  ? 0.4551 0.4624 0.4175 0.0012  0.0059  0.0405  1857 GLU B OE2 
1381 N N   . PHE B 65  ? 0.2826 0.2808 0.3039 -0.0166 0.0239  0.0052  1858 PHE B N   
1382 C CA  . PHE B 65  ? 0.2628 0.2821 0.3007 -0.0190 0.0213  -0.0063 1858 PHE B CA  
1383 C C   . PHE B 65  ? 0.2894 0.3049 0.3347 -0.0246 0.0232  -0.0110 1858 PHE B C   
1384 O O   . PHE B 65  ? 0.2281 0.2544 0.2832 -0.0201 0.0162  -0.0149 1858 PHE B O   
1385 C CB  . PHE B 65  ? 0.2256 0.2641 0.2665 -0.0263 0.0282  -0.0125 1858 PHE B CB  
1386 C CG  . PHE B 65  ? 0.2100 0.2770 0.2697 -0.0244 0.0252  -0.0216 1858 PHE B CG  
1387 C CD1 . PHE B 65  ? 0.1600 0.2428 0.2303 -0.0356 0.0281  -0.0275 1858 PHE B CD1 
1388 C CD2 . PHE B 65  ? 0.2598 0.3374 0.3244 -0.0114 0.0201  -0.0240 1858 PHE B CD2 
1389 C CE1 . PHE B 65  ? 0.2321 0.3493 0.3200 -0.0315 0.0234  -0.0333 1858 PHE B CE1 
1390 C CE2 . PHE B 65  ? 0.3534 0.4565 0.4343 -0.0046 0.0175  -0.0287 1858 PHE B CE2 
1391 C CZ  . PHE B 65  ? 0.2255 0.3530 0.3194 -0.0135 0.0180  -0.0322 1858 PHE B CZ  
1392 N N   . ALA B 66  ? 0.2501 0.2468 0.2870 -0.0360 0.0337  -0.0110 1859 ALA B N   
1393 C CA  . ALA B 66  ? 0.2424 0.2311 0.2811 -0.0453 0.0377  -0.0190 1859 ALA B CA  
1394 C C   . ALA B 66  ? 0.2773 0.2521 0.3156 -0.0325 0.0333  -0.0161 1859 ALA B C   
1395 O O   . ALA B 66  ? 0.2980 0.2821 0.3420 -0.0354 0.0308  -0.0243 1859 ALA B O   
1396 C CB  . ALA B 66  ? 0.3138 0.2723 0.3373 -0.0617 0.0529  -0.0197 1859 ALA B CB  
1397 N N   . ALA B 67  ? 0.2999 0.2579 0.3315 -0.0184 0.0324  -0.0040 1860 ALA B N   
1398 C CA  . ALA B 67  ? 0.3328 0.2872 0.3683 -0.0050 0.0289  -0.0007 1860 ALA B CA  
1399 C C   . ALA B 67  ? 0.3671 0.3508 0.4158 -0.0025 0.0174  -0.0050 1860 ALA B C   
1400 O O   . ALA B 67  ? 0.2681 0.2548 0.3209 -0.0008 0.0169  -0.0093 1860 ALA B O   
1401 C CB  . ALA B 67  ? 0.3737 0.3191 0.4036 0.0109  0.0275  0.0147  1860 ALA B CB  
1402 N N   . ASP B 68  ? 0.2181 0.2196 0.2705 -0.0024 0.0099  -0.0041 1861 ASP B N   
1403 C CA  . ASP B 68  ? 0.2275 0.2468 0.2881 0.0003  0.0013  -0.0067 1861 ASP B CA  
1404 C C   . ASP B 68  ? 0.2028 0.2338 0.2685 -0.0055 0.0012  -0.0147 1861 ASP B C   
1405 O O   . ASP B 68  ? 0.2025 0.2402 0.2708 -0.0031 -0.0029 -0.0151 1861 ASP B O   
1406 C CB  . ASP B 68  ? 0.2249 0.2519 0.2841 0.0019  -0.0035 -0.0058 1861 ASP B CB  
1407 C CG  . ASP B 68  ? 0.2680 0.2946 0.3232 0.0059  -0.0089 0.0003  1861 ASP B CG  
1408 O OD1 . ASP B 68  ? 0.3411 0.3685 0.3995 0.0098  -0.0099 0.0052  1861 ASP B OD1 
1409 O OD2 . ASP B 68  ? 0.2894 0.3178 0.3383 0.0046  -0.0115 -0.0009 1861 ASP B OD2 
1410 N N   . ALA B 69  ? 0.2541 0.2924 0.3208 -0.0143 0.0053  -0.0205 1862 ALA B N   
1411 C CA  . ALA B 69  ? 0.1949 0.2547 0.2673 -0.0212 0.0035  -0.0281 1862 ALA B CA  
1412 C C   . ALA B 69  ? 0.2632 0.3138 0.3294 -0.0264 0.0061  -0.0329 1862 ALA B C   
1413 O O   . ALA B 69  ? 0.2321 0.2981 0.2994 -0.0250 0.0004  -0.0342 1862 ALA B O   
1414 C CB  . ALA B 69  ? 0.2572 0.3320 0.3330 -0.0342 0.0089  -0.0347 1862 ALA B CB  
1415 N N   . LEU B 70  ? 0.2888 0.3114 0.3458 -0.0310 0.0161  -0.0349 1863 LEU B N   
1416 C CA  . LEU B 70  ? 0.2815 0.2896 0.3299 -0.0353 0.0225  -0.0422 1863 LEU B CA  
1417 C C   . LEU B 70  ? 0.3052 0.3159 0.3561 -0.0219 0.0183  -0.0367 1863 LEU B C   
1418 O O   . LEU B 70  ? 0.2536 0.2692 0.2995 -0.0253 0.0197  -0.0434 1863 LEU B O   
1419 C CB  . LEU B 70  ? 0.2893 0.2574 0.3252 -0.0387 0.0369  -0.0437 1863 LEU B CB  
1420 C CG  . LEU B 70  ? 0.3429 0.3045 0.3718 -0.0603 0.0448  -0.0528 1863 LEU B CG  
1421 C CD1 . LEU B 70  ? 0.4305 0.3400 0.4414 -0.0635 0.0617  -0.0523 1863 LEU B CD1 
1422 C CD2 . LEU B 70  ? 0.3798 0.3674 0.4083 -0.0791 0.0424  -0.0685 1863 LEU B CD2 
1423 N N   . LEU B 71  ? 0.2380 0.2487 0.2953 -0.0092 0.0138  -0.0254 1864 LEU B N   
1424 C CA  . LEU B 71  ? 0.2249 0.2449 0.2868 -0.0003 0.0097  -0.0199 1864 LEU B CA  
1425 C C   . LEU B 71  ? 0.2072 0.2470 0.2696 -0.0042 0.0024  -0.0214 1864 LEU B C   
1426 O O   . LEU B 71  ? 0.1808 0.2260 0.2406 -0.0037 0.0038  -0.0221 1864 LEU B O   
1427 C CB  . LEU B 71  ? 0.2400 0.2630 0.3078 0.0078  0.0042  -0.0095 1864 LEU B CB  
1428 C CG  . LEU B 71  ? 0.3097 0.3443 0.3843 0.0147  0.0018  -0.0031 1864 LEU B CG  
1429 C CD1 . LEU B 71  ? 0.2776 0.3081 0.3531 0.0213  0.0113  -0.0051 1864 LEU B CD1 
1430 C CD2 . LEU B 71  ? 0.1852 0.2240 0.2627 0.0198  -0.0028 0.0052  1864 LEU B CD2 
1431 N N   . VAL B 72  ? 0.2167 0.2681 0.2814 -0.0062 -0.0043 -0.0205 1865 VAL B N   
1432 C CA  . VAL B 72  ? 0.1913 0.2597 0.2545 -0.0056 -0.0112 -0.0183 1865 VAL B CA  
1433 C C   . VAL B 72  ? 0.2291 0.3077 0.2843 -0.0134 -0.0092 -0.0257 1865 VAL B C   
1434 O O   . VAL B 72  ? 0.2046 0.2887 0.2533 -0.0125 -0.0105 -0.0226 1865 VAL B O   
1435 C CB  . VAL B 72  ? 0.2009 0.2827 0.2693 -0.0026 -0.0166 -0.0167 1865 VAL B CB  
1436 C CG1 . VAL B 72  ? 0.1801 0.2788 0.2458 0.0029  -0.0236 -0.0110 1865 VAL B CG1 
1437 C CG2 . VAL B 72  ? 0.1795 0.2480 0.2510 0.0040  -0.0169 -0.0119 1865 VAL B CG2 
1438 N N   . PHE B 73  ? 0.2174 0.2973 0.2701 -0.0239 -0.0046 -0.0364 1866 PHE B N   
1439 C CA  . PHE B 73  ? 0.2359 0.3268 0.2774 -0.0357 -0.0025 -0.0472 1866 PHE B CA  
1440 C C   . PHE B 73  ? 0.2587 0.3274 0.2900 -0.0358 0.0083  -0.0528 1866 PHE B C   
1441 O O   . PHE B 73  ? 0.1680 0.2466 0.1874 -0.0411 0.0094  -0.0584 1866 PHE B O   
1442 C CB  . PHE B 73  ? 0.2049 0.3039 0.2455 -0.0520 0.0002  -0.0594 1866 PHE B CB  
1443 C CG  . PHE B 73  ? 0.2260 0.3489 0.2808 -0.0496 -0.0072 -0.0541 1866 PHE B CG  
1444 C CD1 . PHE B 73  ? 0.2060 0.3578 0.2681 -0.0374 -0.0188 -0.0437 1866 PHE B CD1 
1445 C CD2 . PHE B 73  ? 0.1748 0.2889 0.2346 -0.0574 -0.0007 -0.0582 1866 PHE B CD2 
1446 C CE1 . PHE B 73  ? 0.3338 0.5074 0.4102 -0.0310 -0.0232 -0.0393 1866 PHE B CE1 
1447 C CE2 . PHE B 73  ? 0.2380 0.3780 0.3120 -0.0545 -0.0053 -0.0543 1866 PHE B CE2 
1448 C CZ  . PHE B 73  ? 0.2019 0.3728 0.2854 -0.0400 -0.0163 -0.0455 1866 PHE B CZ  
1449 N N   . ASP B 74  ? 0.2568 0.2985 0.2921 -0.0282 0.0169  -0.0507 1867 ASP B N   
1450 C CA  . ASP B 74  ? 0.2438 0.2684 0.2727 -0.0229 0.0286  -0.0549 1867 ASP B CA  
1451 C C   . ASP B 74  ? 0.1765 0.2185 0.2094 -0.0148 0.0250  -0.0462 1867 ASP B C   
1452 O O   . ASP B 74  ? 0.2150 0.2588 0.2390 -0.0156 0.0329  -0.0525 1867 ASP B O   
1453 C CB  . ASP B 74  ? 0.2581 0.2536 0.2911 -0.0123 0.0381  -0.0513 1867 ASP B CB  
1454 C CG  . ASP B 74  ? 0.3005 0.2666 0.3217 -0.0233 0.0482  -0.0618 1867 ASP B CG  
1455 O OD1 . ASP B 74  ? 0.3385 0.3047 0.3464 -0.0411 0.0517  -0.0770 1867 ASP B OD1 
1456 O OD2 . ASP B 74  ? 0.3925 0.3356 0.4154 -0.0160 0.0528  -0.0546 1867 ASP B OD2 
1457 N N   . ASN B 75  ? 0.2330 0.2866 0.2769 -0.0091 0.0149  -0.0332 1868 ASN B N   
1458 C CA  . ASN B 75  ? 0.2901 0.3580 0.3348 -0.0070 0.0123  -0.0251 1868 ASN B CA  
1459 C C   . ASN B 75  ? 0.2729 0.3548 0.3030 -0.0148 0.0085  -0.0266 1868 ASN B C   
1460 O O   . ASN B 75  ? 0.2154 0.3054 0.2369 -0.0169 0.0136  -0.0266 1868 ASN B O   
1461 C CB  . ASN B 75  ? 0.1650 0.2350 0.2193 -0.0037 0.0035  -0.0132 1868 ASN B CB  
1462 C CG  . ASN B 75  ? 0.1467 0.2117 0.2133 0.0030  0.0053  -0.0101 1868 ASN B CG  
1463 O OD1 . ASN B 75  ? 0.1588 0.2220 0.2298 0.0095  0.0137  -0.0126 1868 ASN B OD1 
1464 N ND2 . ASN B 75  ? 0.1860 0.2492 0.2569 0.0031  -0.0022 -0.0043 1868 ASN B ND2 
1465 N N   . CYS B 76  ? 0.1793 0.2691 0.2063 -0.0184 -0.0002 -0.0268 1869 CYS B N   
1466 C CA  . CYS B 76  ? 0.1772 0.2872 0.1896 -0.0237 -0.0060 -0.0258 1869 CYS B CA  
1467 C C   . CYS B 76  ? 0.2259 0.3393 0.2223 -0.0335 0.0031  -0.0398 1869 CYS B C   
1468 O O   . CYS B 76  ? 0.2298 0.3543 0.2118 -0.0359 0.0042  -0.0369 1869 CYS B O   
1469 C CB  . CYS B 76  ? 0.1665 0.2941 0.1819 -0.0248 -0.0163 -0.0255 1869 CYS B CB  
1470 S SG  . CYS B 76  ? 0.2282 0.3899 0.2275 -0.0261 -0.0272 -0.0187 1869 CYS B SG  
1471 N N   . GLN B 77  ? 0.2297 0.3289 0.2254 -0.0398 0.0119  -0.0555 1870 GLN B N   
1472 C CA  . GLN B 77  ? 0.2329 0.3285 0.2090 -0.0510 0.0229  -0.0730 1870 GLN B CA  
1473 C C   . GLN B 77  ? 0.2477 0.3340 0.2201 -0.0433 0.0360  -0.0734 1870 GLN B C   
1474 O O   . GLN B 77  ? 0.3415 0.4347 0.2938 -0.0509 0.0431  -0.0833 1870 GLN B O   
1475 C CB  . GLN B 77  ? 0.2694 0.3406 0.2433 -0.0601 0.0321  -0.0894 1870 GLN B CB  
1476 C CG  . GLN B 77  ? 0.3069 0.3622 0.2570 -0.0730 0.0472  -0.1113 1870 GLN B CG  
1477 C CD  . GLN B 77  ? 0.4672 0.4971 0.4098 -0.0889 0.0552  -0.1280 1870 GLN B CD  
1478 O OE1 . GLN B 77  ? 0.6479 0.6624 0.5670 -0.1060 0.0671  -0.1495 1870 GLN B OE1 
1479 N NE2 . GLN B 77  ? 0.4792 0.5027 0.4390 -0.0858 0.0502  -0.1192 1870 GLN B NE2 
1480 N N   . THR B 78  ? 0.2175 0.2929 0.2087 -0.0291 0.0397  -0.0635 1871 THR B N   
1481 C CA  . THR B 78  ? 0.3315 0.4094 0.3249 -0.0208 0.0518  -0.0624 1871 THR B CA  
1482 C C   . THR B 78  ? 0.2594 0.3621 0.2458 -0.0252 0.0467  -0.0517 1871 THR B C   
1483 O O   . THR B 78  ? 0.2959 0.4078 0.2697 -0.0279 0.0576  -0.0572 1871 THR B O   
1484 C CB  . THR B 78  ? 0.3518 0.4230 0.3695 -0.0054 0.0542  -0.0529 1871 THR B CB  
1485 O OG1 . THR B 78  ? 0.4359 0.4792 0.4555 0.0000  0.0605  -0.0602 1871 THR B OG1 
1486 C CG2 . THR B 78  ? 0.3422 0.4279 0.3679 0.0040  0.0666  -0.0512 1871 THR B CG2 
1487 N N   . PHE B 79  ? 0.2437 0.3540 0.2352 -0.0260 0.0322  -0.0362 1872 PHE B N   
1488 C CA  . PHE B 79  ? 0.2058 0.3297 0.1896 -0.0294 0.0296  -0.0225 1872 PHE B CA  
1489 C C   . PHE B 79  ? 0.2659 0.4028 0.2232 -0.0376 0.0239  -0.0210 1872 PHE B C   
1490 O O   . PHE B 79  ? 0.3204 0.4666 0.2634 -0.0417 0.0264  -0.0113 1872 PHE B O   
1491 C CB  . PHE B 79  ? 0.2354 0.3529 0.2321 -0.0261 0.0194  -0.0065 1872 PHE B CB  
1492 C CG  . PHE B 79  ? 0.2743 0.3964 0.2660 -0.0315 0.0219  0.0071  1872 PHE B CG  
1493 C CD1 . PHE B 79  ? 0.2273 0.3599 0.2320 -0.0334 0.0324  0.0066  1872 PHE B CD1 
1494 C CD2 . PHE B 79  ? 0.2657 0.3824 0.2394 -0.0345 0.0146  0.0214  1872 PHE B CD2 
1495 C CE1 . PHE B 79  ? 0.3267 0.4653 0.3266 -0.0434 0.0363  0.0180  1872 PHE B CE1 
1496 C CE2 . PHE B 79  ? 0.4215 0.5345 0.3865 -0.0424 0.0192  0.0347  1872 PHE B CE2 
1497 C CZ  . PHE B 79  ? 0.4149 0.5394 0.3930 -0.0495 0.0304  0.0320  1872 PHE B CZ  
1498 N N   . ASN B 80  ? 0.2894 0.4308 0.2390 -0.0414 0.0162  -0.0293 1873 ASN B N   
1499 C CA  . ASN B 80  ? 0.3139 0.4772 0.2403 -0.0477 0.0067  -0.0251 1873 ASN B CA  
1500 C C   . ASN B 80  ? 0.3390 0.5130 0.2470 -0.0609 0.0117  -0.0474 1873 ASN B C   
1501 O O   . ASN B 80  ? 0.3848 0.5445 0.3007 -0.0648 0.0180  -0.0648 1873 ASN B O   
1502 C CB  . ASN B 80  ? 0.2361 0.4071 0.1708 -0.0407 -0.0101 -0.0124 1873 ASN B CB  
1503 C CG  . ASN B 80  ? 0.2462 0.3980 0.1949 -0.0294 -0.0127 0.0059  1873 ASN B CG  
1504 O OD1 . ASN B 80  ? 0.3486 0.4845 0.3183 -0.0245 -0.0118 0.0034  1873 ASN B OD1 
1505 N ND2 . ASN B 80  ? 0.2739 0.4243 0.2074 -0.0266 -0.0150 0.0243  1873 ASN B ND2 
1506 N N   . GLU B 81  ? 0.4301 0.6267 0.3100 -0.0694 0.0098  -0.0468 1874 GLU B N   
1507 C CA  . GLU B 81  ? 0.4060 0.6163 0.2624 -0.0862 0.0133  -0.0698 1874 GLU B CA  
1508 C C   . GLU B 81  ? 0.3620 0.5970 0.2210 -0.0936 -0.0034 -0.0731 1874 GLU B C   
1509 O O   . GLU B 81  ? 0.3718 0.6223 0.2445 -0.0826 -0.0191 -0.0535 1874 GLU B O   
1510 C CB  . GLU B 81  ? 0.5724 0.8037 0.3944 -0.0943 0.0164  -0.0681 1874 GLU B CB  
1511 C CG  . GLU B 81  ? 0.5579 0.7729 0.3779 -0.0894 0.0354  -0.0664 1874 GLU B CG  
1512 C CD  . GLU B 81  ? 0.4652 0.6569 0.2872 -0.0919 0.0573  -0.0935 1874 GLU B CD  
1513 O OE1 . GLU B 81  ? 0.5715 0.7580 0.3802 -0.1032 0.0604  -0.1129 1874 GLU B OE1 
1514 O OE2 . GLU B 81  ? 0.5167 0.6894 0.3629 -0.0791 0.0691  -0.0909 1874 GLU B OE2 
1515 N N   . ASP B 82  ? 0.3461 0.5797 0.1987 -0.1105 0.0023  -0.0962 1875 ASP B N   
1516 C CA  . ASP B 82  ? 0.4108 0.6645 0.2768 -0.1190 -0.0086 -0.0995 1875 ASP B CA  
1517 C C   . ASP B 82  ? 0.4274 0.7262 0.2916 -0.1152 -0.0262 -0.0813 1875 ASP B C   
1518 O O   . ASP B 82  ? 0.3785 0.7005 0.2615 -0.1104 -0.0379 -0.0727 1875 ASP B O   
1519 C CB  . ASP B 82  ? 0.3627 0.6002 0.2199 -0.1402 0.0046  -0.1257 1875 ASP B CB  
1520 C CG  . ASP B 82  ? 0.5914 0.7795 0.4557 -0.1405 0.0216  -0.1408 1875 ASP B CG  
1521 O OD1 . ASP B 82  ? 0.4700 0.6438 0.3489 -0.1254 0.0211  -0.1321 1875 ASP B OD1 
1522 O OD2 . ASP B 82  ? 0.6187 0.7808 0.4729 -0.1549 0.0358  -0.1602 1875 ASP B OD2 
1523 N N   . ASP B 83  ? 0.3886 0.7001 0.2302 -0.1162 -0.0268 -0.0752 1876 ASP B N   
1524 C CA  . ASP B 83  ? 0.5577 0.9105 0.3958 -0.1110 -0.0428 -0.0575 1876 ASP B CA  
1525 C C   . ASP B 83  ? 0.5749 0.9288 0.4187 -0.0861 -0.0534 -0.0266 1876 ASP B C   
1526 O O   . ASP B 83  ? 0.6321 1.0143 0.4744 -0.0758 -0.0661 -0.0084 1876 ASP B O   
1527 C CB  . ASP B 83  ? 0.6698 1.0371 0.4789 -0.1239 -0.0397 -0.0637 1876 ASP B CB  
1528 C CG  . ASP B 83  ? 0.8197 1.1587 0.6084 -0.1217 -0.0265 -0.0633 1876 ASP B CG  
1529 O OD1 . ASP B 83  ? 0.8349 1.1416 0.6324 -0.1153 -0.0160 -0.0658 1876 ASP B OD1 
1530 O OD2 . ASP B 83  ? 0.8383 1.1901 0.6023 -0.1268 -0.0256 -0.0608 1876 ASP B OD2 
1531 N N   . SER B 84  ? 0.5265 0.8487 0.3763 -0.0758 -0.0477 -0.0200 1877 SER B N   
1532 C CA  . SER B 84  ? 0.5167 0.8311 0.3720 -0.0536 -0.0557 0.0088  1877 SER B CA  
1533 C C   . SER B 84  ? 0.4756 0.8013 0.3592 -0.0404 -0.0665 0.0157  1877 SER B C   
1534 O O   . SER B 84  ? 0.3142 0.6464 0.2159 -0.0495 -0.0652 -0.0023 1877 SER B O   
1535 C CB  . SER B 84  ? 0.5055 0.7852 0.3584 -0.0504 -0.0449 0.0128  1877 SER B CB  
1536 O OG  . SER B 84  ? 0.4635 0.7223 0.3401 -0.0548 -0.0365 -0.0063 1877 SER B OG  
1537 N N   . GLU B 85  ? 0.5096 0.7717 0.3479 -0.0985 -0.1227 0.0481  1878 GLU B N   
1538 C CA  . GLU B 85  ? 0.4042 0.6396 0.2770 -0.0851 -0.1414 0.0401  1878 GLU B CA  
1539 C C   . GLU B 85  ? 0.4000 0.6169 0.3058 -0.0815 -0.1310 0.0352  1878 GLU B C   
1540 O O   . GLU B 85  ? 0.3174 0.5309 0.2501 -0.0759 -0.1318 0.0125  1878 GLU B O   
1541 C CB  . GLU B 85  ? 0.4248 0.6345 0.2980 -0.0741 -0.1647 0.0653  1878 GLU B CB  
1542 C CG  . GLU B 85  ? 0.5963 0.8023 0.4803 -0.0586 -0.1881 0.0469  1878 GLU B CG  
1543 C CD  . GLU B 85  ? 0.6809 0.9125 0.5380 -0.0651 -0.1942 0.0294  1878 GLU B CD  
1544 O OE1 . GLU B 85  ? 0.6906 0.9379 0.5623 -0.0693 -0.1882 0.0001  1878 GLU B OE1 
1545 O OE2 . GLU B 85  ? 0.8115 1.0451 0.6319 -0.0667 -0.2050 0.0450  1878 GLU B OE2 
1546 N N   . VAL B 86  ? 0.3249 0.5308 0.2305 -0.0853 -0.1216 0.0572  1879 VAL B N   
1547 C CA  . VAL B 86  ? 0.2849 0.4679 0.2171 -0.0802 -0.1144 0.0523  1879 VAL B CA  
1548 C C   . VAL B 86  ? 0.2716 0.4629 0.2054 -0.0859 -0.0869 0.0164  1879 VAL B C   
1549 O O   . VAL B 86  ? 0.2484 0.4145 0.2069 -0.0789 -0.0776 -0.0016 1879 VAL B O   
1550 C CB  . VAL B 86  ? 0.2811 0.4410 0.2189 -0.0797 -0.1133 0.0836  1879 VAL B CB  
1551 C CG1 . VAL B 86  ? 0.2476 0.3747 0.2096 -0.0705 -0.1013 0.0730  1879 VAL B CG1 
1552 C CG2 . VAL B 86  ? 0.4370 0.5610 0.3871 -0.0666 -0.1311 0.1029  1879 VAL B CG2 
1553 N N   . GLY B 87  ? 0.3198 0.5389 0.2265 -0.0955 -0.0713 0.0040  1880 GLY B N   
1554 C CA  . GLY B 87  ? 0.4458 0.6632 0.3534 -0.0974 -0.0491 -0.0355 1880 GLY B CA  
1555 C C   . GLY B 87  ? 0.3199 0.5368 0.2448 -0.1000 -0.0569 -0.0626 1880 GLY B C   
1556 O O   . GLY B 87  ? 0.2760 0.4672 0.2225 -0.1003 -0.0432 -0.0838 1880 GLY B O   
1557 N N   . LYS B 88  ? 0.3545 0.5992 0.2721 -0.1029 -0.0801 -0.0608 1881 LYS B N   
1558 C CA  . LYS B 88  ? 0.3093 0.5542 0.2539 -0.1033 -0.0860 -0.0836 1881 LYS B CA  
1559 C C   . LYS B 88  ? 0.2781 0.5080 0.2634 -0.0986 -0.0870 -0.0797 1881 LYS B C   
1560 O O   . LYS B 88  ? 0.2671 0.4920 0.2804 -0.1043 -0.0764 -0.1006 1881 LYS B O   
1561 C CB  . LYS B 88  ? 0.3435 0.6067 0.2755 -0.0993 -0.1094 -0.0785 1881 LYS B CB  
1562 C CG  . LYS B 88  ? 0.4093 0.6779 0.3767 -0.0988 -0.1224 -0.0954 1881 LYS B CG  
1563 C CD  . LYS B 88  ? 0.5043 0.7846 0.4544 -0.0934 -0.1496 -0.0915 1881 LYS B CD  
1564 C CE  . LYS B 88  ? 0.5612 0.8500 0.5529 -0.0925 -0.1659 -0.1040 1881 LYS B CE  
1565 N NZ  . LYS B 88  ? 0.5840 0.8707 0.5721 -0.0804 -0.1974 -0.0884 1881 LYS B NZ  
1566 N N   . ALA B 89  ? 0.2603 0.4807 0.2491 -0.0870 -0.0995 -0.0515 1882 ALA B N   
1567 C CA  . ALA B 89  ? 0.3980 0.6061 0.4216 -0.0750 -0.1024 -0.0486 1882 ALA B CA  
1568 C C   . ALA B 89  ? 0.2182 0.3907 0.2543 -0.0744 -0.0726 -0.0583 1882 ALA B C   
1569 O O   . ALA B 89  ? 0.2598 0.4313 0.3236 -0.0726 -0.0632 -0.0691 1882 ALA B O   
1570 C CB  . ALA B 89  ? 0.2832 0.4728 0.3023 -0.0565 -0.1250 -0.0172 1882 ALA B CB  
1571 N N   . GLY B 90  ? 0.4217 0.5664 0.4372 -0.0757 -0.0574 -0.0539 1883 GLY B N   
1572 C CA  . GLY B 90  ? 0.3111 0.4143 0.3326 -0.0734 -0.0337 -0.0626 1883 GLY B CA  
1573 C C   . GLY B 90  ? 0.2217 0.3254 0.2488 -0.0902 -0.0174 -0.0920 1883 GLY B C   
1574 O O   . GLY B 90  ? 0.3956 0.4702 0.4349 -0.0919 -0.0016 -0.0995 1883 GLY B O   
1575 N N   . HIS B 91  ? 0.2852 0.4185 0.3006 -0.1027 -0.0233 -0.1083 1884 HIS B N   
1576 C CA  . HIS B 91  ? 0.2591 0.3944 0.2855 -0.1194 -0.0175 -0.1372 1884 HIS B CA  
1577 C C   . HIS B 91  ? 0.3412 0.4940 0.4054 -0.1246 -0.0205 -0.1371 1884 HIS B C   
1578 O O   . HIS B 91  ? 0.3142 0.4468 0.3963 -0.1333 -0.0062 -0.1445 1884 HIS B O   
1579 C CB  . HIS B 91  ? 0.2889 0.4498 0.2928 -0.1215 -0.0283 -0.1492 1884 HIS B CB  
1580 C CG  . HIS B 91  ? 0.3421 0.4910 0.3134 -0.1164 -0.0185 -0.1566 1884 HIS B CG  
1581 N ND1 . HIS B 91  ? 0.3317 0.4378 0.3030 -0.1119 -0.0016 -0.1640 1884 HIS B ND1 
1582 C CD2 . HIS B 91  ? 0.3834 0.5605 0.3217 -0.1122 -0.0229 -0.1562 1884 HIS B CD2 
1583 C CE1 . HIS B 91  ? 0.4045 0.5163 0.3505 -0.1039 0.0035  -0.1707 1884 HIS B CE1 
1584 N NE2 . HIS B 91  ? 0.4231 0.5808 0.3474 -0.1051 -0.0067 -0.1666 1884 HIS B NE2 
1585 N N   . ILE B 92  ? 0.2416 0.4324 0.3182 -0.1177 -0.0396 -0.1262 1885 ILE B N   
1586 C CA  . ILE B 92  ? 0.2475 0.4659 0.3650 -0.1189 -0.0429 -0.1280 1885 ILE B CA  
1587 C C   . ILE B 92  ? 0.2185 0.4175 0.3549 -0.1127 -0.0228 -0.1197 1885 ILE B C   
1588 O O   . ILE B 92  ? 0.2217 0.4321 0.3909 -0.1251 -0.0082 -0.1279 1885 ILE B O   
1589 C CB  . ILE B 92  ? 0.2371 0.4903 0.3580 -0.1045 -0.0711 -0.1165 1885 ILE B CB  
1590 C CG1 . ILE B 92  ? 0.2701 0.5360 0.3725 -0.1095 -0.0883 -0.1240 1885 ILE B CG1 
1591 C CG2 . ILE B 92  ? 0.2260 0.5097 0.3924 -0.0976 -0.0730 -0.1171 1885 ILE B CG2 
1592 C CD1 . ILE B 92  ? 0.2821 0.5661 0.3800 -0.0952 -0.1173 -0.1099 1885 ILE B CD1 
1593 N N   . MET B 93  ? 0.2126 0.3776 0.3253 -0.0918 -0.0212 -0.1000 1886 MET B N   
1594 C CA  . MET B 93  ? 0.2613 0.3999 0.3801 -0.0766 -0.0053 -0.0895 1886 MET B CA  
1595 C C   . MET B 93  ? 0.2785 0.3727 0.3887 -0.0898 0.0222  -0.0962 1886 MET B C   
1596 O O   . MET B 93  ? 0.2914 0.3772 0.4132 -0.0887 0.0408  -0.0932 1886 MET B O   
1597 C CB  . MET B 93  ? 0.1888 0.2983 0.2846 -0.0496 -0.0191 -0.0683 1886 MET B CB  
1598 C CG  . MET B 93  ? 0.1840 0.3259 0.2882 -0.0326 -0.0507 -0.0575 1886 MET B CG  
1599 S SD  . MET B 93  ? 0.1985 0.3924 0.3454 -0.0211 -0.0548 -0.0673 1886 MET B SD  
1600 C CE  . MET B 93  ? 0.1832 0.3425 0.3279 -0.0052 -0.0241 -0.0647 1886 MET B CE  
1601 N N   . ARG B 94  ? 0.3125 0.3774 0.3995 -0.1007 0.0247  -0.1051 1887 ARG B N   
1602 C CA  . ARG B 94  ? 0.2888 0.3058 0.3666 -0.1133 0.0446  -0.1141 1887 ARG B CA  
1603 C C   . ARG B 94  ? 0.3180 0.3541 0.4239 -0.1376 0.0532  -0.1246 1887 ARG B C   
1604 O O   . ARG B 94  ? 0.3014 0.3061 0.4059 -0.1429 0.0708  -0.1186 1887 ARG B O   
1605 C CB  . ARG B 94  ? 0.2938 0.2844 0.3428 -0.1112 0.0405  -0.1217 1887 ARG B CB  
1606 C CG  . ARG B 94  ? 0.3177 0.2613 0.3521 -0.1078 0.0506  -0.1184 1887 ARG B CG  
1607 C CD  . ARG B 94  ? 0.3342 0.2699 0.3533 -0.1057 0.0419  -0.1289 1887 ARG B CD  
1608 N NE  . ARG B 94  ? 0.4498 0.3886 0.4530 -0.0909 0.0371  -0.1270 1887 ARG B NE  
1609 C CZ  . ARG B 94  ? 0.4181 0.3280 0.4088 -0.0721 0.0369  -0.1141 1887 ARG B CZ  
1610 N NH1 . ARG B 94  ? 0.3947 0.2721 0.3812 -0.0632 0.0371  -0.1012 1887 ARG B NH1 
1611 N NH2 . ARG B 94  ? 0.2981 0.2176 0.2811 -0.0636 0.0344  -0.1146 1887 ARG B NH2 
1612 N N   . ARG B 95  ? 0.3452 0.4290 0.4706 -0.1474 0.0378  -0.1346 1888 ARG B N   
1613 C CA  A ARG B 95  ? 0.3277 0.4305 0.4830 -0.1662 0.0408  -0.1396 1888 ARG B CA  
1614 C CA  B ARG B 95  ? 0.3433 0.4458 0.4985 -0.1662 0.0409  -0.1396 1888 ARG B CA  
1615 C C   . ARG B 95  ? 0.3424 0.4810 0.5360 -0.1691 0.0551  -0.1302 1888 ARG B C   
1616 O O   . ARG B 95  ? 0.3377 0.4706 0.5478 -0.1842 0.0712  -0.1249 1888 ARG B O   
1617 C CB  A ARG B 95  ? 0.3609 0.5012 0.5265 -0.1718 0.0173  -0.1527 1888 ARG B CB  
1618 C CB  B ARG B 95  ? 0.3683 0.5073 0.5332 -0.1720 0.0174  -0.1529 1888 ARG B CB  
1619 C CG  A ARG B 95  ? 0.4158 0.5252 0.5486 -0.1716 0.0074  -0.1652 1888 ARG B CG  
1620 C CG  B ARG B 95  ? 0.4086 0.5177 0.5373 -0.1691 0.0072  -0.1647 1888 ARG B CG  
1621 C CD  A ARG B 95  ? 0.4459 0.5899 0.5863 -0.1765 -0.0162 -0.1793 1888 ARG B CD  
1622 C CD  B ARG B 95  ? 0.4411 0.5779 0.5782 -0.1769 -0.0150 -0.1802 1888 ARG B CD  
1623 N NE  A ARG B 95  ? 0.4511 0.6191 0.6353 -0.1941 -0.0210 -0.1819 1888 ARG B NE  
1624 N NE  B ARG B 95  ? 0.4615 0.5965 0.6309 -0.1972 -0.0174 -0.1853 1888 ARG B NE  
1625 C CZ  A ARG B 95  ? 0.4639 0.6078 0.6602 -0.2118 -0.0228 -0.1883 1888 ARG B CZ  
1626 C CZ  B ARG B 95  ? 0.4583 0.6360 0.6709 -0.2081 -0.0239 -0.1840 1888 ARG B CZ  
1627 N NH1 A ARG B 95  ? 0.4821 0.5750 0.6467 -0.2103 -0.0220 -0.1943 1888 ARG B NH1 
1628 N NH1 B ARG B 95  ? 0.4537 0.6770 0.6798 -0.1966 -0.0306 -0.1791 1888 ARG B NH1 
1629 N NH2 A ARG B 95  ? 0.4161 0.5873 0.6582 -0.2303 -0.0279 -0.1875 1888 ARG B NH2 
1630 N NH2 B ARG B 95  ? 0.4291 0.6038 0.6733 -0.2298 -0.0266 -0.1863 1888 ARG B NH2 
1631 N N   . PHE B 96  ? 0.2628 0.4424 0.4715 -0.1528 0.0483  -0.1266 1889 PHE B N   
1632 C CA  . PHE B 96  ? 0.2699 0.4863 0.5094 -0.1427 0.0623  -0.1168 1889 PHE B CA  
1633 C C   . PHE B 96  ? 0.2509 0.4168 0.4653 -0.1363 0.0912  -0.1020 1889 PHE B C   
1634 O O   . PHE B 96  ? 0.2752 0.4599 0.5137 -0.1485 0.1158  -0.0966 1889 PHE B O   
1635 C CB  . PHE B 96  ? 0.2132 0.4615 0.4529 -0.1092 0.0401  -0.1109 1889 PHE B CB  
1636 C CG  . PHE B 96  ? 0.2648 0.5529 0.5326 -0.0899 0.0516  -0.1051 1889 PHE B CG  
1637 C CD1 . PHE B 96  ? 0.3363 0.6896 0.6606 -0.1074 0.0638  -0.1136 1889 PHE B CD1 
1638 C CD2 . PHE B 96  ? 0.2043 0.4671 0.4442 -0.0530 0.0498  -0.0927 1889 PHE B CD2 
1639 C CE1 . PHE B 96  ? 0.2720 0.6721 0.6238 -0.0868 0.0778  -0.1104 1889 PHE B CE1 
1640 C CE2 . PHE B 96  ? 0.3183 0.6206 0.5802 -0.0298 0.0601  -0.0915 1889 PHE B CE2 
1641 C CZ  . PHE B 96  ? 0.2528 0.6269 0.5700 -0.0458 0.0762  -0.1005 1889 PHE B CZ  
1642 N N   . PHE B 97  ? 0.3217 0.4238 0.4875 -0.1187 0.0888  -0.0949 1890 PHE B N   
1643 C CA  . PHE B 97  ? 0.2839 0.3306 0.4188 -0.1081 0.1110  -0.0817 1890 PHE B CA  
1644 C C   . PHE B 97  ? 0.3056 0.3200 0.4407 -0.1417 0.1324  -0.0832 1890 PHE B C   
1645 O O   . PHE B 97  ? 0.3309 0.3365 0.4638 -0.1459 0.1577  -0.0707 1890 PHE B O   
1646 C CB  . PHE B 97  ? 0.2625 0.2483 0.3520 -0.0832 0.0985  -0.0761 1890 PHE B CB  
1647 C CG  . PHE B 97  ? 0.3048 0.2220 0.3574 -0.0740 0.1162  -0.0664 1890 PHE B CG  
1648 C CD1 . PHE B 97  ? 0.3350 0.2462 0.3736 -0.0473 0.1262  -0.0538 1890 PHE B CD1 
1649 C CD2 . PHE B 97  ? 0.3877 0.2447 0.4167 -0.0897 0.1206  -0.0718 1890 PHE B CD2 
1650 C CE1 . PHE B 97  ? 0.3572 0.2019 0.3547 -0.0372 0.1408  -0.0447 1890 PHE B CE1 
1651 C CE2 . PHE B 97  ? 0.4561 0.2648 0.4472 -0.0732 0.1263  -0.0581 1890 PHE B CE2 
1652 C CZ  . PHE B 97  ? 0.4532 0.2374 0.4269 -0.0541 0.1429  -0.0475 1890 PHE B CZ  
1653 N N   . GLU B 98  ? 0.3599 0.3524 0.4887 -0.1596 0.1184  -0.0959 1891 GLU B N   
1654 C CA  A GLU B 98  ? 0.4241 0.3803 0.5408 -0.1753 0.1225  -0.0921 1891 GLU B CA  
1655 C CA  B GLU B 98  ? 0.4230 0.3796 0.5399 -0.1754 0.1222  -0.0923 1891 GLU B CA  
1656 C C   . GLU B 98  ? 0.4008 0.4053 0.5616 -0.2004 0.1322  -0.0871 1891 GLU B C   
1657 O O   . GLU B 98  ? 0.4217 0.4029 0.5783 -0.2144 0.1464  -0.0735 1891 GLU B O   
1658 C CB  A GLU B 98  ? 0.4501 0.3833 0.5496 -0.1750 0.0986  -0.1047 1891 GLU B CB  
1659 C CB  B GLU B 98  ? 0.4477 0.3837 0.5490 -0.1757 0.0980  -0.1054 1891 GLU B CB  
1660 C CG  A GLU B 98  ? 0.4501 0.3390 0.5073 -0.1475 0.0902  -0.1026 1891 GLU B CG  
1661 C CG  B GLU B 98  ? 0.4467 0.3408 0.5067 -0.1485 0.0891  -0.1041 1891 GLU B CG  
1662 C CD  A GLU B 98  ? 0.5010 0.3759 0.5458 -0.1448 0.0697  -0.1132 1891 GLU B CD  
1663 C CD  B GLU B 98  ? 0.4742 0.3175 0.5039 -0.1356 0.0982  -0.0886 1891 GLU B CD  
1664 O OE1 A GLU B 98  ? 0.5154 0.4214 0.5770 -0.1561 0.0584  -0.1280 1891 GLU B OE1 
1665 O OE1 B GLU B 98  ? 0.5463 0.3674 0.5752 -0.1511 0.1031  -0.0834 1891 GLU B OE1 
1666 O OE2 A GLU B 98  ? 0.5401 0.3759 0.5597 -0.1297 0.0623  -0.1074 1891 GLU B OE2 
1667 O OE2 B GLU B 98  ? 0.5229 0.3506 0.5307 -0.1100 0.0966  -0.0799 1891 GLU B OE2 
1668 N N   . SER B 99  ? 0.3775 0.4515 0.5814 -0.2050 0.1220  -0.0957 1892 SER B N   
1669 C CA  . SER B 99  ? 0.3943 0.5220 0.6469 -0.2253 0.1283  -0.0898 1892 SER B CA  
1670 C C   . SER B 99  ? 0.4286 0.5831 0.6919 -0.2192 0.1591  -0.0714 1892 SER B C   
1671 O O   . SER B 99  ? 0.4569 0.6232 0.7391 -0.2390 0.1751  -0.0564 1892 SER B O   
1672 C CB  . SER B 99  ? 0.3544 0.5483 0.6471 -0.2241 0.1057  -0.1040 1892 SER B CB  
1673 O OG  . SER B 99  ? 0.4040 0.6559 0.7498 -0.2398 0.1118  -0.0976 1892 SER B OG  
1674 N N   . ARG B 100 ? 0.3948 0.5613 0.6459 -0.1901 0.1673  -0.0710 1893 ARG B N   
1675 C CA  . ARG B 100 ? 0.4234 0.6189 0.6775 -0.1737 0.1959  -0.0561 1893 ARG B CA  
1676 C C   . ARG B 100 ? 0.4438 0.5665 0.6455 -0.1742 0.2194  -0.0383 1893 ARG B C   
1677 O O   . ARG B 100 ? 0.6071 0.7478 0.8091 -0.1766 0.2442  -0.0209 1893 ARG B O   
1678 C CB  . ARG B 100 ? 0.4065 0.6358 0.6628 -0.1346 0.1907  -0.0642 1893 ARG B CB  
1679 C CG  . ARG B 100 ? 0.4319 0.7127 0.6992 -0.1080 0.2121  -0.0559 1893 ARG B CG  
1680 C CD  . ARG B 100 ? 0.4651 0.8222 0.7894 -0.1275 0.2158  -0.0531 1893 ARG B CD  
1681 N NE  . ARG B 100 ? 0.5673 0.9639 0.8943 -0.1113 0.2465  -0.0380 1893 ARG B NE  
1682 C CZ  . ARG B 100 ? 0.4878 0.9546 0.8442 -0.0786 0.2467  -0.0441 1893 ARG B CZ  
1683 N NH1 . ARG B 100 ? 0.4437 0.9435 0.7973 -0.0620 0.2776  -0.0297 1893 ARG B NH1 
1684 N NH2 . ARG B 100 ? 0.4373 0.9380 0.8226 -0.0606 0.2137  -0.0643 1893 ARG B NH2 
1685 N N   . TRP B 101 ? 0.4419 0.4832 0.5967 -0.1703 0.2097  -0.0420 1894 TRP B N   
1686 C CA  . TRP B 101 ? 0.5177 0.4796 0.6179 -0.1680 0.2236  -0.0270 1894 TRP B CA  
1687 C C   . TRP B 101 ? 0.5507 0.5010 0.6585 -0.2012 0.2253  -0.0168 1894 TRP B C   
1688 O O   . TRP B 101 ? 0.5828 0.5024 0.6621 -0.2043 0.2437  0.0024  1894 TRP B O   
1689 C CB  . TRP B 101 ? 0.5306 0.4139 0.5855 -0.1525 0.2039  -0.0362 1894 TRP B CB  
1690 C CG  . TRP B 101 ? 0.4742 0.2772 0.4686 -0.1357 0.2102  -0.0238 1894 TRP B CG  
1691 C CD1 . TRP B 101 ? 0.5515 0.3062 0.5194 -0.1441 0.1989  -0.0211 1894 TRP B CD1 
1692 C CD2 . TRP B 101 ? 0.5709 0.3363 0.5226 -0.1017 0.2229  -0.0131 1894 TRP B CD2 
1693 N NE1 . TRP B 101 ? 0.6580 0.3571 0.5733 -0.1189 0.2018  -0.0116 1894 TRP B NE1 
1694 C CE2 . TRP B 101 ? 0.6381 0.3372 0.5394 -0.0917 0.2156  -0.0074 1894 TRP B CE2 
1695 C CE3 . TRP B 101 ? 0.5428 0.3427 0.4941 -0.0636 0.2203  -0.0124 1894 TRP B CE3 
1696 C CZ2 . TRP B 101 ? 0.6446 0.2983 0.4942 -0.0559 0.2178  0.0008  1894 TRP B CZ2 
1697 C CZ3 . TRP B 101 ? 0.7042 0.4513 0.6016 -0.0249 0.2203  -0.0039 1894 TRP B CZ3 
1698 C CH2 . TRP B 101 ? 0.7430 0.4009 0.5852 -0.0262 0.2273  0.0058  1894 TRP B CH2 
1699 N N   . GLU B 102 ? 0.5978 0.5692 0.7413 -0.2250 0.2039  -0.0282 1895 GLU B N   
1700 C CA  . GLU B 102 ? 0.7357 0.6975 0.8949 -0.2577 0.2014  -0.0170 1895 GLU B CA  
1701 C C   . GLU B 102 ? 0.6876 0.7191 0.8916 -0.2763 0.2252  0.0029  1895 GLU B C   
1702 O O   . GLU B 102 ? 0.7478 0.7666 0.9584 -0.3031 0.2322  0.0228  1895 GLU B O   
1703 C CB  . GLU B 102 ? 0.8075 0.7712 0.9917 -0.2729 0.1692  -0.0356 1895 GLU B CB  
1704 C CG  . GLU B 102 ? 0.9137 0.8452 1.1081 -0.3036 0.1571  -0.0260 1895 GLU B CG  
1705 C CD  . GLU B 102 ? 0.9866 0.8347 1.1271 -0.2967 0.1548  -0.0165 1895 GLU B CD  
1706 O OE1 . GLU B 102 ? 0.9937 0.8186 1.1401 -0.3214 0.1572  0.0036  1895 GLU B OE1 
1707 O OE2 . GLU B 102 ? 1.0051 0.8139 1.1011 -0.2659 0.1482  -0.0276 1895 GLU B OE2 
1708 N N   . GLU B 103 ? 0.6677 0.7762 0.9050 -0.2611 0.2361  -0.0008 1896 GLU B N   
1709 C CA  . GLU B 103 ? 0.7319 0.9203 1.0166 -0.2725 0.2584  0.0168  1896 GLU B CA  
1710 C C   . GLU B 103 ? 0.8234 1.0106 1.0724 -0.2571 0.2931  0.0397  1896 GLU B C   
1711 O O   . GLU B 103 ? 0.8335 1.0895 1.1168 -0.2654 0.3161  0.0582  1896 GLU B O   
1712 C CB  . GLU B 103 ? 0.6855 0.9621 1.0234 -0.2566 0.2508  0.0008  1896 GLU B CB  
1713 C CG  . GLU B 103 ? 0.7111 1.0062 1.0932 -0.2768 0.2185  -0.0169 1896 GLU B CG  
1714 C CD  . GLU B 103 ? 0.7240 1.1109 1.1652 -0.2650 0.2110  -0.0281 1896 GLU B CD  
1715 O OE1 . GLU B 103 ? 0.7719 1.2063 1.2706 -0.2895 0.2053  -0.0246 1896 GLU B OE1 
1716 O OE2 . GLU B 103 ? 0.6902 1.0993 1.1218 -0.2304 0.2080  -0.0400 1896 GLU B OE2 
1717 N N   . PHE B 104 ? 0.8416 0.9547 1.0224 -0.2329 0.2968  0.0392  1897 PHE B N   
1718 C CA  . PHE B 104 ? 0.8045 0.9009 0.9379 -0.2169 0.3256  0.0604  1897 PHE B CA  
1719 C C   . PHE B 104 ? 0.8403 0.8537 0.9319 -0.2411 0.3254  0.0784  1897 PHE B C   
1720 O O   . PHE B 104 ? 0.8566 0.8921 0.9620 -0.2686 0.3419  0.1039  1897 PHE B O   
1721 C CB  . PHE B 104 ? 0.7950 0.8566 0.8765 -0.1686 0.3264  0.0493  1897 PHE B CB  
1722 C CG  . PHE B 104 ? 0.7680 0.9078 0.8854 -0.1380 0.3230  0.0326  1897 PHE B CG  
1723 C CD1 . PHE B 104 ? 0.8252 1.0704 1.0066 -0.1452 0.3314  0.0335  1897 PHE B CD1 
1724 C CD2 . PHE B 104 ? 0.7881 0.8949 0.8770 -0.0993 0.3084  0.0168  1897 PHE B CD2 
1725 C CE1 . PHE B 104 ? 0.8090 1.1235 1.0235 -0.1122 0.3227  0.0159  1897 PHE B CE1 
1726 C CE2 . PHE B 104 ? 0.7638 0.9385 0.8853 -0.0678 0.2990  0.0009  1897 PHE B CE2 
1727 C CZ  . PHE B 104 ? 0.7651 1.0430 0.9482 -0.0736 0.3051  -0.0011 1897 PHE B CZ  
1728 N N   . TYR B 105 ? 0.8869 0.8083 0.9310 -0.2300 0.3042  0.0658  1898 TYR B N   
1729 C CA  . TYR B 105 ? 0.9519 0.7867 0.9485 -0.2412 0.2969  0.0780  1898 TYR B CA  
1730 C C   . TYR B 105 ? 0.9568 0.7834 0.9907 -0.2809 0.2750  0.0794  1898 TYR B C   
1731 O O   . TYR B 105 ? 1.0396 0.8770 1.0907 -0.3122 0.2851  0.1050  1898 TYR B O   
1732 C CB  . TYR B 105 ? 0.9399 0.6902 0.8783 -0.2072 0.2771  0.0604  1898 TYR B CB  
1733 C CG  . TYR B 105 ? 0.8254 0.5791 0.7358 -0.1647 0.2892  0.0545  1898 TYR B CG  
1734 C CD1 . TYR B 105 ? 0.8093 0.5229 0.6607 -0.1379 0.3051  0.0684  1898 TYR B CD1 
1735 C CD2 . TYR B 105 ? 0.7152 0.5098 0.6566 -0.1494 0.2814  0.0359  1898 TYR B CD2 
1736 C CE1 . TYR B 105 ? 0.7722 0.4839 0.5960 -0.0936 0.3103  0.0631  1898 TYR B CE1 
1737 C CE2 . TYR B 105 ? 0.7203 0.5158 0.6375 -0.1081 0.2881  0.0332  1898 TYR B CE2 
1738 C CZ  . TYR B 105 ? 0.7150 0.4676 0.5728 -0.0784 0.3011  0.0465  1898 TYR B CZ  
1739 O OH  . TYR B 105 ? 0.8103 0.5612 0.6413 -0.0303 0.2993  0.0422  1898 TYR B OH  
# 
