data_27063 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Degenerate heptads 27-52 of human RNA polymerase II C-terminal domain (DNA-directed RNA polymerase II subunit RPB1): assignments and backbone relaxation ; _BMRB_accession_number 27063 _BMRB_flat_file_name bmr27063.str _Entry_type original _Submission_date 2017-04-04 _Accession_date 2017-04-04 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Janke Abigail M. . 2 Burke Kathleen A. . 3 Fawzi Nicolas L. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 heteronucl_NOE 1 T1_relaxation 1 T2_relaxation 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 108 "13C chemical shifts" 425 "15N chemical shifts" 108 "T1 relaxation values" 58 "T2 relaxation values" 59 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-05-18 update BMRB 'update entry citation' 2017-10-04 original author 'original release' stop_ _Original_release_date 2017-04-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Lysines in RNA polymerase II C-terminal domain contribute to TAF15 fibril recruitment ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28945358 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Janke Abigail M. . 2 Seo Dahee . . 3 Burke Kathleen A. . 4 Conicella Alexander E. . 5 Rahmanian Vahid . . 6 Mittal Jeetain . . 7 Fawzi Nicolas L. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 57 _Journal_issue 17 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2549 _Page_last 2563 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'CTD27-52 monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CTD27-52 monomer' $RNA_Pol_II_CTD27-52 stop_ _System_molecular_weight . _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_RNA_Pol_II_CTD27-52 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common RNA_Pol_II_CTD27-52 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 201 _Mol_residue_sequence ; GHMSPNYTPTSPNYSPTSPS YSPTSPSYSPTSPSYSPSSP RYTPQSPTYTPSSPSYSPSS PSYSPASPKYTPTSPSYSPS SPEYTPTSPKYSPTSPKYSP TSPKYSPTSPTYSPTTPKYS PTSPTYSPTSPVYTPTSPKY SPTSPTYSPTSPKYSPTSPT YSPTSPKGSTYSPTSPGYSP TSPTYSLTSPAISPDDSDEE N ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLY 2 2 HIS 3 3 MET 4 1773 SER 5 1774 PRO 6 1775 ASN 7 1776 TYR 8 1777 THR 9 1778 PRO 10 1779 THR 11 1780 SER 12 1781 PRO 13 1782 ASN 14 1783 TYR 15 1784 SER 16 1785 PRO 17 1786 THR 18 1787 SER 19 1788 PRO 20 1789 SER 21 1790 TYR 22 1791 SER 23 1792 PRO 24 1793 THR 25 1794 SER 26 1795 PRO 27 1796 SER 28 1797 TYR 29 1798 SER 30 1799 PRO 31 1800 THR 32 1801 SER 33 1802 PRO 34 1803 SER 35 1804 TYR 36 1805 SER 37 1806 PRO 38 1807 SER 39 1808 SER 40 1809 PRO 41 1810 ARG 42 1811 TYR 43 1812 THR 44 1813 PRO 45 1814 GLN 46 1815 SER 47 1816 PRO 48 1817 THR 49 1818 TYR 50 1819 THR 51 1820 PRO 52 1821 SER 53 1822 SER 54 1823 PRO 55 1824 SER 56 1825 TYR 57 1826 SER 58 1827 PRO 59 1828 SER 60 1829 SER 61 1830 PRO 62 1831 SER 63 1832 TYR 64 1833 SER 65 1834 PRO 66 1835 ALA 67 1836 SER 68 1837 PRO 69 1838 LYS 70 1839 TYR 71 1840 THR 72 1841 PRO 73 1842 THR 74 1843 SER 75 1844 PRO 76 1845 SER 77 1846 TYR 78 1847 SER 79 1848 PRO 80 1849 SER 81 1850 SER 82 1851 PRO 83 1852 GLU 84 1853 TYR 85 1854 THR 86 1855 PRO 87 1856 THR 88 1857 SER 89 1858 PRO 90 1859 LYS 91 1860 TYR 92 1861 SER 93 1862 PRO 94 1863 THR 95 1864 SER 96 1865 PRO 97 1866 LYS 98 1867 TYR 99 1868 SER 100 1869 PRO 101 1870 THR 102 1871 SER 103 1872 PRO 104 1873 LYS 105 1874 TYR 106 1875 SER 107 1876 PRO 108 1877 THR 109 1878 SER 110 1879 PRO 111 1880 THR 112 1881 TYR 113 1882 SER 114 1883 PRO 115 1884 THR 116 1885 THR 117 1886 PRO 118 1887 LYS 119 1888 TYR 120 1889 SER 121 1890 PRO 122 1891 THR 123 1892 SER 124 1893 PRO 125 1894 THR 126 1895 TYR 127 1896 SER 128 1897 PRO 129 1898 THR 130 1899 SER 131 1900 PRO 132 1901 VAL 133 1902 TYR 134 1903 THR 135 1904 PRO 136 1905 THR 137 1906 SER 138 1907 PRO 139 1908 LYS 140 1909 TYR 141 1910 SER 142 1911 PRO 143 1912 THR 144 1913 SER 145 1914 PRO 146 1915 THR 147 1916 TYR 148 1917 SER 149 1918 PRO 150 1919 THR 151 1920 SER 152 1921 PRO 153 1922 LYS 154 1923 TYR 155 1924 SER 156 1925 PRO 157 1926 THR 158 1927 SER 159 1928 PRO 160 1929 THR 161 1930 TYR 162 1931 SER 163 1932 PRO 164 1933 THR 165 1934 SER 166 1935 PRO 167 1936 LYS 168 1937 GLY 169 1938 SER 170 1939 THR 171 1940 TYR 172 1941 SER 173 1942 PRO 174 1943 THR 175 1944 SER 176 1945 PRO 177 1946 GLY 178 1947 TYR 179 1948 SER 180 1949 PRO 181 1950 THR 182 1951 SER 183 1952 PRO 184 1953 THR 185 1954 TYR 186 1955 SER 187 1956 LEU 188 1957 THR 189 1958 SER 190 1959 PRO 191 1960 ALA 192 1961 ILE 193 1962 SER 194 1963 PRO 195 1964 ASP 196 1965 ASP 197 1966 SER 198 1967 ASP 199 1968 GLU 200 1969 GLU 201 1970 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value UNP P24928 'DNA-directed RNA polymerase II subunit RPB1' . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RNA_Pol_II_CTD27-52 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $RNA_Pol_II_CTD27-52 'recombinant technology' . Escherichia coli 'BL21 Star DE3' pJ411 'expressed with N-terminal his fusion tag, cleaved.' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '13C/15N sample for assignment' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RNA_Pol_II_CTD27-52 500 uM '[U-99% 13C; U-99% 15N]' TRIS 20 mM 'natural abundance' 'sodium chloride' 200 mM 'natural abundance' EDTA 0.5 mM 'natural abundance' beta-mercaptoethanol 20 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details '15N sample for backbone relaxation' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RNA_Pol_II_CTD27-52 250 uM '[U-99% 15N]' TRIS 20 mM 'natural abundance' 'sodium chloride' 200 mM 'natural abundance' EDTA 0.5 mM 'natural abundance' beta-mercaptoethanol 20 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _Details 'TCI cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HCACO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_(H)N(CA)NNH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (H)N(CA)NNH' _Sample_label $sample_1 save_ save_15N_R2_8 _Saveframe_category NMR_applied_experiment _Experiment_name '15N R2' _Sample_label $sample_2 save_ save_15N_R1_9 _Saveframe_category NMR_applied_experiment _Experiment_name '15N R1' _Sample_label $sample_2 save_ save_1H_15N_het_NOE_10 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 15N het NOE' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 . pH pressure 1 . atm temperature 277 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details 'referenced to water, water resonance predicted by bruk2pipe. 13C, 15N indirect reference by bruk2pipe.' loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl carbon' ppm 0.00 na indirect . . . 1.0 DSS H 1 'methyl protons' ppm 0.00 external direct . . . 1.0 DSS N 15 nitrogen ppm 0.00 na indirect . . . 1.0 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $CARA stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HCACO' '3D HNCACB' '3D CBCA(CO)NH' '3D HNCA' '3D (H)N(CA)NNH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'CTD27-52 monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1773 4 SER H H 8.494 0.020 1 2 1773 4 SER C C 172.816 0.3 1 3 1773 4 SER CA C 56.535 0.3 1 4 1773 4 SER CB C 63.123 0.3 1 5 1773 4 SER N N 119.107 0.3 1 6 1774 5 PRO C C 176.396 0.3 1 7 1774 5 PRO CA C 63.258 0.3 1 8 1774 5 PRO CB C 31.797 0.3 1 9 1775 6 ASN H H 8.444 0.020 1 10 1775 6 ASN C C 174.560 0.3 1 11 1775 6 ASN CA C 52.973 0.3 1 12 1775 6 ASN CB C 38.519 0.3 1 13 1775 6 ASN N N 118.155 0.3 1 14 1776 7 TYR H H 8.142 0.020 1 15 1776 7 TYR C C 175.245 0.3 1 16 1776 7 TYR CA C 57.813 0.3 1 17 1776 7 TYR CB C 38.721 0.3 1 18 1776 7 TYR N N 121.596 0.3 1 19 1777 8 THR H H 8.135 0.020 1 20 1777 8 THR C C 178.606 0.3 1 21 1777 8 THR CA C 59.090 0.3 1 22 1777 8 THR CB C 69.846 0.3 1 23 1777 8 THR N N 120.624 0.3 1 24 1778 9 PRO C C 176.972 0.3 1 25 1778 9 PRO CA C 63.056 0.3 1 26 1778 9 PRO CB C 31.932 0.3 1 27 1779 10 THR H H 8.180 0.020 1 28 1779 10 THR C C 174.412 0.3 1 29 1779 10 THR CA C 61.779 0.3 1 30 1779 10 THR CB C 69.644 0.3 1 31 1779 10 THR N N 113.516 0.3 1 32 1780 11 SER H H 8.345 0.020 1 33 1780 11 SER C C 172.926 0.3 1 34 1780 11 SER CA C 56.334 0.3 1 35 1780 11 SER CB C 63.325 0.3 1 36 1780 11 SER N N 119.651 0.3 1 37 1781 12 PRO C C 176.387 0.3 1 38 1781 12 PRO CA C 63.325 0.3 1 39 1781 12 PRO CB C 31.797 0.3 1 40 1782 13 ASN H H 8.422 0.020 1 41 1782 13 ASN C C 174.567 0.3 1 42 1782 13 ASN CA C 52.838 0.3 1 43 1782 13 ASN CB C 38.519 0.3 1 44 1782 13 ASN N N 117.858 0.3 1 45 1783 14 TYR H H 8.091 0.020 1 46 1783 14 TYR C C 175.276 0.3 1 47 1783 14 TYR CA C 58.014 0.3 1 48 1783 14 TYR CB C 38.676 0.3 1 49 1783 14 TYR N N 121.404 0.3 1 50 1784 15 SER H H 8.175 0.020 1 51 1784 15 SER C C 178.769 0.3 1 52 1784 15 SER CA C 55.393 0.3 1 53 1784 15 SER CB C 63.527 0.3 1 54 1784 15 SER N N 120.359 0.3 1 55 1785 16 PRO C C 177.050 0.3 1 56 1785 16 PRO CA C 63.191 0.3 1 57 1785 16 PRO CB C 31.932 0.3 1 58 1786 17 THR H H 8.121 0.020 1 59 1786 17 THR C C 174.459 0.3 1 60 1786 17 THR CA C 61.644 0.3 1 61 1786 17 THR CB C 69.577 0.3 1 62 1786 17 THR N N 112.755 0.3 1 63 1787 18 SER H H 8.266 0.020 1 64 1787 18 SER C C 172.778 0.3 1 65 1787 18 SER CA C 56.468 0.3 1 66 1787 18 SER CB C 63.258 0.3 1 67 1787 18 SER N N 119.695 0.3 1 68 1802 33 PRO C C 176.793 0.3 1 69 1802 33 PRO CA C 63.258 0.3 1 70 1802 33 PRO CB C 31.864 0.3 1 71 1803 34 SER H H 8.349 0.020 1 72 1803 34 SER C C 173.852 0.3 1 73 1803 34 SER CA C 58.082 0.3 1 74 1803 34 SER CB C 63.661 0.3 1 75 1803 34 SER N N 115.417 0.3 1 76 1804 35 TYR H H 8.170 0.020 1 77 1804 35 TYR C C 175.221 0.3 1 78 1804 35 TYR CA C 57.880 0.3 1 79 1804 35 TYR CB C 38.856 0.3 1 80 1804 35 TYR N N 122.580 0.3 1 81 1805 36 SER H H 8.222 0.020 1 82 1805 36 SER C C 178.902 0.3 1 83 1805 36 SER CA C 55.527 0.3 1 84 1805 36 SER CB C 63.527 0.3 1 85 1805 36 SER N N 120.260 0.3 1 86 1806 37 PRO C C 176.863 0.3 1 87 1806 37 PRO CA C 63.325 0.3 1 88 1806 37 PRO CB C 31.864 0.3 1 89 1807 38 SER H H 8.238 0.020 1 90 1807 38 SER C C 174.233 0.3 1 91 1807 38 SER CA C 58.216 0.3 1 92 1807 38 SER CB C 63.661 0.3 1 93 1807 38 SER N N 114.490 0.3 1 94 1808 39 SER H H 8.191 0.020 1 95 1808 39 SER C C 172.701 0.3 1 96 1808 39 SER CA C 56.468 0.3 1 97 1808 39 SER CB C 63.325 0.3 1 98 1808 39 SER N N 118.948 0.3 1 99 1809 40 PRO C C 176.700 0.3 1 100 1809 40 PRO CA C 63.325 0.3 1 101 1809 40 PRO CB C 31.864 0.3 1 102 1810 41 ARG H H 8.386 0.020 1 103 1810 41 ARG C C 175.782 0.3 1 104 1810 41 ARG CA C 55.961 0.3 1 105 1810 41 ARG CB C 30.453 0.3 1 106 1810 41 ARG N N 120.768 0.3 1 107 1811 42 TYR H H 8.244 0.020 1 108 1811 42 TYR C C 175.280 0.3 1 109 1811 42 TYR CA C 57.746 0.3 1 110 1811 42 TYR CB C 38.788 0.3 1 111 1811 42 TYR N N 121.938 0.3 1 112 1812 43 THR H H 8.097 0.020 1 113 1812 43 THR C C 178.466 0.3 1 114 1812 43 THR CA C 59.090 0.3 1 115 1812 43 THR CB C 69.980 0.3 1 116 1812 43 THR N N 120.637 0.3 1 117 1813 44 PRO C C 176.692 0.3 1 118 1813 44 PRO CA C 62.922 0.3 1 119 1813 44 PRO CB C 31.797 0.3 1 120 1814 45 GLN H H 8.510 0.020 1 121 1814 45 GLN C C 175.836 0.3 1 122 1814 45 GLN CA C 55.527 0.3 1 123 1814 45 GLN CB C 29.377 0.3 1 124 1814 45 GLN N N 120.511 0.3 1 125 1815 46 SER H H 8.481 0.020 1 126 1815 46 SER C C 172.802 0.3 1 127 1815 46 SER CA C 56.603 0.3 1 128 1815 46 SER CB C 63.056 0.3 1 129 1815 46 SER N N 119.097 0.3 1 130 1816 47 PRO C C 176.894 0.3 1 131 1816 47 PRO CA C 63.191 0.3 1 132 1816 47 PRO CB C 31.999 0.3 1 133 1817 48 THR H H 8.220 0.020 1 134 1817 48 THR C C 174.008 0.3 1 135 1817 48 THR CA C 61.779 0.3 1 136 1817 48 THR CB C 69.779 0.3 1 137 1817 48 THR N N 113.908 0.3 1 138 1818 49 TYR H H 8.268 0.020 1 139 1818 49 TYR C C 175.076 0.3 1 140 1818 49 TYR CA C 57.861 0.3 1 141 1818 49 TYR CB C 39.014 0.3 1 142 1818 49 TYR N N 123.761 0.3 1 143 1819 50 THR H H 8.160 0.020 1 144 1819 50 THR C C 178.512 0.3 1 145 1819 50 THR CA C 59.023 0.3 1 146 1819 50 THR CB C 69.913 0.3 1 147 1819 50 THR N N 121.038 0.3 1 148 1820 51 PRO C C 176.739 0.3 1 149 1820 51 PRO CA C 63.056 0.3 1 150 1820 51 PRO CB C 31.999 0.3 1 151 1821 52 SER H H 8.398 0.020 1 152 1821 52 SER C C 174.210 0.3 1 153 1821 52 SER CA C 58.283 0.3 1 154 1821 52 SER CB C 63.594 0.3 1 155 1821 52 SER N N 115.858 0.3 1 156 1822 53 SER H H 8.348 0.020 1 157 1822 53 SER C C 172.756 0.3 1 158 1822 53 SER CA C 56.334 0.3 1 159 1822 53 SER CB C 63.325 0.3 1 160 1822 53 SER N N 118.872 0.3 1 161 1823 54 PRO C C 176.754 0.3 1 162 1823 54 PRO CA C 63.258 0.3 1 163 1823 54 PRO CB C 31.932 0.3 1 164 1824 55 SER H H 8.365 0.020 1 165 1824 55 SER C C 173.899 0.3 1 166 1824 55 SER CA C 58.082 0.3 1 167 1824 55 SER CB C 63.661 0.3 1 168 1824 55 SER N N 115.567 0.3 1 169 1825 56 TYR H H 8.190 0.020 1 170 1825 56 TYR C C 175.198 0.3 1 171 1825 56 TYR CA C 57.813 0.3 1 172 1825 56 TYR CB C 38.923 0.3 1 173 1825 56 TYR N N 122.591 0.3 1 174 1826 57 SER H H 8.201 0.020 1 175 1826 57 SER C C 178.746 0.3 1 176 1826 57 SER CA C 55.460 0.3 1 177 1826 57 SER CB C 63.527 0.3 1 178 1826 57 SER N N 120.318 0.3 1 179 1827 58 PRO C C 176.824 0.3 1 180 1827 58 PRO CA C 63.191 0.3 1 181 1827 58 PRO CB C 31.797 0.3 1 182 1828 59 SER H H 8.283 0.020 1 183 1828 59 SER C C 174.156 0.3 1 184 1828 59 SER CA C 58.216 0.3 1 185 1828 59 SER CB C 63.661 0.3 1 186 1828 59 SER N N 115.009 0.3 1 187 1829 60 SER H H 8.265 0.020 1 188 1829 60 SER C C 172.810 0.3 1 189 1829 60 SER CA C 56.401 0.3 1 190 1829 60 SER CB C 63.258 0.3 1 191 1829 60 SER N N 118.931 0.3 1 192 1834 65 PRO C C 176.445 0.3 1 193 1834 65 PRO CA C 63.073 0.3 1 194 1834 65 PRO CB C 31.872 0.3 1 195 1835 66 ALA H H 8.303 0.020 1 196 1835 66 ALA C C 177.597 0.3 1 197 1835 66 ALA CA C 52.185 0.3 1 198 1835 66 ALA CB C 19.052 0.3 1 199 1835 66 ALA N N 123.376 0.3 1 200 1836 67 SER H H 8.298 0.020 1 201 1836 67 SER C C 172.740 0.3 1 202 1836 67 SER CA C 56.267 0.3 1 203 1836 67 SER CB C 63.123 0.3 1 204 1836 67 SER N N 116.732 0.3 1 205 1837 68 PRO C C 176.653 0.3 1 206 1837 68 PRO CA C 63.123 0.3 1 207 1837 68 PRO CB C 31.932 0.3 1 208 1838 69 LYS H H 8.376 0.020 1 209 1838 69 LYS C C 176.132 0.3 1 210 1838 69 LYS CA C 56.267 0.3 1 211 1838 69 LYS CB C 32.738 0.3 1 212 1838 69 LYS N N 121.296 0.3 1 213 1839 70 TYR H H 8.267 0.020 1 214 1839 70 TYR C C 175.220 0.3 1 215 1839 70 TYR CA C 57.611 0.3 1 216 1839 70 TYR CB C 38.856 0.3 1 217 1839 70 TYR N N 122.112 0.3 1 218 1840 71 THR H H 8.130 0.020 1 219 1840 71 THR C C 178.489 0.3 1 220 1840 71 THR CA C 59.090 0.3 1 221 1840 71 THR CB C 69.913 0.3 1 222 1840 71 THR N N 121.008 0.3 1 223 1841 72 PRO C C 176.949 0.3 1 224 1841 72 PRO CA C 62.989 0.3 1 225 1841 72 PRO CB C 31.999 0.3 1 226 1842 73 THR H H 8.252 0.020 1 227 1842 73 THR C C 174.389 0.3 1 228 1842 73 THR CA C 61.913 0.3 1 229 1842 73 THR CB C 69.711 0.3 1 230 1842 73 THR N N 114.171 0.3 1 231 1843 74 SER H H 8.387 0.020 1 232 1843 74 SER CA C 56.468 0.3 1 233 1843 74 SER CB C 63.258 0.3 1 234 1843 74 SER N N 119.876 0.3 1 235 1845 76 SER H H 8.361 0.020 1 236 1845 76 SER C C 173.876 0.3 1 237 1845 76 SER CA C 58.036 0.3 1 238 1845 76 SER CB C 63.706 0.3 1 239 1845 76 SER N N 115.563 0.3 1 240 1846 77 TYR H H 8.194 0.020 1 241 1846 77 TYR C C 175.221 0.3 1 242 1846 77 TYR CA C 57.823 0.3 1 243 1846 77 TYR CB C 38.921 0.3 1 244 1846 77 TYR N N 122.600 0.3 1 245 1847 78 SER H H 8.171 0.020 1 246 1847 78 SER C C 178.793 0.3 1 247 1847 78 SER CA C 55.409 0.3 1 248 1847 78 SER CB C 63.490 0.3 1 249 1847 78 SER N N 120.329 0.3 1 250 1848 79 PRO C C 174.233 0.3 1 251 1848 79 PRO CA C 63.215 0.3 1 252 1848 79 PRO CB C 31.831 0.3 1 253 1849 80 SER H H 8.277 0.020 1 254 1849 80 SER C C 176.801 0.3 1 255 1849 80 SER CA C 58.196 0.3 1 256 1849 80 SER CB C 63.677 0.3 1 257 1849 80 SER N N 114.955 0.3 1 258 1850 81 SER H H 8.284 0.020 1 259 1850 81 SER C C 172.887 0.3 1 260 1850 81 SER CA C 56.468 0.3 1 261 1850 81 SER CB C 63.325 0.3 1 262 1850 81 SER N N 119.027 0.3 1 263 1851 82 PRO C C 176.840 0.3 1 264 1851 82 PRO CA C 63.392 0.3 1 265 1851 82 PRO CB C 31.864 0.3 1 266 1852 83 GLU H H 8.544 0.020 1 267 1852 83 GLU C C 175.945 0.3 1 268 1852 83 GLU CA C 56.535 0.3 1 269 1852 83 GLU CB C 29.780 0.3 1 270 1852 83 GLU N N 120.092 0.3 1 271 1853 84 TYR H H 8.160 0.020 1 272 1853 84 TYR C C 175.268 0.3 1 273 1853 84 TYR CA C 57.813 0.3 1 274 1853 84 TYR CB C 38.788 0.3 1 275 1853 84 TYR N N 121.720 0.3 1 276 1854 85 THR H H 8.058 0.020 1 277 1854 85 THR C C 178.637 0.3 1 278 1854 85 THR CA C 59.090 0.3 1 279 1854 85 THR CB C 69.913 0.3 1 280 1854 85 THR N N 120.627 0.3 1 281 1857 88 SER H H 8.338 0.020 1 282 1857 88 SER CA C 56.468 0.3 1 283 1857 88 SER CB C 63.191 0.3 1 284 1857 88 SER N N 119.802 0.3 1 285 1861 92 SER H H 8.233 0.020 1 286 1861 92 SER C C 178.870 0.3 1 287 1861 92 SER CA C 55.460 0.3 1 288 1861 92 SER CB C 63.527 0.3 1 289 1861 92 SER N N 120.353 0.3 1 290 1867 98 TYR H H 8.196 0.020 1 291 1867 98 TYR C C 175.253 0.3 1 292 1867 98 TYR CA C 57.611 0.3 1 293 1867 98 TYR CB C 38.856 0.3 1 294 1867 98 TYR N N 121.524 0.3 1 295 1886 117 PRO C C 176.521 0.3 1 296 1886 117 PRO CA C 63.056 0.3 1 297 1886 117 PRO CB C 31.999 0.3 1 298 1887 118 LYS H H 8.454 0.020 1 299 1887 118 LYS C C 176.131 0.3 1 300 1887 118 LYS CA C 56.267 0.3 1 301 1887 118 LYS CB C 32.873 0.3 1 302 1887 118 LYS N N 122.070 0.3 1 303 1888 119 TYR H H 8.332 0.020 1 304 1888 119 TYR C C 175.221 0.3 1 305 1888 119 TYR CA C 57.611 0.3 1 306 1888 119 TYR CB C 38.856 0.3 1 307 1888 119 TYR N N 122.090 0.3 1 308 1889 120 SER H H 8.236 0.020 1 309 1889 120 SER C C 178.801 0.3 1 310 1889 120 SER CA C 55.410 0.3 1 311 1889 120 SER CB C 63.473 0.3 1 312 1889 120 SER N N 120.528 0.3 1 313 1890 121 PRO C C 177.050 0.3 1 314 1890 121 PRO CA C 63.123 0.3 1 315 1890 121 PRO CB C 31.999 0.3 1 316 1891 122 THR H H 8.246 0.020 1 317 1891 122 THR C C 174.475 0.3 1 318 1891 122 THR CA C 61.712 0.3 1 319 1891 122 THR CB C 69.644 0.3 1 320 1891 122 THR N N 113.784 0.3 1 321 1892 123 SER H H 8.198 0.020 1 322 1892 123 SER CA C 56.535 0.3 1 323 1892 123 SER CB C 63.191 0.3 1 324 1892 123 SER N N 119.730 0.3 1 325 1893 124 PRO C C 176.848 0.3 1 326 1893 124 PRO CA C 63.267 0.3 1 327 1893 124 PRO CB C 32.014 0.3 1 328 1894 125 THR H H 8.227 0.020 1 329 1894 125 THR C C 174.031 0.3 1 330 1894 125 THR CA C 61.749 0.3 1 331 1894 125 THR CB C 69.619 0.3 1 332 1894 125 THR N N 114.092 0.3 1 333 1895 126 TYR H H 8.259 0.020 1 334 1895 126 TYR C C 175.147 0.3 1 335 1895 126 TYR CA C 57.814 0.3 1 336 1895 126 TYR CB C 38.996 0.3 1 337 1895 126 TYR N N 123.486 0.3 1 338 1896 127 SER H H 8.236 0.020 1 339 1896 127 SER C C 178.754 0.3 1 340 1896 127 SER CA C 55.416 0.3 1 341 1896 127 SER CB C 63.499 0.3 1 342 1896 127 SER N N 120.616 0.3 1 343 1897 128 PRO C C 176.995 0.3 1 344 1897 128 PRO CA C 63.056 0.3 1 345 1897 128 PRO CB C 31.999 0.3 1 346 1898 129 THR H H 8.201 0.020 1 347 1898 129 THR C C 174.420 0.3 1 348 1898 129 THR CA C 61.779 0.3 1 349 1898 129 THR CB C 69.711 0.3 1 350 1898 129 THR N N 113.622 0.3 1 351 1899 130 SER H H 8.356 0.020 1 352 1899 130 SER CA C 56.401 0.3 1 353 1899 130 SER CB C 63.191 0.3 1 354 1899 130 SER N N 119.851 0.3 1 355 1900 131 PRO C C 176.442 0.3 1 356 1900 131 PRO CA C 63.056 0.3 1 357 1900 131 PRO CB C 31.932 0.3 1 358 1901 132 VAL H H 8.217 0.020 1 359 1901 132 VAL C C 175.734 0.3 1 360 1901 132 VAL CA C 62.048 0.3 1 361 1901 132 VAL CB C 32.671 0.3 1 362 1901 132 VAL N N 120.505 0.3 1 363 1902 133 TYR H H 8.443 0.020 1 364 1902 133 TYR C C 175.212 0.3 1 365 1902 133 TYR CA C 57.659 0.3 1 366 1902 133 TYR CB C 38.961 0.3 1 367 1902 133 TYR N N 125.559 0.3 1 368 1903 134 THR H H 8.158 0.020 1 369 1903 134 THR C C 178.668 0.3 1 370 1903 134 THR CA C 59.090 0.3 1 371 1903 134 THR CB C 69.779 0.3 1 372 1903 134 THR N N 120.829 0.3 1 373 1904 135 PRO C C 177.004 0.3 1 374 1904 135 PRO CA C 63.123 0.3 1 375 1904 135 PRO CB C 32.011 0.3 1 376 1905 136 THR H H 8.177 0.020 1 377 1905 136 THR C C 174.486 0.3 1 378 1905 136 THR CA C 61.650 0.3 1 379 1905 136 THR CB C 69.600 0.3 1 380 1905 136 THR N N 113.285 0.3 1 381 1907 138 PRO C C 176.653 0.3 1 382 1907 138 PRO CA C 63.191 0.3 1 383 1907 138 PRO CB C 31.932 0.3 1 384 1908 139 LYS H H 8.370 0.020 1 385 1908 139 LYS C C 176.116 0.3 1 386 1908 139 LYS CA C 56.267 0.3 1 387 1908 139 LYS CB C 32.738 0.3 1 388 1908 139 LYS N N 121.272 0.3 1 389 1909 140 TYR H H 8.235 0.020 1 390 1909 140 TYR C C 175.237 0.3 1 391 1909 140 TYR CA C 57.611 0.3 1 392 1909 140 TYR CB C 38.856 0.3 1 393 1909 140 TYR N N 121.743 0.3 1 394 1910 141 SER H H 8.200 0.020 1 395 1910 141 SER C C 178.703 0.3 1 396 1910 141 SER CA C 55.406 0.3 1 397 1910 141 SER CB C 63.479 0.3 1 398 1910 141 SER N N 120.484 0.3 1 399 1914 145 PRO CA C 63.269 0.3 1 400 1914 145 PRO CB C 31.999 0.3 1 401 1915 146 THR H H 8.223 0.020 1 402 1915 146 THR C C 174.020 0.3 1 403 1915 146 THR CA C 61.748 0.3 1 404 1915 146 THR CB C 69.615 0.3 1 405 1915 146 THR N N 114.116 0.3 1 406 1916 147 TYR H H 8.252 0.020 1 407 1916 147 TYR C C 175.124 0.3 1 408 1916 147 TYR CA C 57.826 0.3 1 409 1916 147 TYR CB C 39.010 0.3 1 410 1916 147 TYR N N 123.390 0.3 1 411 1917 148 SER H H 8.254 0.020 1 412 1917 148 SER C C 178.924 0.3 1 413 1917 148 SER CA C 55.393 0.3 1 414 1917 148 SER CB C 63.527 0.3 1 415 1917 148 SER N N 120.485 0.3 1 416 1918 149 PRO C C 177.065 0.3 1 417 1918 149 PRO CA C 63.258 0.3 1 418 1918 149 PRO CB C 31.932 0.3 1 419 1919 150 THR H H 8.100 0.020 1 420 1919 150 THR C C 174.435 0.3 1 421 1919 150 THR CA C 61.510 0.3 1 422 1919 150 THR CB C 69.577 0.3 1 423 1919 150 THR N N 112.402 0.3 1 424 1920 151 SER H H 8.236 0.020 1 425 1920 151 SER C C 172.756 0.3 1 426 1920 151 SER CA C 56.485 0.3 1 427 1920 151 SER CB C 63.209 0.3 1 428 1920 151 SER N N 119.739 0.3 1 429 1921 152 PRO C C 176.691 0.3 1 430 1921 152 PRO CA C 63.191 0.3 1 431 1921 152 PRO CB C 31.932 0.3 1 432 1922 153 LYS H H 8.363 0.020 1 433 1922 153 LYS C C 176.123 0.3 1 434 1922 153 LYS CA C 56.267 0.3 1 435 1922 153 LYS CB C 32.738 0.3 1 436 1922 153 LYS N N 121.144 0.3 1 437 1923 154 TYR H H 8.217 0.020 1 438 1923 154 TYR C C 175.298 0.3 1 439 1923 154 TYR CA C 57.591 0.3 1 440 1923 154 TYR CB C 38.892 0.3 1 441 1923 154 TYR N N 121.691 0.3 1 442 1924 155 SER H H 8.178 0.020 1 443 1924 155 SER C C 178.701 0.3 1 444 1924 155 SER CA C 55.406 0.3 1 445 1924 155 SER CB C 63.499 0.3 1 446 1924 155 SER N N 120.415 0.3 1 447 1925 156 PRO C C 177.096 0.3 1 448 1925 156 PRO CA C 63.258 0.3 1 449 1925 156 PRO CB C 31.999 0.3 1 450 1926 157 THR H H 8.158 0.020 1 451 1926 157 THR C C 174.496 0.3 1 452 1926 157 THR CA C 61.644 0.3 1 453 1926 157 THR CB C 69.644 0.3 1 454 1926 157 THR N N 112.891 0.3 1 455 1927 158 SER H H 8.250 0.020 1 456 1927 158 SER C C 172.764 0.3 1 457 1927 158 SER CA C 56.456 0.3 1 458 1927 158 SER CB C 63.264 0.3 1 459 1927 158 SER N N 119.651 0.3 1 460 1928 159 PRO C C 176.848 0.3 1 461 1928 159 PRO CA C 63.258 0.3 1 462 1928 159 PRO CB C 31.999 0.3 1 463 1929 160 THR H H 8.226 0.020 1 464 1929 160 THR C C 174.000 0.3 1 465 1929 160 THR CA C 61.779 0.3 1 466 1929 160 THR CB C 69.644 0.3 1 467 1929 160 THR N N 114.105 0.3 1 468 1930 161 TYR H H 8.255 0.020 1 469 1930 161 TYR C C 175.131 0.3 1 470 1930 161 TYR CA C 57.870 0.3 1 471 1930 161 TYR CB C 38.974 0.3 1 472 1930 161 TYR N N 123.487 0.3 1 473 1931 162 SER H H 8.223 0.020 1 474 1931 162 SER C C 178.676 0.3 1 475 1931 162 SER CA C 55.393 0.3 1 476 1931 162 SER CB C 63.460 0.3 1 477 1931 162 SER N N 120.675 0.3 1 478 1935 166 PRO C C 177.104 0.3 1 479 1935 166 PRO CA C 63.191 0.3 1 480 1935 166 PRO CB C 31.999 0.3 1 481 1936 167 LYS H H 8.538 0.020 1 482 1936 167 LYS C C 177.299 0.3 1 483 1936 167 LYS CA C 56.535 0.3 1 484 1936 167 LYS CB C 32.671 0.3 1 485 1936 167 LYS N N 121.881 0.3 1 486 1937 168 GLY H H 8.496 0.020 1 487 1937 168 GLY C C 174.143 0.3 1 488 1937 168 GLY CA C 44.970 0.3 1 489 1937 168 GLY N N 110.511 0.3 1 490 1938 169 SER H H 8.320 0.020 1 491 1938 169 SER C C 174.770 0.3 1 492 1938 169 SER CA C 58.325 0.3 1 493 1938 169 SER CB C 63.870 0.3 1 494 1938 169 SER N N 115.679 0.3 1 495 1939 170 THR H H 8.296 0.020 1 496 1939 170 THR C C 174.013 0.3 1 497 1939 170 THR CA C 61.779 0.3 1 498 1939 170 THR CB C 69.644 0.3 1 499 1939 170 THR N N 115.983 0.3 1 500 1940 171 TYR H H 8.310 0.020 1 501 1940 171 TYR C C 175.178 0.3 1 502 1940 171 TYR CA C 58.003 0.3 1 503 1940 171 TYR CB C 38.845 0.3 1 504 1940 171 TYR N N 123.516 0.3 1 505 1941 172 SER H H 8.220 0.020 1 506 1941 172 SER C C 178.684 0.3 1 507 1941 172 SER CA C 55.393 0.3 1 508 1941 172 SER CB C 63.460 0.3 1 509 1941 172 SER N N 120.762 0.3 1 510 1942 173 PRO C C 177.029 0.3 1 511 1942 173 PRO CA C 63.168 0.3 1 512 1942 173 PRO CB C 31.935 0.3 1 513 1943 174 THR H H 8.057 0.020 1 514 1943 174 THR C C 174.507 0.3 1 515 1943 174 THR CA C 61.594 0.3 1 516 1943 174 THR CB C 69.465 0.3 1 517 1943 174 THR N N 112.151 0.3 1 518 1944 175 SER H H 8.254 0.020 1 519 1944 175 SER C C 172.764 0.3 1 520 1944 175 SER CA C 56.468 0.3 1 521 1944 175 SER CB C 63.191 0.3 1 522 1944 175 SER N N 119.791 0.3 1 523 1945 176 PRO C C 177.502 0.3 1 524 1945 176 PRO CA C 63.609 0.3 1 525 1945 176 PRO CB C 31.746 0.3 1 526 1946 177 GLY H H 8.533 0.020 1 527 1946 177 GLY C C 173.582 0.3 1 528 1946 177 GLY CA C 44.907 0.3 1 529 1946 177 GLY N N 109.478 0.3 1 530 1947 178 TYR H H 7.992 0.020 1 531 1947 178 TYR C C 175.384 0.3 1 532 1947 178 TYR CA C 58.149 0.3 1 533 1947 178 TYR CB C 38.923 0.3 1 534 1947 178 TYR N N 120.700 0.3 1 535 1948 179 SER H H 8.120 0.020 1 536 1948 179 SER C C 178.629 0.3 1 537 1948 179 SER CA C 55.333 0.3 1 538 1948 179 SER CB C 63.594 0.3 1 539 1948 179 SER N N 120.832 0.3 1 540 1949 180 PRO C C 177.026 0.3 1 541 1949 180 PRO CA C 63.056 0.3 1 542 1949 180 PRO CB C 31.999 0.3 1 543 1950 181 THR H H 8.157 0.020 1 544 1950 181 THR C C 174.488 0.3 1 545 1950 181 THR CA C 61.644 0.3 1 546 1950 181 THR CB C 69.644 0.3 1 547 1950 181 THR N N 113.167 0.3 1 548 1951 182 SER H H 8.269 0.020 1 549 1951 182 SER C C 172.787 0.3 1 550 1951 182 SER CA C 56.498 0.3 1 551 1951 182 SER CB C 63.263 0.3 1 552 1951 182 SER N N 119.768 0.3 1 553 1952 183 PRO C C 176.899 0.3 1 554 1952 183 PRO CA C 63.230 0.3 1 555 1952 183 PRO CB C 32.002 0.3 1 556 1953 184 THR H H 8.206 0.020 1 557 1953 184 THR C C 174.207 0.3 1 558 1953 184 THR CA C 61.780 0.3 1 559 1953 184 THR CB C 69.716 0.3 1 560 1953 184 THR N N 113.858 0.3 1 561 1954 185 TYR H H 8.158 0.020 1 562 1954 185 TYR C C 175.482 0.3 1 563 1954 185 TYR CA C 57.891 0.3 1 564 1954 185 TYR CB C 38.876 0.3 1 565 1954 185 TYR N N 122.751 0.3 1 566 1955 186 SER H H 8.256 0.020 1 567 1955 186 SER C C 174.209 0.3 1 568 1955 186 SER CA C 57.813 0.3 1 569 1955 186 SER CB C 63.930 0.3 1 570 1955 186 SER N N 117.719 0.3 1 571 1956 187 LEU H H 8.400 0.020 1 572 1956 187 LEU C C 177.656 0.3 1 573 1956 187 LEU CA C 55.422 0.3 1 574 1956 187 LEU CB C 42.175 0.3 1 575 1956 187 LEU N N 124.450 0.3 1 576 1957 188 THR H H 8.162 0.020 1 577 1957 188 THR C C 174.257 0.3 1 578 1957 188 THR CA C 61.577 0.3 1 579 1957 188 THR CB C 69.711 0.3 1 580 1957 188 THR N N 114.093 0.3 1 581 1958 189 SER H H 8.328 0.020 1 582 1958 189 SER C C 178.723 0.3 1 583 1958 189 SER CA C 56.468 0.3 1 584 1958 189 SER CB C 63.191 0.3 1 585 1958 189 SER N N 119.903 0.3 1 586 1959 190 PRO C C 176.396 0.3 1 587 1959 190 PRO CA C 62.989 0.3 1 588 1959 190 PRO CB C 31.864 0.3 1 589 1960 191 ALA H H 8.462 0.020 1 590 1960 191 ALA C C 177.594 0.3 1 591 1960 191 ALA CA C 52.300 0.3 1 592 1960 191 ALA CB C 18.890 0.3 1 593 1960 191 ALA N N 124.751 0.3 1 594 1961 192 ILE H H 8.264 0.020 1 595 1961 192 ILE C C 176.178 0.3 1 596 1961 192 ILE CA C 60.502 0.3 1 597 1961 192 ILE CB C 38.654 0.3 1 598 1961 192 ILE N N 121.052 0.3 1 599 1962 193 SER H H 8.680 0.020 1 600 1962 193 SER C C 172.989 0.3 1 601 1962 193 SER CA C 55.930 0.3 1 602 1962 193 SER CB C 63.325 0.3 1 603 1962 193 SER N N 122.472 0.3 1 604 1963 194 PRO C C 176.645 0.3 1 605 1963 194 PRO CA C 63.258 0.3 1 606 1963 194 PRO CB C 31.932 0.3 1 607 1964 195 ASP H H 8.395 0.020 1 608 1964 195 ASP C C 176.038 0.3 1 609 1964 195 ASP CA C 54.250 0.3 1 610 1964 195 ASP CB C 40.940 0.3 1 611 1964 195 ASP N N 120.136 0.3 1 612 1965 196 ASP H H 8.263 0.020 1 613 1965 196 ASP C C 176.357 0.3 1 614 1965 196 ASP CA C 54.250 0.3 1 615 1965 196 ASP CB C 40.940 0.3 1 616 1965 196 ASP N N 121.309 0.3 1 617 1966 197 SER H H 8.319 0.020 1 618 1966 197 SER C C 174.404 0.3 1 619 1966 197 SER CA C 58.485 0.3 1 620 1966 197 SER CB C 63.930 0.3 1 621 1966 197 SER N N 116.118 0.3 1 622 1967 198 ASP H H 8.510 0.020 1 623 1967 198 ASP C C 176.248 0.3 1 624 1967 198 ASP CA C 54.250 0.3 1 625 1967 198 ASP CB C 40.940 0.3 1 626 1967 198 ASP N N 122.924 0.3 1 627 1968 199 GLU H H 8.338 0.020 1 628 1968 199 GLU C C 176.384 0.3 1 629 1968 199 GLU CA C 56.468 0.3 1 630 1968 199 GLU CB C 30.251 0.3 1 631 1968 199 GLU N N 121.015 0.3 1 632 1969 200 GLU H H 8.511 0.020 1 633 1969 200 GLU C C 175.439 0.3 1 634 1969 200 GLU CA C 56.406 0.3 1 635 1969 200 GLU CB C 30.010 0.3 1 636 1969 200 GLU N N 122.302 0.3 1 637 1970 201 ASN H H 8.156 0.020 1 638 1970 201 ASN C C 173.167 0.3 1 639 1970 201 ASN CA C 54.586 0.3 1 640 1970 201 ASN CB C 40.335 0.3 1 641 1970 201 ASN N N 125.472 0.3 1 stop_ save_ save_heteronuclear_T1_list_1 _Saveframe_category T1_relaxation _Details 'R1 in s-1' loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 850 _T1_coherence_type Sz _T1_value_units s-1 _Mol_system_component_name 'CTD27-52 monomer' _Text_data_format . _Text_data . loop_ _T1_ID _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 1 6 ASN N 1.40872848167244 0.0164837217355536 2 7 TYR N 1.43165972311701 0.0073921144082818 3 8 THR N 1.48729847105717 0.00759452599699206 4 11 SER N 1.35814206165965 0.00876917276508027 5 13 ASN N 1.348199479595 0.0139643230541624 6 14 TYR N 1.36694187763136 0.00848596639236843 7 38 SER N 1.24917242326958 0.0198051361312557 8 39 SER N 1.23421744442936 0.0133390602117378 9 41 ARG N 1.32823291892466 0.0107878605354013 10 42 TYR N 1.37532664007702 0.0114891518162945 11 43 THR N 1.33198358996217 0.0110437144544409 12 45 GLN N 1.27594962550878 0.00985587892171513 13 49 TYR N 1.32074225714852 0.00965621715051213 14 50 THR N 1.33561277914307 0.00970500375169792 15 52 SER N 1.20310883322505 0.0166309474901287 16 53 SER N 1.2479253241486 0.0130678567785725 17 60 SER N 1.2299366582621 0.0124930621477284 18 66 ALA N 1.31483794622313 0.00759169027138085 19 67 SER N 1.21193024129531 0.0079102694372728 20 70 TYR N 1.35703623286742 0.0116105600441416 21 71 THR N 1.32761573490169 0.0105200786574529 22 74 SER N 1.26144763730858 0.0100767271326865 23 81 SER N 1.2441060475995 0.0107113532545564 24 83 GLU N 1.36763358361028 0.00745873665037244 25 84 TYR N 1.39047248254957 0.0090267486355271 26 85 THR N 1.34367063945286 0.0103048627975852 27 118 LYS N 1.35803139768591 0.00808807437994785 28 119 TYR N 1.34867223218741 0.0100697575190309 29 122 THR N 1.23748592359762 0.0119946048726693 30 129 THR N 1.25631297268776 0.00851076147665086 31 130 SER N 1.20770029709427 0.00959834436392404 32 133 TYR N 1.3550502723651 0.00968172293039116 33 134 THR N 1.33086679354263 0.0106605890435352 34 157 THR N 1.30917469627147 0.013225910445928 35 167 LYS N 1.37153515930381 0.0108719681661551 36 168 GLY N 1.30142245474303 0.0238690099823455 37 169 SER N 1.22524995099 0.019568492240053 38 170 THR N 1.26924492619341 0.027558324114259 39 171 TYR N 1.38171166440987 0.0094715174097022 40 174 THR N 1.3603776408331 0.0119853294105075 41 177 GLY N 1.31257711390544 0.0186635091684193 42 178 TYR N 1.41765548136492 0.00744399770421778 43 179 SER N 1.3675026666302 0.0113900163585112 44 181 THR N 1.2956388795315 0.0134550952194838 45 185 TYR N 1.41131308569493 0.0100687902931964 46 186 SER N 1.35976720785402 0.0167892645493311 47 187 LEU N 1.42541515216307 0.0119808612190893 48 188 THR N 1.33750635315518 0.0105729910203987 49 191 ALA N 1.44381397900694 0.00518964263270738 50 192 ILE N 1.39616055846422 0.00513465870500607 51 193 SER N 1.45602795573675 0.00697824989667239 52 195 ASP N 1.5158864904196 0.00523334583489454 53 196 ASP N 1.5504597113044 0.00518064393540718 54 197 SER N 1.54681433587526 0.0045406330681601 55 198 ASP N 1.62482736209278 0.00536244905788363 56 199 GLU N 1.5673244204818 0.0035458636477963 57 200 GLU N 1.51984923095629 0.00340020129056606 58 201 ASN N 1.21860567139079 0.00203949084454358 stop_ save_ save_heteronuclear_T2_list_1 _Saveframe_category T2_relaxation _Details 'in phase component CPMG (555 Hz) derived R2 using bruker tc expt' loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 850 _T2_coherence_type S(+,-) _T2_value_units s-1 _Mol_system_component_name 'CTD27-52 monomer' _Text_data_format . _Text_data . loop_ _T2_ID _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error _Rex_value _Rex_error 1 6 ASN N 4.65484336452078 0.0358763748253015 . . 2 7 TYR N 5.15756356697096 0.0227657693583971 . . 3 8 THR N 6.14854894244958 0.0262661233829009 . . 4 11 SER N 6.23830318153462 0.0306718303936693 . . 5 13 ASN N 6.41807329439702 0.0490063599763735 . . 6 14 TYR N 6.31153749053269 0.032435383146816 . . 7 38 SER N 7.81921964187974 0.114089785747852 . . 8 39 SER N 7.64467548352572 0.0703618958303789 . . 9 41 ARG N 8.49401172173618 0.0775613419240404 . . 10 42 TYR N 8.57927247769389 0.086073590232024 . . 11 43 THR N 8.78966335589347 0.0873185412773463 . . 12 45 GLN N 8.30357884248111 0.0735038049785821 . . 13 49 TYR N 7.52388834549695 0.0599931760723651 . . 14 50 THR N 8.00704620065658 0.0649690909691891 . . 15 52 SER N 7.52275633792221 0.0943761163940335 . . 16 53 SER N 7.02296509586347 0.0597797794164725 . . 17 60 SER N 6.7258541834813 0.0507516179709233 . . 18 66 ALA N 7.0997515086972 0.0402802216038136 . . 19 67 SER N 6.78886625933469 0.0399072970318501 . . 20 70 TYR N 8.19269211863018 0.080426698247642 . . 21 71 THR N 8.34445927903872 0.0766784503530733 . . 22 74 SER N 7.55686541222701 0.0589792001721952 . . 23 81 SER N 7.58898079987858 0.060969704941658 . . 24 83 GLU N 8.5404389785635 0.058559702436094 . . 25 84 TYR N 8.18062827225131 0.0628864722640348 . . 26 85 THR N 8.92379082634303 0.0837169313730257 . . 27 118 LYS N 7.15000715000715 0.0415626042641035 . . 28 119 TYR N 7.97066794197354 0.0667349159661708 . . 29 122 THR N 7.32547066149 0.0626128031665161 . . 30 123 SER N 7.40850496369833 0.0484681152120352 . . 31 133 TYR N 8.24878330446259 0.0721726069525115 . . 32 134 THR N 8.94774516821761 0.0839733239550515 . . 33 140 TYR N 8.17394147457904 0.0756107809722888 . . 34 150 THR N 8.66400970369087 0.096769339824796 . . 35 157 THR N 6.72359308814631 0.0555715560695758 . . 36 167 LYS N 5.75738384478093 0.0385987278586688 . . 37 168 GLY N 5.32453011021777 0.0738107636980381 . . 38 169 SER N 5.46746856205577 0.0624221562438567 . . 39 170 THR N 5.40306894315971 0.0817477131315067 . . 40 171 TYR N 6.20809535634467 0.0364496433140618 . . 41 174 THR N 6.90750846169786 0.0538171974700603 . . 42 177 GLY N 5.98659003831418 0.0651438136930933 . . 43 178 TYR N 6.43542055473325 0.0292171336778058 . . 44 179 SER N 6.4998375040624 0.0441597526939512 . . 45 181 THR N 6.56512605042017 0.0546855894594307 . . 46 185 TYR N 6.23596906959341 0.0374063112475218 . . 47 186 SER N 6.35122261035249 0.0557071248491017 . . 48 187 LEU N 5.47825134217158 0.0413958419804104 . . 49 188 THR N 5.46209307406598 0.0373286617384982 . . 50 191 ALA N 4.33952438812706 0.0135734896245427 . . 51 192 ILE N 4.31685732786531 0.0148084440957872 . . 52 193 SER N 4.61424880029531 0.0190359762135639 . . 53 195 ASP N 4.47367243770411 0.0130307686734685 . . 54 196 ASP N 3.84497077822209 0.0115705135726989 . . 55 197 SER N 3.39904826648538 0.0100625549119138 . . 56 198 ASP N 3.14376434342482 0.0102993680313417 . . 57 199 GLU N 2.80772686433064 0.00750229799764357 . . 58 200 GLU N 2.38994311935376 0.00688367371835641 . . 59 201 ASN N 1.72786177105832 0.0052888419830539 . . stop_ save_ save_heteronuclear_noe_list_1 _Saveframe_category heteronuclear_NOE _Details . loop_ _Experiment_label '1H 15N het NOE' stop_ loop_ _Sample_label . stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 850 _Mol_system_component_name 'CTD27-52 monomer' _Atom_one_atom_name N _Atom_two_atom_name H _Heteronuclear_NOE_value_type 'peak height' _NOE_reference_value 0 _NOE_reference_description . _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 6 ASN 0.3803 0.0215546330749294 7 TYR 0.4091 0.0113254174101582 8 THR 0.4316 0.0116224943428412 11 SER 0.4356 0.0134084416343127 13 ASN 0.4340 0.0208583668598348 14 TYR 0.4635 0.0139436100678466 38 SER 0.3708 0.0335989837467239 39 SER 0.4089 0.0249745495574166 41 ARG 0.4338 0.019490658631995 42 TYR 0.5346 0.0197095615572402 43 THR 0.5375 0.0188977398778047 45 GLN 0.4720 0.0178892956401858 49 TYR 0.4523 0.0173209002040085 50 THR 0.3673 0.0192540763946153 52 SER 0.3975 0.0301416374365984 53 SER 0.3786 0.021872502753618 60 SER 0.3710 0.0217287542752297 66 ALA 0.4507 0.0139057993316299 67 SER 0.3649 0.0154938288471063 70 TYR 0.5281 0.0215720643580371 71 THR 0.4651 0.0187547919528394 74 SER 0.3662 0.0159414142522272 81 SER 0.4517 0.0189368796349062 83 GLU 0.4701 0.0146022946797688 84 TYR 0.4491 0.0166295545675045 85 THR 0.5012 0.0185358554306638 118 LYS 0.4106 0.0143746016594037 119 TYR 0.4826 0.0177056745965121 122 THR 0.4116 0.020769654821173 123 SER 0.3762 0.019071356619299 133 TYR 0.4573 0.0176509463373314 134 THR 0.4131 0.0200268106751124 140 TYR 0.4474 0.0189559385453132 150 THR 0.4682 0.0203967465847343 157 THR 0.4113 0.0227093656626564 167 LYS 0.4414 0.016478787134749 168 GLY 0.4057 0.0333216428595822 169 SER 0.4547 0.0298890863517455 170 THR 0.3553 0.038750415439072 171 TYR 0.5080 0.0148540178396269 174 THR 0.4963 0.0201131832908935 177 GLY 0.4376 0.0291754206295931 178 TYR 0.4865 0.0142637432814394 179 SER 0.4679 0.0175781974187574 181 THR 0.4123 0.023870736316012 185 TYR 0.4170 0.0163443161911247 186 SER 0.4498 0.0262153881619057 187 LEU 0.3723 0.0196959119980009 188 THR 0.3484 0.0183750897220587 191 ALA 0.3328 0.00931966698753572 192 ILE 0.3679 0.0125815356690956 193 SER 0.3258 0.0126540738153763 195 ASP 0.3588 0.00909569421562525 196 ASP 0.4967 0.00909059509077575 197 SER 0.4629 0.00732808094732783 198 ASP 0.4925 0.00707360079189117 199 GLU 0.3807 0.00636155045466077 200 GLU 0.3588 0.0056647004265127 201 ASN -0.3674 0.00525680620661726 stop_ save_