data_27630 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1HN,15N,13CO,13CA and 13CB Chemical Shift Assignments for the FBP21(326-276) Fragment in Complex with the Brr2-CSec63 domain ; _BMRB_accession_number 27630 _BMRB_flat_file_name bmr27630.str _Entry_type original _Submission_date 2018-09-26 _Accession_date 2018-09-26 _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 Sticht Jana . . 2 Freund Christian . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 49 "13C chemical shifts" 133 "15N chemical shifts" 49 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-02-15 update BMRB 'update entry citation' 2018-10-09 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27629 'FBP21(326-276) Fragment' stop_ _Original_release_date 2018-09-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; FBP21's C-Terminal Domain Remains Dynamic When Wrapped around the c-Sec63 Unit of Brr2 Helicase ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30558886 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sticht Jana . . 2 Bertazzon Miriam . . 3 Henning Lisa M. . 4 Licha Jan R. . 5 Abualrous Esam T. . 6 Freund Christian . . stop_ _Journal_abbreviation 'Biophys. J.' _Journal_volume 116 _Journal_issue 3 _Journal_ISSN 1542-0086 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 406 _Page_last 418 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'FBP21(326-376)/Brr2-CSec63 complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label FBP21(326-376) $FBP21(326-376) Brr2-CSec63 $Brr2-CSec63 stop_ _System_molecular_weight 40237 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FBP21(326-376) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FBP21(326-376) _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 54 _Mol_residue_sequence ; GAMEADGGGEPKVVFKEKTV TSLGVMADGVAPVFKKRRTE NGKSRNLRQRGDDQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 323 GLY 2 324 ALA 3 325 MET 4 326 GLU 5 327 ALA 6 328 ASP 7 329 GLY 8 330 GLY 9 331 GLY 10 332 GLU 11 333 PRO 12 334 LYS 13 335 VAL 14 336 VAL 15 337 PHE 16 338 LYS 17 339 GLU 18 340 LYS 19 341 THR 20 342 VAL 21 343 THR 22 344 SER 23 345 LEU 24 346 GLY 25 347 VAL 26 348 MET 27 349 ALA 28 350 ASP 29 351 GLY 30 352 VAL 31 353 ALA 32 354 PRO 33 355 VAL 34 356 PHE 35 357 LYS 36 358 LYS 37 359 ARG 38 360 ARG 39 361 THR 40 362 GLU 41 363 ASN 42 364 GLY 43 365 LYS 44 366 SER 45 367 ARG 46 368 ASN 47 369 LEU 48 370 ARG 49 371 GLN 50 372 ARG 51 373 GLY 52 374 ASP 53 375 ASP 54 376 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_Brr2-CSec63 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Brr2-CSec63 _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 305 _Mol_residue_sequence ; GPLGSPEFTKVRGLIEIISN AAEYENIPIRHHEDNLLRQL AQKVPHKLNNPKFNDPHVKT NLLLQAHLSRMQLSAELQSD TEEILSKAIRLIQACVDVLS SNGWLSPALAAMELAQMVTQ AMWSKDSYLKQLPHFTSEHI KRCTDKGVESVFDIMEMEDE ERNALLQLTDSQIADVARFC NRYPNIELSYEVVDKDSIRS GGPVVVLVQLEREEEVTGPV IAPLFPQKREEGWWVVIGDA KSNSLISIKRLTLQQKAKVK LDFVAPATGAHNYTLYFMSD AYMGCDQEYKFSVDVKEAET DSDSD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -7 GLY 2 -6 PRO 3 -5 LEU 4 -4 GLY 5 -3 SER 6 -2 PRO 7 -1 GLU 8 0 PHE 9 1840 THR 10 1841 LYS 11 1842 VAL 12 1843 ARG 13 1844 GLY 14 1845 LEU 15 1846 ILE 16 1847 GLU 17 1848 ILE 18 1849 ILE 19 1850 SER 20 1851 ASN 21 1852 ALA 22 1853 ALA 23 1854 GLU 24 1855 TYR 25 1856 GLU 26 1857 ASN 27 1858 ILE 28 1859 PRO 29 1860 ILE 30 1861 ARG 31 1862 HIS 32 1863 HIS 33 1864 GLU 34 1865 ASP 35 1866 ASN 36 1867 LEU 37 1868 LEU 38 1869 ARG 39 1870 GLN 40 1871 LEU 41 1872 ALA 42 1873 GLN 43 1874 LYS 44 1875 VAL 45 1876 PRO 46 1877 HIS 47 1878 LYS 48 1879 LEU 49 1880 ASN 50 1881 ASN 51 1882 PRO 52 1883 LYS 53 1884 PHE 54 1885 ASN 55 1886 ASP 56 1887 PRO 57 1888 HIS 58 1889 VAL 59 1890 LYS 60 1891 THR 61 1892 ASN 62 1893 LEU 63 1894 LEU 64 1895 LEU 65 1896 GLN 66 1897 ALA 67 1898 HIS 68 1899 LEU 69 1900 SER 70 1901 ARG 71 1902 MET 72 1903 GLN 73 1904 LEU 74 1905 SER 75 1906 ALA 76 1907 GLU 77 1908 LEU 78 1909 GLN 79 1910 SER 80 1911 ASP 81 1912 THR 82 1913 GLU 83 1914 GLU 84 1915 ILE 85 1916 LEU 86 1917 SER 87 1918 LYS 88 1919 ALA 89 1920 ILE 90 1921 ARG 91 1922 LEU 92 1923 ILE 93 1924 GLN 94 1925 ALA 95 1926 CYS 96 1927 VAL 97 1928 ASP 98 1929 VAL 99 1930 LEU 100 1931 SER 101 1932 SER 102 1933 ASN 103 1934 GLY 104 1935 TRP 105 1936 LEU 106 1937 SER 107 1938 PRO 108 1939 ALA 109 1940 LEU 110 1941 ALA 111 1942 ALA 112 1943 MET 113 1944 GLU 114 1945 LEU 115 1946 ALA 116 1947 GLN 117 1948 MET 118 1949 VAL 119 1950 THR 120 1951 GLN 121 1952 ALA 122 1953 MET 123 1954 TRP 124 1955 SER 125 1956 LYS 126 1957 ASP 127 1958 SER 128 1959 TYR 129 1960 LEU 130 1961 LYS 131 1962 GLN 132 1963 LEU 133 1964 PRO 134 1965 HIS 135 1966 PHE 136 1967 THR 137 1968 SER 138 1969 GLU 139 1970 HIS 140 1971 ILE 141 1972 LYS 142 1973 ARG 143 1974 CYS 144 1975 THR 145 1976 ASP 146 1977 LYS 147 1978 GLY 148 1979 VAL 149 1980 GLU 150 1981 SER 151 1982 VAL 152 1983 PHE 153 1984 ASP 154 1985 ILE 155 1986 MET 156 1987 GLU 157 1988 MET 158 1989 GLU 159 1990 ASP 160 1991 GLU 161 1992 GLU 162 1993 ARG 163 1994 ASN 164 1995 ALA 165 1996 LEU 166 1997 LEU 167 1998 GLN 168 1999 LEU 169 2000 THR 170 2001 ASP 171 2002 SER 172 2003 GLN 173 2004 ILE 174 2005 ALA 175 2006 ASP 176 2007 VAL 177 2008 ALA 178 2009 ARG 179 2010 PHE 180 2011 CYS 181 2012 ASN 182 2013 ARG 183 2014 TYR 184 2015 PRO 185 2016 ASN 186 2017 ILE 187 2018 GLU 188 2019 LEU 189 2020 SER 190 2021 TYR 191 2022 GLU 192 2023 VAL 193 2024 VAL 194 2025 ASP 195 2026 LYS 196 2027 ASP 197 2028 SER 198 2029 ILE 199 2030 ARG 200 2031 SER 201 2032 GLY 202 2033 GLY 203 2034 PRO 204 2035 VAL 205 2036 VAL 206 2037 VAL 207 2038 LEU 208 2039 VAL 209 2040 GLN 210 2041 LEU 211 2042 GLU 212 2043 ARG 213 2044 GLU 214 2045 GLU 215 2046 GLU 216 2047 VAL 217 2048 THR 218 2049 GLY 219 2050 PRO 220 2051 VAL 221 2052 ILE 222 2053 ALA 223 2054 PRO 224 2055 LEU 225 2056 PHE 226 2057 PRO 227 2058 GLN 228 2059 LYS 229 2060 ARG 230 2061 GLU 231 2062 GLU 232 2063 GLY 233 2064 TRP 234 2065 TRP 235 2066 VAL 236 2067 VAL 237 2068 ILE 238 2069 GLY 239 2070 ASP 240 2071 ALA 241 2072 LYS 242 2073 SER 243 2074 ASN 244 2075 SER 245 2076 LEU 246 2077 ILE 247 2078 SER 248 2079 ILE 249 2080 LYS 250 2081 ARG 251 2082 LEU 252 2083 THR 253 2084 LEU 254 2085 GLN 255 2086 GLN 256 2087 LYS 257 2088 ALA 258 2089 LYS 259 2090 VAL 260 2091 LYS 261 2092 LEU 262 2093 ASP 263 2094 PHE 264 2095 VAL 265 2096 ALA 266 2097 PRO 267 2098 ALA 268 2099 THR 269 2100 GLY 270 2101 ALA 271 2102 HIS 272 2103 ASN 273 2104 TYR 274 2105 THR 275 2106 LEU 276 2107 TYR 277 2108 PHE 278 2109 MET 279 2110 SER 280 2111 ASP 281 2112 ALA 282 2113 TYR 283 2114 MET 284 2115 GLY 285 2116 CYS 286 2117 ASP 287 2118 GLN 288 2119 GLU 289 2120 TYR 290 2121 LYS 291 2122 PHE 292 2123 SER 293 2124 VAL 294 2125 ASP 295 2126 VAL 296 2127 LYS 297 2128 GLU 298 2129 ALA 299 2130 GLU 300 2131 THR 301 2132 ASP 302 2133 SER 303 2134 ASP 304 2135 SER 305 2136 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FBP21(326-376) Human 9606 Eukaryota Metazoa Homo sapiens $Brr2-CSec63 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 $FBP21(326-376) 'recombinant technology' . Escherichia coli . pETM11 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FBP21(326-376) 140 uM '[U-13C; U-15N; U-2H]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' $Brr2-CSec63 420 uM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ save_CcpNMR_Analysis _Saveframe_category software _Name CcpNMR_Analysis _Version 2.4.2 loop_ _Vendor _Address _Electronic_address CCPN . . 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 700 _Details 'triple resonance cryo-probe' 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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 . M pH 6.5 . pH pressure 1 . atm temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . 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 protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 external indirect . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 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 $CcpNMR_Analysis stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCO' '3D HNCACB' '3D HN(CO)CA' 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 FBP21(326-376) _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 1 324 2 ALA C C 177.959 0.000 1 2 324 2 ALA CA C 52.438 0.025 1 3 324 2 ALA CB C 18.668 0.000 1 4 325 3 MET H H 8.514 0.003 1 5 325 3 MET C C 176.446 0.000 1 6 325 3 MET CA C 55.239 0.041 1 7 325 3 MET CB C 31.866 0.045 1 8 325 3 MET N N 119.147 0.016 1 9 326 4 GLU H H 8.394 0.002 1 10 326 4 GLU C C 176.444 0.000 1 11 326 4 GLU CA C 56.258 0.023 1 12 326 4 GLU CB C 29.421 0.012 1 13 326 4 GLU N N 121.911 0.060 1 14 327 5 ALA H H 8.349 0.001 1 15 327 5 ALA C C 177.640 0.000 1 16 327 5 ALA CA C 52.228 0.032 1 17 327 5 ALA CB C 18.648 0.000 1 18 327 5 ALA N N 124.639 0.017 1 19 328 6 ASP H H 8.296 0.001 1 20 328 6 ASP C C 177.064 0.000 1 21 328 6 ASP CA C 54.102 0.031 1 22 328 6 ASP CB C 40.577 0.010 1 23 328 6 ASP N N 119.414 0.029 1 24 329 7 GLY H H 8.355 0.002 1 25 329 7 GLY C C 175.165 0.000 1 26 329 7 GLY CA C 45.241 0.014 1 27 329 7 GLY N N 109.592 0.018 1 28 330 8 GLY H H 8.361 0.002 1 29 330 8 GLY C C 174.767 0.000 1 30 330 8 GLY CA C 45.067 0.068 1 31 330 8 GLY N N 108.984 0.079 1 32 331 9 GLY H H 8.259 0.005 1 33 331 9 GLY C C 173.897 0.000 1 34 331 9 GLY CA C 44.555 0.054 1 35 331 9 GLY N N 108.692 0.033 1 36 332 10 GLU H H 8.253 0.001 1 37 332 10 GLU CA C 54.007 0.014 1 38 332 10 GLU CB C 28.818 0.000 1 39 332 10 GLU N N 121.789 0.017 1 40 333 11 PRO C C 176.840 0.000 1 41 333 11 PRO CA C 62.613 0.068 1 42 334 12 LYS H H 8.388 0.004 1 43 334 12 LYS C C 176.531 0.000 1 44 334 12 LYS CA C 55.605 0.045 1 45 334 12 LYS N N 122.020 0.012 1 46 335 13 VAL H H 8.221 0.001 1 47 335 13 VAL C C 174.979 0.000 1 48 335 13 VAL CA C 61.618 0.036 1 49 335 13 VAL CB C 31.917 0.000 1 50 335 13 VAL N N 123.048 0.026 1 51 336 14 VAL H H 8.036 0.002 1 52 336 14 VAL C C 175.494 0.000 1 53 336 14 VAL CA C 61.203 0.044 1 54 336 14 VAL CB C 32.303 0.046 1 55 336 14 VAL N N 124.630 0.043 1 56 337 15 PHE H H 8.555 0.002 1 57 337 15 PHE C C 175.555 0.000 1 58 337 15 PHE CA C 56.877 0.025 1 59 337 15 PHE CB C 38.553 0.000 1 60 337 15 PHE N N 124.251 0.035 1 61 338 16 LYS H H 8.616 0.003 1 62 338 16 LYS C C 175.125 0.000 1 63 338 16 LYS CA C 55.421 0.027 1 64 338 16 LYS N N 123.635 0.056 1 65 339 17 GLU H H 8.435 0.001 1 66 339 17 GLU CA C 55.385 0.024 1 67 339 17 GLU N N 122.167 0.054 1 68 340 18 LYS H H 9.021 0.004 1 69 340 18 LYS C C 175.680 0.000 1 70 340 18 LYS CA C 56.321 0.036 1 71 340 18 LYS N N 125.388 0.043 1 72 341 19 THR H H 8.125 0.003 1 73 341 19 THR C C 173.610 0.000 1 74 341 19 THR CA C 59.739 0.056 1 75 341 19 THR CB C 70.564 0.079 1 76 341 19 THR N N 113.594 0.077 1 77 342 20 VAL H H 8.764 0.008 1 78 342 20 VAL C C 176.106 0.000 1 79 342 20 VAL CA C 62.143 0.030 1 80 342 20 VAL N N 123.220 0.069 1 81 343 21 THR H H 8.510 0.004 1 82 343 21 THR CA C 60.696 0.079 1 83 343 21 THR N N 118.218 0.059 1 84 344 22 SER H H 7.774 0.013 1 85 344 22 SER C C 174.519 0.000 1 86 344 22 SER CA C 57.270 0.030 1 87 344 22 SER N N 114.078 0.027 1 88 345 23 LEU H H 8.783 0.001 1 89 345 23 LEU C C 177.613 0.000 1 90 345 23 LEU CA C 54.658 0.109 1 91 345 23 LEU CB C 41.578 0.000 1 92 345 23 LEU N N 122.689 0.032 1 93 346 24 GLY H H 8.307 0.001 1 94 346 24 GLY C C 174.974 0.000 1 95 346 24 GLY CA C 45.106 0.023 1 96 346 24 GLY N N 107.515 0.036 1 97 347 25 VAL H H 8.204 0.006 1 98 347 25 VAL C C 176.367 0.000 1 99 347 25 VAL CA C 62.154 0.040 1 100 347 25 VAL CB C 31.442 0.000 1 101 347 25 VAL N N 119.194 0.028 1 102 348 26 MET H H 8.768 0.003 1 103 348 26 MET C C 175.987 0.000 1 104 348 26 MET CA C 55.980 0.048 1 105 348 26 MET N N 123.292 0.009 1 106 349 27 ALA H H 8.061 0.005 1 107 349 27 ALA C C 176.978 0.000 1 108 349 27 ALA CA C 51.523 0.081 1 109 349 27 ALA CB C 18.912 0.022 1 110 349 27 ALA N N 122.601 0.040 1 111 350 28 ASP H H 7.869 0.007 1 112 350 28 ASP C C 177.250 0.000 1 113 350 28 ASP CA C 55.068 0.059 1 114 350 28 ASP CB C 40.146 0.044 1 115 350 28 ASP N N 119.296 0.051 1 116 351 29 GLY H H 8.424 0.005 1 117 351 29 GLY C C 174.073 0.000 1 118 351 29 GLY CA C 45.057 0.008 1 119 351 29 GLY N N 109.020 0.025 1 120 352 30 VAL H H 7.684 0.002 1 121 352 30 VAL C C 175.556 0.000 1 122 352 30 VAL CA C 61.188 0.022 1 123 352 30 VAL CB C 31.812 0.050 1 124 352 30 VAL N N 120.387 0.011 1 125 353 31 ALA H H 8.638 0.003 1 126 353 31 ALA CA C 50.196 0.002 1 127 353 31 ALA CB C 17.696 0.000 1 128 353 31 ALA N N 130.367 0.038 1 129 354 32 PRO C C 176.012 0.000 1 130 354 32 PRO CA C 59.281 0.004 1 131 355 33 VAL H H 8.681 0.003 1 132 355 33 VAL C C 176.358 0.000 1 133 355 33 VAL CA C 59.068 0.040 1 134 355 33 VAL N N 123.765 0.065 1 135 356 34 PHE H H 8.695 0.002 1 136 356 34 PHE C C 176.275 0.000 1 137 356 34 PHE CA C 55.876 0.030 1 138 356 34 PHE CB C 38.502 0.000 1 139 356 34 PHE N N 124.685 0.057 1 140 357 35 LYS H H 8.460 0.002 1 141 357 35 LYS CA C 55.717 0.017 1 142 357 35 LYS CB C 32.005 0.000 1 143 357 35 LYS N N 123.455 0.035 1 144 358 36 LYS C C 176.701 0.000 1 145 358 36 LYS CA C 55.560 0.006 1 146 358 36 LYS CB C 31.838 0.000 1 147 359 37 ARG H H 8.737 0.001 1 148 359 37 ARG CA C 55.261 0.042 1 149 359 37 ARG CB C 30.221 0.000 1 150 359 37 ARG N N 124.365 0.103 1 151 360 38 ARG H H 8.771 0.004 1 152 360 38 ARG C C 176.731 0.000 1 153 360 38 ARG CA C 55.964 0.017 1 154 360 38 ARG CB C 29.946 0.047 1 155 360 38 ARG N N 123.314 0.022 1 156 361 39 THR H H 8.273 0.002 1 157 361 39 THR C C 174.867 0.000 1 158 361 39 THR CA C 61.511 0.045 1 159 361 39 THR CB C 69.035 0.000 1 160 361 39 THR N N 115.902 0.016 1 161 362 40 GLU H H 8.650 0.002 1 162 362 40 GLU C C 176.531 0.000 1 163 362 40 GLU CA C 56.461 0.042 1 164 362 40 GLU CB C 29.347 0.009 1 165 362 40 GLU N N 122.879 0.046 1 166 363 41 ASN H H 8.466 0.003 1 167 363 41 ASN C C 176.082 0.000 1 168 363 41 ASN CA C 53.413 0.009 1 169 363 41 ASN CB C 38.164 0.035 1 170 363 41 ASN N N 119.308 0.024 1 171 364 42 GLY H H 8.501 0.001 1 172 364 42 GLY C C 174.471 0.000 1 173 364 42 GLY CA C 45.349 0.020 1 174 364 42 GLY N N 109.537 0.042 1 175 365 43 LYS H H 7.998 0.002 1 176 365 43 LYS C C 176.814 0.000 1 177 365 43 LYS CA C 55.901 0.053 1 178 365 43 LYS CB C 32.078 0.008 1 179 365 43 LYS N N 120.595 0.015 1 180 366 44 SER H H 8.429 0.004 1 181 366 44 SER C C 174.459 0.000 1 182 366 44 SER CA C 57.905 0.021 1 183 366 44 SER CB C 63.030 0.021 1 184 366 44 SER N N 117.006 0.025 1 185 367 45 ARG H H 8.312 0.004 1 186 367 45 ARG C C 175.344 0.000 1 187 367 45 ARG CA C 55.948 0.039 1 188 367 45 ARG CB C 30.380 0.000 1 189 367 45 ARG N N 123.338 0.112 1 190 368 46 ASN H H 8.330 0.001 1 191 368 46 ASN C C 173.787 0.000 1 192 368 46 ASN CA C 52.924 0.047 1 193 368 46 ASN CB C 38.734 0.000 1 194 368 46 ASN N N 121.893 0.060 1 195 369 47 LEU H H 8.098 0.003 1 196 369 47 LEU C C 178.419 0.000 1 197 369 47 LEU CA C 53.863 0.029 1 198 369 47 LEU CB C 41.034 0.065 1 199 369 47 LEU N N 121.212 0.041 1 200 370 48 ARG H H 8.242 0.002 1 201 370 48 ARG C C 176.215 0.000 1 202 370 48 ARG CA C 56.580 0.033 1 203 370 48 ARG N N 122.576 0.042 1 204 371 49 GLN H H 8.749 0.004 1 205 371 49 GLN C C 176.180 0.000 1 206 371 49 GLN CA C 54.781 0.062 1 207 371 49 GLN CB C 29.294 0.000 1 208 371 49 GLN N N 125.326 0.077 1 209 372 50 ARG H H 8.647 0.004 1 210 372 50 ARG C C 177.345 0.000 1 211 372 50 ARG CA C 56.561 0.030 1 212 372 50 ARG CB C 30.275 0.002 1 213 372 50 ARG N N 123.195 0.045 1 214 373 51 GLY H H 8.603 0.002 1 215 373 51 GLY C C 173.831 0.000 1 216 373 51 GLY CA C 44.646 0.007 1 217 373 51 GLY N N 110.683 0.016 1 218 374 52 ASP H H 8.353 0.001 1 219 374 52 ASP C C 176.166 0.000 1 220 374 52 ASP CA C 53.999 0.014 1 221 374 52 ASP CB C 40.803 0.000 1 222 374 52 ASP N N 120.190 0.011 1 223 375 53 ASP H H 8.439 0.001 1 224 375 53 ASP C C 175.291 0.000 1 225 375 53 ASP CA C 54.064 0.019 1 226 375 53 ASP CB C 40.478 0.051 1 227 375 53 ASP N N 120.605 0.022 1 228 376 54 GLN H H 7.875 0.001 1 229 376 54 GLN CA C 57.006 0.014 1 230 376 54 GLN CB C 29.761 0.000 1 231 376 54 GLN N N 124.590 0.014 1 stop_ save_