data_25393 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for IST1 residues 303-366 ; _BMRB_accession_number 25393 _BMRB_flat_file_name bmr25393.str _Entry_type original _Submission_date 2014-12-15 _Accession_date 2014-12-15 _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 Wenzel Dawn M. . 2 Skalicky Jack J. . 3 Sundquist Wesley I. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 56 "13C chemical shifts" 184 "15N chemical shifts" 56 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-02-18 update BMRB 'update entry citation' 2015-05-26 original author 'original release' stop_ _Original_release_date 2015-05-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; ULK3 regulates cytokinetic abscission by phosphorylating ESCRT-III proteins ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26011858 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Caballe Anna . . 2 Wenzel Dawn M. . 3 Agromayor Monica . . 4 Alam Steven L. . 5 Skalicky Jack J. . 6 Kloc Magdalena . . 7 Carlton Jeremy G. . 8 Labrador Leticia . . 9 Sundquist Wesley I. . 10 Martin-Serrano Juan . . stop_ _Journal_abbreviation Elife _Journal_volume 4 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first e06547 _Page_last e06547 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'IST1 peptide' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'IST1 peptide' $IST1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_IST1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common IST1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 67 _Mol_residue_sequence ; GHMGPKPEASAKLPSRPADN YDNFVLPELPSVPDTLPTAS AGASTSASEDIDFDDLSRRF EELKKKT ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLY 2 2 HIS 3 3 MET 4 303 GLY 5 304 PRO 6 305 LYS 7 306 PRO 8 307 GLU 9 308 ALA 10 309 SER 11 310 ALA 12 311 LYS 13 312 LEU 14 313 PRO 15 314 SER 16 315 ARG 17 316 PRO 18 317 ALA 19 318 ASP 20 319 ASN 21 320 TYR 22 321 ASP 23 322 ASN 24 323 PHE 25 324 VAL 26 325 LEU 27 326 PRO 28 327 GLU 29 328 LEU 30 329 PRO 31 330 SER 32 331 VAL 33 332 PRO 34 333 ASP 35 334 THR 36 335 LEU 37 336 PRO 38 337 THR 39 338 ALA 40 339 SER 41 340 ALA 42 341 GLY 43 342 ALA 44 343 SER 45 344 THR 46 345 SER 47 346 ALA 48 347 SER 49 348 GLU 50 349 ASP 51 350 ILE 52 351 ASP 53 352 PHE 54 353 ASP 55 354 ASP 56 355 LEU 57 356 SER 58 357 ARG 59 358 ARG 60 359 PHE 61 360 GLU 62 361 GLU 63 362 LEU 64 363 LYS 65 364 LYS 66 365 LYS 67 366 THR 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 $IST1 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 $IST1 'recombinant technology' . Escherichia coli . pGEX stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '20 mM sodium phosphate, pH 6.2, 25 mM NaCl, 0.1 mM EDTA, 0.5 mM DTT, 0.1 mM sodium azide' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $IST1 0.4 mM '[U-13C; U-15N]' 'sodium phosphate' 20 mM 'natural abundance' NaCl 25 mM 'natural abundance' EDTA 0.1 mM 'natural abundance' DTT 0.5 mM 'natural abundance' 'sodium azide' 0.1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . 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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _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' 0.025 . M pH 6.2 . pH pressure 1 . atm temperature 273 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '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 'IST1 peptide' _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 3 3 MET C C 175.936 0.000 1 2 3 3 MET CA C 55.006 0.000 1 3 3 3 MET CB C 32.755 0.000 1 4 303 4 GLY H H 8.093 0.001 1 5 303 4 GLY CA C 44.360 0.000 1 6 303 4 GLY N N 110.448 0.006 1 7 304 5 PRO C C 176.809 0.000 1 8 304 5 PRO CA C 62.760 0.000 1 9 304 5 PRO CB C 32.018 0.000 1 10 305 6 LYS H H 8.315 0.001 1 11 305 6 LYS CA C 54.141 0.000 1 12 305 6 LYS CB C 32.325 0.000 1 13 305 6 LYS N N 122.852 0.002 1 14 306 7 PRO C C 176.948 0.002 1 15 306 7 PRO CA C 63.124 0.013 1 16 306 7 PRO CB C 31.822 0.011 1 17 307 8 GLU H H 8.472 0.002 1 18 307 8 GLU C C 176.403 0.000 1 19 307 8 GLU CA C 56.500 0.049 1 20 307 8 GLU CB C 30.169 0.093 1 21 307 8 GLU N N 121.270 0.016 1 22 308 9 ALA H H 8.247 0.003 1 23 308 9 ALA C C 177.749 0.001 1 24 308 9 ALA CA C 52.611 0.036 1 25 308 9 ALA CB C 19.056 0.038 1 26 308 9 ALA N N 125.209 0.027 1 27 309 10 SER H H 8.081 0.002 1 28 309 10 SER C C 174.188 0.002 1 29 309 10 SER CA C 58.197 0.033 1 30 309 10 SER CB C 63.590 0.032 1 31 309 10 SER N N 114.597 0.029 1 32 310 11 ALA H H 8.079 0.003 1 33 310 11 ALA C C 177.292 0.005 1 34 310 11 ALA CA C 52.444 0.061 1 35 310 11 ALA CB C 19.193 0.054 1 36 310 11 ALA N N 125.748 0.027 1 37 311 12 LYS H H 8.058 0.004 1 38 311 12 LYS C C 176.165 0.014 1 39 311 12 LYS CA C 55.809 0.026 1 40 311 12 LYS CB C 32.884 0.061 1 41 311 12 LYS N N 120.380 0.017 1 42 312 13 LEU H H 8.118 0.002 1 43 312 13 LEU C C 175.147 0.000 1 44 312 13 LEU CA C 52.878 0.000 1 45 312 13 LEU CB C 41.591 0.000 1 46 312 13 LEU N N 125.028 0.014 1 47 313 14 PRO C C 176.735 0.000 1 48 313 14 PRO CA C 62.889 0.000 1 49 313 14 PRO CB C 31.927 0.000 1 50 314 15 SER H H 8.226 0.000 1 51 314 15 SER C C 173.958 0.000 1 52 314 15 SER CA C 58.147 0.041 1 53 314 15 SER CB C 63.820 0.063 1 54 314 15 SER N N 116.065 0.000 1 55 315 16 ARG H H 8.178 0.002 1 56 315 16 ARG CA C 53.693 0.000 1 57 315 16 ARG CB C 30.342 0.000 1 58 315 16 ARG N N 123.424 0.007 1 59 316 17 PRO C C 176.577 0.007 1 60 316 17 PRO CA C 63.112 0.030 1 61 316 17 PRO CB C 31.947 0.026 1 62 317 18 ALA H H 8.243 0.002 1 63 317 18 ALA C C 177.412 0.003 1 64 317 18 ALA CA C 52.455 0.057 1 65 317 18 ALA CB C 19.088 0.061 1 66 317 18 ALA N N 123.405 0.011 1 67 318 19 ASP H H 8.035 0.002 1 68 318 19 ASP C C 175.609 0.016 1 69 318 19 ASP CA C 54.206 0.043 1 70 318 19 ASP CB C 41.065 0.062 1 71 318 19 ASP N N 118.688 0.011 1 72 319 20 ASN H H 8.023 0.003 1 73 319 20 ASN C C 174.733 0.020 1 74 319 20 ASN CA C 53.000 0.114 1 75 319 20 ASN CB C 38.929 0.000 1 76 319 20 ASN N N 117.815 0.010 1 77 320 21 TYR H H 8.034 0.002 1 78 320 21 TYR CA C 57.982 0.000 1 79 320 21 TYR CB C 38.690 0.000 1 80 320 21 TYR N N 120.496 0.032 1 81 321 22 ASP H H 8.090 0.002 1 82 321 22 ASP C C 175.638 0.010 1 83 321 22 ASP CA C 54.374 0.074 1 84 321 22 ASP CB C 41.010 0.045 1 85 321 22 ASP N N 121.049 0.023 1 86 322 23 ASN H H 8.019 0.002 1 87 322 23 ASN C C 174.490 0.000 1 88 322 23 ASN CA C 53.108 0.029 1 89 322 23 ASN CB C 38.670 0.075 1 90 322 23 ASN N N 118.024 0.033 1 91 323 24 PHE H H 7.949 0.002 1 92 323 24 PHE C C 175.061 0.013 1 93 323 24 PHE CA C 57.745 0.022 1 94 323 24 PHE CB C 39.306 0.057 1 95 323 24 PHE N N 120.375 0.008 1 96 324 25 VAL H H 7.752 0.002 1 97 324 25 VAL C C 175.068 0.022 1 98 324 25 VAL CA C 61.673 0.010 1 99 324 25 VAL CB C 32.936 0.047 1 100 324 25 VAL N N 122.936 0.008 1 101 325 26 LEU H H 8.134 0.002 1 102 325 26 LEU CA C 52.821 0.000 1 103 325 26 LEU CB C 41.730 0.000 1 104 325 26 LEU N N 127.778 0.015 1 105 326 27 PRO CA C 62.736 0.009 1 106 326 27 PRO CB C 31.943 0.030 1 107 327 28 GLU H H 8.198 0.000 1 108 327 28 GLU C C 176.048 0.000 1 109 327 28 GLU CA C 56.073 0.021 1 110 327 28 GLU CB C 30.349 0.045 1 111 327 28 GLU N N 120.763 0.000 1 112 328 29 LEU H H 8.194 0.002 1 113 328 29 LEU CA C 52.718 0.000 1 114 328 29 LEU CB C 41.762 0.000 1 115 328 29 LEU N N 124.998 0.004 1 116 329 30 PRO C C 176.693 0.000 1 117 329 30 PRO CA C 62.633 0.158 1 118 329 30 PRO CB C 32.006 0.050 1 119 330 31 SER H H 8.248 0.002 1 120 330 31 SER C C 174.121 0.000 1 121 330 31 SER CA C 57.990 0.024 1 122 330 31 SER CB C 63.743 0.100 1 123 330 31 SER N N 116.406 0.009 1 124 331 32 VAL H H 8.069 0.001 1 125 331 32 VAL CA C 59.678 0.000 1 126 331 32 VAL CB C 32.659 0.000 1 127 331 32 VAL N N 122.935 0.013 1 128 332 33 PRO C C 176.479 0.000 1 129 332 33 PRO CA C 63.038 0.002 1 130 332 33 PRO CB C 32.036 0.000 1 131 333 34 ASP H H 8.274 0.002 1 132 333 34 ASP C C 176.267 0.024 1 133 333 34 ASP CA C 54.447 0.032 1 134 333 34 ASP CB C 40.965 0.035 1 135 333 34 ASP N N 120.382 0.009 1 136 334 35 THR H H 7.885 0.002 1 137 334 35 THR C C 174.136 0.004 1 138 334 35 THR CA C 61.474 0.009 1 139 334 35 THR CB C 69.823 0.012 1 140 334 35 THR N N 113.896 0.005 1 141 335 36 LEU H H 8.161 0.004 1 142 335 36 LEU C C 175.302 0.000 1 143 335 36 LEU CA C 52.996 0.000 1 144 335 36 LEU CB C 41.636 0.000 1 145 335 36 LEU N N 126.159 0.025 1 146 336 37 PRO C C 177.031 0.007 1 147 336 37 PRO CA C 63.042 0.000 1 148 336 37 PRO CB C 31.928 0.073 1 149 337 38 THR H H 7.993 0.002 1 150 337 38 THR C C 174.419 0.000 1 151 337 38 THR CA C 61.691 0.051 1 152 337 38 THR CB C 69.670 0.007 1 153 337 38 THR N N 114.046 0.016 1 154 338 39 ALA H H 8.191 0.004 1 155 338 39 ALA C C 177.668 0.004 1 156 338 39 ALA CA C 52.535 0.033 1 157 338 39 ALA CB C 19.132 0.000 1 158 338 39 ALA N N 126.362 0.028 1 159 339 40 SER H H 8.142 0.002 1 160 339 40 SER C C 174.350 0.000 1 161 339 40 SER CA C 58.081 0.000 1 162 339 40 SER CB C 63.700 0.023 1 163 339 40 SER N N 115.146 0.005 1 164 340 41 ALA H H 8.215 0.004 1 165 340 41 ALA C C 178.094 0.004 1 166 340 41 ALA CA C 52.628 0.030 1 167 340 41 ALA CB C 19.108 0.073 1 168 340 41 ALA N N 126.134 0.045 1 169 341 42 GLY H H 8.195 0.004 1 170 341 42 GLY C C 173.750 0.002 1 171 341 42 GLY CA C 45.054 0.039 1 172 341 42 GLY N N 108.020 0.011 1 173 342 43 ALA H H 7.999 0.003 1 174 342 43 ALA C C 177.820 0.002 1 175 342 43 ALA CA C 52.354 0.018 1 176 342 43 ALA CB C 19.314 0.069 1 177 342 43 ALA N N 123.588 0.015 1 178 343 44 SER H H 8.260 0.002 1 179 343 44 SER C C 174.855 0.002 1 180 343 44 SER CA C 58.158 0.025 1 181 343 44 SER CB C 63.628 0.040 1 182 343 44 SER N N 115.176 0.016 1 183 344 45 THR H H 8.093 0.003 1 184 344 45 THR C C 174.514 0.002 1 185 344 45 THR CA C 61.569 0.023 1 186 344 45 THR CB C 69.620 0.011 1 187 344 45 THR N N 115.516 0.006 1 188 345 46 SER H H 8.197 0.003 1 189 345 46 SER C C 174.074 0.009 1 190 345 46 SER CA C 58.158 0.023 1 191 345 46 SER CB C 63.775 0.039 1 192 345 46 SER N N 117.995 0.016 1 193 346 47 ALA H H 8.259 0.002 1 194 346 47 ALA C C 177.644 0.000 1 195 346 47 ALA CA C 52.448 0.000 1 196 346 47 ALA CB C 19.184 0.000 1 197 346 47 ALA N N 126.187 0.024 1 198 347 48 SER H H 8.136 0.000 1 199 347 48 SER C C 174.477 0.000 1 200 347 48 SER CA C 58.434 0.032 1 201 347 48 SER CB C 63.645 0.003 1 202 347 48 SER N N 114.954 0.016 1 203 348 49 GLU H H 8.279 0.002 1 204 348 49 GLU C C 175.940 0.022 1 205 348 49 GLU CA C 56.458 0.007 1 206 348 49 GLU CB C 30.219 0.035 1 207 348 49 GLU N N 122.232 0.011 1 208 349 50 ASP H H 8.181 0.004 1 209 349 50 ASP C C 175.903 0.046 1 210 349 50 ASP CA C 54.320 0.104 1 211 349 50 ASP CB C 40.931 0.000 1 212 349 50 ASP N N 121.249 0.023 1 213 350 51 ILE H H 7.813 0.002 1 214 350 51 ILE C C 175.414 0.003 1 215 350 51 ILE CA C 60.976 0.011 1 216 350 51 ILE CB C 39.048 0.017 1 217 350 51 ILE N N 120.562 0.014 1 218 351 52 ASP H H 8.192 0.002 1 219 351 52 ASP C C 176.048 0.016 1 220 351 52 ASP CA C 53.739 0.037 1 221 351 52 ASP CB C 41.056 0.059 1 222 351 52 ASP N N 123.904 0.011 1 223 352 53 PHE H H 8.066 0.002 1 224 352 53 PHE C C 175.980 0.000 1 225 352 53 PHE CA C 58.953 0.036 1 226 352 53 PHE CB C 39.378 0.034 1 227 352 53 PHE N N 121.824 0.005 1 228 353 54 ASP H H 8.193 0.005 1 229 353 54 ASP C C 176.244 0.004 1 230 353 54 ASP CA C 54.456 0.004 1 231 353 54 ASP CB C 40.937 0.030 1 232 353 54 ASP N N 121.247 0.020 1 233 354 55 ASP H H 7.898 0.002 1 234 354 55 ASP C C 177.285 0.002 1 235 354 55 ASP CA C 55.094 0.016 1 236 354 55 ASP CB C 41.166 0.019 1 237 354 55 ASP N N 120.815 0.009 1 238 355 56 LEU H H 8.116 0.002 1 239 355 56 LEU C C 178.681 0.005 1 240 355 56 LEU CA C 56.945 0.035 1 241 355 56 LEU CB C 41.472 0.046 1 242 355 56 LEU N N 121.896 0.018 1 243 356 57 SER H H 8.113 0.002 1 244 356 57 SER C C 175.675 0.005 1 245 356 57 SER CA C 60.356 0.022 1 246 356 57 SER CB C 62.965 0.008 1 247 356 57 SER N N 114.631 0.014 1 248 357 58 ARG H H 7.735 0.003 1 249 357 58 ARG C C 177.159 0.002 1 250 357 58 ARG CA C 57.245 0.003 1 251 357 58 ARG CB C 30.136 0.107 1 252 357 58 ARG N N 121.416 0.008 1 253 358 59 ARG H H 7.810 0.002 1 254 358 59 ARG C C 177.021 0.015 1 255 358 59 ARG CA C 57.264 0.065 1 256 358 59 ARG CB C 30.256 0.045 1 257 358 59 ARG N N 119.823 0.009 1 258 359 60 PHE H H 7.991 0.002 1 259 359 60 PHE C C 176.638 0.003 1 260 359 60 PHE CA C 58.786 0.031 1 261 359 60 PHE CB C 38.917 0.041 1 262 359 60 PHE N N 119.678 0.017 1 263 360 61 GLU H H 8.042 0.002 1 264 360 61 GLU C C 177.289 0.003 1 265 360 61 GLU CA C 57.441 0.036 1 266 360 61 GLU CB C 29.916 0.044 1 267 360 61 GLU N N 120.694 0.044 1 268 361 62 GLU H H 8.108 0.002 1 269 361 62 GLU C C 177.251 0.000 1 270 361 62 GLU CA C 57.196 0.000 1 271 361 62 GLU CB C 29.837 0.051 1 272 361 62 GLU N N 120.378 0.007 1 273 362 63 LEU H H 7.863 0.002 1 274 362 63 LEU C C 177.735 0.003 1 275 362 63 LEU CA C 55.676 0.017 1 276 362 63 LEU CB C 42.015 0.000 1 277 362 63 LEU N N 121.300 0.010 1 278 363 64 LYS H H 7.797 0.002 1 279 363 64 LYS C C 176.538 0.001 1 280 363 64 LYS CA C 56.424 0.094 1 281 363 64 LYS CB C 32.617 0.036 1 282 363 64 LYS N N 120.549 0.014 1 283 364 65 LYS H H 7.880 0.003 1 284 364 65 LYS C C 176.289 0.000 1 285 364 65 LYS CA C 56.249 0.000 1 286 364 65 LYS CB C 33.211 0.000 1 287 364 65 LYS N N 121.465 0.018 1 288 365 66 LYS H H 8.136 0.000 1 289 365 66 LYS C C 175.837 0.000 1 290 365 66 LYS CA C 56.293 0.035 1 291 365 66 LYS CB C 32.937 0.049 1 292 365 66 LYS N N 123.142 0.005 1 293 366 67 THR H H 7.646 0.001 1 294 366 67 THR CA C 63.062 0.000 1 295 366 67 THR CB C 70.534 0.000 1 296 366 67 THR N N 120.734 0.008 1 stop_ save_