data_11545 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N chemical shift assignment for aqMutL-CTD ; _BMRB_accession_number 11545 _BMRB_flat_file_name bmr11545.str _Entry_type original _Submission_date 2013-11-26 _Accession_date 2013-11-26 _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 Mizushima Ryota . . 2 Lee Young-Ho . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 98 "13C chemical shifts" 283 "15N chemical shifts" 98 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-03-13 original BMRB . stop_ _Original_release_date 2013-11-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR characterization of the interaction of the endonuclease domain of MutL with divalent metal ions and ATP ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24901533 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mizushima Ryota . . 2 Kim 'Ju Yaen' Y. . 3 Suetake Isao . . 4 Tanaka Hiroaki . . 5 Takai Tomoyo . . 6 Kamiya Narutoshi . . 7 Takano Yu . . 8 Mishima Yuichi . . 9 Tajima Shoji . . 10 Goto Yuji . . 11 Fukui Kenji . . 12 Lee Young-Ho H. . stop_ _Journal_abbreviation 'PLoS ONE' _Journal_name_full 'PloS one' _Journal_volume 9 _Journal_issue 6 _Journal_ISSN 1932-6203 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first e98554 _Page_last e98554 _Year 2014 _Details . loop_ _Keyword ATP MMR MutL NMR endonuclease stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'aqMutL-CTD homodimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'C-terminal domain, chain 1' $aqMutL-CTD_homodimer 'C-terminal domain, chain 2' $aqMutL-CTD_homodimer stop_ _System_molecular_weight 26600 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function endonuclease stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_aqMutL-CTD_homodimer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common aqMutL-CTD_homodimer _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function endonuclease stop_ _Details 'C-terminal domain of MutL is stably dimerized in solution.' ############################## # Polymer residue sequence # ############################## _Residue_count 110 _Mol_residue_sequence ; PLSQPVKTYKPTYEILGQMD ETFILVKDSEYLYFVDQHLL EERINYEKLKDENLACRISV KAGQKLSEEKIRELIKTWRN LENPHVCPHGRPIYYKIPLR EIYEKVGRNY ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 316 PRO 2 317 LEU 3 318 SER 4 319 GLN 5 320 PRO 6 321 VAL 7 322 LYS 8 323 THR 9 324 TYR 10 325 LYS 11 326 PRO 12 327 THR 13 328 TYR 14 329 GLU 15 330 ILE 16 331 LEU 17 332 GLY 18 333 GLN 19 334 MET 20 335 ASP 21 336 GLU 22 337 THR 23 338 PHE 24 339 ILE 25 340 LEU 26 341 VAL 27 342 LYS 28 343 ASP 29 344 SER 30 345 GLU 31 346 TYR 32 347 LEU 33 348 TYR 34 349 PHE 35 350 VAL 36 351 ASP 37 352 GLN 38 353 HIS 39 354 LEU 40 355 LEU 41 356 GLU 42 357 GLU 43 358 ARG 44 359 ILE 45 360 ASN 46 361 TYR 47 362 GLU 48 363 LYS 49 364 LEU 50 365 LYS 51 366 ASP 52 367 GLU 53 368 ASN 54 369 LEU 55 370 ALA 56 371 CYS 57 372 ARG 58 373 ILE 59 374 SER 60 375 VAL 61 376 LYS 62 377 ALA 63 378 GLY 64 379 GLN 65 380 LYS 66 381 LEU 67 382 SER 68 383 GLU 69 384 GLU 70 385 LYS 71 386 ILE 72 387 ARG 73 388 GLU 74 389 LEU 75 390 ILE 76 391 LYS 77 392 THR 78 393 TRP 79 394 ARG 80 395 ASN 81 396 LEU 82 397 GLU 83 398 ASN 84 399 PRO 85 400 HIS 86 401 VAL 87 402 CYS 88 403 PRO 89 404 HIS 90 405 GLY 91 406 ARG 92 407 PRO 93 408 ILE 94 409 TYR 95 410 TYR 96 411 LYS 97 412 ILE 98 413 PRO 99 414 LEU 100 415 ARG 101 416 GLU 102 417 ILE 103 418 TYR 104 419 GLU 105 420 LYS 106 421 VAL 107 422 GLY 108 423 ARG 109 424 ASN 110 425 TYR 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 $aqMutL-CTD_homodimer 'Aquifex aeolicus' 63363 Bacteria . Aquifex aeolicus 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 $aqMutL-CTD_homodimer 'recombinant technology' 'E. coli' Escherichia coli . pET-11a 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 $aqMutL-CTD_homodimer 500 uM '[U-98% 13C; U-99% 15N]' 'potassium phosphate' 50 mM 'natural abundance' 'potassium chloride' 100 mM 'natural abundance' DTT 1 mM 'natural abundance' EDTA 1 mM 'natural abundance' NaN3 0.02 % 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe;_SPARKY _Saveframe_category software _Name NMRPipe;_SPARKY _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _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_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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' 150 . mM pH 6.8 . pH pressure 1 . atm temperature 313 . 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 water C 13 protons ppm 4.849 internal indirect . . . 0.25144953 water H 1 protons ppm 4.849 internal direct . . . 1 water N 15 protons ppm 4.849 internal 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 HNCO' '3D HN(CA)CO' '3D CBCA(CO)NH' '3D HNCACB' 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 'C-terminal domain, chain 1' _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 1 318 3 SER H H 8.31 . . 2 318 3 SER C C 174 . . 3 318 3 SER CB C 63.88 . . 4 318 3 SER N N 117 . . 5 319 4 GLN H H 8.21 . . 6 319 4 GLN C C 173.84 . . 7 319 4 GLN CA C 53.73 . . 8 319 4 GLN CB C 29.34 . . 9 319 4 GLN N N 122.61 . . 10 320 5 PRO C C 176.77 . . 11 320 5 PRO CA C 63.15 . . 12 320 5 PRO CB C 32.13 . . 13 321 6 VAL H H 8.11 . . 14 321 6 VAL C C 176.2 . . 15 321 6 VAL CA C 62.5 . . 16 321 6 VAL CB C 32.7 . . 17 321 6 VAL N N 120.27 . . 18 322 7 LYS H H 8.3 . . 19 322 7 LYS C C 176.3 . . 20 322 7 LYS CA C 56.3 . . 21 322 7 LYS CB C 33.12 . . 22 322 7 LYS N N 125 . . 23 323 8 THR H H 7.98 . . 24 323 8 THR C C 173.8 . . 25 323 8 THR CA C 61.59 . . 26 323 8 THR CB C 69.91 . . 27 323 8 THR N N 115.37 . . 28 324 9 TYR H H 8.16 . . 29 324 9 TYR C C 174.92 . . 30 324 9 TYR CA C 57.85 . . 31 324 9 TYR CB C 39.05 . . 32 324 9 TYR N N 123.11 . . 33 325 10 LYS H H 8.02 . . 34 325 10 LYS C C 173.78 . . 35 325 10 LYS CA C 53.74 . . 36 325 10 LYS CB C 33.03 . . 37 325 10 LYS N N 125.25 . . 38 326 11 PRO C C 176.77 . . 39 326 11 PRO CA C 62.83 . . 40 326 11 PRO CB C 32.27 . . 41 327 12 THR H H 8.17 . . 42 327 12 THR C C 173.72 . . 43 327 12 THR CA C 62.66 . . 44 327 12 THR CB C 69.72 . . 45 327 12 THR N N 114.85 . . 46 328 13 TYR H H 7.56 . . 47 328 13 TYR C C 174.46 . . 48 328 13 TYR CA C 56.63 . . 49 328 13 TYR CB C 40.14 . . 50 328 13 TYR N N 117.67 . . 51 329 14 GLU H H 9.22 . . 52 329 14 GLU C C 175.33 . . 53 329 14 GLU CA C 55.19 . . 54 329 14 GLU CB C 33.19 . . 55 329 14 GLU N N 120.81 . . 56 330 15 ILE H H 9.01 . . 57 330 15 ILE C C 176.31 . . 58 330 15 ILE CA C 61.98 . . 59 330 15 ILE CB C 38.74 . . 60 330 15 ILE N N 125.63 . . 61 331 16 LEU H H 8.91 . . 62 331 16 LEU CA C 55.68 . . 63 331 16 LEU CB C 43.03 . . 64 331 16 LEU N N 127.61 . . 65 332 17 GLY H H 7.18 . . 66 332 17 GLY C C 171.11 . . 67 332 17 GLY CA C 44.73 . . 68 332 17 GLY N N 102.6 . . 69 333 18 GLN H H 8.74 . . 70 333 18 GLN C C 174.22 . . 71 333 18 GLN CA C 54.47 . . 72 333 18 GLN CB C 32.58 . . 73 333 18 GLN N N 119.18 . . 74 334 19 MET H H 9.12 . . 75 334 19 MET C C 175.3 . . 76 334 19 MET CA C 55.24 . . 77 334 19 MET N N 121.15 . . 78 336 21 GLU H H 9.29 . . 79 336 21 GLU C C 175.22 . . 80 336 21 GLU CA C 58.71 . . 81 336 21 GLU CB C 28.05 . . 82 336 21 GLU N N 116.09 . . 83 337 22 THR H H 8.12 . . 84 337 22 THR CB C 72.74 . . 85 337 22 THR N N 112.2 . . 86 338 23 PHE H H 8.15 . . 87 338 23 PHE C C 175.9 . . 88 338 23 PHE CA C 57 . . 89 338 23 PHE CB C 42.97 . . 90 338 23 PHE N N 116.84 . . 91 339 24 ILE H H 9.65 . . 92 339 24 ILE C C 174.71 . . 93 339 24 ILE CA C 61.05 . . 94 339 24 ILE CB C 40.49 . . 95 339 24 ILE N N 122.84 . . 96 340 25 LEU H H 8.79 . . 97 340 25 LEU C C 175.64 . . 98 340 25 LEU CA C 54.69 . . 99 340 25 LEU CB C 43.43 . . 100 340 25 LEU N N 128.87 . . 101 341 26 VAL H H 8.77 . . 102 341 26 VAL C C 172.76 . . 103 341 26 VAL CA C 59.48 . . 104 341 26 VAL CB C 35.8 . . 105 341 26 VAL N N 123.09 . . 106 342 27 LYS H H 9.42 . . 107 342 27 LYS C C 175.48 . . 108 342 27 LYS CA C 54.41 . . 109 342 27 LYS CB C 36.25 . . 110 342 27 LYS N N 124.02 . . 111 343 28 ASP H H 8.9 . . 112 343 28 ASP C C 175.88 . . 113 343 28 ASP CA C 53.07 . . 114 343 28 ASP CB C 42.19 . . 115 343 28 ASP N N 125.09 . . 116 344 29 SER H H 8.04 . . 117 344 29 SER C C 175 . . 118 344 29 SER CA C 60.82 . . 119 344 29 SER CB C 63.43 . . 120 344 29 SER N N 110.47 . . 121 345 30 GLU H H 8.82 . . 122 345 30 GLU C C 175.75 . . 123 345 30 GLU CA C 57.77 . . 124 345 30 GLU CB C 34.78 . . 125 345 30 GLU N N 121.5 . . 126 346 31 TYR H H 9.47 . . 127 346 31 TYR C C 172.73 . . 128 346 31 TYR CA C 57.86 . . 129 346 31 TYR CB C 42.42 . . 130 346 31 TYR N N 120.39 . . 131 347 32 LEU H H 8.43 . . 132 347 32 LEU C C 174.3 . . 133 347 32 LEU CA C 54.07 . . 134 347 32 LEU CB C 44.34 . . 135 347 32 LEU N N 120.37 . . 136 348 33 TYR H H 9.77 . . 137 348 33 TYR C C 174.33 . . 138 348 33 TYR CA C 56.79 . . 139 348 33 TYR CB C 40.97 . . 140 348 33 TYR N N 123.03 . . 141 349 34 PHE H H 9.39 . . 142 349 34 PHE C C 174.83 . . 143 349 34 PHE CA C 56.54 . . 144 349 34 PHE CB C 39.29 . . 145 349 34 PHE N N 120.62 . . 146 350 35 VAL H H 9.26 . . 147 350 35 VAL C C 175.72 . . 148 350 35 VAL CA C 62.4 . . 149 350 35 VAL CB C 33.12 . . 150 350 35 VAL N N 123.5 . . 151 351 36 ASP H H 9.18 . . 152 351 36 ASP C C 175.86 . . 153 351 36 ASP CB C 42.32 . . 154 351 36 ASP N N 130.4 . . 155 352 37 GLN H H 8.38 . . 156 352 37 GLN C C 176.33 . . 157 352 37 GLN CA C 59.29 . . 158 352 37 GLN CB C 28.12 . . 159 352 37 GLN N N 127.23 . . 160 353 38 HIS H H 8.37 . . 161 353 38 HIS C C 178.01 . . 162 353 38 HIS CA C 58.57 . . 163 353 38 HIS CB C 29.64 . . 164 353 38 HIS N N 119.66 . . 165 354 39 LEU H H 8.22 . . 166 354 39 LEU CA C 57.35 . . 167 354 39 LEU CB C 42.29 . . 168 354 39 LEU N N 121.09 . . 169 355 40 LEU H H 8.37 . . 170 355 40 LEU C C 178 . . 171 355 40 LEU CA C 58.24 . . 172 355 40 LEU CB C 40.94 . . 173 355 40 LEU N N 118.89 . . 174 356 41 GLU H H 7.97 . . 175 356 41 GLU C C 178.5 . . 176 356 41 GLU CA C 60.63 . . 177 356 41 GLU CB C 29.28 . . 178 356 41 GLU N N 119 . . 179 357 42 GLU H H 8.08 . . 180 357 42 GLU C C 179.98 . . 181 357 42 GLU CA C 60.08 . . 182 357 42 GLU N N 118.57 . . 183 358 43 ARG H H 8.3 . . 184 358 43 ARG C C 177.58 . . 185 358 43 ARG CA C 58.46 . . 186 358 43 ARG CB C 29.49 . . 187 358 43 ARG N N 120.77 . . 188 359 44 ILE H H 8.87 . . 189 359 44 ILE C C 178.08 . . 190 359 44 ILE CB C 38.29 . . 191 359 44 ILE N N 120.97 . . 192 360 45 ASN H H 8.52 . . 193 360 45 ASN C C 177.27 . . 194 360 45 ASN CA C 56.03 . . 195 360 45 ASN CB C 38.28 . . 196 360 45 ASN N N 117.15 . . 197 361 46 TYR H H 8.17 . . 198 361 46 TYR C C 177.5 . . 199 361 46 TYR CA C 61.04 . . 200 361 46 TYR CB C 39.68 . . 201 361 46 TYR N N 120.83 . . 202 362 47 GLU H H 8.22 . . 203 362 47 GLU C C 178.37 . . 204 362 47 GLU CA C 59.68 . . 205 362 47 GLU CB C 29.17 . . 206 362 47 GLU N N 117.42 . . 207 363 48 LYS H H 8.08 . . 208 363 48 LYS C C 178.4 . . 209 363 48 LYS CA C 57.94 . . 210 363 48 LYS CB C 33.7 . . 211 363 48 LYS N N 117.85 . . 212 364 49 LEU H H 7.69 . . 213 364 49 LEU C C 177.8 . . 214 364 49 LEU CA C 56.25 . . 215 364 49 LEU CB C 42.01 . . 216 364 49 LEU N N 119.05 . . 217 365 50 LYS H H 7.81 . . 218 365 50 LYS C C 176.13 . . 219 365 50 LYS CA C 56.93 . . 220 365 50 LYS CB C 32.18 . . 221 365 50 LYS N N 118.03 . . 222 366 51 ASP H H 7.69 . . 223 366 51 ASP C C 176.3 . . 224 366 51 ASP CA C 54.28 . . 225 366 51 ASP CB C 42.03 . . 226 366 51 ASP N N 119.05 . . 227 367 52 GLU H H 8.62 . . 228 367 52 GLU C C 176.79 . . 229 367 52 GLU CA C 57.85 . . 230 367 52 GLU CB C 29.91 . . 231 367 52 GLU N N 122.45 . . 232 368 53 ASN H H 8.42 . . 233 368 53 ASN C C 175.85 . . 234 368 53 ASN CA C 54.25 . . 235 368 53 ASN CB C 38.84 . . 236 368 53 ASN N N 118.26 . . 237 369 54 LEU H H 7.9 . . 238 369 54 LEU C C 177.4 . . 239 369 54 LEU CA C 55.9 . . 240 369 54 LEU CB C 42.38 . . 241 369 54 LEU N N 121.55 . . 242 370 55 ALA H H 8.09 . . 243 370 55 ALA C C 177.91 . . 244 370 55 ALA CA C 53.41 . . 245 370 55 ALA CB C 19.03 . . 246 370 55 ALA N N 122.48 . . 247 371 56 CYS H H 7.96 . . 248 371 56 CYS C C 174.5 . . 249 371 56 CYS CA C 58.76 . . 250 371 56 CYS CB C 27.91 . . 251 371 56 CYS N N 116.57 . . 252 372 57 ARG H H 8.15 . . 253 372 57 ARG C C 176.16 . . 254 372 57 ARG CA C 56.36 . . 255 372 57 ARG CB C 30.85 . . 256 372 57 ARG N N 122.74 . . 257 373 58 ILE H H 8.04 . . 258 373 58 ILE C C 175.9 . . 259 373 58 ILE CA C 61.05 . . 260 373 58 ILE CB C 38.96 . . 261 373 58 ILE N N 120.69 . . 262 374 59 SER H H 8.3 . . 263 374 59 SER C C 174.3 . . 264 374 59 SER CA C 58.18 . . 265 374 59 SER CB C 64.1 . . 266 374 59 SER N N 120.32 . . 267 375 60 VAL H H 8.37 . . 268 375 60 VAL C C 175.5 . . 269 375 60 VAL CA C 62.24 . . 270 375 60 VAL CB C 32.96 . . 271 375 60 VAL N N 122.81 . . 272 376 61 LYS H H 8.18 . . 273 376 61 LYS C C 176.22 . . 274 376 61 LYS CA C 55.66 . . 275 376 61 LYS CB C 33.48 . . 276 376 61 LYS N N 124.66 . . 277 377 62 ALA H H 8.33 . . 278 377 62 ALA C C 178.3 . . 279 377 62 ALA CA C 53.02 . . 280 377 62 ALA CB C 19.11 . . 281 377 62 ALA N N 125.14 . . 282 378 63 GLY H H 8.48 . . 283 378 63 GLY C C 174.03 . . 284 378 63 GLY CA C 45.89 . . 285 378 63 GLY N N 109.45 . . 286 379 64 GLN H H 7.88 . . 287 379 64 GLN CA C 55.44 . . 288 379 64 GLN CB C 30.43 . . 289 379 64 GLN N N 119.19 . . 290 380 65 LYS H H 8.39 . . 291 380 65 LYS C C 176.49 . . 292 380 65 LYS CA C 56.59 . . 293 380 65 LYS CB C 32.89 . . 294 380 65 LYS N N 124 . . 295 381 66 LEU H H 8.61 . . 296 381 66 LEU CA C 54.31 . . 297 381 66 LEU CB C 43.48 . . 298 381 66 LEU N N 125.58 . . 299 382 67 SER H H 7.99 . . 300 382 67 SER C C 174.68 . . 301 382 67 SER CA C 57.08 . . 302 382 67 SER CB C 65.08 . . 303 382 67 SER N N 117.25 . . 304 383 68 GLU H H 8.94 . . 305 383 68 GLU C C 178.79 . . 306 383 68 GLU CA C 60.17 . . 307 383 68 GLU CB C 29.57 . . 308 383 68 GLU N N 121.74 . . 309 384 69 GLU H H 8.66 . . 310 384 69 GLU C C 178.7 . . 311 384 69 GLU CA C 59.85 . . 312 384 69 GLU CB C 29.4 . . 313 384 69 GLU N N 118.08 . . 314 385 70 LYS H H 7.76 . . 315 385 70 LYS C C 178.8 . . 316 385 70 LYS CA C 58.41 . . 317 385 70 LYS CB C 32.14 . . 318 385 70 LYS N N 121.34 . . 319 386 71 ILE H H 8.28 . . 320 386 71 ILE C C 177.4 . . 321 386 71 ILE CB C 37.68 . . 322 386 71 ILE N N 119.3 . . 323 387 72 ARG H H 7.98 . . 324 387 72 ARG C C 179.34 . . 325 387 72 ARG CA C 60.43 . . 326 387 72 ARG CB C 30.14 . . 327 387 72 ARG N N 118 . . 328 388 73 GLU H H 7.84 . . 329 388 73 GLU C C 179.53 . . 330 388 73 GLU CA C 59.44 . . 331 388 73 GLU CB C 29.85 . . 332 388 73 GLU N N 119.77 . . 333 389 74 LEU H H 8.55 . . 334 389 74 LEU C C 178.88 . . 335 389 74 LEU CA C 58.34 . . 336 389 74 LEU CB C 41.97 . . 337 389 74 LEU N N 122.26 . . 338 390 75 ILE H H 8.08 . . 339 390 75 ILE C C 177.4 . . 340 390 75 ILE CA C 61.09 . . 341 390 75 ILE CB C 35.07 . . 342 390 75 ILE N N 117.85 . . 343 391 76 LYS H H 8.11 . . 344 391 76 LYS C C 179.22 . . 345 391 76 LYS CA C 60.13 . . 346 391 76 LYS CB C 32.39 . . 347 391 76 LYS N N 121.3 . . 348 392 77 THR H H 8.02 . . 349 392 77 THR C C 176.44 . . 350 392 77 THR CB C 68.3 . . 351 392 77 THR N N 115.25 . . 352 393 78 TRP H H 8.61 . . 353 393 78 TRP CA C 59.17 . . 354 393 78 TRP CB C 29.01 . . 355 393 78 TRP N N 123.05 . . 356 394 79 ARG H H 7.28 . . 357 394 79 ARG C C 176.5 . . 358 394 79 ARG CA C 56.48 . . 359 394 79 ARG N N 111 . . 360 395 80 ASN H H 7.61 . . 361 395 80 ASN C C 175.04 . . 362 395 80 ASN CA C 52.87 . . 363 395 80 ASN CB C 40.52 . . 364 395 80 ASN N N 116.11 . . 365 396 81 LEU H H 7.05 . . 366 396 81 LEU C C 176.91 . . 367 396 81 LEU CA C 55.17 . . 368 396 81 LEU CB C 41.97 . . 369 396 81 LEU N N 121.19 . . 370 399 84 PRO C C 176.5 . . 371 399 84 PRO CA C 62.4 . . 372 399 84 PRO CB C 32.27 . . 373 400 85 HIS H H 8.03 . . 374 400 85 HIS C C 177.5 . . 375 400 85 HIS CA C 57.4 . . 376 400 85 HIS CB C 31.98 . . 377 400 85 HIS N N 115.3 . . 378 401 86 VAL H H 7.23 . . 379 401 86 VAL C C 174.9 . . 380 401 86 VAL CA C 59.23 . . 381 401 86 VAL CB C 36.46 . . 382 401 86 VAL N N 114.1 . . 383 402 87 CYS H H 9.53 . . 384 402 87 CYS C C 174.8 . . 385 402 87 CYS CA C 59.64 . . 386 402 87 CYS CB C 28.73 . . 387 402 87 CYS N N 126.19 . . 388 404 89 HIS H H 8.06 . . 389 404 89 HIS N N 115.6 . . 390 405 90 GLY H H 8.22 . . 391 405 90 GLY C C 174.59 . . 392 405 90 GLY CA C 46 . . 393 405 90 GLY N N 110.75 . . 394 407 92 PRO C C 175.61 . . 395 407 92 PRO CA C 62.94 . . 396 407 92 PRO CB C 32.33 . . 397 408 93 ILE H H 7.63 . . 398 408 93 ILE C C 173.16 . . 399 408 93 ILE CA C 62.98 . . 400 408 93 ILE CB C 39.31 . . 401 408 93 ILE N N 117.58 . . 402 409 94 TYR H H 7.01 . . 403 409 94 TYR C C 173.56 . . 404 409 94 TYR CB C 43.42 . . 405 409 94 TYR N N 108.82 . . 406 410 95 TYR H H 8.43 . . 407 410 95 TYR C C 173.9 . . 408 410 95 TYR CA C 55.71 . . 409 410 95 TYR N N 120.37 . . 410 411 96 LYS H H 8.27 . . 411 411 96 LYS C C 172.85 . . 412 411 96 LYS CA C 53.83 . . 413 411 96 LYS CB C 36.81 . . 414 411 96 LYS N N 127.73 . . 415 412 97 ILE H H 8.83 . . 416 412 97 ILE C C 173.33 . . 417 412 97 ILE CB C 42.62 . . 418 412 97 ILE N N 119.18 . . 419 413 98 PRO C C 177.76 . . 420 413 98 PRO CA C 62.22 . . 421 413 98 PRO CB C 31.68 . . 422 414 99 LEU H H 8.45 . . 423 414 99 LEU C C 179 . . 424 414 99 LEU CA C 57.58 . . 425 414 99 LEU CB C 41.36 . . 426 414 99 LEU N N 126.91 . . 427 415 100 ARG H H 8.62 . . 428 415 100 ARG C C 177.15 . . 429 415 100 ARG CA C 59.36 . . 430 415 100 ARG CB C 29.72 . . 431 415 100 ARG N N 115.42 . . 432 416 101 GLU H H 6.96 . . 433 416 101 GLU C C 177.33 . . 434 416 101 GLU CA C 59.25 . . 435 416 101 GLU CB C 29.98 . . 436 416 101 GLU N N 116.87 . . 437 417 102 ILE H H 6.59 . . 438 417 102 ILE C C 176.51 . . 439 417 102 ILE CA C 64.64 . . 440 417 102 ILE CB C 38.11 . . 441 417 102 ILE N N 118.32 . . 442 418 103 TYR H H 7.34 . . 443 418 103 TYR C C 178.5 . . 444 418 103 TYR CA C 62.69 . . 445 418 103 TYR CB C 38.24 . . 446 418 103 TYR N N 114.2 . . 447 419 104 GLU H H 8.34 . . 448 419 104 GLU CA C 59.35 . . 449 419 104 GLU CB C 29.47 . . 450 419 104 GLU N N 116.77 . . 451 420 105 LYS H H 7.59 . . 452 420 105 LYS C C 178.38 . . 453 420 105 LYS CA C 57.74 . . 454 420 105 LYS CB C 32.17 . . 455 420 105 LYS N N 119.44 . . 456 421 106 VAL H H 7.08 . . 457 421 106 VAL C C 176.09 . . 458 421 106 VAL CA C 61.02 . . 459 421 106 VAL CB C 31.07 . . 460 421 106 VAL N N 108.43 . . 461 422 107 GLY H H 7.88 . . 462 422 107 GLY C C 174.8 . . 463 422 107 GLY CA C 46.28 . . 464 422 107 GLY N N 108.69 . . 465 423 108 ARG H H 8.13 . . 466 423 108 ARG C C 175.05 . . 467 423 108 ARG CA C 55.4 . . 468 423 108 ARG CB C 32.85 . . 469 423 108 ARG N N 119.85 . . 470 424 109 ASN H H 8.3 . . 471 424 109 ASN C C 173.44 . . 472 424 109 ASN CA C 53.23 . . 473 424 109 ASN CB C 39.9 . . 474 424 109 ASN N N 119.43 . . 475 425 110 TYR H H 7.95 . . 476 425 110 TYR C C 179.73 . . 477 425 110 TYR CA C 60.3 . . 478 425 110 TYR CB C 41.16 . . 479 425 110 TYR N N 127.67 . . stop_ save_