data_27242 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Trigger Factor ; _BMRB_accession_number 27242 _BMRB_flat_file_name bmr27242.str _Entry_type original _Submission_date 2017-09-01 _Accession_date 2017-09-01 _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 Morgado Leonor . . 2 Burmann Bjoern . . 3 Hiller Sebastian . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 181 "13C chemical shifts" 201 "15N chemical shifts" 182 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-01-18 update BMRB 'update entry citation' 2017-11-20 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27239 'Trigger factor: RBD; SBD; PPD; RBD-SBD; SBD-PPD' stop_ _Original_release_date 2017-09-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The dynamic dimer structure of the chaperone Trigger Factor. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29222465 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Morgado Leonor . . 2 Burmann Bjoern M. . 3 Sharpe Timothy . . 4 Mazur Adam . . 5 Hiller Sebastian . . stop_ _Journal_abbreviation 'Nat. Commun.' _Journal_name_full 'Nature communications' _Journal_volume 8 _Journal_issue 1 _Journal_ISSN 2041-1723 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1992 _Page_last 1992 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Trigger factor' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TF $TF 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_TF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TF _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 432 _Mol_residue_sequence ; MQVSVETTQGLGRRVTITIA ADSIETAVKSELVNVAKKVR IDGFRKGKVPMNIVAQRYGA SVRQDVLGDLMSRNFIDAII KEKINPAGAPTYVPGEYKLG EDFTYSVEFEVYPEVELQGL EAIEVEKPIVEVTDADVDGM LDTLRKQQATWKEKDGAVEA EDRVTIDFTGSVDGEEFEGG KASDFVLAMGQGRMIPGFED GIKGHKAGEEFTIDVTFPEE YHAENLKGKAAKFAINLKKV EERELPELTAEFIKRFGVED GSVEGLRAEVRKNMERELKS AIRNRVKSQAIEGLVKANDI DVPAALIDSEIDVLRRQAAQ RFGGNEKQALELPRELFEEQ AKRRVVVGLLLGEVIRTNEL KADEERVKGLIEEMASAYED PKEVIEFYSKNKELMDNMRN VALEEQAVEAVLAKAKVTEK ETTFNELMNQQA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLN 3 VAL 4 SER 5 VAL 6 GLU 7 THR 8 THR 9 GLN 10 GLY 11 LEU 12 GLY 13 ARG 14 ARG 15 VAL 16 THR 17 ILE 18 THR 19 ILE 20 ALA 21 ALA 22 ASP 23 SER 24 ILE 25 GLU 26 THR 27 ALA 28 VAL 29 LYS 30 SER 31 GLU 32 LEU 33 VAL 34 ASN 35 VAL 36 ALA 37 LYS 38 LYS 39 VAL 40 ARG 41 ILE 42 ASP 43 GLY 44 PHE 45 ARG 46 LYS 47 GLY 48 LYS 49 VAL 50 PRO 51 MET 52 ASN 53 ILE 54 VAL 55 ALA 56 GLN 57 ARG 58 TYR 59 GLY 60 ALA 61 SER 62 VAL 63 ARG 64 GLN 65 ASP 66 VAL 67 LEU 68 GLY 69 ASP 70 LEU 71 MET 72 SER 73 ARG 74 ASN 75 PHE 76 ILE 77 ASP 78 ALA 79 ILE 80 ILE 81 LYS 82 GLU 83 LYS 84 ILE 85 ASN 86 PRO 87 ALA 88 GLY 89 ALA 90 PRO 91 THR 92 TYR 93 VAL 94 PRO 95 GLY 96 GLU 97 TYR 98 LYS 99 LEU 100 GLY 101 GLU 102 ASP 103 PHE 104 THR 105 TYR 106 SER 107 VAL 108 GLU 109 PHE 110 GLU 111 VAL 112 TYR 113 PRO 114 GLU 115 VAL 116 GLU 117 LEU 118 GLN 119 GLY 120 LEU 121 GLU 122 ALA 123 ILE 124 GLU 125 VAL 126 GLU 127 LYS 128 PRO 129 ILE 130 VAL 131 GLU 132 VAL 133 THR 134 ASP 135 ALA 136 ASP 137 VAL 138 ASP 139 GLY 140 MET 141 LEU 142 ASP 143 THR 144 LEU 145 ARG 146 LYS 147 GLN 148 GLN 149 ALA 150 THR 151 TRP 152 LYS 153 GLU 154 LYS 155 ASP 156 GLY 157 ALA 158 VAL 159 GLU 160 ALA 161 GLU 162 ASP 163 ARG 164 VAL 165 THR 166 ILE 167 ASP 168 PHE 169 THR 170 GLY 171 SER 172 VAL 173 ASP 174 GLY 175 GLU 176 GLU 177 PHE 178 GLU 179 GLY 180 GLY 181 LYS 182 ALA 183 SER 184 ASP 185 PHE 186 VAL 187 LEU 188 ALA 189 MET 190 GLY 191 GLN 192 GLY 193 ARG 194 MET 195 ILE 196 PRO 197 GLY 198 PHE 199 GLU 200 ASP 201 GLY 202 ILE 203 LYS 204 GLY 205 HIS 206 LYS 207 ALA 208 GLY 209 GLU 210 GLU 211 PHE 212 THR 213 ILE 214 ASP 215 VAL 216 THR 217 PHE 218 PRO 219 GLU 220 GLU 221 TYR 222 HIS 223 ALA 224 GLU 225 ASN 226 LEU 227 LYS 228 GLY 229 LYS 230 ALA 231 ALA 232 LYS 233 PHE 234 ALA 235 ILE 236 ASN 237 LEU 238 LYS 239 LYS 240 VAL 241 GLU 242 GLU 243 ARG 244 GLU 245 LEU 246 PRO 247 GLU 248 LEU 249 THR 250 ALA 251 GLU 252 PHE 253 ILE 254 LYS 255 ARG 256 PHE 257 GLY 258 VAL 259 GLU 260 ASP 261 GLY 262 SER 263 VAL 264 GLU 265 GLY 266 LEU 267 ARG 268 ALA 269 GLU 270 VAL 271 ARG 272 LYS 273 ASN 274 MET 275 GLU 276 ARG 277 GLU 278 LEU 279 LYS 280 SER 281 ALA 282 ILE 283 ARG 284 ASN 285 ARG 286 VAL 287 LYS 288 SER 289 GLN 290 ALA 291 ILE 292 GLU 293 GLY 294 LEU 295 VAL 296 LYS 297 ALA 298 ASN 299 ASP 300 ILE 301 ASP 302 VAL 303 PRO 304 ALA 305 ALA 306 LEU 307 ILE 308 ASP 309 SER 310 GLU 311 ILE 312 ASP 313 VAL 314 LEU 315 ARG 316 ARG 317 GLN 318 ALA 319 ALA 320 GLN 321 ARG 322 PHE 323 GLY 324 GLY 325 ASN 326 GLU 327 LYS 328 GLN 329 ALA 330 LEU 331 GLU 332 LEU 333 PRO 334 ARG 335 GLU 336 LEU 337 PHE 338 GLU 339 GLU 340 GLN 341 ALA 342 LYS 343 ARG 344 ARG 345 VAL 346 VAL 347 VAL 348 GLY 349 LEU 350 LEU 351 LEU 352 GLY 353 GLU 354 VAL 355 ILE 356 ARG 357 THR 358 ASN 359 GLU 360 LEU 361 LYS 362 ALA 363 ASP 364 GLU 365 GLU 366 ARG 367 VAL 368 LYS 369 GLY 370 LEU 371 ILE 372 GLU 373 GLU 374 MET 375 ALA 376 SER 377 ALA 378 TYR 379 GLU 380 ASP 381 PRO 382 LYS 383 GLU 384 VAL 385 ILE 386 GLU 387 PHE 388 TYR 389 SER 390 LYS 391 ASN 392 LYS 393 GLU 394 LEU 395 MET 396 ASP 397 ASN 398 MET 399 ARG 400 ASN 401 VAL 402 ALA 403 LEU 404 GLU 405 GLU 406 GLN 407 ALA 408 VAL 409 GLU 410 ALA 411 VAL 412 LEU 413 ALA 414 LYS 415 ALA 416 LYS 417 VAL 418 THR 419 GLU 420 LYS 421 GLU 422 THR 423 THR 424 PHE 425 ASN 426 GLU 427 LEU 428 MET 429 ASN 430 GLN 431 GLN 432 ALA 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 $TF 'E. coli' 562 Bacteria . Escherichia coli 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 $TF 'recombinant technology' . Escherichia coli . pET28b 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 $TF 1 mM '[U-13C; U-15N; U-2H]' 'potassium phosphate' 20 mM 'natural abundance' 'potassium chloride' 100 mM 'natural abundance' EDTA 0.5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_PROSA _Saveframe_category software _Name PROSA _Version . loop_ _Vendor _Address _Electronic_address Guntert . . 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 900 _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 6.5 . pH pressure 1 . atm temperature 298 . 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' 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 TF _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 6 6 GLU CA C 53.8 0.3 1 2 6 6 GLU CB C 32.9 0.3 1 3 7 7 THR H H 8.66 0.02 1 4 7 7 THR CA C 61.7 0.3 1 5 7 7 THR CB C 69.1 0.3 1 6 7 7 THR N N 119.4 0.3 1 7 8 8 THR H H 7.60 0.02 1 8 8 8 THR CA C 59.7 0.3 1 9 8 8 THR CB C 66.6 0.3 1 10 8 8 THR N N 118.3 0.3 1 11 10 10 GLY H H 8.96 0.02 1 12 10 10 GLY CA C 46.8 0.3 1 13 10 10 GLY N N 115.9 0.3 1 14 11 11 LEU H H 9.06 0.02 1 15 11 11 LEU N N 129.7 0.3 1 16 12 12 GLY H H 8.61 0.02 1 17 12 12 GLY N N 107.6 0.3 1 18 16 16 THR H H 8.90 0.02 1 19 16 16 THR N N 125.4 0.3 1 20 17 17 ILE H H 8.75 0.02 1 21 17 17 ILE N N 130.8 0.3 1 22 104 104 THR H H 8.37 0.02 1 23 104 104 THR N N 127.5 0.3 1 24 105 105 TYR H H 8.80 0.02 1 25 105 105 TYR N N 122.1 0.3 1 26 107 107 VAL H H 9.04 0.02 1 27 107 107 VAL N N 122.4 0.3 1 28 108 108 GLU H H 8.94 0.02 1 29 108 108 GLU N N 126.1 0.3 1 30 111 111 VAL H H 8.05 0.02 1 31 111 111 VAL CA C 59.1 0.3 1 32 111 111 VAL CB C 33.0 0.3 1 33 111 111 VAL N N 114.1 0.3 1 34 114 114 GLU H H 8.34 0.02 1 35 114 114 GLU CA C 55.9 0.3 1 36 114 114 GLU CB C 29.3 0.3 1 37 114 114 GLU N N 122.6 0.3 1 38 115 115 VAL CA C 60.7 0.3 1 39 116 116 GLU H H 8.27 0.02 1 40 116 116 GLU CA C 55.6 0.3 1 41 116 116 GLU CB C 29.3 0.3 1 42 116 116 GLU N N 125.4 0.3 1 43 118 118 GLN H H 9.39 0.02 1 44 118 118 GLN N N 122.8 0.3 1 45 119 119 GLY H H 8.41 0.02 1 46 119 119 GLY CA C 45.8 0.3 1 47 119 119 GLY N N 105.1 0.3 1 48 120 120 LEU H H 8.03 0.02 1 49 120 120 LEU N N 121.4 0.3 1 50 121 121 GLU H H 8.58 0.02 1 51 121 121 GLU N N 113.1 0.3 1 52 122 122 ALA H H 7.19 0.02 1 53 122 122 ALA N N 120.2 0.3 1 54 123 123 ILE CA C 62.3 0.3 1 55 123 123 ILE N N 122.9 0.3 1 56 124 124 GLU H H 8.18 0.02 1 57 124 124 GLU CA C 54.6 0.3 1 58 124 124 GLU CB C 29.9 0.3 1 59 124 124 GLU N N 127.5 0.3 1 60 125 125 VAL H H 8.38 0.02 1 61 125 125 VAL CA C 60.5 0.3 1 62 125 125 VAL CB C 34.8 0.3 1 63 125 125 VAL N N 123.7 0.3 1 64 126 126 GLU H H 9.03 0.02 1 65 126 126 GLU CA C 53.6 0.3 1 66 126 126 GLU CB C 30.2 0.3 1 67 126 126 GLU N N 127.9 0.3 1 68 127 127 LYS H H 9.21 0.02 1 69 127 127 LYS CA C 51.9 0.3 1 70 127 127 LYS N N 131.3 0.3 1 71 129 129 ILE H H 8.00 0.02 1 72 129 129 ILE CA C 58.8 0.3 1 73 129 129 ILE CB C 36.6 0.3 1 74 129 129 ILE N N 125.3 0.3 1 75 130 130 VAL H H 7.98 0.02 1 76 130 130 VAL CA C 59.4 0.3 1 77 130 130 VAL CB C 33.3 0.3 1 78 130 130 VAL N N 126.2 0.3 1 79 133 133 THR H H 9.65 0.02 1 80 133 133 THR N N 123.3 0.3 1 81 134 134 ASP H H 8.72 0.02 1 82 134 134 ASP N N 121.0 0.3 1 83 136 136 ASP H H 7.77 0.02 1 84 136 136 ASP N N 121.6 0.3 1 85 137 137 VAL H H 7.54 0.02 1 86 137 137 VAL N N 123.0 0.3 1 87 139 139 GLY H H 8.07 0.02 1 88 139 139 GLY N N 107.6 0.3 1 89 151 151 TRP H H 8.26 0.02 1 90 151 151 TRP HE1 H 9.75 0.02 1 91 151 151 TRP CA C 55.2 0.3 1 92 151 151 TRP CB C 30.0 0.3 1 93 151 151 TRP N N 123.4 0.3 1 94 151 151 TRP NE1 N 129.1 0.3 1 95 152 152 LYS H H 9.28 0.02 1 96 152 152 LYS CA C 53.7 0.3 1 97 152 152 LYS CB C 34.6 0.3 1 98 152 152 LYS N N 123.2 0.3 1 99 153 153 GLU H H 8.78 0.02 1 100 153 153 GLU CA C 57.7 0.3 1 101 153 153 GLU CB C 28.9 0.3 1 102 153 153 GLU N N 124.8 0.3 1 103 154 154 LYS H H 8.70 0.02 1 104 154 154 LYS CA C 53.8 0.3 1 105 154 154 LYS CB C 34.8 0.3 1 106 154 154 LYS N N 123.9 0.3 1 107 155 155 ASP H H 8.56 0.02 1 108 155 155 ASP CA C 52.5 0.3 1 109 155 155 ASP CB C 39.8 0.3 1 110 155 155 ASP N N 123.6 0.3 1 111 156 156 GLY H H 7.15 0.02 1 112 156 156 GLY CA C 43.1 0.3 1 113 156 156 GLY N N 106.7 0.3 1 114 157 157 ALA H H 8.09 0.02 1 115 157 157 ALA CA C 50.6 0.3 1 116 157 157 ALA CB C 18.9 0.3 1 117 157 157 ALA N N 120.3 0.3 1 118 158 158 VAL H H 8.64 0.02 1 119 158 158 VAL CA C 63.6 0.3 1 120 158 158 VAL CB C 31.5 0.3 1 121 158 158 VAL N N 119.6 0.3 1 122 159 159 GLU H H 9.49 0.02 1 123 159 159 GLU CA C 54.1 0.3 1 124 159 159 GLU CB C 31.2 0.3 1 125 159 159 GLU N N 132.5 0.3 1 126 160 160 ALA H H 8.14 0.02 1 127 160 160 ALA CA C 54.9 0.3 1 128 160 160 ALA CB C 18.9 0.3 1 129 160 160 ALA N N 117.5 0.3 1 130 161 161 GLU H H 8.03 0.02 1 131 161 161 GLU CA C 54.7 0.3 1 132 161 161 GLU CB C 28.5 0.3 1 133 161 161 GLU N N 112.1 0.3 1 134 162 162 ASP H H 7.16 0.02 1 135 162 162 ASP CA C 54.9 0.3 1 136 162 162 ASP CB C 40.9 0.3 1 137 162 162 ASP N N 123.1 0.3 1 138 163 163 ARG H H 8.85 0.02 1 139 163 163 ARG CA C 53.9 0.3 1 140 163 163 ARG CB C 33.1 0.3 1 141 163 163 ARG N N 118.9 0.3 1 142 164 164 VAL H H 8.90 0.02 1 143 164 164 VAL CA C 57.7 0.3 1 144 164 164 VAL CB C 33.1 0.3 1 145 164 164 VAL N N 120.0 0.3 1 146 166 166 ILE H H 9.48 0.02 1 147 166 166 ILE CA C 57.9 0.3 1 148 166 166 ILE CB C 41.7 0.3 1 149 166 166 ILE N N 120.2 0.3 1 150 167 167 ASP H H 8.42 0.02 1 151 167 167 ASP CA C 52.0 0.3 1 152 167 167 ASP CB C 41.5 0.3 1 153 167 167 ASP N N 119.5 0.3 1 154 168 168 PHE H H 8.47 0.02 1 155 168 168 PHE N N 115.1 0.3 1 156 169 169 THR H H 8.37 0.02 1 157 169 169 THR N N 115.1 0.3 1 158 170 170 GLY H H 9.14 0.02 1 159 170 170 GLY CA C 44.3 0.3 1 160 170 170 GLY N N 119.4 0.3 1 161 171 171 SER H H 8.87 0.02 1 162 171 171 SER CA C 56.5 0.3 1 163 171 171 SER CB C 65.4 0.3 1 164 171 171 SER N N 116.2 0.3 1 165 172 172 VAL H H 8.73 0.02 1 166 172 172 VAL CA C 60.7 0.3 1 167 172 172 VAL CB C 33.5 0.3 1 168 172 172 VAL N N 120.8 0.3 1 169 173 173 ASP H H 9.46 0.02 1 170 173 173 ASP CA C 55.0 0.3 1 171 173 173 ASP CB C 38.8 0.3 1 172 173 173 ASP N N 129.4 0.3 1 173 174 174 GLY H H 8.51 0.02 1 174 174 174 GLY CA C 44.5 0.3 1 175 174 174 GLY N N 102.9 0.3 1 176 175 175 GLU H H 7.78 0.02 1 177 175 175 GLU CA C 53.9 0.3 1 178 175 175 GLU CB C 30.9 0.3 1 179 175 175 GLU N N 120.9 0.3 1 180 176 176 GLU H H 8.65 0.02 1 181 176 176 GLU CA C 55.1 0.3 1 182 176 176 GLU CB C 29.0 0.3 1 183 176 176 GLU N N 125.3 0.3 1 184 177 177 PHE CA C 53.8 0.3 1 185 177 177 PHE CB C 40.3 0.3 1 186 178 178 GLU H H 8.90 0.02 1 187 178 178 GLU CA C 57.4 0.3 1 188 178 178 GLU CB C 28.3 0.3 1 189 178 178 GLU N N 125.1 0.3 1 190 179 179 GLY H H 8.84 0.02 1 191 179 179 GLY CA C 44.7 0.3 1 192 179 179 GLY N N 114.2 0.3 1 193 180 180 GLY CA C 45.8 0.3 1 194 181 181 LYS H H 7.38 0.02 1 195 181 181 LYS CA C 53.8 0.3 1 196 181 181 LYS CB C 34.6 0.3 1 197 181 181 LYS N N 119.5 0.3 1 198 182 182 ALA H H 7.96 0.02 1 199 182 182 ALA CA C 50.9 0.3 1 200 182 182 ALA CB C 21.9 0.3 1 201 182 182 ALA N N 125.8 0.3 1 202 183 183 SER H H 8.27 0.02 1 203 183 183 SER CA C 55.9 0.3 1 204 183 183 SER CB C 64.5 0.3 1 205 183 183 SER N N 116.0 0.3 1 206 184 184 ASP H H 9.50 0.02 1 207 184 184 ASP CA C 55.6 0.3 1 208 184 184 ASP CB C 38.7 0.3 1 209 184 184 ASP N N 123.8 0.3 1 210 185 185 PHE H H 9.04 0.02 1 211 185 185 PHE CA C 57.3 0.3 1 212 185 185 PHE CB C 39.1 0.3 1 213 185 185 PHE N N 121.9 0.3 1 214 186 186 VAL H H 7.74 0.02 1 215 186 186 VAL CA C 61.6 0.3 1 216 186 186 VAL CB C 30.2 0.3 1 217 186 186 VAL N N 129.8 0.3 1 218 187 187 LEU H H 9.20 0.02 1 219 187 187 LEU CA C 52.2 0.3 1 220 187 187 LEU CB C 43.2 0.3 1 221 187 187 LEU N N 131.4 0.3 1 222 188 188 ALA H H 8.46 0.02 1 223 188 188 ALA CA C 51.0 0.3 1 224 188 188 ALA CB C 15.7 0.3 1 225 188 188 ALA N N 132.7 0.3 1 226 189 189 MET H H 8.52 0.02 1 227 189 189 MET CA C 56.5 0.3 1 228 189 189 MET CB C 32.2 0.3 1 229 189 189 MET N N 125.6 0.3 1 230 190 190 GLY H H 10.07 0.02 1 231 190 190 GLY N N 110.1 0.3 1 232 192 192 GLY H H 9.00 0.02 1 233 192 192 GLY N N 111.4 0.3 1 234 198 198 PHE H H 7.67 0.02 1 235 198 198 PHE N N 123.1 0.3 1 236 200 200 ASP H H 8.21 0.02 1 237 200 200 ASP CA C 56.9 0.3 1 238 200 200 ASP CB C 39.4 0.3 1 239 200 200 ASP N N 117.5 0.3 1 240 201 201 GLY H H 7.27 0.02 1 241 201 201 GLY N N 103.5 0.3 1 242 202 202 ILE H H 7.21 0.02 1 243 202 202 ILE CA C 62.4 0.3 1 244 202 202 ILE N N 119.5 0.3 1 245 203 203 LYS H H 6.87 0.02 1 246 203 203 LYS CA C 57.8 0.3 1 247 203 203 LYS CB C 31.0 0.3 1 248 203 203 LYS N N 117.7 0.3 1 249 204 204 GLY H H 8.78 0.02 1 250 204 204 GLY CA C 44.3 0.3 1 251 204 204 GLY N N 109.7 0.3 1 252 205 205 HIS H H 7.37 0.02 1 253 205 205 HIS CA C 55.2 0.3 1 254 205 205 HIS CB C 29.6 0.3 1 255 205 205 HIS N N 118.3 0.3 1 256 206 206 LYS H H 8.50 0.02 1 257 206 206 LYS CA C 53.9 0.3 1 258 206 206 LYS CB C 35.0 0.3 1 259 206 206 LYS N N 118.3 0.3 1 260 207 207 ALA H H 8.64 0.02 1 261 207 207 ALA CA C 52.8 0.3 1 262 207 207 ALA CB C 16.7 0.3 1 263 207 207 ALA N N 121.4 0.3 1 264 208 208 GLY H H 9.06 0.02 1 265 208 208 GLY CA C 44.0 0.3 1 266 208 208 GLY N N 111.0 0.3 1 267 209 209 GLU H H 7.81 0.02 1 268 209 209 GLU CA C 56.3 0.3 1 269 209 209 GLU CB C 31.4 0.3 1 270 209 209 GLU N N 120.2 0.3 1 271 210 210 GLU H H 8.16 0.02 1 272 210 210 GLU CA C 54.0 0.3 1 273 210 210 GLU CB C 31.1 0.3 1 274 210 210 GLU N N 120.0 0.3 1 275 211 211 PHE H H 8.15 0.02 1 276 211 211 PHE CA C 55.0 0.3 1 277 211 211 PHE CB C 38.1 0.3 1 278 211 211 PHE N N 120.7 0.3 1 279 212 212 THR H H 8.60 0.02 1 280 212 212 THR CA C 60.2 0.3 1 281 212 212 THR CB C 70.5 0.3 1 282 212 212 THR N N 115.7 0.3 1 283 213 213 ILE H H 8.83 0.02 1 284 213 213 ILE CA C 59.0 0.3 1 285 213 213 ILE CB C 40.1 0.3 1 286 213 213 ILE N N 120.0 0.3 1 287 214 214 ASP H H 8.36 0.02 1 288 214 214 ASP CA C 53.2 0.3 1 289 214 214 ASP CB C 41.9 0.3 1 290 214 214 ASP N N 123.4 0.3 1 291 215 215 VAL H H 8.49 0.02 1 292 215 215 VAL N N 119.3 0.3 1 293 217 217 PHE H H 8.80 0.02 1 294 217 217 PHE CA C 57.5 0.3 1 295 217 217 PHE CB C 38.2 0.3 1 296 217 217 PHE N N 127.8 0.3 1 297 218 218 PRO CA C 61.8 0.3 1 298 218 218 PRO CB C 31.3 0.3 1 299 219 219 GLU H H 8.77 0.02 1 300 219 219 GLU CA C 58.8 0.3 1 301 219 219 GLU CB C 28.6 0.3 1 302 219 219 GLU N N 123.4 0.3 1 303 220 220 GLU H H 8.10 0.02 1 304 220 220 GLU CA C 54.8 0.3 1 305 220 220 GLU CB C 27.3 0.3 1 306 220 220 GLU N N 115.4 0.3 1 307 221 221 TYR H H 7.34 0.02 1 308 221 221 TYR CA C 58.7 0.3 1 309 221 221 TYR CB C 39.2 0.3 1 310 221 221 TYR N N 122.4 0.3 1 311 222 222 HIS H H 6.76 0.02 1 312 222 222 HIS N N 120.9 0.3 1 313 223 223 ALA H H 5.49 0.02 1 314 223 223 ALA N N 122.9 0.3 1 315 224 224 GLU H H 8.82 0.02 1 316 224 224 GLU CA C 59.1 0.3 1 317 224 224 GLU CB C 28.3 0.3 1 318 224 224 GLU N N 127.1 0.3 1 319 225 225 ASN H H 8.61 0.02 1 320 225 225 ASN CA C 53.8 0.3 1 321 225 225 ASN CB C 36.1 0.3 1 322 225 225 ASN N N 113.3 0.3 1 323 226 226 LEU H H 6.94 0.02 1 324 226 226 LEU N N 117.7 0.3 1 325 227 227 LYS H H 6.90 0.02 1 326 227 227 LYS CA C 57.7 0.3 1 327 227 227 LYS CB C 31.2 0.3 1 328 227 227 LYS N N 117.7 0.3 1 329 228 228 GLY H H 7.06 0.02 1 330 228 228 GLY CA C 45.5 0.3 1 331 228 228 GLY N N 111.6 0.3 1 332 229 229 LYS H H 7.76 0.02 1 333 229 229 LYS CA C 55.1 0.3 1 334 229 229 LYS CB C 31.9 0.3 1 335 229 229 LYS N N 119.7 0.3 1 336 230 230 ALA H H 8.20 0.02 1 337 230 230 ALA CA C 51.2 0.3 1 338 230 230 ALA CB C 17.8 0.3 1 339 230 230 ALA N N 124.1 0.3 1 340 231 231 ALA H H 9.16 0.02 1 341 231 231 ALA CA C 49.8 0.3 1 342 231 231 ALA CB C 23.0 0.3 1 343 231 231 ALA N N 127.0 0.3 1 344 232 232 LYS H H 8.54 0.02 1 345 232 232 LYS CA C 53.6 0.3 1 346 232 232 LYS CB C 34.6 0.3 1 347 232 232 LYS N N 121.0 0.3 1 348 233 233 PHE H H 9.01 0.02 1 349 233 233 PHE N N 119.3 0.3 1 350 234 234 ALA H H 8.45 0.02 1 351 234 234 ALA CA C 51.1 0.3 1 352 234 234 ALA CB C 17.7 0.3 1 353 234 234 ALA N N 128.2 0.3 1 354 235 235 ILE H H 9.01 0.02 1 355 235 235 ILE CA C 58.0 0.3 1 356 235 235 ILE CB C 37.1 0.3 1 357 235 235 ILE N N 126.7 0.3 1 358 236 236 ASN H H 8.46 0.02 1 359 236 236 ASN CA C 51.4 0.3 1 360 236 236 ASN CB C 39.3 0.3 1 361 236 236 ASN N N 124.5 0.3 1 362 237 237 LEU H H 8.48 0.02 1 363 237 237 LEU CA C 54.0 0.3 1 364 237 237 LEU CB C 41.5 0.3 1 365 237 237 LEU N N 127.8 0.3 1 366 238 238 LYS H H 8.57 0.02 1 367 238 238 LYS CA C 57.8 0.3 1 368 238 238 LYS CB C 32.1 0.3 1 369 238 238 LYS N N 127.7 0.3 1 370 239 239 LYS H H 7.47 0.02 1 371 239 239 LYS CA C 56.1 0.3 1 372 239 239 LYS CB C 35.1 0.3 1 373 239 239 LYS N N 118.1 0.3 1 374 240 240 VAL H H 9.05 0.02 1 375 240 240 VAL CA C 61.7 0.3 1 376 240 240 VAL CB C 33.4 0.3 1 377 240 240 VAL N N 126.7 0.3 1 378 241 241 GLU H H 9.25 0.02 1 379 241 241 GLU CA C 53.6 0.3 1 380 241 241 GLU CB C 35.5 0.3 1 381 241 241 GLU N N 125.2 0.3 1 382 242 242 GLU H H 9.40 0.02 1 383 242 242 GLU CA C 52.4 0.3 1 384 242 242 GLU CB C 32.7 0.3 1 385 242 242 GLU N N 118.7 0.3 1 386 247 247 GLU CA C 52.9 0.3 1 387 247 247 GLU CB C 29.6 0.3 1 388 248 248 LEU H H 8.67 0.02 1 389 248 248 LEU CA C 55.1 0.3 1 390 248 248 LEU CB C 38.3 0.3 1 391 248 248 LEU N N 124.9 0.3 1 392 249 249 THR H H 7.63 0.02 1 393 249 249 THR CA C 59.4 0.3 1 394 249 249 THR CB C 71.1 0.3 1 395 249 249 THR N N 115.4 0.3 1 396 250 250 ALA H H 8.75 0.02 1 397 250 250 ALA N N 123.3 0.3 1 398 251 251 GLU H H 8.20 0.02 1 399 251 251 GLU N N 115.5 0.3 1 400 258 258 VAL CA C 59.0 0.3 1 401 258 258 VAL CB C 28.3 0.3 1 402 259 259 GLU H H 8.38 0.02 1 403 259 259 GLU CA C 61.3 0.3 1 404 259 259 GLU CB C 29.0 0.3 1 405 259 259 GLU N N 128.5 0.3 1 406 260 260 ASP H H 8.14 0.02 1 407 260 260 ASP CA C 52.7 0.3 1 408 260 260 ASP CB C 39.3 0.3 1 409 260 260 ASP N N 114.9 0.3 1 410 261 261 GLY H H 7.83 0.02 1 411 261 261 GLY N N 107.1 0.3 1 412 263 263 VAL H H 8.71 0.02 1 413 263 263 VAL N N 125.3 0.3 1 414 264 264 GLU H H 8.83 0.02 1 415 264 264 GLU N N 120.2 0.3 1 416 265 265 GLY H H 8.26 0.02 1 417 265 265 GLY N N 110.6 0.3 1 418 271 271 ARG H H 7.59 0.02 1 419 271 271 ARG N N 123.1 0.3 1 420 278 278 LEU H H 8.69 0.02 1 421 278 278 LEU N N 122.2 0.3 1 422 280 280 SER H H 7.45 0.02 1 423 280 280 SER N N 114.3 0.3 1 424 281 281 ALA H H 8.08 0.02 1 425 281 281 ALA N N 125.4 0.3 1 426 290 290 ALA H H 8.20 0.02 1 427 290 290 ALA N N 124.2 0.3 1 428 291 291 ILE H H 8.26 0.02 1 429 291 291 ILE N N 116.4 0.3 1 430 293 293 GLY H H 7.95 0.02 1 431 293 293 GLY N N 105.0 0.3 1 432 299 299 ASP H H 8.22 0.02 1 433 299 299 ASP N N 122.8 0.3 1 434 300 300 ILE H H 7.61 0.02 1 435 300 300 ILE N N 120.3 0.3 1 436 310 310 GLU H H 7.55 0.02 1 437 310 310 GLU N N 123.4 0.3 1 438 313 313 VAL H H 7.30 0.02 1 439 313 313 VAL N N 120.9 0.3 1 440 324 324 GLY H H 8.06 0.02 1 441 324 324 GLY N N 108.6 0.3 1 442 326 326 GLU H H 8.43 0.02 1 443 326 326 GLU N N 121.5 0.3 1 444 329 329 ALA H H 7.95 0.02 1 445 329 329 ALA CA C 53.6 0.3 1 446 329 329 ALA CB C 17.4 0.3 1 447 329 329 ALA N N 123.1 0.3 1 448 330 330 LEU H H 7.67 0.02 1 449 330 330 LEU N N 116.9 0.3 1 450 332 332 LEU H H 7.54 0.02 1 451 332 332 LEU N N 123.9 0.3 1 452 334 334 ARG H H 8.62 0.02 1 453 334 334 ARG N N 122.9 0.3 1 454 335 335 GLU H H 9.38 0.02 1 455 335 335 GLU N N 117.6 0.3 1 456 336 336 LEU H H 7.38 0.02 1 457 336 336 LEU N N 119.0 0.3 1 458 338 338 GLU H H 7.26 0.02 1 459 338 338 GLU N N 120.0 0.3 1 460 339 339 GLU H H 8.57 0.02 1 461 339 339 GLU N N 120.2 0.3 1 462 343 343 ARG H H 7.60 0.02 1 463 343 343 ARG N N 118.3 0.3 1 464 344 344 ARG H H 7.83 0.02 1 465 344 344 ARG N N 117.7 0.3 1 466 348 348 GLY H H 7.84 0.02 1 467 348 348 GLY N N 105.4 0.3 1 468 350 350 LEU H H 8.47 0.02 1 469 350 350 LEU N N 120.0 0.3 1 470 351 351 LEU H H 9.08 0.02 1 471 351 351 LEU N N 118.4 0.3 1 472 352 352 GLY H H 8.03 0.02 1 473 352 352 GLY N N 107.1 0.3 1 474 353 353 GLU H H 7.66 0.02 1 475 353 353 GLU N N 123.6 0.3 1 476 357 357 THR H H 8.56 0.02 1 477 357 357 THR N N 112.4 0.3 1 478 358 358 ASN H H 7.30 0.02 1 479 358 358 ASN N N 116.6 0.3 1 480 359 359 GLU H H 7.60 0.02 1 481 359 359 GLU N N 118.7 0.3 1 482 360 360 LEU H H 7.96 0.02 1 483 360 360 LEU CA C 54.3 0.3 1 484 360 360 LEU CB C 41.2 0.3 1 485 360 360 LEU N N 116.5 0.3 1 486 361 361 LYS H H 8.21 0.02 1 487 361 361 LYS CA C 53.5 0.3 1 488 361 361 LYS CB C 33.9 0.3 1 489 361 361 LYS N N 120.8 0.3 1 490 362 362 ALA H H 8.74 0.02 1 491 362 362 ALA CA C 52.1 0.3 1 492 362 362 ALA CB C 17.2 0.3 1 493 362 362 ALA N N 126.3 0.3 1 494 364 364 GLU H H 8.91 0.02 1 495 364 364 GLU N N 127.3 0.3 1 496 369 369 GLY H H 7.83 0.02 1 497 369 369 GLY N N 106.7 0.3 1 498 376 376 SER H H 7.70 0.02 1 499 376 376 SER CA C 60.0 0.3 1 500 376 376 SER N N 112.8 0.3 1 501 377 377 ALA H H 7.20 0.02 1 502 377 377 ALA N N 122.7 0.3 1 503 378 378 TYR H H 7.71 0.02 1 504 378 378 TYR N N 119.0 0.3 1 505 383 383 GLU H H 7.34 0.02 1 506 383 383 GLU N N 119.4 0.3 1 507 385 385 ILE H H 8.06 0.02 1 508 385 385 ILE N N 120.8 0.3 1 509 387 387 PHE H H 7.90 0.02 1 510 387 387 PHE N N 121.5 0.3 1 511 388 388 TYR H H 8.49 0.02 1 512 388 388 TYR N N 119.4 0.3 1 513 391 391 ASN H H 7.35 0.02 1 514 391 391 ASN N N 121.9 0.3 1 515 400 400 ASN H H 7.59 0.02 1 516 400 400 ASN N N 117.8 0.3 1 517 407 407 ALA H H 8.74 0.02 1 518 407 407 ALA N N 125.1 0.3 1 519 411 411 VAL H H 7.67 0.02 1 520 411 411 VAL N N 120.5 0.3 1 521 415 415 ALA H H 7.03 0.02 1 522 415 415 ALA N N 121.5 0.3 1 523 416 416 LYS CA C 55.0 0.3 1 524 416 416 LYS CB C 30.8 0.3 1 525 417 417 VAL H H 8.28 0.02 1 526 417 417 VAL CA C 60.8 0.3 1 527 417 417 VAL CB C 31.8 0.3 1 528 417 417 VAL N N 129.3 0.3 1 529 418 418 THR H H 8.79 0.02 1 530 418 418 THR N N 123.6 0.3 1 531 419 419 GLU H H 8.62 0.02 1 532 419 419 GLU N N 124.1 0.3 1 533 420 420 LYS H H 8.17 0.02 1 534 420 420 LYS CA C 54.2 0.3 1 535 420 420 LYS CB C 34.7 0.3 1 536 420 420 LYS N N 124.3 0.3 1 537 421 421 GLU H H 9.04 0.02 1 538 421 421 GLU CA C 56.9 0.3 1 539 421 421 GLU CB C 28.4 0.3 1 540 421 421 GLU N N 130.7 0.3 1 541 422 422 THR H H 8.35 0.02 1 542 422 422 THR CA C 59.3 0.3 1 543 422 422 THR CB C 69.6 0.3 1 544 422 422 THR N N 120.9 0.3 1 545 423 423 THR H H 8.39 0.02 1 546 423 423 THR CA C 59.4 0.3 1 547 423 423 THR CB C 71.3 0.3 1 548 423 423 THR N N 113.0 0.3 1 549 424 424 PHE H H 9.77 0.02 1 550 424 424 PHE N N 124.8 0.3 1 551 425 425 ASN H H 9.30 0.02 1 552 425 425 ASN N N 116.3 0.3 1 553 429 429 ASN H H 7.50 0.02 1 554 429 429 ASN N N 117.3 0.3 1 555 430 430 GLN CA C 55.5 0.3 1 556 430 430 GLN CB C 28.0 0.3 1 557 431 431 GLN H H 8.22 0.02 1 558 431 431 GLN CA C 55.2 0.3 1 559 431 431 GLN CB C 28.4 0.3 1 560 431 431 GLN N N 122.3 0.3 1 561 432 432 ALA H H 7.77 0.02 1 562 432 432 ALA CA C 53.3 0.3 1 563 432 432 ALA CB C 19.1 0.3 1 564 432 432 ALA N N 131.0 0.3 1 stop_ save_